data_6YHA
# 
_entry.id   6YHA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   6YHA         pdb_00006yha 10.2210/pdb6yha/pdb 
WWPDB D_1292106433 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2021-04-07 
2 'Structure model' 1 1 2021-06-02 
3 'Structure model' 1 2 2024-01-24 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                      
2 2 'Structure model' citation_author               
3 3 'Structure model' chem_comp_atom                
4 3 'Structure model' chem_comp_bond                
5 3 'Structure model' database_2                    
6 3 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                   
2  2 'Structure model' '_citation.journal_abbrev'            
3  2 'Structure model' '_citation.journal_id_CSD'            
4  2 'Structure model' '_citation.journal_id_ISSN'           
5  2 'Structure model' '_citation.journal_volume'            
6  2 'Structure model' '_citation.page_first'                
7  2 'Structure model' '_citation.page_last'                 
8  2 'Structure model' '_citation.pdbx_database_id_DOI'      
9  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
10 2 'Structure model' '_citation.title'                     
11 2 'Structure model' '_citation.year'                      
12 3 'Structure model' '_database_2.pdbx_DOI'                
13 3 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6YHA 
_pdbx_database_status.recvd_initial_deposition_date   2020-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistryopen 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2191-1363 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                567 
_citation.page_last                 580 
_citation.title                     'Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/open.202100042 
_citation.pdbx_database_id_PubMed   33945229 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnoviene, J.'   1  0000-0001-5503-4775 
primary 'Smirnov, A.'       2  ?                   
primary 'Zaksauskas, A.'    3  ?                   
primary 'Zubriene, A.'      4  0000-0001-5996-1883 
primary 'Petrauskas, V.'    5  0000-0001-7983-4128 
primary 'Mickeviciute, A.'  6  ?                   
primary 'Michailoviene, V.' 7  ?                   
primary 'Capkauskaite, E.'  8  ?                   
primary 'Manakova, E.'      9  0000-0002-6027-2265 
primary 'Grazulis, S.'      10 0000-0002-7928-5218 
primary 'Baranauskiene, L.' 11 0000-0002-9924-9177 
primary 'Chen, W.Y.'        12 ?                   
primary 'Ladbury, J.E.'     13 0000-0002-6328-7200 
primary 'Matulis, D.'       14 0000-0002-6178-6276 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                     29220.879 1   4.2.1.1 
'A65S, N67K, I91T, F130A, V134S, L203N' ? ? 
2 non-polymer syn 'ZINC ION'                                                 65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                       78.133    1   ?       ? ? ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                     195.237   1   ?       ? ? ? 
5 non-polymer syn 'ISOBUTYL MALONIC ACID'                                    160.168   1   ?       ? ? ? 
6 non-polymer syn '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 303.297   2   ?       ? ? ? 
7 water       nat water                                                      18.015    255 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                 ZN  
3 'DIMETHYL SULFOXIDE'                                       DMS 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                     MES 
5 'ISOBUTYL MALONIC ACID'                                    LML 
6 '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 3TV 
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  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  SER n 
1 66  PHE n 
1 67  LYS n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  THR n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 ALA n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 SER n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 ASN n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
3TV non-polymer         . '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' ? 'C9 H9 F4 N O2 S2' 303.297 
ALA 'L-peptide linking' y ALANINE                                                    ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                                                   ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                 ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                            ? 'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                                                   ? 'C3 H7 N O2 S'     121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                       ? 'C2 H6 O S'        78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                  ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                            ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                                    ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                                                  ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                      ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                 ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                                    ? 'C6 H13 N O2'      131.173 
LML non-polymer         . 'ISOBUTYL MALONIC ACID'                                    ? 'C7 H12 O4'        160.168 
LYS 'L-peptide linking' y LYSINE                                                     ? 'C6 H15 N2 O2 1'   147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                     ? 'C6 H13 N O4 S'    195.237 
MET 'L-peptide linking' y METHIONINE                                                 ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                              ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                    ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                     ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                  ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                 ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                   ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                                     ? 'C5 H11 N O2'      117.146 
ZN  non-polymer         . 'ZINC ION'                                                 ? 'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 ALA 130 131 131 ALA ALA A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 SER 134 135 135 SER SER A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 ASN 203 204 204 ASN ASN A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 MES 1   303 2   MES MES A . 
E 5 LML 1   304 3   LML LML A . 
F 6 3TV 1   305 1   3TV V05 A . 
G 6 3TV 1   306 2   3TV V05 A . 
H 7 HOH 1   401 121 HOH HOH A . 
H 7 HOH 2   402 60  HOH HOH A . 
H 7 HOH 3   403 179 HOH HOH A . 
H 7 HOH 4   404 30  HOH HOH A . 
H 7 HOH 5   405 228 HOH HOH A . 
H 7 HOH 6   406 46  HOH HOH A . 
H 7 HOH 7   407 174 HOH HOH A . 
H 7 HOH 8   408 129 HOH HOH A . 
H 7 HOH 9   409 69  HOH HOH A . 
H 7 HOH 10  410 192 HOH HOH A . 
H 7 HOH 11  411 195 HOH HOH A . 
H 7 HOH 12  412 118 HOH HOH A . 
H 7 HOH 13  413 123 HOH HOH A . 
H 7 HOH 14  414 110 HOH HOH A . 
H 7 HOH 15  415 149 HOH HOH A . 
H 7 HOH 16  416 111 HOH HOH A . 
H 7 HOH 17  417 63  HOH HOH A . 
H 7 HOH 18  418 156 HOH HOH A . 
H 7 HOH 19  419 162 HOH HOH A . 
H 7 HOH 20  420 103 HOH HOH A . 
H 7 HOH 21  421 101 HOH HOH A . 
H 7 HOH 22  422 7   HOH HOH A . 
H 7 HOH 23  423 92  HOH HOH A . 
H 7 HOH 24  424 134 HOH HOH A . 
H 7 HOH 25  425 40  HOH HOH A . 
H 7 HOH 26  426 217 HOH HOH A . 
H 7 HOH 27  427 247 HOH HOH A . 
H 7 HOH 28  428 51  HOH HOH A . 
H 7 HOH 29  429 27  HOH HOH A . 
H 7 HOH 30  430 54  HOH HOH A . 
H 7 HOH 31  431 22  HOH HOH A . 
H 7 HOH 32  432 209 HOH HOH A . 
H 7 HOH 33  433 105 HOH HOH A . 
H 7 HOH 34  434 74  HOH HOH A . 
H 7 HOH 35  435 205 HOH HOH A . 
H 7 HOH 36  436 20  HOH HOH A . 
H 7 HOH 37  437 53  HOH HOH A . 
H 7 HOH 38  438 102 HOH HOH A . 
H 7 HOH 39  439 203 HOH HOH A . 
H 7 HOH 40  440 35  HOH HOH A . 
H 7 HOH 41  441 81  HOH HOH A . 
H 7 HOH 42  442 254 HOH HOH A . 
H 7 HOH 43  443 120 HOH HOH A . 
H 7 HOH 44  444 165 HOH HOH A . 
H 7 HOH 45  445 12  HOH HOH A . 
H 7 HOH 46  446 65  HOH HOH A . 
H 7 HOH 47  447 128 HOH HOH A . 
H 7 HOH 48  448 97  HOH HOH A . 
H 7 HOH 49  449 251 HOH HOH A . 
H 7 HOH 50  450 24  HOH HOH A . 
H 7 HOH 51  451 18  HOH HOH A . 
H 7 HOH 52  452 112 HOH HOH A . 
H 7 HOH 53  453 94  HOH HOH A . 
H 7 HOH 54  454 188 HOH HOH A . 
H 7 HOH 55  455 133 HOH HOH A . 
H 7 HOH 56  456 59  HOH HOH A . 
H 7 HOH 57  457 29  HOH HOH A . 
H 7 HOH 58  458 70  HOH HOH A . 
H 7 HOH 59  459 56  HOH HOH A . 
H 7 HOH 60  460 177 HOH HOH A . 
H 7 HOH 61  461 152 HOH HOH A . 
H 7 HOH 62  462 5   HOH HOH A . 
H 7 HOH 63  463 187 HOH HOH A . 
H 7 HOH 64  464 159 HOH HOH A . 
H 7 HOH 65  465 32  HOH HOH A . 
H 7 HOH 66  466 33  HOH HOH A . 
H 7 HOH 67  467 38  HOH HOH A . 
H 7 HOH 68  468 11  HOH HOH A . 
H 7 HOH 69  469 49  HOH HOH A . 
H 7 HOH 70  470 220 HOH HOH A . 
H 7 HOH 71  471 39  HOH HOH A . 
H 7 HOH 72  472 17  HOH HOH A . 
H 7 HOH 73  473 83  HOH HOH A . 
H 7 HOH 74  474 242 HOH HOH A . 
H 7 HOH 75  475 173 HOH HOH A . 
H 7 HOH 76  476 147 HOH HOH A . 
H 7 HOH 77  477 96  HOH HOH A . 
H 7 HOH 78  478 84  HOH HOH A . 
H 7 HOH 79  479 57  HOH HOH A . 
H 7 HOH 80  480 67  HOH HOH A . 
H 7 HOH 81  481 184 HOH HOH A . 
H 7 HOH 82  482 45  HOH HOH A . 
H 7 HOH 83  483 61  HOH HOH A . 
H 7 HOH 84  484 114 HOH HOH A . 
H 7 HOH 85  485 181 HOH HOH A . 
H 7 HOH 86  486 6   HOH HOH A . 
H 7 HOH 87  487 3   HOH HOH A . 
H 7 HOH 88  488 161 HOH HOH A . 
H 7 HOH 89  489 193 HOH HOH A . 
H 7 HOH 90  490 125 HOH HOH A . 
H 7 HOH 91  491 1   HOH HOH A . 
H 7 HOH 92  492 99  HOH HOH A . 
H 7 HOH 93  493 47  HOH HOH A . 
H 7 HOH 94  494 106 HOH HOH A . 
H 7 HOH 95  495 19  HOH HOH A . 
H 7 HOH 96  496 15  HOH HOH A . 
H 7 HOH 97  497 25  HOH HOH A . 
H 7 HOH 98  498 167 HOH HOH A . 
H 7 HOH 99  499 8   HOH HOH A . 
H 7 HOH 100 500 52  HOH HOH A . 
H 7 HOH 101 501 127 HOH HOH A . 
H 7 HOH 102 502 10  HOH HOH A . 
H 7 HOH 103 503 108 HOH HOH A . 
H 7 HOH 104 504 76  HOH HOH A . 
H 7 HOH 105 505 36  HOH HOH A . 
H 7 HOH 106 506 58  HOH HOH A . 
H 7 HOH 107 507 122 HOH HOH A . 
H 7 HOH 108 508 42  HOH HOH A . 
H 7 HOH 109 509 182 HOH HOH A . 
H 7 HOH 110 510 158 HOH HOH A . 
H 7 HOH 111 511 79  HOH HOH A . 
H 7 HOH 112 512 116 HOH HOH A . 
H 7 HOH 113 513 88  HOH HOH A . 
H 7 HOH 114 514 4   HOH HOH A . 
H 7 HOH 115 515 2   HOH HOH A . 
H 7 HOH 116 516 244 HOH HOH A . 
H 7 HOH 117 517 34  HOH HOH A . 
H 7 HOH 118 518 87  HOH HOH A . 
H 7 HOH 119 519 235 HOH HOH A . 
H 7 HOH 120 520 150 HOH HOH A . 
H 7 HOH 121 521 85  HOH HOH A . 
H 7 HOH 122 522 50  HOH HOH A . 
H 7 HOH 123 523 31  HOH HOH A . 
H 7 HOH 124 524 185 HOH HOH A . 
H 7 HOH 125 525 72  HOH HOH A . 
H 7 HOH 126 526 89  HOH HOH A . 
H 7 HOH 127 527 41  HOH HOH A . 
H 7 HOH 128 528 137 HOH HOH A . 
H 7 HOH 129 529 206 HOH HOH A . 
H 7 HOH 130 530 64  HOH HOH A . 
H 7 HOH 131 531 113 HOH HOH A . 
H 7 HOH 132 532 93  HOH HOH A . 
H 7 HOH 133 533 154 HOH HOH A . 
H 7 HOH 134 534 95  HOH HOH A . 
H 7 HOH 135 535 104 HOH HOH A . 
H 7 HOH 136 536 82  HOH HOH A . 
H 7 HOH 137 537 86  HOH HOH A . 
H 7 HOH 138 538 163 HOH HOH A . 
H 7 HOH 139 539 91  HOH HOH A . 
H 7 HOH 140 540 28  HOH HOH A . 
H 7 HOH 141 541 73  HOH HOH A . 
H 7 HOH 142 542 214 HOH HOH A . 
H 7 HOH 143 543 180 HOH HOH A . 
H 7 HOH 144 544 145 HOH HOH A . 
H 7 HOH 145 545 189 HOH HOH A . 
H 7 HOH 146 546 117 HOH HOH A . 
H 7 HOH 147 547 55  HOH HOH A . 
H 7 HOH 148 548 248 HOH HOH A . 
H 7 HOH 149 549 44  HOH HOH A . 
H 7 HOH 150 550 169 HOH HOH A . 
H 7 HOH 151 551 107 HOH HOH A . 
H 7 HOH 152 552 71  HOH HOH A . 
H 7 HOH 153 553 212 HOH HOH A . 
H 7 HOH 154 554 23  HOH HOH A . 
H 7 HOH 155 555 9   HOH HOH A . 
H 7 HOH 156 556 171 HOH HOH A . 
H 7 HOH 157 557 26  HOH HOH A . 
H 7 HOH 158 558 215 HOH HOH A . 
H 7 HOH 159 559 14  HOH HOH A . 
H 7 HOH 160 560 16  HOH HOH A . 
H 7 HOH 161 561 166 HOH HOH A . 
H 7 HOH 162 562 13  HOH HOH A . 
H 7 HOH 163 563 153 HOH HOH A . 
H 7 HOH 164 564 37  HOH HOH A . 
H 7 HOH 165 565 90  HOH HOH A . 
H 7 HOH 166 566 237 HOH HOH A . 
H 7 HOH 167 567 77  HOH HOH A . 
H 7 HOH 168 568 232 HOH HOH A . 
H 7 HOH 169 569 62  HOH HOH A . 
H 7 HOH 170 570 75  HOH HOH A . 
H 7 HOH 171 571 130 HOH HOH A . 
H 7 HOH 172 572 222 HOH HOH A . 
H 7 HOH 173 573 238 HOH HOH A . 
H 7 HOH 174 574 146 HOH HOH A . 
H 7 HOH 175 575 98  HOH HOH A . 
H 7 HOH 176 576 151 HOH HOH A . 
H 7 HOH 177 577 48  HOH HOH A . 
H 7 HOH 178 578 164 HOH HOH A . 
H 7 HOH 179 579 68  HOH HOH A . 
H 7 HOH 180 580 231 HOH HOH A . 
H 7 HOH 181 581 216 HOH HOH A . 
H 7 HOH 182 582 178 HOH HOH A . 
H 7 HOH 183 583 21  HOH HOH A . 
H 7 HOH 184 584 78  HOH HOH A . 
H 7 HOH 185 585 199 HOH HOH A . 
H 7 HOH 186 586 143 HOH HOH A . 
H 7 HOH 187 587 226 HOH HOH A . 
H 7 HOH 188 588 250 HOH HOH A . 
H 7 HOH 189 589 239 HOH HOH A . 
H 7 HOH 190 590 66  HOH HOH A . 
H 7 HOH 191 591 160 HOH HOH A . 
H 7 HOH 192 592 229 HOH HOH A . 
H 7 HOH 193 593 139 HOH HOH A . 
H 7 HOH 194 594 245 HOH HOH A . 
H 7 HOH 195 595 132 HOH HOH A . 
H 7 HOH 196 596 233 HOH HOH A . 
H 7 HOH 197 597 135 HOH HOH A . 
H 7 HOH 198 598 191 HOH HOH A . 
H 7 HOH 199 599 131 HOH HOH A . 
H 7 HOH 200 600 236 HOH HOH A . 
H 7 HOH 201 601 109 HOH HOH A . 
H 7 HOH 202 602 194 HOH HOH A . 
H 7 HOH 203 603 100 HOH HOH A . 
H 7 HOH 204 604 246 HOH HOH A . 
H 7 HOH 205 605 119 HOH HOH A . 
H 7 HOH 206 606 144 HOH HOH A . 
H 7 HOH 207 607 204 HOH HOH A . 
H 7 HOH 208 608 230 HOH HOH A . 
H 7 HOH 209 609 253 HOH HOH A . 
H 7 HOH 210 610 142 HOH HOH A . 
H 7 HOH 211 611 80  HOH HOH A . 
H 7 HOH 212 612 186 HOH HOH A . 
H 7 HOH 213 613 224 HOH HOH A . 
H 7 HOH 214 614 213 HOH HOH A . 
H 7 HOH 215 615 208 HOH HOH A . 
H 7 HOH 216 616 210 HOH HOH A . 
H 7 HOH 217 617 183 HOH HOH A . 
H 7 HOH 218 618 176 HOH HOH A . 
H 7 HOH 219 619 168 HOH HOH A . 
H 7 HOH 220 620 249 HOH HOH A . 
H 7 HOH 221 621 197 HOH HOH A . 
H 7 HOH 222 622 256 HOH HOH A . 
H 7 HOH 223 623 43  HOH HOH A . 
H 7 HOH 224 624 115 HOH HOH A . 
H 7 HOH 225 625 198 HOH HOH A . 
H 7 HOH 226 626 240 HOH HOH A . 
H 7 HOH 227 627 136 HOH HOH A . 
H 7 HOH 228 628 170 HOH HOH A . 
H 7 HOH 229 629 124 HOH HOH A . 
H 7 HOH 230 630 225 HOH HOH A . 
H 7 HOH 231 631 155 HOH HOH A . 
H 7 HOH 232 632 243 HOH HOH A . 
H 7 HOH 233 633 223 HOH HOH A . 
H 7 HOH 234 634 190 HOH HOH A . 
H 7 HOH 235 635 157 HOH HOH A . 
H 7 HOH 236 636 241 HOH HOH A . 
H 7 HOH 237 637 126 HOH HOH A . 
H 7 HOH 238 638 172 HOH HOH A . 
H 7 HOH 239 639 202 HOH HOH A . 
H 7 HOH 240 640 255 HOH HOH A . 
H 7 HOH 241 641 219 HOH HOH A . 
H 7 HOH 242 642 175 HOH HOH A . 
H 7 HOH 243 643 227 HOH HOH A . 
H 7 HOH 244 644 141 HOH HOH A . 
H 7 HOH 245 645 148 HOH HOH A . 
H 7 HOH 246 646 207 HOH HOH A . 
H 7 HOH 247 647 211 HOH HOH A . 
H 7 HOH 248 648 196 HOH HOH A . 
H 7 HOH 249 649 221 HOH HOH A . 
H 7 HOH 250 650 252 HOH HOH A . 
H 7 HOH 251 651 218 HOH HOH A . 
H 7 HOH 252 652 234 HOH HOH A . 
H 7 HOH 253 653 201 HOH HOH A . 
H 7 HOH 254 654 140 HOH HOH A . 
H 7 HOH 255 655 200 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
5  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
6  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
7  1 Y 1 A LYS 213 ? CE  ? A LYS 212 CE  
8  1 Y 1 A LYS 213 ? NZ  ? A LYS 212 NZ  
9  1 Y 1 A LEU 224 ? CD1 ? A LEU 223 CD1 
10 1 Y 1 A LEU 224 ? CD2 ? A LEU 223 CD2 
11 1 Y 1 A GLU 234 ? CD  ? A GLU 233 CD  
12 1 Y 1 A GLU 234 ? OE1 ? A GLU 233 OE1 
13 1 Y 1 A GLU 234 ? OE2 ? A GLU 233 OE2 
14 1 Y 1 A ASN 253 ? CG  ? A ASN 252 CG  
15 1 Y 1 A ASN 253 ? OD1 ? A ASN 252 OD1 
16 1 Y 1 A ASN 253 ? ND2 ? A ASN 252 ND2 
17 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
18 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
19 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
20 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
21 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
22 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
23 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
24 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
25 1 N 1 A MES 303 ? S   ? D MES 1   S   
26 1 N 1 A MES 303 ? O1S ? D MES 1   O1S 
27 1 N 1 A MES 303 ? O2S ? D MES 1   O2S 
28 1 N 1 A MES 303 ? O3S ? D MES 1   O3S 
29 1 N 1 A LML 304 ? CB  ? E LML 1   CB  
30 1 N 1 A LML 304 ? CG  ? E LML 1   CG  
31 1 N 1 A LML 304 ? CD1 ? E LML 1   CD1 
32 1 N 1 A LML 304 ? CD2 ? E LML 1   CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.450 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YHA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.846 
_cell.length_a_esd                 ? 
_cell.length_b                     40.768 
_cell.length_b_esd                 ? 
_cell.length_c                     70.369 
_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                         6YHA 
_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                   6YHA 
_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            2.00 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.43 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-21 
_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   0.976300 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976300 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6YHA 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.250 
_reflns.d_resolution_low                 40.768 
_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                       63270 
_reflns.number_obs                       63270 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.300 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.047 
_reflns.pdbx_netI_over_av_sigmaI         7.900 
_reflns.pdbx_netI_over_sigmaI            10.000 
_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                  0.063 
_reflns.pdbx_Rpim_I_all                  0.034 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         210132 
_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 
1.250 1.320  ? 2.000  29754 ? ? ? 9128 98.100 ? ? ? ? 0.340 ? ? ? ? ? ? ? ? 3.300 0.340 ? ? 3.200  0.453 0.246 ? 1  1 ? ? ? 
1.320 1.400  ? 2.900  28201 ? ? ? 8680 98.800 ? ? ? ? 0.242 ? ? ? ? ? ? ? ? 3.200 0.242 ? ? 4.000  0.324 0.176 ? 2  1 ? ? ? 
1.400 1.490  ? 4.500  26064 ? ? ? 8154 98.300 ? ? ? ? 0.160 ? ? ? ? ? ? ? ? 3.200 0.160 ? ? 5.200  0.220 0.120 ? 3  1 ? ? ? 
1.490 1.610  ? 6.600  25409 ? ? ? 7580 98.600 ? ? ? ? 0.108 ? ? ? ? ? ? ? ? 3.400 0.108 ? ? 7.100  0.151 0.082 ? 4  1 ? ? ? 
1.610 1.770  ? 9.100  24070 ? ? ? 7073 99.200 ? ? ? ? 0.077 ? ? ? ? ? ? ? ? 3.400 0.077 ? ? 9.400  0.110 0.059 ? 5  1 ? ? ? 
1.770 1.980  ? 11.700 21693 ? ? ? 6350 99.200 ? ? ? ? 0.057 ? ? ? ? ? ? ? ? 3.400 0.057 ? ? 13.100 0.081 0.044 ? 6  1 ? ? ? 
1.980 2.280  ? 13.100 19184 ? ? ? 5671 99.500 ? ? ? ? 0.049 ? ? ? ? ? ? ? ? 3.400 0.049 ? ? 16.600 0.069 0.037 ? 7  1 ? ? ? 
2.280 2.800  ? 14.600 16514 ? ? ? 4808 99.500 ? ? ? ? 0.043 ? ? ? ? ? ? ? ? 3.400 0.043 ? ? 19.400 0.059 0.031 ? 8  1 ? ? ? 
2.800 3.950  ? 16.500 12040 ? ? ? 3706 99.000 ? ? ? ? 0.037 ? ? ? ? ? ? ? ? 3.200 0.037 ? ? 22.500 0.048 0.026 ? 9  1 ? ? ? 
3.950 40.768 ? 18.300 7203  ? ? ? 2120 99.600 ? ? ? ? 0.031 ? ? ? ? ? ? ? ? 3.400 0.031 ? ? 24.300 0.040 0.021 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.6000 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.1000 
_refine.aniso_B[2][2]                            -0.8900 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            1.3800 
_refine.B_iso_max                                82.760 
_refine.B_iso_mean                               17.7060 
_refine.B_iso_min                                7.960 
_refine.correlation_coeff_Fo_to_Fc               0.9810 
_refine.correlation_coeff_Fo_to_Fc_free          0.9710 
_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                                 6YHA 
_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                            1.2500 
_refine.ls_d_res_low                             39.2200 
_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                     56853 
_refine.ls_number_reflns_R_free                  6366 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.6900 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1326 
_refine.ls_R_factor_R_free                       0.1708 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1283 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4Q09 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0440 
_refine.pdbx_overall_ESU_R_Free                  0.0460 
_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                       1.2500 
_refine_hist.d_res_low                        39.2200 
_refine_hist.number_atoms_solvent             256 
_refine_hist.number_atoms_total               2331 
_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           25.97 
_refine_hist.pdbx_B_iso_mean_solvent          29.05 
_refine_hist.pdbx_number_atoms_protein        2019 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_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' ? 0.014  0.012  2249 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.135  1.659  3078 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.123  5.000  283  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.643 23.714 105  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.654 15.000 356  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 15.044 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.138  0.200  274  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.020  1777 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 5.486  3.000  2249 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 23.174 5.000  155  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 12.524 5.000  2278 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2500 
_refine_ls_shell.d_res_low                        1.2820 
_refine_ls_shell.number_reflns_all                4623 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             475 
_refine_ls_shell.number_reflns_R_work             4148 
_refine_ls_shell.percent_reflns_obs               98.1700 
_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                  0.2330 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2000 
_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                     6YHA 
_struct.title                        
'Crystal structure of chimeric carbonic anhydrase XII with 2,3,5,6-Tetrafluoro-4-(propylthio)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        6YHA 
_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 6 ? 
H 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              6YHA 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6YHA SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YHA LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YHA THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YHA ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YHA SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YHA ASN A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 570   ? 
1 MORE         7     ? 
1 'SSA (A^2)'  11100 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ASP A 19  ? HIS A 15  ASP A 19  5 ? 5 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? SER A 134 ? ASP A 130 SER A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? ASP A 161 ? LEU A 157 ASP A 162 1 ? 6 
HELX_P HELX_P7 AA7 VAL A 162 ? LYS A 167 ? VAL A 163 LYS A 168 5 ? 6 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.969 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
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 F 3TV . N2 ? ? A ZN  301 A 3TV 305 1_555 ? ? ? ? ? ? ? 1.940 ? ? 
# 
_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_555 104.9 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.2 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.5  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? F 3TV .   ? A 3TV 305 ? 1_555 108.9 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? F 3TV .   ? A 3TV 305 ? 1_555 112.0 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? F 3TV .   ? A 3TV 305 ? 1_555 119.1 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.27 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 11.10 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O THR A 91  ? O THR A 91  N PHE A 70  ? N PHE A 70  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 4  'binding site for residue DMS A 302' 
AC3 Software A MES 303 ? 5  'binding site for residue MES A 303' 
AC4 Software A LML 304 ? 6  'binding site for residue LML A 304' 
AC5 Software A 3TV 305 ? 15 'binding site for residue 3TV A 305' 
AC6 Software A 3TV 306 ? 13 'binding site for residue 3TV A 306' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  3TV F .   ? 3TV A 305 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  HOH H .   ? HOH A 580 . ? 1_555 ? 
9  AC3 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
10 AC3 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
11 AC3 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
12 AC3 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
13 AC3 5  HOH H .   ? HOH A 482 . ? 1_555 ? 
14 AC4 6  HIS A 64  ? HIS A 64  . ? 1_555 ? 
15 AC4 6  LYS A 67  ? LYS A 67  . ? 1_555 ? 
16 AC4 6  3TV F .   ? 3TV A 305 . ? 1_555 ? 
17 AC4 6  HOH H .   ? HOH A 421 . ? 1_555 ? 
18 AC4 6  HOH H .   ? HOH A 440 . ? 1_555 ? 
19 AC4 6  HOH H .   ? HOH A 455 . ? 1_555 ? 
20 AC5 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
21 AC5 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
22 AC5 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
23 AC5 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
24 AC5 15 VAL A 121 ? VAL A 121 . ? 1_555 ? 
25 AC5 15 SER A 134 ? SER A 135 . ? 1_555 ? 
26 AC5 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
27 AC5 15 THR A 198 ? THR A 199 . ? 1_555 ? 
28 AC5 15 THR A 199 ? THR A 200 . ? 1_555 ? 
29 AC5 15 PRO A 200 ? PRO A 201 . ? 1_555 ? 
30 AC5 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
31 AC5 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
32 AC5 15 LML E .   ? LML A 304 . ? 1_555 ? 
33 AC5 15 HOH H .   ? HOH A 575 . ? 1_555 ? 
34 AC5 15 HOH H .   ? HOH A 592 . ? 1_555 ? 
35 AC6 13 HIS A 4   ? HIS A 4   . ? 1_555 ? 
36 AC6 13 TRP A 5   ? TRP A 5   . ? 1_555 ? 
37 AC6 13 HIS A 10  ? HIS A 10  . ? 1_555 ? 
38 AC6 13 ASN A 11  ? ASN A 11  . ? 1_555 ? 
39 AC6 13 HIS A 15  ? HIS A 15  . ? 1_555 ? 
40 AC6 13 TRP A 16  ? TRP A 16  . ? 1_555 ? 
41 AC6 13 ASP A 19  ? ASP A 19  . ? 1_555 ? 
42 AC6 13 ASP A 179 ? ASP A 180 . ? 1_655 ? 
43 AC6 13 ARG A 181 ? ARG A 182 . ? 1_655 ? 
44 AC6 13 GLY A 182 ? GLY A 183 . ? 1_655 ? 
45 AC6 13 HOH H .   ? HOH A 506 . ? 1_555 ? 
46 AC6 13 HOH H .   ? HOH A 519 . ? 1_555 ? 
47 AC6 13 HOH H .   ? HOH A 611 . ? 1_555 ? 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              27 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              27 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              27 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                132.93 
_pdbx_validate_rmsd_angle.angle_target_value         123.60 
_pdbx_validate_rmsd_angle.angle_deviation            9.33 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.40 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -142.33 18.31   
2 1 ASP A 75  ? B -63.71  91.18   
3 1 ALA A 77  ? ? -157.53 89.38   
4 1 LYS A 111 ? ? 75.85   -5.76   
5 1 PHE A 176 ? ? -155.50 77.42   
6 1 ASN A 244 ? ? -93.87  50.48   
7 1 LYS A 252 ? ? 57.44   -137.63 
# 
_pdbx_entry_details.entry_id                 6YHA 
_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_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 
3TV F18  F  N N 1   
3TV C7   C  Y N 2   
3TV C6   C  Y N 3   
3TV F17  F  N N 4   
3TV C8   C  Y N 5   
3TV S11  S  N N 6   
3TV C12  C  N N 7   
3TV C13  C  N N 8   
3TV C14  C  N N 9   
3TV C9   C  Y N 10  
3TV F15  F  N N 11  
3TV C10  C  Y N 12  
3TV F16  F  N N 13  
3TV C5   C  Y N 14  
3TV S1   S  N N 15  
3TV O3   O  N N 16  
3TV O4   O  N N 17  
3TV N2   N  N N 18  
3TV H1   H  N N 19  
3TV H2   H  N N 20  
3TV H3   H  N N 21  
3TV H4   H  N N 22  
3TV H5   H  N N 23  
3TV H6   H  N N 24  
3TV H7   H  N N 25  
3TV H8   H  N N 26  
3TV H9   H  N N 27  
ALA N    N  N N 28  
ALA CA   C  N S 29  
ALA C    C  N N 30  
ALA O    O  N N 31  
ALA CB   C  N N 32  
ALA OXT  O  N N 33  
ALA H    H  N N 34  
ALA H2   H  N N 35  
ALA HA   H  N N 36  
ALA HB1  H  N N 37  
ALA HB2  H  N N 38  
ALA HB3  H  N N 39  
ALA HXT  H  N N 40  
ARG N    N  N N 41  
ARG CA   C  N S 42  
ARG C    C  N N 43  
ARG O    O  N N 44  
ARG CB   C  N N 45  
ARG CG   C  N N 46  
ARG CD   C  N N 47  
ARG NE   N  N N 48  
ARG CZ   C  N N 49  
ARG NH1  N  N N 50  
ARG NH2  N  N N 51  
ARG OXT  O  N N 52  
ARG H    H  N N 53  
ARG H2   H  N N 54  
ARG HA   H  N N 55  
ARG HB2  H  N N 56  
ARG HB3  H  N N 57  
ARG HG2  H  N N 58  
ARG HG3  H  N N 59  
ARG HD2  H  N N 60  
ARG HD3  H  N N 61  
ARG HE   H  N N 62  
ARG HH11 H  N N 63  
ARG HH12 H  N N 64  
ARG HH21 H  N N 65  
ARG HH22 H  N N 66  
ARG HXT  H  N N 67  
ASN N    N  N N 68  
ASN CA   C  N S 69  
ASN C    C  N N 70  
ASN O    O  N N 71  
ASN CB   C  N N 72  
ASN CG   C  N N 73  
ASN OD1  O  N N 74  
ASN ND2  N  N N 75  
ASN OXT  O  N N 76  
ASN H    H  N N 77  
ASN H2   H  N N 78  
ASN HA   H  N N 79  
ASN HB2  H  N N 80  
ASN HB3  H  N N 81  
ASN HD21 H  N N 82  
ASN HD22 H  N N 83  
ASN HXT  H  N N 84  
ASP N    N  N N 85  
ASP CA   C  N S 86  
ASP C    C  N N 87  
ASP O    O  N N 88  
ASP CB   C  N N 89  
ASP CG   C  N N 90  
ASP OD1  O  N N 91  
ASP OD2  O  N N 92  
ASP OXT  O  N N 93  
ASP H    H  N N 94  
ASP H2   H  N N 95  
ASP HA   H  N N 96  
ASP HB2  H  N N 97  
ASP HB3  H  N N 98  
ASP HD2  H  N N 99  
ASP HXT  H  N N 100 
CYS N    N  N N 101 
CYS CA   C  N R 102 
CYS C    C  N N 103 
CYS O    O  N N 104 
CYS CB   C  N N 105 
CYS SG   S  N N 106 
CYS OXT  O  N N 107 
CYS H    H  N N 108 
CYS H2   H  N N 109 
CYS HA   H  N N 110 
CYS HB2  H  N N 111 
CYS HB3  H  N N 112 
CYS HG   H  N N 113 
CYS HXT  H  N N 114 
DMS S    S  N N 115 
DMS O    O  N N 116 
DMS C1   C  N N 117 
DMS C2   C  N N 118 
DMS H11  H  N N 119 
DMS H12  H  N N 120 
DMS H13  H  N N 121 
DMS H21  H  N N 122 
DMS H22  H  N N 123 
DMS H23  H  N N 124 
GLN N    N  N N 125 
GLN CA   C  N S 126 
GLN C    C  N N 127 
GLN O    O  N N 128 
GLN CB   C  N N 129 
GLN CG   C  N N 130 
GLN CD   C  N N 131 
GLN OE1  O  N N 132 
GLN NE2  N  N N 133 
GLN OXT  O  N N 134 
GLN H    H  N N 135 
GLN H2   H  N N 136 
GLN HA   H  N N 137 
GLN HB2  H  N N 138 
GLN HB3  H  N N 139 
GLN HG2  H  N N 140 
GLN HG3  H  N N 141 
GLN HE21 H  N N 142 
GLN HE22 H  N N 143 
GLN HXT  H  N N 144 
GLU N    N  N N 145 
GLU CA   C  N S 146 
GLU C    C  N N 147 
GLU O    O  N N 148 
GLU CB   C  N N 149 
GLU CG   C  N N 150 
GLU CD   C  N N 151 
GLU OE1  O  N N 152 
GLU OE2  O  N N 153 
GLU OXT  O  N N 154 
GLU H    H  N N 155 
GLU H2   H  N N 156 
GLU HA   H  N N 157 
GLU HB2  H  N N 158 
GLU HB3  H  N N 159 
GLU HG2  H  N N 160 
GLU HG3  H  N N 161 
GLU HE2  H  N N 162 
GLU HXT  H  N N 163 
GLY N    N  N N 164 
GLY CA   C  N N 165 
GLY C    C  N N 166 
GLY O    O  N N 167 
GLY OXT  O  N N 168 
GLY H    H  N N 169 
GLY H2   H  N N 170 
GLY HA2  H  N N 171 
GLY HA3  H  N N 172 
GLY HXT  H  N N 173 
HIS N    N  N N 174 
HIS CA   C  N S 175 
HIS C    C  N N 176 
HIS O    O  N N 177 
HIS CB   C  N N 178 
HIS CG   C  Y N 179 
HIS ND1  N  Y N 180 
HIS CD2  C  Y N 181 
HIS CE1  C  Y N 182 
HIS NE2  N  Y N 183 
HIS OXT  O  N N 184 
HIS H    H  N N 185 
HIS H2   H  N N 186 
HIS HA   H  N N 187 
HIS HB2  H  N N 188 
HIS HB3  H  N N 189 
HIS HD1  H  N N 190 
HIS HD2  H  N N 191 
HIS HE1  H  N N 192 
HIS HE2  H  N N 193 
HIS HXT  H  N N 194 
HOH O    O  N N 195 
HOH H1   H  N N 196 
HOH H2   H  N N 197 
ILE N    N  N N 198 
ILE CA   C  N S 199 
ILE C    C  N N 200 
ILE O    O  N N 201 
ILE CB   C  N S 202 
ILE CG1  C  N N 203 
ILE CG2  C  N N 204 
ILE CD1  C  N N 205 
ILE OXT  O  N N 206 
ILE H    H  N N 207 
ILE H2   H  N N 208 
ILE HA   H  N N 209 
ILE HB   H  N N 210 
ILE HG12 H  N N 211 
ILE HG13 H  N N 212 
ILE HG21 H  N N 213 
ILE HG22 H  N N 214 
ILE HG23 H  N N 215 
ILE HD11 H  N N 216 
ILE HD12 H  N N 217 
ILE HD13 H  N N 218 
ILE HXT  H  N N 219 
LEU N    N  N N 220 
LEU CA   C  N S 221 
LEU C    C  N N 222 
LEU O    O  N N 223 
LEU CB   C  N N 224 
LEU CG   C  N N 225 
LEU CD1  C  N N 226 
LEU CD2  C  N N 227 
LEU OXT  O  N N 228 
LEU H    H  N N 229 
LEU H2   H  N N 230 
LEU HA   H  N N 231 
LEU HB2  H  N N 232 
LEU HB3  H  N N 233 
LEU HG   H  N N 234 
LEU HD11 H  N N 235 
LEU HD12 H  N N 236 
LEU HD13 H  N N 237 
LEU HD21 H  N N 238 
LEU HD22 H  N N 239 
LEU HD23 H  N N 240 
LEU HXT  H  N N 241 
LML C1   C  N N 242 
LML O1   O  N N 243 
LML OXT  O  N N 244 
LML CA   C  N N 245 
LML CB   C  N N 246 
LML CG   C  N N 247 
LML CD1  C  N N 248 
LML CD2  C  N N 249 
LML C    C  N N 250 
LML O    O  N N 251 
LML O2   O  N N 252 
LML HXT  H  N N 253 
LML HA   H  N N 254 
LML HB1  H  N N 255 
LML HB2  H  N N 256 
LML HG   H  N N 257 
LML HD11 H  N N 258 
LML HD12 H  N N 259 
LML HD13 H  N N 260 
LML HD21 H  N N 261 
LML HD22 H  N N 262 
LML HD23 H  N N 263 
LML HO2  H  N N 264 
LYS N    N  N N 265 
LYS CA   C  N S 266 
LYS C    C  N N 267 
LYS O    O  N N 268 
LYS CB   C  N N 269 
LYS CG   C  N N 270 
LYS CD   C  N N 271 
LYS CE   C  N N 272 
LYS NZ   N  N N 273 
LYS OXT  O  N N 274 
LYS H    H  N N 275 
LYS H2   H  N N 276 
LYS HA   H  N N 277 
LYS HB2  H  N N 278 
LYS HB3  H  N N 279 
LYS HG2  H  N N 280 
LYS HG3  H  N N 281 
LYS HD2  H  N N 282 
LYS HD3  H  N N 283 
LYS HE2  H  N N 284 
LYS HE3  H  N N 285 
LYS HZ1  H  N N 286 
LYS HZ2  H  N N 287 
LYS HZ3  H  N N 288 
LYS HXT  H  N N 289 
MES O1   O  N N 290 
MES C2   C  N N 291 
MES C3   C  N N 292 
MES N4   N  N N 293 
MES C5   C  N N 294 
MES C6   C  N N 295 
MES C7   C  N N 296 
MES C8   C  N N 297 
MES S    S  N N 298 
MES O1S  O  N N 299 
MES O2S  O  N N 300 
MES O3S  O  N N 301 
MES H21  H  N N 302 
MES H22  H  N N 303 
MES H31  H  N N 304 
MES H32  H  N N 305 
MES HN4  H  N N 306 
MES H51  H  N N 307 
MES H52  H  N N 308 
MES H61  H  N N 309 
MES H62  H  N N 310 
MES H71  H  N N 311 
MES H72  H  N N 312 
MES H81  H  N N 313 
MES H82  H  N N 314 
MET N    N  N N 315 
MET CA   C  N S 316 
MET C    C  N N 317 
MET O    O  N N 318 
MET CB   C  N N 319 
MET CG   C  N N 320 
MET SD   S  N N 321 
MET CE   C  N N 322 
MET OXT  O  N N 323 
MET H    H  N N 324 
MET H2   H  N N 325 
MET HA   H  N N 326 
MET HB2  H  N N 327 
MET HB3  H  N N 328 
MET HG2  H  N N 329 
MET HG3  H  N N 330 
MET HE1  H  N N 331 
MET HE2  H  N N 332 
MET HE3  H  N N 333 
MET HXT  H  N N 334 
PHE N    N  N N 335 
PHE CA   C  N S 336 
PHE C    C  N N 337 
PHE O    O  N N 338 
PHE CB   C  N N 339 
PHE CG   C  Y N 340 
PHE CD1  C  Y N 341 
PHE CD2  C  Y N 342 
PHE CE1  C  Y N 343 
PHE CE2  C  Y N 344 
PHE CZ   C  Y N 345 
PHE OXT  O  N N 346 
PHE H    H  N N 347 
PHE H2   H  N N 348 
PHE HA   H  N N 349 
PHE HB2  H  N N 350 
PHE HB3  H  N N 351 
PHE HD1  H  N N 352 
PHE HD2  H  N N 353 
PHE HE1  H  N N 354 
PHE HE2  H  N N 355 
PHE HZ   H  N N 356 
PHE HXT  H  N N 357 
PRO N    N  N N 358 
PRO CA   C  N S 359 
PRO C    C  N N 360 
PRO O    O  N N 361 
PRO CB   C  N N 362 
PRO CG   C  N N 363 
PRO CD   C  N N 364 
PRO OXT  O  N N 365 
PRO H    H  N N 366 
PRO HA   H  N N 367 
PRO HB2  H  N N 368 
PRO HB3  H  N N 369 
PRO HG2  H  N N 370 
PRO HG3  H  N N 371 
PRO HD2  H  N N 372 
PRO HD3  H  N N 373 
PRO HXT  H  N N 374 
SER N    N  N N 375 
SER CA   C  N S 376 
SER C    C  N N 377 
SER O    O  N N 378 
SER CB   C  N N 379 
SER OG   O  N N 380 
SER OXT  O  N N 381 
SER H    H  N N 382 
SER H2   H  N N 383 
SER HA   H  N N 384 
SER HB2  H  N N 385 
SER HB3  H  N N 386 
SER HG   H  N N 387 
SER HXT  H  N N 388 
THR N    N  N N 389 
THR CA   C  N S 390 
THR C    C  N N 391 
THR O    O  N N 392 
THR CB   C  N R 393 
THR OG1  O  N N 394 
THR CG2  C  N N 395 
THR OXT  O  N N 396 
THR H    H  N N 397 
THR H2   H  N N 398 
THR HA   H  N N 399 
THR HB   H  N N 400 
THR HG1  H  N N 401 
THR HG21 H  N N 402 
THR HG22 H  N N 403 
THR HG23 H  N N 404 
THR HXT  H  N N 405 
TRP N    N  N N 406 
TRP CA   C  N S 407 
TRP C    C  N N 408 
TRP O    O  N N 409 
TRP CB   C  N N 410 
TRP CG   C  Y N 411 
TRP CD1  C  Y N 412 
TRP CD2  C  Y N 413 
TRP NE1  N  Y N 414 
TRP CE2  C  Y N 415 
TRP CE3  C  Y N 416 
TRP CZ2  C  Y N 417 
TRP CZ3  C  Y N 418 
TRP CH2  C  Y N 419 
TRP OXT  O  N N 420 
TRP H    H  N N 421 
TRP H2   H  N N 422 
TRP HA   H  N N 423 
TRP HB2  H  N N 424 
TRP HB3  H  N N 425 
TRP HD1  H  N N 426 
TRP HE1  H  N N 427 
TRP HE3  H  N N 428 
TRP HZ2  H  N N 429 
TRP HZ3  H  N N 430 
TRP HH2  H  N N 431 
TRP HXT  H  N N 432 
TYR N    N  N N 433 
TYR CA   C  N S 434 
TYR C    C  N N 435 
TYR O    O  N N 436 
TYR CB   C  N N 437 
TYR CG   C  Y N 438 
TYR CD1  C  Y N 439 
TYR CD2  C  Y N 440 
TYR CE1  C  Y N 441 
TYR CE2  C  Y N 442 
TYR CZ   C  Y N 443 
TYR OH   O  N N 444 
TYR OXT  O  N N 445 
TYR H    H  N N 446 
TYR H2   H  N N 447 
TYR HA   H  N N 448 
TYR HB2  H  N N 449 
TYR HB3  H  N N 450 
TYR HD1  H  N N 451 
TYR HD2  H  N N 452 
TYR HE1  H  N N 453 
TYR HE2  H  N N 454 
TYR HH   H  N N 455 
TYR HXT  H  N N 456 
VAL N    N  N N 457 
VAL CA   C  N S 458 
VAL C    C  N N 459 
VAL O    O  N N 460 
VAL CB   C  N N 461 
VAL CG1  C  N N 462 
VAL CG2  C  N N 463 
VAL OXT  O  N N 464 
VAL H    H  N N 465 
VAL H2   H  N N 466 
VAL HA   H  N N 467 
VAL HB   H  N N 468 
VAL HG11 H  N N 469 
VAL HG12 H  N N 470 
VAL HG13 H  N N 471 
VAL HG21 H  N N 472 
VAL HG22 H  N N 473 
VAL HG23 H  N N 474 
VAL HXT  H  N N 475 
ZN  ZN   ZN N N 476 
# 
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 
3TV C14 C13  sing N N 1   
3TV C13 C12  sing N N 2   
3TV S11 C12  sing N N 3   
3TV S11 C8   sing N N 4   
3TV F18 C7   sing N N 5   
3TV C8  C7   doub Y N 6   
3TV C8  C9   sing Y N 7   
3TV C7  C6   sing Y N 8   
3TV F15 C9   sing N N 9   
3TV C9  C10  doub Y N 10  
3TV C6  F17  sing N N 11  
3TV C6  C5   doub Y N 12  
3TV C10 C5   sing Y N 13  
3TV C10 F16  sing N N 14  
3TV C5  S1   sing N N 15  
3TV N2  S1   sing N N 16  
3TV S1  O4   doub N N 17  
3TV S1  O3   doub N N 18  
3TV C12 H1   sing N N 19  
3TV C12 H2   sing N N 20  
3TV C13 H3   sing N N 21  
3TV C13 H4   sing N N 22  
3TV C14 H5   sing N N 23  
3TV C14 H6   sing N N 24  
3TV C14 H7   sing N N 25  
3TV N2  H8   sing N N 26  
3TV N2  H9   sing N N 27  
ALA N   CA   sing N N 28  
ALA N   H    sing N N 29  
ALA N   H2   sing N N 30  
ALA CA  C    sing N N 31  
ALA CA  CB   sing N N 32  
ALA CA  HA   sing N N 33  
ALA C   O    doub N N 34  
ALA C   OXT  sing N N 35  
ALA CB  HB1  sing N N 36  
ALA CB  HB2  sing N N 37  
ALA CB  HB3  sing N N 38  
ALA OXT HXT  sing N N 39  
ARG N   CA   sing N N 40  
ARG N   H    sing N N 41  
ARG N   H2   sing N N 42  
ARG CA  C    sing N N 43  
ARG CA  CB   sing N N 44  
ARG CA  HA   sing N N 45  
ARG C   O    doub N N 46  
ARG C   OXT  sing N N 47  
ARG CB  CG   sing N N 48  
ARG CB  HB2  sing N N 49  
ARG CB  HB3  sing N N 50  
ARG CG  CD   sing N N 51  
ARG CG  HG2  sing N N 52  
ARG CG  HG3  sing N N 53  
ARG CD  NE   sing N N 54  
ARG CD  HD2  sing N N 55  
ARG CD  HD3  sing N N 56  
ARG NE  CZ   sing N N 57  
ARG NE  HE   sing N N 58  
ARG CZ  NH1  sing N N 59  
ARG CZ  NH2  doub N N 60  
ARG NH1 HH11 sing N N 61  
ARG NH1 HH12 sing N N 62  
ARG NH2 HH21 sing N N 63  
ARG NH2 HH22 sing N N 64  
ARG OXT HXT  sing N N 65  
ASN N   CA   sing N N 66  
ASN N   H    sing N N 67  
ASN N   H2   sing N N 68  
ASN CA  C    sing N N 69  
ASN CA  CB   sing N N 70  
ASN CA  HA   sing N N 71  
ASN C   O    doub N N 72  
ASN C   OXT  sing N N 73  
ASN CB  CG   sing N N 74  
ASN CB  HB2  sing N N 75  
ASN CB  HB3  sing N N 76  
ASN CG  OD1  doub N N 77  
ASN CG  ND2  sing N N 78  
ASN ND2 HD21 sing N N 79  
ASN ND2 HD22 sing N N 80  
ASN OXT HXT  sing N N 81  
ASP N   CA   sing N N 82  
ASP N   H    sing N N 83  
ASP N   H2   sing N N 84  
ASP CA  C    sing N N 85  
ASP CA  CB   sing N N 86  
ASP CA  HA   sing N N 87  
ASP C   O    doub N N 88  
ASP C   OXT  sing N N 89  
ASP CB  CG   sing N N 90  
ASP CB  HB2  sing N N 91  
ASP CB  HB3  sing N N 92  
ASP CG  OD1  doub N N 93  
ASP CG  OD2  sing N N 94  
ASP OD2 HD2  sing N N 95  
ASP OXT HXT  sing N N 96  
CYS N   CA   sing N N 97  
CYS N   H    sing N N 98  
CYS N   H2   sing N N 99  
CYS CA  C    sing N N 100 
CYS CA  CB   sing N N 101 
CYS CA  HA   sing N N 102 
CYS C   O    doub N N 103 
CYS C   OXT  sing N N 104 
CYS CB  SG   sing N N 105 
CYS CB  HB2  sing N N 106 
CYS CB  HB3  sing N N 107 
CYS SG  HG   sing N N 108 
CYS OXT HXT  sing N N 109 
DMS S   O    doub N N 110 
DMS S   C1   sing N N 111 
DMS S   C2   sing N N 112 
DMS C1  H11  sing N N 113 
DMS C1  H12  sing N N 114 
DMS C1  H13  sing N N 115 
DMS C2  H21  sing N N 116 
DMS C2  H22  sing N N 117 
DMS C2  H23  sing N N 118 
GLN N   CA   sing N N 119 
GLN N   H    sing N N 120 
GLN N   H2   sing N N 121 
GLN CA  C    sing N N 122 
GLN CA  CB   sing N N 123 
GLN CA  HA   sing N N 124 
GLN C   O    doub N N 125 
GLN C   OXT  sing N N 126 
GLN CB  CG   sing N N 127 
GLN CB  HB2  sing N N 128 
GLN CB  HB3  sing N N 129 
GLN CG  CD   sing N N 130 
GLN CG  HG2  sing N N 131 
GLN CG  HG3  sing N N 132 
GLN CD  OE1  doub N N 133 
GLN CD  NE2  sing N N 134 
GLN NE2 HE21 sing N N 135 
GLN NE2 HE22 sing N N 136 
GLN OXT HXT  sing N N 137 
GLU N   CA   sing N N 138 
GLU N   H    sing N N 139 
GLU N   H2   sing N N 140 
GLU CA  C    sing N N 141 
GLU CA  CB   sing N N 142 
GLU CA  HA   sing N N 143 
GLU C   O    doub N N 144 
GLU C   OXT  sing N N 145 
GLU CB  CG   sing N N 146 
GLU CB  HB2  sing N N 147 
GLU CB  HB3  sing N N 148 
GLU CG  CD   sing N N 149 
GLU CG  HG2  sing N N 150 
GLU CG  HG3  sing N N 151 
GLU CD  OE1  doub N N 152 
GLU CD  OE2  sing N N 153 
GLU OE2 HE2  sing N N 154 
GLU OXT HXT  sing N N 155 
GLY N   CA   sing N N 156 
GLY N   H    sing N N 157 
GLY N   H2   sing N N 158 
GLY CA  C    sing N N 159 
GLY CA  HA2  sing N N 160 
GLY CA  HA3  sing N N 161 
GLY C   O    doub N N 162 
GLY C   OXT  sing N N 163 
GLY OXT HXT  sing N N 164 
HIS N   CA   sing N N 165 
HIS N   H    sing N N 166 
HIS N   H2   sing N N 167 
HIS CA  C    sing N N 168 
HIS CA  CB   sing N N 169 
HIS CA  HA   sing N N 170 
HIS C   O    doub N N 171 
HIS C   OXT  sing N N 172 
HIS CB  CG   sing N N 173 
HIS CB  HB2  sing N N 174 
HIS CB  HB3  sing N N 175 
HIS CG  ND1  sing Y N 176 
HIS CG  CD2  doub Y N 177 
HIS ND1 CE1  doub Y N 178 
HIS ND1 HD1  sing N N 179 
HIS CD2 NE2  sing Y N 180 
HIS CD2 HD2  sing N N 181 
HIS CE1 NE2  sing Y N 182 
HIS CE1 HE1  sing N N 183 
HIS NE2 HE2  sing N N 184 
HIS OXT HXT  sing N N 185 
HOH O   H1   sing N N 186 
HOH O   H2   sing N N 187 
ILE N   CA   sing N N 188 
ILE N   H    sing N N 189 
ILE N   H2   sing N N 190 
ILE CA  C    sing N N 191 
ILE CA  CB   sing N N 192 
ILE CA  HA   sing N N 193 
ILE C   O    doub N N 194 
ILE C   OXT  sing N N 195 
ILE CB  CG1  sing N N 196 
ILE CB  CG2  sing N N 197 
ILE CB  HB   sing N N 198 
ILE CG1 CD1  sing N N 199 
ILE CG1 HG12 sing N N 200 
ILE CG1 HG13 sing N N 201 
ILE CG2 HG21 sing N N 202 
ILE CG2 HG22 sing N N 203 
ILE CG2 HG23 sing N N 204 
ILE CD1 HD11 sing N N 205 
ILE CD1 HD12 sing N N 206 
ILE CD1 HD13 sing N N 207 
ILE OXT HXT  sing N N 208 
LEU N   CA   sing N N 209 
LEU N   H    sing N N 210 
LEU N   H2   sing N N 211 
LEU CA  C    sing N N 212 
LEU CA  CB   sing N N 213 
LEU CA  HA   sing N N 214 
LEU C   O    doub N N 215 
LEU C   OXT  sing N N 216 
LEU CB  CG   sing N N 217 
LEU CB  HB2  sing N N 218 
LEU CB  HB3  sing N N 219 
LEU CG  CD1  sing N N 220 
LEU CG  CD2  sing N N 221 
LEU CG  HG   sing N N 222 
LEU CD1 HD11 sing N N 223 
LEU CD1 HD12 sing N N 224 
LEU CD1 HD13 sing N N 225 
LEU CD2 HD21 sing N N 226 
LEU CD2 HD22 sing N N 227 
LEU CD2 HD23 sing N N 228 
LEU OXT HXT  sing N N 229 
LML C1  O1   doub N N 230 
LML C1  OXT  sing N N 231 
LML C1  CA   sing N N 232 
LML OXT HXT  sing N N 233 
LML CA  CB   sing N N 234 
LML CA  C    sing N N 235 
LML CA  HA   sing N N 236 
LML CB  CG   sing N N 237 
LML CB  HB1  sing N N 238 
LML CB  HB2  sing N N 239 
LML CG  CD1  sing N N 240 
LML CG  CD2  sing N N 241 
LML CG  HG   sing N N 242 
LML CD1 HD11 sing N N 243 
LML CD1 HD12 sing N N 244 
LML CD1 HD13 sing N N 245 
LML CD2 HD21 sing N N 246 
LML CD2 HD22 sing N N 247 
LML CD2 HD23 sing N N 248 
LML C   O    doub N N 249 
LML C   O2   sing N N 250 
LML O2  HO2  sing N N 251 
LYS N   CA   sing N N 252 
LYS N   H    sing N N 253 
LYS N   H2   sing N N 254 
LYS CA  C    sing N N 255 
LYS CA  CB   sing N N 256 
LYS CA  HA   sing N N 257 
LYS C   O    doub N N 258 
LYS C   OXT  sing N N 259 
LYS CB  CG   sing N N 260 
LYS CB  HB2  sing N N 261 
LYS CB  HB3  sing N N 262 
LYS CG  CD   sing N N 263 
LYS CG  HG2  sing N N 264 
LYS CG  HG3  sing N N 265 
LYS CD  CE   sing N N 266 
LYS CD  HD2  sing N N 267 
LYS CD  HD3  sing N N 268 
LYS CE  NZ   sing N N 269 
LYS CE  HE2  sing N N 270 
LYS CE  HE3  sing N N 271 
LYS NZ  HZ1  sing N N 272 
LYS NZ  HZ2  sing N N 273 
LYS NZ  HZ3  sing N N 274 
LYS OXT HXT  sing N N 275 
MES O1  C2   sing N N 276 
MES O1  C6   sing N N 277 
MES C2  C3   sing N N 278 
MES C2  H21  sing N N 279 
MES C2  H22  sing N N 280 
MES C3  N4   sing N N 281 
MES C3  H31  sing N N 282 
MES C3  H32  sing N N 283 
MES N4  C5   sing N N 284 
MES N4  C7   sing N N 285 
MES N4  HN4  sing N N 286 
MES C5  C6   sing N N 287 
MES C5  H51  sing N N 288 
MES C5  H52  sing N N 289 
MES C6  H61  sing N N 290 
MES C6  H62  sing N N 291 
MES C7  C8   sing N N 292 
MES C7  H71  sing N N 293 
MES C7  H72  sing N N 294 
MES C8  S    sing N N 295 
MES C8  H81  sing N N 296 
MES C8  H82  sing N N 297 
MES S   O1S  doub N N 298 
MES S   O2S  doub N N 299 
MES S   O3S  sing N N 300 
MET N   CA   sing N N 301 
MET N   H    sing N N 302 
MET N   H2   sing N N 303 
MET CA  C    sing N N 304 
MET CA  CB   sing N N 305 
MET CA  HA   sing N N 306 
MET C   O    doub N N 307 
MET C   OXT  sing N N 308 
MET CB  CG   sing N N 309 
MET CB  HB2  sing N N 310 
MET CB  HB3  sing N N 311 
MET CG  SD   sing N N 312 
MET CG  HG2  sing N N 313 
MET CG  HG3  sing N N 314 
MET SD  CE   sing N N 315 
MET CE  HE1  sing N N 316 
MET CE  HE2  sing N N 317 
MET CE  HE3  sing N N 318 
MET OXT HXT  sing N N 319 
PHE N   CA   sing N N 320 
PHE N   H    sing N N 321 
PHE N   H2   sing N N 322 
PHE CA  C    sing N N 323 
PHE CA  CB   sing N N 324 
PHE CA  HA   sing N N 325 
PHE C   O    doub N N 326 
PHE C   OXT  sing N N 327 
PHE CB  CG   sing N N 328 
PHE CB  HB2  sing N N 329 
PHE CB  HB3  sing N N 330 
PHE CG  CD1  doub Y N 331 
PHE CG  CD2  sing Y N 332 
PHE CD1 CE1  sing Y N 333 
PHE CD1 HD1  sing N N 334 
PHE CD2 CE2  doub Y N 335 
PHE CD2 HD2  sing N N 336 
PHE CE1 CZ   doub Y N 337 
PHE CE1 HE1  sing N N 338 
PHE CE2 CZ   sing Y N 339 
PHE CE2 HE2  sing N N 340 
PHE CZ  HZ   sing N N 341 
PHE OXT HXT  sing N N 342 
PRO N   CA   sing N N 343 
PRO N   CD   sing N N 344 
PRO N   H    sing N N 345 
PRO CA  C    sing N N 346 
PRO CA  CB   sing N N 347 
PRO CA  HA   sing N N 348 
PRO C   O    doub N N 349 
PRO C   OXT  sing N N 350 
PRO CB  CG   sing N N 351 
PRO CB  HB2  sing N N 352 
PRO CB  HB3  sing N N 353 
PRO CG  CD   sing N N 354 
PRO CG  HG2  sing N N 355 
PRO CG  HG3  sing N N 356 
PRO CD  HD2  sing N N 357 
PRO CD  HD3  sing N N 358 
PRO OXT HXT  sing N N 359 
SER N   CA   sing N N 360 
SER N   H    sing N N 361 
SER N   H2   sing N N 362 
SER CA  C    sing N N 363 
SER CA  CB   sing N N 364 
SER CA  HA   sing N N 365 
SER C   O    doub N N 366 
SER C   OXT  sing N N 367 
SER CB  OG   sing N N 368 
SER CB  HB2  sing N N 369 
SER CB  HB3  sing N N 370 
SER OG  HG   sing N N 371 
SER OXT HXT  sing N N 372 
THR N   CA   sing N N 373 
THR N   H    sing N N 374 
THR N   H2   sing N N 375 
THR CA  C    sing N N 376 
THR CA  CB   sing N N 377 
THR CA  HA   sing N N 378 
THR C   O    doub N N 379 
THR C   OXT  sing N N 380 
THR CB  OG1  sing N N 381 
THR CB  CG2  sing N N 382 
THR CB  HB   sing N N 383 
THR OG1 HG1  sing N N 384 
THR CG2 HG21 sing N N 385 
THR CG2 HG22 sing N N 386 
THR CG2 HG23 sing N N 387 
THR OXT HXT  sing N N 388 
TRP N   CA   sing N N 389 
TRP N   H    sing N N 390 
TRP N   H2   sing N N 391 
TRP CA  C    sing N N 392 
TRP CA  CB   sing N N 393 
TRP CA  HA   sing N N 394 
TRP C   O    doub N N 395 
TRP C   OXT  sing N N 396 
TRP CB  CG   sing N N 397 
TRP CB  HB2  sing N N 398 
TRP CB  HB3  sing N N 399 
TRP CG  CD1  doub Y N 400 
TRP CG  CD2  sing Y N 401 
TRP CD1 NE1  sing Y N 402 
TRP CD1 HD1  sing N N 403 
TRP CD2 CE2  doub Y N 404 
TRP CD2 CE3  sing Y N 405 
TRP NE1 CE2  sing Y N 406 
TRP NE1 HE1  sing N N 407 
TRP CE2 CZ2  sing Y N 408 
TRP CE3 CZ3  doub Y N 409 
TRP CE3 HE3  sing N N 410 
TRP CZ2 CH2  doub Y N 411 
TRP CZ2 HZ2  sing N N 412 
TRP CZ3 CH2  sing Y N 413 
TRP CZ3 HZ3  sing N N 414 
TRP CH2 HH2  sing N N 415 
TRP OXT HXT  sing N N 416 
TYR N   CA   sing N N 417 
TYR N   H    sing N N 418 
TYR N   H2   sing N N 419 
TYR CA  C    sing N N 420 
TYR CA  CB   sing N N 421 
TYR CA  HA   sing N N 422 
TYR C   O    doub N N 423 
TYR C   OXT  sing N N 424 
TYR CB  CG   sing N N 425 
TYR CB  HB2  sing N N 426 
TYR CB  HB3  sing N N 427 
TYR CG  CD1  doub Y N 428 
TYR CG  CD2  sing Y N 429 
TYR CD1 CE1  sing Y N 430 
TYR CD1 HD1  sing N N 431 
TYR CD2 CE2  doub Y N 432 
TYR CD2 HD2  sing N N 433 
TYR CE1 CZ   doub Y N 434 
TYR CE1 HE1  sing N N 435 
TYR CE2 CZ   sing Y N 436 
TYR CE2 HE2  sing N N 437 
TYR CZ  OH   sing N N 438 
TYR OH  HH   sing N N 439 
TYR OXT HXT  sing N N 440 
VAL N   CA   sing N N 441 
VAL N   H    sing N N 442 
VAL N   H2   sing N N 443 
VAL CA  C    sing N N 444 
VAL CA  CB   sing N N 445 
VAL CA  HA   sing N N 446 
VAL C   O    doub N N 447 
VAL C   OXT  sing N N 448 
VAL CB  CG1  sing N N 449 
VAL CB  CG2  sing N N 450 
VAL CB  HB   sing N N 451 
VAL CG1 HG11 sing N N 452 
VAL CG1 HG12 sing N N 453 
VAL CG1 HG13 sing N N 454 
VAL CG2 HG21 sing N N 455 
VAL CG2 HG22 sing N N 456 
VAL CG2 HG23 sing N N 457 
VAL OXT HXT  sing N N 458 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        3TV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   3TV 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4Q09 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6YHA 
_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]   0.023897 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005716 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024529 
_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]   0.014612 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 11.587  0.021   7.576   1.00 34.61 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.199  0.202   7.946   1.00 35.03 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.712   -0.872  8.924   1.00 24.81 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 10.147  -2.018  8.814   1.00 27.50 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 9.256   0.404   6.749   1.00 32.03 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 8.431   1.644   6.838   1.00 37.14 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 8.857   2.767   7.520   1.00 14.04 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 7.212   1.943   6.339   1.00 39.94 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 7.936   3.706   7.436   1.00 35.81 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 6.916   3.225   6.717   1.00 48.52 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.859   -0.483  9.874   1.00 19.20 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 8.282   -1.439  10.800  1.00 17.98 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 7.288   -2.326  10.040  1.00 17.46 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.766   -1.923  8.999   1.00 19.95 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.619   -0.765  12.000  1.00 17.77 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.433   0.050   11.627  1.00 16.69 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 6.402   1.386   11.331  1.00 18.84 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 5.070   -0.412  11.595  1.00 15.45 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 5.109   1.771   11.109  1.00 17.44 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 4.260   0.698   11.283  1.00 15.61 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.480   -1.661  11.852  1.00 16.06 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.857   0.603   11.177  1.00 14.99 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 3.108   -1.775  11.684  1.00 13.95 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 2.319   -0.648  11.404  1.00 14.98 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 7.069   -3.523  10.569  1.00 15.97 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 6.070   -4.434  10.010  1.00 17.15 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.785   -5.528  11.005  1.00 15.57 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.740   -5.284  12.228  1.00 14.73 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 5.514   -6.737  10.488  1.00 15.19 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 5.078   -7.835  11.324  1.00 15.31 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.964   -9.047  11.099  1.00 19.85 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.682   -10.086 11.674  1.00 23.01 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.624   -8.202  11.016  1.00 15.47 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.694   -7.134  11.529  1.00 13.18 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 2.309   -7.144  12.862  1.00 12.41 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 2.269   -6.108  10.719  1.00 13.71 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 1.486   -6.143  13.378  1.00 12.92 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 1.389   -5.139  11.187  1.00 13.35 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 1.025   -5.165  12.526  1.00 11.73 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 0.179   -4.202  12.964  1.00 14.16 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 7.049   -8.883  10.352  1.00 19.17 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.959   -9.991  10.086  1.00 25.28 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.940   -10.233 11.234  1.00 20.60 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 9.004   -9.472  12.204  1.00 22.93 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.784   -11.259 11.059  1.00 23.64 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.763  -11.651 12.048  1.00 25.44 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.764  -10.516 12.286  1.00 21.00 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 12.287  -10.402 13.368  1.00 21.54 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.526  -12.868 11.486  1.00 28.58 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.796  -13.221 12.236  1.00 31.97 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 12.084  -9.708  11.275  1.00 21.09 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 13.144  -8.722  11.438  1.00 18.71 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 12.618  -7.305  11.655  1.00 20.98 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 13.451  -6.451  12.030  1.00 21.96 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 14.061  -8.763  10.226  1.00 24.03 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 14.781  -10.069 10.221  1.00 24.88 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 15.868  -10.330 11.072  1.00 28.50 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 14.545  -11.171 9.492   1.00 27.41 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 16.298  -11.557 10.832  1.00 28.30 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 15.478  -12.095 9.858   1.00 23.83 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 11.284  -7.070  11.572  1.00 16.89 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 10.776  -5.707  11.793  1.00 17.71 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 9.455   -5.714  12.548  1.00 14.09 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 8.781   -4.688  12.603  1.00 15.85 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 10.588  -4.910  10.508  1.00 17.27 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 9.582   -5.559  9.562   1.00 20.34 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 9.009   -6.614  9.856   1.00 20.30 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 9.317   -4.912  8.430   1.00 23.56 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 9.140   -6.830  13.216  1.00 15.28 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 7.846   -7.020  13.844  1.00 14.14 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 7.819   -6.486  15.258  1.00 13.12 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 8.723   -5.784  15.699  1.00 13.14 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 6.748   -6.827  15.990  1.00 12.34 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 6.534   -6.286  17.339  1.00 12.92 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 7.718   -6.333  18.277  1.00 12.64 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 7.799   -5.430  19.111  1.00 14.50 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 5.367   -7.139  17.822  1.00 14.85 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 4.553   -7.357  16.565  1.00 14.09 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 5.578   -7.564  15.476  1.00 14.10 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 8.586   -7.351  18.199  1.00 15.03 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 9.667   -7.388  19.176  1.00 17.05 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 10.741  -6.347  18.880  1.00 15.99 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 11.632  -6.105  19.706  1.00 15.50 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 10.228  -8.798  19.224  1.00 19.52 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 9.194   -9.849  19.583  1.00 25.38 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 8.387   -9.697  20.862  1.00 40.55 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 8.955   -9.228  21.905  1.00 47.17 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 7.176   -10.094 20.842  1.00 62.71 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 10.674  -5.768  17.683  1.00 12.70 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 11.674  -4.801  17.237  1.00 12.72 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 11.185  -3.372  17.394  1.00 12.71 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 11.994  -2.453  17.374  1.00 13.29 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 12.002  -4.987  15.740  1.00 12.89 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 12.761  -6.224  15.470  1.00 13.68 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 14.143  -6.225  15.496  1.00 16.81 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 12.310  -7.428  15.095  1.00 16.72 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 14.561  -7.454  15.216  1.00 19.12 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 13.445  -8.198  14.961  1.00 18.80 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 9.870   -3.170  17.592  1.00 12.72 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 9.336   -1.816  17.484  1.00 12.32 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 9.911   -0.864  18.529  1.00 12.19 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 10.004  0.339   18.250  1.00 12.29 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 7.818   -1.877  17.626  1.00 11.20 ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 7.148   -2.567  16.468  1.00 11.38 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 7.648   -2.921  15.242  1.00 11.60 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 5.730   -2.900  16.437  1.00 11.03 ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 6.678   -3.524  14.495  1.00 12.80 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 5.492   -3.493  15.183  1.00 12.29 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 4.689   -2.791  17.381  1.00 11.58 ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 4.241   -3.987  14.815  1.00 11.97 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 3.463   -3.293  17.023  1.00 12.19 ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 3.229   -3.853  15.765  1.00 11.75 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 10.256  -1.376  19.713  1.00 11.96 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 10.726  -0.494  20.768  1.00 12.85 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 11.979  0.282   20.357  1.00 12.71 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 12.227  1.331   20.935  1.00 13.86 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 11.019  -1.274  22.068  1.00 12.88 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 12.228  -2.137  21.989  1.00 14.09 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 13.430  -1.739  22.511  1.00 15.83 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 12.436  -3.315  21.348  1.00 13.96 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 14.346  -2.643  22.174  1.00 14.49 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 13.752  -3.647  21.543  1.00 14.48 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 12.768  -0.217  19.384  1.00 12.40 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 13.997  0.516   19.069  1.00 14.27 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 13.677  1.847   18.374  1.00 13.74 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 14.383  2.804   18.567  1.00 20.66 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 14.827  -0.329  18.103  1.00 13.96 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 15.428  -1.564  18.791  1.00 15.07 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 16.134  -2.524  17.873  1.00 15.37 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 15.223  -3.480  17.169  1.00 15.24 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 15.898  -4.230  16.097  1.00 15.05 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 12.614  1.931   17.580  1.00 13.29 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 12.205  3.213   16.976  1.00 14.95 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 11.174  3.922   17.826  1.00 13.41 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 11.038  5.125   17.698  1.00 17.43 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 11.763  3.052   15.517  1.00 18.30 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 13.004  2.788   14.685  1.00 25.54 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 13.758  3.746   14.495  1.00 22.73 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 13.347  1.571   14.478  1.00 27.54 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 10.402  3.157   18.639  1.00 12.39 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 9.271   3.720   19.364  1.00 13.14 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 9.353   3.226   20.796  1.00 14.19 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 8.731   2.213   21.159  1.00 13.81 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 7.946   3.282   18.710  1.00 14.67 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 7.877   3.681   17.248  1.00 15.99 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 7.541   4.970   16.885  1.00 19.14 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 8.297   2.800   16.278  1.00 18.64 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 7.592   5.326   15.531  1.00 18.69 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 8.354   3.134   14.935  1.00 19.32 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 7.971   4.410   14.566  1.00 19.55 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 10.223  3.825   21.625  1.00 13.83 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 10.524  3.293   22.952  1.00 15.20 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 9.320   3.154   23.886  1.00 13.25 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 9.388   2.389   24.837  1.00 14.41 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 11.553  4.237   23.564  1.00 18.93 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 11.984  5.120   22.461  1.00 23.54 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 11.142  4.903   21.237  1.00 17.19 ? 21  PRO A CD  1 
ATOM   158  N  N   A ILE A 1 22  ? 8.224   3.873   23.580  0.50 12.65 ? 22  ILE A N   1 
ATOM   159  N  N   B ILE A 1 22  ? 8.224   3.872   23.582  0.50 13.19 ? 22  ILE A N   1 
ATOM   160  C  CA  A ILE A 1 22  ? 6.992   3.786   24.345  0.50 12.25 ? 22  ILE A CA  1 
ATOM   161  C  CA  B ILE A 1 22  ? 7.012   3.770   24.374  0.50 13.11 ? 22  ILE A CA  1 
ATOM   162  C  C   A ILE A 1 22  ? 6.420   2.365   24.203  0.50 11.79 ? 22  ILE A C   1 
ATOM   163  C  C   B ILE A 1 22  ? 6.432   2.356   24.220  0.50 12.71 ? 22  ILE A C   1 
ATOM   164  O  O   A ILE A 1 22  ? 5.532   2.010   24.944  0.50 12.40 ? 22  ILE A O   1 
ATOM   165  O  O   B ILE A 1 22  ? 5.541   2.006   24.962  0.50 13.56 ? 22  ILE A O   1 
ATOM   166  C  CB  A ILE A 1 22  ? 5.996   4.875   23.880  0.50 12.86 ? 22  ILE A CB  1 
ATOM   167  C  CB  B ILE A 1 22  ? 5.993   4.858   23.973  0.50 13.65 ? 22  ILE A CB  1 
ATOM   168  C  CG1 A ILE A 1 22  ? 4.932   5.204   24.926  0.50 13.47 ? 22  ILE A CG1 1 
ATOM   169  C  CG1 B ILE A 1 22  ? 4.916   5.041   25.040  0.50 14.98 ? 22  ILE A CG1 1 
ATOM   170  C  CG2 A ILE A 1 22  ? 5.378   4.513   22.548  0.50 12.58 ? 22  ILE A CG2 1 
ATOM   171  C  CG2 B ILE A 1 22  ? 5.384   4.554   22.622  0.50 14.08 ? 22  ILE A CG2 1 
ATOM   172  C  CD1 A ILE A 1 22  ? 4.015   6.344   24.531  0.50 17.63 ? 22  ILE A CD1 1 
ATOM   173  C  CD1 B ILE A 1 22  ? 5.441   5.598   26.345  0.50 15.24 ? 22  ILE A CD1 1 
ATOM   174  N  N   . ALA A 1 23  ? 6.950   1.536   23.290  1.00 12.35 ? 23  ALA A N   1 
ATOM   175  C  CA  . ALA A 1 23  ? 6.545   0.144   23.203  1.00 12.93 ? 23  ALA A CA  1 
ATOM   176  C  C   . ALA A 1 23  ? 6.632   -0.575  24.530  1.00 12.78 ? 23  ALA A C   1 
ATOM   177  O  O   . ALA A 1 23  ? 5.931   -1.586  24.665  1.00 14.94 ? 23  ALA A O   1 
ATOM   178  C  CB  . ALA A 1 23  ? 7.366   -0.581  22.131  1.00 12.72 ? 23  ALA A CB  1 
ATOM   179  N  N   . LYS A 1 24  ? 7.563   -0.174  25.409  1.00 15.32 ? 24  LYS A N   1 
ATOM   180  C  CA  . LYS A 1 24  ? 7.751   -0.784  26.716  1.00 15.82 ? 24  LYS A CA  1 
ATOM   181  C  C   . LYS A 1 24  ? 7.132   0.112   27.787  1.00 15.77 ? 24  LYS A C   1 
ATOM   182  O  O   . LYS A 1 24  ? 7.520   0.032   28.945  1.00 18.60 ? 24  LYS A O   1 
ATOM   183  C  CB  . LYS A 1 24  ? 9.234   -1.037  26.950  1.00 16.31 ? 24  LYS A CB  1 
ATOM   184  C  CG  . LYS A 1 24  ? 9.878   -1.987  25.952  1.00 18.83 ? 24  LYS A CG  1 
ATOM   185  C  CD  . LYS A 1 24  ? 11.390  -2.150  26.281  1.00 23.08 ? 24  LYS A CD  1 
ATOM   186  C  CE  . LYS A 1 24  ? 12.083  -3.225  25.474  1.00 25.48 ? 24  LYS A CE  1 
ATOM   187  N  NZ  . LYS A 1 24  ? 11.526  -4.567  25.725  1.00 33.28 ? 24  LYS A NZ  1 
ATOM   188  N  N   . GLY A 1 25  ? 6.139   0.939   27.409  1.00 15.03 ? 25  GLY A N   1 
ATOM   189  C  CA  . GLY A 1 25  ? 5.474   1.859   28.336  1.00 16.69 ? 25  GLY A CA  1 
ATOM   190  C  C   . GLY A 1 25  ? 4.523   1.179   29.304  1.00 15.11 ? 25  GLY A C   1 
ATOM   191  O  O   . GLY A 1 25  ? 4.407   -0.049  29.323  1.00 16.18 ? 25  GLY A O   1 
ATOM   192  N  N   . GLU A 1 26  ? 3.870   2.032   30.099  1.00 15.24 ? 26  GLU A N   1 
ATOM   193  C  CA  . GLU A 1 26  ? 3.023   1.570   31.168  1.00 15.78 ? 26  GLU A CA  1 
ATOM   194  C  C   . GLU A 1 26  ? 1.587   1.331   30.710  1.00 14.82 ? 26  GLU A C   1 
ATOM   195  O  O   . GLU A 1 26  ? 0.787   0.841   31.505  1.00 15.80 ? 26  GLU A O   1 
ATOM   196  C  CB  . GLU A 1 26  ? 3.071   2.564   32.323  1.00 20.99 ? 26  GLU A CB  1 
ATOM   197  C  CG  . GLU A 1 26  ? 4.483   2.770   32.866  1.00 26.73 ? 26  GLU A CG  1 
ATOM   198  C  CD  . GLU A 1 26  ? 5.158   1.524   33.429  1.00 33.36 ? 26  GLU A CD  1 
ATOM   199  O  OE1 . GLU A 1 26  ? 4.525   0.800   34.230  1.00 38.50 ? 26  GLU A OE1 1 
ATOM   200  O  OE2 . GLU A 1 26  ? 6.363   1.314   33.124  1.00 48.85 ? 26  GLU A OE2 1 
ATOM   201  N  N   . ARG A 1 27  ? 1.220   1.769   29.484  1.00 13.24 ? 27  ARG A N   1 
ATOM   202  C  CA  . ARG A 1 27  ? -0.174  1.600   29.075  1.00 11.79 ? 27  ARG A CA  1 
ATOM   203  C  C   . ARG A 1 27  ? -0.239  1.114   27.623  1.00 11.35 ? 27  ARG A C   1 
ATOM   204  O  O   . ARG A 1 27  ? -0.975  1.673   26.808  1.00 12.30 ? 27  ARG A O   1 
ATOM   205  C  CB  . ARG A 1 27  ? -1.074  2.802   29.310  1.00 16.99 ? 27  ARG A CB  1 
ATOM   206  C  CG  . ARG A 1 27  ? -0.642  4.119   28.712  1.00 21.54 ? 27  ARG A CG  1 
ATOM   207  C  CD  . ARG A 1 27  ? -1.375  5.445   28.995  1.00 35.84 ? 27  ARG A CD  1 
ATOM   208  N  NE  . ARG A 1 27  ? -2.632  5.380   28.267  1.00 28.03 ? 27  ARG A NE  1 
ATOM   209  C  CZ  . ARG A 1 27  ? -3.528  6.309   27.909  1.00 21.70 ? 27  ARG A CZ  1 
ATOM   210  N  NH1 . ARG A 1 27  ? -3.332  7.576   28.229  1.00 13.06 ? 27  ARG A NH1 1 
ATOM   211  N  NH2 . ARG A 1 27  ? -4.610  5.960   27.235  1.00 19.14 ? 27  ARG A NH2 1 
ATOM   212  N  N   . GLN A 1 28  ? 0.456   0.010   27.338  1.00 11.44 ? 28  GLN A N   1 
ATOM   213  C  CA  . GLN A 1 28  ? 0.491   -0.494  25.968  1.00 10.55 ? 28  GLN A CA  1 
ATOM   214  C  C   . GLN A 1 28  ? -0.675  -1.445  25.717  1.00 10.61 ? 28  GLN A C   1 
ATOM   215  O  O   . GLN A 1 28  ? -1.186  -2.102  26.609  1.00 12.11 ? 28  GLN A O   1 
ATOM   216  C  CB  . GLN A 1 28  ? 1.860   -1.160  25.766  1.00 11.30 ? 28  GLN A CB  1 
ATOM   217  C  CG  . GLN A 1 28  ? 2.960   -0.138  25.665  1.00 11.35 ? 28  GLN A CG  1 
ATOM   218  C  CD  . GLN A 1 28  ? 2.852   0.686   24.415  1.00 10.63 ? 28  GLN A CD  1 
ATOM   219  O  OE1 . GLN A 1 28  ? 3.026   0.140   23.309  1.00 11.14 ? 28  GLN A OE1 1 
ATOM   220  N  NE2 . GLN A 1 28  ? 2.489   1.974   24.481  1.00 11.85 ? 28  GLN A NE2 1 
ATOM   221  N  N   . SER A 1 29  ? -1.034  -1.515  24.427  1.00 9.42  ? 29  SER A N   1 
ATOM   222  C  CA  . SER A 1 29  ? -2.113  -2.368  23.943  1.00 9.44  ? 29  SER A CA  1 
ATOM   223  C  C   . SER A 1 29  ? -1.594  -3.219  22.810  1.00 9.49  ? 29  SER A C   1 
ATOM   224  O  O   . SER A 1 29  ? -0.614  -2.884  22.106  1.00 10.44 ? 29  SER A O   1 
ATOM   225  C  CB  . SER A 1 29  ? -3.258  -1.478  23.396  1.00 9.74  ? 29  SER A CB  1 
ATOM   226  O  OG  . SER A 1 29  ? -3.809  -0.804  24.508  1.00 10.05 ? 29  SER A OG  1 
ATOM   227  N  N   . PRO A 1 30  ? -2.239  -4.368  22.502  1.00 9.14  ? 30  PRO A N   1 
ATOM   228  C  CA  . PRO A 1 30  ? -3.411  -4.882  23.242  1.00 9.96  ? 30  PRO A CA  1 
ATOM   229  C  C   . PRO A 1 30  ? -3.013  -5.592  24.543  1.00 10.39 ? 30  PRO A C   1 
ATOM   230  O  O   . PRO A 1 30  ? -1.810  -5.638  24.876  1.00 10.91 ? 30  PRO A O   1 
ATOM   231  C  CB  . PRO A 1 30  ? -3.929  -5.943  22.252  1.00 11.34 ? 30  PRO A CB  1 
ATOM   232  C  CG  . PRO A 1 30  ? -2.645  -6.495  21.632  1.00 10.66 ? 30  PRO A CG  1 
ATOM   233  C  CD  . PRO A 1 30  ? -1.739  -5.275  21.461  1.00 10.55 ? 30  PRO A CD  1 
ATOM   234  N  N   . VAL A 1 31  ? -3.992  -6.110  25.271  1.00 10.40 ? 31  VAL A N   1 
ATOM   235  C  CA  . VAL A 1 31  ? -3.798  -6.860  26.477  1.00 11.74 ? 31  VAL A CA  1 
ATOM   236  C  C   . VAL A 1 31  ? -4.683  -8.106  26.351  1.00 11.59 ? 31  VAL A C   1 
ATOM   237  O  O   . VAL A 1 31  ? -5.649  -8.134  25.620  1.00 11.63 ? 31  VAL A O   1 
ATOM   238  C  CB  . VAL A 1 31  ? -4.128  -6.032  27.733  1.00 12.18 ? 31  VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 31  ? -3.200  -4.812  27.836  1.00 14.10 ? 31  VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 31  ? -5.617  -5.647  27.756  1.00 12.76 ? 31  VAL A CG2 1 
ATOM   241  N  N   . ASP A 1 32  ? -4.372  -9.065  27.213  1.00 12.20 ? 32  ASP A N   1 
ATOM   242  C  CA  . ASP A 1 32  ? -5.301  -10.114 27.531  1.00 11.63 ? 32  ASP A CA  1 
ATOM   243  C  C   . ASP A 1 32  ? -6.347  -9.597  28.489  1.00 12.15 ? 32  ASP A C   1 
ATOM   244  O  O   . ASP A 1 32  ? -6.048  -9.026  29.533  1.00 13.81 ? 32  ASP A O   1 
ATOM   245  C  CB  . ASP A 1 32  ? -4.567  -11.298 28.140  1.00 14.55 ? 32  ASP A CB  1 
ATOM   246  C  CG  . ASP A 1 32  ? -5.520  -12.466 28.405  1.00 15.76 ? 32  ASP A CG  1 
ATOM   247  O  OD1 . ASP A 1 32  ? -6.238  -12.898 27.496  1.00 14.87 ? 32  ASP A OD1 1 
ATOM   248  O  OD2 . ASP A 1 32  ? -5.574  -12.923 29.580  1.00 19.06 ? 32  ASP A OD2 1 
ATOM   249  N  N   . ILE A 1 33  ? -7.600  -9.833  28.130  1.00 12.47 ? 33  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 33  ? -8.720  -9.479  29.002  1.00 12.50 ? 33  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 33  ? -9.032  -10.708 29.861  1.00 13.09 ? 33  ILE A C   1 
ATOM   252  O  O   . ILE A 1 33  ? -9.619  -11.660 29.385  1.00 15.20 ? 33  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 33  ? -9.928  -9.031  28.174  1.00 14.11 ? 33  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 33  ? -9.535  -7.817  27.318  1.00 14.07 ? 33  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 33  ? -11.096 -8.742  29.110  1.00 16.54 ? 33  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 33  ? -10.580 -7.482  26.253  1.00 15.95 ? 33  ILE A CD1 1 
ATOM   257  N  N   . ASP A 1 34  ? -8.671  -10.629 31.147  1.00 16.45 ? 34  ASP A N   1 
ATOM   258  C  CA  . ASP A 1 34  ? -8.979  -11.687 32.104  1.00 18.36 ? 34  ASP A CA  1 
ATOM   259  C  C   . ASP A 1 34  ? -10.379 -11.360 32.617  1.00 17.80 ? 34  ASP A C   1 
ATOM   260  O  O   . ASP A 1 34  ? -10.588 -10.351 33.328  1.00 19.45 ? 34  ASP A O   1 
ATOM   261  C  CB  . ASP A 1 34  ? -7.961  -11.686 33.259  1.00 18.78 ? 34  ASP A CB  1 
ATOM   262  C  CG  . ASP A 1 34  ? -8.184  -12.743 34.348  1.00 24.82 ? 34  ASP A CG  1 
ATOM   263  O  OD1 . ASP A 1 34  ? -9.280  -13.096 34.624  1.00 23.68 ? 34  ASP A OD1 1 
ATOM   264  O  OD2 . ASP A 1 34  ? -7.193  -13.239 34.910  1.00 32.77 ? 34  ASP A OD2 1 
ATOM   265  N  N   . THR A 1 35  ? -11.334 -12.140 32.110  1.00 16.64 ? 35  THR A N   1 
ATOM   266  C  CA  . THR A 1 35  ? -12.729 -11.821 32.344  1.00 19.78 ? 35  THR A CA  1 
ATOM   267  C  C   . THR A 1 35  ? -13.105 -11.941 33.827  1.00 20.13 ? 35  THR A C   1 
ATOM   268  O  O   . THR A 1 35  ? -14.070 -11.322 34.286  1.00 20.64 ? 35  THR A O   1 
ATOM   269  C  CB  . THR A 1 35  ? -13.624 -12.671 31.438  1.00 20.88 ? 35  THR A CB  1 
ATOM   270  O  OG1 . THR A 1 35  ? -13.594 -14.025 31.913  1.00 21.30 ? 35  THR A OG1 1 
ATOM   271  C  CG2 . THR A 1 35  ? -13.348 -12.481 29.953  1.00 25.55 ? 35  THR A CG2 1 
ATOM   272  N  N   . HIS A 1 36  ? -12.304 -12.681 34.619  1.00 21.99 ? 36  HIS A N   1 
ATOM   273  C  CA  . HIS A 1 36  ? -12.534 -12.893 36.048  1.00 22.18 ? 36  HIS A CA  1 
ATOM   274  C  C   . HIS A 1 36  ? -11.872 -11.876 36.991  1.00 29.62 ? 36  HIS A C   1 
ATOM   275  O  O   . HIS A 1 36  ? -11.961 -11.908 38.241  1.00 28.43 ? 36  HIS A O   1 
ATOM   276  C  CB  . HIS A 1 36  ? -11.970 -14.264 36.470  1.00 20.69 ? 36  HIS A CB  1 
ATOM   277  C  CG  . HIS A 1 36  ? -12.433 -15.331 35.578  1.00 23.94 ? 36  HIS A CG  1 
ATOM   278  N  ND1 . HIS A 1 36  ? -13.778 -15.769 35.571  1.00 27.52 ? 36  HIS A ND1 1 
ATOM   279  C  CD2 . HIS A 1 36  ? -11.814 -15.909 34.503  1.00 24.25 ? 36  HIS A CD2 1 
ATOM   280  C  CE1 . HIS A 1 36  ? -13.914 -16.674 34.604  1.00 25.95 ? 36  HIS A CE1 1 
ATOM   281  N  NE2 . HIS A 1 36  ? -12.697 -16.807 33.975  1.00 24.47 ? 36  HIS A NE2 1 
ATOM   282  N  N   . THR A 1 37  ? -10.987 -11.097 36.471  1.00 22.51 ? 37  THR A N   1 
ATOM   283  C  CA  . THR A 1 37  ? -10.442 -10.049 37.295  1.00 23.70 ? 37  THR A CA  1 
ATOM   284  C  C   . THR A 1 37  ? -11.014 -8.710  36.824  1.00 19.29 ? 37  THR A C   1 
ATOM   285  O  O   . THR A 1 37  ? -10.768 -7.700  37.481  1.00 25.80 ? 37  THR A O   1 
ATOM   286  C  CB  . THR A 1 37  ? -8.920  -10.165 37.410  1.00 26.56 ? 37  THR A CB  1 
ATOM   287  O  OG1 . THR A 1 37  ? -8.541  -10.272 36.061  1.00 28.65 ? 37  THR A OG1 1 
ATOM   288  C  CG2 . THR A 1 37  ? -8.518  -11.494 37.988  1.00 27.81 ? 37  THR A CG2 1 
ATOM   289  N  N   . ALA A 1 38  ? -11.641 -8.671  35.626  1.00 19.25 ? 38  ALA A N   1 
ATOM   290  C  CA  . ALA A 1 38  ? -12.229 -7.419  35.187  1.00 18.78 ? 38  ALA A CA  1 
ATOM   291  C  C   . ALA A 1 38  ? -13.295 -7.016  36.203  1.00 19.43 ? 38  ALA A C   1 
ATOM   292  O  O   . ALA A 1 38  ? -13.981 -7.852  36.790  1.00 23.48 ? 38  ALA A O   1 
ATOM   293  C  CB  . ALA A 1 38  ? -12.796 -7.552  33.786  1.00 21.21 ? 38  ALA A CB  1 
ATOM   294  N  N   . LYS A 1 39  ? -13.378 -5.740  36.486  1.00 16.17 ? 39  LYS A N   1 
ATOM   295  C  CA  . LYS A 1 39  ? -14.263 -5.192  37.520  1.00 16.39 ? 39  LYS A CA  1 
ATOM   296  C  C   . LYS A 1 39  ? -15.539 -4.682  36.867  1.00 17.88 ? 39  LYS A C   1 
ATOM   297  O  O   . LYS A 1 39  ? -15.497 -3.710  36.111  1.00 18.13 ? 39  LYS A O   1 
ATOM   298  C  CB  . LYS A 1 39  ? -13.533 -4.000  38.168  1.00 19.78 ? 39  LYS A CB  1 
ATOM   299  C  CG  . LYS A 1 39  ? -14.235 -3.141  39.223  1.00 21.67 ? 39  LYS A CG  1 
ATOM   300  C  CD  . LYS A 1 39  ? -14.643 -3.869  40.493  1.00 22.55 ? 39  LYS A CD  1 
ATOM   301  C  CE  . LYS A 1 39  ? -15.537 -3.042  41.388  1.00 28.36 ? 39  LYS A CE  1 
ATOM   302  N  NZ  . LYS A 1 39  ? -15.910 -3.792  42.611  1.00 26.61 ? 39  LYS A NZ  1 
ATOM   303  N  N   . TYR A 1 40  ? -16.669 -5.296  37.215  1.00 18.91 ? 40  TYR A N   1 
ATOM   304  C  CA  . TYR A 1 40  ? -17.976 -4.801  36.812  1.00 18.88 ? 40  TYR A CA  1 
ATOM   305  C  C   . TYR A 1 40  ? -18.137 -3.434  37.444  1.00 20.17 ? 40  TYR A C   1 
ATOM   306  O  O   . TYR A 1 40  ? -18.069 -3.302  38.671  1.00 21.38 ? 40  TYR A O   1 
ATOM   307  C  CB  . TYR A 1 40  ? -19.123 -5.727  37.228  1.00 23.99 ? 40  TYR A CB  1 
ATOM   308  C  CG  . TYR A 1 40  ? -20.488 -5.104  37.081  1.00 23.93 ? 40  TYR A CG  1 
ATOM   309  C  CD1 . TYR A 1 40  ? -20.939 -4.635  35.842  1.00 24.18 ? 40  TYR A CD1 1 
ATOM   310  C  CD2 . TYR A 1 40  ? -21.373 -5.086  38.167  1.00 33.24 ? 40  TYR A CD2 1 
ATOM   311  C  CE1 . TYR A 1 40  ? -22.198 -4.076  35.702  1.00 27.20 ? 40  TYR A CE1 1 
ATOM   312  C  CE2 . TYR A 1 40  ? -22.654 -4.572  38.021  1.00 30.51 ? 40  TYR A CE2 1 
ATOM   313  C  CZ  . TYR A 1 40  ? -23.061 -4.062  36.794  1.00 28.39 ? 40  TYR A CZ  1 
ATOM   314  O  OH  . TYR A 1 40  ? -24.318 -3.550  36.626  1.00 37.73 ? 40  TYR A OH  1 
ATOM   315  N  N   . ASP A 1 41  ? -18.405 -2.420  36.651  1.00 18.93 ? 41  ASP A N   1 
ATOM   316  C  CA  . ASP A 1 41  ? -18.571 -1.069  37.167  1.00 23.39 ? 41  ASP A CA  1 
ATOM   317  C  C   . ASP A 1 41  ? -19.991 -0.605  36.853  1.00 27.52 ? 41  ASP A C   1 
ATOM   318  O  O   . ASP A 1 41  ? -20.276 -0.193  35.732  1.00 25.28 ? 41  ASP A O   1 
ATOM   319  C  CB  . ASP A 1 41  ? -17.502 -0.106  36.631  1.00 25.25 ? 41  ASP A CB  1 
ATOM   320  C  CG  . ASP A 1 41  ? -17.695 1.292   37.201  1.00 36.20 ? 41  ASP A CG  1 
ATOM   321  O  OD1 . ASP A 1 41  ? -18.722 1.492   37.903  1.00 34.57 ? 41  ASP A OD1 1 
ATOM   322  O  OD2 . ASP A 1 41  ? -16.816 2.179   36.953  1.00 43.92 ? 41  ASP A OD2 1 
ATOM   323  N  N   . PRO A 1 42  ? -20.940 -0.690  37.823  1.00 32.92 ? 42  PRO A N   1 
ATOM   324  C  CA  . PRO A 1 42  ? -22.335 -0.306  37.589  1.00 35.15 ? 42  PRO A CA  1 
ATOM   325  C  C   . PRO A 1 42  ? -22.461 1.180   37.266  1.00 27.85 ? 42  PRO A C   1 
ATOM   326  O  O   . PRO A 1 42  ? -23.473 1.598   36.723  1.00 38.89 ? 42  PRO A O   1 
ATOM   327  C  CB  . PRO A 1 42  ? -23.084 -0.699  38.870  1.00 42.67 ? 42  PRO A CB  1 
ATOM   328  C  CG  . PRO A 1 42  ? -22.121 -1.565  39.663  1.00 47.49 ? 42  PRO A CG  1 
ATOM   329  C  CD  . PRO A 1 42  ? -20.732 -1.178  39.198  1.00 33.41 ? 42  PRO A CD  1 
ATOM   330  N  N   . SER A 1 43  ? -21.408 1.974   37.537  1.00 26.41 ? 43  SER A N   1 
ATOM   331  C  CA  . SER A 1 43  ? -21.484 3.386   37.167  1.00 32.09 ? 43  SER A CA  1 
ATOM   332  C  C   . SER A 1 43  ? -21.189 3.660   35.681  1.00 29.51 ? 43  SER A C   1 
ATOM   333  O  O   . SER A 1 43  ? -21.425 4.785   35.224  1.00 35.41 ? 43  SER A O   1 
ATOM   334  C  CB  . SER A 1 43  ? -20.598 4.216   38.051  1.00 42.66 ? 43  SER A CB  1 
ATOM   335  O  OG  . SER A 1 43  ? -19.249 4.180   37.601  1.00 40.89 ? 43  SER A OG  1 
ATOM   336  N  N   . LEU A 1 44  ? -20.716 2.668   34.901  1.00 31.71 ? 44  LEU A N   1 
ATOM   337  C  CA  . LEU A 1 44  ? -20.418 2.953   33.504  1.00 30.74 ? 44  LEU A CA  1 
ATOM   338  C  C   . LEU A 1 44  ? -21.726 3.124   32.746  1.00 31.10 ? 44  LEU A C   1 
ATOM   339  O  O   . LEU A 1 44  ? -22.701 2.408   32.944  1.00 29.93 ? 44  LEU A O   1 
ATOM   340  C  CB  . LEU A 1 44  ? -19.627 1.835   32.826  1.00 28.03 ? 44  LEU A CB  1 
ATOM   341  C  CG  . LEU A 1 44  ? -18.143 1.697   33.164  1.00 24.18 ? 44  LEU A CG  1 
ATOM   342  C  CD1 . LEU A 1 44  ? -17.713 0.310   32.763  1.00 23.66 ? 44  LEU A CD1 1 
ATOM   343  C  CD2 . LEU A 1 44  ? -17.264 2.736   32.474  1.00 25.84 ? 44  LEU A CD2 1 
ATOM   344  N  N   . LYS A 1 45  ? -21.690 4.027   31.774  1.00 29.56 ? 45  LYS A N   1 
ATOM   345  C  CA  . LYS A 1 45  ? -22.889 4.154   30.944  1.00 26.33 ? 45  LYS A CA  1 
ATOM   346  C  C   . LYS A 1 45  ? -22.927 3.153   29.791  1.00 25.51 ? 45  LYS A C   1 
ATOM   347  O  O   . LYS A 1 45  ? -21.932 2.464   29.442  1.00 27.33 ? 45  LYS A O   1 
ATOM   348  C  CB  . LYS A 1 45  ? -23.092 5.583   30.461  1.00 25.20 ? 45  LYS A CB  1 
ATOM   349  C  CG  . LYS A 1 45  ? -22.934 6.580   31.603  1.00 33.15 ? 45  LYS A CG  1 
ATOM   350  C  CD  . LYS A 1 45  ? -22.487 7.965   31.168  1.00 45.31 ? 45  LYS A CD  1 
ATOM   351  N  N   . PRO A 1 46  ? -24.152 2.949   29.217  1.00 21.21 ? 46  PRO A N   1 
ATOM   352  C  CA  . PRO A 1 46  ? -24.267 2.246   27.945  1.00 21.79 ? 46  PRO A CA  1 
ATOM   353  C  C   . PRO A 1 46  ? -23.429 3.072   26.988  1.00 18.62 ? 46  PRO A C   1 
ATOM   354  O  O   . PRO A 1 46  ? -23.352 4.300   27.064  1.00 20.11 ? 46  PRO A O   1 
ATOM   355  C  CB  . PRO A 1 46  ? -25.763 2.339   27.592  1.00 25.58 ? 46  PRO A CB  1 
ATOM   356  C  CG  . PRO A 1 46  ? -26.414 2.504   28.924  1.00 28.46 ? 46  PRO A CG  1 
ATOM   357  C  CD  . PRO A 1 46  ? -25.465 3.381   29.723  1.00 29.94 ? 46  PRO A CD  1 
ATOM   358  N  N   . LEU A 1 47  ? -22.853 2.336   26.025  1.00 20.53 ? 47  LEU A N   1 
ATOM   359  C  CA  . LEU A 1 47  ? -22.157 3.013   24.972  1.00 19.93 ? 47  LEU A CA  1 
ATOM   360  C  C   . LEU A 1 47  ? -23.235 3.624   24.082  1.00 18.60 ? 47  LEU A C   1 
ATOM   361  O  O   . LEU A 1 47  ? -24.243 2.964   23.870  1.00 24.05 ? 47  LEU A O   1 
ATOM   362  C  CB  . LEU A 1 47  ? -21.417 1.891   24.245  1.00 24.01 ? 47  LEU A CB  1 
ATOM   363  C  CG  . LEU A 1 47  ? -20.227 2.311   23.461  1.00 25.95 ? 47  LEU A CG  1 
ATOM   364  C  CD1 . LEU A 1 47  ? -19.294 3.123   24.369  1.00 26.02 ? 47  LEU A CD1 1 
ATOM   365  C  CD2 . LEU A 1 47  ? -19.618 1.040   22.892  1.00 30.89 ? 47  LEU A CD2 1 
ATOM   366  N  N   . SER A 1 48  ? -22.983 4.845   23.595  1.00 15.52 ? 48  SER A N   1 
ATOM   367  C  CA  . SER A 1 48  ? -23.822 5.447   22.567  1.00 16.09 ? 48  SER A CA  1 
ATOM   368  C  C   . SER A 1 48  ? -23.040 5.404   21.242  1.00 15.48 ? 48  SER A C   1 
ATOM   369  O  O   . SER A 1 48  ? -22.012 6.042   21.106  1.00 16.19 ? 48  SER A O   1 
ATOM   370  C  CB  . SER A 1 48  ? -24.110 6.880   22.956  1.00 18.74 ? 48  SER A CB  1 
ATOM   371  O  OG  . SER A 1 48  ? -24.773 7.557   21.932  1.00 20.88 ? 48  SER A OG  1 
ATOM   372  N  N   . VAL A 1 49  ? -23.493 4.580   20.300  1.00 16.89 ? 49  VAL A N   1 
ATOM   373  C  CA  . VAL A 1 49  ? -22.899 4.500   18.962  1.00 16.70 ? 49  VAL A CA  1 
ATOM   374  C  C   . VAL A 1 49  ? -23.899 5.152   18.015  1.00 16.77 ? 49  VAL A C   1 
ATOM   375  O  O   . VAL A 1 49  ? -24.964 4.588   17.866  1.00 21.76 ? 49  VAL A O   1 
ATOM   376  C  CB  . VAL A 1 49  ? -22.653 3.026   18.596  1.00 19.64 ? 49  VAL A CB  1 
ATOM   377  C  CG1 . VAL A 1 49  ? -22.154 2.936   17.161  1.00 22.06 ? 49  VAL A CG1 1 
ATOM   378  C  CG2 . VAL A 1 49  ? -21.734 2.323   19.599  1.00 20.97 ? 49  VAL A CG2 1 
ATOM   379  N  N   . SER A 1 50  ? -23.559 6.320   17.396  1.00 15.42 ? 50  SER A N   1 
ATOM   380  C  CA  . SER A 1 50  ? -24.522 7.029   16.580  1.00 16.65 ? 50  SER A CA  1 
ATOM   381  C  C   . SER A 1 50  ? -23.932 7.100   15.184  1.00 13.95 ? 50  SER A C   1 
ATOM   382  O  O   . SER A 1 50  ? -23.260 8.068   14.840  1.00 16.59 ? 50  SER A O   1 
ATOM   383  C  CB  . SER A 1 50  ? -24.868 8.423   17.112  1.00 22.09 ? 50  SER A CB  1 
ATOM   384  O  OG  . SER A 1 50  ? -25.429 8.323   18.407  1.00 26.62 ? 50  SER A OG  1 
ATOM   385  N  N   . TYR A 1 51  ? -24.154 6.053   14.385  1.00 15.33 ? 51  TYR A N   1 
ATOM   386  C  CA  . TYR A 1 51  ? -23.525 5.963   13.078  1.00 15.39 ? 51  TYR A CA  1 
ATOM   387  C  C   . TYR A 1 51  ? -24.492 6.229   11.926  1.00 14.87 ? 51  TYR A C   1 
ATOM   388  O  O   . TYR A 1 51  ? -24.104 6.081   10.760  1.00 14.50 ? 51  TYR A O   1 
ATOM   389  C  CB  . TYR A 1 51  ? -22.913 4.570   12.891  1.00 14.66 ? 51  TYR A CB  1 
ATOM   390  C  CG  . TYR A 1 51  ? -21.654 4.287   13.669  1.00 12.62 ? 51  TYR A CG  1 
ATOM   391  C  CD1 . TYR A 1 51  ? -20.940 5.259   14.370  1.00 12.65 ? 51  TYR A CD1 1 
ATOM   392  C  CD2 . TYR A 1 51  ? -21.147 2.993   13.647  1.00 12.95 ? 51  TYR A CD2 1 
ATOM   393  C  CE1 . TYR A 1 51  ? -19.742 4.951   15.015  1.00 12.18 ? 51  TYR A CE1 1 
ATOM   394  C  CE2 . TYR A 1 51  ? -19.925 2.684   14.232  1.00 12.35 ? 51  TYR A CE2 1 
ATOM   395  C  CZ  . TYR A 1 51  ? -19.263 3.661   14.974  1.00 12.89 ? 51  TYR A CZ  1 
ATOM   396  O  OH  . TYR A 1 51  ? -18.107 3.299   15.576  1.00 11.87 ? 51  TYR A OH  1 
ATOM   397  N  N   . ASP A 1 52  ? -25.725 6.707   12.203  1.00 16.91 ? 52  ASP A N   1 
ATOM   398  C  CA  . ASP A 1 52  ? -26.707 6.942   11.127  1.00 17.70 ? 52  ASP A CA  1 
ATOM   399  C  C   . ASP A 1 52  ? -26.271 7.861   9.976   1.00 17.65 ? 52  ASP A C   1 
ATOM   400  O  O   . ASP A 1 52  ? -26.658 7.603   8.824   1.00 20.03 ? 52  ASP A O   1 
ATOM   401  C  CB  . ASP A 1 52  ? -28.049 7.438   11.692  1.00 22.74 ? 52  ASP A CB  1 
ATOM   402  C  CG  . ASP A 1 52  ? -27.918 8.394   12.894  1.00 37.91 ? 52  ASP A CG  1 
ATOM   403  O  OD1 . ASP A 1 52  ? -27.139 8.089   13.934  1.00 38.55 ? 52  ASP A OD1 1 
ATOM   404  O  OD2 . ASP A 1 52  ? -28.555 9.490   12.806  1.00 52.65 ? 52  ASP A OD2 1 
ATOM   405  N  N   . GLN A 1 53  ? -25.509 8.896   10.275  1.00 16.82 ? 53  GLN A N   1 
ATOM   406  C  CA  . GLN A 1 53  ? -25.090 9.801   9.217   1.00 16.09 ? 53  GLN A CA  1 
ATOM   407  C  C   . GLN A 1 53  ? -23.654 9.546   8.758   1.00 14.02 ? 53  GLN A C   1 
ATOM   408  O  O   . GLN A 1 53  ? -23.053 10.425  8.123   1.00 14.66 ? 53  GLN A O   1 
ATOM   409  C  CB  . GLN A 1 53  ? -25.279 11.266  9.662   1.00 17.10 ? 53  GLN A CB  1 
ATOM   410  C  CG  . GLN A 1 53  ? -26.743 11.650  9.917   1.00 19.75 ? 53  GLN A CG  1 
ATOM   411  C  CD  . GLN A 1 53  ? -27.608 11.398  8.704   1.00 22.27 ? 53  GLN A CD  1 
ATOM   412  O  OE1 . GLN A 1 53  ? -28.658 10.727  8.728   1.00 32.83 ? 53  GLN A OE1 1 
ATOM   413  N  NE2 . GLN A 1 53  ? -27.184 11.912  7.569   1.00 19.85 ? 53  GLN A NE2 1 
ATOM   414  N  N   . ALA A 1 54  ? -23.084 8.378   9.039   1.00 14.16 ? 54  ALA A N   1 
ATOM   415  C  CA  . ALA A 1 54  ? -21.713 8.153   8.646   1.00 12.46 ? 54  ALA A CA  1 
ATOM   416  C  C   . ALA A 1 54  ? -21.557 8.287   7.138   1.00 12.76 ? 54  ALA A C   1 
ATOM   417  O  O   . ALA A 1 54  ? -22.432 7.879   6.356   1.00 15.24 ? 54  ALA A O   1 
ATOM   418  C  CB  . ALA A 1 54  ? -21.310 6.770   9.027   1.00 14.08 ? 54  ALA A CB  1 
ATOM   419  N  N   . THR A 1 55  ? -20.408 8.853   6.755   1.00 11.98 ? 55  THR A N   1 
ATOM   420  C  CA  . THR A 1 55  ? -20.077 9.023   5.331   1.00 12.52 ? 55  THR A CA  1 
ATOM   421  C  C   . THR A 1 55  ? -18.720 8.371   5.076   1.00 11.00 ? 55  THR A C   1 
ATOM   422  O  O   . THR A 1 55  ? -17.698 8.984   5.334   1.00 11.57 ? 55  THR A O   1 
ATOM   423  C  CB  . THR A 1 55  ? -20.009 10.518  4.941   1.00 13.19 ? 55  THR A CB  1 
ATOM   424  O  OG1 . THR A 1 55  ? -21.300 11.083  5.123   1.00 14.83 ? 55  THR A OG1 1 
ATOM   425  C  CG2 . THR A 1 55  ? -19.591 10.713  3.495   1.00 13.87 ? 55  THR A CG2 1 
ATOM   426  N  N   . SER A 1 56  ? -18.723 7.139   4.590   1.00 10.77 ? 56  SER A N   1 
ATOM   427  C  CA  . SER A 1 56  ? -17.448 6.576   4.196   1.00 10.86 ? 56  SER A CA  1 
ATOM   428  C  C   . SER A 1 56  ? -16.979 7.253   2.899   1.00 10.65 ? 56  SER A C   1 
ATOM   429  O  O   . SER A 1 56  ? -17.800 7.694   2.081   1.00 11.50 ? 56  SER A O   1 
ATOM   430  C  CB  . SER A 1 56  ? -17.586 5.057   4.017   1.00 11.09 ? 56  SER A CB  1 
ATOM   431  O  OG  . SER A 1 56  ? -18.408 4.738   2.865   1.00 11.59 ? 56  SER A OG  1 
ATOM   432  N  N   . LEU A 1 57  ? -15.651 7.313   2.716   1.00 11.29 ? 57  LEU A N   1 
ATOM   433  C  CA  . LEU A 1 57  ? -15.109 7.981   1.529   1.00 11.64 ? 57  LEU A CA  1 
ATOM   434  C  C   . LEU A 1 57  ? -14.288 7.040   0.666   1.00 11.14 ? 57  LEU A C   1 
ATOM   435  O  O   . LEU A 1 57  ? -14.462 7.027   -0.573  1.00 12.75 ? 57  LEU A O   1 
ATOM   436  C  CB  . LEU A 1 57  ? -14.296 9.210   1.886   1.00 13.77 ? 57  LEU A CB  1 
ATOM   437  C  CG  . LEU A 1 57  ? -15.091 10.351  2.510   1.00 13.87 ? 57  LEU A CG  1 
ATOM   438  C  CD1 . LEU A 1 57  ? -14.134 11.411  3.025   1.00 16.76 ? 57  LEU A CD1 1 
ATOM   439  C  CD2 . LEU A 1 57  ? -16.156 10.920  1.521   1.00 15.70 ? 57  LEU A CD2 1 
ATOM   440  N  N   . ARG A 1 58  ? -13.320 6.308   1.292   1.00 11.32 ? 58  ARG A N   1 
ATOM   441  C  CA  . ARG A 1 58  ? -12.300 5.630   0.496   1.00 12.11 ? 58  ARG A CA  1 
ATOM   442  C  C   . ARG A 1 58  ? -11.868 4.398   1.284   1.00 10.21 ? 58  ARG A C   1 
ATOM   443  O  O   . ARG A 1 58  ? -12.018 4.333   2.509   1.00 11.36 ? 58  ARG A O   1 
ATOM   444  C  CB  . ARG A 1 58  ? -11.083 6.545   0.269   1.00 13.94 ? 58  ARG A CB  1 
ATOM   445  C  CG  . ARG A 1 58  ? -11.373 7.792   -0.586  1.00 20.01 ? 58  ARG A CG  1 
ATOM   446  C  CD  . ARG A 1 58  ? -10.108 8.480   -1.120  1.00 25.38 ? 58  ARG A CD  1 
ATOM   447  N  NE  . ARG A 1 58  ? -9.323  7.570   -1.968  1.00 27.50 ? 58  ARG A NE  1 
ATOM   448  C  CZ  . ARG A 1 58  ? -9.628  7.360   -3.249  1.00 23.84 ? 58  ARG A CZ  1 
ATOM   449  N  NH1 . ARG A 1 58  ? -8.919  6.523   -3.989  1.00 26.43 ? 58  ARG A NH1 1 
ATOM   450  N  NH2 . ARG A 1 58  ? -10.665 8.005   -3.777  1.00 31.02 ? 58  ARG A NH2 1 
ATOM   451  N  N   . ILE A 1 59  ? -11.266 3.451   0.567   1.00 10.32 ? 59  ILE A N   1 
ATOM   452  C  CA  . ILE A 1 59  ? -10.640 2.281   1.206   1.00 10.52 ? 59  ILE A CA  1 
ATOM   453  C  C   . ILE A 1 59  ? -9.212  2.213   0.663   1.00 10.91 ? 59  ILE A C   1 
ATOM   454  O  O   . ILE A 1 59  ? -8.997  2.441   -0.548  1.00 11.07 ? 59  ILE A O   1 
ATOM   455  C  CB  . ILE A 1 59  ? -11.507 1.018   0.973   1.00 10.47 ? 59  ILE A CB  1 
ATOM   456  C  CG1 . ILE A 1 59  ? -10.993 -0.155  1.812   1.00 11.50 ? 59  ILE A CG1 1 
ATOM   457  C  CG2 . ILE A 1 59  ? -11.572 0.665   -0.554  1.00 11.27 ? 59  ILE A CG2 1 
ATOM   458  C  CD1 . ILE A 1 59  ? -11.905 -1.333  1.692   1.00 12.34 ? 59  ILE A CD1 1 
ATOM   459  N  N   . LEU A 1 60  ? -8.238  1.838   1.498   1.00 11.23 ? 60  LEU A N   1 
ATOM   460  C  CA  . LEU A 1 60  ? -6.855  1.814   1.034   1.00 12.17 ? 60  LEU A CA  1 
ATOM   461  C  C   . LEU A 1 60  ? -6.105  0.693   1.729   1.00 10.72 ? 60  LEU A C   1 
ATOM   462  O  O   . LEU A 1 60  ? -6.384  0.340   2.889   1.00 13.31 ? 60  LEU A O   1 
ATOM   463  C  CB  . LEU A 1 60  ? -6.225  3.160   1.271   1.00 16.03 ? 60  LEU A CB  1 
ATOM   464  C  CG  . LEU A 1 60  ? -6.057  3.511   2.711   1.00 16.88 ? 60  LEU A CG  1 
ATOM   465  C  CD1 . LEU A 1 60  ? -4.595  3.562   3.011   1.00 33.43 ? 60  LEU A CD1 1 
ATOM   466  C  CD2 . LEU A 1 60  ? -6.606  4.912   2.967   1.00 34.92 ? 60  LEU A CD2 1 
ATOM   467  N  N   . ASN A 1 61  ? -5.076  0.216   1.061   1.00 10.89 ? 61  ASN A N   1 
ATOM   468  C  CA  . ASN A 1 61  ? -4.095  -0.711  1.597   1.00 11.29 ? 61  ASN A CA  1 
ATOM   469  C  C   . ASN A 1 61  ? -2.873  0.141   1.940   1.00 11.29 ? 61  ASN A C   1 
ATOM   470  O  O   . ASN A 1 61  ? -2.266  0.705   1.055   1.00 12.99 ? 61  ASN A O   1 
ATOM   471  C  CB  . ASN A 1 61  ? -3.772  -1.732  0.520   1.00 11.54 ? 61  ASN A CB  1 
ATOM   472  C  CG  . ASN A 1 61  ? -2.731  -2.724  0.981   1.00 11.31 ? 61  ASN A CG  1 
ATOM   473  O  OD1 . ASN A 1 61  ? -1.865  -2.406  1.802   1.00 13.04 ? 61  ASN A OD1 1 
ATOM   474  N  ND2 . ASN A 1 61  ? -2.727  -3.900  0.383   1.00 13.13 ? 61  ASN A ND2 1 
ATOM   475  N  N   . ASN A 1 62  ? -2.585  0.239   3.244   1.00 11.96 ? 62  ASN A N   1 
ATOM   476  C  CA  . ASN A 1 62  ? -1.457  1.057   3.678   1.00 13.52 ? 62  ASN A CA  1 
ATOM   477  C  C   . ASN A 1 62  ? -0.224  0.207   4.022   1.00 13.40 ? 62  ASN A C   1 
ATOM   478  O  O   . ASN A 1 62  ? 0.764   0.730   4.573   1.00 16.45 ? 62  ASN A O   1 
ATOM   479  C  CB  . ASN A 1 62  ? -1.835  1.892   4.897   1.00 13.86 ? 62  ASN A CB  1 
ATOM   480  C  CG  . ASN A 1 62  ? -2.367  1.052   6.050   1.00 13.28 ? 62  ASN A CG  1 
ATOM   481  O  OD1 . ASN A 1 62  ? -2.015  -0.138  6.156   1.00 12.93 ? 62  ASN A OD1 1 
ATOM   482  N  ND2 . ASN A 1 62  ? -3.199  1.630   6.904   1.00 18.15 ? 62  ASN A ND2 1 
ATOM   483  N  N   . GLY A 1 63  ? -0.223  -1.065  3.666   1.00 13.62 ? 63  GLY A N   1 
ATOM   484  C  CA  . GLY A 1 63  ? 0.972   -1.855  3.879   1.00 15.38 ? 63  GLY A CA  1 
ATOM   485  C  C   . GLY A 1 63  ? 0.952   -2.578  5.213   1.00 14.89 ? 63  GLY A C   1 
ATOM   486  O  O   . GLY A 1 63  ? 1.794   -3.471  5.452   1.00 17.08 ? 63  GLY A O   1 
ATOM   487  N  N   A HIS A 1 64  ? -0.002  -2.233  6.108   0.50 13.19 ? 64  HIS A N   1 
ATOM   488  N  N   B HIS A 1 64  ? 0.025   -2.169  6.083   0.50 14.97 ? 64  HIS A N   1 
ATOM   489  C  CA  A HIS A 1 64  ? -0.124  -2.924  7.395   0.50 13.62 ? 64  HIS A CA  1 
ATOM   490  C  CA  B HIS A 1 64  ? -0.090  -2.869  7.345   0.50 17.26 ? 64  HIS A CA  1 
ATOM   491  C  C   A HIS A 1 64  ? -1.536  -3.411  7.701   0.50 11.88 ? 64  HIS A C   1 
ATOM   492  C  C   B HIS A 1 64  ? -1.460  -3.530  7.475   0.50 14.47 ? 64  HIS A C   1 
ATOM   493  O  O   A HIS A 1 64  ? -1.729  -4.243  8.602   0.50 11.59 ? 64  HIS A O   1 
ATOM   494  O  O   B HIS A 1 64  ? -1.528  -4.652  7.972   0.50 17.81 ? 64  HIS A O   1 
ATOM   495  C  CB  A HIS A 1 64  ? 0.423   -2.117  8.588   0.50 13.58 ? 64  HIS A CB  1 
ATOM   496  C  CB  B HIS A 1 64  ? 0.401   -2.005  8.517   0.50 21.53 ? 64  HIS A CB  1 
ATOM   497  C  CG  A HIS A 1 64  ? -0.070  -0.696  8.716   0.50 11.57 ? 64  HIS A CG  1 
ATOM   498  C  CG  B HIS A 1 64  ? 1.649   -1.209  8.244   0.50 24.48 ? 64  HIS A CG  1 
ATOM   499  N  ND1 A HIS A 1 64  ? 0.590   0.400   8.164   0.50 14.33 ? 64  HIS A ND1 1 
ATOM   500  N  ND1 B HIS A 1 64  ? 2.929   -1.782  8.188   0.50 24.51 ? 64  HIS A ND1 1 
ATOM   501  C  CD2 A HIS A 1 64  ? -1.097  -0.183  9.414   0.50 12.83 ? 64  HIS A CD2 1 
ATOM   502  C  CD2 B HIS A 1 64  ? 1.843   0.119   8.070   0.50 22.61 ? 64  HIS A CD2 1 
ATOM   503  C  CE1 A HIS A 1 64  ? -0.099  1.513   8.443   0.50 14.36 ? 64  HIS A CE1 1 
ATOM   504  C  CE1 B HIS A 1 64  ? 3.838   -0.862  7.966   0.50 26.27 ? 64  HIS A CE1 1 
ATOM   505  N  NE2 A HIS A 1 64  ? -1.130  1.156   9.212   0.50 16.39 ? 64  HIS A NE2 1 
ATOM   506  N  NE2 B HIS A 1 64  ? 3.197   0.327   7.926   0.50 25.88 ? 64  HIS A NE2 1 
ATOM   507  N  N   . SER A 1 65  ? -2.519  -2.862  6.968   1.00 11.93 ? 65  SER A N   1 
ATOM   508  C  CA  . SER A 1 65  ? -3.900  -3.296  7.052   1.00 11.63 ? 65  SER A CA  1 
ATOM   509  C  C   . SER A 1 65  ? -4.587  -2.736  5.794   1.00 10.94 ? 65  SER A C   1 
ATOM   510  O  O   . SER A 1 65  ? -3.959  -2.117  4.940   1.00 13.15 ? 65  SER A O   1 
ATOM   511  C  CB  . SER A 1 65  ? -4.549  -2.761  8.373   1.00 15.01 ? 65  SER A CB  1 
ATOM   512  O  OG  . SER A 1 65  ? -5.848  -3.310  8.502   1.00 15.91 ? 65  SER A OG  1 
ATOM   513  N  N   . PHE A 1 66  ? -5.906  -2.859  5.765   1.00 11.33 ? 66  PHE A N   1 
ATOM   514  C  CA  . PHE A 1 66  ? -6.661  -2.002  4.880   1.00 11.07 ? 66  PHE A CA  1 
ATOM   515  C  C   . PHE A 1 66  ? -7.563  -1.163  5.750   1.00 10.75 ? 66  PHE A C   1 
ATOM   516  O  O   . PHE A 1 66  ? -8.019  -1.574  6.846   1.00 10.81 ? 66  PHE A O   1 
ATOM   517  C  CB  . PHE A 1 66  ? -7.475  -2.782  3.833   1.00 12.59 ? 66  PHE A CB  1 
ATOM   518  C  CG  . PHE A 1 66  ? -8.601  -3.589  4.415   1.00 11.41 ? 66  PHE A CG  1 
ATOM   519  C  CD1 . PHE A 1 66  ? -9.854  -3.027  4.584   1.00 11.79 ? 66  PHE A CD1 1 
ATOM   520  C  CD2 . PHE A 1 66  ? -8.421  -4.915  4.772   1.00 12.40 ? 66  PHE A CD2 1 
ATOM   521  C  CE1 . PHE A 1 66  ? -10.902 -3.759  5.103   1.00 13.15 ? 66  PHE A CE1 1 
ATOM   522  C  CE2 . PHE A 1 66  ? -9.476  -5.643  5.323   1.00 14.47 ? 66  PHE A CE2 1 
ATOM   523  C  CZ  . PHE A 1 66  ? -10.734 -5.063  5.480   1.00 13.59 ? 66  PHE A CZ  1 
ATOM   524  N  N   . LYS A 1 67  ? -7.822  0.083   5.311   1.00 10.46 ? 67  LYS A N   1 
ATOM   525  C  CA  . LYS A 1 67  ? -8.528  1.032   6.135   1.00 11.61 ? 67  LYS A CA  1 
ATOM   526  C  C   . LYS A 1 67  ? -9.628  1.689   5.275   1.00 9.66  ? 67  LYS A C   1 
ATOM   527  O  O   . LYS A 1 67  ? -9.394  2.086   4.129   1.00 12.13 ? 67  LYS A O   1 
ATOM   528  C  CB  . LYS A 1 67  ? -7.523  2.100   6.564   1.00 15.19 ? 67  LYS A CB  1 
ATOM   529  C  CG  . LYS A 1 67  ? -8.113  3.215   7.388   1.00 15.14 ? 67  LYS A CG  1 
ATOM   530  C  CD  . LYS A 1 67  ? -7.120  4.403   7.575   1.00 16.10 ? 67  LYS A CD  1 
ATOM   531  C  CE  . LYS A 1 67  ? -5.855  4.025   8.304   1.00 19.57 ? 67  LYS A CE  1 
ATOM   532  N  NZ  . LYS A 1 67  ? -5.088  5.229   8.731   1.00 21.21 ? 67  LYS A NZ  1 
ATOM   533  N  N   . VAL A 1 68  ? -10.807 1.837   5.903   1.00 9.54  ? 68  VAL A N   1 
ATOM   534  C  CA  . VAL A 1 68  ? -11.883 2.617   5.323   1.00 10.17 ? 68  VAL A CA  1 
ATOM   535  C  C   . VAL A 1 68  ? -11.895 3.945   6.065   1.00 9.32  ? 68  VAL A C   1 
ATOM   536  O  O   . VAL A 1 68  ? -12.045 3.964   7.306   1.00 10.10 ? 68  VAL A O   1 
ATOM   537  C  CB  . VAL A 1 68  ? -13.212 1.878   5.487   1.00 10.12 ? 68  VAL A CB  1 
ATOM   538  C  CG1 . VAL A 1 68  ? -14.393 2.761   5.034   1.00 12.92 ? 68  VAL A CG1 1 
ATOM   539  C  CG2 . VAL A 1 68  ? -13.221 0.574   4.681   1.00 10.96 ? 68  VAL A CG2 1 
ATOM   540  N  N   . GLU A 1 69  ? -11.770 5.018   5.292   1.00 10.51 ? 69  GLU A N   1 
ATOM   541  C  CA  . GLU A 1 69  ? -11.782 6.336   5.852   1.00 10.33 ? 69  GLU A CA  1 
ATOM   542  C  C   . GLU A 1 69  ? -13.107 7.019   5.684   1.00 10.37 ? 69  GLU A C   1 
ATOM   543  O  O   . GLU A 1 69  ? -13.742 6.856   4.643   1.00 11.57 ? 69  GLU A O   1 
ATOM   544  C  CB  . GLU A 1 69  ? -10.667 7.180   5.256   1.00 14.22 ? 69  GLU A CB  1 
ATOM   545  C  CG  . GLU A 1 69  ? -9.305  6.720   5.786   1.00 25.38 ? 69  GLU A CG  1 
ATOM   546  C  CD  . GLU A 1 69  ? -8.054  7.497   5.433   1.00 25.33 ? 69  GLU A CD  1 
ATOM   547  O  OE1 . GLU A 1 69  ? -7.690  7.403   4.291   1.00 32.52 ? 69  GLU A OE1 1 
ATOM   548  O  OE2 . GLU A 1 69  ? -7.403  8.185   6.299   1.00 28.01 ? 69  GLU A OE2 1 
ATOM   549  N  N   . PHE A 1 70  ? -13.486 7.771   6.713   1.00 10.12 ? 70  PHE A N   1 
ATOM   550  C  CA  . PHE A 1 70  ? -14.754 8.480   6.746   1.00 9.74  ? 70  PHE A CA  1 
ATOM   551  C  C   . PHE A 1 70  ? -14.559 9.979   6.654   1.00 10.28 ? 70  PHE A C   1 
ATOM   552  O  O   . PHE A 1 70  ? -13.482 10.520  7.000   1.00 11.63 ? 70  PHE A O   1 
ATOM   553  C  CB  . PHE A 1 70  ? -15.485 8.193   8.058   1.00 10.50 ? 70  PHE A CB  1 
ATOM   554  C  CG  . PHE A 1 70  ? -16.061 6.793   8.043   1.00 9.74  ? 70  PHE A CG  1 
ATOM   555  C  CD1 . PHE A 1 70  ? -15.237 5.711   8.297   1.00 11.27 ? 70  PHE A CD1 1 
ATOM   556  C  CD2 . PHE A 1 70  ? -17.394 6.542   7.740   1.00 10.99 ? 70  PHE A CD2 1 
ATOM   557  C  CE1 . PHE A 1 70  ? -15.707 4.417   8.192   1.00 13.03 ? 70  PHE A CE1 1 
ATOM   558  C  CE2 . PHE A 1 70  ? -17.869 5.260   7.638   1.00 11.24 ? 70  PHE A CE2 1 
ATOM   559  C  CZ  . PHE A 1 70  ? -17.027 4.184   7.890   1.00 12.84 ? 70  PHE A CZ  1 
ATOM   560  N  N   A ASP A 1 71  ? -15.633 10.656  6.213   0.50 11.05 ? 71  ASP A N   1 
ATOM   561  N  N   B ASP A 1 71  ? -15.616 10.694  6.218   0.50 11.70 ? 71  ASP A N   1 
ATOM   562  C  CA  A ASP A 1 71  ? -15.706 12.090  6.367   0.50 11.06 ? 71  ASP A CA  1 
ATOM   563  C  CA  B ASP A 1 71  ? -15.611 12.144  6.280   0.50 11.98 ? 71  ASP A CA  1 
ATOM   564  C  C   A ASP A 1 71  ? -15.901 12.375  7.845   0.50 11.34 ? 71  ASP A C   1 
ATOM   565  C  C   B ASP A 1 71  ? -15.918 12.575  7.708   0.50 12.20 ? 71  ASP A C   1 
ATOM   566  O  O   A ASP A 1 71  ? -16.952 12.127  8.415   0.50 12.92 ? 71  ASP A O   1 
ATOM   567  O  O   B ASP A 1 71  ? -17.086 12.649  8.092   0.50 14.25 ? 71  ASP A O   1 
ATOM   568  C  CB  A ASP A 1 71  ? -16.826 12.649  5.499   0.50 13.02 ? 71  ASP A CB  1 
ATOM   569  C  CB  B ASP A 1 71  ? -16.666 12.709  5.328   0.50 14.25 ? 71  ASP A CB  1 
ATOM   570  C  CG  A ASP A 1 71  ? -16.776 14.164  5.451   0.50 15.81 ? 71  ASP A CG  1 
ATOM   571  C  CG  B ASP A 1 71  ? -16.913 14.189  5.580   0.50 18.89 ? 71  ASP A CG  1 
ATOM   572  O  OD1 A ASP A 1 71  ? -16.276 14.738  6.458   0.50 14.92 ? 71  ASP A OD1 1 
ATOM   573  O  OD1 B ASP A 1 71  ? -15.910 14.844  6.028   0.50 13.58 ? 71  ASP A OD1 1 
ATOM   574  O  OD2 A ASP A 1 71  ? -17.246 14.785  4.440   0.50 13.20 ? 71  ASP A OD2 1 
ATOM   575  O  OD2 B ASP A 1 71  ? -18.100 14.697  5.345   0.50 21.16 ? 71  ASP A OD2 1 
ATOM   576  N  N   . ASP A 1 72  ? -14.870 12.898  8.463   1.00 11.00 ? 72  ASP A N   1 
ATOM   577  C  CA  . ASP A 1 72  ? -14.968 13.294  9.867   1.00 12.30 ? 72  ASP A CA  1 
ATOM   578  C  C   . ASP A 1 72  ? -14.835 14.804  10.052  1.00 11.98 ? 72  ASP A C   1 
ATOM   579  O  O   . ASP A 1 72  ? -14.474 15.265  11.133  1.00 14.30 ? 72  ASP A O   1 
ATOM   580  C  CB  . ASP A 1 72  ? -13.881 12.561  10.665  1.00 12.09 ? 72  ASP A CB  1 
ATOM   581  C  CG  . ASP A 1 72  ? -12.453 12.902  10.294  1.00 13.50 ? 72  ASP A CG  1 
ATOM   582  O  OD1 . ASP A 1 72  ? -12.285 13.626  9.275   1.00 15.35 ? 72  ASP A OD1 1 
ATOM   583  O  OD2 . ASP A 1 72  ? -11.541 12.398  10.989  1.00 14.44 ? 72  ASP A OD2 1 
ATOM   584  N  N   . SER A 1 73  ? -15.231 15.535  9.021   1.00 13.14 ? 73  SER A N   1 
ATOM   585  C  CA  . SER A 1 73  ? -15.201 16.990  9.078   1.00 14.07 ? 73  SER A CA  1 
ATOM   586  C  C   . SER A 1 73  ? -16.477 17.601  9.663   1.00 15.74 ? 73  SER A C   1 
ATOM   587  O  O   . SER A 1 73  ? -16.572 18.817  9.766   1.00 16.83 ? 73  SER A O   1 
ATOM   588  C  CB  . SER A 1 73  ? -14.916 17.536  7.695   1.00 16.53 ? 73  SER A CB  1 
ATOM   589  O  OG  . SER A 1 73  ? -16.075 17.428  6.859   1.00 16.01 ? 73  SER A OG  1 
ATOM   590  N  N   . GLN A 1 74  ? -17.456 16.789  10.030  1.00 15.10 ? 74  GLN A N   1 
ATOM   591  C  CA  . GLN A 1 74  ? -18.653 17.256  10.698  1.00 18.56 ? 74  GLN A CA  1 
ATOM   592  C  C   . GLN A 1 74  ? -19.048 16.219  11.711  1.00 18.03 ? 74  GLN A C   1 
ATOM   593  O  O   . GLN A 1 74  ? -18.555 15.127  11.666  1.00 16.72 ? 74  GLN A O   1 
ATOM   594  C  CB  . GLN A 1 74  ? -19.860 17.331  9.735   1.00 24.73 ? 74  GLN A CB  1 
ATOM   595  C  CG  . GLN A 1 74  ? -19.707 18.308  8.604   1.00 30.32 ? 74  GLN A CG  1 
ATOM   596  C  CD  . GLN A 1 74  ? -20.210 17.819  7.257   1.00 32.70 ? 74  GLN A CD  1 
ATOM   597  O  OE1 . GLN A 1 74  ? -21.405 17.661  7.070   1.00 28.15 ? 74  GLN A OE1 1 
ATOM   598  N  NE2 . GLN A 1 74  ? -19.298 17.644  6.284   1.00 27.52 ? 74  GLN A NE2 1 
ATOM   599  N  N   A ASP A 1 75  ? -19.961 16.519  12.656  0.50 23.25 ? 75  ASP A N   1 
ATOM   600  N  N   B ASP A 1 75  ? -20.025 16.647  12.502  0.50 20.04 ? 75  ASP A N   1 
ATOM   601  C  CA  A ASP A 1 75  ? -20.316 15.555  13.700  0.50 26.67 ? 75  ASP A CA  1 
ATOM   602  C  CA  B ASP A 1 75  ? -20.736 15.875  13.484  0.50 21.39 ? 75  ASP A CA  1 
ATOM   603  C  C   A ASP A 1 75  ? -21.392 14.592  13.153  0.50 23.10 ? 75  ASP A C   1 
ATOM   604  C  C   B ASP A 1 75  ? -21.484 14.772  12.706  0.50 20.68 ? 75  ASP A C   1 
ATOM   605  O  O   A ASP A 1 75  ? -22.595 14.766  13.350  0.50 22.71 ? 75  ASP A O   1 
ATOM   606  O  O   B ASP A 1 75  ? -22.578 15.073  12.258  0.50 16.46 ? 75  ASP A O   1 
ATOM   607  C  CB  A ASP A 1 75  ? -20.712 16.244  15.018  0.50 31.14 ? 75  ASP A CB  1 
ATOM   608  C  CB  B ASP A 1 75  ? -21.562 16.913  14.284  0.50 17.56 ? 75  ASP A CB  1 
ATOM   609  C  CG  A ASP A 1 75  ? -19.755 16.202  16.216  0.50 32.03 ? 75  ASP A CG  1 
ATOM   610  C  CG  B ASP A 1 75  ? -22.159 16.282  15.537  0.50 20.57 ? 75  ASP A CG  1 
ATOM   611  O  OD1 A ASP A 1 75  ? -18.987 15.175  16.386  0.50 18.60 ? 75  ASP A OD1 1 
ATOM   612  O  OD1 B ASP A 1 75  ? -21.773 15.094  15.842  0.50 19.73 ? 75  ASP A OD1 1 
ATOM   613  O  OD2 A ASP A 1 75  ? -19.840 17.167  17.052  0.50 39.10 ? 75  ASP A OD2 1 
ATOM   614  O  OD2 B ASP A 1 75  ? -22.983 16.958  16.199  0.50 25.70 ? 75  ASP A OD2 1 
ATOM   615  N  N   . LYS A 1 76  ? -20.939 13.541  12.467  1.00 18.48 ? 76  LYS A N   1 
ATOM   616  C  CA  . LYS A 1 76  ? -21.698 12.581  11.628  1.00 25.09 ? 76  LYS A CA  1 
ATOM   617  C  C   . LYS A 1 76  ? -21.908 11.114  12.082  1.00 28.69 ? 76  LYS A C   1 
ATOM   618  O  O   . LYS A 1 76  ? -22.803 10.422  11.585  1.00 40.80 ? 76  LYS A O   1 
ATOM   619  C  CB  . LYS A 1 76  ? -21.064 12.422  10.239  1.00 26.09 ? 76  LYS A CB  1 
ATOM   620  C  CG  . LYS A 1 76  ? -21.382 13.503  9.241   1.00 31.25 ? 76  LYS A CG  1 
ATOM   621  C  CD  . LYS A 1 76  ? -20.741 13.227  7.928   1.00 28.37 ? 76  LYS A CD  1 
ATOM   622  C  CE  . LYS A 1 76  ? -21.629 13.926  6.913   1.00 31.44 ? 76  LYS A CE  1 
ATOM   623  N  NZ  . LYS A 1 76  ? -21.068 13.843  5.565   1.00 36.94 ? 76  LYS A NZ  1 
ATOM   624  N  N   . ALA A 1 77  ? -21.013 10.563  12.851  1.00 21.18 ? 77  ALA A N   1 
ATOM   625  C  CA  . ALA A 1 77  ? -20.761 9.153   13.272  1.00 17.25 ? 77  ALA A CA  1 
ATOM   626  C  C   . ALA A 1 77  ? -19.967 9.252   14.569  1.00 15.74 ? 77  ALA A C   1 
ATOM   627  O  O   . ALA A 1 77  ? -18.765 9.419   14.585  1.00 22.46 ? 77  ALA A O   1 
ATOM   628  C  CB  . ALA A 1 77  ? -19.951 8.433   12.226  1.00 17.04 ? 77  ALA A CB  1 
ATOM   629  N  N   . VAL A 1 78  ? -20.668 9.307   15.686  1.00 14.76 ? 78  VAL A N   1 
ATOM   630  C  CA  . VAL A 1 78  ? -20.008 9.670   16.921  1.00 17.33 ? 78  VAL A CA  1 
ATOM   631  C  C   . VAL A 1 78  ? -20.260 8.580   17.972  1.00 15.34 ? 78  VAL A C   1 
ATOM   632  O  O   . VAL A 1 78  ? -21.261 7.855   17.992  1.00 16.87 ? 78  VAL A O   1 
ATOM   633  C  CB  . VAL A 1 78  ? -20.407 11.064  17.409  1.00 23.00 ? 78  VAL A CB  1 
ATOM   634  C  CG1 . VAL A 1 78  ? -20.207 12.153  16.393  1.00 28.74 ? 78  VAL A CG1 1 
ATOM   635  C  CG2 . VAL A 1 78  ? -21.832 11.007  17.785  1.00 26.81 ? 78  VAL A CG2 1 
ATOM   636  N  N   . LEU A 1 79  ? -19.219 8.399   18.771  1.00 14.60 ? 79  LEU A N   1 
ATOM   637  C  CA  . LEU A 1 79  ? -19.215 7.537   19.946  1.00 13.55 ? 79  LEU A CA  1 
ATOM   638  C  C   . LEU A 1 79  ? -19.192 8.424   21.182  1.00 15.61 ? 79  LEU A C   1 
ATOM   639  O  O   . LEU A 1 79  ? -18.348 9.316   21.315  1.00 15.85 ? 79  LEU A O   1 
ATOM   640  C  CB  . LEU A 1 79  ? -17.959 6.668   19.850  1.00 14.94 ? 79  LEU A CB  1 
ATOM   641  C  CG  . LEU A 1 79  ? -17.776 5.574   20.915  1.00 15.60 ? 79  LEU A CG  1 
ATOM   642  C  CD1 . LEU A 1 79  ? -18.771 4.449   20.748  1.00 20.90 ? 79  LEU A CD1 1 
ATOM   643  C  CD2 . LEU A 1 79  ? -16.399 5.018   20.773  1.00 17.08 ? 79  LEU A CD2 1 
ATOM   644  N  N   . LYS A 1 80  ? -20.054 8.104   22.128  1.00 15.43 ? 80  LYS A N   1 
ATOM   645  C  CA  . LYS A 1 80  ? -20.003 8.785   23.421  1.00 17.55 ? 80  LYS A CA  1 
ATOM   646  C  C   . LYS A 1 80  ? -20.523 7.837   24.493  1.00 16.77 ? 80  LYS A C   1 
ATOM   647  O  O   . LYS A 1 80  ? -20.847 6.702   24.200  1.00 15.79 ? 80  LYS A O   1 
ATOM   648  C  CB  . LYS A 1 80  ? -20.731 10.124  23.396  1.00 21.44 ? 80  LYS A CB  1 
ATOM   649  C  CG  . LYS A 1 80  ? -22.205 10.005  23.129  1.00 24.03 ? 80  LYS A CG  1 
ATOM   650  C  CD  . LYS A 1 80  ? -22.901 11.374  23.058  1.00 33.22 ? 80  LYS A CD  1 
ATOM   651  C  CE  . LYS A 1 80  ? -24.412 11.300  23.202  1.00 49.21 ? 80  LYS A CE  1 
ATOM   652  N  N   . GLY A 1 81  ? -20.584 8.311   25.745  1.00 19.77 ? 81  GLY A N   1 
ATOM   653  C  CA  . GLY A 1 81  ? -21.146 7.505   26.802  1.00 21.76 ? 81  GLY A CA  1 
ATOM   654  C  C   . GLY A 1 81  ? -20.117 6.465   27.220  1.00 20.77 ? 81  GLY A C   1 
ATOM   655  O  O   . GLY A 1 81  ? -18.906 6.635   26.982  1.00 18.27 ? 81  GLY A O   1 
ATOM   656  N  N   . GLY A 1 82  ? -20.608 5.367   27.801  1.00 23.72 ? 82  GLY A N   1 
ATOM   657  C  CA  . GLY A 1 82  ? -19.646 4.374   28.250  1.00 25.29 ? 82  GLY A CA  1 
ATOM   658  C  C   . GLY A 1 82  ? -18.675 5.007   29.227  1.00 23.64 ? 82  GLY A C   1 
ATOM   659  O  O   . GLY A 1 82  ? -19.074 5.734   30.128  1.00 26.07 ? 82  GLY A O   1 
ATOM   660  N  N   . PRO A 1 83  ? -17.366 4.772   29.091  1.00 19.83 ? 83  PRO A N   1 
ATOM   661  C  CA  . PRO A 1 83  ? -16.381 5.334   29.996  1.00 20.54 ? 83  PRO A CA  1 
ATOM   662  C  C   . PRO A 1 83  ? -15.996 6.740   29.577  1.00 20.40 ? 83  PRO A C   1 
ATOM   663  O  O   . PRO A 1 83  ? -15.193 7.380   30.244  1.00 24.21 ? 83  PRO A O   1 
ATOM   664  C  CB  . PRO A 1 83  ? -15.168 4.418   29.832  1.00 19.37 ? 83  PRO A CB  1 
ATOM   665  C  CG  . PRO A 1 83  ? -15.262 4.065   28.325  1.00 18.93 ? 83  PRO A CG  1 
ATOM   666  C  CD  . PRO A 1 83  ? -16.759 3.874   28.081  1.00 19.17 ? 83  PRO A CD  1 
ATOM   667  N  N   . LEU A 1 84  ? -16.546 7.215   28.450  1.00 16.81 ? 84  LEU A N   1 
ATOM   668  C  CA  . LEU A 1 84  ? -15.929 8.393   27.859  1.00 17.21 ? 84  LEU A CA  1 
ATOM   669  C  C   . LEU A 1 84  ? -16.534 9.691   28.362  1.00 17.66 ? 84  LEU A C   1 
ATOM   670  O  O   . LEU A 1 84  ? -17.731 9.760   28.600  1.00 19.25 ? 84  LEU A O   1 
ATOM   671  C  CB  . LEU A 1 84  ? -16.194 8.424   26.349  1.00 16.68 ? 84  LEU A CB  1 
ATOM   672  C  CG  . LEU A 1 84  ? -15.718 7.191   25.604  1.00 13.81 ? 84  LEU A CG  1 
ATOM   673  C  CD1 . LEU A 1 84  ? -16.206 7.173   24.187  1.00 15.48 ? 84  LEU A CD1 1 
ATOM   674  C  CD2 . LEU A 1 84  ? -14.211 7.062   25.646  1.00 14.23 ? 84  LEU A CD2 1 
ATOM   675  N  N   . ASP A 1 85  ? -15.687 10.726  28.404  1.00 20.31 ? 85  ASP A N   1 
ATOM   676  C  CA  . ASP A 1 85  ? -16.167 12.071  28.710  1.00 21.24 ? 85  ASP A CA  1 
ATOM   677  C  C   . ASP A 1 85  ? -16.228 12.810  27.379  1.00 20.81 ? 85  ASP A C   1 
ATOM   678  O  O   . ASP A 1 85  ? -15.278 12.723  26.584  1.00 25.28 ? 85  ASP A O   1 
ATOM   679  C  CB  . ASP A 1 85  ? -15.217 12.776  29.697  1.00 25.40 ? 85  ASP A CB  1 
ATOM   680  C  CG  . ASP A 1 85  ? -15.337 12.232  31.111  1.00 29.09 ? 85  ASP A CG  1 
ATOM   681  O  OD1 . ASP A 1 85  ? -16.494 11.993  31.534  1.00 38.37 ? 85  ASP A OD1 1 
ATOM   682  O  OD2 . ASP A 1 85  ? -14.273 12.016  31.769  1.00 32.33 ? 85  ASP A OD2 1 
ATOM   683  N  N   . GLY A 1 86  ? -17.305 13.527  27.099  1.00 23.21 ? 86  GLY A N   1 
ATOM   684  C  CA  . GLY A 1 86  ? -17.299 14.201  25.803  1.00 22.70 ? 86  GLY A CA  1 
ATOM   685  C  C   . GLY A 1 86  ? -17.711 13.307  24.619  1.00 23.07 ? 86  GLY A C   1 
ATOM   686  O  O   . GLY A 1 86  ? -18.346 12.261  24.775  1.00 27.31 ? 86  GLY A O   1 
ATOM   687  N  N   A THR A 1 87  ? -17.283 13.700  23.408  0.50 22.51 ? 87  THR A N   1 
ATOM   688  N  N   B THR A 1 87  ? -17.343 13.718  23.408  0.50 19.88 ? 87  THR A N   1 
ATOM   689  C  CA  A THR A 1 87  ? -17.753 13.162  22.130  0.50 19.53 ? 87  THR A CA  1 
ATOM   690  C  CA  B THR A 1 87  ? -17.782 13.011  22.214  0.50 15.58 ? 87  THR A CA  1 
ATOM   691  C  C   A THR A 1 87  ? -16.579 12.760  21.238  0.50 18.40 ? 87  THR A C   1 
ATOM   692  C  C   B THR A 1 87  ? -16.587 12.715  21.312  0.50 15.47 ? 87  THR A C   1 
ATOM   693  O  O   A THR A 1 87  ? -15.639 13.540  21.070  0.50 18.79 ? 87  THR A O   1 
ATOM   694  O  O   B THR A 1 87  ? -15.641 13.505  21.235  0.50 14.25 ? 87  THR A O   1 
ATOM   695  C  CB  A THR A 1 87  ? -18.470 14.262  21.338  0.50 19.69 ? 87  THR A CB  1 
ATOM   696  C  CB  B THR A 1 87  ? -18.834 13.824  21.458  0.50 15.68 ? 87  THR A CB  1 
ATOM   697  O  OG1 A THR A 1 87  ? -19.645 14.538  22.087  0.50 29.29 ? 87  THR A OG1 1 
ATOM   698  O  OG1 B THR A 1 87  ? -18.259 15.116  21.296  0.50 16.96 ? 87  THR A OG1 1 
ATOM   699  C  CG2 A THR A 1 87  ? -18.812 13.877  19.911  0.50 22.56 ? 87  THR A CG2 1 
ATOM   700  C  CG2 B THR A 1 87  ? -20.157 13.887  22.191  0.50 20.88 ? 87  THR A CG2 1 
ATOM   701  N  N   . TYR A 1 88  ? -16.634 11.550  20.649  1.00 14.49 ? 88  TYR A N   1 
ATOM   702  C  CA  . TYR A 1 88  ? -15.558 11.105  19.811  1.00 15.09 ? 88  TYR A CA  1 
ATOM   703  C  C   . TYR A 1 88  ? -16.111 10.801  18.425  1.00 13.88 ? 88  TYR A C   1 
ATOM   704  O  O   . TYR A 1 88  ? -17.149 10.174  18.255  1.00 19.04 ? 88  TYR A O   1 
ATOM   705  C  CB  . TYR A 1 88  ? -14.941 9.840   20.407  1.00 15.49 ? 88  TYR A CB  1 
ATOM   706  C  CG  . TYR A 1 88  ? -14.126 10.047  21.668  1.00 12.96 ? 88  TYR A CG  1 
ATOM   707  C  CD1 . TYR A 1 88  ? -14.717 10.380  22.891  1.00 13.05 ? 88  TYR A CD1 1 
ATOM   708  C  CD2 . TYR A 1 88  ? -12.751 9.801   21.650  1.00 13.19 ? 88  TYR A CD2 1 
ATOM   709  C  CE1 . TYR A 1 88  ? -13.949 10.554  24.051  1.00 14.72 ? 88  TYR A CE1 1 
ATOM   710  C  CE2 . TYR A 1 88  ? -11.969 9.953   22.788  1.00 13.22 ? 88  TYR A CE2 1 
ATOM   711  C  CZ  . TYR A 1 88  ? -12.570 10.341  23.981  1.00 13.32 ? 88  TYR A CZ  1 
ATOM   712  O  OH  . TYR A 1 88  ? -11.834 10.419  25.144  1.00 14.33 ? 88  TYR A OH  1 
ATOM   713  N  N   . ARG A 1 89  ? -15.401 11.233  17.388  1.00 13.56 ? 89  ARG A N   1 
ATOM   714  C  CA  . ARG A 1 89  ? -15.877 11.135  16.031  1.00 12.55 ? 89  ARG A CA  1 
ATOM   715  C  C   . ARG A 1 89  ? -15.196 10.013  15.256  1.00 10.14 ? 89  ARG A C   1 
ATOM   716  O  O   . ARG A 1 89  ? -13.966 9.934   15.267  1.00 9.87  ? 89  ARG A O   1 
ATOM   717  C  CB  . ARG A 1 89  ? -15.595 12.450  15.369  1.00 16.92 ? 89  ARG A CB  1 
ATOM   718  C  CG  . ARG A 1 89  ? -16.389 12.558  14.097  1.00 18.58 ? 89  ARG A CG  1 
ATOM   719  C  CD  . ARG A 1 89  ? -16.182 13.992  13.566  1.00 18.39 ? 89  ARG A CD  1 
ATOM   720  N  NE  . ARG A 1 89  ? -16.790 14.996  14.369  1.00 19.90 ? 89  ARG A NE  1 
ATOM   721  C  CZ  . ARG A 1 89  ? -16.631 16.302  14.188  1.00 13.86 ? 89  ARG A CZ  1 
ATOM   722  N  NH1 . ARG A 1 89  ? -15.863 16.746  13.208  1.00 20.58 ? 89  ARG A NH1 1 
ATOM   723  N  NH2 . ARG A 1 89  ? -17.239 17.159  14.988  1.00 20.24 ? 89  ARG A NH2 1 
ATOM   724  N  N   . LEU A 1 90  ? -15.995 9.191   14.539  1.00 11.26 ? 90  LEU A N   1 
ATOM   725  C  CA  . LEU A 1 90  ? -15.371 8.114   13.771  1.00 11.20 ? 90  LEU A CA  1 
ATOM   726  C  C   . LEU A 1 90  ? -14.563 8.696   12.618  1.00 10.18 ? 90  LEU A C   1 
ATOM   727  O  O   . LEU A 1 90  ? -15.056 9.491   11.828  1.00 12.96 ? 90  LEU A O   1 
ATOM   728  C  CB  . LEU A 1 90  ? -16.507 7.250   13.213  1.00 11.11 ? 90  LEU A CB  1 
ATOM   729  C  CG  . LEU A 1 90  ? -16.084 6.096   12.298  1.00 11.20 ? 90  LEU A CG  1 
ATOM   730  C  CD1 . LEU A 1 90  ? -15.276 5.042   13.068  1.00 12.06 ? 90  LEU A CD1 1 
ATOM   731  C  CD2 . LEU A 1 90  ? -17.310 5.477   11.654  1.00 13.11 ? 90  LEU A CD2 1 
ATOM   732  N  N   . THR A 1 91  ? -13.322 8.246   12.478  1.00 10.01 ? 91  THR A N   1 
ATOM   733  C  CA  . THR A 1 91  ? -12.479 8.656   11.368  1.00 10.08 ? 91  THR A CA  1 
ATOM   734  C  C   . THR A 1 91  ? -12.168 7.506   10.440  1.00 9.24  ? 91  THR A C   1 
ATOM   735  O  O   . THR A 1 91  ? -11.989 7.724   9.223   1.00 9.92  ? 91  THR A O   1 
ATOM   736  C  CB  . THR A 1 91  ? -11.203 9.366   11.914  1.00 11.07 ? 91  THR A CB  1 
ATOM   737  O  OG1 . THR A 1 91  ? -10.505 9.916   10.819  1.00 13.70 ? 91  THR A OG1 1 
ATOM   738  C  CG2 . THR A 1 91  ? -10.257 8.478   12.695  1.00 13.07 ? 91  THR A CG2 1 
ATOM   739  N  N   . GLN A 1 92  ? -12.009 6.265   10.950  1.00 9.25  ? 92  GLN A N   1 
ATOM   740  C  CA  . GLN A 1 92  ? -11.634 5.174   10.045  1.00 8.56  ? 92  GLN A CA  1 
ATOM   741  C  C   . GLN A 1 92  ? -11.918 3.871   10.749  1.00 9.17  ? 92  GLN A C   1 
ATOM   742  O  O   . GLN A 1 92  ? -12.043 3.853   11.985  1.00 8.99  ? 92  GLN A O   1 
ATOM   743  C  CB  . GLN A 1 92  ? -10.149 5.215   9.621   1.00 10.89 ? 92  GLN A CB  1 
ATOM   744  C  CG  . GLN A 1 92  ? -9.200  5.273   10.828  1.00 10.33 ? 92  GLN A CG  1 
ATOM   745  C  CD  . GLN A 1 92  ? -8.381  4.059   11.047  1.00 11.26 ? 92  GLN A CD  1 
ATOM   746  O  OE1 . GLN A 1 92  ? -8.866  2.934   10.898  1.00 11.51 ? 92  GLN A OE1 1 
ATOM   747  N  NE2 . GLN A 1 92  ? -7.124  4.279   11.449  1.00 13.46 ? 92  GLN A NE2 1 
ATOM   748  N  N   . PHE A 1 93  ? -12.013 2.753   10.034  1.00 8.92  ? 93  PHE A N   1 
ATOM   749  C  CA  . PHE A 1 93  ? -11.869 1.447   10.642  1.00 9.36  ? 93  PHE A CA  1 
ATOM   750  C  C   . PHE A 1 93  ? -10.868 0.656   9.837   1.00 8.82  ? 93  PHE A C   1 
ATOM   751  O  O   . PHE A 1 93  ? -10.627 0.888   8.631   1.00 9.17  ? 93  PHE A O   1 
ATOM   752  C  CB  . PHE A 1 93  ? -13.212 0.726   10.823  1.00 9.41  ? 93  PHE A CB  1 
ATOM   753  C  CG  . PHE A 1 93  ? -13.920 0.332   9.557   1.00 9.75  ? 93  PHE A CG  1 
ATOM   754  C  CD1 . PHE A 1 93  ? -13.501 -0.787  8.830   1.00 10.44 ? 93  PHE A CD1 1 
ATOM   755  C  CD2 . PHE A 1 93  ? -15.070 1.017   9.155   1.00 9.64  ? 93  PHE A CD2 1 
ATOM   756  C  CE1 . PHE A 1 93  ? -14.182 -1.164  7.680   1.00 10.32 ? 93  PHE A CE1 1 
ATOM   757  C  CE2 . PHE A 1 93  ? -15.759 0.629   8.011   1.00 11.18 ? 93  PHE A CE2 1 
ATOM   758  C  CZ  . PHE A 1 93  ? -15.315 -0.457  7.283   1.00 10.01 ? 93  PHE A CZ  1 
ATOM   759  N  N   . HIS A 1 94  ? -10.333 -0.377  10.492  1.00 8.55  ? 94  HIS A N   1 
ATOM   760  C  CA  . HIS A 1 94  ? -9.399  -1.303  9.860   1.00 8.99  ? 94  HIS A CA  1 
ATOM   761  C  C   . HIS A 1 94  ? -9.500  -2.620  10.610  1.00 8.95  ? 94  HIS A C   1 
ATOM   762  O  O   . HIS A 1 94  ? -10.133 -2.676  11.680  1.00 9.38  ? 94  HIS A O   1 
ATOM   763  C  CB  . HIS A 1 94  ? -7.966  -0.730  9.798   1.00 9.14  ? 94  HIS A CB  1 
ATOM   764  C  CG  . HIS A 1 94  ? -7.460  -0.516  11.182  1.00 8.80  ? 94  HIS A CG  1 
ATOM   765  N  ND1 . HIS A 1 94  ? -7.698  0.677   11.899  1.00 9.45  ? 94  HIS A ND1 1 
ATOM   766  C  CD2 . HIS A 1 94  ? -6.828  -1.337  12.062  1.00 9.39  ? 94  HIS A CD2 1 
ATOM   767  C  CE1 . HIS A 1 94  ? -7.180  0.567   13.118  1.00 9.70  ? 94  HIS A CE1 1 
ATOM   768  N  NE2 . HIS A 1 94  ? -6.674  -0.689  13.279  1.00 9.30  ? 94  HIS A NE2 1 
ATOM   769  N  N   . PHE A 1 95  ? -8.741  -3.621  10.171  1.00 9.10  ? 95  PHE A N   1 
ATOM   770  C  CA  . PHE A 1 95  ? -8.779  -4.915  10.838  1.00 9.49  ? 95  PHE A CA  1 
ATOM   771  C  C   . PHE A 1 95  ? -7.358  -5.419  11.072  1.00 8.95  ? 95  PHE A C   1 
ATOM   772  O  O   . PHE A 1 95  ? -6.405  -5.002  10.402  1.00 10.17 ? 95  PHE A O   1 
ATOM   773  C  CB  . PHE A 1 95  ? -9.477  -5.960  9.949   1.00 10.22 ? 95  PHE A CB  1 
ATOM   774  C  CG  . PHE A 1 95  ? -10.935 -5.659  9.708   1.00 10.22 ? 95  PHE A CG  1 
ATOM   775  C  CD1 . PHE A 1 95  ? -11.316 -4.788  8.713   1.00 11.25 ? 95  PHE A CD1 1 
ATOM   776  C  CD2 . PHE A 1 95  ? -11.928 -6.372  10.378  1.00 10.69 ? 95  PHE A CD2 1 
ATOM   777  C  CE1 . PHE A 1 95  ? -12.679 -4.568  8.442   1.00 11.92 ? 95  PHE A CE1 1 
ATOM   778  C  CE2 . PHE A 1 95  ? -13.287 -6.207  10.107  1.00 11.48 ? 95  PHE A CE2 1 
ATOM   779  C  CZ  . PHE A 1 95  ? -13.646 -5.283  9.116   1.00 11.91 ? 95  PHE A CZ  1 
ATOM   780  N  N   . HIS A 1 96  ? -7.278  -6.399  11.962  1.00 9.71  ? 96  HIS A N   1 
ATOM   781  C  CA  . HIS A 1 96  ? -6.074  -7.214  12.141  1.00 8.84  ? 96  HIS A CA  1 
ATOM   782  C  C   . HIS A 1 96  ? -6.519  -8.642  12.025  1.00 9.18  ? 96  HIS A C   1 
ATOM   783  O  O   . HIS A 1 96  ? -7.614  -8.958  12.504  1.00 10.02 ? 96  HIS A O   1 
ATOM   784  C  CB  . HIS A 1 96  ? -5.487  -6.971  13.538  1.00 9.48  ? 96  HIS A CB  1 
ATOM   785  C  CG  . HIS A 1 96  ? -5.143  -5.536  13.761  1.00 9.77  ? 96  HIS A CG  1 
ATOM   786  N  ND1 . HIS A 1 96  ? -3.914  -4.996  13.570  1.00 9.93  ? 96  HIS A ND1 1 
ATOM   787  C  CD2 . HIS A 1 96  ? -5.928  -4.520  14.162  1.00 9.38  ? 96  HIS A CD2 1 
ATOM   788  C  CE1 . HIS A 1 96  ? -3.963  -3.694  13.872  1.00 10.71 ? 96  HIS A CE1 1 
ATOM   789  N  NE2 . HIS A 1 96  ? -5.195  -3.362  14.205  1.00 8.68  ? 96  HIS A NE2 1 
ATOM   790  N  N   . TRP A 1 97  ? -5.712  -9.502  11.378  1.00 9.90  ? 97  TRP A N   1 
ATOM   791  C  CA  . TRP A 1 97  ? -6.185  -10.853 11.178  1.00 11.51 ? 97  TRP A CA  1 
ATOM   792  C  C   . TRP A 1 97  ? -4.984  -11.803 11.023  1.00 9.84  ? 97  TRP A C   1 
ATOM   793  O  O   . TRP A 1 97  ? -3.814  -11.377 11.002  1.00 11.05 ? 97  TRP A O   1 
ATOM   794  C  CB  . TRP A 1 97  ? -7.112  -10.974 9.931   1.00 11.73 ? 97  TRP A CB  1 
ATOM   795  C  CG  . TRP A 1 97  ? -6.408  -10.590 8.669   1.00 11.70 ? 97  TRP A CG  1 
ATOM   796  C  CD1 . TRP A 1 97  ? -5.723  -11.441 7.835   1.00 11.81 ? 97  TRP A CD1 1 
ATOM   797  C  CD2 . TRP A 1 97  ? -6.325  -9.288  8.073   1.00 11.17 ? 97  TRP A CD2 1 
ATOM   798  N  NE1 . TRP A 1 97  ? -5.230  -10.747 6.766   1.00 12.18 ? 97  TRP A NE1 1 
ATOM   799  C  CE2 . TRP A 1 97  ? -5.575  -9.415  6.892   1.00 11.45 ? 97  TRP A CE2 1 
ATOM   800  C  CE3 . TRP A 1 97  ? -6.823  -8.021  8.465   1.00 10.62 ? 97  TRP A CE3 1 
ATOM   801  C  CZ2 . TRP A 1 97  ? -5.345  -8.327  6.060   1.00 11.53 ? 97  TRP A CZ2 1 
ATOM   802  C  CZ3 . TRP A 1 97  ? -6.589  -6.950  7.619   1.00 10.21 ? 97  TRP A CZ3 1 
ATOM   803  C  CH2 . TRP A 1 97  ? -5.835  -7.086  6.443   1.00 11.05 ? 97  TRP A CH2 1 
ATOM   804  N  N   . GLY A 1 98  ? -5.292  -13.083 11.003  1.00 11.35 ? 98  GLY A N   1 
ATOM   805  C  CA  . GLY A 1 98  ? -4.289  -14.124 11.078  1.00 11.89 ? 98  GLY A CA  1 
ATOM   806  C  C   . GLY A 1 98  ? -4.038  -14.831 9.749   1.00 12.28 ? 98  GLY A C   1 
ATOM   807  O  O   . GLY A 1 98  ? -4.728  -14.650 8.732   1.00 13.20 ? 98  GLY A O   1 
ATOM   808  N  N   . SER A 1 99  ? -3.051  -15.715 9.776   1.00 12.95 ? 99  SER A N   1 
ATOM   809  C  CA  . SER A 1 99  ? -2.749  -16.590 8.654   1.00 14.55 ? 99  SER A CA  1 
ATOM   810  C  C   . SER A 1 99  ? -3.617  -17.839 8.675   1.00 17.26 ? 99  SER A C   1 
ATOM   811  O  O   . SER A 1 99  ? -3.599  -18.589 7.693   1.00 20.76 ? 99  SER A O   1 
ATOM   812  C  CB  . SER A 1 99  ? -1.287  -17.010 8.712   1.00 15.61 ? 99  SER A CB  1 
ATOM   813  O  OG  . SER A 1 99  ? -0.879  -17.472 9.996   1.00 17.49 ? 99  SER A OG  1 
ATOM   814  N  N   . LEU A 1 100 ? -4.272  -18.089 9.799   1.00 17.11 ? 100 LEU A N   1 
ATOM   815  C  CA  . LEU A 1 100 ? -5.249  -19.143 9.950   1.00 19.42 ? 100 LEU A CA  1 
ATOM   816  C  C   . LEU A 1 100 ? -6.256  -18.739 11.051  1.00 19.34 ? 100 LEU A C   1 
ATOM   817  O  O   . LEU A 1 100 ? -6.103  -17.718 11.716  1.00 19.10 ? 100 LEU A O   1 
ATOM   818  C  CB  . LEU A 1 100 ? -4.504  -20.424 10.230  1.00 21.81 ? 100 LEU A CB  1 
ATOM   819  C  CG  . LEU A 1 100 ? -3.887  -20.429 11.592  1.00 25.92 ? 100 LEU A CG  1 
ATOM   820  C  CD1 . LEU A 1 100 ? -3.699  -21.864 11.990  1.00 35.74 ? 100 LEU A CD1 1 
ATOM   821  C  CD2 . LEU A 1 100 ? -2.534  -19.752 11.559  1.00 25.29 ? 100 LEU A CD2 1 
ATOM   822  N  N   . ASP A 1 101 ? -7.340  -19.511 11.191  1.00 19.53 ? 101 ASP A N   1 
ATOM   823  C  CA  . ASP A 1 101 ? -8.486  -19.017 11.947  1.00 18.01 ? 101 ASP A CA  1 
ATOM   824  C  C   . ASP A 1 101 ? -8.177  -18.949 13.449  1.00 19.87 ? 101 ASP A C   1 
ATOM   825  O  O   . ASP A 1 101 ? -8.842  -18.182 14.155  1.00 21.71 ? 101 ASP A O   1 
ATOM   826  C  CB  . ASP A 1 101 ? -9.763  -19.842 11.759  1.00 19.54 ? 101 ASP A CB  1 
ATOM   827  C  CG  . ASP A 1 101 ? -10.294 -19.903 10.350  1.00 18.76 ? 101 ASP A CG  1 
ATOM   828  O  OD1 . ASP A 1 101 ? -9.899  -19.101 9.477   1.00 18.76 ? 101 ASP A OD1 1 
ATOM   829  O  OD2 . ASP A 1 101 ? -11.234 -20.716 10.144  1.00 24.22 ? 101 ASP A OD2 1 
ATOM   830  N  N   . GLY A 1 102 ? -7.216  -19.756 13.956  1.00 16.53 ? 102 GLY A N   1 
ATOM   831  C  CA  . GLY A 1 102 ? -7.000  -19.729 15.396  1.00 20.22 ? 102 GLY A CA  1 
ATOM   832  C  C   . GLY A 1 102 ? -6.118  -18.587 15.887  1.00 17.54 ? 102 GLY A C   1 
ATOM   833  O  O   . GLY A 1 102 ? -5.720  -18.545 17.066  1.00 19.23 ? 102 GLY A O   1 
ATOM   834  N  N   . GLN A 1 103 ? -5.879  -17.579 15.039  1.00 17.86 ? 103 GLN A N   1 
ATOM   835  C  CA  . GLN A 1 103 ? -5.196  -16.390 15.558  1.00 14.99 ? 103 GLN A CA  1 
ATOM   836  C  C   . GLN A 1 103 ? -5.517  -15.208 14.661  1.00 13.11 ? 103 GLN A C   1 
ATOM   837  O  O   . GLN A 1 103 ? -6.026  -15.403 13.568  1.00 13.90 ? 103 GLN A O   1 
ATOM   838  C  CB  . GLN A 1 103 ? -3.692  -16.611 15.607  1.00 14.41 ? 103 GLN A CB  1 
ATOM   839  C  CG  . GLN A 1 103 ? -3.038  -16.783 14.226  1.00 13.87 ? 103 GLN A CG  1 
ATOM   840  C  CD  . GLN A 1 103 ? -1.670  -17.424 14.329  1.00 15.81 ? 103 GLN A CD  1 
ATOM   841  O  OE1 . GLN A 1 103 ? -1.429  -18.287 15.165  1.00 24.41 ? 103 GLN A OE1 1 
ATOM   842  N  NE2 . GLN A 1 103 ? -0.741  -16.946 13.547  1.00 16.26 ? 103 GLN A NE2 1 
ATOM   843  N  N   . GLY A 1 104 ? -5.174  -13.998 15.121  1.00 12.00 ? 104 GLY A N   1 
ATOM   844  C  CA  . GLY A 1 104 ? -5.484  -12.847 14.309  1.00 11.73 ? 104 GLY A CA  1 
ATOM   845  C  C   . GLY A 1 104 ? -5.870  -11.643 15.144  1.00 10.23 ? 104 GLY A C   1 
ATOM   846  O  O   . GLY A 1 104 ? -5.599  -10.502 14.755  1.00 11.48 ? 104 GLY A O   1 
ATOM   847  N  N   . SER A 1 105 ? -6.559  -11.893 16.269  1.00 10.87 ? 105 SER A N   1 
ATOM   848  C  CA  . SER A 1 105 ? -6.965  -10.766 17.079  1.00 11.02 ? 105 SER A CA  1 
ATOM   849  C  C   . SER A 1 105 ? -5.760  -10.235 17.863  1.00 10.54 ? 105 SER A C   1 
ATOM   850  O  O   . SER A 1 105 ? -4.745  -10.921 18.053  1.00 11.18 ? 105 SER A O   1 
ATOM   851  C  CB  . SER A 1 105 ? -8.101  -11.119 18.026  1.00 11.12 ? 105 SER A CB  1 
ATOM   852  O  OG  . SER A 1 105 ? -7.749  -12.103 19.041  1.00 11.58 ? 105 SER A OG  1 
ATOM   853  N  N   . GLU A 1 106 ? -5.877  -8.979  18.277  1.00 9.85  ? 106 GLU A N   1 
ATOM   854  C  CA  . GLU A 1 106 ? -4.833  -8.350  19.081  1.00 10.16 ? 106 GLU A CA  1 
ATOM   855  C  C   . GLU A 1 106 ? -5.173  -8.532  20.566  1.00 10.04 ? 106 GLU A C   1 
ATOM   856  O  O   . GLU A 1 106 ? -4.399  -9.127  21.321  1.00 11.00 ? 106 GLU A O   1 
ATOM   857  C  CB  . GLU A 1 106 ? -4.775  -6.870  18.692  1.00 10.61 ? 106 GLU A CB  1 
ATOM   858  C  CG  . GLU A 1 106 ? -4.484  -6.701  17.214  1.00 10.42 ? 106 GLU A CG  1 
ATOM   859  C  CD  . GLU A 1 106 ? -3.711  -5.442  16.978  1.00 10.19 ? 106 GLU A CD  1 
ATOM   860  O  OE1 . GLU A 1 106 ? -4.249  -4.344  17.104  1.00 10.32 ? 106 GLU A OE1 1 
ATOM   861  O  OE2 . GLU A 1 106 ? -2.528  -5.559  16.587  1.00 12.38 ? 106 GLU A OE2 1 
ATOM   862  N  N   . HIS A 1 107 ? -6.354  -8.056  20.984  1.00 9.56  ? 107 HIS A N   1 
ATOM   863  C  CA  . HIS A 1 107 ? -6.838  -8.437  22.311  1.00 10.22 ? 107 HIS A CA  1 
ATOM   864  C  C   . HIS A 1 107 ? -7.137  -9.928  22.333  1.00 10.70 ? 107 HIS A C   1 
ATOM   865  O  O   . HIS A 1 107 ? -7.467  -10.519 21.308  1.00 11.10 ? 107 HIS A O   1 
ATOM   866  C  CB  . HIS A 1 107 ? -8.064  -7.636  22.728  1.00 9.96  ? 107 HIS A CB  1 
ATOM   867  C  CG  . HIS A 1 107 ? -7.718  -6.206  22.860  1.00 9.90  ? 107 HIS A CG  1 
ATOM   868  N  ND1 . HIS A 1 107 ? -7.750  -5.301  21.830  1.00 9.42  ? 107 HIS A ND1 1 
ATOM   869  C  CD2 . HIS A 1 107 ? -7.271  -5.513  23.936  1.00 10.51 ? 107 HIS A CD2 1 
ATOM   870  C  CE1 . HIS A 1 107 ? -7.318  -4.115  22.296  1.00 9.64  ? 107 HIS A CE1 1 
ATOM   871  N  NE2 . HIS A 1 107 ? -7.012  -4.214  23.569  1.00 9.64  ? 107 HIS A NE2 1 
ATOM   872  N  N   . THR A 1 108 ? -6.990  -10.484 23.535  1.00 11.37 ? 108 THR A N   1 
ATOM   873  C  CA  . THR A 1 108 ? -7.396  -11.859 23.735  1.00 11.76 ? 108 THR A CA  1 
ATOM   874  C  C   . THR A 1 108 ? -8.363  -11.882 24.930  1.00 12.25 ? 108 THR A C   1 
ATOM   875  O  O   . THR A 1 108 ? -8.415  -10.944 25.710  1.00 12.54 ? 108 THR A O   1 
ATOM   876  C  CB  . THR A 1 108 ? -6.210  -12.813 23.957  1.00 12.34 ? 108 THR A CB  1 
ATOM   877  O  OG1 . THR A 1 108 ? -5.398  -12.311 24.999  1.00 13.73 ? 108 THR A OG1 1 
ATOM   878  C  CG2 . THR A 1 108 ? -5.358  -12.923 22.721  1.00 13.32 ? 108 THR A CG2 1 
ATOM   879  N  N   . VAL A 1 109 ? -9.180  -12.926 25.042  1.00 14.08 ? 109 VAL A N   1 
ATOM   880  C  CA  . VAL A 1 109 ? -10.142 -13.002 26.137  1.00 13.99 ? 109 VAL A CA  1 
ATOM   881  C  C   . VAL A 1 109 ? -9.831  -14.289 26.906  1.00 14.65 ? 109 VAL A C   1 
ATOM   882  O  O   . VAL A 1 109 ? -10.047 -15.390 26.357  1.00 15.63 ? 109 VAL A O   1 
ATOM   883  C  CB  . VAL A 1 109 ? -11.579 -13.020 25.570  1.00 14.71 ? 109 VAL A CB  1 
ATOM   884  C  CG1 . VAL A 1 109 ? -12.552 -13.100 26.725  1.00 17.88 ? 109 VAL A CG1 1 
ATOM   885  C  CG2 . VAL A 1 109 ? -11.889 -11.739 24.765  1.00 15.01 ? 109 VAL A CG2 1 
ATOM   886  N  N   . ASP A 1 110 ? -9.322  -14.171 28.160  1.00 15.02 ? 110 ASP A N   1 
ATOM   887  C  CA  . ASP A 1 110 ? -8.931  -15.403 28.867  1.00 16.68 ? 110 ASP A CA  1 
ATOM   888  C  C   . ASP A 1 110 ? -7.989  -16.210 27.977  1.00 17.04 ? 110 ASP A C   1 
ATOM   889  O  O   . ASP A 1 110 ? -8.086  -17.456 27.919  1.00 18.05 ? 110 ASP A O   1 
ATOM   890  C  CB  . ASP A 1 110 ? -10.137 -16.240 29.339  1.00 20.95 ? 110 ASP A CB  1 
ATOM   891  C  CG  . ASP A 1 110 ? -10.996 -15.422 30.297  1.00 19.47 ? 110 ASP A CG  1 
ATOM   892  O  OD1 . ASP A 1 110 ? -10.435 -14.602 31.040  1.00 21.69 ? 110 ASP A OD1 1 
ATOM   893  O  OD2 . ASP A 1 110 ? -12.211 -15.627 30.301  1.00 26.07 ? 110 ASP A OD2 1 
ATOM   894  N  N   . LYS A 1 111 ? -7.073  -15.511 27.275  1.00 14.65 ? 111 LYS A N   1 
ATOM   895  C  CA  . LYS A 1 111 ? -6.030  -16.057 26.405  1.00 14.79 ? 111 LYS A CA  1 
ATOM   896  C  C   . LYS A 1 111 ? -6.556  -16.544 25.061  1.00 13.83 ? 111 LYS A C   1 
ATOM   897  O  O   . LYS A 1 111 ? -5.781  -16.907 24.192  1.00 15.61 ? 111 LYS A O   1 
ATOM   898  C  CB  . LYS A 1 111 ? -5.183  -17.151 27.062  1.00 16.97 ? 111 LYS A CB  1 
ATOM   899  C  CG  . LYS A 1 111 ? -4.571  -16.766 28.387  1.00 23.59 ? 111 LYS A CG  1 
ATOM   900  C  CD  . LYS A 1 111 ? -3.463  -15.829 28.122  1.00 23.08 ? 111 LYS A CD  1 
ATOM   901  C  CE  . LYS A 1 111 ? -2.776  -15.450 29.409  1.00 33.95 ? 111 LYS A CE  1 
ATOM   902  N  NZ  . LYS A 1 111 ? -1.433  -14.955 29.091  1.00 33.92 ? 111 LYS A NZ  1 
ATOM   903  N  N   . LYS A 1 112 ? -7.891  -16.531 24.880  1.00 14.91 ? 112 LYS A N   1 
ATOM   904  C  CA  . LYS A 1 112 ? -8.409  -16.925 23.579  1.00 16.38 ? 112 LYS A CA  1 
ATOM   905  C  C   . LYS A 1 112 ? -8.118  -15.857 22.503  1.00 13.77 ? 112 LYS A C   1 
ATOM   906  O  O   . LYS A 1 112 ? -8.373  -14.668 22.688  1.00 14.46 ? 112 LYS A O   1 
ATOM   907  C  CB  . LYS A 1 112 ? -9.918  -17.153 23.666  1.00 18.29 ? 112 LYS A CB  1 
ATOM   908  C  CG  . LYS A 1 112 ? -10.632 -17.383 22.335  1.00 21.49 ? 112 LYS A CG  1 
ATOM   909  C  CD  . LYS A 1 112 ? -12.166 -17.531 22.404  1.00 23.16 ? 112 LYS A CD  1 
ATOM   910  C  CE  . LYS A 1 112 ? -12.715 -17.658 20.998  1.00 28.07 ? 112 LYS A CE  1 
ATOM   911  N  NZ  . LYS A 1 112 ? -12.214 -18.883 20.358  1.00 30.77 ? 112 LYS A NZ  1 
ATOM   912  N  N   A LYS A 1 113 ? -7.561  -16.342 21.398  0.50 13.13 ? 113 LYS A N   1 
ATOM   913  N  N   B LYS A 1 113 ? -7.630  -16.345 21.355  0.50 13.46 ? 113 LYS A N   1 
ATOM   914  C  CA  A LYS A 1 113 ? -7.407  -15.531 20.198  0.50 14.00 ? 113 LYS A CA  1 
ATOM   915  C  CA  B LYS A 1 113 ? -7.361  -15.537 20.162  0.50 13.96 ? 113 LYS A CA  1 
ATOM   916  C  C   A LYS A 1 113 ? -8.608  -15.753 19.301  0.50 13.80 ? 113 LYS A C   1 
ATOM   917  C  C   B LYS A 1 113 ? -8.413  -15.753 19.087  0.50 12.86 ? 113 LYS A C   1 
ATOM   918  O  O   A LYS A 1 113 ? -9.164  -16.855 19.271  0.50 13.79 ? 113 LYS A O   1 
ATOM   919  O  O   B LYS A 1 113 ? -8.679  -16.884 18.686  0.50 15.14 ? 113 LYS A O   1 
ATOM   920  C  CB  A LYS A 1 113 ? -6.137  -15.921 19.449  0.50 14.11 ? 113 LYS A CB  1 
ATOM   921  C  CB  B LYS A 1 113 ? -6.032  -15.931 19.530  0.50 15.00 ? 113 LYS A CB  1 
ATOM   922  C  CG  A LYS A 1 113 ? -4.870  -15.808 20.278  0.50 14.28 ? 113 LYS A CG  1 
ATOM   923  C  CG  B LYS A 1 113 ? -4.828  -15.564 20.371  0.50 14.89 ? 113 LYS A CG  1 
ATOM   924  C  CD  A LYS A 1 113 ? -3.714  -16.507 19.605  0.50 15.41 ? 113 LYS A CD  1 
ATOM   925  C  CD  B LYS A 1 113 ? -3.564  -16.143 19.794  0.50 14.57 ? 113 LYS A CD  1 
ATOM   926  C  CE  A LYS A 1 113 ? -2.375  -15.983 20.073  0.50 17.94 ? 113 LYS A CE  1 
ATOM   927  C  CE  B LYS A 1 113 ? -2.350  -15.638 20.546  0.50 17.56 ? 113 LYS A CE  1 
ATOM   928  N  NZ  A LYS A 1 113 ? -2.016  -16.521 21.405  0.50 19.27 ? 113 LYS A NZ  1 
ATOM   929  N  NZ  B LYS A 1 113 ? -1.190  -16.492 20.212  0.50 20.70 ? 113 LYS A NZ  1 
ATOM   930  N  N   . TYR A 1 114 ? -9.041  -14.656 18.680  1.00 12.44 ? 114 TYR A N   1 
ATOM   931  C  CA  . TYR A 1 114 ? -10.049 -14.709 17.646  1.00 12.44 ? 114 TYR A CA  1 
ATOM   932  C  C   . TYR A 1 114 ? -9.387  -14.678 16.286  1.00 11.73 ? 114 TYR A C   1 
ATOM   933  O  O   . TYR A 1 114 ? -8.180  -14.377 16.162  1.00 12.34 ? 114 TYR A O   1 
ATOM   934  C  CB  . TYR A 1 114 ? -11.070 -13.577 17.804  1.00 13.36 ? 114 TYR A CB  1 
ATOM   935  C  CG  . TYR A 1 114 ? -12.011 -13.837 18.960  1.00 12.25 ? 114 TYR A CG  1 
ATOM   936  C  CD1 . TYR A 1 114 ? -11.735 -13.442 20.264  1.00 14.48 ? 114 TYR A CD1 1 
ATOM   937  C  CD2 . TYR A 1 114 ? -13.215 -14.504 18.736  1.00 15.26 ? 114 TYR A CD2 1 
ATOM   938  C  CE1 . TYR A 1 114 ? -12.605 -13.695 21.303  1.00 17.94 ? 114 TYR A CE1 1 
ATOM   939  C  CE2 . TYR A 1 114 ? -14.118 -14.725 19.774  1.00 16.63 ? 114 TYR A CE2 1 
ATOM   940  C  CZ  . TYR A 1 114 ? -13.797 -14.338 21.063  1.00 18.32 ? 114 TYR A CZ  1 
ATOM   941  O  OH  . TYR A 1 114 ? -14.637 -14.521 22.133  1.00 26.28 ? 114 TYR A OH  1 
ATOM   942  N  N   . ALA A 1 115 ? -10.168 -14.899 15.214  1.00 11.79 ? 115 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 115 ? -9.650  -14.907 13.848  1.00 11.53 ? 115 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 115 ? -9.206  -13.527 13.407  1.00 11.91 ? 115 ALA A C   1 
ATOM   945  O  O   . ALA A 1 115 ? -8.375  -13.392 12.514  1.00 12.11 ? 115 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 115 ? -10.652 -15.543 12.899  1.00 14.22 ? 115 ALA A CB  1 
ATOM   947  N  N   . ALA A 1 116 ? -9.892  -12.500 13.917  1.00 11.18 ? 116 ALA A N   1 
ATOM   948  C  CA  . ALA A 1 116 ? -9.564  -11.170 13.457  1.00 10.71 ? 116 ALA A CA  1 
ATOM   949  C  C   . ALA A 1 116 ? -10.147 -10.203 14.468  1.00 9.56  ? 116 ALA A C   1 
ATOM   950  O  O   . ALA A 1 116 ? -10.861 -10.581 15.393  1.00 10.02 ? 116 ALA A O   1 
ATOM   951  C  CB  . ALA A 1 116 ? -10.122 -10.892 12.073  1.00 11.35 ? 116 ALA A CB  1 
ATOM   952  N  N   . GLU A 1 117 ? -9.761  -8.927  14.333  1.00 9.59  ? 117 GLU A N   1 
ATOM   953  C  CA  . GLU A 1 117 ? -10.298 -7.907  15.224  1.00 8.93  ? 117 GLU A CA  1 
ATOM   954  C  C   . GLU A 1 117 ? -10.500 -6.653  14.397  1.00 8.93  ? 117 GLU A C   1 
ATOM   955  O  O   . GLU A 1 117 ? -9.609  -6.244  13.654  1.00 10.55 ? 117 GLU A O   1 
ATOM   956  C  CB  . GLU A 1 117 ? -9.305  -7.630  16.361  1.00 10.19 ? 117 GLU A CB  1 
ATOM   957  C  CG  . GLU A 1 117 ? -9.803  -6.687  17.464  1.00 10.34 ? 117 GLU A CG  1 
ATOM   958  C  CD  . GLU A 1 117 ? -8.898  -6.658  18.668  1.00 10.77 ? 117 GLU A CD  1 
ATOM   959  O  OE1 . GLU A 1 117 ? -8.283  -7.700  18.970  1.00 10.58 ? 117 GLU A OE1 1 
ATOM   960  O  OE2 . GLU A 1 117 ? -8.816  -5.576  19.341  1.00 11.55 ? 117 GLU A OE2 1 
ATOM   961  N  N   . LEU A 1 118 ? -11.675 -6.069  14.546  1.00 9.24  ? 118 LEU A N   1 
ATOM   962  C  CA  . LEU A 1 118 ? -12.051 -4.805  13.868  1.00 8.67  ? 118 LEU A CA  1 
ATOM   963  C  C   . LEU A 1 118 ? -11.824 -3.657  14.863  1.00 7.99  ? 118 LEU A C   1 
ATOM   964  O  O   . LEU A 1 118 ? -12.220 -3.745  16.051  1.00 8.79  ? 118 LEU A O   1 
ATOM   965  C  CB  . LEU A 1 118 ? -13.550 -4.896  13.539  1.00 9.39  ? 118 LEU A CB  1 
ATOM   966  C  CG  . LEU A 1 118 ? -14.270 -3.573  13.219  1.00 9.35  ? 118 LEU A CG  1 
ATOM   967  C  CD1 . LEU A 1 118 ? -13.729 -2.923  11.936  1.00 9.86  ? 118 LEU A CD1 1 
ATOM   968  C  CD2 . LEU A 1 118 ? -15.733 -3.886  12.941  1.00 10.82 ? 118 LEU A CD2 1 
ATOM   969  N  N   . HIS A 1 119 ? -11.190 -2.583  14.374  1.00 8.40  ? 119 HIS A N   1 
ATOM   970  C  CA  . HIS A 1 119 ? -10.957 -1.372  15.152  1.00 8.49  ? 119 HIS A CA  1 
ATOM   971  C  C   . HIS A 1 119 ? -11.683 -0.215  14.477  1.00 8.73  ? 119 HIS A C   1 
ATOM   972  O  O   . HIS A 1 119 ? -11.295 0.172   13.367  1.00 9.24  ? 119 HIS A O   1 
ATOM   973  C  CB  . HIS A 1 119 ? -9.450  -1.091  15.235  1.00 8.90  ? 119 HIS A CB  1 
ATOM   974  C  CG  . HIS A 1 119 ? -8.785  -2.094  16.097  1.00 8.84  ? 119 HIS A CG  1 
ATOM   975  N  ND1 . HIS A 1 119 ? -7.382  -2.284  16.072  1.00 9.35  ? 119 HIS A ND1 1 
ATOM   976  C  CD2 . HIS A 1 119 ? -9.304  -2.884  17.068  1.00 9.63  ? 119 HIS A CD2 1 
ATOM   977  C  CE1 . HIS A 1 119 ? -7.115  -3.200  16.996  1.00 9.66  ? 119 HIS A CE1 1 
ATOM   978  N  NE2 . HIS A 1 119 ? -8.233  -3.590  17.572  1.00 9.24  ? 119 HIS A NE2 1 
ATOM   979  N  N   . LEU A 1 120 ? -12.719 0.285   15.155  1.00 8.84  ? 120 LEU A N   1 
ATOM   980  C  CA  . LEU A 1 120 ? -13.385 1.494   14.726  1.00 8.90  ? 120 LEU A CA  1 
ATOM   981  C  C   . LEU A 1 120 ? -12.791 2.647   15.535  1.00 7.97  ? 120 LEU A C   1 
ATOM   982  O  O   . LEU A 1 120 ? -12.866 2.677   16.766  1.00 8.58  ? 120 LEU A O   1 
ATOM   983  C  CB  . LEU A 1 120 ? -14.885 1.330   15.036  1.00 9.79  ? 120 LEU A CB  1 
ATOM   984  C  CG  . LEU A 1 120 ? -15.588 0.351   14.104  1.00 9.78  ? 120 LEU A CG  1 
ATOM   985  C  CD1 . LEU A 1 120 ? -16.596 -0.469  14.894  1.00 14.55 ? 120 LEU A CD1 1 
ATOM   986  C  CD2 . LEU A 1 120 ? -16.278 1.107   12.963  1.00 11.85 ? 120 LEU A CD2 1 
ATOM   987  N  N   . VAL A 1 121 ? -12.133 3.565   14.858  1.00 9.05  ? 121 VAL A N   1 
ATOM   988  C  CA  . VAL A 1 121 ? -11.229 4.537   15.500  1.00 8.75  ? 121 VAL A CA  1 
ATOM   989  C  C   . VAL A 1 121 ? -11.885 5.913   15.514  1.00 8.62  ? 121 VAL A C   1 
ATOM   990  O  O   . VAL A 1 121 ? -12.343 6.379   14.481  1.00 9.91  ? 121 VAL A O   1 
ATOM   991  C  CB  . VAL A 1 121 ? -9.921  4.649   14.657  1.00 9.37  ? 121 VAL A CB  1 
ATOM   992  C  CG1 . VAL A 1 121 ? -8.971  5.635   15.286  1.00 10.59 ? 121 VAL A CG1 1 
ATOM   993  C  CG2 . VAL A 1 121 ? -9.300  3.256   14.500  1.00 11.32 ? 121 VAL A CG2 1 
ATOM   994  N  N   . HIS A 1 122 ? -11.966 6.467   16.727  1.00 9.00  ? 122 HIS A N   1 
ATOM   995  C  CA  . HIS A 1 122 ? -12.662 7.733   16.899  1.00 9.85  ? 122 HIS A CA  1 
ATOM   996  C  C   . HIS A 1 122 ? -11.740 8.704   17.614  1.00 9.81  ? 122 HIS A C   1 
ATOM   997  O  O   . HIS A 1 122 ? -10.978 8.322   18.494  1.00 10.79 ? 122 HIS A O   1 
ATOM   998  C  CB  . HIS A 1 122 ? -13.917 7.538   17.778  1.00 10.14 ? 122 HIS A CB  1 
ATOM   999  C  CG  . HIS A 1 122 ? -14.805 6.415   17.397  1.00 9.44  ? 122 HIS A CG  1 
ATOM   1000 N  ND1 . HIS A 1 122 ? -14.469 5.101   17.604  1.00 10.12 ? 122 HIS A ND1 1 
ATOM   1001 C  CD2 . HIS A 1 122 ? -16.012 6.391   16.787  1.00 10.74 ? 122 HIS A CD2 1 
ATOM   1002 C  CE1 . HIS A 1 122 ? -15.460 4.324   17.168  1.00 10.47 ? 122 HIS A CE1 1 
ATOM   1003 N  NE2 . HIS A 1 122 ? -16.413 5.064   16.635  1.00 10.88 ? 122 HIS A NE2 1 
ATOM   1004 N  N   . TRP A 1 123 ? -11.867 10.003  17.323  1.00 9.90  ? 123 TRP A N   1 
ATOM   1005 C  CA  . TRP A 1 123 ? -11.035 10.994  18.026  1.00 10.17 ? 123 TRP A CA  1 
ATOM   1006 C  C   . TRP A 1 123 ? -11.902 11.962  18.838  1.00 10.59 ? 123 TRP A C   1 
ATOM   1007 O  O   . TRP A 1 123 ? -13.022 12.327  18.453  1.00 11.90 ? 123 TRP A O   1 
ATOM   1008 C  CB  . TRP A 1 123 ? -10.131 11.770  17.057  1.00 11.09 ? 123 TRP A CB  1 
ATOM   1009 C  CG  . TRP A 1 123 ? -10.816 12.348  15.863  1.00 10.90 ? 123 TRP A CG  1 
ATOM   1010 C  CD1 . TRP A 1 123 ? -10.962 11.760  14.640  1.00 13.76 ? 123 TRP A CD1 1 
ATOM   1011 C  CD2 . TRP A 1 123 ? -11.318 13.688  15.721  1.00 11.80 ? 123 TRP A CD2 1 
ATOM   1012 N  NE1 . TRP A 1 123 ? -11.631 12.604  13.772  1.00 15.42 ? 123 TRP A NE1 1 
ATOM   1013 C  CE2 . TRP A 1 123 ? -11.801 13.811  14.394  1.00 14.59 ? 123 TRP A CE2 1 
ATOM   1014 C  CE3 . TRP A 1 123 ? -11.449 14.791  16.582  1.00 13.26 ? 123 TRP A CE3 1 
ATOM   1015 C  CZ2 . TRP A 1 123 ? -12.352 14.981  13.920  1.00 16.14 ? 123 TRP A CZ2 1 
ATOM   1016 C  CZ3 . TRP A 1 123 ? -12.007 15.957  16.122  1.00 14.36 ? 123 TRP A CZ3 1 
ATOM   1017 C  CH2 . TRP A 1 123 ? -12.442 16.055  14.791  1.00 17.82 ? 123 TRP A CH2 1 
ATOM   1018 N  N   . ASN A 1 124 ? -11.339 12.378  19.954  1.00 11.59 ? 124 ASN A N   1 
ATOM   1019 C  CA  . ASN A 1 124 ? -12.028 13.263  20.892  1.00 13.01 ? 124 ASN A CA  1 
ATOM   1020 C  C   . ASN A 1 124 ? -12.190 14.654  20.270  1.00 11.12 ? 124 ASN A C   1 
ATOM   1021 O  O   . ASN A 1 124 ? -11.207 15.293  19.889  1.00 12.56 ? 124 ASN A O   1 
ATOM   1022 C  CB  . ASN A 1 124 ? -11.166 13.327  22.162  1.00 14.14 ? 124 ASN A CB  1 
ATOM   1023 C  CG  . ASN A 1 124 ? -11.858 13.984  23.328  1.00 13.51 ? 124 ASN A CG  1 
ATOM   1024 O  OD1 . ASN A 1 124 ? -12.712 14.879  23.127  1.00 15.88 ? 124 ASN A OD1 1 
ATOM   1025 N  ND2 . ASN A 1 124 ? -11.515 13.524  24.538  1.00 14.58 ? 124 ASN A ND2 1 
ATOM   1026 N  N   . THR A 1 125 ? -13.449 15.082  20.121  1.00 13.10 ? 125 THR A N   1 
ATOM   1027 C  CA  . THR A 1 125 ? -13.681 16.332  19.400  1.00 14.86 ? 125 THR A CA  1 
ATOM   1028 C  C   . THR A 1 125 ? -13.063 17.531  20.161  1.00 13.15 ? 125 THR A C   1 
ATOM   1029 O  O   . THR A 1 125 ? -12.950 18.562  19.528  1.00 16.23 ? 125 THR A O   1 
ATOM   1030 C  CB  . THR A 1 125 ? -15.191 16.571  19.184  1.00 17.38 ? 125 THR A CB  1 
ATOM   1031 O  OG1 . THR A 1 125 ? -15.856 16.571  20.452  1.00 20.24 ? 125 THR A OG1 1 
ATOM   1032 C  CG2 . THR A 1 125 ? -15.727 15.463  18.294  1.00 20.96 ? 125 THR A CG2 1 
ATOM   1033 N  N   . LYS A 1 126 ? -12.635 17.302  21.416  1.00 14.90 ? 127 LYS A N   1 
ATOM   1034 C  CA  . LYS A 1 126 ? -12.122 18.553  22.036  1.00 20.10 ? 127 LYS A CA  1 
ATOM   1035 C  C   . LYS A 1 126 ? -10.732 18.865  21.471  1.00 18.38 ? 127 LYS A C   1 
ATOM   1036 O  O   . LYS A 1 126 ? -10.232 19.968  21.663  1.00 23.73 ? 127 LYS A O   1 
ATOM   1037 C  CB  . LYS A 1 126 ? -12.077 18.413  23.561  1.00 22.46 ? 127 LYS A CB  1 
ATOM   1038 C  CG  . LYS A 1 126 ? -11.105 17.368  24.091  1.00 22.10 ? 127 LYS A CG  1 
ATOM   1039 C  CD  . LYS A 1 126 ? -11.356 16.993  25.536  1.00 28.50 ? 127 LYS A CD  1 
ATOM   1040 C  CE  . LYS A 1 126 ? -10.114 16.495  26.245  1.00 36.60 ? 127 LYS A CE  1 
ATOM   1041 N  NZ  . LYS A 1 126 ? -10.045 16.987  27.641  1.00 41.69 ? 127 LYS A NZ  1 
ATOM   1042 N  N   . TYR A 1 127 ? -10.160 17.973  20.642  1.00 14.84 ? 128 TYR A N   1 
ATOM   1043 C  CA  . TYR A 1 127 ? -8.822  18.179  20.103  1.00 16.10 ? 128 TYR A CA  1 
ATOM   1044 C  C   . TYR A 1 127 ? -8.860  18.526  18.619  1.00 15.10 ? 128 TYR A C   1 
ATOM   1045 O  O   . TYR A 1 127 ? -7.815  18.765  18.005  1.00 18.40 ? 128 TYR A O   1 
ATOM   1046 C  CB  . TYR A 1 127 ? -7.886  16.992  20.362  1.00 14.53 ? 128 TYR A CB  1 
ATOM   1047 C  CG  . TYR A 1 127 ? -7.764  16.738  21.828  1.00 15.67 ? 128 TYR A CG  1 
ATOM   1048 C  CD1 . TYR A 1 127 ? -7.288  17.720  22.717  1.00 16.52 ? 128 TYR A CD1 1 
ATOM   1049 C  CD2 . TYR A 1 127 ? -8.048  15.493  22.328  1.00 16.12 ? 128 TYR A CD2 1 
ATOM   1050 C  CE1 . TYR A 1 127 ? -7.189  17.453  24.064  1.00 18.59 ? 128 TYR A CE1 1 
ATOM   1051 C  CE2 . TYR A 1 127 ? -7.986  15.214  23.674  1.00 17.87 ? 128 TYR A CE2 1 
ATOM   1052 C  CZ  . TYR A 1 127 ? -7.506  16.206  24.531  1.00 17.17 ? 128 TYR A CZ  1 
ATOM   1053 O  OH  . TYR A 1 127 ? -7.393  16.040  25.864  1.00 18.74 ? 128 TYR A OH  1 
ATOM   1054 N  N   . GLY A 1 128 ? -10.075 18.574  18.041  1.00 17.26 ? 129 GLY A N   1 
ATOM   1055 C  CA  . GLY A 1 128 ? -10.214 19.261  16.773  1.00 19.17 ? 129 GLY A CA  1 
ATOM   1056 C  C   . GLY A 1 128 ? -9.920  18.408  15.544  1.00 17.70 ? 129 GLY A C   1 
ATOM   1057 O  O   . GLY A 1 128 ? -10.564 18.644  14.524  1.00 24.24 ? 129 GLY A O   1 
ATOM   1058 N  N   A ASP A 1 129 ? -9.054  17.410  15.675  0.50 18.82 ? 130 ASP A N   1 
ATOM   1059 N  N   B ASP A 1 129 ? -8.850  17.559  15.564  0.50 19.61 ? 130 ASP A N   1 
ATOM   1060 C  CA  A ASP A 1 129 ? -8.880  16.489  14.576  0.50 18.27 ? 130 ASP A CA  1 
ATOM   1061 C  CA  B ASP A 1 129 ? -8.325  16.723  14.464  0.50 17.90 ? 130 ASP A CA  1 
ATOM   1062 C  C   A ASP A 1 129 ? -8.060  15.305  15.082  0.50 20.23 ? 130 ASP A C   1 
ATOM   1063 C  C   B ASP A 1 129 ? -7.753  15.398  15.000  0.50 17.79 ? 130 ASP A C   1 
ATOM   1064 O  O   A ASP A 1 129 ? -7.633  15.299  16.225  0.50 18.78 ? 130 ASP A O   1 
ATOM   1065 O  O   B ASP A 1 129 ? -7.245  15.355  16.112  0.50 19.33 ? 130 ASP A O   1 
ATOM   1066 C  CB  A ASP A 1 129 ? -8.326  17.198  13.341  0.50 18.72 ? 130 ASP A CB  1 
ATOM   1067 C  CB  B ASP A 1 129 ? -7.251  17.426  13.596  0.50 17.18 ? 130 ASP A CB  1 
ATOM   1068 C  CG  A ASP A 1 129 ? -6.900  17.656  13.571  0.50 17.10 ? 130 ASP A CG  1 
ATOM   1069 C  CG  B ASP A 1 129 ? -6.211  16.539  12.889  0.50 19.10 ? 130 ASP A CG  1 
ATOM   1070 O  OD1 A ASP A 1 129 ? -6.299  17.251  14.590  0.50 20.76 ? 130 ASP A OD1 1 
ATOM   1071 O  OD1 B ASP A 1 129 ? -6.433  16.142  11.709  0.50 24.20 ? 130 ASP A OD1 1 
ATOM   1072 O  OD2 A ASP A 1 129 ? -6.418  18.410  12.753  0.50 23.47 ? 130 ASP A OD2 1 
ATOM   1073 O  OD2 B ASP A 1 129 ? -5.129  16.335  13.461  0.50 20.51 ? 130 ASP A OD2 1 
ATOM   1074 N  N   . ALA A 1 130 ? -7.873  14.314  14.215  1.00 18.33 ? 131 ALA A N   1 
ATOM   1075 C  CA  . ALA A 1 130 ? -7.405  12.991  14.586  1.00 17.45 ? 131 ALA A CA  1 
ATOM   1076 C  C   . ALA A 1 130 ? -5.912  13.055  14.951  1.00 16.55 ? 131 ALA A C   1 
ATOM   1077 O  O   . ALA A 1 130 ? -5.506  12.436  15.923  1.00 14.69 ? 131 ALA A O   1 
ATOM   1078 C  CB  . ALA A 1 130 ? -7.750  12.032  13.454  1.00 18.67 ? 131 ALA A CB  1 
ATOM   1079 N  N   . GLY A 1 131 ? -5.118  13.860  14.230  1.00 20.63 ? 132 GLY A N   1 
ATOM   1080 C  CA  . GLY A 1 131 ? -3.674  13.804  14.445  1.00 25.49 ? 132 GLY A CA  1 
ATOM   1081 C  C   . GLY A 1 131 ? -3.349  14.466  15.777  1.00 17.12 ? 132 GLY A C   1 
ATOM   1082 O  O   . GLY A 1 131 ? -2.566  13.934  16.586  1.00 19.06 ? 132 GLY A O   1 
ATOM   1083 N  N   A LYS A 1 132 ? -3.971  15.616  16.009  0.50 19.25 ? 133 LYS A N   1 
ATOM   1084 N  N   B LYS A 1 132 ? -3.937  15.650  16.014  0.50 19.92 ? 133 LYS A N   1 
ATOM   1085 C  CA  A LYS A 1 132 ? -3.731  16.279  17.279  0.50 17.33 ? 133 LYS A CA  1 
ATOM   1086 C  CA  B LYS A 1 132 ? -3.758  16.302  17.310  0.50 17.17 ? 133 LYS A CA  1 
ATOM   1087 C  C   A LYS A 1 132 ? -4.308  15.453  18.425  0.50 15.30 ? 133 LYS A C   1 
ATOM   1088 C  C   B LYS A 1 132 ? -4.267  15.387  18.413  0.50 15.36 ? 133 LYS A C   1 
ATOM   1089 O  O   A LYS A 1 132 ? -3.715  15.396  19.497  0.50 16.28 ? 133 LYS A O   1 
ATOM   1090 O  O   B LYS A 1 132 ? -3.641  15.278  19.462  0.50 16.09 ? 133 LYS A O   1 
ATOM   1091 C  CB  A LYS A 1 132 ? -4.149  17.750  17.199  0.50 18.04 ? 133 LYS A CB  1 
ATOM   1092 C  CB  B LYS A 1 132 ? -4.546  17.607  17.495  0.50 18.63 ? 133 LYS A CB  1 
ATOM   1093 C  CG  A LYS A 1 132 ? -3.577  18.426  15.968  0.50 18.63 ? 133 LYS A CG  1 
ATOM   1094 C  CG  B LYS A 1 132 ? -4.026  18.837  16.767  0.50 22.38 ? 133 LYS A CG  1 
ATOM   1095 C  CD  A LYS A 1 132 ? -2.055  18.268  15.918  0.50 22.19 ? 133 LYS A CD  1 
ATOM   1096 C  CD  B LYS A 1 132 ? -2.534  19.069  17.034  0.50 22.31 ? 133 LYS A CD  1 
ATOM   1097 C  CE  A LYS A 1 132 ? -1.395  19.164  14.897  0.50 27.56 ? 133 LYS A CE  1 
ATOM   1098 C  CE  B LYS A 1 132 ? -2.158  20.130  18.054  0.50 29.76 ? 133 LYS A CE  1 
ATOM   1099 N  NZ  A LYS A 1 132 ? -0.148  19.801  15.391  0.50 24.57 ? 133 LYS A NZ  1 
ATOM   1100 N  NZ  B LYS A 1 132 ? -3.051  20.220  19.246  0.50 24.89 ? 133 LYS A NZ  1 
ATOM   1101 N  N   . ALA A 1 133 ? -5.421  14.742  18.184  1.00 13.79 ? 134 ALA A N   1 
ATOM   1102 C  CA  . ALA A 1 133 ? -5.962  13.923  19.259  1.00 12.34 ? 134 ALA A CA  1 
ATOM   1103 C  C   . ALA A 1 133 ? -4.985  12.795  19.634  1.00 11.71 ? 134 ALA A C   1 
ATOM   1104 O  O   . ALA A 1 133 ? -4.895  12.417  20.812  1.00 12.90 ? 134 ALA A O   1 
ATOM   1105 C  CB  . ALA A 1 133 ? -7.311  13.333  18.807  1.00 11.57 ? 134 ALA A CB  1 
ATOM   1106 N  N   . SER A 1 134 ? -4.278  12.266  18.609  1.00 12.47 ? 135 SER A N   1 
ATOM   1107 C  CA  . SER A 1 134 ? -3.384  11.147  18.886  1.00 13.20 ? 135 SER A CA  1 
ATOM   1108 C  C   . SER A 1 134 ? -2.215  11.536  19.776  1.00 13.71 ? 135 SER A C   1 
ATOM   1109 O  O   . SER A 1 134 ? -1.489  10.648  20.268  1.00 15.93 ? 135 SER A O   1 
ATOM   1110 C  CB  . SER A 1 134 ? -2.890  10.563  17.623  1.00 16.25 ? 135 SER A CB  1 
ATOM   1111 O  OG  . SER A 1 134 ? -1.888  11.389  17.010  1.00 19.16 ? 135 SER A OG  1 
ATOM   1112 N  N   . GLN A 1 135 ? -2.033  12.841  20.000  1.00 13.95 ? 136 GLN A N   1 
ATOM   1113 C  CA  . GLN A 1 135 ? -0.968  13.327  20.873  1.00 15.01 ? 136 GLN A CA  1 
ATOM   1114 C  C   . GLN A 1 135 ? -1.429  13.525  22.320  1.00 15.02 ? 136 GLN A C   1 
ATOM   1115 O  O   . GLN A 1 135 ? -0.655  14.038  23.150  1.00 19.82 ? 136 GLN A O   1 
ATOM   1116 C  CB  . GLN A 1 135 ? -0.424  14.660  20.329  1.00 17.43 ? 136 GLN A CB  1 
ATOM   1117 C  CG  . GLN A 1 135 ? -0.029  14.603  18.863  1.00 19.77 ? 136 GLN A CG  1 
ATOM   1118 C  CD  . GLN A 1 135 ? 0.950   13.501  18.577  1.00 27.56 ? 136 GLN A CD  1 
ATOM   1119 O  OE1 . GLN A 1 135 ? 1.986   13.371  19.237  1.00 36.82 ? 136 GLN A OE1 1 
ATOM   1120 N  NE2 . GLN A 1 135 ? 0.614   12.690  17.598  1.00 40.63 ? 136 GLN A NE2 1 
ATOM   1121 N  N   . GLN A 1 136 ? -2.671  13.101  22.637  1.00 13.79 ? 137 GLN A N   1 
ATOM   1122 C  CA  . GLN A 1 136 ? -3.258  13.414  23.935  1.00 14.13 ? 137 GLN A CA  1 
ATOM   1123 C  C   . GLN A 1 136 ? -3.618  12.133  24.650  1.00 14.11 ? 137 GLN A C   1 
ATOM   1124 O  O   . GLN A 1 136 ? -3.977  11.127  24.016  1.00 13.02 ? 137 GLN A O   1 
ATOM   1125 C  CB  . GLN A 1 136 ? -4.530  14.259  23.757  1.00 16.32 ? 137 GLN A CB  1 
ATOM   1126 C  CG  . GLN A 1 136 ? -4.365  15.545  22.952  1.00 19.54 ? 137 GLN A CG  1 
ATOM   1127 C  CD  . GLN A 1 136 ? -3.310  16.446  23.549  1.00 22.88 ? 137 GLN A CD  1 
ATOM   1128 O  OE1 . GLN A 1 136 ? -3.120  16.436  24.760  1.00 23.19 ? 137 GLN A OE1 1 
ATOM   1129 N  NE2 . GLN A 1 136 ? -2.622  17.198  22.697  1.00 32.41 ? 137 GLN A NE2 1 
ATOM   1130 N  N   . PRO A 1 137 ? -3.592  12.131  25.995  1.00 14.85 ? 138 PRO A N   1 
ATOM   1131 C  CA  . PRO A 1 137 ? -3.756  10.863  26.705  1.00 15.67 ? 138 PRO A CA  1 
ATOM   1132 C  C   . PRO A 1 137 ? -5.176  10.316  26.622  1.00 13.65 ? 138 PRO A C   1 
ATOM   1133 O  O   . PRO A 1 137 ? -5.345  9.106   26.749  1.00 18.04 ? 138 PRO A O   1 
ATOM   1134 C  CB  . PRO A 1 137 ? -3.405  11.222  28.170  1.00 20.08 ? 138 PRO A CB  1 
ATOM   1135 C  CG  . PRO A 1 137 ? -3.630  12.736  28.168  1.00 22.34 ? 138 PRO A CG  1 
ATOM   1136 C  CD  . PRO A 1 137 ? -3.145  13.255  26.843  1.00 17.87 ? 138 PRO A CD  1 
ATOM   1137 N  N   . ASP A 1 138 ? -6.172  11.184  26.324  1.00 13.58 ? 139 ASP A N   1 
ATOM   1138 C  CA  . ASP A 1 138 ? -7.567  10.788  26.089  1.00 14.65 ? 139 ASP A CA  1 
ATOM   1139 C  C   . ASP A 1 138 ? -7.980  11.221  24.701  1.00 11.99 ? 139 ASP A C   1 
ATOM   1140 O  O   . ASP A 1 138 ? -9.118  11.614  24.470  1.00 14.07 ? 139 ASP A O   1 
ATOM   1141 C  CB  . ASP A 1 138 ? -8.468  11.476  27.130  1.00 18.15 ? 139 ASP A CB  1 
ATOM   1142 C  CG  . ASP A 1 138 ? -8.404  12.984  27.040  1.00 17.84 ? 139 ASP A CG  1 
ATOM   1143 O  OD1 . ASP A 1 138 ? -7.412  13.563  26.428  1.00 19.16 ? 139 ASP A OD1 1 
ATOM   1144 O  OD2 . ASP A 1 138 ? -9.262  13.629  27.735  1.00 25.57 ? 139 ASP A OD2 1 
ATOM   1145 N  N   . GLY A 1 139 ? -7.068  11.086  23.734  1.00 11.54 ? 140 GLY A N   1 
ATOM   1146 C  CA  . GLY A 1 139 ? -7.291  11.568  22.364  1.00 11.42 ? 140 GLY A CA  1 
ATOM   1147 C  C   . GLY A 1 139 ? -8.229  10.656  21.548  1.00 10.42 ? 140 GLY A C   1 
ATOM   1148 O  O   . GLY A 1 139 ? -8.963  11.169  20.726  1.00 10.72 ? 140 GLY A O   1 
ATOM   1149 N  N   . LEU A 1 140 ? -8.092  9.342   21.702  1.00 9.60  ? 141 LEU A N   1 
ATOM   1150 C  CA  . LEU A 1 140 ? -8.796  8.428   20.821  1.00 9.50  ? 141 LEU A CA  1 
ATOM   1151 C  C   . LEU A 1 140 ? -9.618  7.461   21.613  1.00 9.49  ? 141 LEU A C   1 
ATOM   1152 O  O   . LEU A 1 140 ? -9.286  7.169   22.781  1.00 9.41  ? 141 LEU A O   1 
ATOM   1153 C  CB  . LEU A 1 140 ? -7.841  7.601   19.951  1.00 10.63 ? 141 LEU A CB  1 
ATOM   1154 C  CG  . LEU A 1 140 ? -6.876  8.378   19.061  1.00 11.98 ? 141 LEU A CG  1 
ATOM   1155 C  CD1 . LEU A 1 140 ? -6.024  7.431   18.212  1.00 14.14 ? 141 LEU A CD1 1 
ATOM   1156 C  CD2 . LEU A 1 140 ? -7.560  9.378   18.181  1.00 13.29 ? 141 LEU A CD2 1 
ATOM   1157 N  N   . ALA A 1 141 ? -10.685 6.938   21.003  1.00 9.50  ? 142 ALA A N   1 
ATOM   1158 C  CA  . ALA A 1 141 ? -11.464 5.859   21.577  1.00 10.12 ? 142 ALA A CA  1 
ATOM   1159 C  C   . ALA A 1 141 ? -11.544 4.877   20.432  1.00 9.83  ? 142 ALA A C   1 
ATOM   1160 O  O   . ALA A 1 141 ? -12.027 5.220   19.365  1.00 10.13 ? 142 ALA A O   1 
ATOM   1161 C  CB  . ALA A 1 141 ? -12.840 6.307   22.060  1.00 11.35 ? 142 ALA A CB  1 
ATOM   1162 N  N   . VAL A 1 142 ? -11.082 3.654   20.684  1.00 9.42  ? 143 VAL A N   1 
ATOM   1163 C  CA  . VAL A 1 142 ? -11.125 2.605   19.661  1.00 10.23 ? 143 VAL A CA  1 
ATOM   1164 C  C   . VAL A 1 142 ? -12.118 1.552   20.145  1.00 8.64  ? 143 VAL A C   1 
ATOM   1165 O  O   . VAL A 1 142 ? -11.972 1.051   21.271  1.00 9.86  ? 143 VAL A O   1 
ATOM   1166 C  CB  . VAL A 1 142 ? -9.755  1.986   19.325  1.00 8.97  ? 143 VAL A CB  1 
ATOM   1167 C  CG1 . VAL A 1 142 ? -9.966  0.977   18.194  1.00 10.69 ? 143 VAL A CG1 1 
ATOM   1168 C  CG2 . VAL A 1 142 ? -8.817  3.103   18.864  1.00 11.09 ? 143 VAL A CG2 1 
ATOM   1169 N  N   . LEU A 1 143 ? -13.157 1.348   19.336  1.00 8.80  ? 144 LEU A N   1 
ATOM   1170 C  CA  . LEU A 1 143 ? -14.103 0.279   19.577  1.00 9.92  ? 144 LEU A CA  1 
ATOM   1171 C  C   . LEU A 1 143 ? -13.584 -0.982  18.884  1.00 9.35  ? 144 LEU A C   1 
ATOM   1172 O  O   . LEU A 1 143 ? -13.442 -1.003  17.642  1.00 10.29 ? 144 LEU A O   1 
ATOM   1173 C  CB  . LEU A 1 143 ? -15.459 0.715   19.035  1.00 11.16 ? 144 LEU A CB  1 
ATOM   1174 C  CG  . LEU A 1 143 ? -16.635 -0.229  19.251  1.00 11.95 ? 144 LEU A CG  1 
ATOM   1175 C  CD1 . LEU A 1 143 ? -16.872 -0.457  20.736  1.00 14.46 ? 144 LEU A CD1 1 
ATOM   1176 C  CD2 . LEU A 1 143 ? -17.878 0.361   18.600  1.00 14.05 ? 144 LEU A CD2 1 
ATOM   1177 N  N   . GLY A 1 144 ? -13.243 -1.991  19.698  1.00 9.20  ? 145 GLY A N   1 
ATOM   1178 C  CA  . GLY A 1 144 ? -12.685 -3.233  19.196  1.00 8.44  ? 145 GLY A CA  1 
ATOM   1179 C  C   . GLY A 1 144 ? -13.756 -4.310  19.172  1.00 7.96  ? 145 GLY A C   1 
ATOM   1180 O  O   . GLY A 1 144 ? -14.441 -4.453  20.168  1.00 10.15 ? 145 GLY A O   1 
ATOM   1181 N  N   . ILE A 1 145 ? -13.842 -5.032  18.067  1.00 8.71  ? 146 ILE A N   1 
ATOM   1182 C  CA  . ILE A 1 145 ? -14.840 -6.059  17.883  1.00 9.68  ? 146 ILE A CA  1 
ATOM   1183 C  C   . ILE A 1 145 ? -14.112 -7.289  17.374  1.00 9.39  ? 146 ILE A C   1 
ATOM   1184 O  O   . ILE A 1 145 ? -13.428 -7.224  16.341  1.00 10.22 ? 146 ILE A O   1 
ATOM   1185 C  CB  . ILE A 1 145 ? -15.929 -5.589  16.890  1.00 10.10 ? 146 ILE A CB  1 
ATOM   1186 C  CG1 . ILE A 1 145 ? -16.551 -4.282  17.441  1.00 11.66 ? 146 ILE A CG1 1 
ATOM   1187 C  CG2 . ILE A 1 145 ? -16.933 -6.709  16.672  1.00 12.31 ? 146 ILE A CG2 1 
ATOM   1188 C  CD1 . ILE A 1 145 ? -17.650 -3.702  16.570  1.00 11.80 ? 146 ILE A CD1 1 
ATOM   1189 N  N   . PHE A 1 146 ? -14.335 -8.433  18.035  1.00 9.47  ? 147 PHE A N   1 
ATOM   1190 C  CA  . PHE A 1 146 ? -13.692 -9.668  17.625  1.00 10.13 ? 147 PHE A CA  1 
ATOM   1191 C  C   . PHE A 1 146 ? -14.489 -10.306 16.495  1.00 10.31 ? 147 PHE A C   1 
ATOM   1192 O  O   . PHE A 1 146 ? -15.708 -10.159 16.409  1.00 11.83 ? 147 PHE A O   1 
ATOM   1193 C  CB  . PHE A 1 146 ? -13.723 -10.644 18.793  1.00 10.64 ? 147 PHE A CB  1 
ATOM   1194 C  CG  . PHE A 1 146 ? -12.883 -10.183 19.946  1.00 9.76  ? 147 PHE A CG  1 
ATOM   1195 C  CD1 . PHE A 1 146 ? -11.499 -10.039 19.796  1.00 10.52 ? 147 PHE A CD1 1 
ATOM   1196 C  CD2 . PHE A 1 146 ? -13.409 -9.935  21.211  1.00 10.84 ? 147 PHE A CD2 1 
ATOM   1197 C  CE1 . PHE A 1 146 ? -10.686 -9.639  20.842  1.00 9.79  ? 147 PHE A CE1 1 
ATOM   1198 C  CE2 . PHE A 1 146 ? -12.583 -9.528  22.254  1.00 11.26 ? 147 PHE A CE2 1 
ATOM   1199 C  CZ  . PHE A 1 146 ? -11.233 -9.398  22.086  1.00 10.30 ? 147 PHE A CZ  1 
ATOM   1200 N  N   . LEU A 1 147 ? -13.779 -10.987 15.616  1.00 10.33 ? 148 LEU A N   1 
ATOM   1201 C  CA  . LEU A 1 147 ? -14.357 -11.752 14.511  1.00 10.40 ? 148 LEU A CA  1 
ATOM   1202 C  C   . LEU A 1 147 ? -14.046 -13.218 14.786  1.00 10.12 ? 148 LEU A C   1 
ATOM   1203 O  O   . LEU A 1 147 ? -12.877 -13.600 14.957  1.00 11.34 ? 148 LEU A O   1 
ATOM   1204 C  CB  . LEU A 1 147 ? -13.770 -11.357 13.143  1.00 11.29 ? 148 LEU A CB  1 
ATOM   1205 C  CG  . LEU A 1 147 ? -14.336 -10.086 12.509  1.00 10.34 ? 148 LEU A CG  1 
ATOM   1206 C  CD1 . LEU A 1 147 ? -14.118 -8.830  13.402  1.00 12.39 ? 148 LEU A CD1 1 
ATOM   1207 C  CD2 . LEU A 1 147 ? -13.733 -9.852  11.131  1.00 12.34 ? 148 LEU A CD2 1 
ATOM   1208 N  N   . LYS A 1 148 ? -15.105 -14.042 14.759  1.00 10.73 ? 149 LYS A N   1 
ATOM   1209 C  CA  . LYS A 1 148 ? -14.945 -15.480 14.742  1.00 11.73 ? 149 LYS A CA  1 
ATOM   1210 C  C   . LYS A 1 148 ? -15.423 -16.010 13.394  1.00 11.65 ? 149 LYS A C   1 
ATOM   1211 O  O   . LYS A 1 148 ? -16.279 -15.367 12.766  1.00 13.68 ? 149 LYS A O   1 
ATOM   1212 C  CB  . LYS A 1 148 ? -15.691 -16.174 15.885  1.00 14.94 ? 149 LYS A CB  1 
ATOM   1213 C  CG  . LYS A 1 148 ? -17.188 -16.075 15.813  1.00 15.23 ? 149 LYS A CG  1 
ATOM   1214 C  CD  . LYS A 1 148 ? -17.861 -16.801 16.971  1.00 21.96 ? 149 LYS A CD  1 
ATOM   1215 C  CE  . LYS A 1 148 ? -19.374 -16.753 16.891  1.00 32.07 ? 149 LYS A CE  1 
ATOM   1216 N  NZ  . LYS A 1 148 ? -20.000 -17.592 17.939  1.00 46.33 ? 149 LYS A NZ  1 
ATOM   1217 N  N   . VAL A 1 149 ? -14.933 -17.164 12.986  1.00 12.18 ? 150 VAL A N   1 
ATOM   1218 C  CA  . VAL A 1 149 ? -15.289 -17.696 11.680  1.00 12.15 ? 150 VAL A CA  1 
ATOM   1219 C  C   . VAL A 1 149 ? -16.468 -18.644 11.868  1.00 12.04 ? 150 VAL A C   1 
ATOM   1220 O  O   . VAL A 1 149 ? -16.423 -19.606 12.672  1.00 15.00 ? 150 VAL A O   1 
ATOM   1221 C  CB  . VAL A 1 149 ? -14.074 -18.399 11.050  1.00 12.15 ? 150 VAL A CB  1 
ATOM   1222 C  CG1 . VAL A 1 149 ? -14.454 -19.146 9.790   1.00 15.55 ? 150 VAL A CG1 1 
ATOM   1223 C  CG2 . VAL A 1 149 ? -13.030 -17.357 10.758  1.00 15.52 ? 150 VAL A CG2 1 
ATOM   1224 N  N   . GLY A 1 150 ? -17.536 -18.387 11.124  1.00 12.95 ? 151 GLY A N   1 
ATOM   1225 C  CA  . GLY A 1 150 ? -18.710 -19.222 11.195  1.00 13.34 ? 151 GLY A CA  1 
ATOM   1226 C  C   . GLY A 1 150 ? -19.663 -18.777 10.108  1.00 11.91 ? 151 GLY A C   1 
ATOM   1227 O  O   . GLY A 1 150 ? -19.318 -18.809 8.939   1.00 12.19 ? 151 GLY A O   1 
ATOM   1228 N  N   A SER A 1 151 ? -20.849 -18.310 10.470  0.50 13.28 ? 152 SER A N   1 
ATOM   1229 N  N   B SER A 1 151 ? -20.815 -18.235 10.529  0.50 13.10 ? 152 SER A N   1 
ATOM   1230 C  CA  A SER A 1 151 ? -21.682 -17.772 9.392   0.50 13.80 ? 152 SER A CA  1 
ATOM   1231 C  CA  B SER A 1 151 ? -21.750 -17.592 9.594   0.50 13.54 ? 152 SER A CA  1 
ATOM   1232 C  C   A SER A 1 151 ? -21.168 -16.405 8.935   0.50 12.04 ? 152 SER A C   1 
ATOM   1233 C  C   B SER A 1 151 ? -21.138 -16.346 8.950   0.50 12.23 ? 152 SER A C   1 
ATOM   1234 O  O   A SER A 1 151 ? -20.454 -15.701 9.645   0.50 12.64 ? 152 SER A O   1 
ATOM   1235 O  O   B SER A 1 151 ? -20.316 -15.662 9.551   0.50 13.45 ? 152 SER A O   1 
ATOM   1236 C  CB  A SER A 1 151 ? -23.081 -17.669 9.853   0.50 14.78 ? 152 SER A CB  1 
ATOM   1237 C  CB  B SER A 1 151 ? -23.035 -17.233 10.285  0.50 16.59 ? 152 SER A CB  1 
ATOM   1238 O  OG  A SER A 1 151 ? -23.085 -16.713 10.885  0.50 18.79 ? 152 SER A OG  1 
ATOM   1239 O  OG  B SER A 1 151 ? -23.686 -18.393 10.759  0.50 21.80 ? 152 SER A OG  1 
ATOM   1240 N  N   . ALA A 1 152 ? -21.555 -16.026 7.717   1.00 13.72 ? 153 ALA A N   1 
ATOM   1241 C  CA  . ALA A 1 152 ? -21.110 -14.779 7.113   1.00 13.79 ? 153 ALA A CA  1 
ATOM   1242 C  C   . ALA A 1 152 ? -21.742 -13.572 7.811   1.00 12.29 ? 153 ALA A C   1 
ATOM   1243 O  O   . ALA A 1 152 ? -22.811 -13.659 8.392   1.00 13.77 ? 153 ALA A O   1 
ATOM   1244 C  CB  . ALA A 1 152 ? -21.501 -14.752 5.656   1.00 13.76 ? 153 ALA A CB  1 
ATOM   1245 N  N   . LYS A 1 153 ? -21.057 -12.421 7.757   1.00 11.58 ? 154 LYS A N   1 
ATOM   1246 C  CA  . LYS A 1 153 ? -21.590 -11.150 8.216   1.00 11.21 ? 154 LYS A CA  1 
ATOM   1247 C  C   . LYS A 1 153 ? -22.024 -10.404 6.960   1.00 10.59 ? 154 LYS A C   1 
ATOM   1248 O  O   . LYS A 1 153 ? -21.170 -9.925  6.184   1.00 11.45 ? 154 LYS A O   1 
ATOM   1249 C  CB  . LYS A 1 153 ? -20.489 -10.360 8.948   1.00 11.25 ? 154 LYS A CB  1 
ATOM   1250 C  CG  . LYS A 1 153 ? -21.074 -9.131  9.671   1.00 11.43 ? 154 LYS A CG  1 
ATOM   1251 C  CD  . LYS A 1 153 ? -21.908 -9.496  10.842  1.00 13.78 ? 154 LYS A CD  1 
ATOM   1252 C  CE  . LYS A 1 153 ? -22.202 -8.321  11.755  1.00 18.07 ? 154 LYS A CE  1 
ATOM   1253 N  NZ  . LYS A 1 153 ? -23.129 -8.733  12.829  1.00 21.74 ? 154 LYS A NZ  1 
ATOM   1254 N  N   A PRO A 1 154 ? -23.335 -10.365 6.643   0.50 11.52 ? 155 PRO A N   1 
ATOM   1255 N  N   B PRO A 1 154 ? -23.331 -10.243 6.672   0.50 10.94 ? 155 PRO A N   1 
ATOM   1256 C  CA  A PRO A 1 154 ? -23.789 -9.675  5.427   0.50 12.66 ? 155 PRO A CA  1 
ATOM   1257 C  CA  B PRO A 1 154 ? -23.672 -9.699  5.351   0.50 11.73 ? 155 PRO A CA  1 
ATOM   1258 C  C   A PRO A 1 154 ? -23.225 -8.275  5.248   0.50 11.25 ? 155 PRO A C   1 
ATOM   1259 C  C   B PRO A 1 154 ? -23.190 -8.259  5.226   0.50 11.33 ? 155 PRO A C   1 
ATOM   1260 O  O   A PRO A 1 154 ? -22.845 -7.922  4.133   0.50 12.27 ? 155 PRO A O   1 
ATOM   1261 O  O   B PRO A 1 154 ? -22.834 -7.846  4.123   0.50 12.78 ? 155 PRO A O   1 
ATOM   1262 C  CB  A PRO A 1 154 ? -25.305 -9.708  5.672   0.50 13.79 ? 155 PRO A CB  1 
ATOM   1263 C  CB  B PRO A 1 154 ? -25.200 -9.836  5.216   0.50 13.89 ? 155 PRO A CB  1 
ATOM   1264 C  CG  A PRO A 1 154 ? -25.407 -11.150 6.137   0.50 13.13 ? 155 PRO A CG  1 
ATOM   1265 C  CG  B PRO A 1 154 ? -25.645 -10.585 6.485   0.50 15.20 ? 155 PRO A CG  1 
ATOM   1266 C  CD  A PRO A 1 154 ? -24.433 -11.113 7.306   0.50 11.77 ? 155 PRO A CD  1 
ATOM   1267 C  CD  B PRO A 1 154 ? -24.504 -10.613 7.505   0.50 10.99 ? 155 PRO A CD  1 
ATOM   1268 N  N   . GLY A 1 155 ? -23.121 -7.524  6.357   1.00 11.77 ? 156 GLY A N   1 
ATOM   1269 C  CA  . GLY A 1 155 ? -22.683 -6.128  6.309   1.00 12.87 ? 156 GLY A CA  1 
ATOM   1270 C  C   . GLY A 1 155 ? -21.198 -5.984  6.033   1.00 12.73 ? 156 GLY A C   1 
ATOM   1271 O  O   . GLY A 1 155 ? -20.800 -4.857  5.772   1.00 14.58 ? 156 GLY A O   1 
ATOM   1272 N  N   . LEU A 1 156 ? -20.435 -7.069  6.109   1.00 10.34 ? 157 LEU A N   1 
ATOM   1273 C  CA  . LEU A 1 156 ? -19.027 -7.007  5.725   1.00 9.93  ? 157 LEU A CA  1 
ATOM   1274 C  C   . LEU A 1 156 ? -18.790 -7.199  4.238   1.00 9.68  ? 157 LEU A C   1 
ATOM   1275 O  O   . LEU A 1 156 ? -17.712 -6.923  3.705   1.00 11.04 ? 157 LEU A O   1 
ATOM   1276 C  CB  . LEU A 1 156 ? -18.281 -8.056  6.541   1.00 11.48 ? 157 LEU A CB  1 
ATOM   1277 C  CG  . LEU A 1 156 ? -16.783 -8.188  6.351   1.00 10.69 ? 157 LEU A CG  1 
ATOM   1278 C  CD1 . LEU A 1 156 ? -16.023 -6.895  6.680   1.00 13.19 ? 157 LEU A CD1 1 
ATOM   1279 C  CD2 . LEU A 1 156 ? -16.267 -9.347  7.172   1.00 12.98 ? 157 LEU A CD2 1 
ATOM   1280 N  N   . GLN A 1 157 ? -19.791 -7.751  3.529   1.00 10.92 ? 158 GLN A N   1 
ATOM   1281 C  CA  . GLN A 1 157 ? -19.550 -8.206  2.180   1.00 10.70 ? 158 GLN A CA  1 
ATOM   1282 C  C   . GLN A 1 157 ? -19.113 -7.082  1.251   1.00 10.51 ? 158 GLN A C   1 
ATOM   1283 O  O   . GLN A 1 157 ? -18.271 -7.329  0.390   1.00 10.75 ? 158 GLN A O   1 
ATOM   1284 C  CB  . GLN A 1 157 ? -20.761 -8.995  1.685   1.00 12.69 ? 158 GLN A CB  1 
ATOM   1285 C  CG  . GLN A 1 157 ? -20.441 -9.763  0.403   1.00 12.28 ? 158 GLN A CG  1 
ATOM   1286 C  CD  . GLN A 1 157 ? -19.369 -10.787 0.644   1.00 11.78 ? 158 GLN A CD  1 
ATOM   1287 O  OE1 . GLN A 1 157 ? -19.239 -11.365 1.715   1.00 13.55 ? 158 GLN A OE1 1 
ATOM   1288 N  NE2 . GLN A 1 157 ? -18.616 -11.142 -0.381  1.00 13.93 ? 158 GLN A NE2 1 
ATOM   1289 N  N   . LYS A 1 158 ? -19.641 -5.856  1.398   1.00 11.05 ? 159 LYS A N   1 
ATOM   1290 C  CA  . LYS A 1 158 ? -19.295 -4.811  0.486   1.00 11.45 ? 159 LYS A CA  1 
ATOM   1291 C  C   . LYS A 1 158 ? -17.788 -4.512  0.589   1.00 10.85 ? 159 LYS A C   1 
ATOM   1292 O  O   . LYS A 1 158 ? -17.160 -4.157  -0.406  1.00 13.15 ? 159 LYS A O   1 
ATOM   1293 C  CB  . LYS A 1 158 ? -20.107 -3.566  0.823   1.00 14.76 ? 159 LYS A CB  1 
ATOM   1294 C  CG  . LYS A 1 158 ? -19.819 -2.374  -0.079  1.00 18.57 ? 159 LYS A CG  1 
ATOM   1295 C  CD  . LYS A 1 158 ? -20.724 -1.152  0.280   1.00 23.63 ? 159 LYS A CD  1 
ATOM   1296 C  CE  . LYS A 1 158 ? -20.417 0.175   -0.429  1.00 28.38 ? 159 LYS A CE  1 
ATOM   1297 N  NZ  . LYS A 1 158 ? -20.832 0.145   -1.855  1.00 22.03 ? 159 LYS A NZ  1 
ATOM   1298 N  N   . VAL A 1 159 ? -17.226 -4.620  1.828   1.00 10.73 ? 160 VAL A N   1 
ATOM   1299 C  CA  . VAL A 1 159 ? -15.799 -4.453  2.013   1.00 11.39 ? 160 VAL A CA  1 
ATOM   1300 C  C   . VAL A 1 159 ? -15.031 -5.593  1.348   1.00 10.92 ? 160 VAL A C   1 
ATOM   1301 O  O   . VAL A 1 159 ? -14.101 -5.375  0.571   1.00 12.37 ? 160 VAL A O   1 
ATOM   1302 C  CB  . VAL A 1 159 ? -15.492 -4.457  3.521   1.00 11.79 ? 160 VAL A CB  1 
ATOM   1303 C  CG1 . VAL A 1 159 ? -13.970 -4.528  3.745   1.00 13.23 ? 160 VAL A CG1 1 
ATOM   1304 C  CG2 . VAL A 1 159 ? -16.015 -3.183  4.156   1.00 14.72 ? 160 VAL A CG2 1 
ATOM   1305 N  N   . VAL A 1 160 ? -15.392 -6.835  1.623   1.00 11.40 ? 161 VAL A N   1 
ATOM   1306 C  CA  . VAL A 1 160 ? -14.670 -8.006  1.125   1.00 12.87 ? 161 VAL A CA  1 
ATOM   1307 C  C   . VAL A 1 160 ? -14.586 -7.953  -0.393  1.00 11.44 ? 161 VAL A C   1 
ATOM   1308 O  O   . VAL A 1 160 ? -13.559 -8.287  -1.018  1.00 12.44 ? 161 VAL A O   1 
ATOM   1309 C  CB  . VAL A 1 160 ? -15.354 -9.348  1.592   1.00 17.43 ? 161 VAL A CB  1 
ATOM   1310 C  CG1 . VAL A 1 160 ? -15.142 -10.589 0.715   1.00 20.00 ? 161 VAL A CG1 1 
ATOM   1311 C  CG2 . VAL A 1 160 ? -15.068 -9.527  3.079   1.00 22.51 ? 161 VAL A CG2 1 
ATOM   1312 N  N   . ASP A 1 161 ? -15.704 -7.546  -1.006  1.00 11.69 ? 162 ASP A N   1 
ATOM   1313 C  CA  . ASP A 1 161 ? -15.800 -7.608  -2.443  1.00 11.46 ? 162 ASP A CA  1 
ATOM   1314 C  C   . ASP A 1 161 ? -14.951 -6.588  -3.203  1.00 12.50 ? 162 ASP A C   1 
ATOM   1315 O  O   . ASP A 1 161 ? -14.748 -6.776  -4.389  1.00 14.99 ? 162 ASP A O   1 
ATOM   1316 C  CB  . ASP A 1 161 ? -17.231 -7.500  -2.912  1.00 14.88 ? 162 ASP A CB  1 
ATOM   1317 C  CG  . ASP A 1 161 ? -17.981 -8.825  -2.851  1.00 14.80 ? 162 ASP A CG  1 
ATOM   1318 O  OD1 . ASP A 1 161 ? -17.357 -9.902  -2.847  1.00 18.19 ? 162 ASP A OD1 1 
ATOM   1319 O  OD2 . ASP A 1 161 ? -19.223 -8.759  -2.751  1.00 15.74 ? 162 ASP A OD2 1 
ATOM   1320 N  N   A VAL A 1 162 ? -14.393 -5.576  -2.538  0.50 12.72 ? 163 VAL A N   1 
ATOM   1321 N  N   B VAL A 1 162 ? -14.462 -5.534  -2.541  0.50 13.11 ? 163 VAL A N   1 
ATOM   1322 C  CA  A VAL A 1 162 ? -13.558 -4.576  -3.178  0.50 12.05 ? 163 VAL A CA  1 
ATOM   1323 C  CA  B VAL A 1 162 ? -13.566 -4.619  -3.227  0.50 12.24 ? 163 VAL A CA  1 
ATOM   1324 C  C   A VAL A 1 162 ? -12.084 -4.851  -2.917  0.50 11.13 ? 163 VAL A C   1 
ATOM   1325 C  C   B VAL A 1 162 ? -12.104 -4.808  -2.859  0.50 11.40 ? 163 VAL A C   1 
ATOM   1326 O  O   A VAL A 1 162 ? -11.223 -4.233  -3.547  0.50 11.95 ? 163 VAL A O   1 
ATOM   1327 O  O   B VAL A 1 162 ? -11.271 -4.072  -3.385  0.50 12.59 ? 163 VAL A O   1 
ATOM   1328 C  CB  A VAL A 1 162 ? -13.948 -3.161  -2.712  0.50 14.17 ? 163 VAL A CB  1 
ATOM   1329 C  CB  B VAL A 1 162 ? -13.953 -3.144  -3.064  0.50 12.89 ? 163 VAL A CB  1 
ATOM   1330 C  CG1 A VAL A 1 162 ? -13.513 -2.858  -1.293  0.50 15.10 ? 163 VAL A CG1 1 
ATOM   1331 C  CG1 B VAL A 1 162 ? -15.368 -2.897  -3.553  0.50 10.58 ? 163 VAL A CG1 1 
ATOM   1332 C  CG2 A VAL A 1 162 ? -13.461 -2.060  -3.616  0.50 17.92 ? 163 VAL A CG2 1 
ATOM   1333 C  CG2 B VAL A 1 162 ? -13.768 -2.632  -1.645  0.50 13.78 ? 163 VAL A CG2 1 
ATOM   1334 N  N   . LEU A 1 163 ? -11.757 -5.802  -2.036  1.00 11.38 ? 164 LEU A N   1 
ATOM   1335 C  CA  . LEU A 1 163 ? -10.360 -5.940  -1.647  1.00 10.94 ? 164 LEU A CA  1 
ATOM   1336 C  C   . LEU A 1 163 ? -9.481  -6.307  -2.850  1.00 11.16 ? 164 LEU A C   1 
ATOM   1337 O  O   . LEU A 1 163 ? -8.279  -5.997  -2.853  1.00 12.42 ? 164 LEU A O   1 
ATOM   1338 C  CB  . LEU A 1 163 ? -10.252 -6.972  -0.534  1.00 10.99 ? 164 LEU A CB  1 
ATOM   1339 C  CG  . LEU A 1 163 ? -10.908 -6.549  0.800   1.00 10.77 ? 164 LEU A CG  1 
ATOM   1340 C  CD1 . LEU A 1 163 ? -10.700 -7.643  1.843   1.00 12.85 ? 164 LEU A CD1 1 
ATOM   1341 C  CD2 . LEU A 1 163 ? -10.303 -5.198  1.287   1.00 12.40 ? 164 LEU A CD2 1 
ATOM   1342 N  N   . ASP A 1 164 ? -9.996  -7.016  -3.845  1.00 12.21 ? 165 ASP A N   1 
ATOM   1343 C  CA  . ASP A 1 164 ? -9.186  -7.358  -5.019  1.00 15.41 ? 165 ASP A CA  1 
ATOM   1344 C  C   . ASP A 1 164 ? -8.644  -6.097  -5.701  1.00 13.21 ? 165 ASP A C   1 
ATOM   1345 O  O   . ASP A 1 164 ? -7.659  -6.207  -6.449  1.00 17.52 ? 165 ASP A O   1 
ATOM   1346 C  CB  . ASP A 1 164 ? -9.933  -8.245  -6.019  1.00 17.49 ? 165 ASP A CB  1 
ATOM   1347 C  CG  . ASP A 1 164 ? -11.017 -7.430  -6.725  1.00 19.77 ? 165 ASP A CG  1 
ATOM   1348 O  OD1 . ASP A 1 164 ? -12.035 -7.003  -6.049  1.00 22.38 ? 165 ASP A OD1 1 
ATOM   1349 O  OD2 . ASP A 1 164 ? -10.836 -7.154  -7.978  1.00 29.88 ? 165 ASP A OD2 1 
ATOM   1350 N  N   . SER A 1 165 ? -9.320  -4.954  -5.504  1.00 13.38 ? 166 SER A N   1 
ATOM   1351 C  CA  . SER A 1 165 ? -8.900  -3.719  -6.158  1.00 15.41 ? 166 SER A CA  1 
ATOM   1352 C  C   . SER A 1 165 ? -7.794  -2.985  -5.398  1.00 13.83 ? 166 SER A C   1 
ATOM   1353 O  O   . SER A 1 165 ? -7.263  -1.969  -5.879  1.00 14.65 ? 166 SER A O   1 
ATOM   1354 C  CB  . SER A 1 165 ? -10.059 -2.827  -6.414  1.00 17.35 ? 166 SER A CB  1 
ATOM   1355 O  OG  . SER A 1 165 ? -10.545 -2.273  -5.205  1.00 16.40 ? 166 SER A OG  1 
ATOM   1356 N  N   . ILE A 1 166 ? -7.501  -3.414  -4.176  1.00 11.82 ? 167 ILE A N   1 
ATOM   1357 C  CA  . ILE A 1 166 ? -6.476  -2.746  -3.371  1.00 11.45 ? 167 ILE A CA  1 
ATOM   1358 C  C   . ILE A 1 166 ? -5.458  -3.769  -2.869  1.00 11.23 ? 167 ILE A C   1 
ATOM   1359 O  O   . ILE A 1 166 ? -5.067  -3.778  -1.698  1.00 12.13 ? 167 ILE A O   1 
ATOM   1360 C  CB  . ILE A 1 166 ? -7.086  -1.914  -2.220  1.00 11.44 ? 167 ILE A CB  1 
ATOM   1361 C  CG1 . ILE A 1 166 ? -7.945  -2.740  -1.266  1.00 10.92 ? 167 ILE A CG1 1 
ATOM   1362 C  CG2 . ILE A 1 166 ? -7.882  -0.711  -2.781  1.00 12.79 ? 167 ILE A CG2 1 
ATOM   1363 C  CD1 . ILE A 1 166 ? -8.107  -2.117  0.113   1.00 11.62 ? 167 ILE A CD1 1 
ATOM   1364 N  N   . LYS A 1 167 ? -5.028  -4.677  -3.760  1.00 12.28 ? 168 LYS A N   1 
ATOM   1365 C  CA  . LYS A 1 167 ? -4.266  -5.808  -3.311  1.00 12.52 ? 168 LYS A CA  1 
ATOM   1366 C  C   . LYS A 1 167 ? -2.935  -5.402  -2.670  1.00 13.77 ? 168 LYS A C   1 
ATOM   1367 O  O   . LYS A 1 167 ? -2.521  -6.012  -1.698  1.00 14.23 ? 168 LYS A O   1 
ATOM   1368 C  CB  . LYS A 1 167 ? -4.016  -6.752  -4.492  1.00 14.18 ? 168 LYS A CB  1 
ATOM   1369 C  CG  . LYS A 1 167 ? -3.228  -8.002  -4.101  1.00 16.31 ? 168 LYS A CG  1 
ATOM   1370 C  CD  . LYS A 1 167 ? -3.015  -8.894  -5.309  1.00 23.79 ? 168 LYS A CD  1 
ATOM   1371 C  CE  . LYS A 1 167 ? -1.728  -9.686  -5.282  1.00 34.51 ? 168 LYS A CE  1 
ATOM   1372 N  NZ  . LYS A 1 167 ? -1.533  -10.428 -6.559  1.00 37.54 ? 168 LYS A NZ  1 
ATOM   1373 N  N   . THR A 1 168 ? -2.265  -4.362  -3.214  1.00 14.37 ? 169 THR A N   1 
ATOM   1374 C  CA  . THR A 1 168 ? -0.895  -4.102  -2.751  1.00 15.37 ? 169 THR A CA  1 
ATOM   1375 C  C   . THR A 1 168 ? -0.837  -2.743  -2.069  1.00 13.87 ? 169 THR A C   1 
ATOM   1376 O  O   . THR A 1 168 ? -1.716  -1.891  -2.221  1.00 14.93 ? 169 THR A O   1 
ATOM   1377 C  CB  . THR A 1 168 ? 0.099   -4.164  -3.918  1.00 17.46 ? 169 THR A CB  1 
ATOM   1378 O  OG1 . THR A 1 168 ? -0.482  -3.435  -5.015  1.00 18.10 ? 169 THR A OG1 1 
ATOM   1379 C  CG2 . THR A 1 168 ? 0.320   -5.606  -4.351  1.00 17.71 ? 169 THR A CG2 1 
ATOM   1380 N  N   . LYS A 1 169 ? 0.246   -2.596  -1.300  1.00 14.44 ? 170 LYS A N   1 
ATOM   1381 C  CA  . LYS A 1 169 ? 0.474   -1.401  -0.526  1.00 15.32 ? 170 LYS A CA  1 
ATOM   1382 C  C   . LYS A 1 169 ? 0.395   -0.202  -1.426  1.00 15.14 ? 170 LYS A C   1 
ATOM   1383 O  O   . LYS A 1 169 ? 1.062   -0.119  -2.486  1.00 18.08 ? 170 LYS A O   1 
ATOM   1384 C  CB  . LYS A 1 169 ? 1.877   -1.447  0.080   1.00 16.77 ? 170 LYS A CB  1 
ATOM   1385 C  CG  . LYS A 1 169 ? 2.204   -0.231  0.950   1.00 18.01 ? 170 LYS A CG  1 
ATOM   1386 C  CD  . LYS A 1 169 ? 3.531   -0.378  1.581   1.00 22.35 ? 170 LYS A CD  1 
ATOM   1387 C  CE  . LYS A 1 169 ? 3.925   0.827   2.377   1.00 30.49 ? 170 LYS A CE  1 
ATOM   1388 N  NZ  . LYS A 1 169 ? 5.384   0.733   2.620   1.00 47.76 ? 170 LYS A NZ  1 
ATOM   1389 N  N   . GLY A 1 170 ? -0.358  0.781   -0.988  1.00 14.67 ? 171 GLY A N   1 
ATOM   1390 C  CA  . GLY A 1 170 ? -0.499  2.032   -1.703  1.00 16.75 ? 171 GLY A CA  1 
ATOM   1391 C  C   . GLY A 1 170 ? -1.739  2.146   -2.579  1.00 19.04 ? 171 GLY A C   1 
ATOM   1392 O  O   . GLY A 1 170 ? -2.035  3.262   -3.042  1.00 25.15 ? 171 GLY A O   1 
ATOM   1393 N  N   . LYS A 1 171 ? -2.421  1.017   -2.846  1.00 14.63 ? 172 LYS A N   1 
ATOM   1394 C  CA  . LYS A 1 171 ? -3.622  1.113   -3.681  1.00 15.13 ? 172 LYS A CA  1 
ATOM   1395 C  C   . LYS A 1 171 ? -4.815  1.604   -2.864  1.00 11.62 ? 172 LYS A C   1 
ATOM   1396 O  O   . LYS A 1 171 ? -4.934  1.312   -1.666  1.00 13.48 ? 172 LYS A O   1 
ATOM   1397 C  CB  . LYS A 1 171 ? -3.938  -0.236  -4.314  1.00 14.98 ? 172 LYS A CB  1 
ATOM   1398 C  CG  . LYS A 1 171 ? -2.865  -0.669  -5.324  1.00 17.25 ? 172 LYS A CG  1 
ATOM   1399 C  CD  . LYS A 1 171 ? -3.308  -1.781  -6.209  1.00 18.57 ? 172 LYS A CD  1 
ATOM   1400 C  CE  . LYS A 1 171 ? -4.285  -1.275  -7.263  1.00 24.17 ? 172 LYS A CE  1 
ATOM   1401 N  NZ  . LYS A 1 171 ? -4.908  -2.310  -8.119  1.00 27.21 ? 172 LYS A NZ  1 
ATOM   1402 N  N   . SER A 1 172 ? -5.699  2.350   -3.519  1.00 12.34 ? 173 SER A N   1 
ATOM   1403 C  CA  . SER A 1 172 ? -6.893  2.795   -2.822  1.00 13.46 ? 173 SER A CA  1 
ATOM   1404 C  C   . SER A 1 172 ? -8.031  2.874   -3.846  1.00 12.84 ? 173 SER A C   1 
ATOM   1405 O  O   . SER A 1 172 ? -7.809  2.856   -5.072  1.00 15.33 ? 173 SER A O   1 
ATOM   1406 C  CB  . SER A 1 172 ? -6.721  4.176   -2.195  1.00 15.11 ? 173 SER A CB  1 
ATOM   1407 O  OG  . SER A 1 172 ? -6.427  5.214   -3.131  1.00 19.03 ? 173 SER A OG  1 
ATOM   1408 N  N   . ALA A 1 173 ? -9.266  2.997   -3.352  1.00 14.02 ? 174 ALA A N   1 
ATOM   1409 C  CA  . ALA A 1 173 ? -10.437 3.166   -4.205  1.00 14.45 ? 174 ALA A CA  1 
ATOM   1410 C  C   . ALA A 1 173 ? -11.480 4.011   -3.480  1.00 13.85 ? 174 ALA A C   1 
ATOM   1411 O  O   . ALA A 1 173 ? -11.541 4.025   -2.248  1.00 13.63 ? 174 ALA A O   1 
ATOM   1412 C  CB  . ALA A 1 173 ? -11.072 1.839   -4.528  1.00 16.65 ? 174 ALA A CB  1 
ATOM   1413 N  N   . ASP A 1 174 ? -12.356 4.641   -4.250  1.00 17.03 ? 175 ASP A N   1 
ATOM   1414 C  CA  . ASP A 1 174 ? -13.525 5.262   -3.648  1.00 16.55 ? 175 ASP A CA  1 
ATOM   1415 C  C   . ASP A 1 174 ? -14.364 4.181   -2.975  1.00 14.83 ? 175 ASP A C   1 
ATOM   1416 O  O   . ASP A 1 174 ? -14.461 3.031   -3.392  1.00 16.28 ? 175 ASP A O   1 
ATOM   1417 C  CB  . ASP A 1 174 ? -14.271 6.156   -4.651  1.00 20.04 ? 175 ASP A CB  1 
ATOM   1418 C  CG  . ASP A 1 174 ? -13.429 7.231   -5.335  1.00 27.77 ? 175 ASP A CG  1 
ATOM   1419 O  OD1 . ASP A 1 174 ? -13.099 8.248   -4.686  1.00 42.59 ? 175 ASP A OD1 1 
ATOM   1420 O  OD2 . ASP A 1 174 ? -13.153 7.072   -6.574  1.00 53.16 ? 175 ASP A OD2 1 
ATOM   1421 N  N   . PHE A 1 175 ? -15.005 4.560   -1.869  1.00 13.48 ? 176 PHE A N   1 
ATOM   1422 C  CA  . PHE A 1 175 ? -15.739 3.582   -1.096  1.00 12.11 ? 176 PHE A CA  1 
ATOM   1423 C  C   . PHE A 1 175 ? -16.801 4.330   -0.329  1.00 12.12 ? 176 PHE A C   1 
ATOM   1424 O  O   . PHE A 1 175 ? -16.643 4.567   0.866   1.00 13.44 ? 176 PHE A O   1 
ATOM   1425 C  CB  . PHE A 1 175 ? -14.814 2.797   -0.174  1.00 11.77 ? 176 PHE A CB  1 
ATOM   1426 C  CG  . PHE A 1 175 ? -15.449 1.546   0.329   1.00 12.25 ? 176 PHE A CG  1 
ATOM   1427 C  CD1 . PHE A 1 175 ? -15.759 0.482   -0.508  1.00 14.01 ? 176 PHE A CD1 1 
ATOM   1428 C  CD2 . PHE A 1 175 ? -15.711 1.382   1.692   1.00 12.71 ? 176 PHE A CD2 1 
ATOM   1429 C  CE1 . PHE A 1 175 ? -16.355 -0.689  -0.023  1.00 13.45 ? 176 PHE A CE1 1 
ATOM   1430 C  CE2 . PHE A 1 175 ? -16.301 0.207   2.193   1.00 13.56 ? 176 PHE A CE2 1 
ATOM   1431 C  CZ  . PHE A 1 175 ? -16.602 -0.826  1.340   1.00 12.41 ? 176 PHE A CZ  1 
ATOM   1432 N  N   . THR A 1 176 ? -17.884 4.703   -1.031  1.00 13.68 ? 177 THR A N   1 
ATOM   1433 C  CA  . THR A 1 176 ? -18.923 5.478   -0.413  1.00 12.79 ? 177 THR A CA  1 
ATOM   1434 C  C   . THR A 1 176 ? -20.126 4.628   -0.008  1.00 11.17 ? 177 THR A C   1 
ATOM   1435 O  O   . THR A 1 176 ? -20.292 3.470   -0.436  1.00 13.74 ? 177 THR A O   1 
ATOM   1436 C  CB  . THR A 1 176 ? -19.418 6.597   -1.340  1.00 13.84 ? 177 THR A CB  1 
ATOM   1437 O  OG1 . THR A 1 176 ? -19.885 6.020   -2.559  1.00 16.73 ? 177 THR A OG1 1 
ATOM   1438 C  CG2 . THR A 1 176 ? -18.341 7.638   -1.585  1.00 19.55 ? 177 THR A CG2 1 
ATOM   1439 N  N   . ASN A 1 177 ? -20.935 5.190   0.892   1.00 11.99 ? 178 ASN A N   1 
ATOM   1440 C  CA  . ASN A 1 177 ? -22.183 4.586   1.303   1.00 13.99 ? 178 ASN A CA  1 
ATOM   1441 C  C   . ASN A 1 177 ? -21.955 3.254   2.029   1.00 12.78 ? 178 ASN A C   1 
ATOM   1442 O  O   . ASN A 1 177 ? -22.896 2.444   2.055   1.00 17.34 ? 178 ASN A O   1 
ATOM   1443 C  CB  . ASN A 1 177 ? -23.197 4.439   0.165   1.00 15.46 ? 178 ASN A CB  1 
ATOM   1444 C  CG  . ASN A 1 177 ? -23.590 5.809   -0.343  1.00 16.16 ? 178 ASN A CG  1 
ATOM   1445 O  OD1 . ASN A 1 177 ? -24.277 6.573   0.322   1.00 19.62 ? 178 ASN A OD1 1 
ATOM   1446 N  ND2 . ASN A 1 177 ? -22.965 6.179   -1.421  1.00 16.06 ? 178 ASN A ND2 1 
ATOM   1447 N  N   . PHE A 1 178 ? -20.776 3.050   2.637   1.00 11.70 ? 179 PHE A N   1 
ATOM   1448 C  CA  . PHE A 1 178 ? -20.640 1.898   3.474   1.00 12.20 ? 179 PHE A CA  1 
ATOM   1449 C  C   . PHE A 1 178 ? -21.160 2.161   4.899   1.00 11.32 ? 179 PHE A C   1 
ATOM   1450 O  O   . PHE A 1 178 ? -20.708 3.154   5.504   1.00 13.81 ? 179 PHE A O   1 
ATOM   1451 C  CB  . PHE A 1 178 ? -19.170 1.455   3.586   1.00 12.47 ? 179 PHE A CB  1 
ATOM   1452 C  CG  . PHE A 1 178 ? -19.087 0.206   4.425   1.00 11.91 ? 179 PHE A CG  1 
ATOM   1453 C  CD1 . PHE A 1 178 ? -19.477 -1.035  3.913   1.00 13.20 ? 179 PHE A CD1 1 
ATOM   1454 C  CD2 . PHE A 1 178 ? -18.699 0.280   5.754   1.00 11.38 ? 179 PHE A CD2 1 
ATOM   1455 C  CE1 . PHE A 1 178 ? -19.460 -2.144  4.738   1.00 12.87 ? 179 PHE A CE1 1 
ATOM   1456 C  CE2 . PHE A 1 178 ? -18.734 -0.818  6.607   1.00 11.84 ? 179 PHE A CE2 1 
ATOM   1457 C  CZ  . PHE A 1 178 ? -19.119 -2.060  6.082   1.00 11.84 ? 179 PHE A CZ  1 
ATOM   1458 N  N   . ASP A 1 179 ? -22.119 1.342   5.364   1.00 11.44 ? 180 ASP A N   1 
ATOM   1459 C  CA  . ASP A 1 179 ? -22.711 1.567   6.669   1.00 12.13 ? 180 ASP A CA  1 
ATOM   1460 C  C   . ASP A 1 179 ? -21.993 0.764   7.741   1.00 12.28 ? 180 ASP A C   1 
ATOM   1461 O  O   . ASP A 1 179 ? -22.130 -0.454  7.812   1.00 12.63 ? 180 ASP A O   1 
ATOM   1462 C  CB  . ASP A 1 179 ? -24.180 1.157   6.618   1.00 13.53 ? 180 ASP A CB  1 
ATOM   1463 C  CG  . ASP A 1 179 ? -24.953 1.578   7.854   1.00 13.86 ? 180 ASP A CG  1 
ATOM   1464 O  OD1 . ASP A 1 179 ? -24.323 1.913   8.862   1.00 14.20 ? 180 ASP A OD1 1 
ATOM   1465 O  OD2 . ASP A 1 179 ? -26.211 1.620   7.768   1.00 21.83 ? 180 ASP A OD2 1 
ATOM   1466 N  N   . PRO A 1 180 ? -21.201 1.388   8.628   1.00 12.36 ? 181 PRO A N   1 
ATOM   1467 C  CA  . PRO A 1 180 ? -20.482 0.576   9.621   1.00 11.99 ? 181 PRO A CA  1 
ATOM   1468 C  C   . PRO A 1 180 ? -21.374 -0.011  10.679  1.00 11.80 ? 181 PRO A C   1 
ATOM   1469 O  O   . PRO A 1 180 ? -20.905 -0.868  11.423  1.00 12.94 ? 181 PRO A O   1 
ATOM   1470 C  CB  . PRO A 1 180 ? -19.512 1.597   10.214  1.00 14.03 ? 181 PRO A CB  1 
ATOM   1471 C  CG  . PRO A 1 180 ? -20.202 2.959   10.019  1.00 12.87 ? 181 PRO A CG  1 
ATOM   1472 C  CD  . PRO A 1 180 ? -20.888 2.834   8.679   1.00 12.29 ? 181 PRO A CD  1 
ATOM   1473 N  N   . ARG A 1 181 ? -22.661 0.361   10.702  1.00 11.16 ? 182 ARG A N   1 
ATOM   1474 C  CA  . ARG A 1 181 ? -23.597 -0.322  11.596  1.00 11.95 ? 182 ARG A CA  1 
ATOM   1475 C  C   . ARG A 1 181 ? -23.695 -1.806  11.261  1.00 12.36 ? 182 ARG A C   1 
ATOM   1476 O  O   . ARG A 1 181 ? -24.025 -2.611  12.121  1.00 13.81 ? 182 ARG A O   1 
ATOM   1477 C  CB  . ARG A 1 181 ? -24.987 0.338   11.546  1.00 13.07 ? 182 ARG A CB  1 
ATOM   1478 C  CG  . ARG A 1 181 ? -24.926 1.763   12.112  1.00 14.58 ? 182 ARG A CG  1 
ATOM   1479 C  CD  . ARG A 1 181 ? -26.274 2.420   12.067  1.00 16.75 ? 182 ARG A CD  1 
ATOM   1480 N  NE  . ARG A 1 181 ? -26.654 2.582   10.676  1.00 15.19 ? 182 ARG A NE  1 
ATOM   1481 C  CZ  . ARG A 1 181 ? -27.714 3.292   10.325  1.00 15.70 ? 182 ARG A CZ  1 
ATOM   1482 N  NH1 . ARG A 1 181 ? -28.465 3.844   11.291  1.00 20.52 ? 182 ARG A NH1 1 
ATOM   1483 N  NH2 . ARG A 1 181 ? -27.999 3.441   9.038   1.00 19.39 ? 182 ARG A NH2 1 
ATOM   1484 N  N   . GLY A 1 182 ? -23.398 -2.176  10.012  1.00 13.22 ? 183 GLY A N   1 
ATOM   1485 C  CA  . GLY A 1 182 ? -23.520 -3.582  9.647   1.00 13.63 ? 183 GLY A CA  1 
ATOM   1486 C  C   . GLY A 1 182 ? -22.344 -4.425  10.120  1.00 13.29 ? 183 GLY A C   1 
ATOM   1487 O  O   . GLY A 1 182 ? -22.320 -5.630  9.830   1.00 14.89 ? 183 GLY A O   1 
ATOM   1488 N  N   . LEU A 1 183 ? -21.389 -3.830  10.869  1.00 12.14 ? 184 LEU A N   1 
ATOM   1489 C  CA  . LEU A 1 183 ? -20.258 -4.597  11.407  1.00 12.43 ? 184 LEU A CA  1 
ATOM   1490 C  C   . LEU A 1 183 ? -20.385 -4.815  12.914  1.00 12.05 ? 184 LEU A C   1 
ATOM   1491 O  O   . LEU A 1 183 ? -19.492 -5.407  13.487  1.00 13.81 ? 184 LEU A O   1 
ATOM   1492 C  CB  . LEU A 1 183 ? -18.972 -3.824  11.179  1.00 12.20 ? 184 LEU A CB  1 
ATOM   1493 C  CG  . LEU A 1 183 ? -18.655 -3.606  9.709   1.00 13.08 ? 184 LEU A CG  1 
ATOM   1494 C  CD1 . LEU A 1 183 ? -17.392 -2.786  9.572   1.00 15.10 ? 184 LEU A CD1 1 
ATOM   1495 C  CD2 . LEU A 1 183 ? -18.526 -4.908  8.948   1.00 16.81 ? 184 LEU A CD2 1 
ATOM   1496 N  N   . LEU A 1 184 ? -21.481 -4.389  13.550  1.00 11.28 ? 185 LEU A N   1 
ATOM   1497 C  CA  . LEU A 1 184 ? -21.639 -4.483  14.997  1.00 11.57 ? 185 LEU A CA  1 
ATOM   1498 C  C   . LEU A 1 184 ? -22.395 -5.751  15.381  1.00 12.86 ? 185 LEU A C   1 
ATOM   1499 O  O   . LEU A 1 184 ? -23.332 -6.182  14.709  1.00 18.36 ? 185 LEU A O   1 
ATOM   1500 C  CB  . LEU A 1 184 ? -22.434 -3.254  15.513  1.00 12.76 ? 185 LEU A CB  1 
ATOM   1501 C  CG  . LEU A 1 184 ? -21.872 -1.900  15.096  1.00 15.13 ? 185 LEU A CG  1 
ATOM   1502 C  CD1 . LEU A 1 184 ? -22.719 -0.729  15.641  1.00 15.62 ? 185 LEU A CD1 1 
ATOM   1503 C  CD2 . LEU A 1 184 ? -20.431 -1.817  15.539  1.00 16.01 ? 185 LEU A CD2 1 
ATOM   1504 N  N   . PRO A 1 185 ? -22.063 -6.344  16.550  1.00 11.73 ? 186 PRO A N   1 
ATOM   1505 C  CA  . PRO A 1 185 ? -22.827 -7.469  17.093  1.00 12.45 ? 186 PRO A CA  1 
ATOM   1506 C  C   . PRO A 1 185 ? -24.114 -6.929  17.724  1.00 11.33 ? 186 PRO A C   1 
ATOM   1507 O  O   . PRO A 1 185 ? -24.318 -5.716  17.786  1.00 13.36 ? 186 PRO A O   1 
ATOM   1508 C  CB  . PRO A 1 185 ? -21.867 -8.037  18.157  1.00 13.02 ? 186 PRO A CB  1 
ATOM   1509 C  CG  . PRO A 1 185 ? -21.137 -6.802  18.668  1.00 11.56 ? 186 PRO A CG  1 
ATOM   1510 C  CD  . PRO A 1 185 ? -20.942 -5.943  17.417  1.00 11.05 ? 186 PRO A CD  1 
ATOM   1511 N  N   . GLU A 1 186 ? -24.961 -7.828  18.228  1.00 14.83 ? 187 GLU A N   1 
ATOM   1512 C  CA  . GLU A 1 186 ? -26.215 -7.379  18.819  1.00 15.29 ? 187 GLU A CA  1 
ATOM   1513 C  C   . GLU A 1 186 ? -25.950 -6.552  20.065  1.00 13.26 ? 187 GLU A C   1 
ATOM   1514 O  O   . GLU A 1 186 ? -26.553 -5.526  20.260  1.00 16.44 ? 187 GLU A O   1 
ATOM   1515 C  CB  . GLU A 1 186 ? -27.016 -8.571  19.261  1.00 18.12 ? 187 GLU A CB  1 
ATOM   1516 C  CG  . GLU A 1 186 ? -27.755 -9.229  18.155  1.00 22.37 ? 187 GLU A CG  1 
ATOM   1517 C  CD  . GLU A 1 186 ? -28.472 -10.510 18.585  1.00 20.24 ? 187 GLU A CD  1 
ATOM   1518 O  OE1 . GLU A 1 186 ? -28.530 -10.814 19.787  1.00 23.43 ? 187 GLU A OE1 1 
ATOM   1519 O  OE2 . GLU A 1 186 ? -28.870 -11.262 17.706  1.00 26.43 ? 187 GLU A OE2 1 
ATOM   1520 N  N   . SER A 1 187 ? -25.084 -7.049  20.970  1.00 13.99 ? 188 SER A N   1 
ATOM   1521 C  CA  . SER A 1 187 ? -24.882 -6.451  22.266  1.00 13.65 ? 188 SER A CA  1 
ATOM   1522 C  C   . SER A 1 187 ? -23.769 -5.404  22.220  1.00 13.89 ? 188 SER A C   1 
ATOM   1523 O  O   . SER A 1 187 ? -22.758 -5.613  21.526  1.00 15.46 ? 188 SER A O   1 
ATOM   1524 C  CB  . SER A 1 187 ? -24.505 -7.540  23.251  1.00 15.68 ? 188 SER A CB  1 
ATOM   1525 O  OG  . SER A 1 187 ? -24.270 -7.008  24.550  1.00 16.36 ? 188 SER A OG  1 
ATOM   1526 N  N   . LEU A 1 188 ? -23.940 -4.352  23.023  1.00 14.12 ? 189 LEU A N   1 
ATOM   1527 C  CA  . LEU A 1 188 ? -22.870 -3.372  23.188  1.00 13.70 ? 189 LEU A CA  1 
ATOM   1528 C  C   . LEU A 1 188 ? -22.279 -3.510  24.595  1.00 12.80 ? 189 LEU A C   1 
ATOM   1529 O  O   . LEU A 1 188 ? -21.574 -2.619  25.055  1.00 14.86 ? 189 LEU A O   1 
ATOM   1530 C  CB  . LEU A 1 188 ? -23.417 -1.948  22.973  1.00 14.85 ? 189 LEU A CB  1 
ATOM   1531 C  CG  . LEU A 1 188 ? -23.798 -1.579  21.561  1.00 14.95 ? 189 LEU A CG  1 
ATOM   1532 C  CD1 . LEU A 1 188 ? -24.328 -0.147  21.540  1.00 19.05 ? 189 LEU A CD1 1 
ATOM   1533 C  CD2 . LEU A 1 188 ? -22.640 -1.786  20.561  1.00 18.74 ? 189 LEU A CD2 1 
ATOM   1534 N  N   . ASP A 1 189 ? -22.408 -4.692  25.256  1.00 15.79 ? 190 ASP A N   1 
ATOM   1535 C  CA  . ASP A 1 189 ? -21.664 -4.921  26.471  1.00 14.74 ? 190 ASP A CA  1 
ATOM   1536 C  C   . ASP A 1 189 ? -20.161 -4.927  26.166  1.00 13.70 ? 190 ASP A C   1 
ATOM   1537 O  O   . ASP A 1 189 ? -19.733 -5.410  25.096  1.00 12.99 ? 190 ASP A O   1 
ATOM   1538 C  CB  . ASP A 1 189 ? -22.013 -6.290  27.058  1.00 16.37 ? 190 ASP A CB  1 
ATOM   1539 C  CG  . ASP A 1 189 ? -23.413 -6.397  27.651  1.00 21.75 ? 190 ASP A CG  1 
ATOM   1540 O  OD1 . ASP A 1 189 ? -24.087 -5.354  27.804  1.00 27.41 ? 190 ASP A OD1 1 
ATOM   1541 O  OD2 . ASP A 1 189 ? -23.780 -7.507  27.947  1.00 26.78 ? 190 ASP A OD2 1 
ATOM   1542 N  N   . TYR A 1 190 ? -19.330 -4.413  27.074  1.00 13.00 ? 191 TYR A N   1 
ATOM   1543 C  CA  . TYR A 1 190 ? -17.957 -4.125  26.721  1.00 12.49 ? 191 TYR A CA  1 
ATOM   1544 C  C   . TYR A 1 190 ? -17.079 -4.180  27.956  1.00 11.62 ? 191 TYR A C   1 
ATOM   1545 O  O   . TYR A 1 190 ? -17.505 -4.062  29.109  1.00 12.47 ? 191 TYR A O   1 
ATOM   1546 C  CB  . TYR A 1 190 ? -17.837 -2.732  26.069  1.00 11.67 ? 191 TYR A CB  1 
ATOM   1547 C  CG  . TYR A 1 190 ? -18.207 -1.580  26.981  1.00 11.95 ? 191 TYR A CG  1 
ATOM   1548 C  CD1 . TYR A 1 190 ? -17.275 -0.966  27.823  1.00 12.91 ? 191 TYR A CD1 1 
ATOM   1549 C  CD2 . TYR A 1 190 ? -19.478 -1.051  26.938  1.00 13.25 ? 191 TYR A CD2 1 
ATOM   1550 C  CE1 . TYR A 1 190 ? -17.637 0.104   28.654  1.00 13.35 ? 191 TYR A CE1 1 
ATOM   1551 C  CE2 . TYR A 1 190 ? -19.858 0.017   27.741  1.00 14.58 ? 191 TYR A CE2 1 
ATOM   1552 C  CZ  . TYR A 1 190 ? -18.935 0.594   28.598  1.00 15.16 ? 191 TYR A CZ  1 
ATOM   1553 O  OH  . TYR A 1 190 ? -19.277 1.587   29.475  1.00 15.78 ? 191 TYR A OH  1 
ATOM   1554 N  N   . TRP A 1 191 ? -15.789 -4.355  27.656  1.00 12.40 ? 192 TRP A N   1 
ATOM   1555 C  CA  . TRP A 1 191 ? -14.694 -4.116  28.565  1.00 11.07 ? 192 TRP A CA  1 
ATOM   1556 C  C   . TRP A 1 191 ? -14.014 -2.816  28.209  1.00 10.63 ? 192 TRP A C   1 
ATOM   1557 O  O   . TRP A 1 191 ? -13.976 -2.485  27.015  1.00 11.41 ? 192 TRP A O   1 
ATOM   1558 C  CB  . TRP A 1 191 ? -13.668 -5.210  28.536  1.00 12.19 ? 192 TRP A CB  1 
ATOM   1559 C  CG  . TRP A 1 191 ? -14.227 -6.542  28.948  1.00 11.79 ? 192 TRP A CG  1 
ATOM   1560 C  CD1 . TRP A 1 191 ? -14.461 -6.963  30.236  1.00 13.09 ? 192 TRP A CD1 1 
ATOM   1561 C  CD2 . TRP A 1 191 ? -14.510 -7.664  28.088  1.00 11.87 ? 192 TRP A CD2 1 
ATOM   1562 N  NE1 . TRP A 1 191 ? -14.929 -8.250  30.179  1.00 13.96 ? 192 TRP A NE1 1 
ATOM   1563 C  CE2 . TRP A 1 191 ? -14.932 -8.733  28.903  1.00 12.35 ? 192 TRP A CE2 1 
ATOM   1564 C  CE3 . TRP A 1 191 ? -14.398 -7.871  26.704  1.00 13.20 ? 192 TRP A CE3 1 
ATOM   1565 C  CZ2 . TRP A 1 191 ? -15.259 -10.000 28.399  1.00 13.70 ? 192 TRP A CZ2 1 
ATOM   1566 C  CZ3 . TRP A 1 191 ? -14.695 -9.123  26.204  1.00 15.27 ? 192 TRP A CZ3 1 
ATOM   1567 C  CH2 . TRP A 1 191 ? -15.155 -10.153 27.019  1.00 14.41 ? 192 TRP A CH2 1 
ATOM   1568 N  N   . THR A 1 192 ? -13.426 -2.095  29.158  1.00 10.82 ? 193 THR A N   1 
ATOM   1569 C  CA  . THR A 1 192 ? -12.696 -0.903  28.795  1.00 11.48 ? 193 THR A CA  1 
ATOM   1570 C  C   . THR A 1 192 ? -11.458 -0.751  29.659  1.00 10.20 ? 193 THR A C   1 
ATOM   1571 O  O   . THR A 1 192 ? -11.452 -1.124  30.840  1.00 11.78 ? 193 THR A O   1 
ATOM   1572 C  CB  . THR A 1 192 ? -13.607 0.352   28.905  1.00 10.98 ? 193 THR A CB  1 
ATOM   1573 O  OG1 . THR A 1 192 ? -12.904 1.520   28.489  1.00 13.01 ? 193 THR A OG1 1 
ATOM   1574 C  CG2 . THR A 1 192 ? -14.158 0.567   30.316  1.00 12.17 ? 193 THR A CG2 1 
ATOM   1575 N  N   . TYR A 1 193 ? -10.419 -0.172  29.071  1.00 11.03 ? 194 TYR A N   1 
ATOM   1576 C  CA  . TYR A 1 193 ? -9.191  0.059   29.834  1.00 10.82 ? 194 TYR A CA  1 
ATOM   1577 C  C   . TYR A 1 193 ? -8.404  1.116   29.073  1.00 10.56 ? 194 TYR A C   1 
ATOM   1578 O  O   . TYR A 1 193 ? -8.601  1.322   27.853  1.00 11.02 ? 194 TYR A O   1 
ATOM   1579 C  CB  . TYR A 1 193 ? -8.380  -1.242  30.017  1.00 11.70 ? 194 TYR A CB  1 
ATOM   1580 C  CG  . TYR A 1 193 ? -7.657  -1.676  28.772  1.00 11.33 ? 194 TYR A CG  1 
ATOM   1581 C  CD1 . TYR A 1 193 ? -8.328  -2.376  27.773  1.00 10.72 ? 194 TYR A CD1 1 
ATOM   1582 C  CD2 . TYR A 1 193 ? -6.314  -1.376  28.568  1.00 11.66 ? 194 TYR A CD2 1 
ATOM   1583 C  CE1 . TYR A 1 193 ? -7.700  -2.712  26.583  1.00 10.42 ? 194 TYR A CE1 1 
ATOM   1584 C  CE2 . TYR A 1 193 ? -5.669  -1.677  27.381  1.00 11.53 ? 194 TYR A CE2 1 
ATOM   1585 C  CZ  . TYR A 1 193 ? -6.373  -2.347  26.371  1.00 9.38  ? 194 TYR A CZ  1 
ATOM   1586 O  OH  . TYR A 1 193 ? -5.715  -2.662  25.227  1.00 10.20 ? 194 TYR A OH  1 
ATOM   1587 N  N   . PRO A 1 194 ? -7.455  1.804   29.734  1.00 10.40 ? 195 PRO A N   1 
ATOM   1588 C  CA  . PRO A 1 194 ? -6.625  2.808   29.058  1.00 10.83 ? 195 PRO A CA  1 
ATOM   1589 C  C   . PRO A 1 194 ? -5.395  2.159   28.448  1.00 11.33 ? 195 PRO A C   1 
ATOM   1590 O  O   . PRO A 1 194 ? -4.707  1.345   29.067  1.00 11.69 ? 195 PRO A O   1 
ATOM   1591 C  CB  . PRO A 1 194 ? -6.153  3.689   30.235  1.00 13.35 ? 195 PRO A CB  1 
ATOM   1592 C  CG  . PRO A 1 194 ? -6.118  2.764   31.451  1.00 15.37 ? 195 PRO A CG  1 
ATOM   1593 C  CD  . PRO A 1 194 ? -7.245  1.775   31.192  1.00 13.72 ? 195 PRO A CD  1 
ATOM   1594 N  N   . GLY A 1 195 ? -5.153  2.500   27.183  1.00 10.37 ? 196 GLY A N   1 
ATOM   1595 C  CA  . GLY A 1 195 ? -4.087  1.871   26.434  1.00 10.89 ? 196 GLY A CA  1 
ATOM   1596 C  C   . GLY A 1 195 ? -3.527  2.741   25.336  1.00 10.50 ? 196 GLY A C   1 
ATOM   1597 O  O   . GLY A 1 195 ? -3.413  3.944   25.446  1.00 10.40 ? 196 GLY A O   1 
ATOM   1598 N  N   . SER A 1 196 ? -3.100  2.050   24.294  1.00 10.16 ? 197 SER A N   1 
ATOM   1599 C  CA  . SER A 1 196 ? -2.272  2.655   23.253  1.00 10.64 ? 197 SER A CA  1 
ATOM   1600 C  C   . SER A 1 196 ? -2.725  2.259   21.866  1.00 9.90  ? 197 SER A C   1 
ATOM   1601 O  O   . SER A 1 196 ? -3.493  1.318   21.683  1.00 9.53  ? 197 SER A O   1 
ATOM   1602 C  CB  . SER A 1 196 ? -0.799  2.284   23.426  1.00 10.51 ? 197 SER A CB  1 
ATOM   1603 O  OG  . SER A 1 196 ? -0.565  0.911   22.985  1.00 11.12 ? 197 SER A OG  1 
ATOM   1604 N  N   . LEU A 1 197 ? -2.144  2.953   20.891  1.00 9.79  ? 198 LEU A N   1 
ATOM   1605 C  CA  . LEU A 1 197 ? -2.127  2.429   19.512  1.00 9.47  ? 198 LEU A CA  1 
ATOM   1606 C  C   . LEU A 1 197 ? -1.428  1.067   19.534  1.00 9.49  ? 198 LEU A C   1 
ATOM   1607 O  O   . LEU A 1 197 ? -0.433  0.856   20.235  1.00 10.73 ? 198 LEU A O   1 
ATOM   1608 C  CB  . LEU A 1 197 ? -1.386  3.384   18.574  1.00 11.37 ? 198 LEU A CB  1 
ATOM   1609 C  CG  . LEU A 1 197 ? -1.895  4.812   18.610  1.00 10.65 ? 198 LEU A CG  1 
ATOM   1610 C  CD1 . LEU A 1 197 ? -1.013  5.647   17.683  1.00 13.55 ? 198 LEU A CD1 1 
ATOM   1611 C  CD2 . LEU A 1 197 ? -3.347  4.887   18.215  1.00 11.60 ? 198 LEU A CD2 1 
ATOM   1612 N  N   . THR A 1 198 ? -1.896  0.120   18.724  1.00 9.92  ? 199 THR A N   1 
ATOM   1613 C  CA  . THR A 1 198 ? -1.280  -1.207  18.692  1.00 9.88  ? 199 THR A CA  1 
ATOM   1614 C  C   . THR A 1 198 ? -0.252  -1.363  17.576  1.00 10.37 ? 199 THR A C   1 
ATOM   1615 O  O   . THR A 1 198 ? 0.345   -2.431  17.430  1.00 11.74 ? 199 THR A O   1 
ATOM   1616 C  CB  . THR A 1 198 ? -2.336  -2.322  18.519  1.00 9.24  ? 199 THR A CB  1 
ATOM   1617 O  OG1 . THR A 1 198 ? -2.895  -2.173  17.219  1.00 9.67  ? 199 THR A OG1 1 
ATOM   1618 C  CG2 . THR A 1 198 ? -3.397  -2.280  19.593  1.00 10.53 ? 199 THR A CG2 1 
ATOM   1619 N  N   . THR A 1 199 ? 0.011   -0.297  16.828  1.00 11.09 ? 200 THR A N   1 
ATOM   1620 C  CA  . THR A 1 199 ? 1.080   -0.263  15.878  1.00 11.96 ? 200 THR A CA  1 
ATOM   1621 C  C   . THR A 1 199 ? 1.907   0.972   16.151  1.00 11.71 ? 200 THR A C   1 
ATOM   1622 O  O   . THR A 1 199 ? 1.411   1.913   16.761  1.00 11.59 ? 200 THR A O   1 
ATOM   1623 C  CB  . THR A 1 199 ? 0.660   -0.247  14.400  1.00 12.21 ? 200 THR A CB  1 
ATOM   1624 O  OG1 . THR A 1 199 ? 0.280   1.080   14.074  1.00 14.70 ? 200 THR A OG1 1 
ATOM   1625 C  CG2 . THR A 1 199 ? -0.480  -1.164  14.072  1.00 14.00 ? 200 THR A CG2 1 
ATOM   1626 N  N   . PRO A 1 200 ? 3.151   1.053   15.648  1.00 12.22 ? 201 PRO A N   1 
ATOM   1627 C  CA  . PRO A 1 200 ? 3.878   2.311   15.711  1.00 12.51 ? 201 PRO A CA  1 
ATOM   1628 C  C   . PRO A 1 200 ? 2.979   3.425   15.179  1.00 12.15 ? 201 PRO A C   1 
ATOM   1629 O  O   . PRO A 1 200 ? 2.224   3.220   14.196  1.00 13.22 ? 201 PRO A O   1 
ATOM   1630 C  CB  . PRO A 1 200 ? 5.072   2.022   14.786  1.00 13.57 ? 201 PRO A CB  1 
ATOM   1631 C  CG  . PRO A 1 200 ? 5.348   0.561   15.021  1.00 14.31 ? 201 PRO A CG  1 
ATOM   1632 C  CD  . PRO A 1 200 ? 3.943   -0.034  15.054  1.00 13.20 ? 201 PRO A CD  1 
ATOM   1633 N  N   . PRO A 1 201 ? 2.957   4.617   15.788  1.00 12.36 ? 202 PRO A N   1 
ATOM   1634 C  CA  . PRO A 1 201 ? 3.920   5.032   16.820  1.00 11.64 ? 202 PRO A CA  1 
ATOM   1635 C  C   . PRO A 1 201 ? 3.617   4.628   18.268  1.00 11.94 ? 202 PRO A C   1 
ATOM   1636 O  O   . PRO A 1 201 ? 4.366   5.014   19.146  1.00 12.75 ? 202 PRO A O   1 
ATOM   1637 C  CB  . PRO A 1 201 ? 3.910   6.553   16.666  1.00 13.53 ? 202 PRO A CB  1 
ATOM   1638 C  CG  . PRO A 1 201 ? 2.484   6.855   16.257  1.00 15.41 ? 202 PRO A CG  1 
ATOM   1639 C  CD  . PRO A 1 201 ? 2.136   5.723   15.321  1.00 13.85 ? 202 PRO A CD  1 
ATOM   1640 N  N   . LEU A 1 202 ? 2.587   3.790   18.504  1.00 11.76 ? 203 LEU A N   1 
ATOM   1641 C  CA  . LEU A 1 202 ? 2.332   3.199   19.820  1.00 10.82 ? 203 LEU A CA  1 
ATOM   1642 C  C   . LEU A 1 202 ? 1.949   4.210   20.890  1.00 10.02 ? 203 LEU A C   1 
ATOM   1643 O  O   . LEU A 1 202 ? 1.954   3.897   22.092  1.00 11.97 ? 203 LEU A O   1 
ATOM   1644 C  CB  . LEU A 1 202 ? 3.503   2.310   20.263  1.00 11.39 ? 203 LEU A CB  1 
ATOM   1645 C  CG  . LEU A 1 202 ? 3.808   1.147   19.316  1.00 11.26 ? 203 LEU A CG  1 
ATOM   1646 C  CD1 . LEU A 1 202 ? 5.165   0.558   19.723  1.00 13.11 ? 203 LEU A CD1 1 
ATOM   1647 C  CD2 . LEU A 1 202 ? 2.705   0.107   19.363  1.00 12.01 ? 203 LEU A CD2 1 
ATOM   1648 N  N   . ASN A 1 203 ? 1.503   5.390   20.453  1.00 11.85 ? 204 ASN A N   1 
ATOM   1649 C  CA  . ASN A 1 203 ? 1.140   6.425   21.396  1.00 11.84 ? 204 ASN A CA  1 
ATOM   1650 C  C   . ASN A 1 203 ? 0.133   5.940   22.420  1.00 10.84 ? 204 ASN A C   1 
ATOM   1651 O  O   . ASN A 1 203 ? -0.857  5.239   22.094  1.00 11.05 ? 204 ASN A O   1 
ATOM   1652 C  CB  . ASN A 1 203 ? 0.460   7.604   20.708  1.00 14.50 ? 204 ASN A CB  1 
ATOM   1653 C  CG  . ASN A 1 203 ? 1.344   8.292   19.690  1.00 15.49 ? 204 ASN A CG  1 
ATOM   1654 O  OD1 . ASN A 1 203 ? 2.461   7.869   19.366  1.00 18.04 ? 204 ASN A OD1 1 
ATOM   1655 N  ND2 . ASN A 1 203 ? 0.845   9.372   19.120  1.00 17.31 ? 204 ASN A ND2 1 
ATOM   1656 N  N   . GLU A 1 204 ? 0.299   6.365   23.671  1.00 11.67 ? 205 GLU A N   1 
ATOM   1657 C  CA  . GLU A 1 204 ? -0.610  6.004   24.766  1.00 11.72 ? 205 GLU A CA  1 
ATOM   1658 C  C   . GLU A 1 204 ? -1.776  6.992   24.813  1.00 12.10 ? 205 GLU A C   1 
ATOM   1659 O  O   . GLU A 1 204 ? -1.938  7.722   25.795  1.00 15.24 ? 205 GLU A O   1 
ATOM   1660 C  CB  . GLU A 1 204 ? 0.166   5.857   26.081  1.00 12.57 ? 205 GLU A CB  1 
ATOM   1661 C  CG  . GLU A 1 204 ? 1.115   4.659   25.932  1.00 13.01 ? 205 GLU A CG  1 
ATOM   1662 C  CD  . GLU A 1 204 ? 1.997   4.407   27.134  1.00 12.98 ? 205 GLU A CD  1 
ATOM   1663 O  OE1 . GLU A 1 204 ? 2.223   5.348   27.977  1.00 16.65 ? 205 GLU A OE1 1 
ATOM   1664 O  OE2 . GLU A 1 204 ? 2.411   3.219   27.275  1.00 13.12 ? 205 GLU A OE2 1 
ATOM   1665 N  N   . CYS A 1 205 ? -2.639  6.931   23.800  1.00 10.17 ? 206 CYS A N   1 
ATOM   1666 C  CA  . CYS A 1 205 ? -3.666  7.922   23.609  1.00 10.13 ? 206 CYS A CA  1 
ATOM   1667 C  C   . CYS A 1 205 ? -5.067  7.327   23.496  1.00 10.61 ? 206 CYS A C   1 
ATOM   1668 O  O   . CYS A 1 205 ? -5.959  8.030   23.048  1.00 11.69 ? 206 CYS A O   1 
ATOM   1669 C  CB  . CYS A 1 205 ? -3.363  8.727   22.330  1.00 12.20 ? 206 CYS A CB  1 
ATOM   1670 S  SG  . CYS A 1 205 ? -3.319  7.718   20.816  1.00 12.38 ? 206 CYS A SG  1 
ATOM   1671 N  N   . VAL A 1 206 ? -5.221  6.022   23.795  1.00 10.34 ? 207 VAL A N   1 
ATOM   1672 C  CA  . VAL A 1 206 ? -6.454  5.306   23.447  1.00 10.09 ? 207 VAL A CA  1 
ATOM   1673 C  C   . VAL A 1 206 ? -7.211  4.915   24.709  1.00 10.15 ? 207 VAL A C   1 
ATOM   1674 O  O   . VAL A 1 206 ? -6.681  4.243   25.568  1.00 12.06 ? 207 VAL A O   1 
ATOM   1675 C  CB  . VAL A 1 206 ? -6.156  4.059   22.625  1.00 9.78  ? 207 VAL A CB  1 
ATOM   1676 C  CG1 . VAL A 1 206 ? -7.473  3.384   22.276  1.00 10.34 ? 207 VAL A CG1 1 
ATOM   1677 C  CG2 . VAL A 1 206 ? -5.443  4.410   21.350  1.00 10.78 ? 207 VAL A CG2 1 
ATOM   1678 N  N   . THR A 1 207 ? -8.499  5.231   24.741  1.00 9.70  ? 208 THR A N   1 
ATOM   1679 C  CA  . THR A 1 207 ? -9.418  4.517   25.617  1.00 10.11 ? 208 THR A CA  1 
ATOM   1680 C  C   . THR A 1 207 ? -9.960  3.360   24.794  1.00 9.93  ? 208 THR A C   1 
ATOM   1681 O  O   . THR A 1 207 ? -10.644 3.561   23.786  1.00 10.37 ? 208 THR A O   1 
ATOM   1682 C  CB  . THR A 1 207 ? -10.599 5.391   26.097  1.00 11.95 ? 208 THR A CB  1 
ATOM   1683 O  OG1 . THR A 1 207 ? -10.090 6.517   26.839  1.00 12.81 ? 208 THR A OG1 1 
ATOM   1684 C  CG2 . THR A 1 207 ? -11.595 4.627   26.947  1.00 13.08 ? 208 THR A CG2 1 
ATOM   1685 N  N   . TRP A 1 208 ? -9.632  2.142   25.220  1.00 9.66  ? 209 TRP A N   1 
ATOM   1686 C  CA  . TRP A 1 208 ? -10.118 0.960   24.525  1.00 9.84  ? 209 TRP A CA  1 
ATOM   1687 C  C   . TRP A 1 208 ? -11.483 0.527   25.024  1.00 9.58  ? 209 TRP A C   1 
ATOM   1688 O  O   . TRP A 1 208 ? -11.704 0.500   26.247  1.00 10.19 ? 209 TRP A O   1 
ATOM   1689 C  CB  . TRP A 1 208 ? -9.129  -0.204  24.733  1.00 10.39 ? 209 TRP A CB  1 
ATOM   1690 C  CG  . TRP A 1 208 ? -7.989  -0.108  23.775  1.00 8.80  ? 209 TRP A CG  1 
ATOM   1691 C  CD1 . TRP A 1 208 ? -6.763  0.467   23.993  1.00 9.47  ? 209 TRP A CD1 1 
ATOM   1692 C  CD2 . TRP A 1 208 ? -8.036  -0.470  22.389  1.00 8.51  ? 209 TRP A CD2 1 
ATOM   1693 N  NE1 . TRP A 1 208 ? -6.058  0.481   22.816  1.00 9.91  ? 209 TRP A NE1 1 
ATOM   1694 C  CE2 . TRP A 1 208 ? -6.811  -0.105  21.792  1.00 9.30  ? 209 TRP A CE2 1 
ATOM   1695 C  CE3 . TRP A 1 208 ? -9.017  -1.077  21.593  1.00 9.28  ? 209 TRP A CE3 1 
ATOM   1696 C  CZ2 . TRP A 1 208 ? -6.524  -0.325  20.440  1.00 9.94  ? 209 TRP A CZ2 1 
ATOM   1697 C  CZ3 . TRP A 1 208 ? -8.740  -1.328  20.249  1.00 10.16 ? 209 TRP A CZ3 1 
ATOM   1698 C  CH2 . TRP A 1 208 ? -7.528  -0.939  19.685  1.00 10.10 ? 209 TRP A CH2 1 
ATOM   1699 N  N   . ILE A 1 209 ? -12.378 0.226   24.085  1.00 9.35  ? 210 ILE A N   1 
ATOM   1700 C  CA  . ILE A 1 209 ? -13.711 -0.277  24.442  1.00 9.71  ? 210 ILE A CA  1 
ATOM   1701 C  C   . ILE A 1 209 ? -13.840 -1.518  23.587  1.00 9.07  ? 210 ILE A C   1 
ATOM   1702 O  O   . ILE A 1 209 ? -13.896 -1.435  22.358  1.00 9.55  ? 210 ILE A O   1 
ATOM   1703 C  CB  . ILE A 1 209 ? -14.791 0.755   24.082  1.00 10.12 ? 210 ILE A CB  1 
ATOM   1704 C  CG1 . ILE A 1 209 ? -14.514 2.041   24.866  1.00 11.91 ? 210 ILE A CG1 1 
ATOM   1705 C  CG2 . ILE A 1 209 ? -16.187 0.177   24.356  1.00 12.05 ? 210 ILE A CG2 1 
ATOM   1706 C  CD1 . ILE A 1 209 ? -15.353 3.196   24.458  1.00 13.15 ? 210 ILE A CD1 1 
ATOM   1707 N  N   . VAL A 1 210 ? -13.784 -2.685  24.205  1.00 9.98  ? 211 VAL A N   1 
ATOM   1708 C  CA  . VAL A 1 210 ? -13.732 -3.955  23.467  1.00 9.59  ? 211 VAL A CA  1 
ATOM   1709 C  C   . VAL A 1 210 ? -15.053 -4.665  23.701  1.00 8.88  ? 211 VAL A C   1 
ATOM   1710 O  O   . VAL A 1 210 ? -15.403 -4.923  24.858  1.00 10.60 ? 211 VAL A O   1 
ATOM   1711 C  CB  . VAL A 1 210 ? -12.530 -4.807  23.894  1.00 10.41 ? 211 VAL A CB  1 
ATOM   1712 C  CG1 . VAL A 1 210 ? -12.569 -6.145  23.185  1.00 12.05 ? 211 VAL A CG1 1 
ATOM   1713 C  CG2 . VAL A 1 210 ? -11.209 -4.087  23.611  1.00 11.86 ? 211 VAL A CG2 1 
ATOM   1714 N  N   . LEU A 1 211 ? -15.843 -4.931  22.682  1.00 9.80  ? 212 LEU A N   1 
ATOM   1715 C  CA  . LEU A 1 211 ? -17.131 -5.558  22.859  1.00 10.31 ? 212 LEU A CA  1 
ATOM   1716 C  C   . LEU A 1 211 ? -16.962 -7.016  23.255  1.00 11.28 ? 212 LEU A C   1 
ATOM   1717 O  O   . LEU A 1 211 ? -16.147 -7.754  22.741  1.00 11.70 ? 212 LEU A O   1 
ATOM   1718 C  CB  . LEU A 1 211 ? -17.920 -5.440  21.553  1.00 11.36 ? 212 LEU A CB  1 
ATOM   1719 C  CG  . LEU A 1 211 ? -18.313 -4.002  21.157  1.00 11.04 ? 212 LEU A CG  1 
ATOM   1720 C  CD1 . LEU A 1 211 ? -19.344 -4.076  20.017  1.00 14.39 ? 212 LEU A CD1 1 
ATOM   1721 C  CD2 . LEU A 1 211 ? -18.873 -3.199  22.324  1.00 12.83 ? 212 LEU A CD2 1 
ATOM   1722 N  N   . LYS A 1 212 ? -17.851 -7.442  24.152  1.00 11.55 ? 213 LYS A N   1 
ATOM   1723 C  CA  . LYS A 1 212 ? -17.861 -8.831  24.610  1.00 12.64 ? 213 LYS A CA  1 
ATOM   1724 C  C   . LYS A 1 212 ? -18.267 -9.807  23.515  1.00 11.08 ? 213 LYS A C   1 
ATOM   1725 O  O   . LYS A 1 212 ? -17.750 -10.934 23.440  1.00 13.90 ? 213 LYS A O   1 
ATOM   1726 C  CB  . LYS A 1 212 ? -18.784 -8.932  25.838  1.00 18.69 ? 213 LYS A CB  1 
ATOM   1727 C  CG  . LYS A 1 212 ? -19.133 -10.328 26.328  1.00 26.74 ? 213 LYS A CG  1 
ATOM   1728 C  CD  . LYS A 1 212 ? -20.419 -10.302 27.201  1.00 37.29 ? 213 LYS A CD  1 
ATOM   1729 N  N   . GLU A 1 213 ? -19.264 -9.432  22.724  1.00 11.62 ? 214 GLU A N   1 
ATOM   1730 C  CA  . GLU A 1 213 ? -19.824 -10.346 21.718  1.00 10.64 ? 214 GLU A CA  1 
ATOM   1731 C  C   . GLU A 1 213 ? -19.059 -10.216 20.413  1.00 11.10 ? 214 GLU A C   1 
ATOM   1732 O  O   . GLU A 1 213 ? -18.981 -9.150  19.822  1.00 11.28 ? 214 GLU A O   1 
ATOM   1733 C  CB  . GLU A 1 213 ? -21.278 -9.963  21.420  1.00 13.24 ? 214 GLU A CB  1 
ATOM   1734 C  CG  . GLU A 1 213 ? -22.016 -10.939 20.522  1.00 17.71 ? 214 GLU A CG  1 
ATOM   1735 C  CD  . GLU A 1 213 ? -23.460 -10.492 20.198  1.00 22.69 ? 214 GLU A CD  1 
ATOM   1736 O  OE1 . GLU A 1 213 ? -24.074 -9.820  21.050  1.00 19.10 ? 214 GLU A OE1 1 
ATOM   1737 O  OE2 . GLU A 1 213 ? -23.947 -10.823 19.099  1.00 32.73 ? 214 GLU A OE2 1 
ATOM   1738 N  N   . PRO A 1 214 ? -18.444 -11.310 19.922  1.00 11.37 ? 215 PRO A N   1 
ATOM   1739 C  CA  . PRO A 1 214 ? -17.833 -11.273 18.607  1.00 11.49 ? 215 PRO A CA  1 
ATOM   1740 C  C   . PRO A 1 214 ? -18.872 -11.243 17.506  1.00 11.42 ? 215 PRO A C   1 
ATOM   1741 O  O   . PRO A 1 214 ? -20.018 -11.651 17.740  1.00 14.68 ? 215 PRO A O   1 
ATOM   1742 C  CB  . PRO A 1 214 ? -17.083 -12.625 18.547  1.00 12.80 ? 215 PRO A CB  1 
ATOM   1743 C  CG  . PRO A 1 214 ? -17.784 -13.521 19.457  1.00 20.82 ? 215 PRO A CG  1 
ATOM   1744 C  CD  . PRO A 1 214 ? -18.385 -12.636 20.546  1.00 14.89 ? 215 PRO A CD  1 
ATOM   1745 N  N   . ILE A 1 215 ? -18.483 -10.750 16.339  1.00 10.80 ? 216 ILE A N   1 
ATOM   1746 C  CA  . ILE A 1 215 ? -19.284 -10.987 15.154  1.00 11.21 ? 216 ILE A CA  1 
ATOM   1747 C  C   . ILE A 1 215 ? -18.782 -12.243 14.493  1.00 11.59 ? 216 ILE A C   1 
ATOM   1748 O  O   . ILE A 1 215 ? -17.605 -12.604 14.624  1.00 11.93 ? 216 ILE A O   1 
ATOM   1749 C  CB  . ILE A 1 215 ? -19.281 -9.768  14.210  1.00 11.56 ? 216 ILE A CB  1 
ATOM   1750 C  CG1 . ILE A 1 215 ? -17.883 -9.415  13.675  1.00 11.37 ? 216 ILE A CG1 1 
ATOM   1751 C  CG2 . ILE A 1 215 ? -19.975 -8.560  14.872  1.00 12.68 ? 216 ILE A CG2 1 
ATOM   1752 C  CD1 . ILE A 1 215 ? -17.907 -8.492  12.490  1.00 13.11 ? 216 ILE A CD1 1 
ATOM   1753 N  N   . SER A 1 216 ? -19.666 -12.909 13.792  1.00 12.13 ? 217 SER A N   1 
ATOM   1754 C  CA  A SER A 1 216 ? -19.246 -14.052 12.996  0.50 12.94 ? 217 SER A CA  1 
ATOM   1755 C  CA  B SER A 1 216 ? -19.331 -14.069 12.983  0.50 13.16 ? 217 SER A CA  1 
ATOM   1756 C  C   . SER A 1 216 ? -19.089 -13.599 11.554  1.00 11.33 ? 217 SER A C   1 
ATOM   1757 O  O   . SER A 1 216 ? -19.940 -12.870 11.017  1.00 12.43 ? 217 SER A O   1 
ATOM   1758 C  CB  A SER A 1 216 ? -20.291 -15.171 13.015  0.50 14.40 ? 217 SER A CB  1 
ATOM   1759 C  CB  B SER A 1 216 ? -20.514 -15.053 13.016  0.50 16.51 ? 217 SER A CB  1 
ATOM   1760 O  OG  A SER A 1 216 ? -20.549 -15.702 14.298  0.50 14.51 ? 217 SER A OG  1 
ATOM   1761 O  OG  B SER A 1 216 ? -20.173 -16.252 12.331  0.50 19.84 ? 217 SER A OG  1 
ATOM   1762 N  N   . VAL A 1 217 ? -18.002 -14.043 10.938  1.00 11.65 ? 218 VAL A N   1 
ATOM   1763 C  CA  . VAL A 1 217 ? -17.762 -13.845 9.509   1.00 11.39 ? 218 VAL A CA  1 
ATOM   1764 C  C   . VAL A 1 217 ? -17.515 -15.232 8.887   1.00 10.81 ? 218 VAL A C   1 
ATOM   1765 O  O   . VAL A 1 217 ? -17.120 -16.174 9.606   1.00 11.93 ? 218 VAL A O   1 
ATOM   1766 C  CB  . VAL A 1 217 ? -16.568 -12.896 9.268   1.00 12.63 ? 218 VAL A CB  1 
ATOM   1767 C  CG1 . VAL A 1 217 ? -16.824 -11.554 9.996   1.00 12.32 ? 218 VAL A CG1 1 
ATOM   1768 C  CG2 . VAL A 1 217 ? -15.256 -13.543 9.773   1.00 13.56 ? 218 VAL A CG2 1 
ATOM   1769 N  N   . SER A 1 218 ? -17.683 -15.333 7.571   1.00 10.39 ? 219 SER A N   1 
ATOM   1770 C  CA  . SER A 1 218 ? -17.473 -16.648 6.995   1.00 11.58 ? 219 SER A CA  1 
ATOM   1771 C  C   . SER A 1 218 ? -16.000 -16.868 6.670   1.00 11.29 ? 219 SER A C   1 
ATOM   1772 O  O   . SER A 1 218 ? -15.201 -15.936 6.485   1.00 11.58 ? 219 SER A O   1 
ATOM   1773 C  CB  . SER A 1 218 ? -18.327 -16.845 5.768   1.00 12.74 ? 219 SER A CB  1 
ATOM   1774 O  OG  . SER A 1 218 ? -17.950 -15.917 4.762   1.00 12.87 ? 219 SER A OG  1 
ATOM   1775 N  N   . SER A 1 219 ? -15.653 -18.156 6.500   1.00 11.71 ? 220 SER A N   1 
ATOM   1776 C  CA  . SER A 1 219 ? -14.326 -18.512 6.006   1.00 13.66 ? 220 SER A CA  1 
ATOM   1777 C  C   . SER A 1 219 ? -14.054 -17.800 4.686   1.00 12.36 ? 220 SER A C   1 
ATOM   1778 O  O   . SER A 1 219 ? -12.928 -17.321 4.479   1.00 13.35 ? 220 SER A O   1 
ATOM   1779 C  CB  . SER A 1 219 ? -14.203 -20.038 5.891   1.00 15.98 ? 220 SER A CB  1 
ATOM   1780 O  OG  . SER A 1 219 ? -15.184 -20.529 4.994   1.00 18.40 ? 220 SER A OG  1 
ATOM   1781 N  N   . GLU A 1 220 ? -15.039 -17.675 3.770   1.00 12.72 ? 221 GLU A N   1 
ATOM   1782 C  CA  . GLU A 1 220 ? -14.743 -17.039 2.485   1.00 13.22 ? 221 GLU A CA  1 
ATOM   1783 C  C   . GLU A 1 220 ? -14.449 -15.552 2.687   1.00 11.68 ? 221 GLU A C   1 
ATOM   1784 O  O   . GLU A 1 220 ? -13.623 -14.978 1.964   1.00 13.82 ? 221 GLU A O   1 
ATOM   1785 C  CB  . GLU A 1 220 ? -15.955 -17.115 1.543   1.00 14.44 ? 221 GLU A CB  1 
ATOM   1786 C  CG  . GLU A 1 220 ? -16.292 -18.529 1.062   1.00 18.02 ? 221 GLU A CG  1 
ATOM   1787 C  CD  . GLU A 1 220 ? -17.302 -19.260 1.922   1.00 20.20 ? 221 GLU A CD  1 
ATOM   1788 O  OE1 . GLU A 1 220 ? -17.544 -18.880 3.061   1.00 17.69 ? 221 GLU A OE1 1 
ATOM   1789 O  OE2 . GLU A 1 220 ? -17.899 -20.250 1.407   1.00 25.19 ? 221 GLU A OE2 1 
ATOM   1790 N  N   . GLN A 1 221 ? -15.125 -14.898 3.663   1.00 11.41 ? 222 GLN A N   1 
ATOM   1791 C  CA  . GLN A 1 221 ? -14.843 -13.499 3.916   1.00 11.14 ? 222 GLN A CA  1 
ATOM   1792 C  C   . GLN A 1 221 ? -13.414 -13.304 4.445   1.00 12.83 ? 222 GLN A C   1 
ATOM   1793 O  O   . GLN A 1 221 ? -12.671 -12.449 3.942   1.00 12.96 ? 222 GLN A O   1 
ATOM   1794 C  CB  . GLN A 1 221 ? -15.860 -12.939 4.886   1.00 11.50 ? 222 GLN A CB  1 
ATOM   1795 C  CG  . GLN A 1 221 ? -17.245 -12.828 4.217   1.00 10.08 ? 222 GLN A CG  1 
ATOM   1796 C  CD  . GLN A 1 221 ? -18.320 -12.310 5.153   1.00 10.00 ? 222 GLN A CD  1 
ATOM   1797 O  OE1 . GLN A 1 221 ? -18.424 -12.692 6.343   1.00 11.59 ? 222 GLN A OE1 1 
ATOM   1798 N  NE2 . GLN A 1 221 ? -19.132 -11.398 4.624   1.00 11.33 ? 222 GLN A NE2 1 
ATOM   1799 N  N   . VAL A 1 222 ? -13.006 -14.090 5.438   1.00 11.95 ? 223 VAL A N   1 
ATOM   1800 C  CA  . VAL A 1 222 ? -11.672 -13.847 5.974   1.00 12.64 ? 223 VAL A CA  1 
ATOM   1801 C  C   . VAL A 1 222 ? -10.586 -14.296 4.974   1.00 12.33 ? 223 VAL A C   1 
ATOM   1802 O  O   . VAL A 1 222 ? -9.499  -13.735 4.943   1.00 13.17 ? 223 VAL A O   1 
ATOM   1803 C  CB  . VAL A 1 222 ? -11.510 -14.467 7.379   1.00 16.17 ? 223 VAL A CB  1 
ATOM   1804 C  CG1 . VAL A 1 222 ? -11.541 -15.958 7.341   1.00 19.52 ? 223 VAL A CG1 1 
ATOM   1805 C  CG2 . VAL A 1 222 ? -10.255 -13.959 8.118   1.00 17.81 ? 223 VAL A CG2 1 
ATOM   1806 N  N   A LEU A 1 223 ? -10.889 -15.305 4.152   0.50 13.46 ? 224 LEU A N   1 
ATOM   1807 N  N   B LEU A 1 223 ? -10.879 -15.316 4.148   0.50 13.61 ? 224 LEU A N   1 
ATOM   1808 C  CA  A LEU A 1 223 ? -9.960  -15.704 3.104   0.50 14.26 ? 224 LEU A CA  1 
ATOM   1809 C  CA  B LEU A 1 223 ? -9.925  -15.711 3.114   0.50 14.33 ? 224 LEU A CA  1 
ATOM   1810 C  C   A LEU A 1 223 ? -9.608  -14.522 2.201   0.50 12.77 ? 224 LEU A C   1 
ATOM   1811 C  C   B LEU A 1 223 ? -9.617  -14.546 2.167   0.50 13.03 ? 224 LEU A C   1 
ATOM   1812 O  O   A LEU A 1 223 ? -8.452  -14.410 1.773   0.50 14.70 ? 224 LEU A O   1 
ATOM   1813 O  O   B LEU A 1 223 ? -8.486  -14.459 1.675   0.50 15.05 ? 224 LEU A O   1 
ATOM   1814 C  CB  A LEU A 1 223 ? -10.608 -16.831 2.307   0.50 18.83 ? 224 LEU A CB  1 
ATOM   1815 C  CB  B LEU A 1 223 ? -10.408 -16.952 2.349   0.50 16.66 ? 224 LEU A CB  1 
ATOM   1816 C  CG  A LEU A 1 223 ? -9.970  -17.187 0.976   0.50 20.60 ? 224 LEU A CG  1 
ATOM   1817 C  CG  B LEU A 1 223 ? -10.217 -18.294 3.059   0.50 19.61 ? 224 LEU A CG  1 
ATOM   1818 N  N   . LYS A 1 224 ? -10.575 -13.618 1.962   1.00 12.88 ? 225 LYS A N   1 
ATOM   1819 C  CA  . LYS A 1 224 ? -10.281 -12.514 1.080   1.00 13.83 ? 225 LYS A CA  1 
ATOM   1820 C  C   . LYS A 1 224 ? -9.344  -11.519 1.776   1.00 11.98 ? 225 LYS A C   1 
ATOM   1821 O  O   . LYS A 1 224 ? -8.527  -10.928 1.110   1.00 13.52 ? 225 LYS A O   1 
ATOM   1822 C  CB  . LYS A 1 224 ? -11.566 -11.833 0.603   1.00 16.95 ? 225 LYS A CB  1 
ATOM   1823 C  CG  . LYS A 1 224 ? -12.406 -12.694 -0.334  1.00 21.47 ? 225 LYS A CG  1 
ATOM   1824 C  CD  . LYS A 1 224 ? -13.656 -12.013 -0.912  1.00 33.09 ? 225 LYS A CD  1 
ATOM   1825 C  CE  . LYS A 1 224 ? -14.081 -12.424 -2.316  1.00 38.73 ? 225 LYS A CE  1 
ATOM   1826 N  NZ  . LYS A 1 224 ? -14.626 -13.802 -2.398  1.00 47.11 ? 225 LYS A NZ  1 
ATOM   1827 N  N   . PHE A 1 225 ? -9.451  -11.369 3.098   1.00 11.57 ? 226 PHE A N   1 
ATOM   1828 C  CA  . PHE A 1 225 ? -8.494  -10.520 3.792   1.00 11.14 ? 226 PHE A CA  1 
ATOM   1829 C  C   . PHE A 1 225 ? -7.070  -11.040 3.544   1.00 12.30 ? 226 PHE A C   1 
ATOM   1830 O  O   . PHE A 1 225 ? -6.124  -10.281 3.334   1.00 12.51 ? 226 PHE A O   1 
ATOM   1831 C  CB  . PHE A 1 225 ? -8.656  -10.594 5.319   1.00 12.06 ? 226 PHE A CB  1 
ATOM   1832 C  CG  . PHE A 1 225 ? -9.875  -9.891  5.881   1.00 12.27 ? 226 PHE A CG  1 
ATOM   1833 C  CD1 . PHE A 1 225 ? -10.879 -9.432  5.044   1.00 14.93 ? 226 PHE A CD1 1 
ATOM   1834 C  CD2 . PHE A 1 225 ? -10.014 -9.691  7.245   1.00 14.11 ? 226 PHE A CD2 1 
ATOM   1835 C  CE1 . PHE A 1 225 ? -11.994 -8.789  5.558   1.00 14.22 ? 226 PHE A CE1 1 
ATOM   1836 C  CE2 . PHE A 1 225 ? -11.129 -9.048  7.759   1.00 15.19 ? 226 PHE A CE2 1 
ATOM   1837 C  CZ  . PHE A 1 225 ? -12.117 -8.598  6.915   1.00 15.39 ? 226 PHE A CZ  1 
ATOM   1838 N  N   . ARG A 1 226 ? -6.930  -12.378 3.580   1.00 12.26 ? 227 ARG A N   1 
ATOM   1839 C  CA  . ARG A 1 226 ? -5.630  -13.021 3.483   1.00 13.55 ? 227 ARG A CA  1 
ATOM   1840 C  C   . ARG A 1 226 ? -5.028  -12.979 2.076   1.00 13.72 ? 227 ARG A C   1 
ATOM   1841 O  O   . ARG A 1 226 ? -3.889  -13.443 1.927   1.00 17.00 ? 227 ARG A O   1 
ATOM   1842 C  CB  . ARG A 1 226 ? -5.749  -14.475 3.940   1.00 14.41 ? 227 ARG A CB  1 
ATOM   1843 C  CG  . ARG A 1 226 ? -6.159  -14.601 5.401   1.00 14.70 ? 227 ARG A CG  1 
ATOM   1844 C  CD  . ARG A 1 226 ? -5.992  -16.056 5.840   1.00 17.23 ? 227 ARG A CD  1 
ATOM   1845 N  NE  . ARG A 1 226 ? -6.525  -16.200 7.186   1.00 14.98 ? 227 ARG A NE  1 
ATOM   1846 C  CZ  . ARG A 1 226 ? -7.509  -17.052 7.536   1.00 15.38 ? 227 ARG A CZ  1 
ATOM   1847 N  NH1 . ARG A 1 226 ? -7.985  -17.905 6.645   1.00 22.50 ? 227 ARG A NH1 1 
ATOM   1848 N  NH2 . ARG A 1 226 ? -8.006  -17.102 8.746   1.00 17.95 ? 227 ARG A NH2 1 
ATOM   1849 N  N   . LYS A 1 227 ? -5.740  -12.503 1.061   1.00 13.86 ? 228 LYS A N   1 
ATOM   1850 C  CA  . LYS A 1 227 ? -5.217  -12.368 -0.285  1.00 14.64 ? 228 LYS A CA  1 
ATOM   1851 C  C   . LYS A 1 227 ? -4.508  -11.027 -0.460  1.00 13.51 ? 228 LYS A C   1 
ATOM   1852 O  O   . LYS A 1 227 ? -3.845  -10.833 -1.462  1.00 15.73 ? 228 LYS A O   1 
ATOM   1853 C  CB  . LYS A 1 227 ? -6.337  -12.575 -1.323  1.00 18.84 ? 228 LYS A CB  1 
ATOM   1854 C  CG  . LYS A 1 227 ? -6.869  -14.005 -1.393  1.00 20.93 ? 228 LYS A CG  1 
ATOM   1855 C  CD  . LYS A 1 227 ? -7.989  -14.087 -2.452  1.00 28.84 ? 228 LYS A CD  1 
ATOM   1856 C  CE  . LYS A 1 227 ? -8.353  -15.497 -2.880  1.00 50.31 ? 228 LYS A CE  1 
ATOM   1857 N  NZ  . LYS A 1 227 ? -9.286  -16.174 -1.942  1.00 45.81 ? 228 LYS A NZ  1 
ATOM   1858 N  N   . LEU A 1 228 ? -4.693  -10.099 0.499   1.00 13.25 ? 229 LEU A N   1 
ATOM   1859 C  CA  . LEU A 1 228 ? -4.009  -8.827  0.400   1.00 12.42 ? 229 LEU A CA  1 
ATOM   1860 C  C   . LEU A 1 228 ? -2.515  -9.053  0.556   1.00 13.80 ? 229 LEU A C   1 
ATOM   1861 O  O   . LEU A 1 228 ? -2.049  -10.085 1.035   1.00 15.51 ? 229 LEU A O   1 
ATOM   1862 C  CB  . LEU A 1 228 ? -4.518  -7.895  1.511   1.00 12.93 ? 229 LEU A CB  1 
ATOM   1863 C  CG  . LEU A 1 228 ? -5.988  -7.456  1.362   1.00 12.90 ? 229 LEU A CG  1 
ATOM   1864 C  CD1 . LEU A 1 228 ? -6.470  -6.790  2.628   1.00 14.68 ? 229 LEU A CD1 1 
ATOM   1865 C  CD2 . LEU A 1 228 ? -6.096  -6.481  0.196   1.00 17.29 ? 229 LEU A CD2 1 
ATOM   1866 N  N   . ASN A 1 229 ? -1.735  -8.062  0.162   1.00 13.59 ? 230 ASN A N   1 
ATOM   1867 C  CA  . ASN A 1 229 ? -0.274  -8.126  0.243   1.00 12.96 ? 230 ASN A CA  1 
ATOM   1868 C  C   . ASN A 1 229 ? 0.256   -6.970  1.083   1.00 14.45 ? 230 ASN A C   1 
ATOM   1869 O  O   . ASN A 1 229 ? -0.235  -5.850  1.041   1.00 14.63 ? 230 ASN A O   1 
ATOM   1870 C  CB  . ASN A 1 229 ? 0.306   -7.907  -1.168  1.00 14.89 ? 230 ASN A CB  1 
ATOM   1871 C  CG  . ASN A 1 229 ? 0.250   -9.074  -2.132  1.00 15.68 ? 230 ASN A CG  1 
ATOM   1872 O  OD1 . ASN A 1 229 ? 0.878   -9.027  -3.183  1.00 24.74 ? 230 ASN A OD1 1 
ATOM   1873 N  ND2 . ASN A 1 229 ? -0.434  -10.163 -1.824  1.00 19.25 ? 230 ASN A ND2 1 
ATOM   1874 N  N   . PHE A 1 230 ? 1.254   -7.283  1.887   1.00 14.90 ? 231 PHE A N   1 
ATOM   1875 C  CA  . PHE A 1 230 ? 1.956   -6.225  2.580   1.00 15.77 ? 231 PHE A CA  1 
ATOM   1876 C  C   . PHE A 1 230 ? 2.757   -5.365  1.637   1.00 16.47 ? 231 PHE A C   1 
ATOM   1877 O  O   . PHE A 1 230 ? 3.012   -4.191  1.927   1.00 17.79 ? 231 PHE A O   1 
ATOM   1878 C  CB  . PHE A 1 230 ? 2.976   -6.779  3.577   1.00 15.98 ? 231 PHE A CB  1 
ATOM   1879 C  CG  . PHE A 1 230 ? 2.444   -7.412  4.849   1.00 16.19 ? 231 PHE A CG  1 
ATOM   1880 C  CD1 . PHE A 1 230 ? 1.662   -6.684  5.778   1.00 14.61 ? 231 PHE A CD1 1 
ATOM   1881 C  CD2 . PHE A 1 230 ? 2.744   -8.744  5.190   1.00 17.24 ? 231 PHE A CD2 1 
ATOM   1882 C  CE1 . PHE A 1 230 ? 1.280   -7.196  7.010   1.00 15.30 ? 231 PHE A CE1 1 
ATOM   1883 C  CE2 . PHE A 1 230 ? 2.285   -9.265  6.403   1.00 16.60 ? 231 PHE A CE2 1 
ATOM   1884 C  CZ  . PHE A 1 230 ? 1.572   -8.518  7.318   1.00 17.63 ? 231 PHE A CZ  1 
ATOM   1885 N  N   . ASN A 1 231 ? 3.308   -5.993  0.595   1.00 17.86 ? 232 ASN A N   1 
ATOM   1886 C  CA  . ASN A 1 231 ? 4.294   -5.372  -0.289  1.00 18.35 ? 232 ASN A CA  1 
ATOM   1887 C  C   . ASN A 1 231 ? 3.597   -4.442  -1.288  1.00 16.50 ? 232 ASN A C   1 
ATOM   1888 O  O   . ASN A 1 231 ? 2.401   -4.593  -1.568  1.00 17.29 ? 232 ASN A O   1 
ATOM   1889 C  CB  . ASN A 1 231 ? 5.040   -6.432  -1.117  1.00 20.27 ? 232 ASN A CB  1 
ATOM   1890 C  CG  . ASN A 1 231 ? 4.042   -7.376  -1.746  1.00 20.11 ? 232 ASN A CG  1 
ATOM   1891 O  OD1 . ASN A 1 231 ? 3.484   -8.279  -1.081  1.00 19.56 ? 232 ASN A OD1 1 
ATOM   1892 N  ND2 . ASN A 1 231 ? 3.893   -7.220  -3.056  1.00 22.18 ? 232 ASN A ND2 1 
ATOM   1893 N  N   . GLY A 1 232 ? 4.343   -3.502  -1.879  1.00 19.69 ? 233 GLY A N   1 
ATOM   1894 C  CA  . GLY A 1 232 ? 3.887   -2.750  -3.035  1.00 20.26 ? 233 GLY A CA  1 
ATOM   1895 C  C   . GLY A 1 232 ? 4.001   -3.594  -4.295  1.00 25.72 ? 233 GLY A C   1 
ATOM   1896 O  O   . GLY A 1 232 ? 4.727   -4.605  -4.299  1.00 24.01 ? 233 GLY A O   1 
ATOM   1897 N  N   . GLU A 1 233 ? 3.205   -3.222  -5.317  1.00 26.11 ? 234 GLU A N   1 
ATOM   1898 C  CA  . GLU A 1 233 ? 3.225   -3.909  -6.612  1.00 32.46 ? 234 GLU A CA  1 
ATOM   1899 C  C   . GLU A 1 233 ? 4.631   -3.811  -7.193  1.00 38.96 ? 234 GLU A C   1 
ATOM   1900 O  O   . GLU A 1 233 ? 5.136   -2.693  -7.317  1.00 32.17 ? 234 GLU A O   1 
ATOM   1901 C  CB  . GLU A 1 233 ? 2.238   -3.274  -7.604  1.00 37.13 ? 234 GLU A CB  1 
ATOM   1902 C  CG  . GLU A 1 233 ? 2.131   -3.966  -8.960  1.00 47.05 ? 234 GLU A CG  1 
ATOM   1903 N  N   . GLY A 1 234 ? 5.257   -4.956  -7.527  1.00 41.44 ? 235 GLY A N   1 
ATOM   1904 C  CA  . GLY A 1 234 ? 6.622   -4.908  -8.044  1.00 38.54 ? 235 GLY A CA  1 
ATOM   1905 C  C   . GLY A 1 234 ? 7.671   -5.382  -7.035  1.00 47.54 ? 235 GLY A C   1 
ATOM   1906 O  O   . GLY A 1 234 ? 8.821   -5.561  -7.446  1.00 57.52 ? 235 GLY A O   1 
ATOM   1907 N  N   . GLU A 1 235 ? 7.296   -5.574  -5.746  1.00 39.81 ? 236 GLU A N   1 
ATOM   1908 C  CA  . GLU A 1 235 ? 8.200   -6.096  -4.719  1.00 31.75 ? 236 GLU A CA  1 
ATOM   1909 C  C   . GLU A 1 235 ? 7.895   -7.570  -4.449  1.00 25.28 ? 236 GLU A C   1 
ATOM   1910 O  O   . GLU A 1 235 ? 6.789   -7.952  -4.800  1.00 29.18 ? 236 GLU A O   1 
ATOM   1911 C  CB  . GLU A 1 235 ? 7.955   -5.285  -3.438  1.00 36.46 ? 236 GLU A CB  1 
ATOM   1912 C  CG  . GLU A 1 235 ? 8.476   -3.862  -3.554  1.00 49.97 ? 236 GLU A CG  1 
ATOM   1913 C  CD  . GLU A 1 235 ? 7.898   -2.812  -2.610  1.00 72.02 ? 236 GLU A CD  1 
ATOM   1914 O  OE1 . GLU A 1 235 ? 7.158   -3.171  -1.654  1.00 54.51 ? 236 GLU A OE1 1 
ATOM   1915 O  OE2 . GLU A 1 235 ? 8.206   -1.622  -2.868  1.00 75.44 ? 236 GLU A OE2 1 
ATOM   1916 N  N   . PRO A 1 236 ? 8.731   -8.421  -3.764  1.00 24.09 ? 237 PRO A N   1 
ATOM   1917 C  CA  . PRO A 1 236 ? 8.354   -9.807  -3.475  1.00 24.03 ? 237 PRO A CA  1 
ATOM   1918 C  C   . PRO A 1 236 ? 7.022   -9.853  -2.764  1.00 22.06 ? 237 PRO A C   1 
ATOM   1919 O  O   . PRO A 1 236 ? 6.678   -9.030  -1.897  1.00 25.88 ? 237 PRO A O   1 
ATOM   1920 C  CB  . PRO A 1 236 ? 9.462   -10.345 -2.549  1.00 25.13 ? 237 PRO A CB  1 
ATOM   1921 C  CG  . PRO A 1 236 ? 10.648  -9.551  -3.040  1.00 27.27 ? 237 PRO A CG  1 
ATOM   1922 C  CD  . PRO A 1 236 ? 10.099  -8.159  -3.260  1.00 29.90 ? 237 PRO A CD  1 
ATOM   1923 N  N   . GLU A 1 237 ? 6.289   -10.910 -3.069  1.00 22.32 ? 238 GLU A N   1 
ATOM   1924 C  CA  . GLU A 1 237 ? 4.950   -11.101 -2.565  1.00 18.62 ? 238 GLU A CA  1 
ATOM   1925 C  C   . GLU A 1 237 ? 4.989   -11.656 -1.134  1.00 21.38 ? 238 GLU A C   1 
ATOM   1926 O  O   . GLU A 1 237 ? 5.414   -12.796 -0.885  1.00 23.40 ? 238 GLU A O   1 
ATOM   1927 C  CB  . GLU A 1 237 ? 4.247   -12.070 -3.516  1.00 19.21 ? 238 GLU A CB  1 
ATOM   1928 C  CG  . GLU A 1 237 ? 2.849   -12.429 -3.055  1.00 19.79 ? 238 GLU A CG  1 
ATOM   1929 C  CD  . GLU A 1 237 ? 2.200   -13.418 -4.051  1.00 23.37 ? 238 GLU A CD  1 
ATOM   1930 O  OE1 . GLU A 1 237 ? 2.794   -13.698 -5.122  1.00 28.15 ? 238 GLU A OE1 1 
ATOM   1931 O  OE2 . GLU A 1 237 ? 1.108   -13.922 -3.784  1.00 33.21 ? 238 GLU A OE2 1 
ATOM   1932 N  N   . GLU A 1 238 ? 4.410   -10.902 -0.196  1.00 19.32 ? 239 GLU A N   1 
ATOM   1933 C  CA  . GLU A 1 238 ? 4.265   -11.338 1.187   1.00 20.54 ? 239 GLU A CA  1 
ATOM   1934 C  C   . GLU A 1 238 ? 2.812   -11.102 1.573   1.00 16.08 ? 239 GLU A C   1 
ATOM   1935 O  O   . GLU A 1 238 ? 2.360   -9.945  1.618   1.00 21.39 ? 239 GLU A O   1 
ATOM   1936 C  CB  . GLU A 1 238 ? 5.173   -10.532 2.102   1.00 25.61 ? 239 GLU A CB  1 
ATOM   1937 C  CG  . GLU A 1 238 ? 6.635   -10.828 1.910   1.00 24.58 ? 239 GLU A CG  1 
ATOM   1938 C  CD  . GLU A 1 238 ? 7.471   -10.149 2.984   1.00 28.37 ? 239 GLU A CD  1 
ATOM   1939 O  OE1 . GLU A 1 238 ? 7.358   -10.532 4.195   1.00 31.05 ? 239 GLU A OE1 1 
ATOM   1940 O  OE2 . GLU A 1 238 ? 8.189   -9.193  2.607   1.00 34.47 ? 239 GLU A OE2 1 
ATOM   1941 N  N   . LEU A 1 239 ? 2.029   -12.192 1.699   1.00 18.55 ? 240 LEU A N   1 
ATOM   1942 C  CA  . LEU A 1 239 ? 0.622   -12.010 1.988   1.00 16.34 ? 240 LEU A CA  1 
ATOM   1943 C  C   . LEU A 1 239 ? 0.511   -11.216 3.288   1.00 15.08 ? 240 LEU A C   1 
ATOM   1944 O  O   . LEU A 1 239 ? 1.231   -11.396 4.272   1.00 16.35 ? 240 LEU A O   1 
ATOM   1945 C  CB  . LEU A 1 239 ? -0.058  -13.364 2.202   1.00 18.60 ? 240 LEU A CB  1 
ATOM   1946 C  CG  . LEU A 1 239 ? -0.197  -14.228 0.957   1.00 20.12 ? 240 LEU A CG  1 
ATOM   1947 C  CD1 . LEU A 1 239 ? -1.014  -15.438 1.335   1.00 25.09 ? 240 LEU A CD1 1 
ATOM   1948 C  CD2 . LEU A 1 239 ? -0.857  -13.380 -0.131  1.00 19.63 ? 240 LEU A CD2 1 
ATOM   1949 N  N   . MET A 1 240 ? -0.486  -10.322 3.280   1.00 14.13 ? 241 MET A N   1 
ATOM   1950 C  CA  . MET A 1 240 ? -0.850  -9.560  4.471   1.00 13.33 ? 241 MET A CA  1 
ATOM   1951 C  C   . MET A 1 240 ? -1.663  -10.438 5.429   1.00 12.19 ? 241 MET A C   1 
ATOM   1952 O  O   . MET A 1 240 ? -2.872  -10.587 5.277   1.00 13.97 ? 241 MET A O   1 
ATOM   1953 C  CB  . MET A 1 240 ? -1.612  -8.287  4.068   1.00 12.79 ? 241 MET A CB  1 
ATOM   1954 C  CG  . MET A 1 240 ? -2.004  -7.434  5.263   1.00 13.38 ? 241 MET A CG  1 
ATOM   1955 S  SD  . MET A 1 240 ? -2.917  -5.971  4.796   1.00 14.34 ? 241 MET A SD  1 
ATOM   1956 C  CE  . MET A 1 240 ? -1.616  -4.956  4.055   1.00 14.50 ? 241 MET A CE  1 
ATOM   1957 N  N   . VAL A 1 241 ? -0.945  -11.128 6.317   1.00 13.50 ? 242 VAL A N   1 
ATOM   1958 C  CA  . VAL A 1 241 ? -1.515  -11.997 7.349   1.00 13.33 ? 242 VAL A CA  1 
ATOM   1959 C  C   . VAL A 1 241 ? -0.705  -11.821 8.619   1.00 11.52 ? 242 VAL A C   1 
ATOM   1960 O  O   . VAL A 1 241 ? 0.455   -11.402 8.554   1.00 13.15 ? 242 VAL A O   1 
ATOM   1961 C  CB  . VAL A 1 241 ? -1.515  -13.494 6.896   1.00 13.07 ? 242 VAL A CB  1 
ATOM   1962 C  CG1 . VAL A 1 241 ? -2.423  -13.736 5.669   1.00 15.53 ? 242 VAL A CG1 1 
ATOM   1963 C  CG2 . VAL A 1 241 ? -0.092  -13.988 6.558   1.00 17.42 ? 242 VAL A CG2 1 
ATOM   1964 N  N   . ASP A 1 242 ? -1.315  -12.148 9.763   1.00 11.21 ? 243 ASP A N   1 
ATOM   1965 C  CA  . ASP A 1 242 ? -0.654  -12.021 11.053  1.00 12.08 ? 243 ASP A CA  1 
ATOM   1966 C  C   . ASP A 1 242 ? -0.166  -10.598 11.267  1.00 11.59 ? 243 ASP A C   1 
ATOM   1967 O  O   . ASP A 1 242 ? 0.936   -10.355 11.749  1.00 13.33 ? 243 ASP A O   1 
ATOM   1968 C  CB  . ASP A 1 242 ? 0.432   -13.067 11.256  1.00 12.15 ? 243 ASP A CB  1 
ATOM   1969 C  CG  . ASP A 1 242 ? -0.177  -14.444 11.329  1.00 12.82 ? 243 ASP A CG  1 
ATOM   1970 O  OD1 . ASP A 1 242 ? -1.249  -14.610 11.942  1.00 12.75 ? 243 ASP A OD1 1 
ATOM   1971 O  OD2 . ASP A 1 242 ? 0.444   -15.394 10.813  1.00 15.42 ? 243 ASP A OD2 1 
ATOM   1972 N  N   . ASN A 1 243 ? -1.053  -9.652  10.957  1.00 10.30 ? 244 ASN A N   1 
ATOM   1973 C  CA  . ASN A 1 243 ? -0.782  -8.232  11.226  1.00 10.45 ? 244 ASN A CA  1 
ATOM   1974 C  C   . ASN A 1 243 ? -1.357  -7.806  12.580  1.00 9.49  ? 244 ASN A C   1 
ATOM   1975 O  O   . ASN A 1 243 ? -2.040  -6.792  12.664  1.00 12.08 ? 244 ASN A O   1 
ATOM   1976 C  CB  . ASN A 1 243 ? -1.285  -7.352  10.065  1.00 11.06 ? 244 ASN A CB  1 
ATOM   1977 C  CG  . ASN A 1 243 ? -2.756  -7.510  9.786   1.00 11.85 ? 244 ASN A CG  1 
ATOM   1978 O  OD1 . ASN A 1 243 ? -3.389  -8.398  10.328  1.00 12.68 ? 244 ASN A OD1 1 
ATOM   1979 N  ND2 . ASN A 1 243 ? -3.315  -6.604  9.014   1.00 12.47 ? 244 ASN A ND2 1 
ATOM   1980 N  N   . TRP A 1 244 ? -1.057  -8.558  13.616  1.00 10.44 ? 245 TRP A N   1 
ATOM   1981 C  CA  . TRP A 1 244 ? -1.495  -8.324  14.978  1.00 10.31 ? 245 TRP A CA  1 
ATOM   1982 C  C   . TRP A 1 244 ? -0.294  -8.262  15.906  1.00 10.22 ? 245 TRP A C   1 
ATOM   1983 O  O   . TRP A 1 244 ? 0.691   -8.957  15.730  1.00 11.95 ? 245 TRP A O   1 
ATOM   1984 C  CB  . TRP A 1 244 ? -2.459  -9.411  15.439  1.00 10.41 ? 245 TRP A CB  1 
ATOM   1985 C  CG  . TRP A 1 244 ? -2.011  -10.815 15.224  1.00 11.14 ? 245 TRP A CG  1 
ATOM   1986 C  CD1 . TRP A 1 244 ? -2.138  -11.558 14.068  1.00 10.73 ? 245 TRP A CD1 1 
ATOM   1987 C  CD2 . TRP A 1 244 ? -1.447  -11.685 16.225  1.00 11.49 ? 245 TRP A CD2 1 
ATOM   1988 N  NE1 . TRP A 1 244 ? -1.625  -12.810 14.280  1.00 11.74 ? 245 TRP A NE1 1 
ATOM   1989 C  CE2 . TRP A 1 244 ? -1.164  -12.914 15.574  1.00 11.42 ? 245 TRP A CE2 1 
ATOM   1990 C  CE3 . TRP A 1 244 ? -1.126  -11.545 17.587  1.00 12.58 ? 245 TRP A CE3 1 
ATOM   1991 C  CZ2 . TRP A 1 244 ? -0.651  -14.022 16.292  1.00 12.20 ? 245 TRP A CZ2 1 
ATOM   1992 C  CZ3 . TRP A 1 244 ? -0.616  -12.633 18.284  1.00 13.51 ? 245 TRP A CZ3 1 
ATOM   1993 C  CH2 . TRP A 1 244 ? -0.380  -13.850 17.628  1.00 14.08 ? 245 TRP A CH2 1 
ATOM   1994 N  N   . ARG A 1 245 ? -0.395  -7.363  16.892  1.00 11.08 ? 246 ARG A N   1 
ATOM   1995 C  CA  . ARG A 1 245 ? 0.566   -7.273  18.000  1.00 10.84 ? 246 ARG A CA  1 
ATOM   1996 C  C   . ARG A 1 245 ? 0.092   -8.175  19.112  1.00 12.16 ? 246 ARG A C   1 
ATOM   1997 O  O   . ARG A 1 245 ? -1.091  -8.200  19.421  1.00 12.14 ? 246 ARG A O   1 
ATOM   1998 C  CB  . ARG A 1 245 ? 0.635   -5.835  18.480  1.00 9.98  ? 246 ARG A CB  1 
ATOM   1999 C  CG  . ARG A 1 245 ? 1.759   -5.614  19.463  1.00 10.97 ? 246 ARG A CG  1 
ATOM   2000 C  CD  . ARG A 1 245 ? 1.659   -4.285  20.166  1.00 11.11 ? 246 ARG A CD  1 
ATOM   2001 N  NE  . ARG A 1 245 ? 2.911   -3.958  20.865  1.00 10.99 ? 246 ARG A NE  1 
ATOM   2002 C  CZ  . ARG A 1 245 ? 3.063   -2.936  21.699  1.00 11.47 ? 246 ARG A CZ  1 
ATOM   2003 N  NH1 . ARG A 1 245 ? 2.046   -2.128  21.948  1.00 11.83 ? 246 ARG A NH1 1 
ATOM   2004 N  NH2 . ARG A 1 245 ? 4.230   -2.724  22.280  1.00 11.87 ? 246 ARG A NH2 1 
ATOM   2005 N  N   . PRO A 1 246 ? 0.970   -8.997  19.709  1.00 12.12 ? 247 PRO A N   1 
ATOM   2006 C  CA  . PRO A 1 246 ? 0.558   -9.818  20.833  1.00 12.42 ? 247 PRO A CA  1 
ATOM   2007 C  C   . PRO A 1 246 ? 0.230   -8.998  22.078  1.00 12.70 ? 247 PRO A C   1 
ATOM   2008 O  O   . PRO A 1 246 ? 0.592   -7.822  22.197  1.00 12.11 ? 247 PRO A O   1 
ATOM   2009 C  CB  . PRO A 1 246 ? 1.785   -10.701 21.149  1.00 16.27 ? 247 PRO A CB  1 
ATOM   2010 C  CG  . PRO A 1 246 ? 2.670   -10.586 19.924  1.00 20.46 ? 247 PRO A CG  1 
ATOM   2011 C  CD  . PRO A 1 246 ? 2.389   -9.221  19.317  1.00 15.07 ? 247 PRO A CD  1 
ATOM   2012 N  N   . ALA A 1 247 ? -0.482  -9.647  23.018  1.00 13.09 ? 248 ALA A N   1 
ATOM   2013 C  CA  . ALA A 1 247 ? -0.825  -9.042  24.285  1.00 12.21 ? 248 ALA A CA  1 
ATOM   2014 C  C   . ALA A 1 247 ? 0.420   -8.496  24.955  1.00 11.80 ? 248 ALA A C   1 
ATOM   2015 O  O   . ALA A 1 247 ? 1.468   -9.174  25.049  1.00 15.15 ? 248 ALA A O   1 
ATOM   2016 C  CB  . ALA A 1 247 ? -1.587  -10.056 25.126  1.00 15.19 ? 248 ALA A CB  1 
ATOM   2017 N  N   . GLN A 1 248 ? 0.250   -7.322  25.556  1.00 12.23 ? 249 GLN A N   1 
ATOM   2018 C  CA  . GLN A 1 248 ? 1.313   -6.633  26.281  1.00 13.34 ? 249 GLN A CA  1 
ATOM   2019 C  C   . GLN A 1 248 ? 0.984   -6.607  27.776  1.00 14.55 ? 249 GLN A C   1 
ATOM   2020 O  O   . GLN A 1 248 ? -0.172  -6.807  28.198  1.00 14.56 ? 249 GLN A O   1 
ATOM   2021 C  CB  . GLN A 1 248 ? 1.388   -5.196  25.800  1.00 13.28 ? 249 GLN A CB  1 
ATOM   2022 C  CG  . GLN A 1 248 ? 1.731   -5.112  24.308  1.00 13.74 ? 249 GLN A CG  1 
ATOM   2023 C  CD  . GLN A 1 248 ? 3.030   -5.803  23.973  1.00 13.98 ? 249 GLN A CD  1 
ATOM   2024 O  OE1 . GLN A 1 248 ? 4.066   -5.483  24.552  1.00 16.49 ? 249 GLN A OE1 1 
ATOM   2025 N  NE2 . GLN A 1 248 ? 3.009   -6.751  23.037  1.00 14.87 ? 249 GLN A NE2 1 
ATOM   2026 N  N   . PRO A 1 249 ? 1.989   -6.358  28.642  1.00 15.13 ? 250 PRO A N   1 
ATOM   2027 C  CA  . PRO A 1 249 ? 1.767   -6.460  30.081  1.00 16.09 ? 250 PRO A CA  1 
ATOM   2028 C  C   . PRO A 1 249 ? 0.726   -5.434  30.541  1.00 16.57 ? 250 PRO A C   1 
ATOM   2029 O  O   . PRO A 1 249 ? 0.802   -4.254  30.207  1.00 16.15 ? 250 PRO A O   1 
ATOM   2030 C  CB  . PRO A 1 249 ? 3.153   -6.095  30.687  1.00 22.69 ? 250 PRO A CB  1 
ATOM   2031 C  CG  . PRO A 1 249 ? 4.163   -6.317  29.583  1.00 21.39 ? 250 PRO A CG  1 
ATOM   2032 C  CD  . PRO A 1 249 ? 3.407   -6.132  28.283  1.00 18.69 ? 250 PRO A CD  1 
ATOM   2033 N  N   . LEU A 1 250 ? -0.206  -5.889  31.372  1.00 16.63 ? 251 LEU A N   1 
ATOM   2034 C  CA  . LEU A 1 250 ? -1.246  -5.009  31.885  1.00 15.12 ? 251 LEU A CA  1 
ATOM   2035 C  C   . LEU A 1 250 ? -0.672  -3.961  32.853  1.00 14.77 ? 251 LEU A C   1 
ATOM   2036 O  O   . LEU A 1 250 ? -1.196  -2.849  32.971  1.00 14.89 ? 251 LEU A O   1 
ATOM   2037 C  CB  . LEU A 1 250 ? -2.290  -5.873  32.563  1.00 18.33 ? 251 LEU A CB  1 
ATOM   2038 C  CG  . LEU A 1 250 ? -3.568  -5.169  32.960  1.00 17.66 ? 251 LEU A CG  1 
ATOM   2039 C  CD1 . LEU A 1 250 ? -4.283  -4.516  31.769  1.00 17.99 ? 251 LEU A CD1 1 
ATOM   2040 C  CD2 . LEU A 1 250 ? -4.497  -6.156  33.636  1.00 22.61 ? 251 LEU A CD2 1 
ATOM   2041 N  N   . LYS A 1 251 ? 0.426   -4.309  33.537  1.00 16.85 ? 252 LYS A N   1 
ATOM   2042 C  CA  . LYS A 1 251 ? 1.057   -3.327  34.438  1.00 17.48 ? 252 LYS A CA  1 
ATOM   2043 C  C   . LYS A 1 251 ? 0.049   -2.837  35.499  1.00 18.62 ? 252 LYS A C   1 
ATOM   2044 O  O   . LYS A 1 251 ? -0.639  -3.652  36.085  1.00 28.95 ? 252 LYS A O   1 
ATOM   2045 C  CB  . LYS A 1 251 ? 1.910   -2.281  33.720  1.00 18.50 ? 252 LYS A CB  1 
ATOM   2046 C  CG  . LYS A 1 251 ? 3.018   -2.918  32.911  1.00 23.62 ? 252 LYS A CG  1 
ATOM   2047 C  CD  . LYS A 1 251 ? 3.889   -1.941  32.249  1.00 23.89 ? 252 LYS A CD  1 
ATOM   2048 C  CE  . LYS A 1 251 ? 5.153   -2.657  31.841  1.00 26.95 ? 252 LYS A CE  1 
ATOM   2049 N  NZ  . LYS A 1 251 ? 6.039   -1.823  30.973  1.00 31.15 ? 252 LYS A NZ  1 
ATOM   2050 N  N   . ASN A 1 252 ? -0.052  -1.567  35.858  1.00 20.16 ? 253 ASN A N   1 
ATOM   2051 C  CA  . ASN A 1 252 ? -0.966  -1.397  37.027  1.00 30.88 ? 253 ASN A CA  1 
ATOM   2052 C  C   . ASN A 1 252 ? -2.443  -1.267  36.630  1.00 29.14 ? 253 ASN A C   1 
ATOM   2053 O  O   . ASN A 1 252 ? -3.235  -1.119  37.503  1.00 28.81 ? 253 ASN A O   1 
ATOM   2054 C  CB  . ASN A 1 252 ? -0.536  -0.221  37.910  1.00 38.13 ? 253 ASN A CB  1 
ATOM   2055 N  N   . ARG A 1 253 ? -2.843  -1.630  35.428  1.00 17.39 ? 254 ARG A N   1 
ATOM   2056 C  CA  . ARG A 1 253 ? -4.143  -1.183  34.947  1.00 15.30 ? 254 ARG A CA  1 
ATOM   2057 C  C   . ARG A 1 253 ? -5.256  -2.136  35.360  1.00 15.39 ? 254 ARG A C   1 
ATOM   2058 O  O   . ARG A 1 253 ? -5.029  -3.336  35.522  1.00 19.72 ? 254 ARG A O   1 
ATOM   2059 C  CB  . ARG A 1 253 ? -4.133  -1.067  33.414  1.00 14.70 ? 254 ARG A CB  1 
ATOM   2060 C  CG  . ARG A 1 253 ? -3.215  0.083   32.982  1.00 14.80 ? 254 ARG A CG  1 
ATOM   2061 C  CD  . ARG A 1 253 ? -3.101  0.055   31.484  1.00 14.25 ? 254 ARG A CD  1 
ATOM   2062 N  NE  . ARG A 1 253 ? -2.322  -1.096  31.023  1.00 11.92 ? 254 ARG A NE  1 
ATOM   2063 C  CZ  . ARG A 1 253 ? -2.050  -1.310  29.736  1.00 10.63 ? 254 ARG A CZ  1 
ATOM   2064 N  NH1 . ARG A 1 253 ? -2.684  -0.646  28.766  1.00 11.22 ? 254 ARG A NH1 1 
ATOM   2065 N  NH2 . ARG A 1 253 ? -1.227  -2.304  29.407  1.00 11.42 ? 254 ARG A NH2 1 
ATOM   2066 N  N   A GLN A 1 254 ? -6.445  -1.557  35.524  0.50 16.02 ? 255 GLN A N   1 
ATOM   2067 N  N   B GLN A 1 254 ? -6.479  -1.610  35.504  0.50 17.21 ? 255 GLN A N   1 
ATOM   2068 C  CA  A GLN A 1 254 ? -7.663  -2.318  35.679  0.50 15.52 ? 255 GLN A CA  1 
ATOM   2069 C  CA  B GLN A 1 254 ? -7.641  -2.440  35.769  0.50 16.92 ? 255 GLN A CA  1 
ATOM   2070 C  C   A GLN A 1 254 ? -8.426  -2.330  34.360  0.50 12.73 ? 255 GLN A C   1 
ATOM   2071 C  C   B GLN A 1 254 ? -8.635  -2.330  34.617  0.50 16.85 ? 255 GLN A C   1 
ATOM   2072 O  O   A GLN A 1 254 ? -8.530  -1.325  33.646  0.50 14.16 ? 255 GLN A O   1 
ATOM   2073 O  O   B GLN A 1 254 ? -9.036  -1.233  34.224  0.50 22.34 ? 255 GLN A O   1 
ATOM   2074 C  CB  A GLN A 1 254 ? -8.497  -1.701  36.804  0.50 18.89 ? 255 GLN A CB  1 
ATOM   2075 C  CB  B GLN A 1 254 ? -8.301  -1.991  37.073  0.50 20.23 ? 255 GLN A CB  1 
ATOM   2076 C  CG  A GLN A 1 254 ? -7.772  -1.698  38.148  0.50 25.47 ? 255 GLN A CG  1 
ATOM   2077 C  CG  B GLN A 1 254 ? -9.668  -2.607  37.323  0.50 22.53 ? 255 GLN A CG  1 
ATOM   2078 N  N   . ILE A 1 255 ? -9.003  -3.482  34.067  1.00 13.68 ? 256 ILE A N   1 
ATOM   2079 C  CA  . ILE A 1 255 ? -10.023 -3.555  33.035  1.00 13.98 ? 256 ILE A CA  1 
ATOM   2080 C  C   . ILE A 1 255 ? -11.388 -3.550  33.712  1.00 13.51 ? 256 ILE A C   1 
ATOM   2081 O  O   . ILE A 1 255 ? -11.629 -4.263  34.679  1.00 14.91 ? 256 ILE A O   1 
ATOM   2082 C  CB  . ILE A 1 255 ? -9.830  -4.828  32.195  1.00 14.11 ? 256 ILE A CB  1 
ATOM   2083 C  CG1 . ILE A 1 255 ? -8.394  -4.829  31.645  1.00 16.75 ? 256 ILE A CG1 1 
ATOM   2084 C  CG2 . ILE A 1 255 ? -10.882 -4.921  31.077  1.00 16.64 ? 256 ILE A CG2 1 
ATOM   2085 C  CD1 . ILE A 1 255 ? -8.112  -6.114  30.818  1.00 17.98 ? 256 ILE A CD1 1 
ATOM   2086 N  N   . LYS A 1 256 ? -12.245 -2.656  33.235  1.00 13.24 ? 257 LYS A N   1 
ATOM   2087 C  CA  . LYS A 1 256 ? -13.607 -2.552  33.757  1.00 13.58 ? 257 LYS A CA  1 
ATOM   2088 C  C   . LYS A 1 256 ? -14.588 -3.219  32.795  1.00 12.48 ? 257 LYS A C   1 
ATOM   2089 O  O   . LYS A 1 256 ? -14.380 -3.197  31.579  1.00 14.59 ? 257 LYS A O   1 
ATOM   2090 C  CB  . LYS A 1 256 ? -13.939 -1.063  33.890  1.00 15.47 ? 257 LYS A CB  1 
ATOM   2091 C  CG  . LYS A 1 256 ? -13.123 -0.334  34.941  1.00 22.06 ? 257 LYS A CG  1 
ATOM   2092 C  CD  . LYS A 1 256 ? -13.466 1.138   35.145  1.00 30.14 ? 257 LYS A CD  1 
ATOM   2093 N  N   . ALA A 1 257 ? -15.646 -3.817  33.339  1.00 14.12 ? 258 ALA A N   1 
ATOM   2094 C  CA  . ALA A 1 257 ? -16.711 -4.405  32.535  1.00 14.98 ? 258 ALA A CA  1 
ATOM   2095 C  C   . ALA A 1 257 ? -17.984 -3.587  32.715  1.00 14.59 ? 258 ALA A C   1 
ATOM   2096 O  O   . ALA A 1 257 ? -18.320 -3.183  33.842  1.00 16.49 ? 258 ALA A O   1 
ATOM   2097 C  CB  . ALA A 1 257 ? -16.921 -5.842  32.944  1.00 16.69 ? 258 ALA A CB  1 
ATOM   2098 N  N   . SER A 1 258 ? -18.745 -3.440  31.615  1.00 13.40 ? 259 SER A N   1 
ATOM   2099 C  CA  . SER A 1 258 ? -20.040 -2.765  31.681  1.00 15.45 ? 259 SER A CA  1 
ATOM   2100 C  C   . SER A 1 258 ? -21.157 -3.723  32.100  1.00 15.19 ? 259 SER A C   1 
ATOM   2101 O  O   . SER A 1 258 ? -22.333 -3.310  32.158  1.00 20.51 ? 259 SER A O   1 
ATOM   2102 C  CB  . SER A 1 258 ? -20.344 -2.185  30.319  1.00 15.52 ? 259 SER A CB  1 
ATOM   2103 O  OG  . SER A 1 258 ? -20.773 -3.216  29.415  1.00 15.16 ? 259 SER A OG  1 
ATOM   2104 N  N   . PHE A 1 259 ? -20.807 -4.992  32.351  1.00 16.49 ? 260 PHE A N   1 
ATOM   2105 C  CA  . PHE A 1 259 ? -21.824 -6.018  32.522  1.00 19.58 ? 260 PHE A CA  1 
ATOM   2106 C  C   . PHE A 1 259 ? -21.300 -7.047  33.513  1.00 23.09 ? 260 PHE A C   1 
ATOM   2107 O  O   . PHE A 1 259 ? -20.079 -7.133  33.750  1.00 20.00 ? 260 PHE A O   1 
ATOM   2108 C  CB  . PHE A 1 259 ? -22.081 -6.698  31.174  1.00 19.66 ? 260 PHE A CB  1 
ATOM   2109 C  CG  . PHE A 1 259 ? -20.877 -7.474  30.661  1.00 17.61 ? 260 PHE A CG  1 
ATOM   2110 C  CD1 . PHE A 1 259 ? -19.840 -6.797  30.030  1.00 16.65 ? 260 PHE A CD1 1 
ATOM   2111 C  CD2 . PHE A 1 259 ? -20.694 -8.836  30.925  1.00 22.12 ? 260 PHE A CD2 1 
ATOM   2112 C  CE1 . PHE A 1 259 ? -18.678 -7.475  29.661  1.00 18.14 ? 260 PHE A CE1 1 
ATOM   2113 C  CE2 . PHE A 1 259 ? -19.551 -9.514  30.530  1.00 22.28 ? 260 PHE A CE2 1 
ATOM   2114 C  CZ  . PHE A 1 259 ? -18.548 -8.822  29.904  1.00 22.19 ? 260 PHE A CZ  1 
ATOM   2115 N  N   . LYS A 1 260 ? -22.278 -7.815  34.011  1.00 28.58 ? 261 LYS A N   1 
ATOM   2116 C  CA  . LYS A 1 260 ? -22.247 -9.064  34.762  1.00 43.33 ? 261 LYS A CA  1 
ATOM   2117 C  C   . LYS A 1 260 ? -21.927 -8.823  36.236  1.00 53.84 ? 261 LYS A C   1 
ATOM   2118 O  O   . LYS A 1 260 ? -22.708 -8.173  36.947  1.00 63.42 ? 261 LYS A O   1 
ATOM   2119 C  CB  . LYS A 1 260 ? -21.580 -10.245 34.044  1.00 58.39 ? 261 LYS A CB  1 
ATOM   2120 C  CG  . LYS A 1 260 ? -22.497 -10.966 33.052  1.00 51.40 ? 261 LYS A CG  1 
ATOM   2121 O  OXT . LYS A 1 260 ? -20.904 -9.299  36.697  1.00 82.76 ? 261 LYS A OXT 1 
HETATM 2122 ZN ZN  . ZN  B 2 .   ? -5.943  -1.571  14.881  1.00 9.01  ? 301 ZN  A ZN  1 
HETATM 2123 S  S   . DMS C 3 .   ? 1.990   -11.738 14.585  1.00 27.05 ? 302 DMS A S   1 
HETATM 2124 O  O   . DMS C 3 .   ? 2.560   -13.140 14.157  1.00 30.64 ? 302 DMS A O   1 
HETATM 2125 C  C1  . DMS C 3 .   ? 2.190   -11.658 16.341  1.00 20.81 ? 302 DMS A C1  1 
HETATM 2126 C  C2  . DMS C 3 .   ? 3.321   -10.605 14.258  1.00 33.46 ? 302 DMS A C2  1 
HETATM 2127 O  O1  . MES D 4 .   ? -6.809  -8.968  -2.838  1.00 33.26 ? 303 MES A O1  1 
HETATM 2128 C  C2  . MES D 4 .   ? -7.732  -9.186  -1.763  1.00 24.74 ? 303 MES A C2  1 
HETATM 2129 C  C3  . MES D 4 .   ? -8.889  -10.106 -1.938  1.00 24.67 ? 303 MES A C3  1 
HETATM 2130 N  N4  . MES D 4 .   ? -9.227  -10.286 -3.388  1.00 38.63 ? 303 MES A N4  1 
HETATM 2131 C  C5  . MES D 4 .   ? -8.026  -10.736 -4.175  1.00 36.54 ? 303 MES A C5  1 
HETATM 2132 C  C6  . MES D 4 .   ? -6.781  -9.911  -3.931  1.00 36.50 ? 303 MES A C6  1 
HETATM 2133 C  C7  . MES D 4 .   ? -10.385 -11.230 -3.593  1.00 32.87 ? 303 MES A C7  1 
HETATM 2134 C  C8  . MES D 4 .   ? -10.083 -12.224 -4.711  1.00 44.07 ? 303 MES A C8  1 
HETATM 2135 C  C1  . LML E 5 .   ? -2.032  4.383   10.422  1.00 22.39 ? 304 LML A C1  1 
HETATM 2136 O  O1  . LML E 5 .   ? -3.208  4.084   10.210  1.00 23.56 ? 304 LML A O1  1 
HETATM 2137 O  OXT . LML E 5 .   ? -1.253  3.698   11.101  1.00 23.32 ? 304 LML A OXT 1 
HETATM 2138 C  CA  . LML E 5 .   ? -1.484  5.688   9.806   1.00 23.96 ? 304 LML A CA  1 
HETATM 2139 C  C   . LML E 5 .   ? -0.416  5.440   8.714   1.00 33.27 ? 304 LML A C   1 
HETATM 2140 O  O   . LML E 5 .   ? -0.469  4.331   8.049   1.00 33.43 ? 304 LML A O   1 
HETATM 2141 O  O2  . LML E 5 .   ? 0.501   6.331   8.565   1.00 38.22 ? 304 LML A O2  1 
HETATM 2142 F  F18 . 3TV F 6 .   ? -1.030  3.500   14.810  1.00 14.97 ? 305 3TV A F18 1 
HETATM 2143 C  C7  . 3TV F 6 .   ? -2.359  3.476   14.803  1.00 12.99 ? 305 3TV A C7  1 
HETATM 2144 C  C6  . 3TV F 6 .   ? -2.978  2.363   15.394  1.00 12.28 ? 305 3TV A C6  1 
HETATM 2145 F  F17 . 3TV F 6 .   ? -2.221  1.400   15.890  1.00 12.35 ? 305 3TV A F17 1 
HETATM 2146 C  C8  . 3TV F 6 .   ? -3.113  4.491   14.279  1.00 13.40 ? 305 3TV A C8  1 
HETATM 2147 S  S11 . 3TV F 6 .   ? -2.179  5.837   13.584  1.00 17.33 ? 305 3TV A S11 1 
HETATM 2148 C  C12 . 3TV F 6 .   ? -3.147  7.337   13.411  1.00 25.59 ? 305 3TV A C12 1 
HETATM 2149 C  C13 . 3TV F 6 .   ? -3.040  7.717   14.863  1.00 26.18 ? 305 3TV A C13 1 
HETATM 2150 C  C14 . 3TV F 6 .   ? -1.736  8.533   14.842  1.00 35.14 ? 305 3TV A C14 1 
HETATM 2151 C  C9  . 3TV F 6 .   ? -4.475  4.416   14.386  1.00 13.04 ? 305 3TV A C9  1 
HETATM 2152 F  F15 . 3TV F 6 .   ? -5.254  5.374   13.902  1.00 19.53 ? 305 3TV A F15 1 
HETATM 2153 C  C10 . 3TV F 6 .   ? -5.068  3.362   15.048  1.00 14.30 ? 305 3TV A C10 1 
HETATM 2154 F  F16 . 3TV F 6 .   ? -6.381  3.373   15.041  1.00 17.21 ? 305 3TV A F16 1 
HETATM 2155 C  C5  . 3TV F 6 .   ? -4.356  2.286   15.511  1.00 11.20 ? 305 3TV A C5  1 
HETATM 2156 S  S1  . 3TV F 6 .   ? -5.102  0.884   16.414  1.00 10.36 ? 305 3TV A S1  1 
HETATM 2157 O  O3  . 3TV F 6 .   ? -6.509  1.004   16.241  1.00 10.84 ? 305 3TV A O3  1 
HETATM 2158 O  O4  . 3TV F 6 .   ? -4.574  1.011   17.733  1.00 10.11 ? 305 3TV A O4  1 
HETATM 2159 N  N2  . 3TV F 6 .   ? -4.559  -0.446  15.643  1.00 9.13  ? 305 3TV A N2  1 
HETATM 2160 F  F18 . 3TV G 6 .   ? 13.605  -0.138  9.027   1.00 37.44 ? 306 3TV A F18 1 
HETATM 2161 C  C7  . 3TV G 6 .   ? 13.456  -0.870  10.094  1.00 31.03 ? 306 3TV A C7  1 
HETATM 2162 C  C6  . 3TV G 6 .   ? 12.605  -0.475  11.145  1.00 30.49 ? 306 3TV A C6  1 
HETATM 2163 F  F17 . 3TV G 6 .   ? 11.918  0.686   10.997  1.00 31.21 ? 306 3TV A F17 1 
HETATM 2164 C  C8  . 3TV G 6 .   ? 14.222  -1.986  10.209  1.00 26.24 ? 306 3TV A C8  1 
HETATM 2165 S  S11 . 3TV G 6 .   ? 15.321  -2.414  8.894   1.00 34.38 ? 306 3TV A S11 1 
HETATM 2166 C  C12 . 3TV G 6 .   ? 14.758  -4.148  8.425   1.00 37.88 ? 306 3TV A C12 1 
HETATM 2167 C  C13 . 3TV G 6 .   ? 15.770  -5.133  7.772   1.00 40.70 ? 306 3TV A C13 1 
HETATM 2168 C  C14 . 3TV G 6 .   ? 15.223  -6.137  6.781   1.00 47.77 ? 306 3TV A C14 1 
HETATM 2169 C  C9  . 3TV G 6 .   ? 14.130  -2.771  11.301  1.00 31.90 ? 306 3TV A C9  1 
HETATM 2170 F  F15 . 3TV G 6 .   ? 14.879  -3.852  11.482  1.00 35.86 ? 306 3TV A F15 1 
HETATM 2171 C  C10 . 3TV G 6 .   ? 13.305  -2.475  12.325  1.00 27.48 ? 306 3TV A C10 1 
HETATM 2172 F  F16 . 3TV G 6 .   ? 13.375  -3.395  13.309  1.00 28.88 ? 306 3TV A F16 1 
HETATM 2173 C  C5  . 3TV G 6 .   ? 12.512  -1.301  12.304  1.00 26.67 ? 306 3TV A C5  1 
HETATM 2174 S  S1  . 3TV G 6 .   ? 11.301  -0.953  13.643  1.00 28.02 ? 306 3TV A S1  1 
HETATM 2175 O  O3  . 3TV G 6 .   ? 10.611  -2.299  13.662  1.00 25.58 ? 306 3TV A O3  1 
HETATM 2176 O  O4  . 3TV G 6 .   ? 10.535  0.317   13.469  1.00 31.70 ? 306 3TV A O4  1 
HETATM 2177 N  N2  . 3TV G 6 .   ? 12.078  -0.631  15.240  1.00 25.00 ? 306 3TV A N2  1 
HETATM 2178 O  O   . HOH H 7 .   ? -19.179 11.871  12.982  1.00 24.71 ? 401 HOH A O   1 
HETATM 2179 O  O   . HOH H 7 .   ? -19.580 17.764  4.047   1.00 23.02 ? 402 HOH A O   1 
HETATM 2180 O  O   . HOH H 7 .   ? -24.484 9.828   12.983  1.00 24.91 ? 403 HOH A O   1 
HETATM 2181 O  O   . HOH H 7 .   ? -17.272 19.005  5.711   1.00 12.17 ? 404 HOH A O   1 
HETATM 2182 O  O   . HOH H 7 .   ? 7.634   2.334   31.414  1.00 46.11 ? 405 HOH A O   1 
HETATM 2183 O  O   . HOH H 7 .   ? -0.646  -12.333 -3.650  1.00 29.34 ? 406 HOH A O   1 
HETATM 2184 O  O   . HOH H 7 .   ? -28.206 11.589  5.445   1.00 14.10 ? 407 HOH A O   1 
HETATM 2185 O  O   . HOH H 7 .   ? 10.117  -7.497  -7.988  1.00 27.98 ? 408 HOH A O   1 
HETATM 2186 O  O   . HOH H 7 .   ? -13.760 -16.367 28.602  1.00 36.92 ? 409 HOH A O   1 
HETATM 2187 O  O   . HOH H 7 .   ? 2.080   -9.060  -5.317  1.00 33.79 ? 410 HOH A O   1 
HETATM 2188 O  O   . HOH H 7 .   ? -9.856  1.023   33.676  1.00 34.85 ? 411 HOH A O   1 
HETATM 2189 O  O   . HOH H 7 .   ? -25.854 13.821  6.664   1.00 18.49 ? 412 HOH A O   1 
HETATM 2190 O  O   . HOH H 7 .   ? 15.539  0.420   14.890  1.00 32.05 ? 413 HOH A O   1 
HETATM 2191 O  O   . HOH H 7 .   ? -11.903 12.779  31.338  1.00 36.38 ? 414 HOH A O   1 
HETATM 2192 O  O   . HOH H 7 .   ? -2.362  17.587  20.192  1.00 26.01 ? 415 HOH A O   1 
HETATM 2193 O  O   . HOH H 7 .   ? -6.898  7.085   27.096  1.00 28.77 ? 416 HOH A O   1 
HETATM 2194 O  O   . HOH H 7 .   ? -21.385 -18.250 13.381  1.00 23.86 ? 417 HOH A O   1 
HETATM 2195 O  O   . HOH H 7 .   ? 2.745   7.771   27.326  1.00 25.16 ? 418 HOH A O   1 
HETATM 2196 O  O   . HOH H 7 .   ? -14.844 -10.255 37.103  1.00 23.13 ? 419 HOH A O   1 
HETATM 2197 O  O   . HOH H 7 .   ? -13.747 -5.272  -6.910  1.00 28.25 ? 420 HOH A O   1 
HETATM 2198 O  O   . HOH H 7 .   ? -1.672  1.411   12.230  1.00 22.03 ? 421 HOH A O   1 
HETATM 2199 O  O   . HOH H 7 .   ? -0.513  -4.242  15.470  1.00 12.89 ? 422 HOH A O   1 
HETATM 2200 O  O   . HOH H 7 .   ? -9.742  -18.211 16.595  1.00 22.26 ? 423 HOH A O   1 
HETATM 2201 O  O   . HOH H 7 .   ? -19.740 -16.589 2.994   1.00 25.92 ? 424 HOH A O   1 
HETATM 2202 O  O   . HOH H 7 .   ? -23.378 8.763   20.090  1.00 22.23 ? 425 HOH A O   1 
HETATM 2203 O  O   . HOH H 7 .   ? -16.006 -14.523 32.807  1.00 36.24 ? 426 HOH A O   1 
HETATM 2204 O  O   . HOH H 7 .   ? -19.061 -4.124  40.956  1.00 36.63 ? 427 HOH A O   1 
HETATM 2205 O  O   . HOH H 7 .   ? -20.451 -6.448  -2.527  1.00 24.45 ? 428 HOH A O   1 
HETATM 2206 O  O   . HOH H 7 .   ? -18.571 10.062  8.614   1.00 13.45 ? 429 HOH A O   1 
HETATM 2207 O  O   . HOH H 7 .   ? -19.429 10.814  26.694  1.00 22.05 ? 430 HOH A O   1 
HETATM 2208 O  O   . HOH H 7 .   ? -5.993  20.435  18.924  1.00 20.60 ? 431 HOH A O   1 
HETATM 2209 O  O   . HOH H 7 .   ? -13.951 -18.353 18.437  1.00 27.53 ? 432 HOH A O   1 
HETATM 2210 O  O   . HOH H 7 .   ? 5.022   -3.603  26.151  1.00 22.27 ? 433 HOH A O   1 
HETATM 2211 O  O   . HOH H 7 .   ? -4.155  -12.010 31.624  1.00 23.94 ? 434 HOH A O   1 
HETATM 2212 O  O   . HOH H 7 .   ? 12.128  -6.981  22.163  1.00 30.33 ? 435 HOH A O   1 
HETATM 2213 O  O   . HOH H 7 .   ? -9.692  8.590   25.228  1.00 14.20 ? 436 HOH A O   1 
HETATM 2214 O  O   . HOH H 7 .   ? 4.140   4.839   29.746  1.00 22.25 ? 437 HOH A O   1 
HETATM 2215 O  O   . HOH H 7 .   ? -0.356  -15.179 -5.613  1.00 33.61 ? 438 HOH A O   1 
HETATM 2216 O  O   . HOH H 7 .   ? -19.667 8.518   29.938  1.00 31.79 ? 439 HOH A O   1 
HETATM 2217 O  O   . HOH H 7 .   ? -4.864  2.408   11.464  1.00 17.51 ? 440 HOH A O   1 
HETATM 2218 O  O   . HOH H 7 .   ? 4.990   -2.540  28.561  1.00 36.27 ? 441 HOH A O   1 
HETATM 2219 O  O   . HOH H 7 .   ? 4.043   -9.083  25.750  1.00 41.96 ? 442 HOH A O   1 
HETATM 2220 O  O   . HOH H 7 .   ? -14.699 19.129  12.891  1.00 23.67 ? 443 HOH A O   1 
HETATM 2221 O  O   . HOH H 7 .   ? 13.944  6.268   15.357  1.00 50.00 ? 444 HOH A O   1 
HETATM 2222 O  O   . HOH H 7 .   ? -22.337 -5.703  2.592   1.00 17.54 ? 445 HOH A O   1 
HETATM 2223 O  O   . HOH H 7 .   ? -3.665  5.366   -3.363  1.00 25.34 ? 446 HOH A O   1 
HETATM 2224 O  O   . HOH H 7 .   ? 6.423   -0.724  -0.840  1.00 43.12 ? 447 HOH A O   1 
HETATM 2225 O  O   . HOH H 7 .   ? 16.332  3.594   15.256  1.00 22.50 ? 448 HOH A O   1 
HETATM 2226 O  O   . HOH H 7 .   ? -23.376 -2.901  28.809  1.00 38.85 ? 449 HOH A O   1 
HETATM 2227 O  O   . HOH H 7 .   ? -17.369 10.681  11.137  1.00 15.46 ? 450 HOH A O   1 
HETATM 2228 O  O   . HOH H 7 .   ? -7.404  -15.336 10.921  1.00 15.31 ? 451 HOH A O   1 
HETATM 2229 O  O   . HOH H 7 .   ? -15.501 -10.306 -4.760  1.00 23.03 ? 452 HOH A O   1 
HETATM 2230 O  O   . HOH H 7 .   ? 2.972   -15.849 -6.741  1.00 22.00 ? 453 HOH A O   1 
HETATM 2231 O  O   . HOH H 7 .   ? -8.410  5.628   28.762  1.00 32.22 ? 454 HOH A O   1 
HETATM 2232 O  O   . HOH H 7 .   ? 1.205   4.414   11.971  1.00 24.50 ? 455 HOH A O   1 
HETATM 2233 O  O   . HOH H 7 .   ? -24.264 4.656   8.467   1.00 30.17 ? 456 HOH A O   1 
HETATM 2234 O  O   . HOH H 7 .   ? -12.962 10.415  27.606  1.00 23.01 ? 457 HOH A O   1 
HETATM 2235 O  O   . HOH H 7 .   ? -3.326  -12.853 -3.191  1.00 23.10 ? 458 HOH A O   1 
HETATM 2236 O  O   . HOH H 7 .   ? 3.311   -12.972 5.001   1.00 18.64 ? 459 HOH A O   1 
HETATM 2237 O  O   . HOH H 7 .   ? -18.930 -20.597 4.634   1.00 18.60 ? 460 HOH A O   1 
HETATM 2238 O  O   . HOH H 7 .   ? -3.701  -8.717  30.853  1.00 25.16 ? 461 HOH A O   1 
HETATM 2239 O  O   . HOH H 7 .   ? -3.938  -13.473 17.622  1.00 13.07 ? 462 HOH A O   1 
HETATM 2240 O  O   . HOH H 7 .   ? -6.444  -14.975 31.124  1.00 26.82 ? 463 HOH A O   1 
HETATM 2241 O  O   . HOH H 7 .   ? 11.108  -10.863 15.769  1.00 23.63 ? 464 HOH A O   1 
HETATM 2242 O  O   . HOH H 7 .   ? -2.873  -11.223 20.512  1.00 14.31 ? 465 HOH A O   1 
HETATM 2243 O  O   . HOH H 7 .   ? -1.893  -8.827  28.792  1.00 16.87 ? 466 HOH A O   1 
HETATM 2244 O  O   . HOH H 7 .   ? -5.436  -4.654  -6.694  1.00 17.90 ? 467 HOH A O   1 
HETATM 2245 O  O   . HOH H 7 .   ? -3.243  -15.932 23.999  1.00 17.38 ? 468 HOH A O   1 
HETATM 2246 O  O   . HOH H 7 .   ? 2.584   -15.532 9.127   1.00 22.03 ? 469 HOH A O   1 
HETATM 2247 O  O   . HOH H 7 .   ? -7.992  6.618   0.216   1.00 27.58 ? 470 HOH A O   1 
HETATM 2248 O  O   . HOH H 7 .   ? -5.022  6.855   6.405   1.00 34.48 ? 471 HOH A O   1 
HETATM 2249 O  O   . HOH H 7 .   ? 1.116   -1.221  -5.024  1.00 24.37 ? 472 HOH A O   1 
HETATM 2250 O  O   . HOH H 7 .   ? 0.506   1.017   34.218  1.00 31.35 ? 473 HOH A O   1 
HETATM 2251 O  O   . HOH H 7 .   ? -21.242 -13.932 18.618  1.00 38.53 ? 474 HOH A O   1 
HETATM 2252 O  O   . HOH H 7 .   ? -11.446 12.347  28.764  1.00 24.21 ? 475 HOH A O   1 
HETATM 2253 O  O   . HOH H 7 .   ? -7.946  0.538   -6.742  1.00 25.68 ? 476 HOH A O   1 
HETATM 2254 O  O   . HOH H 7 .   ? 2.554   10.849  17.006  1.00 33.74 ? 477 HOH A O   1 
HETATM 2255 O  O   . HOH H 7 .   ? -0.915  -4.885  -7.300  1.00 30.29 ? 478 HOH A O   1 
HETATM 2256 O  O   . HOH H 7 .   ? -11.402 2.916   30.314  1.00 24.48 ? 479 HOH A O   1 
HETATM 2257 O  O   . HOH H 7 .   ? -0.713  -17.942 17.793  1.00 43.06 ? 480 HOH A O   1 
HETATM 2258 O  O   . HOH H 7 .   ? -26.905 2.734   23.233  1.00 30.87 ? 481 HOH A O   1 
HETATM 2259 O  O   . HOH H 7 .   ? -12.376 -8.879  -3.435  1.00 17.17 ? 482 HOH A O   1 
HETATM 2260 O  O   . HOH H 7 .   ? 13.977  0.326   24.252  1.00 18.84 ? 483 HOH A O   1 
HETATM 2261 O  O   . HOH H 7 .   ? 3.515   -4.379  7.406   1.00 28.72 ? 484 HOH A O   1 
HETATM 2262 O  O   . HOH H 7 .   ? 8.313   -7.867  -0.005  1.00 29.79 ? 485 HOH A O   1 
HETATM 2263 O  O   . HOH H 7 .   ? -1.882  -3.503  11.255  1.00 17.06 ? 486 HOH A O   1 
HETATM 2264 O  O   . HOH H 7 .   ? -21.203 5.724   4.632   1.00 13.49 ? 487 HOH A O   1 
HETATM 2265 O  O   . HOH H 7 .   ? -22.605 -11.288 16.734  1.00 31.57 ? 488 HOH A O   1 
HETATM 2266 O  O   . HOH H 7 .   ? -14.287 11.022  34.345  1.00 32.92 ? 489 HOH A O   1 
HETATM 2267 O  O   . HOH H 7 .   ? 4.423   -3.451  4.183   1.00 34.55 ? 490 HOH A O   1 
HETATM 2268 O  O   . HOH H 7 .   ? -16.322 -8.274  20.034  1.00 11.48 ? 491 HOH A O   1 
HETATM 2269 O  O   . HOH H 7 .   ? 5.727   7.123   20.301  1.00 21.48 ? 492 HOH A O   1 
HETATM 2270 O  O   . HOH H 7 .   ? -15.275 15.870  23.453  1.00 21.63 ? 493 HOH A O   1 
HETATM 2271 O  O   . HOH H 7 .   ? -18.839 -12.143 -3.512  1.00 17.73 ? 494 HOH A O   1 
HETATM 2272 O  O   . HOH H 7 .   ? -15.481 -12.344 24.167  1.00 22.62 ? 495 HOH A O   1 
HETATM 2273 O  O   . HOH H 7 .   ? -22.549 -2.779  6.367   1.00 16.54 ? 496 HOH A O   1 
HETATM 2274 O  O   . HOH H 7 .   ? 9.234   -3.814  20.844  1.00 15.70 ? 497 HOH A O   1 
HETATM 2275 O  O   . HOH H 7 .   ? -4.071  -15.807 0.489   1.00 31.34 ? 498 HOH A O   1 
HETATM 2276 O  O   . HOH H 7 .   ? -2.825  -13.326 24.788  1.00 14.49 ? 499 HOH A O   1 
HETATM 2277 O  O   . HOH H 7 .   ? -12.479 -16.721 26.203  1.00 25.65 ? 500 HOH A O   1 
HETATM 2278 O  O   . HOH H 7 .   ? -25.209 7.952   6.318   1.00 33.35 ? 501 HOH A O   1 
HETATM 2279 O  O   . HOH H 7 .   ? -17.335 -20.269 7.651   1.00 13.22 ? 502 HOH A O   1 
HETATM 2280 O  O   . HOH H 7 .   ? -12.913 14.110  27.065  1.00 25.86 ? 503 HOH A O   1 
HETATM 2281 O  O   . HOH H 7 .   ? -18.496 -4.167  -2.848  1.00 20.30 ? 504 HOH A O   1 
HETATM 2282 O  O   . HOH H 7 .   ? -25.989 3.427   20.737  1.00 29.41 ? 505 HOH A O   1 
HETATM 2283 O  O   . HOH H 7 .   ? 16.059  -2.164  14.236  1.00 18.46 ? 506 HOH A O   1 
HETATM 2284 O  O   . HOH H 7 .   ? -15.183 9.053   -2.345  1.00 29.47 ? 507 HOH A O   1 
HETATM 2285 O  O   . HOH H 7 .   ? -10.866 10.038  7.830   1.00 17.43 ? 508 HOH A O   1 
HETATM 2286 O  O   . HOH H 7 .   ? -7.769  -22.121 10.312  1.00 26.40 ? 509 HOH A O   1 
HETATM 2287 O  O   . HOH H 7 .   ? -13.903 -20.943 2.549   1.00 41.03 ? 510 HOH A O   1 
HETATM 2288 O  O   . HOH H 7 .   ? -6.031  6.916   10.746  1.00 21.57 ? 511 HOH A O   1 
HETATM 2289 O  O   . HOH H 7 .   ? -4.939  17.312  26.689  1.00 38.13 ? 512 HOH A O   1 
HETATM 2290 O  O   . HOH H 7 .   ? -25.244 6.329   26.742  1.00 29.85 ? 513 HOH A O   1 
HETATM 2291 O  O   . HOH H 7 .   ? -20.571 7.829   1.736   1.00 12.98 ? 514 HOH A O   1 
HETATM 2292 O  O   . HOH H 7 .   ? -20.914 -7.012  23.130  1.00 13.82 ? 515 HOH A O   1 
HETATM 2293 O  O   . HOH H 7 .   ? -5.995  -5.584  36.883  1.00 27.86 ? 516 HOH A O   1 
HETATM 2294 O  O   . HOH H 7 .   ? 5.586   -4.993  20.770  1.00 16.18 ? 517 HOH A O   1 
HETATM 2295 O  O   . HOH H 7 .   ? -17.165 17.553  4.002   1.00 28.67 ? 518 HOH A O   1 
HETATM 2296 O  O   . HOH H 7 .   ? 9.893   2.332   11.625  1.00 31.39 ? 519 HOH A O   1 
HETATM 2297 O  O   . HOH H 7 .   ? -5.474  -19.575 23.364  1.00 28.90 ? 520 HOH A O   1 
HETATM 2298 O  O   . HOH H 7 .   ? 1.973   -11.913 24.668  1.00 24.20 ? 521 HOH A O   1 
HETATM 2299 O  O   . HOH H 7 .   ? -8.971  -8.078  33.681  1.00 29.64 ? 522 HOH A O   1 
HETATM 2300 O  O   . HOH H 7 .   ? -24.336 11.960  6.145   1.00 17.25 ? 523 HOH A O   1 
HETATM 2301 O  O   . HOH H 7 .   ? -17.811 19.882  14.547  1.00 31.59 ? 524 HOH A O   1 
HETATM 2302 O  O   . HOH H 7 .   ? 11.842  1.404   25.813  1.00 21.73 ? 525 HOH A O   1 
HETATM 2303 O  O   . HOH H 7 .   ? -12.781 -0.724  -5.962  1.00 24.07 ? 526 HOH A O   1 
HETATM 2304 O  O   . HOH H 7 .   ? -13.208 -15.871 -0.683  1.00 26.95 ? 527 HOH A O   1 
HETATM 2305 O  O   . HOH H 7 .   ? -16.759 -16.301 21.543  1.00 34.89 ? 528 HOH A O   1 
HETATM 2306 O  O   . HOH H 7 .   ? 4.594   -0.216  -6.056  1.00 27.44 ? 529 HOH A O   1 
HETATM 2307 O  O   . HOH H 7 .   ? -24.274 -7.496  8.956   1.00 17.08 ? 530 HOH A O   1 
HETATM 2308 O  O   . HOH H 7 .   ? -6.767  -8.723  32.264  1.00 23.52 ? 531 HOH A O   1 
HETATM 2309 O  O   . HOH H 7 .   ? -16.517 -7.243  39.280  1.00 30.95 ? 532 HOH A O   1 
HETATM 2310 O  O   . HOH H 7 .   ? 5.463   -7.734  21.991  1.00 33.12 ? 533 HOH A O   1 
HETATM 2311 O  O   . HOH H 7 .   ? -16.453 19.224  21.293  1.00 40.56 ? 534 HOH A O   1 
HETATM 2312 O  O   . HOH H 7 .   ? -13.116 19.875  14.801  1.00 32.54 ? 535 HOH A O   1 
HETATM 2313 O  O   . HOH H 7 .   ? 8.782   -9.282  16.116  1.00 25.54 ? 536 HOH A O   1 
HETATM 2314 O  O   . HOH H 7 .   ? -22.759 -13.202 11.247  1.00 27.32 ? 537 HOH A O   1 
HETATM 2315 O  O   . HOH H 7 .   ? -25.373 -14.893 8.155   1.00 38.53 ? 538 HOH A O   1 
HETATM 2316 O  O   . HOH H 7 .   ? 5.117   -6.876  7.659   1.00 28.62 ? 539 HOH A O   1 
HETATM 2317 O  O   . HOH H 7 .   ? -23.123 -0.775  3.716   1.00 21.52 ? 540 HOH A O   1 
HETATM 2318 O  O   . HOH H 7 .   ? -0.987  -13.289 26.801  1.00 25.52 ? 541 HOH A O   1 
HETATM 2319 O  O   . HOH H 7 .   ? -6.713  -16.597 0.953   1.00 27.03 ? 542 HOH A O   1 
HETATM 2320 O  O   . HOH H 7 .   ? 2.293   8.404   23.999  1.00 27.22 ? 543 HOH A O   1 
HETATM 2321 O  O   . HOH H 7 .   ? -23.251 -0.612  26.240  1.00 20.37 ? 544 HOH A O   1 
HETATM 2322 O  O   . HOH H 7 .   ? 13.645  -5.811  24.236  1.00 29.27 ? 545 HOH A O   1 
HETATM 2323 O  O   . HOH H 7 .   ? -17.985 -9.064  34.135  1.00 24.53 ? 546 HOH A O   1 
HETATM 2324 O  O   . HOH H 7 .   ? -12.721 -18.345 14.393  1.00 23.02 ? 547 HOH A O   1 
HETATM 2325 O  O   . HOH H 7 .   ? -13.218 14.922  5.017   1.00 40.73 ? 548 HOH A O   1 
HETATM 2326 O  O   . HOH H 7 .   ? -25.939 -3.931  25.054  1.00 20.85 ? 549 HOH A O   1 
HETATM 2327 O  O   . HOH H 7 .   ? -10.680 -19.207 6.703   1.00 44.19 ? 550 HOH A O   1 
HETATM 2328 O  O   . HOH H 7 .   ? -8.458  -5.889  35.560  1.00 24.50 ? 551 HOH A O   1 
HETATM 2329 O  O   . HOH H 7 .   ? -6.340  -8.555  -7.482  1.00 28.76 ? 552 HOH A O   1 
HETATM 2330 O  O   . HOH H 7 .   ? -3.095  -4.708  37.194  1.00 38.19 ? 553 HOH A O   1 
HETATM 2331 O  O   . HOH H 7 .   ? -15.821 -9.885  32.484  1.00 21.73 ? 554 HOH A O   1 
HETATM 2332 O  O   . HOH H 7 .   ? -17.892 4.227   -3.891  1.00 32.57 ? 555 HOH A O   1 
HETATM 2333 O  O   . HOH H 7 .   ? -22.564 -0.637  33.993  1.00 31.85 ? 556 HOH A O   1 
HETATM 2334 O  O   . HOH H 7 .   ? 3.235   -11.477 9.412   1.00 24.47 ? 557 HOH A O   1 
HETATM 2335 O  O   . HOH H 7 .   ? 1.188   -16.229 -2.008  1.00 42.77 ? 558 HOH A O   1 
HETATM 2336 O  O   . HOH H 7 .   ? -7.408  -19.248 21.233  1.00 22.55 ? 559 HOH A O   1 
HETATM 2337 O  O   . HOH H 7 .   ? -1.461  -12.348 22.528  1.00 14.07 ? 560 HOH A O   1 
HETATM 2338 O  O   . HOH H 7 .   ? 6.501   -9.999  -6.861  1.00 37.50 ? 561 HOH A O   1 
HETATM 2339 O  O   . HOH H 7 .   ? 1.928   -1.766  29.134  1.00 17.72 ? 562 HOH A O   1 
HETATM 2340 O  O   . HOH H 7 .   ? 3.742   4.232   10.316  1.00 46.49 ? 563 HOH A O   1 
HETATM 2341 O  O   . HOH H 7 .   ? -22.345 -11.401 13.760  1.00 20.28 ? 564 HOH A O   1 
HETATM 2342 O  O   . HOH H 7 .   ? 0.107   10.490  22.727  1.00 27.13 ? 565 HOH A O   1 
HETATM 2343 O  O   . HOH H 7 .   ? -23.979 5.380   6.311   1.00 41.31 ? 566 HOH A O   1 
HETATM 2344 O  O   . HOH H 7 .   ? -4.807  2.988   -6.250  1.00 23.26 ? 567 HOH A O   1 
HETATM 2345 O  O   . HOH H 7 .   ? 10.944  -9.029  8.644   1.00 31.06 ? 568 HOH A O   1 
HETATM 2346 O  O   . HOH H 7 .   ? -0.111  -8.727  32.165  1.00 27.18 ? 569 HOH A O   1 
HETATM 2347 O  O   . HOH H 7 .   ? -4.695  0.646   9.248   1.00 22.56 ? 570 HOH A O   1 
HETATM 2348 O  O   . HOH H 7 .   ? -23.774 -17.523 6.438   1.00 29.53 ? 571 HOH A O   1 
HETATM 2349 O  O   . HOH H 7 .   ? 3.597   -14.550 0.805   1.00 36.68 ? 572 HOH A O   1 
HETATM 2350 O  O   . HOH H 7 .   ? -21.155 19.398  12.201  1.00 32.31 ? 573 HOH A O   1 
HETATM 2351 O  O   . HOH H 7 .   ? -12.196 4.076   -7.186  1.00 33.23 ? 574 HOH A O   1 
HETATM 2352 O  O   . HOH H 7 .   ? -3.704  0.294   12.866  1.00 18.89 ? 575 HOH A O   1 
HETATM 2353 O  O   . HOH H 7 .   ? -0.323  2.854   -5.475  1.00 32.12 ? 576 HOH A O   1 
HETATM 2354 O  O   . HOH H 7 .   ? -2.443  -17.502 5.137   1.00 27.49 ? 577 HOH A O   1 
HETATM 2355 O  O   . HOH H 7 .   ? 8.857   3.325   27.649  1.00 37.93 ? 578 HOH A O   1 
HETATM 2356 O  O   . HOH H 7 .   ? -24.458 -9.157  1.909   1.00 22.41 ? 579 HOH A O   1 
HETATM 2357 O  O   . HOH H 7 .   ? 4.136   -12.696 11.627  1.00 42.28 ? 580 HOH A O   1 
HETATM 2358 O  O   . HOH H 7 .   ? -14.506 19.961  17.358  1.00 35.01 ? 581 HOH A O   1 
HETATM 2359 O  O   . HOH H 7 .   ? -20.708 -19.420 6.327   1.00 20.39 ? 582 HOH A O   1 
HETATM 2360 O  O   . HOH H 7 .   ? -9.173  14.396  11.473  1.00 32.66 ? 583 HOH A O   1 
HETATM 2361 O  O   . HOH H 7 .   ? 8.095   6.135   21.530  1.00 17.35 ? 584 HOH A O   1 
HETATM 2362 O  O   . HOH H 7 .   ? -6.391  -19.515 4.588   1.00 33.08 ? 585 HOH A O   1 
HETATM 2363 O  O   . HOH H 7 .   ? -6.150  1.452   35.030  1.00 34.86 ? 586 HOH A O   1 
HETATM 2364 O  O   . HOH H 7 .   ? -8.060  8.192   9.293   1.00 29.79 ? 587 HOH A O   1 
HETATM 2365 O  O   . HOH H 7 .   ? -19.844 -1.966  -3.868  1.00 30.41 ? 588 HOH A O   1 
HETATM 2366 O  O   . HOH H 7 .   ? -18.783 17.507  23.204  1.00 39.30 ? 589 HOH A O   1 
HETATM 2367 O  O   . HOH H 7 .   ? 0.339   -14.321 21.835  1.00 29.23 ? 590 HOH A O   1 
HETATM 2368 O  O   . HOH H 7 .   ? -12.286 18.425  11.929  1.00 34.24 ? 591 HOH A O   1 
HETATM 2369 O  O   . HOH H 7 .   ? -5.223  9.804   14.223  1.00 37.86 ? 592 HOH A O   1 
HETATM 2370 O  O   . HOH H 7 .   ? 0.148   9.501   27.365  1.00 31.40 ? 593 HOH A O   1 
HETATM 2371 O  O   . HOH H 7 .   ? -4.081  7.835   10.207  1.00 36.73 ? 594 HOH A O   1 
HETATM 2372 O  O   . HOH H 7 .   ? 9.352   -4.757  23.400  1.00 27.25 ? 595 HOH A O   1 
HETATM 2373 O  O   . HOH H 7 .   ? 14.311  6.003   18.699  1.00 41.65 ? 596 HOH A O   1 
HETATM 2374 O  O   . HOH H 7 .   ? -24.505 11.233  19.389  1.00 38.28 ? 597 HOH A O   1 
HETATM 2375 O  O   . HOH H 7 .   ? 10.649  6.654   14.899  1.00 40.10 ? 598 HOH A O   1 
HETATM 2376 O  O   . HOH H 7 .   ? -0.612  11.199  25.191  1.00 38.90 ? 599 HOH A O   1 
HETATM 2377 O  O   . HOH H 7 .   ? 14.305  0.367   5.857   1.00 37.29 ? 600 HOH A O   1 
HETATM 2378 O  O   . HOH H 7 .   ? 6.931   -10.890 14.562  1.00 46.74 ? 601 HOH A O   1 
HETATM 2379 O  O   . HOH H 7 .   ? -31.105 5.342   12.448  1.00 37.95 ? 602 HOH A O   1 
HETATM 2380 O  O   . HOH H 7 .   ? -4.042  2.011   36.985  1.00 35.15 ? 603 HOH A O   1 
HETATM 2381 O  O   . HOH H 7 .   ? -1.498  8.341   6.898   1.00 36.46 ? 604 HOH A O   1 
HETATM 2382 O  O   . HOH H 7 .   ? -12.219 -17.141 16.496  1.00 20.99 ? 605 HOH A O   1 
HETATM 2383 O  O   . HOH H 7 .   ? -14.969 -11.826 39.595  1.00 32.53 ? 606 HOH A O   1 
HETATM 2384 O  O   . HOH H 7 .   ? -16.989 19.649  17.139  1.00 32.30 ? 607 HOH A O   1 
HETATM 2385 O  O   . HOH H 7 .   ? 5.211   -10.005 7.827   1.00 33.72 ? 608 HOH A O   1 
HETATM 2386 O  O   . HOH H 7 .   ? 7.093   -6.667  23.014  1.00 40.64 ? 609 HOH A O   1 
HETATM 2387 O  O   . HOH H 7 .   ? 1.205   -2.501  38.847  1.00 45.60 ? 610 HOH A O   1 
HETATM 2388 O  O   . HOH H 7 .   ? 16.718  -5.884  12.667  1.00 35.92 ? 611 HOH A O   1 
HETATM 2389 O  O   . HOH H 7 .   ? -16.339 -13.933 36.820  1.00 29.99 ? 612 HOH A O   1 
HETATM 2390 O  O   . HOH H 7 .   ? 5.617   -10.753 17.884  1.00 45.31 ? 613 HOH A O   1 
HETATM 2391 O  O   . HOH H 7 .   ? -1.562  -12.183 31.120  1.00 36.53 ? 614 HOH A O   1 
HETATM 2392 O  O   . HOH H 7 .   ? -4.537  9.266   7.950   1.00 40.35 ? 615 HOH A O   1 
HETATM 2393 O  O   . HOH H 7 .   ? -7.563  -21.419 8.073   1.00 34.57 ? 616 HOH A O   1 
HETATM 2394 O  O   . HOH H 7 .   ? -18.083 13.600  34.317  1.00 33.55 ? 617 HOH A O   1 
HETATM 2395 O  O   . HOH H 7 .   ? 1.490   7.299   11.893  1.00 35.77 ? 618 HOH A O   1 
HETATM 2396 O  O   . HOH H 7 .   ? -17.688 -4.955  -5.450  1.00 27.76 ? 619 HOH A O   1 
HETATM 2397 O  O   . HOH H 7 .   ? -23.421 -3.343  3.736   1.00 34.53 ? 620 HOH A O   1 
HETATM 2398 O  O   . HOH H 7 .   ? -1.323  -17.475 24.967  1.00 30.02 ? 621 HOH A O   1 
HETATM 2399 O  O   . HOH H 7 .   ? -14.682 20.708  22.089  1.00 44.65 ? 622 HOH A O   1 
HETATM 2400 O  O   . HOH H 7 .   ? -0.570  -11.261 28.675  1.00 24.77 ? 623 HOH A O   1 
HETATM 2401 O  O   . HOH H 7 .   ? -3.274  -1.437  11.024  1.00 20.89 ? 624 HOH A O   1 
HETATM 2402 O  O   . HOH H 7 .   ? 11.071  -8.908  0.109   1.00 47.41 ? 625 HOH A O   1 
HETATM 2403 O  O   . HOH H 7 .   ? -21.236 -18.107 3.779   1.00 32.83 ? 626 HOH A O   1 
HETATM 2404 O  O   . HOH H 7 .   ? -3.386  -5.866  -8.101  1.00 26.00 ? 627 HOH A O   1 
HETATM 2405 O  O   . HOH H 7 .   ? 4.628   8.531   22.558  1.00 36.70 ? 628 HOH A O   1 
HETATM 2406 O  O   . HOH H 7 .   ? -24.493 8.796   25.862  1.00 40.32 ? 629 HOH A O   1 
HETATM 2407 O  O   . HOH H 7 .   ? -26.415 -10.365 14.359  1.00 26.81 ? 630 HOH A O   1 
HETATM 2408 O  O   . HOH H 7 .   ? 4.632   -11.792 23.420  1.00 37.58 ? 631 HOH A O   1 
HETATM 2409 O  O   . HOH H 7 .   ? 2.088   -17.568 7.303   1.00 28.95 ? 632 HOH A O   1 
HETATM 2410 O  O   . HOH H 7 .   ? 6.987   -8.253  -9.783  1.00 42.61 ? 633 HOH A O   1 
HETATM 2411 O  O   . HOH H 7 .   ? -14.081 -2.718  -7.092  1.00 33.32 ? 634 HOH A O   1 
HETATM 2412 O  O   . HOH H 7 .   ? 15.830  -1.199  25.744  1.00 23.81 ? 635 HOH A O   1 
HETATM 2413 O  O   . HOH H 7 .   ? 0.843   -7.233  -7.458  1.00 39.46 ? 636 HOH A O   1 
HETATM 2414 O  O   . HOH H 7 .   ? -23.744 -6.911  0.211   1.00 32.92 ? 637 HOH A O   1 
HETATM 2415 O  O   . HOH H 7 .   ? -17.253 -12.175 31.095  1.00 34.90 ? 638 HOH A O   1 
HETATM 2416 O  O   . HOH H 7 .   ? -8.744  5.159   31.929  1.00 34.75 ? 639 HOH A O   1 
HETATM 2417 O  O   . HOH H 7 .   ? -23.270 14.002  20.001  1.00 46.94 ? 640 HOH A O   1 
HETATM 2418 O  O   . HOH H 7 .   ? -16.324 -17.984 20.006  1.00 35.20 ? 641 HOH A O   1 
HETATM 2419 O  O   . HOH H 7 .   ? 2.693   -14.281 20.435  1.00 33.99 ? 642 HOH A O   1 
HETATM 2420 O  O   . HOH H 7 .   ? 6.833   5.303   29.298  1.00 40.13 ? 643 HOH A O   1 
HETATM 2421 O  O   . HOH H 7 .   ? -15.329 17.348  25.812  1.00 43.91 ? 644 HOH A O   1 
HETATM 2422 O  O   . HOH H 7 .   ? -3.530  -15.443 -2.250  1.00 30.53 ? 645 HOH A O   1 
HETATM 2423 O  O   . HOH H 7 .   ? -2.992  -18.136 2.684   1.00 32.60 ? 646 HOH A O   1 
HETATM 2424 O  O   . HOH H 7 .   ? -1.888  -17.427 -5.270  1.00 38.95 ? 647 HOH A O   1 
HETATM 2425 O  O   . HOH H 7 .   ? -9.254  1.554   38.246  1.00 43.98 ? 648 HOH A O   1 
HETATM 2426 O  O   . HOH H 7 .   ? -2.422  -19.839 26.358  1.00 40.64 ? 649 HOH A O   1 
HETATM 2427 O  O   . HOH H 7 .   ? -27.124 -1.254  28.173  1.00 36.65 ? 650 HOH A O   1 
HETATM 2428 O  O   . HOH H 7 .   ? -4.151  1.007   42.473  1.00 34.73 ? 651 HOH A O   1 
HETATM 2429 O  O   . HOH H 7 .   ? 14.686  5.016   24.870  1.00 34.13 ? 652 HOH A O   1 
HETATM 2430 O  O   . HOH H 7 .   ? -3.397  6.819   -7.680  1.00 28.10 ? 653 HOH A O   1 
HETATM 2431 O  O   . HOH H 7 .   ? 2.069   -4.628  -12.298 1.00 36.85 ? 654 HOH A O   1 
HETATM 2432 O  O   . HOH H 7 .   ? -0.750  0.876   -10.568 1.00 46.62 ? 655 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   ? 0.3097 0.3700 0.6351 -0.0849 0.1184  0.0599  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.3316 0.5465 0.4526 -0.0425 0.1231  0.1784  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.3309 0.3913 0.2201 -0.0095 0.0952  0.0148  4   HIS A C   
4    O  O   . HIS A 4   ? 0.3194 0.4038 0.3216 -0.0285 0.0611  0.0508  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.3078 0.3564 0.5528 0.1018  0.1588  0.2226  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.4835 0.4505 0.4771 0.0162  -0.0827 -0.0753 4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.1323 0.2484 0.1527 0.0108  0.0592  0.0599  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.4881 0.3628 0.6666 -0.0115 -0.1162 0.1786  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.4200 0.3718 0.5687 0.1471  0.0592  -0.0003 4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.5527 0.5146 0.7763 -0.0454 -0.1220 0.0884  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.2105 0.2945 0.2244 -0.0287 0.0456  0.0421  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.1605 0.3025 0.2199 -0.0559 0.0205  0.0370  5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1842 0.2805 0.1987 -0.0265 0.0063  0.0141  5   TRP A C   
14   O  O   . TRP A 5   ? 0.2015 0.3538 0.2027 -0.0111 0.0171  0.0324  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1535 0.2627 0.2587 -0.0444 0.0121  0.0230  5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1659 0.2265 0.2416 -0.0447 -0.0006 0.0081  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2439 0.2509 0.2208 -0.0288 -0.0130 0.0688  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1436 0.2454 0.1980 -0.0171 0.0033  0.0287  5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2435 0.2423 0.1768 -0.0161 0.0183  0.0528  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.1928 0.2496 0.1508 -0.0179 -0.0245 0.0408  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1678 0.2737 0.1685 -0.0783 0.0212  -0.0154 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.1747 0.2619 0.1326 -0.0001 -0.0151 0.0034  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1632 0.2354 0.1313 -0.0220 0.0242  -0.0383 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1844 0.2658 0.1187 -0.0067 0.0046  -0.0254 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1424 0.2472 0.2172 -0.0071 0.0277  -0.0234 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1933 0.2332 0.2248 -0.0366 0.0367  -0.0203 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1453 0.2813 0.1646 -0.0026 -0.0065 -0.0166 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1412 0.2526 0.1659 -0.0061 0.0237  -0.0340 6   GLY A O   
29   N  N   . TYR A 7   ? 0.1444 0.2579 0.1747 0.0093  0.0486  -0.0312 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1284 0.2368 0.2165 0.0011  0.0342  -0.0370 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.1772 0.2691 0.3078 0.0296  0.0548  -0.0228 7   TYR A C   
32   O  O   . TYR A 7   ? 0.2131 0.2169 0.4440 0.0201  0.0608  -0.0116 7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1220 0.2266 0.2391 0.0013  0.0170  -0.0533 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1318 0.2064 0.1626 -0.0013 0.0232  -0.0207 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1002 0.2100 0.1615 -0.0049 0.0055  -0.0379 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1340 0.2142 0.1725 -0.0369 0.0103  -0.0229 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1217 0.1847 0.1845 -0.0189 -0.0148 -0.0401 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1370 0.2289 0.1414 -0.0337 0.0072  -0.0332 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1192 0.1786 0.1476 -0.0298 0.0102  -0.0236 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1689 0.1958 0.1729 0.0167  -0.0035 -0.0267 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.1613 0.3287 0.2382 0.0416  0.0436  -0.0820 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.1897 0.3751 0.3955 0.0657  0.0325  -0.1544 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.1333 0.2972 0.3521 0.0017  0.0970  -0.0453 8   GLY A C   
44   O  O   . GLY A 8   ? 0.1953 0.3564 0.3195 0.0200  0.0432  -0.0809 8   GLY A O   
45   N  N   . LYS A 9   ? 0.1865 0.2846 0.4268 0.0227  0.0855  -0.0377 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.2091 0.3047 0.4526 0.0111  0.0304  -0.0510 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.2129 0.2475 0.3373 0.0473  0.0593  -0.0453 9   LYS A C   
48   O  O   . LYS A 9   ? 0.2095 0.2971 0.3118 0.0043  0.0769  0.0138  9   LYS A O   
49   C  CB  . LYS A 9   ? 0.2956 0.2328 0.5574 0.0260  0.0434  0.0066  9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.3553 0.3007 0.5588 0.1069  0.0859  0.0491  9   LYS A CG  
51   N  N   . HIS A 10  ? 0.1653 0.2763 0.3595 0.0108  0.0795  -0.0168 10  HIS A N   
52   C  CA  . HIS A 10  ? 0.1804 0.2249 0.3054 0.0110  0.1154  0.0217  10  HIS A CA  
53   C  C   . HIS A 10  ? 0.1614 0.2454 0.3902 0.0089  0.0864  -0.0315 10  HIS A C   
54   O  O   . HIS A 10  ? 0.1426 0.2805 0.4113 -0.0062 0.0596  0.0140  10  HIS A O   
55   C  CB  . HIS A 10  ? 0.2737 0.2812 0.3578 0.0724  0.1802  0.0071  10  HIS A CB  
56   C  CG  . HIS A 10  ? 0.2276 0.3186 0.3991 0.0778  0.1269  0.0751  10  HIS A CG  
57   N  ND1 . HIS A 10  ? 0.2561 0.3669 0.4597 0.1419  0.1558  0.1183  10  HIS A ND1 
58   C  CD2 . HIS A 10  ? 0.2841 0.3632 0.3941 0.0166  0.2127  0.1151  10  HIS A CD2 
59   C  CE1 . HIS A 10  ? 0.3546 0.3277 0.3929 0.0839  0.0215  0.0546  10  HIS A CE1 
60   N  NE2 . HIS A 10  ? 0.2806 0.3110 0.3140 0.0316  0.1020  0.0145  10  HIS A NE2 
61   N  N   . ASN A 11  ? 0.1642 0.2173 0.2601 0.0273  0.0822  -0.0217 11  ASN A N   
62   C  CA  . ASN A 11  ? 0.1894 0.2004 0.2830 -0.0009 0.0916  0.0144  11  ASN A CA  
63   C  C   . ASN A 11  ? 0.1797 0.1980 0.1577 0.0020  0.0543  -0.0195 11  ASN A C   
64   O  O   . ASN A 11  ? 0.1714 0.2113 0.2196 0.0158  0.0323  -0.0140 11  ASN A O   
65   C  CB  . ASN A 11  ? 0.2099 0.2359 0.2105 -0.0004 0.0868  -0.0173 11  ASN A CB  
66   C  CG  . ASN A 11  ? 0.3647 0.3011 0.1067 -0.0196 0.0670  -0.0499 11  ASN A CG  
67   O  OD1 . ASN A 11  ? 0.2156 0.3010 0.2547 0.0232  0.0436  -0.0295 11  ASN A OD1 
68   N  ND2 . ASN A 11  ? 0.3082 0.3736 0.2133 0.0452  0.0938  0.0543  11  ASN A ND2 
69   N  N   . GLY A 12  ? 0.1511 0.2081 0.2213 0.0097  0.0442  0.0166  12  GLY A N   
70   C  CA  . GLY A 12  ? 0.1351 0.2339 0.1680 -0.0076 0.0370  -0.0340 12  GLY A CA  
71   C  C   . GLY A 12  ? 0.1511 0.1822 0.1653 -0.0100 0.0281  0.0238  12  GLY A C   
72   O  O   . GLY A 12  ? 0.1295 0.1703 0.1994 -0.0036 0.0208  0.0061  12  GLY A O   
73   N  N   . PRO A 13  ? 0.1300 0.1826 0.1562 0.0081  0.0377  -0.0109 13  PRO A N   
74   C  CA  . PRO A 13  ? 0.1363 0.1926 0.1620 -0.0097 0.0305  -0.0157 13  PRO A CA  
75   C  C   . PRO A 13  ? 0.1371 0.1915 0.1517 -0.0087 0.0266  -0.0044 13  PRO A C   
76   O  O   . PRO A 13  ? 0.1328 0.2336 0.1847 -0.0077 0.0210  -0.0326 13  PRO A O   
77   C  CB  . PRO A 13  ? 0.1419 0.2172 0.2052 -0.0265 0.0250  -0.0037 13  PRO A CB  
78   C  CG  . PRO A 13  ? 0.1571 0.2380 0.1404 -0.0189 0.0480  0.0042  13  PRO A CG  
79   C  CD  . PRO A 13  ? 0.1414 0.2205 0.1738 -0.0418 0.0511  -0.0057 13  PRO A CD  
80   N  N   . GLU A 14  ? 0.1525 0.2033 0.2154 -0.0043 0.0111  0.0192  14  GLU A N   
81   C  CA  . GLU A 14  ? 0.1865 0.1973 0.2637 -0.0133 -0.0317 0.0308  14  GLU A CA  
82   C  C   . GLU A 14  ? 0.2080 0.1937 0.2059 0.0111  -0.0209 0.0368  14  GLU A C   
83   O  O   . GLU A 14  ? 0.1659 0.2145 0.2084 0.0181  0.0015  0.0269  14  GLU A O   
84   C  CB  . GLU A 14  ? 0.1782 0.2239 0.3394 -0.0050 -0.0483 0.0750  14  GLU A CB  
85   C  CG  . GLU A 14  ? 0.3859 0.2503 0.3281 -0.1197 -0.0228 0.0486  14  GLU A CG  
86   C  CD  . GLU A 14  ? 0.7789 0.5459 0.2160 -0.2748 0.0029  0.1009  14  GLU A CD  
87   O  OE1 . GLU A 14  ? 0.8899 0.4640 0.4385 -0.2040 -0.1832 -0.0216 14  GLU A OE1 
88   O  OE2 . GLU A 14  ? 0.8531 0.7756 0.7537 -0.3670 0.1340  0.2043  14  GLU A OE2 
89   N  N   . HIS A 15  ? 0.1146 0.1942 0.1736 0.0005  0.0221  0.0173  15  HIS A N   
90   C  CA  . HIS A 15  ? 0.1346 0.1716 0.1771 0.0076  0.0383  0.0232  15  HIS A CA  
91   C  C   . HIS A 15  ? 0.1099 0.1785 0.1947 0.0172  0.0081  0.0195  15  HIS A C   
92   O  O   . HIS A 15  ? 0.1083 0.1836 0.2130 0.0081  0.0149  0.0047  15  HIS A O   
93   C  CB  . HIS A 15  ? 0.1373 0.1635 0.1890 0.0354  0.0076  0.0044  15  HIS A CB  
94   C  CG  . HIS A 15  ? 0.1205 0.1768 0.2223 0.0383  0.0171  0.0248  15  HIS A CG  
95   N  ND1 . HIS A 15  ? 0.1259 0.2336 0.2791 0.0289  0.0116  -0.0111 15  HIS A ND1 
96   C  CD2 . HIS A 15  ? 0.2478 0.1574 0.2302 0.0725  0.0249  0.0085  15  HIS A CD2 
97   C  CE1 . HIS A 15  ? 0.1897 0.2588 0.2780 0.0863  -0.0245 -0.0153 15  HIS A CE1 
98   N  NE2 . HIS A 15  ? 0.1982 0.2156 0.3003 0.0556  0.0402  -0.0307 15  HIS A NE2 
99   N  N   . TRP A 16  ? 0.1090 0.1851 0.1893 0.0281  0.0099  0.0142  16  TRP A N   
100  C  CA  . TRP A 16  ? 0.1059 0.1811 0.1808 0.0183  -0.0082 -0.0006 16  TRP A CA  
101  C  C   . TRP A 16  ? 0.1181 0.1857 0.1591 0.0016  0.0026  0.0082  16  TRP A C   
102  O  O   . TRP A 16  ? 0.1144 0.1747 0.1779 -0.0164 0.0065  0.0111  16  TRP A O   
103  C  CB  . TRP A 16  ? 0.1104 0.1684 0.1469 0.0108  0.0206  -0.0172 16  TRP A CB  
104  C  CG  . TRP A 16  ? 0.1226 0.1657 0.1439 0.0097  0.0250  -0.0197 16  TRP A CG  
105  C  CD1 . TRP A 16  ? 0.1050 0.1810 0.1546 0.0167  0.0337  -0.0302 16  TRP A CD1 
106  C  CD2 . TRP A 16  ? 0.1113 0.1627 0.1449 0.0087  0.0155  0.0006  16  TRP A CD2 
107  N  NE1 . TRP A 16  ? 0.1199 0.2029 0.1635 0.0125  0.0238  -0.0018 16  TRP A NE1 
108  C  CE2 . TRP A 16  ? 0.1169 0.2045 0.1455 0.0106  0.0206  -0.0035 16  TRP A CE2 
109  C  CE3 . TRP A 16  ? 0.1037 0.1671 0.1691 0.0110  0.0195  0.0120  16  TRP A CE3 
110  C  CZ2 . TRP A 16  ? 0.1118 0.1784 0.1646 0.0041  0.0268  0.0027  16  TRP A CZ2 
111  C  CZ3 . TRP A 16  ? 0.1075 0.1840 0.1717 0.0192  -0.0095 0.0000  16  TRP A CZ3 
112  C  CH2 . TRP A 16  ? 0.1107 0.1984 0.1373 0.0087  0.0147  0.0204  16  TRP A CH2 
113  N  N   . HIS A 17  ? 0.1159 0.2020 0.1365 0.0095  0.0210  -0.0092 17  HIS A N   
114  C  CA  . HIS A 17  ? 0.1267 0.1962 0.1655 -0.0117 0.0008  0.0075  17  HIS A CA  
115  C  C   . HIS A 17  ? 0.1065 0.2137 0.1627 0.0026  0.0203  0.0097  17  HIS A C   
116  O  O   . HIS A 17  ? 0.1333 0.2109 0.1825 -0.0070 0.0254  -0.0073 17  HIS A O   
117  C  CB  . HIS A 17  ? 0.1441 0.1957 0.1497 0.0023  0.0113  0.0057  17  HIS A CB  
118  C  CG  . HIS A 17  ? 0.1481 0.2309 0.1564 -0.0078 0.0116  0.0073  17  HIS A CG  
119  N  ND1 . HIS A 17  ? 0.1317 0.2953 0.1745 0.0025  0.0080  0.0047  17  HIS A ND1 
120  C  CD2 . HIS A 17  ? 0.1414 0.2533 0.1357 -0.0075 0.0120  0.0065  17  HIS A CD2 
121  C  CE1 . HIS A 17  ? 0.1687 0.2345 0.1474 -0.0025 0.0375  0.0245  17  HIS A CE1 
122  N  NE2 . HIS A 17  ? 0.1485 0.2392 0.1623 0.0154  0.0288  0.0260  17  HIS A NE2 
123  N  N   . LYS A 18  ? 0.1054 0.1903 0.1754 -0.0104 0.0120  0.0012  18  LYS A N   
124  C  CA  . LYS A 18  ? 0.1222 0.2230 0.1969 -0.0127 0.0523  0.0244  18  LYS A CA  
125  C  C   . LYS A 18  ? 0.1065 0.2116 0.2037 -0.0141 0.0189  0.0233  18  LYS A C   
126  O  O   . LYS A 18  ? 0.1790 0.2512 0.3546 -0.0638 -0.0549 0.0710  18  LYS A O   
127  C  CB  . LYS A 18  ? 0.1269 0.2109 0.1926 -0.0017 0.0384  0.0132  18  LYS A CB  
128  C  CG  . LYS A 18  ? 0.1304 0.2216 0.2206 0.0326  0.0377  0.0168  18  LYS A CG  
129  C  CD  . LYS A 18  ? 0.1355 0.2898 0.1586 0.0087  0.0557  0.0008  18  LYS A CD  
130  C  CE  . LYS A 18  ? 0.1331 0.2399 0.2059 0.0221  0.0442  0.0298  18  LYS A CE  
131  N  NZ  . LYS A 18  ? 0.1374 0.1960 0.2385 0.0237  0.0452  0.0227  18  LYS A NZ  
132  N  N   . ASP A 19  ? 0.1226 0.2362 0.1461 0.0079  0.0307  0.0179  19  ASP A N   
133  C  CA  . ASP A 19  ? 0.1539 0.2018 0.2124 -0.0094 0.0523  0.0061  19  ASP A CA  
134  C  C   . ASP A 19  ? 0.1337 0.1793 0.1966 -0.0205 0.0472  0.0097  19  ASP A C   
135  O  O   . ASP A 19  ? 0.1631 0.2029 0.2964 -0.0204 0.0623  0.0479  19  ASP A O   
136  C  CB  . ASP A 19  ? 0.2105 0.2795 0.2052 0.0288  -0.0100 0.0317  19  ASP A CB  
137  C  CG  . ASP A 19  ? 0.3550 0.2727 0.3424 -0.0163 0.1423  -0.0701 19  ASP A CG  
138  O  OD1 . ASP A 19  ? 0.2846 0.2928 0.2860 -0.0047 0.0216  0.0379  19  ASP A OD1 
139  O  OD2 . ASP A 19  ? 0.4835 0.3086 0.2541 0.0320  0.1142  -0.0442 19  ASP A OD2 
140  N  N   . PHE A 20  ? 0.1153 0.1869 0.1682 -0.0035 0.0361  0.0215  20  PHE A N   
141  C  CA  . PHE A 20  ? 0.1138 0.2100 0.1753 0.0013  0.0433  -0.0040 20  PHE A CA  
142  C  C   . PHE A 20  ? 0.1453 0.1872 0.2064 0.0125  0.0162  -0.0036 20  PHE A C   
143  O  O   . PHE A 20  ? 0.1388 0.1761 0.2095 0.0085  0.0215  -0.0071 20  PHE A O   
144  C  CB  . PHE A 20  ? 0.1049 0.2519 0.2004 -0.0204 0.0303  0.0334  20  PHE A CB  
145  C  CG  . PHE A 20  ? 0.1049 0.2590 0.2435 -0.0313 -0.0065 0.0550  20  PHE A CG  
146  C  CD1 . PHE A 20  ? 0.1403 0.3032 0.2838 -0.0113 0.0139  0.1176  20  PHE A CD1 
147  C  CD2 . PHE A 20  ? 0.1620 0.3349 0.2113 -0.0615 -0.0241 0.0649  20  PHE A CD2 
148  C  CE1 . PHE A 20  ? 0.1424 0.3201 0.2475 -0.0340 0.0179  0.0741  20  PHE A CE1 
149  C  CE2 . PHE A 20  ? 0.1303 0.3840 0.2196 -0.0508 0.0216  0.0710  20  PHE A CE2 
150  C  CZ  . PHE A 20  ? 0.1367 0.3348 0.2712 -0.0514 -0.0240 0.0623  20  PHE A CZ  
151  N  N   . PRO A 21  ? 0.1293 0.1948 0.2014 -0.0068 0.0196  -0.0070 21  PRO A N   
152  C  CA  . PRO A 21  ? 0.1384 0.2569 0.1821 -0.0280 0.0161  -0.0170 21  PRO A CA  
153  C  C   . PRO A 21  ? 0.1192 0.2312 0.1527 -0.0407 -0.0125 -0.0017 21  PRO A C   
154  O  O   . PRO A 21  ? 0.1248 0.2428 0.1800 -0.0217 -0.0148 0.0033  21  PRO A O   
155  C  CB  . PRO A 21  ? 0.1273 0.3279 0.2640 -0.0768 0.0174  0.0029  21  PRO A CB  
156  C  CG  . PRO A 21  ? 0.2813 0.3295 0.2835 -0.1296 -0.0216 0.0268  21  PRO A CG  
157  C  CD  . PRO A 21  ? 0.1244 0.2423 0.2864 -0.0469 0.0162  -0.0004 21  PRO A CD  
158  N  N   A ILE A 22  ? 0.1093 0.2310 0.1404 -0.0214 0.0077  -0.0272 22  ILE A N   
159  N  N   B ILE A 22  ? 0.1084 0.2418 0.1507 -0.0190 0.0077  -0.0296 22  ILE A N   
160  C  CA  A ILE A 22  ? 0.1254 0.1904 0.1497 -0.0115 0.0214  -0.0223 22  ILE A CA  
161  C  CA  B ILE A 22  ? 0.1357 0.2080 0.1544 -0.0163 0.0276  -0.0348 22  ILE A CA  
162  C  C   A ILE A 22  ? 0.1156 0.1948 0.1373 -0.0113 0.0181  -0.0089 22  ILE A C   
163  C  C   B ILE A 22  ? 0.1311 0.2043 0.1476 -0.0086 0.0237  -0.0159 22  ILE A C   
164  O  O   A ILE A 22  ? 0.1208 0.2093 0.1411 -0.0031 0.0222  0.0093  22  ILE A O   
165  O  O   B ILE A 22  ? 0.1323 0.2256 0.1575 -0.0006 0.0261  0.0086  22  ILE A O   
166  C  CB  A ILE A 22  ? 0.1458 0.2068 0.1362 -0.0012 -0.0005 -0.0341 22  ILE A CB  
167  C  CB  B ILE A 22  ? 0.1593 0.2260 0.1335 0.0005  0.0130  -0.0589 22  ILE A CB  
168  C  CG1 A ILE A 22  ? 0.1483 0.1966 0.1669 -0.0179 0.0297  -0.0034 22  ILE A CG1 
169  C  CG1 B ILE A 22  ? 0.1742 0.2526 0.1423 -0.0008 0.0230  -0.0763 22  ILE A CG1 
170  C  CG2 A ILE A 22  ? 0.1542 0.2009 0.1226 -0.0076 -0.0018 -0.0122 22  ILE A CG2 
171  C  CG2 B ILE A 22  ? 0.1811 0.2425 0.1113 -0.0098 0.0122  -0.0262 22  ILE A CG2 
172  C  CD1 A ILE A 22  ? 0.2245 0.2321 0.2131 0.0364  -0.0062 -0.0260 22  ILE A CD1 
173  C  CD1 B ILE A 22  ? 0.2296 0.2467 0.1025 -0.0204 0.0719  -0.0829 22  ILE A CD1 
174  N  N   . ALA A 23  ? 0.1239 0.1954 0.1500 0.0124  -0.0081 -0.0288 23  ALA A N   
175  C  CA  . ALA A 23  ? 0.1561 0.2019 0.1333 -0.0009 0.0294  -0.0110 23  ALA A CA  
176  C  C   . ALA A 23  ? 0.1241 0.2309 0.1307 0.0030  0.0311  -0.0200 23  ALA A C   
177  O  O   . ALA A 23  ? 0.1903 0.2029 0.1746 -0.0072 0.0384  -0.0071 23  ALA A O   
178  C  CB  . ALA A 23  ? 0.1336 0.2045 0.1452 0.0044  0.0239  -0.0232 23  ALA A CB  
179  N  N   . LYS A 24  ? 0.1487 0.2228 0.2107 0.0071  -0.0086 -0.0287 24  LYS A N   
180  C  CA  . LYS A 24  ? 0.1527 0.2346 0.2137 0.0010  -0.0077 -0.0189 24  LYS A CA  
181  C  C   . LYS A 24  ? 0.1430 0.3019 0.1540 0.0068  0.0305  0.0208  24  LYS A C   
182  O  O   . LYS A 24  ? 0.1828 0.3427 0.1811 0.0389  -0.0027 0.0143  24  LYS A O   
183  C  CB  . LYS A 24  ? 0.1710 0.2579 0.1905 0.0247  -0.0133 -0.0047 24  LYS A CB  
184  C  CG  . LYS A 24  ? 0.1883 0.3801 0.1468 0.0411  0.0248  -0.0217 24  LYS A CG  
185  C  CD  . LYS A 24  ? 0.2034 0.3475 0.3259 0.0732  -0.0218 -0.0370 24  LYS A CD  
186  C  CE  . LYS A 24  ? 0.3585 0.3868 0.2228 0.0707  0.1438  0.0359  24  LYS A CE  
187  N  NZ  . LYS A 24  ? 0.3610 0.4468 0.4566 -0.0336 0.1021  0.0458  24  LYS A NZ  
188  N  N   . GLY A 25  ? 0.1327 0.2565 0.1817 0.0115  0.0288  -0.0277 25  GLY A N   
189  C  CA  . GLY A 25  ? 0.1592 0.2788 0.1962 0.0098  0.0606  -0.0321 25  GLY A CA  
190  C  C   . GLY A 25  ? 0.1407 0.2882 0.1451 0.0105  -0.0053 -0.0292 25  GLY A C   
191  O  O   . GLY A 25  ? 0.1929 0.2856 0.1363 -0.0026 -0.0116 -0.0075 25  GLY A O   
192  N  N   . GLU A 26  ? 0.1415 0.2924 0.1452 0.0084  0.0053  -0.0421 26  GLU A N   
193  C  CA  . GLU A 26  ? 0.1677 0.3036 0.1283 0.0020  0.0077  -0.0366 26  GLU A CA  
194  C  C   . GLU A 26  ? 0.1465 0.2541 0.1623 0.0179  0.0047  0.0192  26  GLU A C   
195  O  O   . GLU A 26  ? 0.2014 0.3021 0.0968 -0.0005 -0.0077 0.0070  26  GLU A O   
196  C  CB  . GLU A 26  ? 0.1976 0.4497 0.1502 -0.0337 0.0057  -0.1121 26  GLU A CB  
197  C  CG  . GLU A 26  ? 0.2404 0.6397 0.1355 -0.0565 -0.0528 -0.0674 26  GLU A CG  
198  C  CD  . GLU A 26  ? 0.2910 0.6822 0.2942 -0.0907 -0.1442 -0.0289 26  GLU A CD  
199  O  OE1 . GLU A 26  ? 0.4210 0.5050 0.5368 -0.0369 -0.1168 0.0628  26  GLU A OE1 
200  O  OE2 . GLU A 26  ? 0.2680 0.9868 0.6009 -0.0807 -0.1211 0.1155  26  GLU A OE2 
201  N  N   . ARG A 27  ? 0.1559 0.2101 0.1370 0.0042  -0.0240 -0.0251 27  ARG A N   
202  C  CA  . ARG A 27  ? 0.1445 0.1840 0.1192 -0.0027 -0.0099 -0.0183 27  ARG A CA  
203  C  C   . ARG A 27  ? 0.1511 0.1696 0.1104 -0.0081 -0.0091 0.0010  27  ARG A C   
204  O  O   . ARG A 27  ? 0.1514 0.2097 0.1061 0.0086  -0.0030 -0.0032 27  ARG A O   
205  C  CB  . ARG A 27  ? 0.2949 0.2271 0.1234 0.0451  -0.0201 -0.0680 27  ARG A CB  
206  C  CG  . ARG A 27  ? 0.2828 0.3146 0.2209 -0.0302 0.0111  -0.0330 27  ARG A CG  
207  C  CD  . ARG A 27  ? 0.3407 0.4821 0.5387 0.1025  0.1160  -0.0806 27  ARG A CD  
208  N  NE  . ARG A 27  ? 0.3448 0.3589 0.3611 0.0805  0.1337  0.0305  27  ARG A NE  
209  C  CZ  . ARG A 27  ? 0.3069 0.2505 0.2667 0.0477  0.0269  -0.0694 27  ARG A CZ  
210  N  NH1 . ARG A 27  ? 0.1853 0.1876 0.1234 0.0064  0.0040  -0.0631 27  ARG A NH1 
211  N  NH2 . ARG A 27  ? 0.2338 0.2353 0.2579 -0.0236 0.0908  -0.0824 27  ARG A NH2 
212  N  N   . GLN A 28  ? 0.1408 0.1958 0.0979 -0.0058 0.0079  -0.0222 28  GLN A N   
213  C  CA  . GLN A 28  ? 0.1179 0.1951 0.0880 -0.0147 0.0189  -0.0160 28  GLN A CA  
214  C  C   . GLN A 28  ? 0.1585 0.1472 0.0973 -0.0259 -0.0034 -0.0015 28  GLN A C   
215  O  O   . GLN A 28  ? 0.1555 0.1975 0.1072 -0.0193 0.0065  0.0032  28  GLN A O   
216  C  CB  . GLN A 28  ? 0.1100 0.1742 0.1450 0.0010  0.0081  -0.0085 28  GLN A CB  
217  C  CG  . GLN A 28  ? 0.1208 0.1768 0.1333 -0.0026 0.0076  0.0006  28  GLN A CG  
218  C  CD  . GLN A 28  ? 0.1307 0.1818 0.0912 0.0065  0.0052  -0.0289 28  GLN A CD  
219  O  OE1 . GLN A 28  ? 0.1237 0.1847 0.1146 0.0031  0.0061  -0.0384 28  GLN A OE1 
220  N  NE2 . GLN A 28  ? 0.1243 0.1718 0.1539 -0.0116 -0.0037 -0.0325 28  GLN A NE2 
221  N  N   . SER A 29  ? 0.1099 0.1496 0.0983 0.0165  0.0009  -0.0215 29  SER A N   
222  C  CA  . SER A 29  ? 0.1217 0.1240 0.1129 0.0110  -0.0092 -0.0124 29  SER A CA  
223  C  C   . SER A 29  ? 0.1229 0.1430 0.0948 0.0019  0.0034  0.0094  29  SER A C   
224  O  O   . SER A 29  ? 0.1195 0.1655 0.1117 -0.0139 0.0031  -0.0023 29  SER A O   
225  C  CB  . SER A 29  ? 0.1076 0.1693 0.0928 0.0267  0.0158  -0.0095 29  SER A CB  
226  O  OG  . SER A 29  ? 0.1368 0.1462 0.0986 0.0122  0.0231  -0.0104 29  SER A OG  
227  N  N   . PRO A 30  ? 0.1082 0.1412 0.0980 0.0042  0.0033  0.0025  30  PRO A N   
228  C  CA  . PRO A 30  ? 0.1265 0.1464 0.1054 -0.0064 0.0134  0.0060  30  PRO A CA  
229  C  C   . PRO A 30  ? 0.1362 0.1478 0.1108 -0.0111 0.0075  0.0040  30  PRO A C   
230  O  O   . PRO A 30  ? 0.1315 0.1705 0.1124 0.0040  -0.0089 0.0006  30  PRO A O   
231  C  CB  . PRO A 30  ? 0.1251 0.1693 0.1363 0.0114  0.0015  -0.0419 30  PRO A CB  
232  C  CG  . PRO A 30  ? 0.1295 0.1536 0.1221 -0.0013 0.0233  -0.0168 30  PRO A CG  
233  C  CD  . PRO A 30  ? 0.1438 0.1544 0.1025 -0.0039 0.0190  -0.0267 30  PRO A CD  
234  N  N   . VAL A 31  ? 0.1469 0.1436 0.1046 0.0000  0.0163  0.0220  31  VAL A N   
235  C  CA  . VAL A 31  ? 0.1779 0.1650 0.1029 -0.0081 0.0018  0.0335  31  VAL A CA  
236  C  C   . VAL A 31  ? 0.1511 0.1710 0.1183 -0.0004 -0.0026 0.0124  31  VAL A C   
237  O  O   . VAL A 31  ? 0.1333 0.1562 0.1522 -0.0034 0.0051  0.0293  31  VAL A O   
238  C  CB  . VAL A 31  ? 0.1544 0.1802 0.1280 0.0019  0.0020  -0.0078 31  VAL A CB  
239  C  CG1 . VAL A 31  ? 0.2062 0.2141 0.1156 -0.0209 0.0148  -0.0002 31  VAL A CG1 
240  C  CG2 . VAL A 31  ? 0.1714 0.1944 0.1188 0.0165  -0.0054 0.0214  31  VAL A CG2 
241  N  N   . ASP A 32  ? 0.1561 0.1709 0.1364 -0.0053 0.0020  0.0310  32  ASP A N   
242  C  CA  . ASP A 32  ? 0.1472 0.1611 0.1333 0.0165  0.0372  0.0411  32  ASP A CA  
243  C  C   . ASP A 32  ? 0.1754 0.1867 0.0995 0.0033  0.0228  0.0058  32  ASP A C   
244  O  O   . ASP A 32  ? 0.1738 0.2059 0.1449 -0.0097 0.0089  -0.0067 32  ASP A O   
245  C  CB  . ASP A 32  ? 0.2159 0.1659 0.1710 0.0335  0.0079  0.0406  32  ASP A CB  
246  C  CG  . ASP A 32  ? 0.2224 0.1897 0.1867 0.0218  -0.0110 0.0583  32  ASP A CG  
247  O  OD1 . ASP A 32  ? 0.2145 0.1793 0.1709 0.0149  0.0218  0.0447  32  ASP A OD1 
248  O  OD2 . ASP A 32  ? 0.2834 0.2285 0.2123 0.0076  -0.0077 0.0824  32  ASP A OD2 
249  N  N   . ILE A 33  ? 0.1568 0.1756 0.1414 0.0182  0.0238  0.0253  33  ILE A N   
250  C  CA  . ILE A 33  ? 0.1763 0.1796 0.1190 0.0093  0.0355  0.0373  33  ILE A CA  
251  C  C   . ILE A 33  ? 0.1659 0.1833 0.1480 0.0128  0.0494  0.0391  33  ILE A C   
252  O  O   . ILE A 33  ? 0.2136 0.1790 0.1849 -0.0030 0.0285  0.0501  33  ILE A O   
253  C  CB  . ILE A 33  ? 0.1632 0.1872 0.1856 0.0279  0.0317  0.0396  33  ILE A CB  
254  C  CG1 . ILE A 33  ? 0.2012 0.1675 0.1657 0.0117  -0.0027 0.0283  33  ILE A CG1 
255  C  CG2 . ILE A 33  ? 0.1747 0.2385 0.2150 0.0190  0.0624  0.0452  33  ILE A CG2 
256  C  CD1 . ILE A 33  ? 0.2063 0.2249 0.1749 -0.0016 -0.0034 0.0513  33  ILE A CD1 
257  N  N   . ASP A 34  ? 0.2573 0.2400 0.1276 0.0055  0.0588  0.0469  34  ASP A N   
258  C  CA  . ASP A 34  ? 0.2043 0.2855 0.2079 0.0136  0.0476  0.1195  34  ASP A CA  
259  C  C   . ASP A 34  ? 0.2597 0.2533 0.1634 0.0184  0.0558  0.0796  34  ASP A C   
260  O  O   . ASP A 34  ? 0.2825 0.2795 0.1771 0.0384  0.0341  0.0621  34  ASP A O   
261  C  CB  . ASP A 34  ? 0.2213 0.2728 0.2192 0.0376  0.0187  0.1022  34  ASP A CB  
262  C  CG  . ASP A 34  ? 0.2874 0.3776 0.2781 0.0391  0.0759  0.1618  34  ASP A CG  
263  O  OD1 . ASP A 34  ? 0.2931 0.3748 0.2316 0.0465  0.0593  0.1081  34  ASP A OD1 
264  O  OD2 . ASP A 34  ? 0.3791 0.4845 0.3814 0.0542  -0.0030 0.2218  34  ASP A OD2 
265  N  N   . THR A 35  ? 0.2156 0.2288 0.1878 0.0344  0.0425  0.1183  35  THR A N   
266  C  CA  . THR A 35  ? 0.2380 0.2820 0.2313 0.0631  0.1024  0.0831  35  THR A CA  
267  C  C   . THR A 35  ? 0.2791 0.2703 0.2152 0.0566  0.0806  0.0658  35  THR A C   
268  O  O   . THR A 35  ? 0.2267 0.2680 0.2893 0.0466  0.0612  0.0606  35  THR A O   
269  C  CB  . THR A 35  ? 0.2098 0.2837 0.3000 0.0646  0.1026  0.0904  35  THR A CB  
270  O  OG1 . THR A 35  ? 0.2488 0.2705 0.2899 0.0039  0.0649  0.1112  35  THR A OG1 
271  C  CG2 . THR A 35  ? 0.2746 0.3801 0.3158 0.1213  0.1357  0.1681  35  THR A CG2 
272  N  N   . HIS A 36  ? 0.3121 0.2716 0.2518 0.0966  0.1657  0.1183  36  HIS A N   
273  C  CA  . HIS A 36  ? 0.3693 0.2816 0.1919 0.1270  0.1419  0.0954  36  HIS A CA  
274  C  C   . HIS A 36  ? 0.5256 0.3001 0.2996 0.0359  0.0829  0.1119  36  HIS A C   
275  O  O   . HIS A 36  ? 0.3628 0.4102 0.3071 -0.0268 0.0785  0.0549  36  HIS A O   
276  C  CB  . HIS A 36  ? 0.3905 0.2346 0.1609 0.0751  0.1083  0.0291  36  HIS A CB  
277  C  CG  . HIS A 36  ? 0.4516 0.3463 0.1116 0.0279  -0.0111 0.0242  36  HIS A CG  
278  N  ND1 . HIS A 36  ? 0.4401 0.3779 0.2275 0.0483  -0.0480 0.0433  36  HIS A ND1 
279  C  CD2 . HIS A 36  ? 0.4471 0.3198 0.1544 0.0677  0.0006  0.0240  36  HIS A CD2 
280  C  CE1 . HIS A 36  ? 0.5189 0.2400 0.2271 0.1536  0.0485  0.0587  36  HIS A CE1 
281  N  NE2 . HIS A 36  ? 0.3805 0.2579 0.2913 0.0291  -0.0096 0.0528  36  HIS A NE2 
282  N  N   . THR A 37  ? 0.3420 0.2519 0.2613 0.0969  0.0673  0.0741  37  THR A N   
283  C  CA  . THR A 37  ? 0.3620 0.3098 0.2287 0.1317  0.0966  0.0362  37  THR A CA  
284  C  C   . THR A 37  ? 0.2216 0.2759 0.2355 0.0491  0.0346  0.0783  37  THR A C   
285  O  O   . THR A 37  ? 0.3722 0.3424 0.2656 0.1152  -0.0074 0.0586  37  THR A O   
286  C  CB  . THR A 37  ? 0.3664 0.4139 0.2285 0.1668  0.1018  0.0756  37  THR A CB  
287  O  OG1 . THR A 37  ? 0.4292 0.4264 0.2331 0.1731  0.0685  0.0443  37  THR A OG1 
288  C  CG2 . THR A 37  ? 0.3855 0.3610 0.3100 0.1498  0.0444  0.0519  37  THR A CG2 
289  N  N   . ALA A 38  ? 0.2692 0.2475 0.2148 0.0637  0.0732  0.0780  38  ALA A N   
290  C  CA  . ALA A 38  ? 0.2391 0.2565 0.2180 0.0791  0.0615  0.0680  38  ALA A CA  
291  C  C   . ALA A 38  ? 0.2536 0.2454 0.2391 0.0653  0.0881  0.0679  38  ALA A C   
292  O  O   . ALA A 38  ? 0.3042 0.3010 0.2870 0.0249  0.1149  0.0834  38  ALA A O   
293  C  CB  . ALA A 38  ? 0.2946 0.2856 0.2256 0.0405  0.0608  0.0509  38  ALA A CB  
294  N  N   . LYS A 39  ? 0.2231 0.2637 0.1273 0.0414  0.0510  0.0422  39  LYS A N   
295  C  CA  . LYS A 39  ? 0.2020 0.2843 0.1363 0.0675  0.0263  0.0060  39  LYS A CA  
296  C  C   . LYS A 39  ? 0.1911 0.3125 0.1759 0.0627  0.0785  0.0758  39  LYS A C   
297  O  O   . LYS A 39  ? 0.2160 0.3341 0.1386 0.0581  0.0370  0.0635  39  LYS A O   
298  C  CB  . LYS A 39  ? 0.2875 0.3216 0.1421 0.0602  -0.0184 0.0042  39  LYS A CB  
299  C  CG  . LYS A 39  ? 0.3147 0.3244 0.1843 0.0278  0.0277  0.0097  39  LYS A CG  
300  C  CD  . LYS A 39  ? 0.3657 0.2734 0.2178 0.0798  0.0413  0.0605  39  LYS A CD  
301  C  CE  . LYS A 39  ? 0.3948 0.4623 0.2206 0.0706  0.0656  -0.0158 39  LYS A CE  
302  N  NZ  . LYS A 39  ? 0.2982 0.4153 0.2975 0.0541  0.0385  0.0462  39  LYS A NZ  
303  N  N   . TYR A 40  ? 0.1958 0.3759 0.1467 0.0403  0.0373  0.0744  40  TYR A N   
304  C  CA  . TYR A 40  ? 0.2138 0.3722 0.1313 0.0607  0.0589  0.0670  40  TYR A CA  
305  C  C   . TYR A 40  ? 0.2479 0.3887 0.1297 0.0635  0.0469  0.0276  40  TYR A C   
306  O  O   . TYR A 40  ? 0.2334 0.4529 0.1259 0.0576  0.0166  0.0255  40  TYR A O   
307  C  CB  . TYR A 40  ? 0.2172 0.4626 0.2319 0.0374  0.0921  0.1382  40  TYR A CB  
308  C  CG  . TYR A 40  ? 0.2339 0.4952 0.1802 0.0266  0.0978  0.1211  40  TYR A CG  
309  C  CD1 . TYR A 40  ? 0.2611 0.4629 0.1948 -0.0042 0.0491  0.0886  40  TYR A CD1 
310  C  CD2 . TYR A 40  ? 0.3231 0.7153 0.2242 0.0572  0.1597  0.1198  40  TYR A CD2 
311  C  CE1 . TYR A 40  ? 0.2332 0.5834 0.2167 0.0074  0.0484  0.0493  40  TYR A CE1 
312  C  CE2 . TYR A 40  ? 0.3202 0.6377 0.2011 0.0375  0.1067  0.0838  40  TYR A CE2 
313  C  CZ  . TYR A 40  ? 0.2385 0.6032 0.2371 0.0236  0.0649  0.0905  40  TYR A CZ  
314  O  OH  . TYR A 40  ? 0.2450 0.7434 0.4451 0.1097  0.0978  0.0037  40  TYR A OH  
315  N  N   . ASP A 41  ? 0.2133 0.3098 0.1962 0.0403  0.0245  0.0383  41  ASP A N   
316  C  CA  . ASP A 41  ? 0.2891 0.3396 0.2597 0.0158  0.0111  0.0036  41  ASP A CA  
317  C  C   . ASP A 41  ? 0.3682 0.4396 0.2379 0.1935  0.0937  0.0509  41  ASP A C   
318  O  O   . ASP A 41  ? 0.2983 0.4317 0.2303 0.0841  0.0119  -0.0063 41  ASP A O   
319  C  CB  . ASP A 41  ? 0.2620 0.3481 0.3491 -0.0203 -0.0342 -0.0189 41  ASP A CB  
320  C  CG  . ASP A 41  ? 0.5519 0.4314 0.3920 0.0295  -0.0532 -0.0956 41  ASP A CG  
321  O  OD1 . ASP A 41  ? 0.5705 0.4528 0.2902 0.1631  -0.1099 -0.1064 41  ASP A OD1 
322  O  OD2 . ASP A 41  ? 0.6463 0.4835 0.5389 -0.0252 -0.1118 0.0058  41  ASP A OD2 
323  N  N   . PRO A 42  ? 0.3974 0.6857 0.1675 0.2068  0.0792  0.0285  42  PRO A N   
324  C  CA  . PRO A 42  ? 0.4288 0.6039 0.3028 0.2913  0.1640  0.0965  42  PRO A CA  
325  C  C   . PRO A 42  ? 0.3560 0.5230 0.1792 0.1250  0.0724  -0.0162 42  PRO A C   
326  O  O   . PRO A 42  ? 0.2935 0.7898 0.3941 0.1357  -0.0076 -0.0138 42  PRO A O   
327  C  CB  . PRO A 42  ? 0.5061 0.7497 0.3653 0.1983  0.2544  0.0710  42  PRO A CB  
328  C  CG  . PRO A 42  ? 0.4821 0.7655 0.5567 0.1832  0.2385  0.0629  42  PRO A CG  
329  C  CD  . PRO A 42  ? 0.4479 0.5761 0.2454 0.3001  0.1599  0.1364  42  PRO A CD  
330  N  N   . SER A 43  ? 0.4401 0.3761 0.1872 0.0650  0.0452  -0.0259 43  SER A N   
331  C  CA  . SER A 43  ? 0.6355 0.3439 0.2395 0.0335  0.0973  -0.0427 43  SER A CA  
332  C  C   . SER A 43  ? 0.5030 0.3933 0.2251 0.1008  0.0656  -0.0557 43  SER A C   
333  O  O   . SER A 43  ? 0.6074 0.3858 0.3521 0.0938  -0.0051 -0.0704 43  SER A O   
334  C  CB  . SER A 43  ? 0.6466 0.5339 0.4403 0.0203  0.0464  -0.1722 43  SER A CB  
335  O  OG  . SER A 43  ? 0.5501 0.7009 0.3026 0.1728  -0.0762 -0.0879 43  SER A OG  
336  N  N   . LEU A 44  ? 0.5739 0.5023 0.1288 0.1756  -0.0086 -0.0846 44  LEU A N   
337  C  CA  . LEU A 44  ? 0.4271 0.6240 0.1168 0.0958  -0.0515 -0.0805 44  LEU A CA  
338  C  C   . LEU A 44  ? 0.3334 0.5376 0.3105 0.0031  -0.0058 0.1424  44  LEU A C   
339  O  O   . LEU A 44  ? 0.2949 0.5716 0.2705 -0.0252 0.0264  0.1160  44  LEU A O   
340  C  CB  . LEU A 44  ? 0.3108 0.5762 0.1778 0.0226  0.0260  -0.0283 44  LEU A CB  
341  C  CG  . LEU A 44  ? 0.2931 0.3905 0.2350 -0.0331 -0.0145 -0.0027 44  LEU A CG  
342  C  CD1 . LEU A 44  ? 0.3136 0.3802 0.2050 0.0142  0.0113  0.0205  44  LEU A CD1 
343  C  CD2 . LEU A 44  ? 0.4673 0.2792 0.2352 0.0176  0.0198  0.0530  44  LEU A CD2 
344  N  N   . LYS A 45  ? 0.2821 0.5962 0.2447 0.0495  -0.0446 0.1573  45  LYS A N   
345  C  CA  . LYS A 45  ? 0.2913 0.4210 0.2879 0.0458  -0.0998 0.0203  45  LYS A CA  
346  C  C   . LYS A 45  ? 0.2809 0.5699 0.1185 0.0927  -0.0131 0.0335  45  LYS A C   
347  O  O   . LYS A 45  ? 0.2186 0.5001 0.3194 -0.0535 0.0888  -0.0649 45  LYS A O   
348  C  CB  . LYS A 45  ? 0.3545 0.4128 0.1901 0.1368  0.0326  -0.0421 45  LYS A CB  
349  C  CG  . LYS A 45  ? 0.4286 0.6202 0.2107 -0.0895 0.0704  -0.1279 45  LYS A CG  
350  C  CD  . LYS A 45  ? 0.3991 0.7212 0.6014 -0.1246 0.2255  -0.0301 45  LYS A CD  
351  N  N   . PRO A 46  ? 0.2486 0.3901 0.1670 -0.0347 0.0264  0.0092  46  PRO A N   
352  C  CA  . PRO A 46  ? 0.2511 0.4278 0.1490 -0.0776 0.0144  0.0216  46  PRO A CA  
353  C  C   . PRO A 46  ? 0.2140 0.3036 0.1897 -0.0155 0.0396  0.0152  46  PRO A C   
354  O  O   . PRO A 46  ? 0.1786 0.3746 0.2108 -0.0293 0.0355  0.0692  46  PRO A O   
355  C  CB  . PRO A 46  ? 0.2144 0.4918 0.2658 -0.0434 0.1016  0.0293  46  PRO A CB  
356  C  CG  . PRO A 46  ? 0.2454 0.5549 0.2810 0.0245  0.0853  -0.0941 46  PRO A CG  
357  C  CD  . PRO A 46  ? 0.2861 0.5189 0.3323 0.0369  0.0129  -0.0648 46  PRO A CD  
358  N  N   . LEU A 47  ? 0.2002 0.3543 0.2253 0.0321  -0.0116 0.0179  47  LEU A N   
359  C  CA  . LEU A 47  ? 0.2088 0.3398 0.2087 0.0258  0.0082  0.0052  47  LEU A CA  
360  C  C   . LEU A 47  ? 0.1790 0.2440 0.2834 -0.0258 -0.0142 0.0322  47  LEU A C   
361  O  O   . LEU A 47  ? 0.1887 0.2798 0.4451 -0.0522 -0.0551 0.0942  47  LEU A O   
362  C  CB  . LEU A 47  ? 0.3128 0.3631 0.2362 0.0182  0.0487  -0.0076 47  LEU A CB  
363  C  CG  . LEU A 47  ? 0.1843 0.4035 0.3980 -0.0015 -0.0168 -0.0928 47  LEU A CG  
364  C  CD1 . LEU A 47  ? 0.1998 0.2957 0.4932 -0.0402 -0.0718 -0.0379 47  LEU A CD1 
365  C  CD2 . LEU A 47  ? 0.2252 0.3929 0.5556 0.0144  -0.0487 -0.1419 47  LEU A CD2 
366  N  N   . SER A 48  ? 0.1624 0.2447 0.1824 0.0071  0.0317  0.0161  48  SER A N   
367  C  CA  . SER A 48  ? 0.1493 0.2724 0.1894 0.0340  0.0296  0.0053  48  SER A CA  
368  C  C   . SER A 48  ? 0.1562 0.2691 0.1626 0.0070  -0.0030 -0.0033 48  SER A C   
369  O  O   . SER A 48  ? 0.1720 0.2341 0.2090 -0.0052 0.0395  -0.0254 48  SER A O   
370  C  CB  . SER A 48  ? 0.2050 0.2792 0.2276 0.0256  0.0629  0.0207  48  SER A CB  
371  O  OG  . SER A 48  ? 0.2421 0.3046 0.2465 0.0182  0.0491  0.0700  48  SER A OG  
372  N  N   . VAL A 49  ? 0.2053 0.2982 0.1383 -0.0433 0.0350  -0.0190 49  VAL A N   
373  C  CA  . VAL A 49  ? 0.2523 0.2323 0.1500 -0.0178 0.0487  0.0032  49  VAL A CA  
374  C  C   . VAL A 49  ? 0.1918 0.2774 0.1677 -0.0606 0.0244  -0.0250 49  VAL A C   
375  O  O   . VAL A 49  ? 0.2370 0.3414 0.2481 -0.1276 0.0049  0.0046  49  VAL A O   
376  C  CB  . VAL A 49  ? 0.2734 0.2551 0.2174 0.0304  0.0680  -0.0287 49  VAL A CB  
377  C  CG1 . VAL A 49  ? 0.4066 0.2508 0.1807 -0.0151 0.0586  -0.0175 49  VAL A CG1 
378  C  CG2 . VAL A 49  ? 0.2540 0.3147 0.2280 -0.0220 0.0423  -0.0200 49  VAL A CG2 
379  N  N   . SER A 50  ? 0.1923 0.2396 0.1538 -0.0286 0.0433  0.0024  50  SER A N   
380  C  CA  . SER A 50  ? 0.1714 0.2551 0.2061 -0.0238 0.0254  -0.0320 50  SER A CA  
381  C  C   . SER A 50  ? 0.1388 0.2084 0.1829 -0.0005 0.0113  -0.0136 50  SER A C   
382  O  O   . SER A 50  ? 0.1745 0.2318 0.2241 -0.0313 -0.0055 0.0174  50  SER A O   
383  C  CB  . SER A 50  ? 0.2388 0.2946 0.3061 -0.0244 0.0977  -0.1042 50  SER A CB  
384  O  OG  . SER A 50  ? 0.2600 0.4433 0.3082 -0.0172 0.0405  -0.0624 50  SER A OG  
385  N  N   . TYR A 51  ? 0.1790 0.2237 0.1796 -0.0292 0.0100  -0.0284 51  TYR A N   
386  C  CA  . TYR A 51  ? 0.2044 0.2245 0.1559 0.0223  0.0106  0.0109  51  TYR A CA  
387  C  C   . TYR A 51  ? 0.1731 0.2206 0.1713 0.0237  0.0233  0.0225  51  TYR A C   
388  O  O   . TYR A 51  ? 0.1678 0.2030 0.1802 0.0248  0.0021  0.0087  51  TYR A O   
389  C  CB  . TYR A 51  ? 0.1587 0.2194 0.1790 0.0146  -0.0152 -0.0021 51  TYR A CB  
390  C  CG  . TYR A 51  ? 0.1537 0.1937 0.1321 -0.0201 0.0227  0.0023  51  TYR A CG  
391  C  CD1 . TYR A 51  ? 0.1532 0.1698 0.1577 -0.0017 0.0109  -0.0024 51  TYR A CD1 
392  C  CD2 . TYR A 51  ? 0.1673 0.2014 0.1234 0.0113  0.0161  0.0078  51  TYR A CD2 
393  C  CE1 . TYR A 51  ? 0.1558 0.1638 0.1433 -0.0189 0.0051  0.0152  51  TYR A CE1 
394  C  CE2 . TYR A 51  ? 0.1239 0.1774 0.1681 -0.0386 0.0109  0.0017  51  TYR A CE2 
395  C  CZ  . TYR A 51  ? 0.1336 0.1771 0.1792 -0.0157 0.0096  0.0091  51  TYR A CZ  
396  O  OH  . TYR A 51  ? 0.1327 0.1793 0.1389 -0.0081 0.0006  -0.0073 51  TYR A OH  
397  N  N   . ASP A 52  ? 0.1500 0.2446 0.2477 0.0025  0.0073  -0.0003 52  ASP A N   
398  C  CA  . ASP A 52  ? 0.1644 0.2622 0.2461 -0.0117 0.0120  0.0491  52  ASP A CA  
399  C  C   . ASP A 52  ? 0.2285 0.2163 0.2258 0.0013  0.0024  0.0002  52  ASP A C   
400  O  O   . ASP A 52  ? 0.2547 0.2529 0.2534 0.0201  -0.0245 0.0436  52  ASP A O   
401  C  CB  . ASP A 52  ? 0.1478 0.3976 0.3184 -0.0020 0.0718  0.1104  52  ASP A CB  
402  C  CG  . ASP A 52  ? 0.3233 0.4715 0.6457 0.1503  0.0225  -0.0833 52  ASP A CG  
403  O  OD1 . ASP A 52  ? 0.2410 0.5323 0.6912 0.0587  0.0836  -0.0719 52  ASP A OD1 
404  O  OD2 . ASP A 52  ? 0.6625 0.3589 0.9790 0.1107  -0.0923 0.0738  52  ASP A OD2 
405  N  N   . GLN A 53  ? 0.1721 0.1987 0.2680 0.0208  0.0566  0.0160  53  GLN A N   
406  C  CA  . GLN A 53  ? 0.1785 0.2120 0.2206 0.0044  0.0234  0.0150  53  GLN A CA  
407  C  C   . GLN A 53  ? 0.1923 0.1971 0.1430 0.0145  0.0022  0.0063  53  GLN A C   
408  O  O   . GLN A 53  ? 0.1736 0.1876 0.1955 0.0199  0.0118  0.0156  53  GLN A O   
409  C  CB  . GLN A 53  ? 0.2113 0.2285 0.2101 0.0476  0.0469  0.0097  53  GLN A CB  
410  C  CG  . GLN A 53  ? 0.1786 0.2965 0.2752 0.0314  0.0310  0.0107  53  GLN A CG  
411  C  CD  . GLN A 53  ? 0.2057 0.3911 0.2492 0.0303  0.0179  0.0995  53  GLN A CD  
412  O  OE1 . GLN A 53  ? 0.2500 0.4835 0.5136 -0.0616 0.0275  0.0670  53  GLN A OE1 
413  N  NE2 . GLN A 53  ? 0.2000 0.3021 0.2521 0.0079  0.0262  0.0682  53  GLN A NE2 
414  N  N   . ALA A 54  ? 0.1766 0.1972 0.1641 0.0154  0.0307  -0.0049 54  ALA A N   
415  C  CA  . ALA A 54  ? 0.1577 0.1779 0.1377 0.0227  0.0145  0.0098  54  ALA A CA  
416  C  C   . ALA A 54  ? 0.1615 0.1788 0.1444 0.0124  0.0179  -0.0156 54  ALA A C   
417  O  O   . ALA A 54  ? 0.1799 0.2405 0.1587 0.0023  0.0094  -0.0119 54  ALA A O   
418  C  CB  . ALA A 54  ? 0.1509 0.2094 0.1747 0.0272  0.0222  0.0370  54  ALA A CB  
419  N  N   . THR A 55  ? 0.1463 0.1597 0.1492 0.0310  0.0244  0.0110  55  THR A N   
420  C  CA  . THR A 55  ? 0.1576 0.1782 0.1400 0.0431  0.0204  0.0223  55  THR A CA  
421  C  C   . THR A 55  ? 0.1351 0.1490 0.1337 0.0109  0.0019  0.0264  55  THR A C   
422  O  O   . THR A 55  ? 0.1474 0.1592 0.1328 -0.0006 -0.0183 -0.0038 55  THR A O   
423  C  CB  . THR A 55  ? 0.1711 0.1833 0.1465 0.0407  0.0044  0.0150  55  THR A CB  
424  O  OG1 . THR A 55  ? 0.1653 0.2137 0.1846 0.0262  0.0005  0.0055  55  THR A OG1 
425  C  CG2 . THR A 55  ? 0.2117 0.1896 0.1257 0.0178  -0.0113 0.0155  55  THR A CG2 
426  N  N   . SER A 56  ? 0.1468 0.1388 0.1237 0.0152  -0.0075 0.0194  56  SER A N   
427  C  CA  . SER A 56  ? 0.1379 0.1509 0.1238 0.0128  0.0172  0.0163  56  SER A CA  
428  C  C   . SER A 56  ? 0.1458 0.1423 0.1167 0.0088  0.0039  0.0147  56  SER A C   
429  O  O   . SER A 56  ? 0.1741 0.1368 0.1261 0.0197  -0.0087 0.0135  56  SER A O   
430  C  CB  . SER A 56  ? 0.1608 0.1427 0.1177 0.0122  -0.0127 0.0040  56  SER A CB  
431  O  OG  . SER A 56  ? 0.1626 0.1459 0.1319 0.0054  -0.0083 0.0062  56  SER A OG  
432  N  N   . LEU A 57  ? 0.1482 0.1458 0.1350 0.0102  0.0118  0.0092  57  LEU A N   
433  C  CA  . LEU A 57  ? 0.1632 0.1450 0.1342 -0.0040 0.0154  0.0142  57  LEU A CA  
434  C  C   . LEU A 57  ? 0.1849 0.1450 0.0935 0.0057  0.0079  0.0107  57  LEU A C   
435  O  O   . LEU A 57  ? 0.2230 0.1659 0.0955 0.0144  0.0034  0.0166  57  LEU A O   
436  C  CB  . LEU A 57  ? 0.2011 0.1546 0.1675 -0.0198 0.0135  0.0102  57  LEU A CB  
437  C  CG  . LEU A 57  ? 0.1854 0.1923 0.1492 -0.0094 0.0223  -0.0128 57  LEU A CG  
438  C  CD1 . LEU A 57  ? 0.2083 0.2076 0.2208 -0.0442 0.0189  -0.0026 57  LEU A CD1 
439  C  CD2 . LEU A 57  ? 0.2400 0.1688 0.1879 0.0012  -0.0088 0.0232  57  LEU A CD2 
440  N  N   . ARG A 58  ? 0.1581 0.1417 0.1303 0.0165  0.0049  0.0172  58  ARG A N   
441  C  CA  . ARG A 58  ? 0.1814 0.1364 0.1425 0.0065  0.0214  0.0211  58  ARG A CA  
442  C  C   . ARG A 58  ? 0.1395 0.1533 0.0949 0.0089  0.0127  0.0245  58  ARG A C   
443  O  O   . ARG A 58  ? 0.1786 0.1588 0.0941 0.0010  0.0052  0.0176  58  ARG A O   
444  C  CB  . ARG A 58  ? 0.1890 0.1743 0.1663 -0.0031 0.0665  0.0310  58  ARG A CB  
445  C  CG  . ARG A 58  ? 0.2656 0.2583 0.2364 -0.0164 0.0619  0.1107  58  ARG A CG  
446  C  CD  . ARG A 58  ? 0.3347 0.2999 0.3298 -0.0344 0.1808  0.0622  58  ARG A CD  
447  N  NE  . ARG A 58  ? 0.4916 0.2630 0.2902 -0.0447 0.1802  0.0679  58  ARG A NE  
448  C  CZ  . ARG A 58  ? 0.3179 0.2870 0.3007 0.0419  0.1398  0.1009  58  ARG A CZ  
449  N  NH1 . ARG A 58  ? 0.4203 0.2569 0.3270 0.0775  0.1546  0.1044  58  ARG A NH1 
450  N  NH2 . ARG A 58  ? 0.3786 0.4062 0.3937 0.0820  0.1169  0.2060  58  ARG A NH2 
451  N  N   . ILE A 59  ? 0.1419 0.1524 0.0979 0.0010  0.0154  0.0189  59  ILE A N   
452  C  CA  . ILE A 59  ? 0.1367 0.1406 0.1224 0.0073  0.0152  0.0109  59  ILE A CA  
453  C  C   . ILE A 59  ? 0.1583 0.1529 0.1034 0.0029  0.0318  0.0192  59  ILE A C   
454  O  O   . ILE A 59  ? 0.1516 0.1632 0.1058 -0.0060 0.0173  0.0192  59  ILE A O   
455  C  CB  . ILE A 59  ? 0.1594 0.1527 0.0856 0.0006  0.0052  0.0320  59  ILE A CB  
456  C  CG1 . ILE A 59  ? 0.1650 0.1391 0.1327 0.0009  0.0104  0.0345  59  ILE A CG1 
457  C  CG2 . ILE A 59  ? 0.1632 0.1742 0.0907 0.0093  0.0002  0.0072  59  ILE A CG2 
458  C  CD1 . ILE A 59  ? 0.1628 0.1547 0.1514 -0.0125 0.0220  0.0152  59  ILE A CD1 
459  N  N   . LEU A 60  ? 0.1324 0.1500 0.1444 0.0158  0.0354  0.0006  60  LEU A N   
460  C  CA  . LEU A 60  ? 0.1280 0.1782 0.1559 0.0063  0.0297  0.0137  60  LEU A CA  
461  C  C   . LEU A 60  ? 0.1333 0.1671 0.1068 0.0040  0.0141  -0.0125 60  LEU A C   
462  O  O   . LEU A 60  ? 0.1874 0.2061 0.1124 0.0381  0.0347  0.0019  60  LEU A O   
463  C  CB  . LEU A 60  ? 0.1807 0.2150 0.2132 -0.0366 0.0222  -0.0004 60  LEU A CB  
464  C  CG  . LEU A 60  ? 0.2406 0.1745 0.2260 -0.0629 0.0661  -0.0491 60  LEU A CG  
465  C  CD1 . LEU A 60  ? 0.2443 0.5999 0.4259 0.1065  -0.0449 -0.1136 60  LEU A CD1 
466  C  CD2 . LEU A 60  ? 0.5353 0.2292 0.5622 0.0541  0.0511  -0.0637 60  LEU A CD2 
467  N  N   . ASN A 61  ? 0.1430 0.1509 0.1198 -0.0005 0.0283  -0.0189 61  ASN A N   
468  C  CA  . ASN A 61  ? 0.1326 0.1564 0.1400 0.0047  0.0124  -0.0348 61  ASN A CA  
469  C  C   . ASN A 61  ? 0.1523 0.1599 0.1165 -0.0070 0.0122  -0.0127 61  ASN A C   
470  O  O   . ASN A 61  ? 0.1549 0.1973 0.1414 -0.0107 0.0126  -0.0012 61  ASN A O   
471  C  CB  . ASN A 61  ? 0.1502 0.1341 0.1542 0.0100  0.0311  -0.0237 61  ASN A CB  
472  C  CG  . ASN A 61  ? 0.1309 0.1569 0.1421 -0.0143 0.0106  -0.0089 61  ASN A CG  
473  O  OD1 . ASN A 61  ? 0.1357 0.2037 0.1560 -0.0095 0.0190  -0.0365 61  ASN A OD1 
474  N  ND2 . ASN A 61  ? 0.1653 0.1727 0.1608 -0.0013 0.0217  -0.0414 61  ASN A ND2 
475  N  N   . ASN A 62  ? 0.1304 0.2000 0.1239 -0.0086 0.0027  -0.0369 62  ASN A N   
476  C  CA  . ASN A 62  ? 0.1492 0.1828 0.1817 -0.0195 -0.0048 -0.0359 62  ASN A CA  
477  C  C   . ASN A 62  ? 0.1562 0.2029 0.1499 -0.0212 0.0016  -0.0130 62  ASN A C   
478  O  O   . ASN A 62  ? 0.1483 0.2464 0.2303 -0.0399 -0.0100 -0.0445 62  ASN A O   
479  C  CB  . ASN A 62  ? 0.1911 0.1749 0.1606 -0.0080 0.0104  -0.0122 62  ASN A CB  
480  C  CG  . ASN A 62  ? 0.1984 0.1774 0.1289 0.0027  -0.0018 -0.0335 62  ASN A CG  
481  O  OD1 . ASN A 62  ? 0.1770 0.1864 0.1278 -0.0084 0.0222  -0.0201 62  ASN A OD1 
482  N  ND2 . ASN A 62  ? 0.2242 0.2048 0.2606 -0.0121 0.0756  -0.0429 62  ASN A ND2 
483  N  N   . GLY A 63  ? 0.1553 0.1940 0.1680 -0.0039 0.0192  -0.0291 63  GLY A N   
484  C  CA  . GLY A 63  ? 0.1381 0.2235 0.2226 0.0118  0.0020  -0.0294 63  GLY A CA  
485  C  C   . GLY A 63  ? 0.1460 0.2252 0.1944 0.0337  -0.0062 -0.0510 63  GLY A C   
486  O  O   . GLY A 63  ? 0.1962 0.2518 0.2008 0.0550  -0.0164 -0.0274 63  GLY A O   
487  N  N   A HIS A 64  ? 0.1594 0.1847 0.1569 -0.0149 0.0042  -0.0262 64  HIS A N   
488  N  N   B HIS A 64  ? 0.1436 0.2489 0.1764 -0.0195 0.0157  -0.0397 64  HIS A N   
489  C  CA  A HIS A 64  ? 0.1490 0.2209 0.1477 -0.0064 -0.0171 -0.0238 64  HIS A CA  
490  C  CA  B HIS A 64  ? 0.1815 0.2737 0.2004 -0.0337 0.0033  -0.0194 64  HIS A CA  
491  C  C   A HIS A 64  ? 0.1451 0.1881 0.1181 -0.0012 -0.0188 -0.0298 64  HIS A C   
492  C  C   B HIS A 64  ? 0.1446 0.2212 0.1839 0.0150  0.0134  0.0291  64  HIS A C   
493  O  O   A HIS A 64  ? 0.1304 0.1797 0.1304 0.0205  0.0052  -0.0424 64  HIS A O   
494  O  O   B HIS A 64  ? 0.1714 0.2213 0.2838 -0.0450 -0.0194 0.0332  64  HIS A O   
495  C  CB  A HIS A 64  ? 0.1716 0.2226 0.1216 0.0061  -0.0394 -0.0062 64  HIS A CB  
496  C  CB  B HIS A 64  ? 0.2492 0.4088 0.1599 -0.0527 -0.0257 -0.0358 64  HIS A CB  
497  C  CG  A HIS A 64  ? 0.1265 0.2138 0.0993 0.0043  -0.0363 0.0021  64  HIS A CG  
498  C  CG  B HIS A 64  ? 0.3028 0.3671 0.2600 -0.0908 -0.0188 -0.1013 64  HIS A CG  
499  N  ND1 A HIS A 64  ? 0.2285 0.2073 0.1086 -0.0121 -0.0361 -0.0223 64  HIS A ND1 
500  N  ND1 B HIS A 64  ? 0.3697 0.3606 0.2008 -0.0332 0.0589  -0.0216 64  HIS A ND1 
501  C  CD2 A HIS A 64  ? 0.2213 0.1958 0.0702 0.0193  -0.0023 -0.0141 64  HIS A CD2 
502  C  CD2 B HIS A 64  ? 0.3416 0.3708 0.1465 -0.0351 -0.0074 -0.0296 64  HIS A CD2 
503  C  CE1 A HIS A 64  ? 0.2396 0.2177 0.0882 -0.0267 -0.0395 -0.0737 64  HIS A CE1 
504  C  CE1 B HIS A 64  ? 0.1606 0.4694 0.3682 -0.0315 0.0421  -0.0632 64  HIS A CE1 
505  N  NE2 A HIS A 64  ? 0.2950 0.1962 0.1315 -0.0048 -0.0082 -0.0394 64  HIS A NE2 
506  N  NE2 B HIS A 64  ? 0.3373 0.3535 0.2922 -0.0731 0.0204  -0.1135 64  HIS A NE2 
507  N  N   . SER A 65  ? 0.1353 0.1717 0.1461 -0.0080 -0.0031 0.0051  65  SER A N   
508  C  CA  . SER A 65  ? 0.1434 0.1826 0.1156 -0.0263 0.0004  0.0113  65  SER A CA  
509  C  C   . SER A 65  ? 0.1452 0.1711 0.0991 -0.0120 -0.0067 -0.0366 65  SER A C   
510  O  O   . SER A 65  ? 0.1564 0.1969 0.1461 -0.0052 0.0027  0.0022  65  SER A O   
511  C  CB  . SER A 65  ? 0.1965 0.3186 0.0553 -0.0458 -0.0132 0.0359  65  SER A CB  
512  O  OG  . SER A 65  ? 0.2168 0.2472 0.1404 -0.0011 0.0107  0.0178  65  SER A OG  
513  N  N   . PHE A 66  ? 0.1288 0.1597 0.1421 0.0240  -0.0001 -0.0130 66  PHE A N   
514  C  CA  . PHE A 66  ? 0.1478 0.1662 0.1066 0.0190  0.0159  -0.0077 66  PHE A CA  
515  C  C   . PHE A 66  ? 0.1619 0.1673 0.0791 0.0206  0.0152  -0.0204 66  PHE A C   
516  O  O   . PHE A 66  ? 0.1577 0.1580 0.0950 0.0214  0.0048  -0.0079 66  PHE A O   
517  C  CB  . PHE A 66  ? 0.1564 0.1546 0.1675 0.0109  -0.0288 -0.0212 66  PHE A CB  
518  C  CG  . PHE A 66  ? 0.1549 0.1815 0.0970 0.0219  -0.0173 -0.0269 66  PHE A CG  
519  C  CD1 . PHE A 66  ? 0.1500 0.1714 0.1265 0.0040  -0.0217 -0.0369 66  PHE A CD1 
520  C  CD2 . PHE A 66  ? 0.1797 0.1671 0.1244 0.0201  -0.0044 -0.0217 66  PHE A CD2 
521  C  CE1 . PHE A 66  ? 0.1525 0.2005 0.1464 -0.0059 -0.0253 -0.0091 66  PHE A CE1 
522  C  CE2 . PHE A 66  ? 0.1960 0.2075 0.1462 -0.0005 -0.0157 -0.0139 66  PHE A CE2 
523  C  CZ  . PHE A 66  ? 0.1680 0.1829 0.1653 -0.0125 -0.0214 -0.0108 66  PHE A CZ  
524  N  N   . LYS A 67  ? 0.1632 0.1525 0.0818 0.0172  0.0168  -0.0186 67  LYS A N   
525  C  CA  . LYS A 67  ? 0.1650 0.1718 0.1044 0.0428  -0.0060 -0.0074 67  LYS A CA  
526  C  C   . LYS A 67  ? 0.1310 0.1649 0.0713 0.0059  0.0109  0.0143  67  LYS A C   
527  O  O   . LYS A 67  ? 0.1742 0.2162 0.0705 0.0344  0.0269  0.0147  67  LYS A O   
528  C  CB  . LYS A 67  ? 0.1634 0.2149 0.1989 0.0435  -0.0517 -0.0680 67  LYS A CB  
529  C  CG  . LYS A 67  ? 0.1984 0.1961 0.1808 0.0133  -0.0174 -0.0489 67  LYS A CG  
530  C  CD  . LYS A 67  ? 0.2278 0.1858 0.1979 -0.0218 0.0036  -0.0133 67  LYS A CD  
531  C  CE  . LYS A 67  ? 0.2856 0.2477 0.2102 -0.0031 -0.0052 -0.0146 67  LYS A CE  
532  N  NZ  . LYS A 67  ? 0.2971 0.2077 0.3008 0.0077  0.0251  -0.0498 67  LYS A NZ  
533  N  N   . VAL A 68  ? 0.1208 0.1351 0.1064 0.0042  0.0054  -0.0044 68  VAL A N   
534  C  CA  . VAL A 68  ? 0.1456 0.1476 0.0930 0.0189  -0.0046 -0.0132 68  VAL A CA  
535  C  C   . VAL A 68  ? 0.1417 0.1292 0.0833 0.0211  0.0017  0.0006  68  VAL A C   
536  O  O   . VAL A 68  ? 0.1540 0.1382 0.0917 0.0241  0.0141  -0.0027 68  VAL A O   
537  C  CB  . VAL A 68  ? 0.1523 0.1372 0.0952 0.0138  0.0012  -0.0025 68  VAL A CB  
538  C  CG1 . VAL A 68  ? 0.1588 0.1738 0.1584 0.0379  -0.0257 -0.0023 68  VAL A CG1 
539  C  CG2 . VAL A 68  ? 0.1524 0.1583 0.1056 0.0063  0.0195  -0.0206 68  VAL A CG2 
540  N  N   . GLU A 69  ? 0.1390 0.1438 0.1167 0.0188  0.0042  0.0172  69  GLU A N   
541  C  CA  . GLU A 69  ? 0.1439 0.1295 0.1190 0.0087  0.0027  0.0146  69  GLU A CA  
542  C  C   . GLU A 69  ? 0.1455 0.1190 0.1297 0.0115  -0.0145 -0.0038 69  GLU A C   
543  O  O   . GLU A 69  ? 0.1677 0.1728 0.0991 0.0344  -0.0128 0.0059  69  GLU A O   
544  C  CB  . GLU A 69  ? 0.1666 0.1434 0.2303 -0.0046 0.0531  0.0211  69  GLU A CB  
545  C  CG  . GLU A 69  ? 0.1621 0.3140 0.4882 0.0279  0.0197  0.0183  69  GLU A CG  
546  C  CD  . GLU A 69  ? 0.3545 0.3128 0.2949 -0.0687 0.0142  0.1113  69  GLU A CD  
547  O  OE1 . GLU A 69  ? 0.3606 0.4745 0.4005 -0.0370 0.2008  0.1289  69  GLU A OE1 
548  O  OE2 . GLU A 69  ? 0.2634 0.3661 0.4346 -0.0200 -0.0039 -0.0379 69  GLU A OE2 
549  N  N   . PHE A 70  ? 0.1459 0.1254 0.1134 0.0157  0.0047  0.0044  70  PHE A N   
550  C  CA  . PHE A 70  ? 0.1374 0.1252 0.1074 0.0125  0.0063  0.0000  70  PHE A CA  
551  C  C   . PHE A 70  ? 0.1512 0.1331 0.1062 0.0006  -0.0031 -0.0050 70  PHE A C   
552  O  O   . PHE A 70  ? 0.1524 0.1743 0.1153 -0.0057 -0.0017 0.0044  70  PHE A O   
553  C  CB  . PHE A 70  ? 0.1582 0.1437 0.0969 0.0099  0.0131  0.0042  70  PHE A CB  
554  C  CG  . PHE A 70  ? 0.1333 0.1469 0.0900 0.0141  0.0174  0.0032  70  PHE A CG  
555  C  CD1 . PHE A 70  ? 0.1538 0.1566 0.1178 0.0176  0.0247  0.0314  70  PHE A CD1 
556  C  CD2 . PHE A 70  ? 0.1410 0.1707 0.1059 -0.0012 0.0040  0.0058  70  PHE A CD2 
557  C  CE1 . PHE A 70  ? 0.1714 0.1534 0.1702 0.0168  0.0545  0.0351  70  PHE A CE1 
558  C  CE2 . PHE A 70  ? 0.1674 0.1663 0.0935 -0.0026 -0.0004 0.0247  70  PHE A CE2 
559  C  CZ  . PHE A 70  ? 0.1815 0.1703 0.1357 0.0060  0.0247  0.0281  70  PHE A CZ  
560  N  N   A ASP A 71  ? 0.1727 0.1321 0.1151 0.0081  -0.0152 -0.0002 71  ASP A N   
561  N  N   B ASP A 71  ? 0.1741 0.1354 0.1351 0.0095  -0.0179 0.0048  71  ASP A N   
562  C  CA  A ASP A 71  ? 0.1760 0.1252 0.1192 0.0038  -0.0047 0.0027  71  ASP A CA  
563  C  CA  B ASP A 71  ? 0.1646 0.1304 0.1600 0.0078  0.0079  0.0098  71  ASP A CA  
564  C  C   A ASP A 71  ? 0.1770 0.1208 0.1332 0.0000  0.0390  -0.0001 71  ASP A C   
565  C  C   B ASP A 71  ? 0.1912 0.1125 0.1599 -0.0009 0.0127  0.0171  71  ASP A C   
566  O  O   A ASP A 71  ? 0.1793 0.1621 0.1495 -0.0120 0.0484  0.0181  71  ASP A O   
567  O  O   B ASP A 71  ? 0.1829 0.1613 0.1973 -0.0216 0.0209  0.0134  71  ASP A O   
568  C  CB  A ASP A 71  ? 0.1851 0.1333 0.1764 0.0302  -0.0353 -0.0158 71  ASP A CB  
569  C  CB  B ASP A 71  ? 0.1824 0.1736 0.1851 0.0150  -0.0076 0.0413  71  ASP A CB  
570  C  CG  A ASP A 71  ? 0.2528 0.1416 0.2064 0.0157  -0.0776 0.0121  71  ASP A CG  
571  C  CG  B ASP A 71  ? 0.2396 0.1777 0.3003 0.0255  -0.0916 0.0283  71  ASP A CG  
572  O  OD1 A ASP A 71  ? 0.2385 0.1435 0.1847 0.0250  -0.0308 -0.0122 71  ASP A OD1 
573  O  OD1 B ASP A 71  ? 0.1696 0.1685 0.1777 0.0270  -0.0015 0.0566  71  ASP A OD1 
574  O  OD2 A ASP A 71  ? 0.2043 0.1678 0.1295 0.0160  -0.0038 0.0088  71  ASP A OD2 
575  O  OD2 B ASP A 71  ? 0.2421 0.2294 0.3323 0.0534  -0.0620 0.0457  71  ASP A OD2 
576  N  N   . ASP A 72  ? 0.1835 0.1222 0.1120 0.0040  0.0136  0.0135  72  ASP A N   
577  C  CA  . ASP A 72  ? 0.2346 0.1222 0.1104 0.0063  0.0094  0.0268  72  ASP A CA  
578  C  C   . ASP A 72  ? 0.1894 0.1301 0.1355 0.0037  0.0055  0.0060  72  ASP A C   
579  O  O   . ASP A 72  ? 0.2497 0.1393 0.1543 0.0061  -0.0221 -0.0006 72  ASP A O   
580  C  CB  . ASP A 72  ? 0.2037 0.1605 0.0951 0.0071  -0.0048 0.0082  72  ASP A CB  
581  C  CG  . ASP A 72  ? 0.2145 0.1521 0.1464 0.0136  -0.0075 -0.0117 72  ASP A CG  
582  O  OD1 . ASP A 72  ? 0.2188 0.2026 0.1617 -0.0015 -0.0227 0.0298  72  ASP A OD1 
583  O  OD2 . ASP A 72  ? 0.2367 0.1876 0.1244 0.0066  -0.0334 0.0156  72  ASP A OD2 
584  N  N   . SER A 73  ? 0.2169 0.1210 0.1615 0.0066  -0.0163 0.0128  73  SER A N   
585  C  CA  . SER A 73  ? 0.2336 0.1284 0.1725 -0.0072 0.0058  -0.0063 73  SER A CA  
586  C  C   . SER A 73  ? 0.2397 0.1289 0.2294 0.0195  -0.0245 -0.0150 73  SER A C   
587  O  O   . SER A 73  ? 0.3175 0.1257 0.1962 0.0335  -0.0427 -0.0157 73  SER A O   
588  C  CB  . SER A 73  ? 0.2809 0.1618 0.1851 -0.0037 -0.0162 0.0217  73  SER A CB  
589  O  OG  . SER A 73  ? 0.2842 0.1386 0.1854 0.0242  -0.0245 0.0285  73  SER A OG  
590  N  N   . GLN A 74  ? 0.2257 0.1481 0.2000 0.0022  0.0009  -0.0091 74  GLN A N   
591  C  CA  . GLN A 74  ? 0.2633 0.2288 0.2130 0.0324  0.0326  0.0053  74  GLN A CA  
592  C  C   . GLN A 74  ? 0.2330 0.2600 0.1919 -0.0194 -0.0022 -0.0471 74  GLN A C   
593  O  O   . GLN A 74  ? 0.2144 0.2227 0.1980 -0.0281 -0.0148 0.0135  74  GLN A O   
594  C  CB  . GLN A 74  ? 0.2751 0.3087 0.3556 0.0878  -0.0121 0.0732  74  GLN A CB  
595  C  CG  . GLN A 74  ? 0.5154 0.2040 0.4325 -0.0362 -0.0204 0.0522  74  GLN A CG  
596  C  CD  . GLN A 74  ? 0.3301 0.3733 0.5389 -0.1635 -0.0581 0.0184  74  GLN A CD  
597  O  OE1 . GLN A 74  ? 0.2436 0.4528 0.3732 0.0430  -0.0535 0.0431  74  GLN A OE1 
598  N  NE2 . GLN A 74  ? 0.2532 0.3140 0.4782 -0.0825 -0.1271 0.1535  74  GLN A NE2 
599  N  N   A ASP A 75  ? 0.2627 0.3499 0.2706 -0.0722 0.0460  -0.1342 75  ASP A N   
600  N  N   B ASP A 75  ? 0.2645 0.2658 0.2310 -0.0369 0.0242  -0.1064 75  ASP A N   
601  C  CA  A ASP A 75  ? 0.2352 0.4032 0.3750 -0.0768 -0.0257 -0.0583 75  ASP A CA  
602  C  CA  B ASP A 75  ? 0.2590 0.2463 0.3075 0.0400  0.0337  -0.0323 75  ASP A CA  
603  C  C   A ASP A 75  ? 0.2134 0.3606 0.3036 -0.0452 -0.0423 -0.0263 75  ASP A C   
604  C  C   B ASP A 75  ? 0.1951 0.2995 0.2911 -0.0002 -0.0017 0.0041  75  ASP A C   
605  O  O   A ASP A 75  ? 0.2505 0.4688 0.1433 -0.0609 0.0234  -0.0369 75  ASP A O   
606  O  O   B ASP A 75  ? 0.2518 0.1996 0.1739 0.0132  -0.0259 0.0087  75  ASP A O   
607  C  CB  A ASP A 75  ? 0.2806 0.4873 0.4149 -0.0461 0.0343  -0.0680 75  ASP A CB  
608  C  CB  B ASP A 75  ? 0.2764 0.1671 0.2235 0.0268  0.0106  0.0182  75  ASP A CB  
609  C  CG  A ASP A 75  ? 0.3988 0.3445 0.4735 0.1242  -0.0489 -0.0996 75  ASP A CG  
610  C  CG  B ASP A 75  ? 0.3100 0.2144 0.2570 0.0616  0.0507  0.0527  75  ASP A CG  
611  O  OD1 A ASP A 75  ? 0.2166 0.3126 0.1775 0.0399  0.0137  -0.0597 75  ASP A OD1 
612  O  OD1 B ASP A 75  ? 0.1955 0.2177 0.3365 0.0370  -0.0402 0.0342  75  ASP A OD1 
613  O  OD2 A ASP A 75  ? 0.5543 0.3442 0.5870 0.2282  0.1852  -0.0955 75  ASP A OD2 
614  O  OD2 B ASP A 75  ? 0.3926 0.3240 0.2600 0.0983  0.1053  0.0683  75  ASP A OD2 
615  N  N   . LYS A 76  ? 0.1560 0.2906 0.2555 0.0241  0.0068  0.0926  76  LYS A N   
616  C  CA  . LYS A 76  ? 0.2457 0.2087 0.4989 -0.0225 0.0300  -0.0027 76  LYS A CA  
617  C  C   . LYS A 76  ? 0.2856 0.3507 0.4537 0.0107  -0.0643 0.1516  76  LYS A C   
618  O  O   . LYS A 76  ? 0.3273 0.5912 0.6317 -0.1459 -0.0950 0.1636  76  LYS A O   
619  C  CB  . LYS A 76  ? 0.4177 0.2456 0.3280 0.0189  -0.1485 -0.0190 76  LYS A CB  
620  C  CG  . LYS A 76  ? 0.4522 0.3126 0.4223 -0.0293 -0.0630 0.0586  76  LYS A CG  
621  C  CD  . LYS A 76  ? 0.3421 0.3122 0.4234 -0.0509 -0.1151 -0.0961 76  LYS A CD  
622  C  CE  . LYS A 76  ? 0.2465 0.3173 0.6308 0.1289  0.0082  0.0697  76  LYS A CE  
623  N  NZ  . LYS A 76  ? 0.6210 0.2417 0.5409 0.0644  -0.1122 -0.0355 76  LYS A NZ  
624  N  N   . ALA A 77  ? 0.2220 0.3042 0.2785 0.0372  -0.0702 0.0203  77  ALA A N   
625  C  CA  . ALA A 77  ? 0.2263 0.2874 0.1418 -0.0103 0.0398  0.0318  77  ALA A CA  
626  C  C   . ALA A 77  ? 0.1518 0.1987 0.2476 0.0395  -0.0234 -0.0268 77  ALA A C   
627  O  O   . ALA A 77  ? 0.1696 0.3391 0.3442 0.0073  0.0044  -0.1163 77  ALA A O   
628  C  CB  . ALA A 77  ? 0.2440 0.2111 0.1923 0.0312  0.0221  0.0479  77  ALA A CB  
629  N  N   . VAL A 78  ? 0.1856 0.1635 0.2118 0.0100  -0.0195 0.0278  78  VAL A N   
630  C  CA  . VAL A 78  ? 0.2484 0.1941 0.2161 0.0251  -0.0601 0.0425  78  VAL A CA  
631  C  C   . VAL A 78  ? 0.1885 0.2159 0.1785 -0.0352 -0.0337 -0.0027 78  VAL A C   
632  O  O   . VAL A 78  ? 0.2084 0.2079 0.2244 -0.0298 -0.0411 0.0263  78  VAL A O   
633  C  CB  . VAL A 78  ? 0.3983 0.2630 0.2124 0.0364  0.0177  -0.0087 78  VAL A CB  
634  C  CG1 . VAL A 78  ? 0.4895 0.1882 0.4142 -0.0384 -0.0559 0.0451  78  VAL A CG1 
635  C  CG2 . VAL A 78  ? 0.3832 0.3865 0.2489 0.0254  0.0077  -0.0663 78  VAL A CG2 
636  N  N   . LEU A 79  ? 0.1865 0.2140 0.1542 0.0231  -0.0212 0.0078  79  LEU A N   
637  C  CA  . LEU A 79  ? 0.1662 0.2186 0.1301 -0.0051 0.0072  -0.0076 79  LEU A CA  
638  C  C   . LEU A 79  ? 0.2235 0.1976 0.1720 -0.0219 0.0188  -0.0258 79  LEU A C   
639  O  O   . LEU A 79  ? 0.2166 0.2034 0.1821 -0.0377 0.0128  -0.0179 79  LEU A O   
640  C  CB  . LEU A 79  ? 0.1418 0.2515 0.1743 -0.0245 0.0027  0.0073  79  LEU A CB  
641  C  CG  . LEU A 79  ? 0.1822 0.1998 0.2108 0.0318  0.0008  -0.0146 79  LEU A CG  
642  C  CD1 . LEU A 79  ? 0.1760 0.2514 0.3667 -0.0197 0.0560  0.0348  79  LEU A CD1 
643  C  CD2 . LEU A 79  ? 0.1881 0.2357 0.2252 0.0230  0.0538  -0.0067 79  LEU A CD2 
644  N  N   . LYS A 80  ? 0.2181 0.2134 0.1547 -0.0075 0.0179  0.0027  80  LYS A N   
645  C  CA  . LYS A 80  ? 0.2518 0.2227 0.1923 -0.0037 0.0366  -0.0248 80  LYS A CA  
646  C  C   . LYS A 80  ? 0.1984 0.2136 0.2249 0.0380  0.0714  -0.0155 80  LYS A C   
647  O  O   . LYS A 80  ? 0.1901 0.2344 0.1752 0.0019  0.0168  -0.0166 80  LYS A O   
648  C  CB  . LYS A 80  ? 0.2431 0.2694 0.3019 0.0339  0.0136  0.0325  80  LYS A CB  
649  C  CG  . LYS A 80  ? 0.2590 0.2895 0.3646 0.0425  0.0208  -0.0910 80  LYS A CG  
650  C  CD  . LYS A 80  ? 0.4814 0.2932 0.4874 0.1098  -0.0059 0.0418  80  LYS A CD  
651  C  CE  . LYS A 80  ? 0.5156 0.5707 0.7833 0.0675  0.0170  -0.0383 80  LYS A CE  
652  N  N   . GLY A 81  ? 0.2737 0.2579 0.2192 0.0478  0.0792  -0.0280 81  GLY A N   
653  C  CA  . GLY A 81  ? 0.2939 0.2637 0.2691 0.0560  0.1002  0.0148  81  GLY A CA  
654  C  C   . GLY A 81  ? 0.2530 0.2669 0.2688 0.0351  0.1175  -0.0203 81  GLY A C   
655  O  O   . GLY A 81  ? 0.2256 0.2738 0.1944 0.0015  0.0691  -0.0289 81  GLY A O   
656  N  N   . GLY A 82  ? 0.3003 0.2583 0.3423 0.0541  0.1057  0.0587  82  GLY A N   
657  C  CA  . GLY A 82  ? 0.3118 0.2091 0.4399 0.0381  0.0845  0.0372  82  GLY A CA  
658  C  C   . GLY A 82  ? 0.3308 0.2432 0.3241 0.0583  0.1684  -0.0251 82  GLY A C   
659  O  O   . GLY A 82  ? 0.3948 0.3626 0.2328 0.1295  0.1488  -0.0004 82  GLY A O   
660  N  N   . PRO A 83  ? 0.2909 0.2066 0.2558 0.0223  0.1163  0.0148  83  PRO A N   
661  C  CA  . PRO A 83  ? 0.3032 0.2364 0.2409 0.0695  0.0514  -0.0158 83  PRO A CA  
662  C  C   . PRO A 83  ? 0.3233 0.2831 0.1684 0.0281  0.0449  -0.0039 83  PRO A C   
663  O  O   . PRO A 83  ? 0.3136 0.3029 0.3031 0.0591  0.0269  -0.0223 83  PRO A O   
664  C  CB  . PRO A 83  ? 0.3078 0.2366 0.1914 0.0798  0.0387  0.0074  83  PRO A CB  
665  C  CG  . PRO A 83  ? 0.2573 0.2644 0.1973 0.0469  0.0359  -0.0067 83  PRO A CG  
666  C  CD  . PRO A 83  ? 0.2730 0.2212 0.2339 0.0089  0.0665  -0.0318 83  PRO A CD  
667  N  N   . LEU A 84  ? 0.2896 0.1840 0.1650 0.0339  0.0597  -0.0199 84  LEU A N   
668  C  CA  . LEU A 84  ? 0.2691 0.1778 0.2070 0.0006  0.0361  -0.0258 84  LEU A CA  
669  C  C   . LEU A 84  ? 0.2429 0.2080 0.2199 0.0243  0.0168  -0.0238 84  LEU A C   
670  O  O   . LEU A 84  ? 0.2856 0.2327 0.2131 0.0364  0.0741  -0.0612 84  LEU A O   
671  C  CB  . LEU A 84  ? 0.2253 0.2134 0.1950 0.0530  0.0563  -0.0147 84  LEU A CB  
672  C  CG  . LEU A 84  ? 0.1990 0.1843 0.1415 0.0187  0.0179  -0.0120 84  LEU A CG  
673  C  CD1 . LEU A 84  ? 0.2468 0.2109 0.1304 0.0579  0.0182  0.0032  84  LEU A CD1 
674  C  CD2 . LEU A 84  ? 0.1890 0.1847 0.1669 0.0039  0.0060  -0.0270 84  LEU A CD2 
675  N  N   . ASP A 85  ? 0.3556 0.1890 0.2269 -0.0027 0.0801  -0.0465 85  ASP A N   
676  C  CA  . ASP A 85  ? 0.3510 0.2000 0.2561 0.0227  0.0288  -0.0482 85  ASP A CA  
677  C  C   . ASP A 85  ? 0.2924 0.1785 0.3195 -0.0027 -0.0173 0.0282  85  ASP A C   
678  O  O   . ASP A 85  ? 0.3431 0.2749 0.3426 0.0549  0.0166  -0.0658 85  ASP A O   
679  C  CB  . ASP A 85  ? 0.4196 0.3078 0.2375 0.0739  -0.0179 -0.0697 85  ASP A CB  
680  C  CG  . ASP A 85  ? 0.3959 0.3392 0.3700 0.0441  0.0092  0.0826  85  ASP A CG  
681  O  OD1 . ASP A 85  ? 0.4037 0.6740 0.3802 -0.0212 0.0429  0.0534  85  ASP A OD1 
682  O  OD2 . ASP A 85  ? 0.4383 0.4472 0.3427 -0.0564 -0.0812 0.0688  85  ASP A OD2 
683  N  N   . GLY A 86  ? 0.3033 0.2536 0.3248 0.0163  -0.0158 0.0590  86  GLY A N   
684  C  CA  . GLY A 86  ? 0.4124 0.2366 0.2136 0.0155  0.0606  -0.0223 86  GLY A CA  
685  C  C   . GLY A 86  ? 0.3935 0.2380 0.2451 -0.0128 0.0835  -0.0449 86  GLY A C   
686  O  O   . GLY A 86  ? 0.3334 0.3366 0.3672 -0.0677 -0.0063 0.0663  86  GLY A O   
687  N  N   A THR A 87  ? 0.3256 0.2977 0.2319 0.0317  0.0910  -0.0529 87  THR A N   
688  N  N   B THR A 87  ? 0.2978 0.2486 0.2087 0.0204  0.0547  -0.0641 87  THR A N   
689  C  CA  A THR A 87  ? 0.2400 0.2536 0.2485 0.0389  0.0453  -0.0337 87  THR A CA  
690  C  CA  B THR A 87  ? 0.2075 0.2073 0.1770 0.0385  0.0153  -0.0140 87  THR A CA  
691  C  C   A THR A 87  ? 0.2456 0.1840 0.2695 0.0082  0.0578  -0.0616 87  THR A C   
692  C  C   B THR A 87  ? 0.1973 0.1698 0.2206 -0.0013 0.0345  -0.0370 87  THR A C   
693  O  O   A THR A 87  ? 0.2809 0.1775 0.2552 0.0163  0.0757  -0.0345 87  THR A O   
694  O  O   B THR A 87  ? 0.2388 0.1397 0.1628 0.0009  0.0425  -0.0362 87  THR A O   
695  C  CB  A THR A 87  ? 0.2565 0.2321 0.2595 0.0328  0.1201  0.0146  87  THR A CB  
696  C  CB  B THR A 87  ? 0.1858 0.1759 0.2339 0.0133  0.0172  0.0195  87  THR A CB  
697  O  OG1 A THR A 87  ? 0.3129 0.3363 0.4634 0.0785  0.1825  -0.1039 87  THR A OG1 
698  O  OG1 B THR A 87  ? 0.2655 0.1345 0.2445 0.0485  0.0122  0.0560  87  THR A OG1 
699  C  CG2 A THR A 87  ? 0.2885 0.2831 0.2856 0.0935  0.0092  0.0774  87  THR A CG2 
700  C  CG2 B THR A 87  ? 0.2318 0.2708 0.2906 0.0614  0.0594  -0.0110 87  THR A CG2 
701  N  N   . TYR A 88  ? 0.1653 0.1993 0.1860 0.0018  0.0159  -0.0566 88  TYR A N   
702  C  CA  . TYR A 88  ? 0.2011 0.1865 0.1856 0.0227  0.0333  -0.0068 88  TYR A CA  
703  C  C   . TYR A 88  ? 0.1445 0.1725 0.2105 0.0407  -0.0012 -0.0332 88  TYR A C   
704  O  O   . TYR A 88  ? 0.2034 0.2685 0.2515 -0.0399 -0.0198 0.0120  88  TYR A O   
705  C  CB  . TYR A 88  ? 0.2077 0.1782 0.2026 0.0375  -0.0219 -0.0264 88  TYR A CB  
706  C  CG  . TYR A 88  ? 0.1932 0.1349 0.1644 -0.0145 0.0150  -0.0301 88  TYR A CG  
707  C  CD1 . TYR A 88  ? 0.1497 0.1825 0.1635 0.0094  0.0263  -0.0027 88  TYR A CD1 
708  C  CD2 . TYR A 88  ? 0.2016 0.1331 0.1662 0.0091  0.0089  0.0066  88  TYR A CD2 
709  C  CE1 . TYR A 88  ? 0.2113 0.1581 0.1897 -0.0012 0.0069  -0.0226 88  TYR A CE1 
710  C  CE2 . TYR A 88  ? 0.1896 0.1386 0.1741 0.0190  0.0062  0.0019  88  TYR A CE2 
711  C  CZ  . TYR A 88  ? 0.1969 0.1351 0.1739 0.0048  0.0088  -0.0096 88  TYR A CZ  
712  O  OH  . TYR A 88  ? 0.2082 0.1953 0.1410 0.0003  0.0313  -0.0336 88  TYR A OH  
713  N  N   . ARG A 89  ? 0.1696 0.1696 0.1759 0.0241  -0.0120 -0.0515 89  ARG A N   
714  C  CA  . ARG A 89  ? 0.1342 0.1632 0.1793 0.0583  -0.0080 -0.0245 89  ARG A CA  
715  C  C   . ARG A 89  ? 0.1345 0.1267 0.1239 0.0074  0.0203  -0.0086 89  ARG A C   
716  O  O   . ARG A 89  ? 0.1379 0.1254 0.1119 0.0043  0.0043  -0.0102 89  ARG A O   
717  C  CB  . ARG A 89  ? 0.2583 0.1335 0.2508 0.0498  -0.0734 -0.0208 89  ARG A CB  
718  C  CG  . ARG A 89  ? 0.3455 0.1699 0.1905 0.0451  -0.0579 0.0080  89  ARG A CG  
719  C  CD  . ARG A 89  ? 0.2591 0.1904 0.2490 0.0730  -0.0285 0.0209  89  ARG A CD  
720  N  NE  . ARG A 89  ? 0.3697 0.1749 0.2113 0.0375  -0.0620 0.0132  89  ARG A NE  
721  C  CZ  . ARG A 89  ? 0.2231 0.1425 0.1610 0.0346  -0.0255 -0.0111 89  ARG A CZ  
722  N  NH1 . ARG A 89  ? 0.3579 0.2622 0.1618 0.0480  -0.0496 0.0220  89  ARG A NH1 
723  N  NH2 . ARG A 89  ? 0.3529 0.2179 0.1980 0.0594  0.0088  -0.0170 89  ARG A NH2 
724  N  N   . LEU A 90  ? 0.1561 0.1275 0.1441 0.0110  -0.0051 -0.0067 90  LEU A N   
725  C  CA  . LEU A 90  ? 0.1605 0.1513 0.1138 -0.0010 0.0237  -0.0221 90  LEU A CA  
726  C  C   . LEU A 90  ? 0.1669 0.1383 0.0817 0.0209  -0.0164 -0.0138 90  LEU A C   
727  O  O   . LEU A 90  ? 0.1566 0.1671 0.1687 0.0184  -0.0215 0.0356  90  LEU A O   
728  C  CB  . LEU A 90  ? 0.1603 0.1435 0.1183 0.0129  -0.0086 -0.0160 90  LEU A CB  
729  C  CG  . LEU A 90  ? 0.1612 0.1465 0.1177 -0.0041 -0.0107 -0.0186 90  LEU A CG  
730  C  CD1 . LEU A 90  ? 0.1646 0.1468 0.1467 0.0023  -0.0061 -0.0075 90  LEU A CD1 
731  C  CD2 . LEU A 90  ? 0.1631 0.1539 0.1811 -0.0158 -0.0227 -0.0242 90  LEU A CD2 
732  N  N   . THR A 91  ? 0.1441 0.1204 0.1160 0.0030  0.0154  -0.0140 91  THR A N   
733  C  CA  . THR A 91  ? 0.1421 0.1305 0.1102 0.0059  0.0139  -0.0070 91  THR A CA  
734  C  C   . THR A 91  ? 0.1544 0.1235 0.0731 0.0087  0.0089  0.0063  91  THR A C   
735  O  O   . THR A 91  ? 0.1601 0.1393 0.0775 0.0178  0.0062  0.0038  91  THR A O   
736  C  CB  . THR A 91  ? 0.1571 0.1614 0.1020 -0.0057 0.0009  -0.0073 91  THR A CB  
737  O  OG1 . THR A 91  ? 0.2069 0.1904 0.1231 -0.0344 0.0046  0.0109  91  THR A OG1 
738  C  CG2 . THR A 91  ? 0.2036 0.1244 0.1685 0.0122  -0.0238 -0.0132 91  THR A CG2 
739  N  N   . GLN A 92  ? 0.1530 0.0998 0.0987 0.0106  0.0001  -0.0096 92  GLN A N   
740  C  CA  . GLN A 92  ? 0.1364 0.1120 0.0768 0.0072  0.0176  -0.0022 92  GLN A CA  
741  C  C   . GLN A 92  ? 0.1415 0.1237 0.0831 0.0096  0.0030  0.0096  92  GLN A C   
742  O  O   . GLN A 92  ? 0.1415 0.1183 0.0818 0.0066  0.0098  0.0087  92  GLN A O   
743  C  CB  . GLN A 92  ? 0.1208 0.1601 0.1327 0.0205  -0.0063 0.0075  92  GLN A CB  
744  C  CG  . GLN A 92  ? 0.1566 0.1327 0.1032 0.0113  -0.0066 0.0055  92  GLN A CG  
745  C  CD  . GLN A 92  ? 0.1729 0.1415 0.1132 -0.0023 0.0096  0.0121  92  GLN A CD  
746  O  OE1 . GLN A 92  ? 0.1567 0.1415 0.1391 0.0072  -0.0044 -0.0024 92  GLN A OE1 
747  N  NE2 . GLN A 92  ? 0.1495 0.2043 0.1577 0.0125  -0.0070 0.0221  92  GLN A NE2 
748  N  N   . PHE A 93  ? 0.1129 0.1189 0.1071 0.0018  -0.0025 0.0029  93  PHE A N   
749  C  CA  . PHE A 93  ? 0.1237 0.0971 0.1349 0.0096  0.0109  -0.0009 93  PHE A CA  
750  C  C   . PHE A 93  ? 0.1113 0.1280 0.0958 -0.0089 0.0201  -0.0029 93  PHE A C   
751  O  O   . PHE A 93  ? 0.1379 0.1230 0.0874 0.0031  0.0047  -0.0031 93  PHE A O   
752  C  CB  . PHE A 93  ? 0.1301 0.1233 0.1041 -0.0019 0.0015  -0.0005 93  PHE A CB  
753  C  CG  . PHE A 93  ? 0.1417 0.1248 0.1040 0.0016  -0.0073 0.0108  93  PHE A CG  
754  C  CD1 . PHE A 93  ? 0.1315 0.1300 0.1350 -0.0076 -0.0110 -0.0097 93  PHE A CD1 
755  C  CD2 . PHE A 93  ? 0.1254 0.1339 0.1068 -0.0053 -0.0017 0.0229  93  PHE A CD2 
756  C  CE1 . PHE A 93  ? 0.1258 0.1543 0.1120 0.0064  -0.0110 -0.0013 93  PHE A CE1 
757  C  CE2 . PHE A 93  ? 0.1666 0.1390 0.1190 0.0062  -0.0051 0.0030  93  PHE A CE2 
758  C  CZ  . PHE A 93  ? 0.1221 0.1219 0.1364 -0.0024 -0.0113 0.0058  93  PHE A CZ  
759  N  N   . HIS A 94  ? 0.0968 0.1146 0.1134 0.0073  0.0017  -0.0079 94  HIS A N   
760  C  CA  . HIS A 94  ? 0.1230 0.1264 0.0919 0.0078  0.0171  -0.0027 94  HIS A CA  
761  C  C   . HIS A 94  ? 0.1098 0.1406 0.0898 0.0128  -0.0046 0.0018  94  HIS A C   
762  O  O   . HIS A 94  ? 0.1415 0.1212 0.0937 0.0126  0.0193  0.0012  94  HIS A O   
763  C  CB  . HIS A 94  ? 0.1309 0.1599 0.0565 0.0013  -0.0046 -0.0049 94  HIS A CB  
764  C  CG  . HIS A 94  ? 0.1467 0.1300 0.0576 -0.0073 -0.0095 0.0087  94  HIS A CG  
765  N  ND1 . HIS A 94  ? 0.1229 0.1332 0.1030 -0.0109 -0.0061 -0.0173 94  HIS A ND1 
766  C  CD2 . HIS A 94  ? 0.1292 0.1721 0.0555 -0.0035 -0.0225 0.0092  94  HIS A CD2 
767  C  CE1 . HIS A 94  ? 0.1150 0.1389 0.1145 -0.0035 -0.0042 0.0052  94  HIS A CE1 
768  N  NE2 . HIS A 94  ? 0.1300 0.1512 0.0722 -0.0108 -0.0064 -0.0001 94  HIS A NE2 
769  N  N   . PHE A 95  ? 0.1300 0.1145 0.1014 0.0154  -0.0047 -0.0039 95  PHE A N   
770  C  CA  . PHE A 95  ? 0.1237 0.1027 0.1342 0.0099  -0.0159 -0.0049 95  PHE A CA  
771  C  C   . PHE A 95  ? 0.1181 0.1162 0.1056 0.0065  0.0130  -0.0237 95  PHE A C   
772  O  O   . PHE A 95  ? 0.1372 0.1289 0.1201 -0.0026 0.0156  -0.0094 95  PHE A O   
773  C  CB  . PHE A 95  ? 0.1206 0.1251 0.1426 0.0067  -0.0088 -0.0322 95  PHE A CB  
774  C  CG  . PHE A 95  ? 0.1374 0.1280 0.1226 0.0143  -0.0068 -0.0232 95  PHE A CG  
775  C  CD1 . PHE A 95  ? 0.1465 0.1573 0.1234 0.0125  -0.0350 -0.0331 95  PHE A CD1 
776  C  CD2 . PHE A 95  ? 0.1300 0.1464 0.1298 0.0089  -0.0062 -0.0390 95  PHE A CD2 
777  C  CE1 . PHE A 95  ? 0.1491 0.1373 0.1664 0.0063  -0.0324 -0.0326 95  PHE A CE1 
778  C  CE2 . PHE A 95  ? 0.1439 0.1520 0.1402 0.0148  0.0019  -0.0322 95  PHE A CE2 
779  C  CZ  . PHE A 95  ? 0.1462 0.1390 0.1673 0.0042  -0.0154 -0.0392 95  PHE A CZ  
780  N  N   . HIS A 96  ? 0.1322 0.1192 0.1177 0.0096  -0.0114 -0.0158 96  HIS A N   
781  C  CA  . HIS A 96  ? 0.1253 0.1154 0.0951 0.0042  -0.0128 -0.0128 96  HIS A CA  
782  C  C   . HIS A 96  ? 0.1199 0.1246 0.1041 -0.0044 0.0058  -0.0037 96  HIS A C   
783  O  O   . HIS A 96  ? 0.1131 0.1386 0.1291 0.0143  0.0168  -0.0142 96  HIS A O   
784  C  CB  . HIS A 96  ? 0.1287 0.1219 0.1097 0.0100  -0.0186 -0.0262 96  HIS A CB  
785  C  CG  . HIS A 96  ? 0.1274 0.1181 0.1258 0.0074  0.0161  -0.0078 96  HIS A CG  
786  N  ND1 . HIS A 96  ? 0.1257 0.1292 0.1225 -0.0081 -0.0062 -0.0098 96  HIS A ND1 
787  C  CD2 . HIS A 96  ? 0.1433 0.1180 0.0952 0.0055  0.0149  -0.0004 96  HIS A CD2 
788  C  CE1 . HIS A 96  ? 0.1277 0.1530 0.1261 0.0085  0.0099  -0.0149 96  HIS A CE1 
789  N  NE2 . HIS A 96  ? 0.1243 0.1075 0.0980 0.0068  0.0122  -0.0100 96  HIS A NE2 
790  N  N   . TRP A 97  ? 0.1342 0.1213 0.1205 0.0198  -0.0111 -0.0139 97  TRP A N   
791  C  CA  . TRP A 97  ? 0.1464 0.1198 0.1711 0.0196  -0.0312 -0.0135 97  TRP A CA  
792  C  C   . TRP A 97  ? 0.1306 0.1247 0.1186 0.0115  0.0019  -0.0215 97  TRP A C   
793  O  O   . TRP A 97  ? 0.1315 0.1286 0.1597 0.0156  0.0037  -0.0135 97  TRP A O   
794  C  CB  . TRP A 97  ? 0.1551 0.1524 0.1380 0.0173  -0.0121 -0.0220 97  TRP A CB  
795  C  CG  . TRP A 97  ? 0.1536 0.1456 0.1451 0.0230  -0.0104 -0.0184 97  TRP A CG  
796  C  CD1 . TRP A 97  ? 0.1655 0.1456 0.1375 0.0291  -0.0163 -0.0208 97  TRP A CD1 
797  C  CD2 . TRP A 97  ? 0.1461 0.1541 0.1242 0.0264  -0.0196 -0.0077 97  TRP A CD2 
798  N  NE1 . TRP A 97  ? 0.1736 0.1502 0.1389 0.0317  -0.0223 -0.0133 97  TRP A NE1 
799  C  CE2 . TRP A 97  ? 0.1492 0.1420 0.1439 0.0130  -0.0091 -0.0295 97  TRP A CE2 
800  C  CE3 . TRP A 97  ? 0.1314 0.1329 0.1393 0.0031  -0.0062 -0.0104 97  TRP A CE3 
801  C  CZ2 . TRP A 97  ? 0.1310 0.1646 0.1423 0.0053  -0.0170 -0.0209 97  TRP A CZ2 
802  C  CZ3 . TRP A 97  ? 0.1271 0.1588 0.1018 0.0106  -0.0027 -0.0080 97  TRP A CZ3 
803  C  CH2 . TRP A 97  ? 0.1471 0.1602 0.1125 0.0140  0.0032  -0.0076 97  TRP A CH2 
804  N  N   . GLY A 98  ? 0.1465 0.1203 0.1642 0.0182  -0.0127 -0.0184 98  GLY A N   
805  C  CA  . GLY A 98  ? 0.1549 0.1284 0.1685 0.0303  -0.0104 -0.0375 98  GLY A CA  
806  C  C   . GLY A 98  ? 0.1644 0.1317 0.1705 0.0108  -0.0284 -0.0438 98  GLY A C   
807  O  O   . GLY A 98  ? 0.1781 0.1522 0.1711 0.0173  -0.0252 -0.0526 98  GLY A O   
808  N  N   . SER A 99  ? 0.1847 0.1204 0.1871 0.0312  -0.0067 -0.0418 99  SER A N   
809  C  CA  . SER A 99  ? 0.1901 0.1663 0.1965 0.0364  0.0035  -0.0652 99  SER A CA  
810  C  C   . SER A 99  ? 0.2521 0.1800 0.2237 0.0294  -0.0574 -0.0376 99  SER A C   
811  O  O   . SER A 99  ? 0.3044 0.2018 0.2823 0.0137  -0.0321 -0.1028 99  SER A O   
812  C  CB  . SER A 99  ? 0.2002 0.2075 0.1853 0.0159  -0.0128 -0.0531 99  SER A CB  
813  O  OG  . SER A 99  ? 0.2386 0.2016 0.2240 0.0596  -0.0174 -0.0362 99  SER A OG  
814  N  N   . LEU A 100 ? 0.1450 0.1527 0.3523 0.0105  -0.0134 -0.0291 100 LEU A N   
815  C  CA  . LEU A 100 ? 0.2068 0.1727 0.3585 -0.0156 0.0478  -0.0046 100 LEU A CA  
816  C  C   . LEU A 100 ? 0.1998 0.1691 0.3657 0.0243  0.0274  -0.0595 100 LEU A C   
817  O  O   . LEU A 100 ? 0.2158 0.1692 0.3406 0.0326  -0.0049 -0.0513 100 LEU A O   
818  C  CB  . LEU A 100 ? 0.2903 0.1743 0.3638 0.0074  0.0158  -0.0309 100 LEU A CB  
819  C  CG  . LEU A 100 ? 0.4048 0.2382 0.3416 -0.0083 -0.0286 0.0201  100 LEU A CG  
820  C  CD1 . LEU A 100 ? 0.5236 0.2423 0.5921 -0.0577 -0.0996 0.0320  100 LEU A CD1 
821  C  CD2 . LEU A 100 ? 0.3644 0.3067 0.2896 0.0283  0.1015  0.0886  100 LEU A CD2 
822  N  N   . ASP A 101 ? 0.1943 0.1675 0.3801 0.0114  -0.0053 -0.0546 101 ASP A N   
823  C  CA  . ASP A 101 ? 0.1482 0.1655 0.3705 0.0138  -0.0097 0.0115  101 ASP A CA  
824  C  C   . ASP A 101 ? 0.2449 0.1185 0.3916 -0.0284 -0.0644 -0.0137 101 ASP A C   
825  O  O   . ASP A 101 ? 0.2953 0.1854 0.3438 0.0767  -0.0342 0.0282  101 ASP A O   
826  C  CB  . ASP A 101 ? 0.2205 0.1571 0.3647 -0.0106 -0.0639 0.0067  101 ASP A CB  
827  C  CG  . ASP A 101 ? 0.2255 0.1728 0.3144 -0.0136 -0.0095 -0.0124 101 ASP A CG  
828  O  OD1 . ASP A 101 ? 0.2274 0.1889 0.2964 0.0054  0.0166  -0.0418 101 ASP A OD1 
829  O  OD2 . ASP A 101 ? 0.2443 0.2317 0.4443 -0.0324 -0.0814 0.0125  101 ASP A OD2 
830  N  N   . GLY A 102 ? 0.2150 0.1215 0.2917 -0.0195 -0.0337 0.0089  102 GLY A N   
831  C  CA  . GLY A 102 ? 0.2655 0.2166 0.2859 -0.0255 -0.0525 0.0215  102 GLY A CA  
832  C  C   . GLY A 102 ? 0.2438 0.1361 0.2867 0.0111  -0.0461 0.0387  102 GLY A C   
833  O  O   . GLY A 102 ? 0.2469 0.2040 0.2795 -0.0117 -0.0102 0.0545  102 GLY A O   
834  N  N   . GLN A 103 ? 0.1914 0.1523 0.3349 0.0106  -0.0209 0.0543  103 GLN A N   
835  C  CA  . GLN A 103 ? 0.1854 0.1688 0.2154 0.0131  0.0019  0.0309  103 GLN A CA  
836  C  C   . GLN A 103 ? 0.1743 0.1221 0.2016 0.0083  -0.0003 -0.0009 103 GLN A C   
837  O  O   . GLN A 103 ? 0.1662 0.1282 0.2337 0.0172  -0.0102 -0.0194 103 GLN A O   
838  C  CB  . GLN A 103 ? 0.2034 0.1544 0.1896 0.0554  -0.0044 -0.0129 103 GLN A CB  
839  C  CG  . GLN A 103 ? 0.1890 0.1546 0.1833 0.0447  0.0039  0.0044  103 GLN A CG  
840  C  CD  . GLN A 103 ? 0.2208 0.2172 0.1627 0.0635  0.0104  0.0111  103 GLN A CD  
841  O  OE1 . GLN A 103 ? 0.3240 0.3121 0.2913 0.1567  0.0726  0.1104  103 GLN A OE1 
842  N  NE2 . GLN A 103 ? 0.1692 0.1907 0.2577 0.0479  0.0228  0.0049  103 GLN A NE2 
843  N  N   . GLY A 104 ? 0.1365 0.1309 0.1885 0.0140  0.0185  -0.0132 104 GLY A N   
844  C  CA  . GLY A 104 ? 0.1251 0.1264 0.1941 0.0179  0.0175  -0.0190 104 GLY A CA  
845  C  C   . GLY A 104 ? 0.1199 0.1300 0.1386 0.0018  -0.0049 -0.0055 104 GLY A C   
846  O  O   . GLY A 104 ? 0.1328 0.1335 0.1699 -0.0037 0.0174  -0.0023 104 GLY A O   
847  N  N   . SER A 105 ? 0.1404 0.1455 0.1271 0.0092  0.0037  -0.0068 105 SER A N   
848  C  CA  . SER A 105 ? 0.1253 0.1611 0.1322 -0.0116 0.0251  -0.0305 105 SER A CA  
849  C  C   . SER A 105 ? 0.1295 0.1237 0.1472 -0.0051 0.0099  0.0031  105 SER A C   
850  O  O   . SER A 105 ? 0.1331 0.1222 0.1693 0.0039  -0.0092 0.0022  105 SER A O   
851  C  CB  . SER A 105 ? 0.1323 0.1535 0.1368 0.0089  0.0150  0.0039  105 SER A CB  
852  O  OG  . SER A 105 ? 0.1512 0.1198 0.1689 -0.0042 0.0068  0.0012  105 SER A OG  
853  N  N   . GLU A 106 ? 0.1438 0.1187 0.1117 -0.0020 0.0037  -0.0071 106 GLU A N   
854  C  CA  . GLU A 106 ? 0.1400 0.1250 0.1210 -0.0110 0.0025  -0.0077 106 GLU A CA  
855  C  C   . GLU A 106 ? 0.1389 0.1315 0.1109 0.0089  0.0055  0.0012  106 GLU A C   
856  O  O   . GLU A 106 ? 0.1149 0.1465 0.1566 -0.0002 -0.0189 0.0050  106 GLU A O   
857  C  CB  . GLU A 106 ? 0.1632 0.1307 0.1093 -0.0190 0.0197  0.0026  106 GLU A CB  
858  C  CG  . GLU A 106 ? 0.1544 0.1399 0.1016 -0.0168 0.0240  -0.0079 106 GLU A CG  
859  C  CD  . GLU A 106 ? 0.1196 0.1452 0.1225 -0.0051 0.0147  -0.0058 106 GLU A CD  
860  O  OE1 . GLU A 106 ? 0.1145 0.1444 0.1332 0.0079  -0.0009 -0.0002 106 GLU A OE1 
861  O  OE2 . GLU A 106 ? 0.1445 0.1513 0.1746 0.0029  0.0297  -0.0118 106 GLU A OE2 
862  N  N   . HIS A 107 ? 0.1326 0.1289 0.1016 0.0145  0.0059  -0.0012 107 HIS A N   
863  C  CA  . HIS A 107 ? 0.1553 0.1375 0.0955 0.0077  0.0185  -0.0068 107 HIS A CA  
864  C  C   . HIS A 107 ? 0.1544 0.1372 0.1151 -0.0037 -0.0069 0.0050  107 HIS A C   
865  O  O   . HIS A 107 ? 0.1495 0.1359 0.1365 0.0124  -0.0027 0.0009  107 HIS A O   
866  C  CB  . HIS A 107 ? 0.1287 0.1278 0.1221 -0.0042 0.0030  0.0067  107 HIS A CB  
867  C  CG  . HIS A 107 ? 0.1275 0.1237 0.1248 -0.0036 -0.0034 0.0133  107 HIS A CG  
868  N  ND1 . HIS A 107 ? 0.1303 0.1165 0.1111 0.0030  0.0032  0.0111  107 HIS A ND1 
869  C  CD2 . HIS A 107 ? 0.1409 0.1309 0.1274 0.0097  0.0091  -0.0142 107 HIS A CD2 
870  C  CE1 . HIS A 107 ? 0.1363 0.1298 0.1000 -0.0129 0.0033  0.0051  107 HIS A CE1 
871  N  NE2 . HIS A 107 ? 0.1439 0.1244 0.0979 0.0015  0.0072  -0.0083 107 HIS A NE2 
872  N  N   . THR A 108 ? 0.1566 0.1424 0.1329 0.0008  0.0098  0.0305  108 THR A N   
873  C  CA  . THR A 108 ? 0.1353 0.1298 0.1815 0.0052  0.0103  0.0174  108 THR A CA  
874  C  C   . THR A 108 ? 0.1652 0.1332 0.1671 -0.0002 0.0070  0.0022  108 THR A C   
875  O  O   . THR A 108 ? 0.1718 0.1524 0.1521 0.0170  0.0092  0.0122  108 THR A O   
876  C  CB  . THR A 108 ? 0.1666 0.1538 0.1483 0.0323  0.0084  0.0024  108 THR A CB  
877  O  OG1 . THR A 108 ? 0.1772 0.1681 0.1764 0.0047  -0.0119 0.0131  108 THR A OG1 
878  C  CG2 . THR A 108 ? 0.1882 0.1858 0.1321 0.0078  0.0291  0.0054  108 THR A CG2 
879  N  N   . VAL A 109 ? 0.1546 0.1797 0.2005 -0.0111 0.0217  0.0701  109 VAL A N   
880  C  CA  . VAL A 109 ? 0.1613 0.1797 0.1905 0.0190  0.0223  0.0575  109 VAL A CA  
881  C  C   . VAL A 109 ? 0.1802 0.1667 0.2095 0.0024  0.0064  0.0502  109 VAL A C   
882  O  O   . VAL A 109 ? 0.1693 0.1761 0.2485 0.0048  0.0172  0.0419  109 VAL A O   
883  C  CB  . VAL A 109 ? 0.1605 0.1793 0.2188 -0.0032 0.0217  0.0514  109 VAL A CB  
884  C  CG1 . VAL A 109 ? 0.1905 0.2594 0.2293 0.0305  0.0348  0.0682  109 VAL A CG1 
885  C  CG2 . VAL A 109 ? 0.1998 0.1761 0.1942 0.0209  0.0179  0.0363  109 VAL A CG2 
886  N  N   . ASP A 110 ? 0.2070 0.1517 0.2120 0.0029  0.0033  0.0490  110 ASP A N   
887  C  CA  . ASP A 110 ? 0.2075 0.1901 0.2361 0.0514  0.0297  0.0864  110 ASP A CA  
888  C  C   . ASP A 110 ? 0.2384 0.1759 0.2330 0.0320  0.0454  0.0778  110 ASP A C   
889  O  O   . ASP A 110 ? 0.2469 0.1739 0.2651 0.0141  0.0260  0.0863  110 ASP A O   
890  C  CB  . ASP A 110 ? 0.2785 0.1831 0.3342 0.0185  0.0195  0.0815  110 ASP A CB  
891  C  CG  . ASP A 110 ? 0.2575 0.2041 0.2780 0.0533  0.0121  0.1252  110 ASP A CG  
892  O  OD1 . ASP A 110 ? 0.3189 0.2440 0.2612 0.0312  0.0979  0.0693  110 ASP A OD1 
893  O  OD2 . ASP A 110 ? 0.2539 0.3808 0.3559 0.0674  0.0723  0.1232  110 ASP A OD2 
894  N  N   . LYS A 111 ? 0.1937 0.1662 0.1969 0.0158  0.0157  0.0429  111 LYS A N   
895  C  CA  . LYS A 111 ? 0.1768 0.1828 0.2025 0.0412  -0.0055 0.0284  111 LYS A CA  
896  C  C   . LYS A 111 ? 0.1842 0.1315 0.2098 0.0286  -0.0152 0.0054  111 LYS A C   
897  O  O   . LYS A 111 ? 0.1826 0.1724 0.2381 0.0179  0.0004  0.0137  111 LYS A O   
898  C  CB  . LYS A 111 ? 0.2285 0.1615 0.2547 0.0496  -0.0436 0.0150  111 LYS A CB  
899  C  CG  . LYS A 111 ? 0.2612 0.3747 0.2601 -0.0149 -0.0650 0.0321  111 LYS A CG  
900  C  CD  . LYS A 111 ? 0.2119 0.3468 0.3182 0.0286  -0.0472 -0.0644 111 LYS A CD  
901  C  CE  . LYS A 111 ? 0.3345 0.6627 0.2927 -0.0655 -0.0307 -0.0907 111 LYS A CE  
902  N  NZ  . LYS A 111 ? 0.4207 0.4694 0.3987 -0.1825 -0.0581 0.0316  111 LYS A NZ  
903  N  N   . LYS A 112 ? 0.1817 0.1524 0.2323 0.0008  -0.0234 0.0223  112 LYS A N   
904  C  CA  . LYS A 112 ? 0.1944 0.1850 0.2429 -0.0143 -0.0244 0.0505  112 LYS A CA  
905  C  C   . LYS A 112 ? 0.1575 0.1664 0.1991 0.0262  -0.0223 0.0267  112 LYS A C   
906  O  O   . LYS A 112 ? 0.1833 0.1527 0.2134 0.0031  -0.0004 0.0178  112 LYS A O   
907  C  CB  . LYS A 112 ? 0.1933 0.2053 0.2963 -0.0228 0.0016  0.0044  112 LYS A CB  
908  C  CG  . LYS A 112 ? 0.1993 0.2677 0.3492 -0.0688 -0.0620 0.0079  112 LYS A CG  
909  C  CD  . LYS A 112 ? 0.1969 0.3373 0.3456 -0.0127 -0.0538 0.0591  112 LYS A CD  
910  C  CE  . LYS A 112 ? 0.4008 0.4414 0.2245 0.0886  0.0240  0.0336  112 LYS A CE  
911  N  NZ  . LYS A 112 ? 0.4291 0.3093 0.4306 0.0501  -0.1772 0.0709  112 LYS A NZ  
912  N  N   A LYS A 113 ? 0.1707 0.1533 0.1747 0.0190  -0.0271 0.0278  113 LYS A N   
913  N  N   B LYS A 113 ? 0.1706 0.1487 0.1919 0.0184  -0.0210 0.0196  113 LYS A N   
914  C  CA  A LYS A 113 ? 0.1772 0.1659 0.1887 0.0186  -0.0378 0.0445  113 LYS A CA  
915  C  CA  B LYS A 113 ? 0.1702 0.1447 0.2155 0.0162  -0.0208 0.0348  113 LYS A CA  
916  C  C   A LYS A 113 ? 0.1795 0.1456 0.1991 0.0285  -0.0370 0.0122  113 LYS A C   
917  C  C   B LYS A 113 ? 0.1564 0.1095 0.2224 -0.0015 -0.0070 0.0200  113 LYS A C   
918  O  O   A LYS A 113 ? 0.2148 0.1283 0.1807 0.0362  0.0047  0.0220  113 LYS A O   
919  O  O   B LYS A 113 ? 0.1890 0.1204 0.2658 -0.0042 0.0021  -0.0044 113 LYS A O   
920  C  CB  A LYS A 113 ? 0.1786 0.1600 0.1976 0.0074  -0.0391 0.0129  113 LYS A CB  
921  C  CB  B LYS A 113 ? 0.1767 0.1659 0.2275 0.0204  -0.0206 0.0019  113 LYS A CB  
922  C  CG  A LYS A 113 ? 0.1447 0.2201 0.1779 0.0304  -0.0103 0.0366  113 LYS A CG  
923  C  CG  B LYS A 113 ? 0.1341 0.2127 0.2188 0.0337  0.0019  0.0130  113 LYS A CG  
924  C  CD  A LYS A 113 ? 0.1932 0.2149 0.1772 0.0582  -0.0084 0.0063  113 LYS A CD  
925  C  CD  B LYS A 113 ? 0.1429 0.1256 0.2852 0.0316  -0.0133 -0.0496 113 LYS A CD  
926  C  CE  A LYS A 113 ? 0.2104 0.2500 0.2213 0.0189  0.0077  0.0373  113 LYS A CE  
927  C  CE  B LYS A 113 ? 0.1359 0.2335 0.2978 -0.0134 -0.0234 0.0199  113 LYS A CE  
928  N  NZ  A LYS A 113 ? 0.2199 0.2548 0.2572 0.0723  -0.0337 0.0482  113 LYS A NZ  
929  N  NZ  B LYS A 113 ? 0.2077 0.2478 0.3309 0.0357  -0.0094 0.0212  113 LYS A NZ  
930  N  N   . TYR A 114 ? 0.1569 0.1368 0.1786 0.0167  -0.0165 0.0168  114 TYR A N   
931  C  CA  . TYR A 114 ? 0.1456 0.1335 0.1933 0.0004  -0.0228 0.0079  114 TYR A CA  
932  C  C   . TYR A 114 ? 0.1503 0.1077 0.1876 -0.0084 -0.0157 0.0129  114 TYR A C   
933  O  O   . TYR A 114 ? 0.1373 0.1340 0.1976 0.0015  -0.0072 -0.0067 114 TYR A O   
934  C  CB  . TYR A 114 ? 0.1493 0.1480 0.2104 0.0122  0.0025  0.0208  114 TYR A CB  
935  C  CG  . TYR A 114 ? 0.1612 0.1203 0.1838 0.0113  -0.0097 0.0183  114 TYR A CG  
936  C  CD1 . TYR A 114 ? 0.2091 0.1547 0.1861 0.0464  0.0064  0.0490  114 TYR A CD1 
937  C  CD2 . TYR A 114 ? 0.1559 0.1459 0.2781 0.0198  0.0159  0.0229  114 TYR A CD2 
938  C  CE1 . TYR A 114 ? 0.2608 0.2203 0.2004 0.0259  0.0206  0.0519  114 TYR A CE1 
939  C  CE2 . TYR A 114 ? 0.1644 0.2020 0.2654 0.0003  0.0174  0.0296  114 TYR A CE2 
940  C  CZ  . TYR A 114 ? 0.2746 0.2095 0.2118 0.0081  0.0505  0.0939  114 TYR A CZ  
941  O  OH  . TYR A 114 ? 0.3175 0.4105 0.2703 0.0336  0.1108  0.1469  114 TYR A OH  
942  N  N   . ALA A 115 ? 0.1573 0.1331 0.1577 0.0111  -0.0122 -0.0013 115 ALA A N   
943  C  CA  . ALA A 115 ? 0.1738 0.1066 0.1576 -0.0046 -0.0223 -0.0173 115 ALA A CA  
944  C  C   . ALA A 115 ? 0.1407 0.1150 0.1969 0.0052  -0.0019 -0.0084 115 ALA A C   
945  O  O   . ALA A 115 ? 0.1470 0.1168 0.1962 0.0013  0.0088  -0.0242 115 ALA A O   
946  C  CB  . ALA A 115 ? 0.1523 0.1775 0.2104 -0.0178 -0.0385 -0.0294 115 ALA A CB  
947  N  N   . ALA A 116 ? 0.1570 0.0978 0.1700 0.0082  -0.0179 -0.0203 116 ALA A N   
948  C  CA  . ALA A 116 ? 0.1623 0.0977 0.1471 0.0021  -0.0015 -0.0229 116 ALA A CA  
949  C  C   . ALA A 116 ? 0.1240 0.1335 0.1059 0.0100  0.0052  0.0049  116 ALA A C   
950  O  O   . ALA A 116 ? 0.1201 0.1250 0.1355 0.0002  0.0035  0.0044  116 ALA A O   
951  C  CB  . ALA A 116 ? 0.1558 0.1298 0.1456 0.0021  -0.0168 -0.0155 116 ALA A CB  
952  N  N   . GLU A 117 ? 0.1341 0.1199 0.1102 0.0052  -0.0054 -0.0199 117 GLU A N   
953  C  CA  . GLU A 117 ? 0.1448 0.1226 0.0718 0.0139  -0.0110 -0.0092 117 GLU A CA  
954  C  C   . GLU A 117 ? 0.1169 0.1298 0.0924 0.0020  0.0000  0.0034  117 GLU A C   
955  O  O   . GLU A 117 ? 0.1257 0.1359 0.1394 0.0195  0.0348  0.0080  117 GLU A O   
956  C  CB  . GLU A 117 ? 0.1434 0.1386 0.1050 0.0186  -0.0236 -0.0164 117 GLU A CB  
957  C  CG  . GLU A 117 ? 0.1552 0.1393 0.0983 -0.0105 -0.0148 -0.0287 117 GLU A CG  
958  C  CD  . GLU A 117 ? 0.1231 0.1562 0.1301 0.0117  -0.0102 -0.0016 117 GLU A CD  
959  O  OE1 . GLU A 117 ? 0.1382 0.1403 0.1235 0.0168  -0.0064 0.0017  117 GLU A OE1 
960  O  OE2 . GLU A 117 ? 0.1641 0.1579 0.1169 0.0006  -0.0071 -0.0021 117 GLU A OE2 
961  N  N   . LEU A 118 ? 0.1235 0.0971 0.1301 0.0119  -0.0032 -0.0030 118 LEU A N   
962  C  CA  . LEU A 118 ? 0.1222 0.1119 0.0953 -0.0003 -0.0027 -0.0122 118 LEU A CA  
963  C  C   . LEU A 118 ? 0.1018 0.1155 0.0861 0.0044  0.0076  -0.0178 118 LEU A C   
964  O  O   . LEU A 118 ? 0.1293 0.1133 0.0912 0.0016  0.0176  -0.0055 118 LEU A O   
965  C  CB  . LEU A 118 ? 0.1036 0.1201 0.1329 0.0083  0.0084  0.0059  118 LEU A CB  
966  C  CG  . LEU A 118 ? 0.1207 0.1199 0.1147 0.0026  0.0086  0.0098  118 LEU A CG  
967  C  CD1 . LEU A 118 ? 0.1398 0.1309 0.1040 0.0062  -0.0104 0.0154  118 LEU A CD1 
968  C  CD2 . LEU A 118 ? 0.1240 0.1555 0.1315 -0.0099 -0.0017 0.0233  118 LEU A CD2 
969  N  N   . HIS A 119 ? 0.1129 0.1097 0.0962 0.0035  -0.0011 -0.0103 119 HIS A N   
970  C  CA  . HIS A 119 ? 0.1074 0.1108 0.1043 0.0127  0.0043  -0.0163 119 HIS A CA  
971  C  C   . HIS A 119 ? 0.1174 0.1188 0.0953 0.0188  0.0103  -0.0121 119 HIS A C   
972  O  O   . HIS A 119 ? 0.1395 0.1208 0.0906 0.0302  0.0107  -0.0119 119 HIS A O   
973  C  CB  . HIS A 119 ? 0.1007 0.1407 0.0964 -0.0010 0.0054  0.0190  119 HIS A CB  
974  C  CG  . HIS A 119 ? 0.1226 0.1203 0.0928 0.0009  -0.0062 -0.0022 119 HIS A CG  
975  N  ND1 . HIS A 119 ? 0.1291 0.1507 0.0756 0.0199  -0.0018 -0.0051 119 HIS A ND1 
976  C  CD2 . HIS A 119 ? 0.1600 0.1425 0.0633 0.0108  -0.0117 0.0075  119 HIS A CD2 
977  C  CE1 . HIS A 119 ? 0.1167 0.1494 0.1009 -0.0095 -0.0086 0.0124  119 HIS A CE1 
978  N  NE2 . HIS A 119 ? 0.1219 0.1291 0.1002 0.0059  0.0081  -0.0027 119 HIS A NE2 
979  N  N   . LEU A 120 ? 0.0953 0.1230 0.1176 0.0149  0.0009  -0.0136 120 LEU A N   
980  C  CA  . LEU A 120 ? 0.1186 0.1110 0.1086 0.0118  -0.0077 -0.0135 120 LEU A CA  
981  C  C   . LEU A 120 ? 0.1014 0.1101 0.0912 0.0150  -0.0012 -0.0061 120 LEU A C   
982  O  O   . LEU A 120 ? 0.1235 0.1156 0.0865 0.0062  -0.0009 -0.0032 120 LEU A O   
983  C  CB  . LEU A 120 ? 0.1032 0.1359 0.1327 0.0175  -0.0054 -0.0190 120 LEU A CB  
984  C  CG  . LEU A 120 ? 0.1465 0.1575 0.0675 -0.0046 0.0102  -0.0088 120 LEU A CG  
985  C  CD1 . LEU A 120 ? 0.2005 0.1468 0.2054 -0.0563 0.0287  -0.0085 120 LEU A CD1 
986  C  CD2 . LEU A 120 ? 0.1666 0.1761 0.1074 0.0245  0.0010  -0.0044 120 LEU A CD2 
987  N  N   . VAL A 121 ? 0.1307 0.1073 0.1057 -0.0015 0.0111  0.0021  121 VAL A N   
988  C  CA  . VAL A 121 ? 0.1206 0.1088 0.1032 -0.0044 0.0206  0.0104  121 VAL A CA  
989  C  C   . VAL A 121 ? 0.1213 0.1199 0.0862 0.0026  0.0000  -0.0025 121 VAL A C   
990  O  O   . VAL A 121 ? 0.1597 0.1260 0.0908 0.0075  -0.0038 0.0073  121 VAL A O   
991  C  CB  . VAL A 121 ? 0.1226 0.1181 0.1151 -0.0034 0.0208  0.0085  121 VAL A CB  
992  C  CG1 . VAL A 121 ? 0.1328 0.1465 0.1232 -0.0088 0.0133  0.0000  121 VAL A CG1 
993  C  CG2 . VAL A 121 ? 0.1289 0.1336 0.1674 0.0083  0.0139  -0.0053 121 VAL A CG2 
994  N  N   . HIS A 122 ? 0.1310 0.1109 0.1000 0.0001  -0.0055 -0.0158 122 HIS A N   
995  C  CA  . HIS A 122 ? 0.1208 0.1137 0.1395 0.0054  0.0039  -0.0057 122 HIS A CA  
996  C  C   . HIS A 122 ? 0.1507 0.1107 0.1113 0.0073  -0.0018 -0.0063 122 HIS A C   
997  O  O   . HIS A 122 ? 0.1586 0.1232 0.1280 0.0000  -0.0110 0.0064  122 HIS A O   
998  C  CB  . HIS A 122 ? 0.1360 0.1291 0.1201 -0.0006 0.0069  -0.0095 122 HIS A CB  
999  C  CG  . HIS A 122 ? 0.1423 0.1176 0.0988 0.0114  0.0136  -0.0269 122 HIS A CG  
1000 N  ND1 . HIS A 122 ? 0.1311 0.1213 0.1323 0.0166  0.0171  -0.0176 122 HIS A ND1 
1001 C  CD2 . HIS A 122 ? 0.1342 0.1668 0.1068 -0.0097 0.0293  -0.0222 122 HIS A CD2 
1002 C  CE1 . HIS A 122 ? 0.1307 0.1419 0.1252 0.0034  0.0193  -0.0019 122 HIS A CE1 
1003 N  NE2 . HIS A 122 ? 0.1412 0.1380 0.1342 0.0039  0.0064  -0.0076 122 HIS A NE2 
1004 N  N   . TRP A 123 ? 0.1592 0.1102 0.1066 0.0050  0.0048  -0.0141 123 TRP A N   
1005 C  CA  . TRP A 123 ? 0.1427 0.1132 0.1307 -0.0099 0.0240  -0.0298 123 TRP A CA  
1006 C  C   . TRP A 123 ? 0.1577 0.1231 0.1216 0.0033  0.0006  -0.0243 123 TRP A C   
1007 O  O   . TRP A 123 ? 0.1562 0.1454 0.1504 0.0064  -0.0048 -0.0209 123 TRP A O   
1008 C  CB  . TRP A 123 ? 0.1772 0.1367 0.1072 -0.0221 -0.0111 0.0148  123 TRP A CB  
1009 C  CG  . TRP A 123 ? 0.1782 0.1266 0.1093 -0.0098 -0.0211 -0.0042 123 TRP A CG  
1010 C  CD1 . TRP A 123 ? 0.2362 0.1711 0.1156 0.0324  -0.0313 -0.0167 123 TRP A CD1 
1011 C  CD2 . TRP A 123 ? 0.2079 0.1342 0.1064 -0.0100 -0.0146 -0.0061 123 TRP A CD2 
1012 N  NE1 . TRP A 123 ? 0.2960 0.1479 0.1421 0.0122  -0.0609 -0.0040 123 TRP A NE1 
1013 C  CE2 . TRP A 123 ? 0.3017 0.1244 0.1283 -0.0145 -0.0424 0.0148  123 TRP A CE2 
1014 C  CE3 . TRP A 123 ? 0.2576 0.1183 0.1280 -0.0047 -0.0095 -0.0003 123 TRP A CE3 
1015 C  CZ2 . TRP A 123 ? 0.3180 0.1497 0.1455 0.0113  -0.0491 0.0131  123 TRP A CZ2 
1016 C  CZ3 . TRP A 123 ? 0.2570 0.1351 0.1534 -0.0234 -0.0245 0.0296  123 TRP A CZ3 
1017 C  CH2 . TRP A 123 ? 0.3687 0.1718 0.1364 -0.0258 -0.0255 -0.0152 123 TRP A CH2 
1018 N  N   . ASN A 124 ? 0.1842 0.1418 0.1144 0.0071  -0.0004 -0.0347 124 ASN A N   
1019 C  CA  . ASN A 124 ? 0.2064 0.1317 0.1562 0.0243  0.0107  -0.0336 124 ASN A CA  
1020 C  C   . ASN A 124 ? 0.1717 0.1306 0.1203 0.0064  0.0071  -0.0403 124 ASN A C   
1021 O  O   . ASN A 124 ? 0.1700 0.1398 0.1673 0.0026  0.0041  -0.0341 124 ASN A O   
1022 C  CB  . ASN A 124 ? 0.2133 0.1923 0.1316 0.0091  0.0166  -0.0267 124 ASN A CB  
1023 C  CG  . ASN A 124 ? 0.1803 0.1984 0.1346 0.0139  0.0097  -0.0200 124 ASN A CG  
1024 O  OD1 . ASN A 124 ? 0.2519 0.1951 0.1561 0.0361  0.0175  -0.0300 124 ASN A OD1 
1025 N  ND2 . ASN A 124 ? 0.2521 0.1668 0.1351 -0.0252 -0.0133 -0.0100 124 ASN A ND2 
1026 N  N   . THR A 125 ? 0.1890 0.1330 0.1756 0.0357  -0.0071 -0.0302 125 THR A N   
1027 C  CA  . THR A 125 ? 0.2057 0.1404 0.2186 0.0122  -0.0372 -0.0239 125 THR A CA  
1028 C  C   . THR A 125 ? 0.1863 0.1141 0.1993 0.0299  0.0160  -0.0308 125 THR A C   
1029 O  O   . THR A 125 ? 0.2465 0.1375 0.2325 0.0159  -0.0236 0.0016  125 THR A O   
1030 C  CB  . THR A 125 ? 0.2076 0.2109 0.2417 0.0238  -0.0387 -0.0189 125 THR A CB  
1031 O  OG1 . THR A 125 ? 0.2319 0.2014 0.3355 0.0400  0.0413  -0.0214 125 THR A OG1 
1032 C  CG2 . THR A 125 ? 0.2400 0.3209 0.2355 -0.0209 -0.0548 -0.0362 125 THR A CG2 
1033 N  N   . LYS A 126 ? 0.2300 0.1389 0.1971 0.0242  -0.0066 -0.0511 127 LYS A N   
1034 C  CA  . LYS A 126 ? 0.3553 0.1630 0.2454 -0.0489 0.0226  -0.0621 127 LYS A CA  
1035 C  C   . LYS A 126 ? 0.2691 0.1327 0.2967 0.0009  -0.0488 -0.0498 127 LYS A C   
1036 O  O   . LYS A 126 ? 0.3218 0.1301 0.4496 -0.0036 -0.0522 -0.0908 127 LYS A O   
1037 C  CB  . LYS A 126 ? 0.4300 0.1565 0.2666 -0.0205 0.0363  -0.0348 127 LYS A CB  
1038 C  CG  . LYS A 126 ? 0.4084 0.2364 0.1948 -0.0494 -0.0089 -0.0713 127 LYS A CG  
1039 C  CD  . LYS A 126 ? 0.4085 0.5025 0.1718 -0.0934 0.0564  -0.0959 127 LYS A CD  
1040 C  CE  . LYS A 126 ? 0.5248 0.5377 0.3283 0.0201  -0.0027 -0.0278 127 LYS A CE  
1041 N  NZ  . LYS A 126 ? 0.6983 0.5363 0.3495 -0.1541 -0.2006 -0.0546 127 LYS A NZ  
1042 N  N   . TYR A 127 ? 0.2133 0.1460 0.2044 0.0036  -0.0391 -0.0208 128 TYR A N   
1043 C  CA  . TYR A 127 ? 0.2217 0.1627 0.2275 0.0135  -0.0317 0.0156  128 TYR A CA  
1044 C  C   . TYR A 127 ? 0.2069 0.1221 0.2447 0.0078  -0.0515 0.0299  128 TYR A C   
1045 O  O   . TYR A 127 ? 0.2259 0.1614 0.3118 -0.0161 -0.0471 0.0159  128 TYR A O   
1046 C  CB  . TYR A 127 ? 0.2122 0.1344 0.2055 0.0013  -0.0358 -0.0182 128 TYR A CB  
1047 C  CG  . TYR A 127 ? 0.2456 0.1427 0.2072 0.0132  -0.0454 -0.0135 128 TYR A CG  
1048 C  CD1 . TYR A 127 ? 0.2597 0.1518 0.2159 -0.0023 -0.0286 -0.0296 128 TYR A CD1 
1049 C  CD2 . TYR A 127 ? 0.2583 0.1516 0.2027 0.0067  0.0036  -0.0115 128 TYR A CD2 
1050 C  CE1 . TYR A 127 ? 0.3068 0.1732 0.2263 -0.0078 -0.0434 -0.0387 128 TYR A CE1 
1051 C  CE2 . TYR A 127 ? 0.2824 0.1991 0.1975 0.0379  -0.0441 -0.0697 128 TYR A CE2 
1052 C  CZ  . TYR A 127 ? 0.2799 0.1750 0.1973 0.0263  -0.0464 -0.0417 128 TYR A CZ  
1053 O  OH  . TYR A 127 ? 0.3119 0.2115 0.1886 0.0166  -0.0306 -0.0794 128 TYR A OH  
1054 N  N   . GLY A 128 ? 0.2248 0.1489 0.2820 -0.0230 -0.0675 0.0450  129 GLY A N   
1055 C  CA  . GLY A 128 ? 0.2526 0.2105 0.2651 -0.0356 -0.0282 0.0623  129 GLY A CA  
1056 C  C   . GLY A 128 ? 0.2616 0.1732 0.2374 -0.0462 -0.0746 0.0759  129 GLY A C   
1057 O  O   . GLY A 128 ? 0.4659 0.1939 0.2611 -0.0260 -0.1601 0.0688  129 GLY A O   
1058 N  N   A ASP A 129 ? 0.2802 0.1671 0.2677 -0.0294 -0.0341 0.0581  130 ASP A N   
1059 N  N   B ASP A 129 ? 0.2741 0.2366 0.2345 -0.0054 -0.0326 0.0656  130 ASP A N   
1060 C  CA  A ASP A 129 ? 0.3047 0.1820 0.2073 -0.0848 -0.0582 0.0697  130 ASP A CA  
1061 C  CA  B ASP A 129 ? 0.2115 0.2409 0.2277 -0.0873 -0.0187 0.0586  130 ASP A CA  
1062 C  C   A ASP A 129 ? 0.3407 0.2308 0.1969 -0.0378 -0.0912 0.0418  130 ASP A C   
1063 C  C   B ASP A 129 ? 0.1901 0.2590 0.2269 -0.0602 -0.0436 0.0288  130 ASP A C   
1064 O  O   A ASP A 129 ? 0.3265 0.1951 0.1918 0.0040  -0.0951 0.0600  130 ASP A O   
1065 O  O   B ASP A 129 ? 0.2215 0.3180 0.1948 -0.0135 -0.0208 0.0165  130 ASP A O   
1066 C  CB  A ASP A 129 ? 0.3211 0.1742 0.2159 -0.0776 -0.0082 0.0435  130 ASP A CB  
1067 C  CB  B ASP A 129 ? 0.2099 0.2472 0.1957 -0.0884 0.0216  -0.0222 130 ASP A CB  
1068 C  CG  A ASP A 129 ? 0.2828 0.1677 0.1991 -0.0088 0.0032  -0.0201 130 ASP A CG  
1069 C  CG  B ASP A 129 ? 0.3155 0.2314 0.1786 0.0155  -0.0022 0.0433  130 ASP A CG  
1070 O  OD1 A ASP A 129 ? 0.3836 0.2116 0.1936 -0.0522 -0.0348 0.0233  130 ASP A OD1 
1071 O  OD1 B ASP A 129 ? 0.4184 0.3445 0.1566 0.0555  0.0029  0.0461  130 ASP A OD1 
1072 O  OD2 A ASP A 129 ? 0.3499 0.2294 0.3122 -0.0064 0.1025  0.0120  130 ASP A OD2 
1073 O  OD2 B ASP A 129 ? 0.2552 0.3273 0.1965 -0.0595 0.0405  0.0969  130 ASP A OD2 
1074 N  N   . ALA A 130 ? 0.2820 0.2224 0.1917 -0.0236 -0.0350 0.0572  131 ALA A N   
1075 C  CA  . ALA A 130 ? 0.2526 0.2332 0.1771 -0.0264 -0.0575 0.0160  131 ALA A CA  
1076 C  C   . ALA A 130 ? 0.2375 0.2418 0.1496 -0.0449 -0.0117 0.0176  131 ALA A C   
1077 O  O   . ALA A 130 ? 0.2287 0.1930 0.1365 -0.0209 -0.0037 0.0035  131 ALA A O   
1078 C  CB  . ALA A 130 ? 0.2612 0.2511 0.1971 -0.0342 -0.0065 -0.0281 131 ALA A CB  
1079 N  N   . GLY A 131 ? 0.3409 0.3003 0.1426 -0.0511 0.0265  0.0408  132 GLY A N   
1080 C  CA  . GLY A 131 ? 0.3466 0.4324 0.1894 -0.0846 0.0302  -0.0051 132 GLY A CA  
1081 C  C   . GLY A 131 ? 0.2302 0.2301 0.1901 -0.0614 0.0303  0.0428  132 GLY A C   
1082 O  O   . GLY A 131 ? 0.2470 0.2735 0.2037 -0.0505 0.0010  0.0471  132 GLY A O   
1083 N  N   A LYS A 132 ? 0.2554 0.2249 0.2508 -0.0505 0.0130  0.0526  133 LYS A N   
1084 N  N   B LYS A 132 ? 0.2395 0.2312 0.2860 -0.0421 0.0168  0.0549  133 LYS A N   
1085 C  CA  A LYS A 132 ? 0.2143 0.1865 0.2576 -0.0429 -0.0201 0.0454  133 LYS A CA  
1086 C  CA  B LYS A 132 ? 0.1840 0.1588 0.3093 -0.0330 -0.0237 0.0407  133 LYS A CA  
1087 C  C   A LYS A 132 ? 0.2246 0.1818 0.1747 -0.0406 -0.0256 -0.0003 133 LYS A C   
1088 C  C   B LYS A 132 ? 0.2126 0.1876 0.1835 -0.0325 -0.0297 -0.0080 133 LYS A C   
1089 O  O   A LYS A 132 ? 0.2497 0.1747 0.1941 -0.0269 -0.0547 0.0043  133 LYS A O   
1090 O  O   B LYS A 132 ? 0.2420 0.1750 0.1944 -0.0350 -0.0533 0.0000  133 LYS A O   
1091 C  CB  A LYS A 132 ? 0.2151 0.2055 0.2648 -0.0251 0.0265  0.1237  133 LYS A CB  
1092 C  CB  B LYS A 132 ? 0.1007 0.2212 0.3858 -0.0087 0.0285  0.0490  133 LYS A CB  
1093 C  CG  A LYS A 132 ? 0.3019 0.3014 0.1043 0.0033  -0.0053 0.0723  133 LYS A CG  
1094 C  CG  B LYS A 132 ? 0.1879 0.2817 0.3808 -0.0438 0.0421  0.0837  133 LYS A CG  
1095 C  CD  A LYS A 132 ? 0.2620 0.3345 0.2465 -0.1183 -0.0023 0.0569  133 LYS A CD  
1096 C  CD  B LYS A 132 ? 0.1648 0.2684 0.4144 0.0825  0.0037  0.0825  133 LYS A CD  
1097 C  CE  A LYS A 132 ? 0.4684 0.4073 0.1714 -0.1159 -0.0331 0.1211  133 LYS A CE  
1098 C  CE  B LYS A 132 ? 0.2925 0.3536 0.4842 0.0741  0.0907  -0.0315 133 LYS A CE  
1099 N  NZ  A LYS A 132 ? 0.3157 0.3829 0.2348 0.0772  -0.0434 -0.0637 133 LYS A NZ  
1100 N  NZ  B LYS A 132 ? 0.3441 0.2835 0.3180 0.1057  0.0113  -0.0353 133 LYS A NZ  
1101 N  N   . ALA A 133 ? 0.2000 0.1626 0.1615 -0.0298 -0.0011 0.0173  134 ALA A N   
1102 C  CA  . ALA A 133 ? 0.1747 0.1547 0.1393 -0.0190 0.0060  0.0002  134 ALA A CA  
1103 C  C   . ALA A 133 ? 0.1706 0.1532 0.1210 -0.0185 0.0053  -0.0030 134 ALA A C   
1104 O  O   . ALA A 133 ? 0.1725 0.1847 0.1329 -0.0108 0.0015  0.0013  134 ALA A O   
1105 C  CB  . ALA A 133 ? 0.1789 0.1635 0.0971 -0.0414 0.0118  -0.0166 134 ALA A CB  
1106 N  N   . SER A 134 ? 0.1860 0.1596 0.1283 -0.0264 0.0121  -0.0132 135 SER A N   
1107 C  CA  . SER A 134 ? 0.2068 0.1804 0.1145 0.0066  0.0033  -0.0054 135 SER A CA  
1108 C  C   . SER A 134 ? 0.1997 0.1735 0.1477 -0.0181 0.0237  0.0222  135 SER A C   
1109 O  O   . SER A 134 ? 0.1964 0.2104 0.1983 0.0099  0.0203  0.0111  135 SER A O   
1110 C  CB  . SER A 134 ? 0.2598 0.2195 0.1379 0.0137  0.0512  -0.0185 135 SER A CB  
1111 O  OG  . SER A 134 ? 0.2734 0.2767 0.1777 0.0111  0.0488  -0.0248 135 SER A OG  
1112 N  N   . GLN A 135 ? 0.1808 0.1802 0.1689 -0.0304 0.0058  -0.0010 136 GLN A N   
1113 C  CA  . GLN A 135 ? 0.1872 0.1973 0.1858 -0.0111 -0.0175 0.0071  136 GLN A CA  
1114 C  C   . GLN A 135 ? 0.2138 0.1799 0.1770 -0.0337 -0.0326 0.0039  136 GLN A C   
1115 O  O   . GLN A 135 ? 0.2760 0.2537 0.2231 -0.0580 -0.0766 -0.0159 136 GLN A O   
1116 C  CB  . GLN A 135 ? 0.2221 0.2416 0.1984 -0.0939 -0.0111 -0.0196 136 GLN A CB  
1117 C  CG  . GLN A 135 ? 0.2651 0.2892 0.1966 -0.0420 0.0106  0.0115  136 GLN A CG  
1118 C  CD  . GLN A 135 ? 0.2849 0.4717 0.2903 0.0267  0.0044  -0.0006 136 GLN A CD  
1119 O  OE1 . GLN A 135 ? 0.2831 0.6001 0.5156 0.1234  -0.0160 0.0418  136 GLN A OE1 
1120 N  NE2 . GLN A 135 ? 0.6113 0.6140 0.3184 0.0209  -0.1089 -0.0257 136 GLN A NE2 
1121 N  N   . GLN A 136 ? 0.2145 0.1811 0.1284 -0.0011 -0.0122 -0.0185 137 GLN A N   
1122 C  CA  . GLN A 136 ? 0.2372 0.1925 0.1070 -0.0034 -0.0195 -0.0356 137 GLN A CA  
1123 C  C   . GLN A 136 ? 0.2111 0.2184 0.1065 -0.0035 -0.0002 -0.0328 137 GLN A C   
1124 O  O   . GLN A 136 ? 0.2025 0.1779 0.1143 0.0115  0.0057  -0.0276 137 GLN A O   
1125 C  CB  . GLN A 136 ? 0.2382 0.2212 0.1605 0.0241  -0.0313 -0.0550 137 GLN A CB  
1126 C  CG  . GLN A 136 ? 0.2940 0.2305 0.2180 0.0506  0.0175  -0.0125 137 GLN A CG  
1127 C  CD  . GLN A 136 ? 0.3092 0.3268 0.2332 -0.0068 -0.0013 0.0445  137 GLN A CD  
1128 O  OE1 . GLN A 136 ? 0.3981 0.2154 0.2674 -0.0301 -0.0688 -0.0519 137 GLN A OE1 
1129 N  NE2 . GLN A 136 ? 0.4273 0.3985 0.4056 -0.0598 0.0746  0.0848  137 GLN A NE2 
1130 N  N   . PRO A 137 ? 0.2321 0.2183 0.1137 0.0154  -0.0274 -0.0263 138 PRO A N   
1131 C  CA  . PRO A 137 ? 0.2454 0.2457 0.1040 -0.0209 -0.0279 -0.0103 138 PRO A CA  
1132 C  C   . PRO A 137 ? 0.2285 0.2274 0.0628 0.0174  -0.0029 -0.0256 138 PRO A C   
1133 O  O   . PRO A 137 ? 0.2918 0.2172 0.1763 0.0363  -0.0066 -0.0070 138 PRO A O   
1134 C  CB  . PRO A 137 ? 0.3248 0.3438 0.0942 0.0325  -0.0419 -0.0220 138 PRO A CB  
1135 C  CG  . PRO A 137 ? 0.3854 0.3629 0.1004 -0.0585 -0.0615 -0.0395 138 PRO A CG  
1136 C  CD  . PRO A 137 ? 0.2677 0.3209 0.0900 -0.0413 -0.0378 -0.0635 138 PRO A CD  
1137 N  N   . ASP A 138 ? 0.2174 0.2075 0.0908 0.0077  -0.0105 -0.0141 139 ASP A N   
1138 C  CA  . ASP A 138 ? 0.2436 0.2395 0.0732 -0.0022 0.0091  -0.0278 139 ASP A CA  
1139 C  C   . ASP A 138 ? 0.1897 0.1729 0.0926 -0.0258 0.0124  -0.0129 139 ASP A C   
1140 O  O   . ASP A 138 ? 0.2047 0.2090 0.1208 -0.0063 -0.0094 -0.0203 139 ASP A O   
1141 C  CB  . ASP A 138 ? 0.2796 0.2795 0.1304 0.0484  0.0209  -0.0686 139 ASP A CB  
1142 C  CG  . ASP A 138 ? 0.2361 0.3074 0.1342 0.0394  -0.0287 -0.0677 139 ASP A CG  
1143 O  OD1 . ASP A 138 ? 0.2723 0.2364 0.2191 0.0314  -0.0247 -0.0800 139 ASP A OD1 
1144 O  OD2 . ASP A 138 ? 0.3557 0.3574 0.2583 0.1085  0.0365  -0.1069 139 ASP A OD2 
1145 N  N   . GLY A 139 ? 0.1655 0.1750 0.0980 -0.0012 0.0144  -0.0113 140 GLY A N   
1146 C  CA  . GLY A 139 ? 0.1817 0.1518 0.1000 -0.0211 -0.0176 -0.0114 140 GLY A CA  
1147 C  C   . GLY A 139 ? 0.1673 0.1392 0.0892 -0.0060 0.0022  -0.0135 140 GLY A C   
1148 O  O   . GLY A 139 ? 0.1700 0.1426 0.0946 0.0168  -0.0048 -0.0150 140 GLY A O   
1149 N  N   . LEU A 140 ? 0.1386 0.1314 0.0946 -0.0160 0.0173  -0.0004 141 LEU A N   
1150 C  CA  . LEU A 140 ? 0.1333 0.1201 0.1072 -0.0026 0.0216  -0.0174 141 LEU A CA  
1151 C  C   . LEU A 140 ? 0.1307 0.1304 0.0995 -0.0012 0.0009  -0.0060 141 LEU A C   
1152 O  O   . LEU A 140 ? 0.1487 0.1190 0.0899 0.0119  0.0095  -0.0032 141 LEU A O   
1153 C  CB  . LEU A 140 ? 0.1550 0.1568 0.0921 0.0086  0.0280  -0.0126 141 LEU A CB  
1154 C  CG  . LEU A 140 ? 0.1784 0.1525 0.1242 0.0330  0.0422  0.0289  141 LEU A CG  
1155 C  CD1 . LEU A 140 ? 0.1618 0.2152 0.1602 0.0557  0.0264  -0.0097 141 LEU A CD1 
1156 C  CD2 . LEU A 140 ? 0.1991 0.1795 0.1265 0.0315  0.0089  0.0358  141 LEU A CD2 
1157 N  N   . ALA A 141 ? 0.1390 0.1176 0.1044 -0.0077 0.0048  -0.0219 142 ALA A N   
1158 C  CA  . ALA A 141 ? 0.1400 0.1226 0.1220 -0.0114 0.0083  -0.0162 142 ALA A CA  
1159 C  C   . ALA A 141 ? 0.1412 0.1206 0.1115 -0.0013 -0.0079 -0.0111 142 ALA A C   
1160 O  O   . ALA A 141 ? 0.1414 0.1295 0.1138 0.0053  -0.0069 -0.0027 142 ALA A O   
1161 C  CB  . ALA A 141 ? 0.1333 0.1796 0.1183 -0.0118 0.0148  -0.0234 142 ALA A CB  
1162 N  N   . VAL A 142 ? 0.1285 0.1125 0.1171 0.0043  0.0174  -0.0156 143 VAL A N   
1163 C  CA  . VAL A 142 ? 0.1395 0.1448 0.1045 0.0038  0.0201  -0.0219 143 VAL A CA  
1164 C  C   . VAL A 142 ? 0.1277 0.1220 0.0785 0.0006  0.0038  0.0005  143 VAL A C   
1165 O  O   . VAL A 142 ? 0.1455 0.1449 0.0840 0.0099  -0.0011 -0.0013 143 VAL A O   
1166 C  CB  . VAL A 142 ? 0.1250 0.1417 0.0743 0.0048  0.0210  -0.0201 143 VAL A CB  
1167 C  CG1 . VAL A 142 ? 0.1447 0.1864 0.0750 0.0248  0.0239  -0.0421 143 VAL A CG1 
1168 C  CG2 . VAL A 142 ? 0.1289 0.1926 0.0998 -0.0111 0.0156  0.0216  143 VAL A CG2 
1169 N  N   . LEU A 143 ? 0.1186 0.1172 0.0983 0.0059  0.0113  -0.0154 144 LEU A N   
1170 C  CA  . LEU A 143 ? 0.1099 0.1448 0.1221 0.0016  0.0148  -0.0026 144 LEU A CA  
1171 C  C   . LEU A 143 ? 0.1205 0.1351 0.0996 -0.0143 -0.0005 0.0003  144 LEU A C   
1172 O  O   . LEU A 143 ? 0.1559 0.1301 0.1048 -0.0054 0.0122  0.0051  144 LEU A O   
1173 C  CB  . LEU A 143 ? 0.1385 0.1499 0.1357 -0.0070 -0.0070 0.0343  144 LEU A CB  
1174 C  CG  . LEU A 143 ? 0.1301 0.1790 0.1451 -0.0036 0.0082  0.0186  144 LEU A CG  
1175 C  CD1 . LEU A 143 ? 0.1717 0.2353 0.1423 -0.0161 0.0118  0.0461  144 LEU A CD1 
1176 C  CD2 . LEU A 143 ? 0.1249 0.2651 0.1437 0.0279  0.0068  -0.0268 144 LEU A CD2 
1177 N  N   . GLY A 144 ? 0.1330 0.1239 0.0925 0.0044  0.0027  -0.0168 145 GLY A N   
1178 C  CA  . GLY A 144 ? 0.1232 0.1152 0.0824 -0.0116 0.0152  -0.0159 145 GLY A CA  
1179 C  C   . GLY A 144 ? 0.1151 0.1009 0.0863 -0.0023 0.0215  -0.0030 145 GLY A C   
1180 O  O   . GLY A 144 ? 0.1444 0.1398 0.1014 -0.0060 0.0328  0.0100  145 GLY A O   
1181 N  N   . ILE A 145 ? 0.1179 0.1058 0.1073 0.0044  0.0106  -0.0137 146 ILE A N   
1182 C  CA  . ILE A 145 ? 0.1214 0.1177 0.1287 -0.0027 -0.0130 -0.0079 146 ILE A CA  
1183 C  C   . ILE A 145 ? 0.1366 0.1189 0.1011 -0.0006 -0.0026 0.0027  146 ILE A C   
1184 O  O   . ILE A 145 ? 0.1368 0.1201 0.1313 0.0041  0.0241  0.0015  146 ILE A O   
1185 C  CB  . ILE A 145 ? 0.1272 0.1269 0.1296 -0.0031 -0.0117 0.0031  146 ILE A CB  
1186 C  CG1 . ILE A 145 ? 0.1703 0.1430 0.1298 0.0261  -0.0099 0.0119  146 ILE A CG1 
1187 C  CG2 . ILE A 145 ? 0.1416 0.1574 0.1687 -0.0008 -0.0372 -0.0141 146 ILE A CG2 
1188 C  CD1 . ILE A 145 ? 0.1502 0.1415 0.1567 0.0119  -0.0083 0.0261  146 ILE A CD1 
1189 N  N   . PHE A 146 ? 0.1407 0.1129 0.1063 0.0173  0.0053  0.0046  147 PHE A N   
1190 C  CA  . PHE A 146 ? 0.1523 0.1038 0.1289 0.0078  -0.0098 0.0167  147 PHE A CA  
1191 C  C   . PHE A 146 ? 0.1297 0.1289 0.1331 0.0073  -0.0041 -0.0074 147 PHE A C   
1192 O  O   . PHE A 146 ? 0.1344 0.1525 0.1626 0.0013  0.0036  0.0018  147 PHE A O   
1193 C  CB  . PHE A 146 ? 0.1447 0.1481 0.1116 0.0047  -0.0126 0.0274  147 PHE A CB  
1194 C  CG  . PHE A 146 ? 0.1401 0.1150 0.1156 0.0107  0.0023  0.0082  147 PHE A CG  
1195 C  CD1 . PHE A 146 ? 0.1494 0.1289 0.1212 0.0186  -0.0187 0.0035  147 PHE A CD1 
1196 C  CD2 . PHE A 146 ? 0.1597 0.1230 0.1292 0.0097  0.0027  -0.0146 147 PHE A CD2 
1197 C  CE1 . PHE A 146 ? 0.1430 0.1385 0.0905 0.0085  0.0019  -0.0029 147 PHE A CE1 
1198 C  CE2 . PHE A 146 ? 0.1609 0.1395 0.1272 -0.0044 0.0021  0.0163  147 PHE A CE2 
1199 C  CZ  . PHE A 146 ? 0.1429 0.1483 0.1000 0.0040  0.0211  0.0058  147 PHE A CZ  
1200 N  N   . LEU A 147 ? 0.1332 0.1287 0.1306 -0.0035 0.0046  -0.0195 148 LEU A N   
1201 C  CA  . LEU A 147 ? 0.1368 0.1410 0.1174 0.0232  -0.0044 -0.0206 148 LEU A CA  
1202 C  C   . LEU A 147 ? 0.1156 0.1386 0.1303 0.0125  0.0077  -0.0358 148 LEU A C   
1203 O  O   . LEU A 147 ? 0.1247 0.1328 0.1732 0.0031  0.0046  0.0030  148 LEU A O   
1204 C  CB  . LEU A 147 ? 0.1565 0.1438 0.1288 0.0266  0.0070  -0.0232 148 LEU A CB  
1205 C  CG  . LEU A 147 ? 0.1377 0.1197 0.1351 0.0072  0.0075  -0.0167 148 LEU A CG  
1206 C  CD1 . LEU A 147 ? 0.1867 0.1141 0.1699 -0.0033 -0.0278 -0.0195 148 LEU A CD1 
1207 C  CD2 . LEU A 147 ? 0.1657 0.1793 0.1237 -0.0055 0.0100  -0.0008 148 LEU A CD2 
1208 N  N   . LYS A 148 ? 0.1469 0.1310 0.1298 -0.0106 -0.0066 -0.0059 149 LYS A N   
1209 C  CA  . LYS A 148 ? 0.1696 0.1284 0.1476 -0.0047 -0.0179 -0.0130 149 LYS A CA  
1210 C  C   . LYS A 148 ? 0.1702 0.1366 0.1359 0.0190  -0.0252 -0.0089 149 LYS A C   
1211 O  O   . LYS A 148 ? 0.2034 0.1721 0.1443 0.0525  -0.0366 -0.0190 149 LYS A O   
1212 C  CB  . LYS A 148 ? 0.1917 0.2300 0.1461 -0.0361 -0.0054 0.0082  149 LYS A CB  
1213 C  CG  . LYS A 148 ? 0.2126 0.1753 0.1907 0.0170  0.0174  0.0168  149 LYS A CG  
1214 C  CD  . LYS A 148 ? 0.2623 0.3197 0.2523 -0.0226 0.0609  0.0590  149 LYS A CD  
1215 C  CE  . LYS A 148 ? 0.2733 0.5174 0.4278 0.0066  0.1328  0.0644  149 LYS A CE  
1216 N  NZ  . LYS A 148 ? 0.4128 0.5550 0.7923 -0.1813 0.1531  0.2005  149 LYS A NZ  
1217 N  N   . VAL A 149 ? 0.1838 0.1238 0.1552 0.0170  -0.0199 -0.0095 150 VAL A N   
1218 C  CA  . VAL A 149 ? 0.1538 0.1346 0.1734 0.0115  -0.0210 -0.0167 150 VAL A CA  
1219 C  C   . VAL A 149 ? 0.1736 0.1374 0.1465 0.0065  -0.0141 -0.0075 150 VAL A C   
1220 O  O   . VAL A 149 ? 0.2155 0.1659 0.1885 0.0035  -0.0430 0.0262  150 VAL A O   
1221 C  CB  . VAL A 149 ? 0.1624 0.1412 0.1579 -0.0006 0.0039  -0.0248 150 VAL A CB  
1222 C  CG1 . VAL A 149 ? 0.1878 0.2320 0.1711 0.0058  -0.0126 -0.0592 150 VAL A CG1 
1223 C  CG2 . VAL A 149 ? 0.1590 0.1910 0.2395 -0.0197 -0.0054 0.0139  150 VAL A CG2 
1224 N  N   . GLY A 150 ? 0.1685 0.1465 0.1768 -0.0044 -0.0293 -0.0006 151 GLY A N   
1225 C  CA  . GLY A 150 ? 0.1689 0.1641 0.1738 -0.0164 -0.0215 0.0276  151 GLY A CA  
1226 C  C   . GLY A 150 ? 0.1803 0.1337 0.1386 -0.0230 0.0054  0.0072  151 GLY A C   
1227 O  O   . GLY A 150 ? 0.1815 0.1419 0.1398 -0.0043 -0.0092 -0.0080 151 GLY A O   
1228 N  N   A SER A 151 ? 0.1747 0.1693 0.1604 -0.0073 -0.0036 0.0084  152 SER A N   
1229 N  N   B SER A 151 ? 0.1635 0.1919 0.1421 -0.0128 0.0000  0.0071  152 SER A N   
1230 C  CA  A SER A 151 ? 0.1770 0.1656 0.1815 -0.0291 -0.0175 0.0107  152 SER A CA  
1231 C  CA  B SER A 151 ? 0.1641 0.1614 0.1889 0.0001  -0.0086 -0.0125 152 SER A CA  
1232 C  C   A SER A 151 ? 0.1826 0.1448 0.1302 -0.0069 0.0009  -0.0039 152 SER A C   
1233 C  C   B SER A 151 ? 0.1804 0.1597 0.1246 -0.0016 -0.0042 -0.0204 152 SER A C   
1234 O  O   A SER A 151 ? 0.1592 0.1693 0.1517 -0.0150 -0.0136 0.0047  152 SER A O   
1235 O  O   B SER A 151 ? 0.1693 0.1849 0.1568 -0.0168 -0.0179 -0.0127 152 SER A O   
1236 C  CB  A SER A 151 ? 0.1833 0.2117 0.1667 -0.0153 -0.0018 0.0257  152 SER A CB  
1237 C  CB  B SER A 151 ? 0.1772 0.1865 0.2666 -0.0165 0.0248  -0.0750 152 SER A CB  
1238 O  OG  A SER A 151 ? 0.2030 0.3402 0.1706 -0.0272 0.0156  -0.0296 152 SER A OG  
1239 O  OG  B SER A 151 ? 0.2073 0.2989 0.3219 -0.0436 0.0267  0.0449  152 SER A OG  
1240 N  N   . ALA A 152 ? 0.2213 0.1553 0.1447 -0.0034 -0.0376 -0.0193 153 ALA A N   
1241 C  CA  . ALA A 152 ? 0.2409 0.1606 0.1225 -0.0038 -0.0378 -0.0132 153 ALA A CA  
1242 C  C   . ALA A 152 ? 0.1424 0.1768 0.1476 -0.0070 -0.0130 -0.0052 153 ALA A C   
1243 O  O   . ALA A 152 ? 0.1688 0.1552 0.1991 -0.0111 -0.0001 0.0166  153 ALA A O   
1244 C  CB  . ALA A 152 ? 0.2569 0.1750 0.0910 -0.0089 0.0015  -0.0104 153 ALA A CB  
1245 N  N   . LYS A 153 ? 0.1282 0.1499 0.1617 0.0031  -0.0111 -0.0099 154 LYS A N   
1246 C  CA  . LYS A 153 ? 0.1452 0.1564 0.1244 0.0051  -0.0043 -0.0055 154 LYS A CA  
1247 C  C   . LYS A 153 ? 0.1276 0.1469 0.1277 -0.0145 -0.0048 -0.0089 154 LYS A C   
1248 O  O   . LYS A 153 ? 0.1324 0.1628 0.1397 -0.0042 -0.0017 0.0118  154 LYS A O   
1249 C  CB  . LYS A 153 ? 0.1430 0.1483 0.1359 0.0116  -0.0046 -0.0096 154 LYS A CB  
1250 C  CG  . LYS A 153 ? 0.1666 0.1592 0.1084 0.0025  0.0030  -0.0261 154 LYS A CG  
1251 C  CD  . LYS A 153 ? 0.2755 0.1682 0.0798 0.0293  0.0237  0.0012  154 LYS A CD  
1252 C  CE  . LYS A 153 ? 0.3384 0.1919 0.1564 0.0436  0.0348  -0.0309 154 LYS A CE  
1253 N  NZ  . LYS A 153 ? 0.3488 0.2935 0.1838 0.0215  0.0811  -0.0288 154 LYS A NZ  
1254 N  N   A PRO A 154 ? 0.1226 0.1619 0.1531 -0.0115 0.0000  -0.0044 155 PRO A N   
1255 N  N   B PRO A 154 ? 0.1256 0.1739 0.1161 -0.0264 -0.0064 -0.0105 155 PRO A N   
1256 C  CA  A PRO A 154 ? 0.1439 0.1681 0.1689 -0.0044 -0.0197 0.0027  155 PRO A CA  
1257 C  CA  B PRO A 154 ? 0.1555 0.1688 0.1212 -0.0033 -0.0157 -0.0097 155 PRO A CA  
1258 C  C   A PRO A 154 ? 0.1171 0.1591 0.1512 0.0184  0.0037  -0.0002 155 PRO A C   
1259 C  C   B PRO A 154 ? 0.1164 0.1618 0.1521 0.0223  0.0051  -0.0048 155 PRO A C   
1260 O  O   A PRO A 154 ? 0.1379 0.1729 0.1555 0.0089  0.0075  0.0018  155 PRO A O   
1261 O  O   B PRO A 154 ? 0.1356 0.1881 0.1618 0.0071  0.0171  -0.0035 155 PRO A O   
1262 C  CB  A PRO A 154 ? 0.1419 0.1853 0.1969 -0.0533 -0.0121 0.0388  155 PRO A CB  
1263 C  CB  B PRO A 154 ? 0.1569 0.1736 0.1971 -0.0109 -0.0310 0.0170  155 PRO A CB  
1264 C  CG  A PRO A 154 ? 0.1714 0.1423 0.1851 -0.0496 -0.0086 -0.0228 155 PRO A CG  
1265 C  CG  B PRO A 154 ? 0.1503 0.2215 0.2059 -0.0159 -0.0238 0.0290  155 PRO A CG  
1266 C  CD  A PRO A 154 ? 0.1102 0.1462 0.1907 0.0091  0.0105  0.0002  155 PRO A CD  
1267 C  CD  B PRO A 154 ? 0.1687 0.1335 0.1154 -0.0244 0.0050  0.0277  155 PRO A CD  
1268 N  N   . GLY A 155 ? 0.1229 0.1535 0.1709 0.0017  0.0097  -0.0181 156 GLY A N   
1269 C  CA  . GLY A 155 ? 0.1365 0.1637 0.1887 -0.0094 -0.0130 -0.0073 156 GLY A CA  
1270 C  C   . GLY A 155 ? 0.1498 0.1568 0.1772 0.0013  0.0084  0.0278  156 GLY A C   
1271 O  O   . GLY A 155 ? 0.1693 0.1498 0.2348 -0.0024 0.0126  0.0353  156 GLY A O   
1272 N  N   . LEU A 156 ? 0.1206 0.1476 0.1248 -0.0050 -0.0019 -0.0054 157 LEU A N   
1273 C  CA  . LEU A 156 ? 0.1176 0.1536 0.1059 -0.0122 -0.0030 -0.0083 157 LEU A CA  
1274 C  C   . LEU A 156 ? 0.1156 0.1366 0.1155 0.0065  -0.0012 -0.0127 157 LEU A C   
1275 O  O   . LEU A 156 ? 0.1415 0.1614 0.1164 -0.0072 0.0125  -0.0110 157 LEU A O   
1276 C  CB  . LEU A 156 ? 0.1324 0.1439 0.1597 -0.0086 0.0001  0.0181  157 LEU A CB  
1277 C  CG  . LEU A 156 ? 0.1252 0.1729 0.1081 -0.0053 -0.0084 -0.0026 157 LEU A CG  
1278 C  CD1 . LEU A 156 ? 0.1458 0.1993 0.1559 -0.0257 -0.0036 -0.0194 157 LEU A CD1 
1279 C  CD2 . LEU A 156 ? 0.1717 0.2084 0.1129 0.0269  -0.0172 -0.0013 157 LEU A CD2 
1280 N  N   . GLN A 157 ? 0.1436 0.1549 0.1164 0.0008  -0.0064 -0.0401 158 GLN A N   
1281 C  CA  . GLN A 157 ? 0.1265 0.1894 0.0905 -0.0259 0.0002  -0.0138 158 GLN A CA  
1282 C  C   . GLN A 157 ? 0.1156 0.1627 0.1208 0.0004  0.0092  -0.0110 158 GLN A C   
1283 O  O   . GLN A 157 ? 0.1214 0.1664 0.1205 -0.0054 0.0131  -0.0204 158 GLN A O   
1284 C  CB  . GLN A 157 ? 0.1525 0.2077 0.1217 -0.0341 -0.0117 -0.0307 158 GLN A CB  
1285 C  CG  . GLN A 157 ? 0.1993 0.1729 0.0941 -0.0078 -0.0059 0.0025  158 GLN A CG  
1286 C  CD  . GLN A 157 ? 0.1847 0.1500 0.1127 -0.0210 -0.0027 -0.0201 158 GLN A CD  
1287 O  OE1 . GLN A 157 ? 0.2328 0.1687 0.1134 -0.0146 0.0047  -0.0065 158 GLN A OE1 
1288 N  NE2 . GLN A 157 ? 0.2069 0.2023 0.1201 -0.0185 0.0103  -0.0359 158 GLN A NE2 
1289 N  N   . LYS A 158 ? 0.1306 0.1675 0.1216 0.0031  -0.0171 0.0111  159 LYS A N   
1290 C  CA  . LYS A 158 ? 0.1518 0.1578 0.1253 -0.0021 -0.0417 0.0199  159 LYS A CA  
1291 C  C   . LYS A 158 ? 0.1533 0.1438 0.1150 -0.0142 -0.0017 -0.0084 159 LYS A C   
1292 O  O   . LYS A 158 ? 0.1828 0.1775 0.1391 -0.0232 -0.0089 0.0052  159 LYS A O   
1293 C  CB  . LYS A 158 ? 0.2201 0.1639 0.1767 0.0184  -0.0414 0.0036  159 LYS A CB  
1294 C  CG  . LYS A 158 ? 0.2544 0.1757 0.2753 -0.0067 0.0068  0.0228  159 LYS A CG  
1295 C  CD  . LYS A 158 ? 0.4020 0.2216 0.2742 0.0906  0.0031  -0.0060 159 LYS A CD  
1296 C  CE  . LYS A 158 ? 0.4780 0.3495 0.2508 -0.0381 0.0087  0.0691  159 LYS A CE  
1297 N  NZ  . LYS A 158 ? 0.2356 0.3305 0.2708 -0.0004 0.0124  0.0754  159 LYS A NZ  
1298 N  N   . VAL A 159 ? 0.1442 0.1368 0.1266 0.0039  -0.0297 -0.0088 160 VAL A N   
1299 C  CA  . VAL A 159 ? 0.1448 0.1650 0.1228 -0.0157 -0.0124 0.0068  160 VAL A CA  
1300 C  C   . VAL A 159 ? 0.1605 0.1500 0.1044 -0.0074 0.0026  0.0161  160 VAL A C   
1301 O  O   . VAL A 159 ? 0.1673 0.1764 0.1263 -0.0087 0.0083  0.0046  160 VAL A O   
1302 C  CB  . VAL A 159 ? 0.1612 0.1547 0.1319 -0.0083 -0.0227 0.0004  160 VAL A CB  
1303 C  CG1 . VAL A 159 ? 0.1508 0.2111 0.1407 -0.0209 -0.0312 -0.0013 160 VAL A CG1 
1304 C  CG2 . VAL A 159 ? 0.2337 0.2012 0.1242 0.0359  -0.0261 -0.0398 160 VAL A CG2 
1305 N  N   . VAL A 160 ? 0.1524 0.1426 0.1383 -0.0099 -0.0082 -0.0143 161 VAL A N   
1306 C  CA  . VAL A 160 ? 0.2113 0.1584 0.1192 0.0302  0.0329  -0.0008 161 VAL A CA  
1307 C  C   . VAL A 160 ? 0.1544 0.1472 0.1328 -0.0004 0.0215  -0.0115 161 VAL A C   
1308 O  O   . VAL A 160 ? 0.1777 0.1652 0.1296 -0.0055 0.0411  -0.0108 161 VAL A O   
1309 C  CB  . VAL A 160 ? 0.3887 0.1600 0.1136 0.0763  0.0825  0.0186  161 VAL A CB  
1310 C  CG1 . VAL A 160 ? 0.3281 0.2316 0.2001 0.0006  0.0264  -0.0400 161 VAL A CG1 
1311 C  CG2 . VAL A 160 ? 0.4932 0.2372 0.1246 0.0955  0.0858  0.0243  161 VAL A CG2 
1312 N  N   . ASP A 161 ? 0.1659 0.1660 0.1122 -0.0188 -0.0086 -0.0200 162 ASP A N   
1313 C  CA  . ASP A 161 ? 0.1526 0.1721 0.1108 -0.0410 0.0081  -0.0158 162 ASP A CA  
1314 C  C   . ASP A 161 ? 0.1503 0.2045 0.1203 -0.0303 0.0357  -0.0067 162 ASP A C   
1315 O  O   . ASP A 161 ? 0.1813 0.2623 0.1259 -0.0236 0.0436  -0.0222 162 ASP A O   
1316 C  CB  . ASP A 161 ? 0.1513 0.2238 0.1901 -0.0378 -0.0073 -0.0266 162 ASP A CB  
1317 C  CG  . ASP A 161 ? 0.1666 0.2400 0.1558 -0.0333 -0.0114 0.0253  162 ASP A CG  
1318 O  OD1 . ASP A 161 ? 0.2106 0.2623 0.2181 -0.0293 -0.0158 -0.0099 162 ASP A OD1 
1319 O  OD2 . ASP A 161 ? 0.1689 0.2509 0.1779 -0.0277 0.0047  -0.0277 162 ASP A OD2 
1320 N  N   A VAL A 162 ? 0.1687 0.2098 0.1047 -0.0528 0.0013  0.0195  163 VAL A N   
1321 N  N   B VAL A 162 ? 0.1579 0.2000 0.1401 -0.0508 -0.0237 0.0257  163 VAL A N   
1322 C  CA  A VAL A 162 ? 0.1553 0.1729 0.1296 -0.0175 0.0171  0.0296  163 VAL A CA  
1323 C  CA  B VAL A 162 ? 0.1645 0.1645 0.1361 -0.0100 0.0146  0.0281  163 VAL A CA  
1324 C  C   A VAL A 162 ? 0.1502 0.1743 0.0983 -0.0220 0.0223  0.0051  163 VAL A C   
1325 C  C   B VAL A 162 ? 0.1623 0.1937 0.0770 -0.0105 0.0223  0.0058  163 VAL A C   
1326 O  O   A VAL A 162 ? 0.1590 0.1947 0.1004 -0.0239 0.0416  0.0017  163 VAL A O   
1327 O  O   B VAL A 162 ? 0.1522 0.1838 0.1425 -0.0170 0.0051  0.0212  163 VAL A O   
1328 C  CB  A VAL A 162 ? 0.1926 0.1677 0.1779 0.0077  0.0011  0.0450  163 VAL A CB  
1329 C  CB  B VAL A 162 ? 0.1547 0.1673 0.1678 0.0053  0.0218  0.0414  163 VAL A CB  
1330 C  CG1 A VAL A 162 ? 0.2055 0.1731 0.1951 -0.0036 -0.0011 0.0366  163 VAL A CG1 
1331 C  CG1 B VAL A 162 ? 0.1597 0.1364 0.1059 -0.0111 -0.0041 0.0125  163 VAL A CG1 
1332 C  CG2 A VAL A 162 ? 0.2154 0.2355 0.2298 -0.0538 0.0297  0.0558  163 VAL A CG2 
1333 C  CG2 B VAL A 162 ? 0.2059 0.1550 0.1627 -0.0172 0.0443  0.0666  163 VAL A CG2 
1334 N  N   . LEU A 163 ? 0.1468 0.1585 0.1270 -0.0179 0.0087  0.0008  164 LEU A N   
1335 C  CA  . LEU A 163 ? 0.1526 0.1778 0.0854 -0.0011 0.0171  0.0032  164 LEU A CA  
1336 C  C   . LEU A 163 ? 0.1772 0.1768 0.0698 0.0001  0.0078  -0.0131 164 LEU A C   
1337 O  O   . LEU A 163 ? 0.1623 0.2019 0.1076 -0.0231 0.0295  -0.0133 164 LEU A O   
1338 C  CB  . LEU A 163 ? 0.1682 0.1644 0.0847 -0.0170 0.0175  -0.0040 164 LEU A CB  
1339 C  CG  . LEU A 163 ? 0.1575 0.1604 0.0915 -0.0128 0.0167  0.0049  164 LEU A CG  
1340 C  CD1 . LEU A 163 ? 0.1624 0.1948 0.1307 0.0061  0.0179  0.0430  164 LEU A CD1 
1341 C  CD2 . LEU A 163 ? 0.1754 0.1887 0.1070 -0.0206 0.0236  -0.0274 164 LEU A CD2 
1342 N  N   . ASP A 164 ? 0.2089 0.1687 0.0863 -0.0107 0.0292  -0.0341 165 ASP A N   
1343 C  CA  . ASP A 164 ? 0.2694 0.2143 0.1018 -0.0480 0.0648  -0.0578 165 ASP A CA  
1344 C  C   . ASP A 164 ? 0.1905 0.2313 0.0802 -0.0259 0.0341  -0.0203 165 ASP A C   
1345 O  O   . ASP A 164 ? 0.2084 0.2953 0.1619 -0.0419 0.0902  -0.0330 165 ASP A O   
1346 C  CB  . ASP A 164 ? 0.2759 0.2752 0.1133 -0.0494 0.0427  -0.0804 165 ASP A CB  
1347 C  CG  . ASP A 164 ? 0.2615 0.3014 0.1879 -0.0644 0.0070  -0.0451 165 ASP A CG  
1348 O  OD1 . ASP A 164 ? 0.2572 0.3809 0.2120 -0.0425 -0.0024 0.0043  165 ASP A OD1 
1349 O  OD2 . ASP A 164 ? 0.3651 0.5430 0.2271 -0.0447 0.0529  -0.0200 165 ASP A OD2 
1350 N  N   . SER A 165 ? 0.1699 0.2155 0.1228 -0.0445 0.0174  -0.0236 166 SER A N   
1351 C  CA  . SER A 165 ? 0.2052 0.2163 0.1639 -0.0469 -0.0016 -0.0044 166 SER A CA  
1352 C  C   . SER A 165 ? 0.1919 0.2213 0.1122 -0.0372 0.0100  0.0052  166 SER A C   
1353 O  O   . SER A 165 ? 0.1886 0.2209 0.1473 -0.0424 0.0193  0.0148  166 SER A O   
1354 C  CB  . SER A 165 ? 0.2162 0.2835 0.1595 -0.0111 0.0324  0.0138  166 SER A CB  
1355 O  OG  . SER A 165 ? 0.2179 0.2336 0.1717 0.0027  0.0163  0.0253  166 SER A OG  
1356 N  N   . ILE A 166 ? 0.1584 0.1860 0.1046 -0.0152 0.0046  -0.0138 167 ILE A N   
1357 C  CA  . ILE A 166 ? 0.1454 0.1806 0.1090 -0.0168 0.0310  -0.0206 167 ILE A CA  
1358 C  C   . ILE A 166 ? 0.1583 0.1808 0.0873 0.0052  0.0323  -0.0151 167 ILE A C   
1359 O  O   . ILE A 166 ? 0.1644 0.1872 0.1090 -0.0315 0.0168  -0.0220 167 ILE A O   
1360 C  CB  . ILE A 166 ? 0.1597 0.1659 0.1088 -0.0292 0.0339  -0.0220 167 ILE A CB  
1361 C  CG1 . ILE A 166 ? 0.1430 0.1817 0.0901 -0.0193 0.0212  -0.0204 167 ILE A CG1 
1362 C  CG2 . ILE A 166 ? 0.1682 0.1675 0.1503 -0.0232 0.0374  -0.0138 167 ILE A CG2 
1363 C  CD1 . ILE A 166 ? 0.1664 0.1905 0.0845 -0.0220 0.0310  -0.0228 167 ILE A CD1 
1364 N  N   . LYS A 167 ? 0.1716 0.1693 0.1256 -0.0093 0.0403  -0.0210 168 LYS A N   
1365 C  CA  . LYS A 167 ? 0.1734 0.1958 0.1063 0.0029  0.0274  -0.0458 168 LYS A CA  
1366 C  C   . LYS A 167 ? 0.1778 0.2095 0.1359 -0.0076 0.0201  -0.0187 168 LYS A C   
1367 O  O   . LYS A 167 ? 0.1800 0.1951 0.1652 0.0240  0.0277  -0.0150 168 LYS A O   
1368 C  CB  . LYS A 167 ? 0.2194 0.2231 0.0962 0.0082  0.0319  -0.0579 168 LYS A CB  
1369 C  CG  . LYS A 167 ? 0.2325 0.2043 0.1829 0.0216  0.0300  -0.0609 168 LYS A CG  
1370 C  CD  . LYS A 167 ? 0.3359 0.3459 0.2220 0.0287  -0.0403 -0.1567 168 LYS A CD  
1371 C  CE  . LYS A 167 ? 0.3934 0.5114 0.4064 0.1020  -0.0551 -0.2332 168 LYS A CE  
1372 N  NZ  . LYS A 167 ? 0.5202 0.6041 0.3018 0.1419  0.0424  -0.1264 168 LYS A NZ  
1373 N  N   . THR A 168 ? 0.1750 0.2174 0.1536 -0.0207 0.0467  -0.0166 169 THR A N   
1374 C  CA  . THR A 168 ? 0.1749 0.2395 0.1695 -0.0323 0.0502  -0.0542 169 THR A CA  
1375 C  C   . THR A 168 ? 0.1872 0.2161 0.1235 -0.0198 0.0265  -0.0086 169 THR A C   
1376 O  O   . THR A 168 ? 0.1972 0.1936 0.1764 -0.0173 0.0318  -0.0170 169 THR A O   
1377 C  CB  . THR A 168 ? 0.2559 0.2802 0.1270 -0.0166 0.0642  -0.0288 169 THR A CB  
1378 O  OG1 . THR A 168 ? 0.2058 0.3259 0.1559 -0.0304 0.0391  -0.0281 169 THR A OG1 
1379 C  CG2 . THR A 168 ? 0.2479 0.2536 0.1714 -0.0024 0.0653  -0.0374 169 THR A CG2 
1380 N  N   . LYS A 169 ? 0.1606 0.2476 0.1404 -0.0312 0.0260  -0.0262 170 LYS A N   
1381 C  CA  . LYS A 169 ? 0.1502 0.2169 0.2151 -0.0081 -0.0044 -0.0331 170 LYS A CA  
1382 C  C   . LYS A 169 ? 0.1406 0.2452 0.1893 -0.0170 0.0572  -0.0050 170 LYS A C   
1383 O  O   . LYS A 169 ? 0.1833 0.3171 0.1865 -0.0505 0.0699  -0.0024 170 LYS A O   
1384 C  CB  . LYS A 169 ? 0.1456 0.3155 0.1757 0.0013  0.0122  -0.0561 170 LYS A CB  
1385 C  CG  . LYS A 169 ? 0.1950 0.3204 0.1687 -0.0072 -0.0057 -0.0539 170 LYS A CG  
1386 C  CD  . LYS A 169 ? 0.1448 0.3915 0.3128 -0.0068 0.0186  -0.0963 170 LYS A CD  
1387 C  CE  . LYS A 169 ? 0.3115 0.4304 0.4164 -0.1103 -0.0467 -0.1058 170 LYS A CE  
1388 N  NZ  . LYS A 169 ? 0.3430 0.7280 0.7435 -0.1328 -0.1329 -0.1667 170 LYS A NZ  
1389 N  N   . GLY A 170 ? 0.1420 0.2034 0.2119 -0.0339 0.0141  -0.0063 171 GLY A N   
1390 C  CA  . GLY A 170 ? 0.1649 0.2576 0.2138 -0.0435 0.0406  0.0491  171 GLY A CA  
1391 C  C   . GLY A 170 ? 0.2221 0.2337 0.2677 -0.0514 -0.0229 -0.0304 171 GLY A C   
1392 O  O   . GLY A 170 ? 0.3531 0.2464 0.3559 -0.1079 -0.0781 0.0399  171 GLY A O   
1393 N  N   . LYS A 171 ? 0.1567 0.2190 0.1800 -0.0277 0.0310  -0.0171 172 LYS A N   
1394 C  CA  . LYS A 171 ? 0.1678 0.2210 0.1861 -0.0148 0.0252  -0.0110 172 LYS A CA  
1395 C  C   . LYS A 171 ? 0.1570 0.1674 0.1172 -0.0266 0.0110  -0.0054 172 LYS A C   
1396 O  O   . LYS A 171 ? 0.1930 0.1975 0.1215 -0.0081 0.0210  0.0026  172 LYS A O   
1397 C  CB  . LYS A 171 ? 0.1953 0.2368 0.1370 -0.0480 0.0544  -0.0152 172 LYS A CB  
1398 C  CG  . LYS A 171 ? 0.2336 0.2100 0.2117 -0.0104 0.0812  -0.0499 172 LYS A CG  
1399 C  CD  . LYS A 171 ? 0.2885 0.2296 0.1872 -0.0488 0.0223  -0.0044 172 LYS A CD  
1400 C  CE  . LYS A 171 ? 0.3572 0.3057 0.2552 -0.0358 -0.0185 0.0267  172 LYS A CE  
1401 N  NZ  . LYS A 171 ? 0.4363 0.3838 0.2138 -0.0911 0.0254  0.0237  172 LYS A NZ  
1402 N  N   . SER A 172 ? 0.1471 0.1732 0.1486 -0.0083 0.0314  0.0212  173 SER A N   
1403 C  CA  . SER A 172 ? 0.1612 0.1904 0.1599 -0.0197 0.0493  0.0139  173 SER A CA  
1404 C  C   . SER A 172 ? 0.1849 0.1944 0.1084 -0.0149 0.0283  0.0114  173 SER A C   
1405 O  O   . SER A 172 ? 0.2059 0.2652 0.1113 0.0160  0.0369  0.0321  173 SER A O   
1406 C  CB  . SER A 172 ? 0.2321 0.1923 0.1495 -0.0362 0.0527  0.0274  173 SER A CB  
1407 O  OG  . SER A 172 ? 0.2605 0.2216 0.2407 -0.0318 0.0523  0.0811  173 SER A OG  
1408 N  N   . ALA A 173 ? 0.1700 0.2052 0.1573 0.0197  0.0222  0.0326  174 ALA A N   
1409 C  CA  . ALA A 173 ? 0.1987 0.2328 0.1174 0.0506  0.0155  0.0000  174 ALA A CA  
1410 C  C   . ALA A 173 ? 0.1829 0.2439 0.0996 0.0309  0.0292  0.0097  174 ALA A C   
1411 O  O   . ALA A 173 ? 0.2037 0.2234 0.0905 0.0185  0.0038  0.0261  174 ALA A O   
1412 C  CB  . ALA A 173 ? 0.2320 0.2658 0.1349 0.0088  0.0471  -0.0160 174 ALA A CB  
1413 N  N   . ASP A 174 ? 0.2397 0.2891 0.1181 0.0637  0.0245  0.0436  175 ASP A N   
1414 C  CA  . ASP A 174 ? 0.1839 0.2665 0.1782 0.0306  0.0290  0.0574  175 ASP A CA  
1415 C  C   . ASP A 174 ? 0.1908 0.2303 0.1421 0.0151  -0.0070 0.0192  175 ASP A C   
1416 O  O   . ASP A 174 ? 0.2127 0.2749 0.1309 0.0182  0.0238  -0.0115 175 ASP A O   
1417 C  CB  . ASP A 174 ? 0.2529 0.3517 0.1567 0.0035  -0.0425 0.0516  175 ASP A CB  
1418 C  CG  . ASP A 174 ? 0.3639 0.3873 0.3037 -0.0178 -0.0600 0.1195  175 ASP A CG  
1419 O  OD1 . ASP A 174 ? 0.5732 0.6560 0.3890 -0.0637 0.0650  -0.1306 175 ASP A OD1 
1420 O  OD2 . ASP A 174 ? 0.6958 0.9502 0.3736 0.3391  0.0015  0.0553  175 ASP A OD2 
1421 N  N   . PHE A 175 ? 0.1980 0.2088 0.1052 -0.0048 0.0110  0.0268  176 PHE A N   
1422 C  CA  . PHE A 175 ? 0.1723 0.1718 0.1158 0.0043  -0.0178 0.0065  176 PHE A CA  
1423 C  C   . PHE A 175 ? 0.1813 0.1530 0.1261 0.0200  -0.0153 -0.0068 176 PHE A C   
1424 O  O   . PHE A 175 ? 0.1804 0.1965 0.1335 0.0229  -0.0128 -0.0071 176 PHE A O   
1425 C  CB  . PHE A 175 ? 0.1663 0.1711 0.1098 0.0171  -0.0022 0.0208  176 PHE A CB  
1426 C  CG  . PHE A 175 ? 0.1696 0.1646 0.1311 0.0211  0.0119  -0.0026 176 PHE A CG  
1427 C  CD1 . PHE A 175 ? 0.1980 0.1850 0.1492 0.0010  0.0313  -0.0104 176 PHE A CD1 
1428 C  CD2 . PHE A 175 ? 0.1890 0.1677 0.1262 0.0223  0.0013  0.0249  176 PHE A CD2 
1429 C  CE1 . PHE A 175 ? 0.1905 0.1874 0.1332 -0.0100 0.0145  0.0195  176 PHE A CE1 
1430 C  CE2 . PHE A 175 ? 0.1613 0.1861 0.1675 -0.0020 -0.0171 0.0026  176 PHE A CE2 
1431 C  CZ  . PHE A 175 ? 0.1624 0.1854 0.1238 0.0095  -0.0141 0.0013  176 PHE A CZ  
1432 N  N   . THR A 176 ? 0.1696 0.1930 0.1571 0.0287  -0.0113 0.0032  177 THR A N   
1433 C  CA  . THR A 176 ? 0.1678 0.1854 0.1327 0.0150  0.0204  0.0373  177 THR A CA  
1434 C  C   . THR A 176 ? 0.1831 0.1374 0.1038 0.0117  -0.0166 0.0386  177 THR A C   
1435 O  O   . THR A 176 ? 0.2242 0.1527 0.1453 0.0066  -0.0304 0.0220  177 THR A O   
1436 C  CB  . THR A 176 ? 0.1885 0.1741 0.1632 -0.0094 -0.0359 0.0376  177 THR A CB  
1437 O  OG1 . THR A 176 ? 0.2481 0.2461 0.1416 0.0178  -0.0179 0.0384  177 THR A OG1 
1438 C  CG2 . THR A 176 ? 0.2168 0.2095 0.3165 -0.0319 -0.0555 0.0908  177 THR A CG2 
1439 N  N   . ASN A 177 ? 0.1670 0.1711 0.1172 -0.0036 -0.0063 0.0113  178 ASN A N   
1440 C  CA  . ASN A 177 ? 0.1678 0.1756 0.1881 -0.0234 -0.0294 0.0356  178 ASN A CA  
1441 C  C   . ASN A 177 ? 0.1754 0.1544 0.1559 -0.0217 -0.0161 0.0137  178 ASN A C   
1442 O  O   . ASN A 177 ? 0.2039 0.2026 0.2523 -0.0536 -0.0591 0.0871  178 ASN A O   
1443 C  CB  . ASN A 177 ? 0.1843 0.1944 0.2087 -0.0062 -0.0531 0.0745  178 ASN A CB  
1444 C  CG  . ASN A 177 ? 0.2215 0.1993 0.1932 -0.0034 -0.0451 0.0383  178 ASN A CG  
1445 O  OD1 . ASN A 177 ? 0.2055 0.2199 0.3198 -0.0131 -0.0178 0.0156  178 ASN A OD1 
1446 N  ND2 . ASN A 177 ? 0.2132 0.2041 0.1929 -0.0198 -0.0392 0.0392  178 ASN A ND2 
1447 N  N   . PHE A 178 ? 0.1793 0.1513 0.1141 0.0062  -0.0108 0.0171  179 PHE A N   
1448 C  CA  . PHE A 178 ? 0.1840 0.1588 0.1205 -0.0114 -0.0025 0.0193  179 PHE A CA  
1449 C  C   . PHE A 178 ? 0.1628 0.1342 0.1330 -0.0063 0.0064  0.0167  179 PHE A C   
1450 O  O   . PHE A 178 ? 0.2307 0.1641 0.1300 -0.0189 -0.0186 0.0133  179 PHE A O   
1451 C  CB  . PHE A 178 ? 0.1650 0.1828 0.1259 0.0147  0.0044  0.0480  179 PHE A CB  
1452 C  CG  . PHE A 178 ? 0.1814 0.1487 0.1224 0.0059  -0.0046 0.0263  179 PHE A CG  
1453 C  CD1 . PHE A 178 ? 0.1889 0.1693 0.1432 0.0020  0.0222  0.0216  179 PHE A CD1 
1454 C  CD2 . PHE A 178 ? 0.1395 0.1659 0.1268 0.0100  -0.0258 0.0261  179 PHE A CD2 
1455 C  CE1 . PHE A 178 ? 0.1965 0.1628 0.1295 0.0000  0.0200  0.0187  179 PHE A CE1 
1456 C  CE2 . PHE A 178 ? 0.1406 0.1543 0.1549 0.0109  0.0096  0.0201  179 PHE A CE2 
1457 C  CZ  . PHE A 178 ? 0.1539 0.1632 0.1328 0.0001  0.0015  0.0146  179 PHE A CZ  
1458 N  N   . ASP A 179 ? 0.1356 0.1675 0.1313 0.0015  0.0010  0.0185  180 ASP A N   
1459 C  CA  . ASP A 179 ? 0.1472 0.1721 0.1415 0.0114  -0.0039 -0.0013 180 ASP A CA  
1460 C  C   . ASP A 179 ? 0.1775 0.1618 0.1274 -0.0077 0.0210  0.0121  180 ASP A C   
1461 O  O   . ASP A 179 ? 0.1872 0.1561 0.1363 -0.0041 0.0100  0.0004  180 ASP A O   
1462 C  CB  . ASP A 179 ? 0.1579 0.2190 0.1370 -0.0094 -0.0003 -0.0019 180 ASP A CB  
1463 C  CG  . ASP A 179 ? 0.1657 0.2027 0.1580 0.0200  0.0117  0.0179  180 ASP A CG  
1464 O  OD1 . ASP A 179 ? 0.1968 0.1817 0.1612 0.0505  0.0156  0.0096  180 ASP A OD1 
1465 O  OD2 . ASP A 179 ? 0.1642 0.3717 0.2935 0.0184  0.0330  -0.0172 180 ASP A OD2 
1466 N  N   . PRO A 180 ? 0.1508 0.1543 0.1645 0.0185  0.0006  0.0151  181 PRO A N   
1467 C  CA  . PRO A 180 ? 0.1304 0.1761 0.1492 -0.0093 -0.0086 0.0204  181 PRO A CA  
1468 C  C   . PRO A 180 ? 0.1582 0.1516 0.1384 -0.0069 -0.0067 0.0144  181 PRO A C   
1469 O  O   . PRO A 180 ? 0.1711 0.1840 0.1365 0.0295  -0.0141 0.0179  181 PRO A O   
1470 C  CB  . PRO A 180 ? 0.1650 0.1576 0.2102 -0.0076 -0.0156 0.0111  181 PRO A CB  
1471 C  CG  . PRO A 180 ? 0.1849 0.1808 0.1234 0.0129  -0.0083 0.0088  181 PRO A CG  
1472 C  CD  . PRO A 180 ? 0.1811 0.1569 0.1287 -0.0026 -0.0085 0.0064  181 PRO A CD  
1473 N  N   . ARG A 181 ? 0.1530 0.1546 0.1163 0.0072  0.0179  -0.0117 182 ARG A N   
1474 C  CA  . ARG A 181 ? 0.1639 0.1603 0.1298 0.0237  0.0237  0.0174  182 ARG A CA  
1475 C  C   . ARG A 181 ? 0.1746 0.1642 0.1307 0.0389  -0.0008 0.0242  182 ARG A C   
1476 O  O   . ARG A 181 ? 0.1779 0.1887 0.1582 0.0131  -0.0076 0.0115  182 ARG A O   
1477 C  CB  . ARG A 181 ? 0.1720 0.1566 0.1678 0.0295  0.0071  -0.0228 182 ARG A CB  
1478 C  CG  . ARG A 181 ? 0.2285 0.1471 0.1782 0.0339  0.0326  -0.0040 182 ARG A CG  
1479 C  CD  . ARG A 181 ? 0.2285 0.1998 0.2082 0.0511  0.0370  0.0008  182 ARG A CD  
1480 N  NE  . ARG A 181 ? 0.1646 0.1984 0.2141 0.0254  0.0309  0.0429  182 ARG A NE  
1481 C  CZ  . ARG A 181 ? 0.1483 0.2138 0.2345 0.0075  0.0434  0.0274  182 ARG A CZ  
1482 N  NH1 . ARG A 181 ? 0.1858 0.2701 0.3237 0.0315  0.0978  0.0258  182 ARG A NH1 
1483 N  NH2 . ARG A 181 ? 0.1975 0.2764 0.2626 0.0620  0.0000  0.0621  182 ARG A NH2 
1484 N  N   . GLY A 182 ? 0.1768 0.1747 0.1506 0.0175  -0.0122 -0.0097 183 GLY A N   
1485 C  CA  . GLY A 182 ? 0.1935 0.1465 0.1779 0.0411  -0.0070 -0.0013 183 GLY A CA  
1486 C  C   . GLY A 182 ? 0.1693 0.1660 0.1695 0.0145  -0.0058 0.0103  183 GLY A C   
1487 O  O   . GLY A 182 ? 0.2407 0.1649 0.1601 0.0229  -0.0139 0.0106  183 GLY A O   
1488 N  N   . LEU A 183 ? 0.1590 0.1724 0.1298 0.0139  -0.0130 0.0135  184 LEU A N   
1489 C  CA  . LEU A 183 ? 0.1606 0.1838 0.1277 0.0192  -0.0083 0.0197  184 LEU A CA  
1490 C  C   . LEU A 183 ? 0.1729 0.1652 0.1198 0.0266  0.0160  -0.0070 184 LEU A C   
1491 O  O   . LEU A 183 ? 0.1928 0.1980 0.1338 0.0336  0.0025  0.0305  184 LEU A O   
1492 C  CB  . LEU A 183 ? 0.1847 0.1743 0.1043 0.0226  -0.0057 0.0124  184 LEU A CB  
1493 C  CG  . LEU A 183 ? 0.1828 0.2140 0.1003 0.0423  0.0110  0.0038  184 LEU A CG  
1494 C  CD1 . LEU A 183 ? 0.1881 0.2398 0.1456 0.0223  -0.0031 0.0402  184 LEU A CD1 
1495 C  CD2 . LEU A 183 ? 0.2861 0.2234 0.1292 0.0612  0.0506  -0.0111 184 LEU A CD2 
1496 N  N   . LEU A 184 ? 0.1597 0.1659 0.1030 0.0190  0.0140  0.0065  185 LEU A N   
1497 C  CA  . LEU A 184 ? 0.1700 0.1667 0.1030 -0.0097 0.0288  0.0055  185 LEU A CA  
1498 C  C   . LEU A 184 ? 0.1944 0.1764 0.1176 -0.0275 -0.0195 0.0295  185 LEU A C   
1499 O  O   . LEU A 184 ? 0.2834 0.2294 0.1847 -0.0722 -0.1008 0.0639  185 LEU A O   
1500 C  CB  . LEU A 184 ? 0.1714 0.1761 0.1375 -0.0113 0.0084  -0.0257 185 LEU A CB  
1501 C  CG  . LEU A 184 ? 0.1351 0.2039 0.2357 -0.0149 0.0452  -0.0162 185 LEU A CG  
1502 C  CD1 . LEU A 184 ? 0.1522 0.1840 0.2570 -0.0089 0.0262  -0.0237 185 LEU A CD1 
1503 C  CD2 . LEU A 184 ? 0.1605 0.1937 0.2540 0.0390  -0.0317 0.0082  185 LEU A CD2 
1504 N  N   . PRO A 185 ? 0.1434 0.1763 0.1260 0.0131  -0.0013 0.0238  186 PRO A N   
1505 C  CA  . PRO A 185 ? 0.1429 0.1659 0.1641 0.0012  -0.0047 0.0262  186 PRO A CA  
1506 C  C   . PRO A 185 ? 0.1477 0.1456 0.1372 -0.0071 -0.0040 0.0114  186 PRO A C   
1507 O  O   . PRO A 185 ? 0.1192 0.1496 0.2389 0.0000  0.0093  0.0162  186 PRO A O   
1508 C  CB  . PRO A 185 ? 0.1388 0.1889 0.1670 0.0126  -0.0004 0.0377  186 PRO A CB  
1509 C  CG  . PRO A 185 ? 0.1463 0.1969 0.0960 0.0097  0.0076  0.0113  186 PRO A CG  
1510 C  CD  . PRO A 185 ? 0.1536 0.1930 0.0732 0.0229  -0.0017 -0.0076 186 PRO A CD  
1511 N  N   . GLU A 186 ? 0.1557 0.2130 0.1948 -0.0222 0.0159  0.0453  187 GLU A N   
1512 C  CA  . GLU A 186 ? 0.1389 0.2008 0.2411 -0.0146 -0.0021 0.0057  187 GLU A CA  
1513 C  C   . GLU A 186 ? 0.1309 0.1815 0.1914 -0.0063 0.0033  0.0399  187 GLU A C   
1514 O  O   . GLU A 186 ? 0.1345 0.2273 0.2626 0.0209  -0.0099 0.0001  187 GLU A O   
1515 C  CB  . GLU A 186 ? 0.2094 0.2554 0.2237 -0.0616 -0.0351 0.0774  187 GLU A CB  
1516 C  CG  . GLU A 186 ? 0.2528 0.2670 0.3301 -0.0796 -0.0606 0.0381  187 GLU A CG  
1517 C  CD  . GLU A 186 ? 0.2326 0.2350 0.3013 -0.0256 -0.0254 0.0474  187 GLU A CD  
1518 O  OE1 . GLU A 186 ? 0.2609 0.2981 0.3310 -0.0641 -0.0232 0.1172  187 GLU A OE1 
1519 O  OE2 . GLU A 186 ? 0.3236 0.2536 0.4270 -0.0666 -0.1102 0.0299  187 GLU A OE2 
1520 N  N   . SER A 187 ? 0.1316 0.2159 0.1839 0.0073  -0.0044 0.0103  188 SER A N   
1521 C  CA  . SER A 187 ? 0.1374 0.1897 0.1915 0.0006  0.0115  0.0103  188 SER A CA  
1522 C  C   . SER A 187 ? 0.1380 0.1983 0.1912 -0.0100 0.0163  -0.0109 188 SER A C   
1523 O  O   . SER A 187 ? 0.1370 0.2533 0.1969 0.0026  0.0300  0.0002  188 SER A O   
1524 C  CB  . SER A 187 ? 0.1912 0.2404 0.1641 0.0166  0.0409  0.0225  188 SER A CB  
1525 O  OG  . SER A 187 ? 0.1863 0.2494 0.1858 -0.0297 0.0193  0.0190  188 SER A OG  
1526 N  N   . LEU A 188 ? 0.1418 0.2069 0.1876 -0.0100 0.0102  -0.0168 189 LEU A N   
1527 C  CA  . LEU A 188 ? 0.1459 0.1998 0.1747 -0.0150 -0.0023 -0.0273 189 LEU A CA  
1528 C  C   . LEU A 188 ? 0.1483 0.1929 0.1452 -0.0008 0.0309  -0.0110 189 LEU A C   
1529 O  O   . LEU A 188 ? 0.1797 0.2253 0.1594 -0.0248 0.0059  -0.0288 189 LEU A O   
1530 C  CB  . LEU A 188 ? 0.1608 0.2188 0.1845 -0.0050 0.0052  0.0004  189 LEU A CB  
1531 C  CG  . LEU A 188 ? 0.1456 0.2151 0.2073 -0.0225 0.0314  0.0383  189 LEU A CG  
1532 C  CD1 . LEU A 188 ? 0.1717 0.2155 0.3365 0.0017  0.0129  0.0082  189 LEU A CD1 
1533 C  CD2 . LEU A 188 ? 0.1771 0.3413 0.1936 -0.0214 0.0407  0.0469  189 LEU A CD2 
1534 N  N   . ASP A 189 ? 0.1628 0.2449 0.1923 0.0240  0.0352  0.0125  190 ASP A N   
1535 C  CA  . ASP A 189 ? 0.1210 0.2407 0.1980 0.0031  0.0414  0.0011  190 ASP A CA  
1536 C  C   . ASP A 189 ? 0.1285 0.2117 0.1802 -0.0321 0.0386  -0.0230 190 ASP A C   
1537 O  O   . ASP A 189 ? 0.1321 0.2145 0.1470 0.0055  0.0238  -0.0070 190 ASP A O   
1538 C  CB  . ASP A 189 ? 0.1964 0.2764 0.1492 -0.0541 0.0400  0.0326  190 ASP A CB  
1539 C  CG  . ASP A 189 ? 0.1948 0.3703 0.2611 -0.0464 0.0480  0.0348  190 ASP A CG  
1540 O  OD1 . ASP A 189 ? 0.2370 0.4960 0.3082 -0.0446 0.1093  -0.0566 190 ASP A OD1 
1541 O  OD2 . ASP A 189 ? 0.3007 0.4396 0.2773 -0.1368 0.0310  0.0873  190 ASP A OD2 
1542 N  N   . TYR A 190 ? 0.1383 0.2104 0.1452 -0.0107 0.0304  0.0134  191 TYR A N   
1543 C  CA  . TYR A 190 ? 0.1361 0.2145 0.1237 -0.0207 0.0326  0.0178  191 TYR A CA  
1544 C  C   . TYR A 190 ? 0.1621 0.1885 0.0910 -0.0060 0.0337  0.0086  191 TYR A C   
1545 O  O   . TYR A 190 ? 0.1641 0.2204 0.0894 0.0000  0.0300  0.0016  191 TYR A O   
1546 C  CB  . TYR A 190 ? 0.1693 0.1979 0.0761 -0.0005 0.0206  -0.0018 191 TYR A CB  
1547 C  CG  . TYR A 190 ? 0.1656 0.1692 0.1190 -0.0154 0.0097  0.0012  191 TYR A CG  
1548 C  CD1 . TYR A 190 ? 0.2030 0.1900 0.0974 -0.0343 0.0087  -0.0074 191 TYR A CD1 
1549 C  CD2 . TYR A 190 ? 0.1669 0.2289 0.1077 0.0027  0.0320  0.0118  191 TYR A CD2 
1550 C  CE1 . TYR A 190 ? 0.1940 0.2036 0.1098 0.0002  0.0042  -0.0004 191 TYR A CE1 
1551 C  CE2 . TYR A 190 ? 0.1969 0.2235 0.1336 -0.0122 0.0145  -0.0103 191 TYR A CE2 
1552 C  CZ  . TYR A 190 ? 0.2213 0.2425 0.1120 0.0168  0.0065  -0.0270 191 TYR A CZ  
1553 O  OH  . TYR A 190 ? 0.2320 0.2120 0.1556 0.0091  0.0251  -0.0200 191 TYR A OH  
1554 N  N   . TRP A 191 ? 0.1458 0.1716 0.1538 -0.0146 0.0038  -0.0008 192 TRP A N   
1555 C  CA  . TRP A 191 ? 0.1458 0.1627 0.1122 0.0093  0.0033  0.0166  192 TRP A CA  
1556 C  C   . TRP A 191 ? 0.1461 0.1808 0.0770 -0.0034 0.0220  0.0100  192 TRP A C   
1557 O  O   . TRP A 191 ? 0.1688 0.1905 0.0741 -0.0211 0.0231  0.0087  192 TRP A O   
1558 C  CB  . TRP A 191 ? 0.1502 0.1781 0.1349 0.0099  0.0417  0.0262  192 TRP A CB  
1559 C  CG  . TRP A 191 ? 0.1474 0.1593 0.1412 0.0232  0.0317  0.0281  192 TRP A CG  
1560 C  CD1 . TRP A 191 ? 0.1741 0.1688 0.1544 -0.0022 0.0443  0.0352  192 TRP A CD1 
1561 C  CD2 . TRP A 191 ? 0.1377 0.1500 0.1632 0.0175  0.0317  0.0161  192 TRP A CD2 
1562 N  NE1 . TRP A 191 ? 0.1960 0.1626 0.1720 0.0178  0.0434  -0.0012 192 TRP A NE1 
1563 C  CE2 . TRP A 191 ? 0.1500 0.1494 0.1698 0.0361  0.0467  0.0102  192 TRP A CE2 
1564 C  CE3 . TRP A 191 ? 0.1306 0.2124 0.1584 -0.0043 0.0174  -0.0120 192 TRP A CE3 
1565 C  CZ2 . TRP A 191 ? 0.1575 0.1746 0.1886 0.0230  -0.0025 -0.0049 192 TRP A CZ2 
1566 C  CZ3 . TRP A 191 ? 0.1714 0.2133 0.1955 0.0089  0.0105  0.0077  192 TRP A CZ3 
1567 C  CH2 . TRP A 191 ? 0.1438 0.2154 0.1883 0.0188  -0.0103 0.0396  192 TRP A CH2 
1568 N  N   . THR A 192 ? 0.1391 0.1736 0.0983 0.0002  0.0018  0.0131  193 THR A N   
1569 C  CA  . THR A 192 ? 0.1338 0.1817 0.1207 -0.0092 0.0097  0.0098  193 THR A CA  
1570 C  C   . THR A 192 ? 0.1351 0.1850 0.0671 0.0008  0.0324  -0.0039 193 THR A C   
1571 O  O   . THR A 192 ? 0.1668 0.2083 0.0723 0.0092  0.0131  0.0044  193 THR A O   
1572 C  CB  . THR A 192 ? 0.1480 0.1822 0.0870 0.0058  0.0226  0.0008  193 THR A CB  
1573 O  OG1 . THR A 192 ? 0.1615 0.1889 0.1439 -0.0096 0.0160  -0.0032 193 THR A OG1 
1574 C  CG2 . THR A 192 ? 0.1796 0.2036 0.0792 0.0379  0.0201  0.0062  193 THR A CG2 
1575 N  N   . TYR A 193 ? 0.1293 0.1815 0.1081 -0.0073 0.0166  -0.0086 194 TYR A N   
1576 C  CA  . TYR A 193 ? 0.1323 0.1738 0.1050 0.0067  0.0166  -0.0102 194 TYR A CA  
1577 C  C   . TYR A 193 ? 0.1309 0.1790 0.0910 0.0058  0.0105  -0.0129 194 TYR A C   
1578 O  O   . TYR A 193 ? 0.1624 0.1635 0.0926 0.0064  -0.0020 0.0034  194 TYR A O   
1579 C  CB  . TYR A 193 ? 0.1707 0.1825 0.0915 0.0321  0.0106  -0.0159 194 TYR A CB  
1580 C  CG  . TYR A 193 ? 0.1575 0.1933 0.0794 0.0088  0.0085  0.0072  194 TYR A CG  
1581 C  CD1 . TYR A 193 ? 0.1659 0.1514 0.0901 0.0255  0.0089  0.0040  194 TYR A CD1 
1582 C  CD2 . TYR A 193 ? 0.1577 0.1772 0.1081 0.0051  0.0037  -0.0108 194 TYR A CD2 
1583 C  CE1 . TYR A 193 ? 0.1437 0.1644 0.0879 0.0052  0.0054  0.0029  194 TYR A CE1 
1584 C  CE2 . TYR A 193 ? 0.1678 0.1764 0.0937 0.0207  -0.0093 -0.0152 194 TYR A CE2 
1585 C  CZ  . TYR A 193 ? 0.1348 0.1356 0.0860 0.0171  0.0082  -0.0069 194 TYR A CZ  
1586 O  OH  . TYR A 193 ? 0.1377 0.1571 0.0925 0.0006  0.0122  0.0008  194 TYR A OH  
1587 N  N   . PRO A 194 ? 0.1321 0.1905 0.0725 0.0000  0.0131  -0.0078 195 PRO A N   
1588 C  CA  . PRO A 194 ? 0.1507 0.1650 0.0958 -0.0118 0.0023  -0.0223 195 PRO A CA  
1589 C  C   . PRO A 194 ? 0.1460 0.1646 0.1197 -0.0011 -0.0044 -0.0066 195 PRO A C   
1590 O  O   . PRO A 194 ? 0.1586 0.1822 0.1034 0.0075  0.0034  0.0029  195 PRO A O   
1591 C  CB  . PRO A 194 ? 0.1979 0.2055 0.1039 -0.0057 -0.0013 -0.0500 195 PRO A CB  
1592 C  CG  . PRO A 194 ? 0.2077 0.2782 0.0980 -0.0505 0.0261  -0.0133 195 PRO A CG  
1593 C  CD  . PRO A 194 ? 0.1883 0.2662 0.0664 -0.0276 0.0100  -0.0211 195 PRO A CD  
1594 N  N   . GLY A 195 ? 0.1181 0.1725 0.1032 -0.0068 0.0009  -0.0223 196 GLY A N   
1595 C  CA  . GLY A 195 ? 0.1506 0.1472 0.1161 0.0086  0.0158  0.0049  196 GLY A CA  
1596 C  C   . GLY A 195 ? 0.1421 0.1416 0.1152 -0.0047 0.0042  0.0033  196 GLY A C   
1597 O  O   . GLY A 195 ? 0.1342 0.1499 0.1108 -0.0039 0.0074  -0.0144 196 GLY A O   
1598 N  N   . SER A 196 ? 0.1192 0.1515 0.1151 -0.0052 -0.0009 -0.0070 197 SER A N   
1599 C  CA  . SER A 196 ? 0.1142 0.1707 0.1192 -0.0042 0.0075  -0.0147 197 SER A CA  
1600 C  C   . SER A 196 ? 0.1172 0.1393 0.1194 0.0027  0.0145  -0.0183 197 SER A C   
1601 O  O   . SER A 196 ? 0.1216 0.1309 0.1095 -0.0113 -0.0037 -0.0051 197 SER A O   
1602 C  CB  . SER A 196 ? 0.1229 0.1639 0.1127 0.0097  0.0032  -0.0100 197 SER A CB  
1603 O  OG  . SER A 196 ? 0.1221 0.1656 0.1349 0.0085  0.0051  -0.0081 197 SER A OG  
1604 N  N   . LEU A 197 ? 0.1312 0.1423 0.0982 0.0063  0.0087  -0.0126 198 LEU A N   
1605 C  CA  . LEU A 197 ? 0.1225 0.1480 0.0892 0.0103  0.0080  -0.0155 198 LEU A CA  
1606 C  C   . LEU A 197 ? 0.1047 0.1391 0.1168 -0.0041 0.0257  -0.0008 198 LEU A C   
1607 O  O   . LEU A 197 ? 0.1150 0.1675 0.1251 -0.0038 0.0111  -0.0027 198 LEU A O   
1608 C  CB  . LEU A 197 ? 0.1559 0.1467 0.1294 0.0006  0.0311  0.0027  198 LEU A CB  
1609 C  CG  . LEU A 197 ? 0.1514 0.1442 0.1089 -0.0179 0.0074  -0.0084 198 LEU A CG  
1610 C  CD1 . LEU A 197 ? 0.1669 0.1987 0.1491 -0.0308 0.0148  0.0219  198 LEU A CD1 
1611 C  CD2 . LEU A 197 ? 0.1389 0.1532 0.1488 -0.0020 0.0064  0.0030  198 LEU A CD2 
1612 N  N   . THR A 198 ? 0.1286 0.1287 0.1197 -0.0016 0.0047  -0.0132 199 THR A N   
1613 C  CA  . THR A 198 ? 0.1372 0.1133 0.1250 -0.0059 0.0196  -0.0057 199 THR A CA  
1614 C  C   . THR A 198 ? 0.1217 0.1540 0.1183 -0.0091 -0.0050 -0.0071 199 THR A C   
1615 O  O   . THR A 198 ? 0.1381 0.1592 0.1488 -0.0077 0.0088  -0.0212 199 THR A O   
1616 C  CB  . THR A 198 ? 0.1323 0.1271 0.0916 -0.0006 -0.0013 -0.0073 199 THR A CB  
1617 O  OG1 . THR A 198 ? 0.1199 0.1373 0.1102 0.0005  -0.0040 0.0000  199 THR A OG1 
1618 C  CG2 . THR A 198 ? 0.1364 0.1655 0.0980 0.0064  0.0114  -0.0021 199 THR A CG2 
1619 N  N   . THR A 199 ? 0.1302 0.1645 0.1266 -0.0084 0.0178  -0.0149 200 THR A N   
1620 C  CA  . THR A 199 ? 0.1537 0.1928 0.1080 -0.0266 0.0379  -0.0383 200 THR A CA  
1621 C  C   . THR A 199 ? 0.1271 0.1760 0.1419 -0.0076 0.0146  -0.0196 200 THR A C   
1622 O  O   . THR A 199 ? 0.1516 0.1663 0.1223 -0.0168 0.0241  -0.0102 200 THR A O   
1623 C  CB  . THR A 199 ? 0.1677 0.1815 0.1149 0.0000  0.0343  -0.0164 200 THR A CB  
1624 O  OG1 . THR A 199 ? 0.2076 0.2048 0.1463 -0.0111 -0.0002 0.0083  200 THR A OG1 
1625 C  CG2 . THR A 199 ? 0.1741 0.1802 0.1777 -0.0099 -0.0144 -0.0193 200 THR A CG2 
1626 N  N   . PRO A 200 ? 0.1323 0.1868 0.1451 -0.0117 0.0132  -0.0165 201 PRO A N   
1627 C  CA  . PRO A 200 ? 0.1238 0.1761 0.1754 -0.0134 0.0304  0.0061  201 PRO A CA  
1628 C  C   . PRO A 200 ? 0.1140 0.1782 0.1692 -0.0274 0.0175  0.0038  201 PRO A C   
1629 O  O   . PRO A 200 ? 0.1373 0.2132 0.1518 -0.0168 0.0084  0.0021  201 PRO A O   
1630 C  CB  . PRO A 200 ? 0.1125 0.2105 0.1925 -0.0027 0.0361  0.0089  201 PRO A CB  
1631 C  CG  . PRO A 200 ? 0.1158 0.2117 0.2163 0.0057  0.0200  -0.0165 201 PRO A CG  
1632 C  CD  . PRO A 200 ? 0.1235 0.1887 0.1893 -0.0004 0.0396  -0.0114 201 PRO A CD  
1633 N  N   . PRO A 201 ? 0.1384 0.1925 0.1386 -0.0173 0.0170  0.0053  202 PRO A N   
1634 C  CA  . PRO A 201 ? 0.1331 0.1675 0.1414 -0.0299 0.0212  0.0122  202 PRO A CA  
1635 C  C   . PRO A 201 ? 0.1309 0.1779 0.1447 0.0057  0.0165  0.0149  202 PRO A C   
1636 O  O   . PRO A 201 ? 0.1309 0.1840 0.1695 -0.0018 0.0099  -0.0055 202 PRO A O   
1637 C  CB  . PRO A 201 ? 0.1644 0.1660 0.1835 -0.0082 0.0135  0.0155  202 PRO A CB  
1638 C  CG  . PRO A 201 ? 0.1745 0.1876 0.2234 -0.0031 -0.0086 -0.0124 202 PRO A CG  
1639 C  CD  . PRO A 201 ? 0.1908 0.1736 0.1615 0.0049  0.0118  0.0026  202 PRO A CD  
1640 N  N   . LEU A 202 ? 0.1321 0.1732 0.1417 -0.0086 0.0245  0.0153  203 LEU A N   
1641 C  CA  . LEU A 202 ? 0.1186 0.1717 0.1210 0.0155  0.0231  -0.0049 203 LEU A CA  
1642 C  C   . LEU A 202 ? 0.1098 0.1366 0.1342 -0.0215 0.0130  -0.0060 203 LEU A C   
1643 O  O   . LEU A 202 ? 0.1336 0.1829 0.1381 -0.0111 -0.0073 -0.0005 203 LEU A O   
1644 C  CB  . LEU A 202 ? 0.1197 0.1731 0.1401 0.0178  -0.0026 -0.0226 203 LEU A CB  
1645 C  CG  . LEU A 202 ? 0.1113 0.1756 0.1410 0.0036  0.0111  -0.0244 203 LEU A CG  
1646 C  CD1 . LEU A 202 ? 0.1138 0.2109 0.1734 0.0022  -0.0048 -0.0211 203 LEU A CD1 
1647 C  CD2 . LEU A 202 ? 0.1327 0.1761 0.1474 -0.0158 0.0071  -0.0077 203 LEU A CD2 
1648 N  N   . ASN A 203 ? 0.1206 0.1518 0.1778 -0.0100 -0.0025 -0.0140 204 ASN A N   
1649 C  CA  . ASN A 203 ? 0.1468 0.1558 0.1473 -0.0106 0.0186  -0.0184 204 ASN A CA  
1650 C  C   . ASN A 203 ? 0.1351 0.1657 0.1108 -0.0102 -0.0060 -0.0020 204 ASN A C   
1651 O  O   . ASN A 203 ? 0.1220 0.1564 0.1412 -0.0083 -0.0095 -0.0184 204 ASN A O   
1652 C  CB  . ASN A 203 ? 0.1685 0.1610 0.2213 0.0060  0.0440  0.0145  204 ASN A CB  
1653 C  CG  . ASN A 203 ? 0.1933 0.1549 0.2400 -0.0155 0.0521  -0.0078 204 ASN A CG  
1654 O  OD1 . ASN A 203 ? 0.2008 0.2099 0.2748 -0.0163 0.0802  0.0167  204 ASN A OD1 
1655 N  ND2 . ASN A 203 ? 0.2309 0.1818 0.2447 0.0119  0.0493  0.0348  204 ASN A ND2 
1656 N  N   . GLU A 204 ? 0.1540 0.1555 0.1338 -0.0035 -0.0109 -0.0321 205 GLU A N   
1657 C  CA  . GLU A 204 ? 0.1540 0.1831 0.1083 0.0105  -0.0082 -0.0286 205 GLU A CA  
1658 C  C   . GLU A 204 ? 0.1717 0.1802 0.1079 0.0136  -0.0142 -0.0310 205 GLU A C   
1659 O  O   . GLU A 204 ? 0.2007 0.2433 0.1351 0.0517  -0.0407 -0.0661 205 GLU A O   
1660 C  CB  . GLU A 204 ? 0.1438 0.1673 0.1666 -0.0001 -0.0480 -0.0228 205 GLU A CB  
1661 C  CG  . GLU A 204 ? 0.1527 0.1736 0.1681 0.0033  -0.0267 -0.0080 205 GLU A CG  
1662 C  CD  . GLU A 204 ? 0.1579 0.2012 0.1339 0.0005  -0.0124 -0.0290 205 GLU A CD  
1663 O  OE1 . GLU A 204 ? 0.1706 0.2476 0.2145 -0.0011 -0.0419 -0.0776 205 GLU A OE1 
1664 O  OE2 . GLU A 204 ? 0.1493 0.2161 0.1330 0.0074  -0.0061 -0.0085 205 GLU A OE2 
1665 N  N   . CYS A 205 ? 0.1409 0.1262 0.1192 0.0076  -0.0113 -0.0151 206 CYS A N   
1666 C  CA  . CYS A 205 ? 0.1412 0.1469 0.0966 0.0146  -0.0012 -0.0143 206 CYS A CA  
1667 C  C   . CYS A 205 ? 0.1490 0.1398 0.1144 0.0139  0.0078  -0.0137 206 CYS A C   
1668 O  O   . CYS A 205 ? 0.1527 0.1397 0.1516 -0.0065 -0.0181 0.0020  206 CYS A O   
1669 C  CB  . CYS A 205 ? 0.1735 0.2005 0.0897 0.0018  -0.0055 -0.0057 206 CYS A CB  
1670 S  SG  . CYS A 205 ? 0.1795 0.1655 0.1252 0.0054  -0.0077 -0.0110 206 CYS A SG  
1671 N  N   . VAL A 206 ? 0.1472 0.1495 0.0961 -0.0145 -0.0012 -0.0129 207 VAL A N   
1672 C  CA  . VAL A 206 ? 0.1222 0.1451 0.1162 0.0000  -0.0031 -0.0115 207 VAL A CA  
1673 C  C   . VAL A 206 ? 0.1379 0.1280 0.1198 0.0111  -0.0046 -0.0035 207 VAL A C   
1674 O  O   . VAL A 206 ? 0.1623 0.1691 0.1269 0.0104  -0.0201 -0.0063 207 VAL A O   
1675 C  CB  . VAL A 206 ? 0.1360 0.1409 0.0948 -0.0126 0.0198  -0.0027 207 VAL A CB  
1676 C  CG1 . VAL A 206 ? 0.1407 0.1482 0.1039 -0.0154 0.0065  -0.0153 207 VAL A CG1 
1677 C  CG2 . VAL A 206 ? 0.1495 0.1516 0.1084 0.0000  0.0153  0.0192  207 VAL A CG2 
1678 N  N   . THR A 207 ? 0.1268 0.1232 0.1183 -0.0015 0.0047  -0.0072 208 THR A N   
1679 C  CA  . THR A 207 ? 0.1350 0.1561 0.0928 -0.0111 0.0241  -0.0157 208 THR A CA  
1680 C  C   . THR A 207 ? 0.1368 0.1289 0.1115 -0.0058 0.0031  0.0017  208 THR A C   
1681 O  O   . THR A 207 ? 0.1430 0.1467 0.1044 -0.0026 0.0035  0.0002  208 THR A O   
1682 C  CB  . THR A 207 ? 0.1578 0.1446 0.1517 -0.0027 0.0337  -0.0201 208 THR A CB  
1683 O  OG1 . THR A 207 ? 0.1984 0.1544 0.1337 0.0055  0.0018  -0.0205 208 THR A OG1 
1684 C  CG2 . THR A 207 ? 0.1682 0.1767 0.1521 -0.0068 0.0463  0.0029  208 THR A CG2 
1685 N  N   . TRP A 208 ? 0.1301 0.1263 0.1107 0.0147  0.0148  -0.0115 209 TRP A N   
1686 C  CA  . TRP A 208 ? 0.1195 0.1181 0.1361 0.0021  0.0165  0.0027  209 TRP A CA  
1687 C  C   . TRP A 208 ? 0.1168 0.1559 0.0914 0.0141  0.0326  -0.0076 209 TRP A C   
1688 O  O   . TRP A 208 ? 0.1259 0.1685 0.0926 0.0027  0.0286  -0.0083 209 TRP A O   
1689 C  CB  . TRP A 208 ? 0.1416 0.1584 0.0948 0.0411  0.0265  0.0100  209 TRP A CB  
1690 C  CG  . TRP A 208 ? 0.1329 0.1238 0.0777 0.0061  0.0099  0.0044  209 TRP A CG  
1691 C  CD1 . TRP A 208 ? 0.1160 0.1446 0.0994 0.0129  0.0194  0.0063  209 TRP A CD1 
1692 C  CD2 . TRP A 208 ? 0.1118 0.1235 0.0881 0.0205  0.0126  -0.0074 209 TRP A CD2 
1693 N  NE1 . TRP A 208 ? 0.1470 0.1368 0.0926 0.0092  0.0156  -0.0095 209 TRP A NE1 
1694 C  CE2 . TRP A 208 ? 0.1275 0.1273 0.0986 0.0131  0.0171  -0.0049 209 TRP A CE2 
1695 C  CE3 . TRP A 208 ? 0.1335 0.1113 0.1079 0.0139  -0.0131 0.0003  209 TRP A CE3 
1696 C  CZ2 . TRP A 208 ? 0.1335 0.1408 0.1032 0.0321  0.0197  -0.0188 209 TRP A CZ2 
1697 C  CZ3 . TRP A 208 ? 0.1251 0.1454 0.1156 0.0270  0.0165  -0.0060 209 TRP A CZ3 
1698 C  CH2 . TRP A 208 ? 0.1307 0.1428 0.1102 0.0273  0.0166  -0.0115 209 TRP A CH2 
1699 N  N   . ILE A 209 ? 0.1090 0.1328 0.1133 0.0117  0.0161  0.0019  210 ILE A N   
1700 C  CA  . ILE A 209 ? 0.1125 0.1386 0.1178 0.0100  0.0181  -0.0228 210 ILE A CA  
1701 C  C   . ILE A 209 ? 0.1250 0.1411 0.0786 0.0021  0.0140  -0.0117 210 ILE A C   
1702 O  O   . ILE A 209 ? 0.1470 0.1328 0.0831 0.0010  0.0304  0.0025  210 ILE A O   
1703 C  CB  . ILE A 209 ? 0.1244 0.1326 0.1273 0.0207  0.0223  -0.0147 210 ILE A CB  
1704 C  CG1 . ILE A 209 ? 0.1573 0.1273 0.1680 0.0214  0.0206  -0.0092 210 ILE A CG1 
1705 C  CG2 . ILE A 209 ? 0.1082 0.1894 0.1604 0.0029  0.0207  0.0165  210 ILE A CG2 
1706 C  CD1 . ILE A 209 ? 0.1764 0.1659 0.1575 0.0559  0.0027  -0.0074 210 ILE A CD1 
1707 N  N   . VAL A 210 ? 0.1336 0.1296 0.1160 0.0179  0.0100  -0.0006 211 VAL A N   
1708 C  CA  . VAL A 210 ? 0.1196 0.1205 0.1241 0.0051  0.0153  0.0080  211 VAL A CA  
1709 C  C   . VAL A 210 ? 0.1347 0.1164 0.0862 -0.0002 0.0205  0.0001  211 VAL A C   
1710 O  O   . VAL A 210 ? 0.1537 0.1464 0.1028 -0.0053 0.0276  0.0170  211 VAL A O   
1711 C  CB  . VAL A 210 ? 0.1168 0.1328 0.1460 0.0088  0.0156  0.0096  211 VAL A CB  
1712 C  CG1 . VAL A 210 ? 0.1591 0.1235 0.1750 0.0100  0.0228  -0.0018 211 VAL A CG1 
1713 C  CG2 . VAL A 210 ? 0.1043 0.1611 0.1853 -0.0021 0.0029  -0.0105 211 VAL A CG2 
1714 N  N   . LEU A 211 ? 0.1214 0.1481 0.1029 0.0052  0.0232  -0.0077 212 LEU A N   
1715 C  CA  . LEU A 211 ? 0.1199 0.1437 0.1280 -0.0075 0.0095  -0.0109 212 LEU A CA  
1716 C  C   . LEU A 211 ? 0.1292 0.1452 0.1543 -0.0184 0.0245  0.0006  212 LEU A C   
1717 O  O   . LEU A 211 ? 0.1480 0.1732 0.1234 0.0027  0.0082  -0.0003 212 LEU A O   
1718 C  CB  . LEU A 211 ? 0.1414 0.1615 0.1285 0.0038  0.0029  0.0088  212 LEU A CB  
1719 C  CG  . LEU A 211 ? 0.1207 0.1659 0.1328 0.0127  0.0079  0.0103  212 LEU A CG  
1720 C  CD1 . LEU A 211 ? 0.1380 0.2253 0.1833 -0.0136 -0.0271 0.0093  212 LEU A CD1 
1721 C  CD2 . LEU A 211 ? 0.1707 0.1818 0.1348 -0.0040 0.0505  0.0027  212 LEU A CD2 
1722 N  N   . LYS A 212 ? 0.1412 0.1747 0.1230 -0.0238 0.0156  0.0150  213 LYS A N   
1723 C  CA  . LYS A 212 ? 0.1788 0.1702 0.1311 -0.0174 -0.0013 0.0230  213 LYS A CA  
1724 C  C   . LYS A 212 ? 0.1454 0.1577 0.1180 -0.0120 0.0175  0.0285  213 LYS A C   
1725 O  O   . LYS A 212 ? 0.1664 0.1590 0.2029 -0.0127 -0.0001 0.0168  213 LYS A O   
1726 C  CB  . LYS A 212 ? 0.3513 0.2577 0.1009 -0.0414 0.0462  0.0416  213 LYS A CB  
1727 C  CG  . LYS A 212 ? 0.5074 0.3132 0.1953 -0.1274 0.0621  0.0197  213 LYS A CG  
1728 C  CD  . LYS A 212 ? 0.5935 0.5804 0.2429 -0.2653 0.1553  -0.0759 213 LYS A CD  
1729 N  N   . GLU A 213 ? 0.1462 0.1747 0.1205 -0.0094 -0.0034 0.0048  214 GLU A N   
1730 C  CA  . GLU A 213 ? 0.1328 0.1552 0.1161 0.0042  0.0068  0.0003  214 GLU A CA  
1731 C  C   . GLU A 213 ? 0.1479 0.1596 0.1141 0.0207  -0.0019 0.0345  214 GLU A C   
1732 O  O   . GLU A 213 ? 0.1280 0.1436 0.1569 0.0004  0.0139  0.0308  214 GLU A O   
1733 C  CB  . GLU A 213 ? 0.1257 0.2278 0.1494 0.0024  0.0094  0.0145  214 GLU A CB  
1734 C  CG  . GLU A 213 ? 0.2040 0.2503 0.2185 -0.0433 -0.0086 -0.0098 214 GLU A CG  
1735 C  CD  . GLU A 213 ? 0.1879 0.3301 0.3441 -0.0590 0.0092  -0.0347 214 GLU A CD  
1736 O  OE1 . GLU A 213 ? 0.1473 0.2889 0.2896 -0.0243 0.0053  0.0002  214 GLU A OE1 
1737 O  OE2 . GLU A 213 ? 0.2283 0.6063 0.4089 -0.0111 0.0190  -0.0872 214 GLU A OE2 
1738 N  N   . PRO A 214 ? 0.1680 0.1399 0.1240 0.0055  0.0059  0.0190  215 PRO A N   
1739 C  CA  . PRO A 214 ? 0.1541 0.1604 0.1222 0.0144  0.0004  0.0145  215 PRO A CA  
1740 C  C   . PRO A 214 ? 0.1511 0.1621 0.1207 -0.0208 0.0027  -0.0165 215 PRO A C   
1741 O  O   . PRO A 214 ? 0.1605 0.2122 0.1850 -0.0277 -0.0179 0.0238  215 PRO A O   
1742 C  CB  . PRO A 214 ? 0.1678 0.1199 0.1984 -0.0119 0.0067  0.0098  215 PRO A CB  
1743 C  CG  . PRO A 214 ? 0.3326 0.1821 0.2763 0.0666  0.1189  0.0659  215 PRO A CG  
1744 C  CD  . PRO A 214 ? 0.2086 0.1473 0.2099 0.0218  0.0357  0.0390  215 PRO A CD  
1745 N  N   . ILE A 215 ? 0.1275 0.1571 0.1258 -0.0020 -0.0020 0.0064  216 ILE A N   
1746 C  CA  . ILE A 215 ? 0.1446 0.1555 0.1258 -0.0089 -0.0157 0.0089  216 ILE A CA  
1747 C  C   . ILE A 215 ? 0.1495 0.1483 0.1427 -0.0110 -0.0033 -0.0001 216 ILE A C   
1748 O  O   . ILE A 215 ? 0.1493 0.1455 0.1586 0.0032  -0.0232 -0.0186 216 ILE A O   
1749 C  CB  . ILE A 215 ? 0.1458 0.1410 0.1524 0.0120  0.0259  0.0068  216 ILE A CB  
1750 C  CG1 . ILE A 215 ? 0.1558 0.1695 0.1067 -0.0104 0.0190  0.0227  216 ILE A CG1 
1751 C  CG2 . ILE A 215 ? 0.1562 0.1644 0.1609 0.0178  0.0215  -0.0337 216 ILE A CG2 
1752 C  CD1 . ILE A 215 ? 0.1869 0.1624 0.1485 0.0148  0.0359  0.0432  216 ILE A CD1 
1753 N  N   . SER A 216 ? 0.1656 0.1435 0.1517 -0.0089 -0.0155 -0.0103 217 SER A N   
1754 C  CA  A SER A 216 ? 0.2170 0.1414 0.1330 -0.0033 -0.0326 -0.0239 217 SER A CA  
1755 C  CA  B SER A 216 ? 0.2073 0.1523 0.1406 0.0042  -0.0237 -0.0195 217 SER A CA  
1756 C  C   . SER A 216 ? 0.1511 0.1385 0.1407 -0.0073 -0.0297 -0.0178 217 SER A C   
1757 O  O   . SER A 216 ? 0.1815 0.1437 0.1468 0.0042  -0.0231 0.0096  217 SER A O   
1758 C  CB  A SER A 216 ? 0.3112 0.1188 0.1170 -0.0330 0.0416  -0.0342 217 SER A CB  
1759 C  CB  B SER A 216 ? 0.3079 0.1536 0.1659 -0.0620 0.0376  0.0104  217 SER A CB  
1760 O  OG  A SER A 216 ? 0.2292 0.2156 0.1066 -0.0468 0.0141  -0.0203 217 SER A OG  
1761 O  OG  B SER A 216 ? 0.3171 0.2079 0.2287 -0.0260 0.0074  -0.0244 217 SER A OG  
1762 N  N   . VAL A 217 ? 0.1600 0.1389 0.1437 0.0013  -0.0147 -0.0068 218 VAL A N   
1763 C  CA  . VAL A 217 ? 0.1653 0.1292 0.1382 0.0156  -0.0164 0.0001  218 VAL A CA  
1764 C  C   . VAL A 217 ? 0.1606 0.1371 0.1131 0.0065  0.0053  -0.0004 218 VAL A C   
1765 O  O   . VAL A 217 ? 0.1611 0.1497 0.1425 -0.0031 -0.0176 0.0021  218 VAL A O   
1766 C  CB  . VAL A 217 ? 0.1362 0.1404 0.2032 0.0095  -0.0142 -0.0242 218 VAL A CB  
1767 C  CG1 . VAL A 217 ? 0.1530 0.1386 0.1764 0.0089  -0.0263 -0.0258 218 VAL A CG1 
1768 C  CG2 . VAL A 217 ? 0.1306 0.1373 0.2472 0.0050  -0.0285 -0.0257 218 VAL A CG2 
1769 N  N   . SER A 218 ? 0.1471 0.1373 0.1104 -0.0069 -0.0063 0.0071  219 SER A N   
1770 C  CA  . SER A 218 ? 0.1588 0.1351 0.1460 0.0098  -0.0088 0.0006  219 SER A CA  
1771 C  C   . SER A 218 ? 0.1493 0.1333 0.1464 0.0025  -0.0037 0.0013  219 SER A C   
1772 O  O   . SER A 218 ? 0.1657 0.1234 0.1508 -0.0059 -0.0157 -0.0068 219 SER A O   
1773 C  CB  . SER A 218 ? 0.1746 0.1713 0.1381 -0.0203 -0.0128 0.0027  219 SER A CB  
1774 O  OG  . SER A 218 ? 0.1620 0.1795 0.1474 -0.0159 0.0070  -0.0065 219 SER A OG  
1775 N  N   . SER A 219 ? 0.1604 0.1196 0.1650 -0.0055 0.0022  -0.0080 220 SER A N   
1776 C  CA  . SER A 219 ? 0.1817 0.1447 0.1928 0.0282  0.0220  0.0052  220 SER A CA  
1777 C  C   . SER A 219 ? 0.1582 0.1183 0.1930 -0.0032 -0.0093 0.0064  220 SER A C   
1778 O  O   . SER A 219 ? 0.1500 0.1540 0.2032 -0.0087 -0.0036 0.0048  220 SER A O   
1779 C  CB  . SER A 219 ? 0.2093 0.1304 0.2673 -0.0304 0.0160  -0.0121 220 SER A CB  
1780 O  OG  . SER A 219 ? 0.2643 0.1700 0.2649 -0.0122 0.0256  -0.0166 220 SER A OG  
1781 N  N   . GLU A 220 ? 0.1693 0.1482 0.1657 0.0049  -0.0016 -0.0130 221 GLU A N   
1782 C  CA  . GLU A 220 ? 0.1883 0.1450 0.1691 0.0154  -0.0103 0.0146  221 GLU A CA  
1783 C  C   . GLU A 220 ? 0.1423 0.1593 0.1421 -0.0063 0.0048  -0.0174 221 GLU A C   
1784 O  O   . GLU A 220 ? 0.1863 0.1653 0.1732 0.0113  0.0284  -0.0172 221 GLU A O   
1785 C  CB  . GLU A 220 ? 0.1890 0.1689 0.1908 -0.0089 -0.0171 -0.0471 221 GLU A CB  
1786 C  CG  . GLU A 220 ? 0.2149 0.1869 0.2825 -0.0263 0.0245  -0.0787 221 GLU A CG  
1787 C  CD  . GLU A 220 ? 0.3650 0.1574 0.2451 -0.0337 0.0343  -0.0406 221 GLU A CD  
1788 O  OE1 . GLU A 220 ? 0.2260 0.2249 0.2210 -0.0678 0.0195  -0.0511 221 GLU A OE1 
1789 O  OE2 . GLU A 220 ? 0.3615 0.2176 0.3778 -0.0936 -0.0133 -0.0398 221 GLU A OE2 
1790 N  N   . GLN A 221 ? 0.1520 0.1363 0.1454 0.0082  -0.0064 -0.0032 222 GLN A N   
1791 C  CA  . GLN A 221 ? 0.1288 0.1320 0.1626 0.0043  -0.0010 -0.0062 222 GLN A CA  
1792 C  C   . GLN A 221 ? 0.1420 0.1639 0.1817 0.0067  -0.0143 0.0074  222 GLN A C   
1793 O  O   . GLN A 221 ? 0.1617 0.1684 0.1624 -0.0020 0.0089  0.0072  222 GLN A O   
1794 C  CB  . GLN A 221 ? 0.1571 0.1354 0.1444 0.0065  -0.0098 -0.0215 222 GLN A CB  
1795 C  CG  . GLN A 221 ? 0.1454 0.1261 0.1113 0.0017  0.0075  -0.0121 222 GLN A CG  
1796 C  CD  . GLN A 221 ? 0.1505 0.1165 0.1128 0.0001  0.0106  -0.0080 222 GLN A CD  
1797 O  OE1 . GLN A 221 ? 0.1626 0.1578 0.1201 0.0035  -0.0002 0.0072  222 GLN A OE1 
1798 N  NE2 . GLN A 221 ? 0.1675 0.1345 0.1284 0.0174  -0.0066 -0.0078 222 GLN A NE2 
1799 N  N   . VAL A 222 ? 0.1433 0.1405 0.1703 0.0080  -0.0170 -0.0083 223 VAL A N   
1800 C  CA  . VAL A 222 ? 0.1368 0.1760 0.1675 0.0076  -0.0121 0.0161  223 VAL A CA  
1801 C  C   . VAL A 222 ? 0.1567 0.1500 0.1619 -0.0059 0.0025  0.0199  223 VAL A C   
1802 O  O   . VAL A 222 ? 0.1666 0.1897 0.1439 -0.0197 0.0044  0.0012  223 VAL A O   
1803 C  CB  . VAL A 222 ? 0.1918 0.2413 0.1811 -0.0295 -0.0530 0.0411  223 VAL A CB  
1804 C  CG1 . VAL A 222 ? 0.2241 0.2504 0.2669 -0.0119 -0.0372 0.0551  223 VAL A CG1 
1805 C  CG2 . VAL A 222 ? 0.2088 0.2504 0.2174 -0.0557 -0.0406 0.0013  223 VAL A CG2 
1806 N  N   A LEU A 223 ? 0.1631 0.1682 0.1803 0.0255  0.0134  -0.0092 224 LEU A N   
1807 N  N   B LEU A 223 ? 0.1660 0.1678 0.1829 0.0230  0.0160  -0.0092 224 LEU A N   
1808 C  CA  A LEU A 223 ? 0.1680 0.1857 0.1883 0.0086  0.0243  -0.0272 224 LEU A CA  
1809 C  CA  B LEU A 223 ? 0.1681 0.1757 0.2007 0.0081  0.0293  -0.0285 224 LEU A CA  
1810 C  C   A LEU A 223 ? 0.1596 0.2023 0.1232 0.0223  0.0168  -0.0308 224 LEU A C   
1811 C  C   B LEU A 223 ? 0.1659 0.1923 0.1366 0.0237  0.0227  -0.0332 224 LEU A C   
1812 O  O   A LEU A 223 ? 0.1527 0.2034 0.2020 0.0125  0.0236  -0.0017 224 LEU A O   
1813 O  O   B LEU A 223 ? 0.1485 0.2069 0.2166 0.0185  0.0225  -0.0108 224 LEU A O   
1814 C  CB  A LEU A 223 ? 0.2374 0.1829 0.2949 0.0092  0.0004  -0.0613 224 LEU A CB  
1815 C  CB  B LEU A 223 ? 0.2050 0.1655 0.2626 0.0478  0.0203  -0.0630 224 LEU A CB  
1816 C  CG  A LEU A 223 ? 0.2299 0.2227 0.3301 0.0265  0.0286  -0.0394 224 LEU A CG  
1817 C  CG  B LEU A 223 ? 0.2206 0.1620 0.3625 0.0201  0.0031  -0.0352 224 LEU A CG  
1818 N  N   . LYS A 224 ? 0.1720 0.1760 0.1414 0.0070  0.0104  -0.0026 225 LYS A N   
1819 C  CA  . LYS A 224 ? 0.1657 0.1756 0.1839 0.0100  -0.0183 0.0023  225 LYS A CA  
1820 C  C   . LYS A 224 ? 0.1818 0.1565 0.1169 0.0022  0.0168  -0.0137 225 LYS A C   
1821 O  O   . LYS A 224 ? 0.1781 0.1782 0.1575 -0.0044 -0.0046 0.0004  225 LYS A O   
1822 C  CB  . LYS A 224 ? 0.1815 0.2284 0.2342 0.0463  -0.0326 -0.0004 225 LYS A CB  
1823 C  CG  . LYS A 224 ? 0.2034 0.2913 0.3207 0.0158  -0.0651 -0.0125 225 LYS A CG  
1824 C  CD  . LYS A 224 ? 0.2810 0.5787 0.3976 0.1003  -0.1344 -0.0211 225 LYS A CD  
1825 C  CE  . LYS A 224 ? 0.4767 0.4156 0.5792 0.0555  -0.3403 -0.0875 225 LYS A CE  
1826 N  NZ  . LYS A 224 ? 0.7309 0.4791 0.5799 -0.0134 -0.1671 -0.3097 225 LYS A NZ  
1827 N  N   . PHE A 225 ? 0.1597 0.1631 0.1169 0.0186  -0.0105 -0.0160 226 PHE A N   
1828 C  CA  . PHE A 225 ? 0.1570 0.1652 0.1011 0.0172  0.0080  -0.0251 226 PHE A CA  
1829 C  C   . PHE A 225 ? 0.1574 0.1711 0.1389 0.0161  0.0100  -0.0017 226 PHE A C   
1830 O  O   . PHE A 225 ? 0.1601 0.1667 0.1487 0.0145  0.0190  -0.0186 226 PHE A O   
1831 C  CB  . PHE A 225 ? 0.1646 0.1854 0.1081 0.0219  0.0057  -0.0205 226 PHE A CB  
1832 C  CG  . PHE A 225 ? 0.1573 0.1638 0.1450 0.0017  0.0236  -0.0100 226 PHE A CG  
1833 C  CD1 . PHE A 225 ? 0.1600 0.2093 0.1979 0.0416  0.0170  -0.0375 226 PHE A CD1 
1834 C  CD2 . PHE A 225 ? 0.1655 0.2119 0.1588 0.0339  0.0162  -0.0258 226 PHE A CD2 
1835 C  CE1 . PHE A 225 ? 0.1553 0.2106 0.1742 0.0204  0.0410  -0.0098 226 PHE A CE1 
1836 C  CE2 . PHE A 225 ? 0.1517 0.2350 0.1905 0.0299  0.0070  -0.0659 226 PHE A CE2 
1837 C  CZ  . PHE A 225 ? 0.1653 0.2230 0.1962 0.0291  -0.0070 -0.0322 226 PHE A CZ  
1838 N  N   . ARG A 226 ? 0.1562 0.1483 0.1613 0.0113  0.0050  -0.0238 227 ARG A N   
1839 C  CA  . ARG A 226 ? 0.1824 0.1597 0.1729 0.0284  0.0000  -0.0098 227 ARG A CA  
1840 C  C   . ARG A 226 ? 0.1621 0.1742 0.1849 0.0113  0.0004  -0.0340 227 ARG A C   
1841 O  O   . ARG A 226 ? 0.1678 0.2289 0.2490 0.0446  -0.0044 -0.0493 227 ARG A O   
1842 C  CB  . ARG A 226 ? 0.1646 0.1602 0.2227 0.0388  -0.0346 0.0124  227 ARG A CB  
1843 C  CG  . ARG A 226 ? 0.1942 0.1564 0.2079 0.0260  -0.0219 -0.0031 227 ARG A CG  
1844 C  CD  . ARG A 226 ? 0.2393 0.1724 0.2427 0.0269  -0.0042 0.0120  227 ARG A CD  
1845 N  NE  . ARG A 226 ? 0.1965 0.1691 0.2037 0.0061  -0.0214 -0.0027 227 ARG A NE  
1846 C  CZ  . ARG A 226 ? 0.2134 0.1599 0.2108 -0.0163 -0.0299 -0.0092 227 ARG A CZ  
1847 N  NH1 . ARG A 226 ? 0.2184 0.2709 0.3654 -0.0264 -0.0361 -0.1382 227 ARG A NH1 
1848 N  NH2 . ARG A 226 ? 0.2215 0.2113 0.2490 -0.0354 0.0034  -0.0281 227 ARG A NH2 
1849 N  N   . LYS A 227 ? 0.1671 0.2194 0.1399 -0.0009 0.0040  -0.0279 228 LYS A N   
1850 C  CA  . LYS A 227 ? 0.2155 0.2091 0.1315 0.0048  0.0022  -0.0519 228 LYS A CA  
1851 C  C   . LYS A 227 ? 0.1756 0.2141 0.1238 0.0157  0.0280  -0.0521 228 LYS A C   
1852 O  O   . LYS A 227 ? 0.2124 0.2372 0.1479 0.0247  0.0490  -0.0677 228 LYS A O   
1853 C  CB  . LYS A 227 ? 0.2960 0.2456 0.1743 0.0079  -0.0616 -0.0464 228 LYS A CB  
1854 C  CG  . LYS A 227 ? 0.2909 0.2877 0.2166 -0.0484 -0.0151 -0.0829 228 LYS A CG  
1855 C  CD  . LYS A 227 ? 0.3462 0.3841 0.3653 -0.0627 -0.1148 -0.0424 228 LYS A CD  
1856 C  CE  . LYS A 227 ? 0.8063 0.3880 0.7174 -0.1905 -0.0212 -0.0209 228 LYS A CE  
1857 N  NZ  . LYS A 227 ? 0.8419 0.3556 0.5431 -0.1209 -0.0504 0.0395  228 LYS A NZ  
1858 N  N   . LEU A 228 ? 0.1904 0.1867 0.1263 0.0193  -0.0006 -0.0487 229 LEU A N   
1859 C  CA  . LEU A 228 ? 0.1462 0.1976 0.1280 0.0172  0.0172  -0.0572 229 LEU A CA  
1860 C  C   . LEU A 228 ? 0.1693 0.2151 0.1401 0.0259  0.0115  -0.0412 229 LEU A C   
1861 O  O   . LEU A 228 ? 0.2057 0.2199 0.1635 0.0447  -0.0104 -0.0294 229 LEU A O   
1862 C  CB  . LEU A 228 ? 0.1659 0.2143 0.1109 0.0402  0.0200  -0.0439 229 LEU A CB  
1863 C  CG  . LEU A 228 ? 0.1518 0.1782 0.1600 0.0157  0.0098  -0.0383 229 LEU A CG  
1864 C  CD1 . LEU A 228 ? 0.1703 0.2231 0.1641 0.0561  0.0027  -0.0480 229 LEU A CD1 
1865 C  CD2 . LEU A 228 ? 0.2134 0.2423 0.2012 0.0405  0.0160  0.0206  229 LEU A CD2 
1866 N  N   . ASN A 229 ? 0.1711 0.1966 0.1486 0.0223  0.0150  -0.0400 230 ASN A N   
1867 C  CA  . ASN A 229 ? 0.1407 0.2321 0.1196 0.0168  0.0223  -0.0580 230 ASN A CA  
1868 C  C   . ASN A 229 ? 0.1883 0.2174 0.1432 0.0325  0.0280  -0.0504 230 ASN A C   
1869 O  O   . ASN A 229 ? 0.1689 0.2147 0.1723 0.0201  0.0126  -0.0609 230 ASN A O   
1870 C  CB  . ASN A 229 ? 0.2072 0.2432 0.1153 0.0369  0.0336  -0.0701 230 ASN A CB  
1871 C  CG  . ASN A 229 ? 0.1770 0.2719 0.1468 0.0353  0.0264  -0.0920 230 ASN A CG  
1872 O  OD1 . ASN A 229 ? 0.3844 0.3298 0.2258 0.0216  0.1350  -0.0938 230 ASN A OD1 
1873 N  ND2 . ASN A 229 ? 0.2447 0.2763 0.2106 0.0039  0.0533  -0.0619 230 ASN A ND2 
1874 N  N   . PHE A 230 ? 0.1739 0.2421 0.1502 0.0206  0.0263  -0.0548 231 PHE A N   
1875 C  CA  . PHE A 230 ? 0.1639 0.2411 0.1939 0.0144  0.0095  -0.0442 231 PHE A CA  
1876 C  C   . PHE A 230 ? 0.1770 0.2735 0.1752 0.0172  0.0084  -0.0480 231 PHE A C   
1877 O  O   . PHE A 230 ? 0.1869 0.2690 0.2199 0.0066  0.0348  -0.0800 231 PHE A O   
1878 C  CB  . PHE A 230 ? 0.1772 0.2778 0.1521 0.0530  0.0157  -0.0419 231 PHE A CB  
1879 C  CG  . PHE A 230 ? 0.1814 0.2924 0.1414 0.0002  0.0214  -0.0769 231 PHE A CG  
1880 C  CD1 . PHE A 230 ? 0.1587 0.2673 0.1289 0.0055  0.0339  -0.0330 231 PHE A CD1 
1881 C  CD2 . PHE A 230 ? 0.1745 0.2809 0.1993 0.0261  -0.0002 -0.0612 231 PHE A CD2 
1882 C  CE1 . PHE A 230 ? 0.1984 0.2481 0.1348 -0.0181 0.0453  -0.0558 231 PHE A CE1 
1883 C  CE2 . PHE A 230 ? 0.1593 0.2612 0.2100 0.0266  -0.0125 -0.0611 231 PHE A CE2 
1884 C  CZ  . PHE A 230 ? 0.1843 0.2477 0.2377 0.0231  0.0070  -0.0692 231 PHE A CZ  
1885 N  N   . ASN A 231 ? 0.1415 0.3072 0.2298 0.0331  0.0427  -0.0736 232 ASN A N   
1886 C  CA  . ASN A 231 ? 0.1483 0.2885 0.2602 0.0281  0.0478  -0.0493 232 ASN A CA  
1887 C  C   . ASN A 231 ? 0.1721 0.2788 0.1757 0.0107  0.0572  -0.0499 232 ASN A C   
1888 O  O   . ASN A 231 ? 0.1804 0.2684 0.2080 -0.0076 0.0469  -0.0342 232 ASN A O   
1889 C  CB  . ASN A 231 ? 0.1553 0.3345 0.2801 0.0192  0.0702  -0.0886 232 ASN A CB  
1890 C  CG  . ASN A 231 ? 0.1876 0.2799 0.2964 0.0363  0.0293  -0.0522 232 ASN A CG  
1891 O  OD1 . ASN A 231 ? 0.2230 0.2522 0.2680 0.0512  0.0285  -0.0831 232 ASN A OD1 
1892 N  ND2 . ASN A 231 ? 0.2602 0.3190 0.2633 0.0352  0.0226  -0.1036 232 ASN A ND2 
1893 N  N   . GLY A 232 ? 0.2089 0.2748 0.2644 -0.0057 0.0563  -0.0709 233 GLY A N   
1894 C  CA  . GLY A 232 ? 0.2309 0.2746 0.2641 -0.0362 0.0921  -0.0873 233 GLY A CA  
1895 C  C   . GLY A 232 ? 0.3197 0.3642 0.2931 -0.0008 0.0952  -0.1266 233 GLY A C   
1896 O  O   . GLY A 232 ? 0.3141 0.3392 0.2586 -0.0457 0.1293  -0.1405 233 GLY A O   
1897 N  N   . GLU A 233 ? 0.3176 0.4465 0.2278 -0.1233 0.1221  -0.0756 234 GLU A N   
1898 C  CA  . GLU A 233 ? 0.4821 0.5845 0.1667 -0.1341 0.1338  -0.0710 234 GLU A CA  
1899 C  C   . GLU A 233 ? 0.5605 0.5644 0.3553 -0.1200 0.2624  -0.0257 234 GLU A C   
1900 O  O   . GLU A 233 ? 0.4205 0.5554 0.2465 -0.0038 0.1723  -0.0066 234 GLU A O   
1901 C  CB  . GLU A 233 ? 0.4148 0.7738 0.2220 -0.0754 0.1160  -0.1273 234 GLU A CB  
1902 C  CG  . GLU A 233 ? 0.4634 1.0112 0.3130 -0.1427 0.0864  -0.2578 234 GLU A CG  
1903 N  N   . GLY A 234 ? 0.5884 0.5489 0.4371 -0.1251 0.1709  -0.2750 235 GLY A N   
1904 C  CA  . GLY A 234 ? 0.5439 0.6442 0.2763 0.0557  0.2540  -0.1074 235 GLY A CA  
1905 C  C   . GLY A 234 ? 0.5116 0.8231 0.4716 -0.0105 0.1886  -0.0996 235 GLY A C   
1906 O  O   . GLY A 234 ? 0.6066 0.8840 0.6948 -0.0289 0.4610  -0.2090 235 GLY A O   
1907 N  N   . GLU A 235 ? 0.4763 0.5998 0.4364 -0.0326 0.2608  -0.2319 236 GLU A N   
1908 C  CA  . GLU A 235 ? 0.3926 0.4724 0.3410 -0.1244 0.2000  -0.1678 236 GLU A CA  
1909 C  C   . GLU A 235 ? 0.2776 0.4275 0.2554 0.0017  0.0620  -0.1229 236 GLU A C   
1910 O  O   . GLU A 235 ? 0.2570 0.4225 0.4292 0.0032  0.0842  -0.1728 236 GLU A O   
1911 C  CB  . GLU A 235 ? 0.3287 0.5889 0.4677 -0.0736 0.1649  -0.2768 236 GLU A CB  
1912 C  CG  . GLU A 235 ? 0.7251 0.6032 0.5705 -0.1684 0.1717  -0.0282 236 GLU A CG  
1913 C  CD  . GLU A 235 ? 0.9702 0.7202 1.0459 0.0411  0.0378  -0.4769 236 GLU A CD  
1914 O  OE1 . GLU A 235 ? 0.2867 0.7521 1.0324 -0.2233 0.0502  -0.1850 236 GLU A OE1 
1915 O  OE2 . GLU A 235 ? 0.9945 0.8549 1.0170 -0.0108 0.3238  -0.5929 236 GLU A OE2 
1916 N  N   . PRO A 236 ? 0.2433 0.3212 0.3507 -0.0905 0.0624  -0.0561 237 PRO A N   
1917 C  CA  . PRO A 236 ? 0.1595 0.3244 0.4291 0.0055  0.0751  -0.0117 237 PRO A CA  
1918 C  C   . PRO A 236 ? 0.1860 0.3328 0.3193 0.0555  0.0948  -0.0972 237 PRO A C   
1919 O  O   . PRO A 236 ? 0.2206 0.4356 0.3272 0.0655  0.0413  -0.1641 237 PRO A O   
1920 C  CB  . PRO A 236 ? 0.1858 0.3079 0.4611 -0.0179 0.0142  -0.0342 237 PRO A CB  
1921 C  CG  . PRO A 236 ? 0.2271 0.4465 0.3625 -0.0335 0.0657  0.0176  237 PRO A CG  
1922 C  CD  . PRO A 236 ? 0.2346 0.4075 0.4936 -0.0398 0.0063  -0.0136 237 PRO A CD  
1923 N  N   . GLU A 237 ? 0.2308 0.3136 0.3035 0.0501  0.0170  -0.0974 238 GLU A N   
1924 C  CA  . GLU A 237 ? 0.2386 0.2221 0.2465 0.0438  0.0351  -0.0581 238 GLU A CA  
1925 C  C   . GLU A 237 ? 0.3013 0.2634 0.2476 0.0939  -0.0168 -0.1051 238 GLU A C   
1926 O  O   . GLU A 237 ? 0.3312 0.3079 0.2499 0.1122  -0.0384 -0.0902 238 GLU A O   
1927 C  CB  . GLU A 237 ? 0.2536 0.2301 0.2461 -0.0102 0.0148  -0.0162 238 GLU A CB  
1928 C  CG  . GLU A 237 ? 0.2565 0.3173 0.1779 0.0252  0.0690  0.0273  238 GLU A CG  
1929 C  CD  . GLU A 237 ? 0.2868 0.2759 0.3250 0.0659  0.0122  0.0029  238 GLU A CD  
1930 O  OE1 . GLU A 237 ? 0.3643 0.3481 0.3571 -0.0570 0.0297  -0.0245 238 GLU A OE1 
1931 O  OE2 . GLU A 237 ? 0.3583 0.6080 0.2954 -0.0629 0.0254  0.1162  238 GLU A OE2 
1932 N  N   . GLU A 238 ? 0.2210 0.2565 0.2564 0.0282  0.0480  -0.0895 239 GLU A N   
1933 C  CA  . GLU A 238 ? 0.1923 0.3093 0.2788 0.0506  0.0230  -0.1037 239 GLU A CA  
1934 C  C   . GLU A 238 ? 0.2066 0.2434 0.1606 0.0552  0.0500  -0.0725 239 GLU A C   
1935 O  O   . GLU A 238 ? 0.2156 0.2756 0.3213 0.0806  0.0334  -0.0841 239 GLU A O   
1936 C  CB  . GLU A 238 ? 0.1725 0.3653 0.4350 0.0216  0.0021  -0.1791 239 GLU A CB  
1937 C  CG  . GLU A 238 ? 0.1982 0.4839 0.2518 0.0201  0.0521  -0.0920 239 GLU A CG  
1938 C  CD  . GLU A 238 ? 0.3412 0.4112 0.3256 -0.0545 -0.0023 -0.0618 239 GLU A CD  
1939 O  OE1 . GLU A 238 ? 0.3546 0.5165 0.3083 -0.0859 0.0436  -0.0223 239 GLU A OE1 
1940 O  OE2 . GLU A 238 ? 0.5299 0.4805 0.2992 -0.1759 0.1141  -0.0772 239 GLU A OE2 
1941 N  N   . LEU A 239 ? 0.2363 0.2548 0.2137 0.0646  -0.0077 -0.0505 240 LEU A N   
1942 C  CA  . LEU A 239 ? 0.2239 0.2282 0.1688 0.0414  -0.0003 -0.0644 240 LEU A CA  
1943 C  C   . LEU A 239 ? 0.2023 0.2360 0.1345 0.0608  -0.0027 -0.0276 240 LEU A C   
1944 O  O   . LEU A 239 ? 0.1990 0.2407 0.1817 0.0831  0.0000  -0.0595 240 LEU A O   
1945 C  CB  . LEU A 239 ? 0.2598 0.2361 0.2108 -0.0083 -0.0265 -0.0432 240 LEU A CB  
1946 C  CG  . LEU A 239 ? 0.2368 0.2978 0.2299 0.0210  -0.0034 -0.0663 240 LEU A CG  
1947 C  CD1 . LEU A 239 ? 0.2256 0.2534 0.4741 0.0550  -0.0373 -0.0037 240 LEU A CD1 
1948 C  CD2 . LEU A 239 ? 0.2273 0.3050 0.2133 0.0623  -0.0157 -0.0760 240 LEU A CD2 
1949 N  N   . MET A 240 ? 0.1914 0.1942 0.1511 0.0539  0.0065  -0.0410 241 MET A N   
1950 C  CA  . MET A 240 ? 0.1556 0.1929 0.1580 0.0414  0.0141  -0.0398 241 MET A CA  
1951 C  C   . MET A 240 ? 0.1523 0.1750 0.1356 0.0449  -0.0002 -0.0557 241 MET A C   
1952 O  O   . MET A 240 ? 0.1420 0.1829 0.2058 0.0337  -0.0172 -0.0331 241 MET A O   
1953 C  CB  . MET A 240 ? 0.1845 0.1872 0.1141 0.0297  0.0217  -0.0234 241 MET A CB  
1954 C  CG  . MET A 240 ? 0.1738 0.2104 0.1243 0.0271  0.0248  -0.0445 241 MET A CG  
1955 S  SD  . MET A 240 ? 0.1743 0.1821 0.1883 0.0234  0.0295  -0.0367 241 MET A SD  
1956 C  CE  . MET A 240 ? 0.1666 0.2258 0.1584 0.0227  0.0465  -0.0081 241 MET A CE  
1957 N  N   . VAL A 241 ? 0.1724 0.1580 0.1826 0.0406  -0.0212 -0.0196 242 VAL A N   
1958 C  CA  . VAL A 241 ? 0.1825 0.1826 0.1412 0.0317  -0.0221 -0.0568 242 VAL A CA  
1959 C  C   . VAL A 241 ? 0.1521 0.1487 0.1368 0.0410  -0.0073 -0.0212 242 VAL A C   
1960 O  O   . VAL A 241 ? 0.1509 0.1871 0.1615 0.0337  -0.0071 -0.0491 242 VAL A O   
1961 C  CB  . VAL A 241 ? 0.1527 0.1741 0.1696 0.0011  -0.0179 -0.0384 242 VAL A CB  
1962 C  CG1 . VAL A 241 ? 0.2062 0.1795 0.2044 0.0301  -0.0550 -0.0771 242 VAL A CG1 
1963 C  CG2 . VAL A 241 ? 0.1710 0.2451 0.2459 0.0285  -0.0004 -0.0647 242 VAL A CG2 
1964 N  N   . ASP A 242 ? 0.1546 0.1426 0.1286 0.0296  0.0092  -0.0195 243 ASP A N   
1965 C  CA  . ASP A 242 ? 0.1571 0.1421 0.1595 0.0387  -0.0155 -0.0326 243 ASP A CA  
1966 C  C   . ASP A 242 ? 0.1529 0.1678 0.1198 0.0241  -0.0009 -0.0281 243 ASP A C   
1967 O  O   . ASP A 242 ? 0.1439 0.1682 0.1942 0.0195  -0.0205 -0.0316 243 ASP A O   
1968 C  CB  . ASP A 242 ? 0.1355 0.1497 0.1766 0.0330  0.0001  -0.0351 243 ASP A CB  
1969 C  CG  . ASP A 242 ? 0.1415 0.1562 0.1892 0.0392  -0.0001 -0.0195 243 ASP A CG  
1970 O  OD1 . ASP A 242 ? 0.1613 0.1412 0.1820 0.0280  -0.0018 -0.0301 243 ASP A OD1 
1971 O  OD2 . ASP A 242 ? 0.1856 0.1714 0.2285 0.0518  0.0086  -0.0323 243 ASP A OD2 
1972 N  N   . ASN A 243 ? 0.1272 0.1388 0.1253 0.0245  0.0113  -0.0263 244 ASN A N   
1973 C  CA  . ASN A 243 ? 0.1376 0.1455 0.1140 -0.0018 0.0061  -0.0124 244 ASN A CA  
1974 C  C   . ASN A 243 ? 0.0867 0.1430 0.1307 -0.0114 0.0032  -0.0269 244 ASN A C   
1975 O  O   . ASN A 243 ? 0.1486 0.1558 0.1544 0.0292  0.0149  -0.0102 244 ASN A O   
1976 C  CB  . ASN A 243 ? 0.1259 0.1804 0.1140 0.0106  0.0069  -0.0125 244 ASN A CB  
1977 C  CG  . ASN A 243 ? 0.1386 0.1617 0.1498 0.0168  0.0223  -0.0097 244 ASN A CG  
1978 O  OD1 . ASN A 243 ? 0.1295 0.1687 0.1835 0.0043  0.0114  0.0069  244 ASN A OD1 
1979 N  ND2 . ASN A 243 ? 0.1481 0.1543 0.1714 0.0068  -0.0184 0.0154  244 ASN A ND2 
1980 N  N   . TRP A 244 ? 0.1153 0.1459 0.1355 0.0103  0.0065  -0.0156 245 TRP A N   
1981 C  CA  . TRP A 244 ? 0.1071 0.1549 0.1296 0.0064  0.0092  -0.0252 245 TRP A CA  
1982 C  C   . TRP A 244 ? 0.1092 0.1395 0.1395 0.0146  0.0089  0.0036  245 TRP A C   
1983 O  O   . TRP A 244 ? 0.1195 0.1728 0.1619 0.0319  -0.0069 -0.0329 245 TRP A O   
1984 C  CB  . TRP A 244 ? 0.1185 0.1294 0.1478 0.0076  0.0046  -0.0137 245 TRP A CB  
1985 C  CG  . TRP A 244 ? 0.1333 0.1368 0.1531 0.0221  -0.0010 -0.0168 245 TRP A CG  
1986 C  CD1 . TRP A 244 ? 0.1342 0.1304 0.1430 0.0127  0.0212  -0.0212 245 TRP A CD1 
1987 C  CD2 . TRP A 244 ? 0.1456 0.1515 0.1395 0.0034  0.0012  -0.0058 245 TRP A CD2 
1988 N  NE1 . TRP A 244 ? 0.1520 0.1491 0.1450 0.0263  0.0091  -0.0175 245 TRP A NE1 
1989 C  CE2 . TRP A 244 ? 0.1250 0.1571 0.1518 0.0171  -0.0026 -0.0037 245 TRP A CE2 
1990 C  CE3 . TRP A 244 ? 0.1534 0.1750 0.1496 0.0070  -0.0144 -0.0035 245 TRP A CE3 
1991 C  CZ2 . TRP A 244 ? 0.1644 0.1479 0.1511 0.0134  -0.0050 0.0006  245 TRP A CZ2 
1992 C  CZ3 . TRP A 244 ? 0.1926 0.1914 0.1295 0.0208  0.0052  -0.0006 245 TRP A CZ3 
1993 C  CH2 . TRP A 244 ? 0.1840 0.1951 0.1556 0.0149  0.0065  -0.0096 245 TRP A CH2 
1994 N  N   . ARG A 245 ? 0.1275 0.1707 0.1226 0.0089  -0.0064 -0.0138 246 ARG A N   
1995 C  CA  . ARG A 245 ? 0.1379 0.1509 0.1229 0.0016  -0.0019 -0.0133 246 ARG A CA  
1996 C  C   . ARG A 245 ? 0.1556 0.1905 0.1159 0.0108  0.0081  -0.0111 246 ARG A C   
1997 O  O   . ARG A 245 ? 0.1470 0.1634 0.1508 -0.0074 0.0186  -0.0185 246 ARG A O   
1998 C  CB  . ARG A 245 ? 0.1318 0.1515 0.0960 0.0155  0.0009  -0.0276 246 ARG A CB  
1999 C  CG  . ARG A 245 ? 0.1263 0.1687 0.1217 -0.0024 -0.0025 -0.0212 246 ARG A CG  
2000 C  CD  . ARG A 245 ? 0.1324 0.1766 0.1131 -0.0017 0.0046  -0.0257 246 ARG A CD  
2001 N  NE  . ARG A 245 ? 0.1401 0.1763 0.1009 -0.0237 0.0048  -0.0098 246 ARG A NE  
2002 C  CZ  . ARG A 245 ? 0.1390 0.1548 0.1419 -0.0197 0.0205  -0.0125 246 ARG A CZ  
2003 N  NH1 . ARG A 245 ? 0.1168 0.2008 0.1318 0.0006  0.0115  -0.0152 246 ARG A NH1 
2004 N  NH2 . ARG A 245 ? 0.1279 0.1786 0.1445 -0.0291 0.0185  -0.0089 246 ARG A NH2 
2005 N  N   . PRO A 246 ? 0.1381 0.1775 0.1449 0.0201  0.0156  -0.0044 247 PRO A N   
2006 C  CA  . PRO A 246 ? 0.1675 0.1453 0.1592 0.0188  0.0242  -0.0004 247 PRO A CA  
2007 C  C   . PRO A 246 ? 0.1486 0.1890 0.1451 -0.0071 0.0099  0.0040  247 PRO A C   
2008 O  O   . PRO A 246 ? 0.1747 0.1450 0.1404 -0.0027 -0.0109 0.0099  247 PRO A O   
2009 C  CB  . PRO A 246 ? 0.1983 0.2204 0.1993 0.0627  0.0296  0.0306  247 PRO A CB  
2010 C  CG  . PRO A 246 ? 0.2176 0.2673 0.2924 0.0521  0.0642  0.0823  247 PRO A CG  
2011 C  CD  . PRO A 246 ? 0.1390 0.2009 0.2328 0.0329  0.0134  0.0188  247 PRO A CD  
2012 N  N   . ALA A 247 ? 0.1536 0.1958 0.1480 0.0229  0.0271  0.0176  248 ALA A N   
2013 C  CA  . ALA A 247 ? 0.1526 0.1839 0.1274 0.0044  0.0267  0.0034  248 ALA A CA  
2014 C  C   . ALA A 247 ? 0.1472 0.1746 0.1264 0.0278  0.0277  0.0129  248 ALA A C   
2015 O  O   . ALA A 247 ? 0.1797 0.2108 0.1851 0.0469  -0.0156 0.0288  248 ALA A O   
2016 C  CB  . ALA A 247 ? 0.2573 0.1887 0.1309 -0.0073 0.0292  0.0298  248 ALA A CB  
2017 N  N   . GLN A 248 ? 0.1520 0.1587 0.1540 0.0138  -0.0098 -0.0041 249 GLN A N   
2018 C  CA  . GLN A 248 ? 0.1525 0.1876 0.1664 0.0082  -0.0069 0.0250  249 GLN A CA  
2019 C  C   . GLN A 248 ? 0.1721 0.2140 0.1667 0.0184  -0.0225 0.0093  249 GLN A C   
2020 O  O   . GLN A 248 ? 0.1908 0.2224 0.1400 0.0168  0.0049  0.0248  249 GLN A O   
2021 C  CB  . GLN A 248 ? 0.1675 0.1872 0.1498 0.0117  0.0179  0.0060  249 GLN A CB  
2022 C  CG  . GLN A 248 ? 0.1746 0.2077 0.1395 0.0052  0.0062  0.0089  249 GLN A CG  
2023 C  CD  . GLN A 248 ? 0.1574 0.2129 0.1610 -0.0128 -0.0013 0.0111  249 GLN A CD  
2024 O  OE1 . GLN A 248 ? 0.1641 0.2705 0.1919 -0.0185 -0.0006 -0.0084 249 GLN A OE1 
2025 N  NE2 . GLN A 248 ? 0.1745 0.2326 0.1580 0.0117  -0.0118 -0.0024 249 GLN A NE2 
2026 N  N   . PRO A 249 ? 0.1707 0.2698 0.1344 0.0286  -0.0069 -0.0066 250 PRO A N   
2027 C  CA  . PRO A 249 ? 0.2082 0.2723 0.1307 0.0638  -0.0008 -0.0020 250 PRO A CA  
2028 C  C   . PRO A 249 ? 0.2169 0.2397 0.1731 0.0521  -0.0116 -0.0040 250 PRO A C   
2029 O  O   . PRO A 249 ? 0.1917 0.2594 0.1623 0.0493  -0.0164 -0.0044 250 PRO A O   
2030 C  CB  . PRO A 249 ? 0.2149 0.4446 0.2027 0.1275  -0.0564 -0.0477 250 PRO A CB  
2031 C  CG  . PRO A 249 ? 0.2441 0.3784 0.1901 0.0114  -0.0518 -0.0452 250 PRO A CG  
2032 C  CD  . PRO A 249 ? 0.1588 0.3532 0.1980 0.0526  -0.0210 0.0080  250 PRO A CD  
2033 N  N   . LEU A 250 ? 0.2257 0.2366 0.1695 0.0560  0.0024  0.0395  251 LEU A N   
2034 C  CA  . LEU A 250 ? 0.1983 0.2318 0.1444 0.0311  -0.0089 -0.0032 251 LEU A CA  
2035 C  C   . LEU A 250 ? 0.2222 0.2230 0.1159 0.0550  -0.0156 0.0092  251 LEU A C   
2036 O  O   . LEU A 250 ? 0.1919 0.2280 0.1460 0.0333  -0.0184 -0.0027 251 LEU A O   
2037 C  CB  . LEU A 250 ? 0.2780 0.2372 0.1813 0.0153  -0.0111 0.0414  251 LEU A CB  
2038 C  CG  . LEU A 250 ? 0.2370 0.2633 0.1706 -0.0185 0.0273  0.0368  251 LEU A CG  
2039 C  CD1 . LEU A 250 ? 0.2319 0.2972 0.1543 -0.0059 -0.0159 -0.0089 251 LEU A CD1 
2040 C  CD2 . LEU A 250 ? 0.3358 0.2989 0.2242 -0.0498 0.0691  0.0584  251 LEU A CD2 
2041 N  N   . LYS A 251 ? 0.2143 0.2813 0.1447 0.0600  -0.0299 -0.0092 252 LYS A N   
2042 C  CA  . LYS A 251 ? 0.2289 0.3424 0.0928 0.0408  -0.0131 -0.0106 252 LYS A CA  
2043 C  C   . LYS A 251 ? 0.2557 0.3222 0.1297 0.0623  -0.0179 -0.0589 252 LYS A C   
2044 O  O   . LYS A 251 ? 0.3511 0.4978 0.2508 -0.0163 0.0110  -0.0165 252 LYS A O   
2045 C  CB  . LYS A 251 ? 0.2400 0.2936 0.1691 0.0346  0.0079  -0.0428 252 LYS A CB  
2046 C  CG  . LYS A 251 ? 0.2634 0.4073 0.2267 0.0220  0.0555  -0.0710 252 LYS A CG  
2047 C  CD  . LYS A 251 ? 0.2500 0.3796 0.2778 -0.0102 0.0089  -0.0693 252 LYS A CD  
2048 C  CE  . LYS A 251 ? 0.2414 0.3969 0.3855 0.0283  0.0158  -0.0854 252 LYS A CE  
2049 N  NZ  . LYS A 251 ? 0.2273 0.4766 0.4795 0.0085  0.0310  -0.0369 252 LYS A NZ  
2050 N  N   . ASN A 252 ? 0.2134 0.3682 0.1845 0.0798  -0.0333 -0.0798 253 ASN A N   
2051 C  CA  . ASN A 252 ? 0.2733 0.6244 0.2756 0.1165  0.0179  -0.1609 253 ASN A CA  
2052 C  C   . ASN A 252 ? 0.2748 0.6281 0.2043 0.1130  0.0010  -0.1470 253 ASN A C   
2053 O  O   . ASN A 252 ? 0.3750 0.5791 0.1404 0.1011  0.0005  -0.0039 253 ASN A O   
2054 C  CB  . ASN A 252 ? 0.3730 0.7322 0.3432 0.1283  -0.0378 -0.2624 253 ASN A CB  
2055 N  N   . ARG A 253 ? 0.2323 0.3173 0.1111 0.0545  0.0080  0.0184  254 ARG A N   
2056 C  CA  . ARG A 253 ? 0.1788 0.2942 0.1083 0.0151  0.0355  0.0003  254 ARG A CA  
2057 C  C   . ARG A 253 ? 0.2113 0.2658 0.1076 0.0178  0.0285  -0.0144 254 ARG A C   
2058 O  O   . ARG A 253 ? 0.2794 0.2499 0.2201 0.0264  0.0749  0.0414  254 ARG A O   
2059 C  CB  . ARG A 253 ? 0.2481 0.2041 0.1063 0.0041  0.0207  -0.0079 254 ARG A CB  
2060 C  CG  . ARG A 253 ? 0.2396 0.2310 0.0917 -0.0055 0.0018  -0.0174 254 ARG A CG  
2061 C  CD  . ARG A 253 ? 0.2285 0.2231 0.0895 0.0466  -0.0114 -0.0301 254 ARG A CD  
2062 N  NE  . ARG A 253 ? 0.1635 0.1987 0.0906 0.0130  0.0197  -0.0006 254 ARG A NE  
2063 C  CZ  . ARG A 253 ? 0.1456 0.1799 0.0785 -0.0054 -0.0106 -0.0158 254 ARG A CZ  
2064 N  NH1 . ARG A 253 ? 0.1305 0.1869 0.1089 -0.0081 -0.0127 0.0085  254 ARG A NH1 
2065 N  NH2 . ARG A 253 ? 0.1611 0.1702 0.1027 0.0141  0.0051  0.0036  254 ARG A NH2 
2066 N  N   A GLN A 254 ? 0.1919 0.3043 0.1122 0.0205  0.0193  -0.0100 255 GLN A N   
2067 N  N   B GLN A 254 ? 0.1923 0.3342 0.1273 0.0234  0.0226  -0.0172 255 GLN A N   
2068 C  CA  A GLN A 254 ? 0.2281 0.2661 0.0955 -0.0017 0.0048  -0.0033 255 GLN A CA  
2069 C  CA  B GLN A 254 ? 0.2167 0.3456 0.0804 -0.0136 -0.0114 -0.0461 255 GLN A CA  
2070 C  C   A GLN A 254 ? 0.2122 0.1955 0.0761 0.0265  0.0287  -0.0003 255 GLN A C   
2071 C  C   B GLN A 254 ? 0.2605 0.2810 0.0986 -0.0230 -0.0365 -0.0126 255 GLN A C   
2072 O  O   A GLN A 254 ? 0.2068 0.2167 0.1145 0.0186  -0.0115 0.0302  255 GLN A O   
2073 O  O   B GLN A 254 ? 0.3007 0.2992 0.2488 0.0431  -0.0542 -0.0583 255 GLN A O   
2074 C  CB  A GLN A 254 ? 0.2723 0.3114 0.1338 0.0325  0.0363  -0.0142 255 GLN A CB  
2075 C  CB  B GLN A 254 ? 0.2393 0.4008 0.1284 0.0206  0.0219  -0.0727 255 GLN A CB  
2076 C  CG  A GLN A 254 ? 0.3714 0.4625 0.1338 0.0581  0.0155  0.0188  255 GLN A CG  
2077 C  CG  B GLN A 254 ? 0.2323 0.5100 0.1137 -0.0094 0.0242  -0.1420 255 GLN A CG  
2078 N  N   . ILE A 255 ? 0.1483 0.2429 0.1286 -0.0152 0.0171  0.0006  256 ILE A N   
2079 C  CA  . ILE A 255 ? 0.1597 0.2385 0.1328 0.0162  0.0060  0.0135  256 ILE A CA  
2080 C  C   . ILE A 255 ? 0.1693 0.2241 0.1197 -0.0025 0.0071  0.0374  256 ILE A C   
2081 O  O   . ILE A 255 ? 0.1908 0.2345 0.1412 0.0110  0.0100  0.0549  256 ILE A O   
2082 C  CB  . ILE A 255 ? 0.1707 0.2282 0.1373 0.0217  0.0172  0.0250  256 ILE A CB  
2083 C  CG1 . ILE A 255 ? 0.1619 0.2759 0.1986 0.0353  0.0153  -0.0047 256 ILE A CG1 
2084 C  CG2 . ILE A 255 ? 0.2127 0.2770 0.1424 0.0019  0.0104  -0.0414 256 ILE A CG2 
2085 C  CD1 . ILE A 255 ? 0.2008 0.2339 0.2486 0.0130  0.0085  0.0041  256 ILE A CD1 
2086 N  N   . LYS A 256 ? 0.1698 0.2320 0.1013 0.0108  0.0075  0.0321  257 LYS A N   
2087 C  CA  . LYS A 256 ? 0.1610 0.2389 0.1162 -0.0095 0.0206  0.0271  257 LYS A CA  
2088 C  C   . LYS A 256 ? 0.1800 0.2354 0.0589 0.0034  0.0312  0.0289  257 LYS A C   
2089 O  O   . LYS A 256 ? 0.2098 0.2806 0.0639 -0.0461 0.0280  0.0245  257 LYS A O   
2090 C  CB  . LYS A 256 ? 0.2352 0.2345 0.1181 0.0164  0.0099  0.0021  257 LYS A CB  
2091 C  CG  . LYS A 256 ? 0.2830 0.2960 0.2588 -0.0272 -0.0059 -0.0750 257 LYS A CG  
2092 C  CD  . LYS A 256 ? 0.4019 0.3398 0.4032 0.0403  -0.0271 0.0055  257 LYS A CD  
2093 N  N   . ALA A 257 ? 0.1578 0.2489 0.1298 0.0068  0.0414  0.0210  258 ALA A N   
2094 C  CA  . ALA A 257 ? 0.1621 0.2170 0.1899 -0.0044 0.0067  0.0282  258 ALA A CA  
2095 C  C   . ALA A 257 ? 0.1907 0.2655 0.0980 0.0148  0.0221  0.0143  258 ALA A C   
2096 O  O   . ALA A 257 ? 0.2045 0.3096 0.1125 -0.0137 0.0552  0.0107  258 ALA A O   
2097 C  CB  . ALA A 257 ? 0.2168 0.2203 0.1969 0.0410  0.0398  0.0585  258 ALA A CB  
2098 N  N   . SER A 258 ? 0.1650 0.2302 0.1141 0.0179  0.0243  0.0266  259 SER A N   
2099 C  CA  . SER A 258 ? 0.1632 0.2809 0.1430 0.0209  0.0108  0.0251  259 SER A CA  
2100 C  C   . SER A 258 ? 0.1600 0.2895 0.1278 0.0141  0.0357  0.0034  259 SER A C   
2101 O  O   . SER A 258 ? 0.1723 0.3901 0.2166 0.0567  0.0641  0.0422  259 SER A O   
2102 C  CB  . SER A 258 ? 0.2082 0.2305 0.1508 0.0075  -0.0133 0.0307  259 SER A CB  
2103 O  OG  . SER A 258 ? 0.1856 0.2570 0.1333 0.0200  0.0584  0.0199  259 SER A OG  
2104 N  N   . PHE A 259 ? 0.1890 0.2927 0.1448 -0.0126 0.0564  0.0272  260 PHE A N   
2105 C  CA  . PHE A 259 ? 0.1872 0.3103 0.2464 -0.0328 0.0222  0.0412  260 PHE A CA  
2106 C  C   . PHE A 259 ? 0.2385 0.4077 0.2309 -0.0328 0.0706  0.1053  260 PHE A C   
2107 O  O   . PHE A 259 ? 0.2474 0.2997 0.2126 -0.0288 0.0442  0.0714  260 PHE A O   
2108 C  CB  . PHE A 259 ? 0.1782 0.2881 0.2805 -0.0266 0.0100  0.0082  260 PHE A CB  
2109 C  CG  . PHE A 259 ? 0.1728 0.2573 0.2388 -0.0089 0.0236  0.0368  260 PHE A CG  
2110 C  CD1 . PHE A 259 ? 0.1557 0.2734 0.2034 -0.0043 0.0150  0.0198  260 PHE A CD1 
2111 C  CD2 . PHE A 259 ? 0.2362 0.2752 0.3290 -0.0168 0.0822  0.0117  260 PHE A CD2 
2112 C  CE1 . PHE A 259 ? 0.1548 0.2651 0.2694 0.0010  0.0248  0.0079  260 PHE A CE1 
2113 C  CE2 . PHE A 259 ? 0.2220 0.2470 0.3776 -0.0136 0.0396  0.0050  260 PHE A CE2 
2114 C  CZ  . PHE A 259 ? 0.2362 0.2582 0.3486 -0.0082 0.0555  -0.0099 260 PHE A CZ  
2115 N  N   . LYS A 260 ? 0.3564 0.4497 0.2796 -0.1207 0.0795  0.1122  261 LYS A N   
2116 C  CA  . LYS A 260 ? 0.5224 0.6957 0.4284 0.0336  0.1450  0.3494  261 LYS A CA  
2117 C  C   . LYS A 260 ? 0.6521 0.9078 0.4859 0.0724  -0.0839 0.4232  261 LYS A C   
2118 O  O   . LYS A 260 ? 0.4713 1.1616 0.7766 -0.0097 0.1410  0.3962  261 LYS A O   
2119 C  CB  . LYS A 260 ? 0.6933 0.7965 0.7288 -0.0122 0.0614  0.0641  261 LYS A CB  
2120 C  CG  . LYS A 260 ? 0.5116 0.5363 0.9049 -0.1022 -0.0330 0.4812  261 LYS A CG  
2121 O  OXT . LYS A 260 ? 0.7731 1.2383 1.1331 0.1960  -0.1427 0.6143  261 LYS A OXT 
2122 ZN ZN  . ZN  B .   ? 0.1147 0.1316 0.0959 0.0054  0.0060  -0.0097 301 ZN  A ZN  
2123 S  S   . DMS C .   ? 0.2878 0.4031 0.3366 0.0068  0.0013  -0.0559 302 DMS A S   
2124 O  O   . DMS C .   ? 0.4284 0.4091 0.3266 0.1261  0.0701  -0.1030 302 DMS A O   
2125 C  C1  . DMS C .   ? 0.2420 0.2881 0.2605 0.0798  -0.0037 -0.0326 302 DMS A C1  
2126 C  C2  . DMS C .   ? 0.4167 0.2432 0.6115 -0.0122 0.0769  -0.0280 302 DMS A C2  
2127 O  O1  . MES D .   ? 0.5008 0.4895 0.2733 0.0230  0.0522  0.0017  303 MES A O1  
2128 C  C2  . MES D .   ? 0.4023 0.3182 0.2195 0.0586  -0.0650 -0.0215 303 MES A C2  
2129 C  C3  . MES D .   ? 0.3385 0.2472 0.3513 0.0905  -0.0120 -0.0103 303 MES A C3  
2130 N  N4  . MES D .   ? 0.5356 0.4875 0.4447 -0.0383 -0.1230 0.0133  303 MES A N4  
2131 C  C5  . MES D .   ? 0.5220 0.4173 0.4489 0.0937  -0.2474 -0.0785 303 MES A C5  
2132 C  C6  . MES D .   ? 0.5865 0.2738 0.5265 0.0233  -0.0641 -0.0265 303 MES A C6  
2133 C  C7  . MES D .   ? 0.5868 0.2417 0.4203 -0.0124 -0.2500 0.0002  303 MES A C7  
2134 C  C8  . MES D .   ? 0.6783 0.4644 0.5317 -0.0289 -0.2819 -0.1725 303 MES A C8  
2135 C  C1  . LML E .   ? 0.2888 0.3758 0.1858 -0.0184 0.0034  0.0769  304 LML A C1  
2136 O  O1  . LML E .   ? 0.2849 0.3316 0.2784 -0.0554 -0.0266 0.0165  304 LML A O1  
2137 O  OXT . LML E .   ? 0.3269 0.3146 0.2447 0.0666  0.0231  0.0102  304 LML A OXT 
2138 C  CA  . LML E .   ? 0.3279 0.3212 0.2611 -0.0710 0.0164  0.0135  304 LML A CA  
2139 C  C   . LML E .   ? 0.5529 0.3826 0.3283 -0.1263 0.1613  0.0295  304 LML A C   
2140 O  O   . LML E .   ? 0.5029 0.4013 0.3661 -0.0634 -0.0254 -0.0341 304 LML A O   
2141 O  O2  . LML E .   ? 0.5112 0.3929 0.5479 -0.1061 -0.0104 0.0400  304 LML A O2  
2142 F  F18 . 3TV F .   ? 0.1752 0.2016 0.1919 -0.0046 0.0251  -0.0130 305 3TV A F18 
2143 C  C7  . 3TV F .   ? 0.1766 0.1790 0.1380 0.0022  -0.0165 -0.0074 305 3TV A C7  
2144 C  C6  . 3TV F .   ? 0.1766 0.1681 0.1217 -0.0100 -0.0198 -0.0131 305 3TV A C6  
2145 F  F17 . 3TV F .   ? 0.1410 0.1678 0.1605 0.0055  0.0160  -0.0142 305 3TV A F17 
2146 C  C8  . 3TV F .   ? 0.2129 0.1717 0.1247 -0.0096 -0.0083 0.0190  305 3TV A C8  
2147 S  S11 . 3TV F .   ? 0.2727 0.1857 0.2001 -0.0291 0.0087  0.0095  305 3TV A S11 
2148 C  C12 . 3TV F .   ? 0.3668 0.2170 0.3883 0.0058  0.0044  -0.0635 305 3TV A C12 
2149 C  C13 . 3TV F .   ? 0.4935 0.2233 0.2778 -0.0167 -0.0502 0.0548  305 3TV A C13 
2150 C  C14 . 3TV F .   ? 0.6060 0.2341 0.4950 -0.0603 0.1194  0.0269  305 3TV A C14 
2151 C  C9  . 3TV F .   ? 0.1897 0.1129 0.1928 -0.0003 -0.0528 -0.0128 305 3TV A C9  
2152 F  F15 . 3TV F .   ? 0.2252 0.1562 0.3607 -0.0020 -0.1007 0.0403  305 3TV A F15 
2153 C  C10 . 3TV F .   ? 0.1575 0.1666 0.2191 -0.0116 -0.0381 -0.0027 305 3TV A C10 
2154 F  F16 . 3TV F .   ? 0.1728 0.1811 0.2997 0.0026  -0.0433 0.0161  305 3TV A F16 
2155 C  C5  . 3TV F .   ? 0.1606 0.1577 0.1071 -0.0189 -0.0227 0.0119  305 3TV A C5  
2156 S  S1  . 3TV F .   ? 0.1333 0.1459 0.1144 0.0042  -0.0049 -0.0126 305 3TV A S1  
2157 O  O3  . 3TV F .   ? 0.1164 0.1617 0.1339 0.0082  0.0124  -0.0150 305 3TV A O3  
2158 O  O4  . 3TV F .   ? 0.1359 0.1516 0.0967 0.0065  -0.0070 -0.0142 305 3TV A O4  
2159 N  N2  . 3TV F .   ? 0.1072 0.1276 0.1122 -0.0273 0.0099  -0.0074 305 3TV A N2  
2160 F  F18 . 3TV G .   ? 0.4021 0.4778 0.5426 0.1415  0.0817  0.1056  306 3TV A F18 
2161 C  C7  . 3TV G .   ? 0.2882 0.4030 0.4875 -0.0039 -0.0089 0.0185  306 3TV A C7  
2162 C  C6  . 3TV G .   ? 0.3001 0.3820 0.4762 0.0208  0.0242  0.1087  306 3TV A C6  
2163 F  F17 . 3TV G .   ? 0.2916 0.3578 0.5366 -0.0043 0.0039  0.1328  306 3TV A F17 
2164 C  C8  . 3TV G .   ? 0.2019 0.4156 0.3794 0.0070  0.0348  -0.0044 306 3TV A C8  
2165 S  S11 . 3TV G .   ? 0.3129 0.5574 0.4357 0.0329  0.0768  -0.1069 306 3TV A S11 
2166 C  C12 . 3TV G .   ? 0.2920 0.5826 0.5647 0.0368  -0.1029 -0.2304 306 3TV A C12 
2167 C  C13 . 3TV G .   ? 0.4613 0.4415 0.6434 0.1395  -0.1211 -0.1331 306 3TV A C13 
2168 C  C14 . 3TV G .   ? 0.3610 0.5022 0.9520 0.0708  -0.2085 -0.2160 306 3TV A C14 
2169 C  C9  . 3TV G .   ? 0.2900 0.4533 0.4684 0.0372  0.0100  0.0722  306 3TV A C9  
2170 F  F15 . 3TV G .   ? 0.2798 0.4324 0.6504 0.0455  0.1005  0.0633  306 3TV A F15 
2171 C  C10 . 3TV G .   ? 0.2935 0.3277 0.4228 0.0881  -0.0172 0.0541  306 3TV A C10 
2172 F  F16 . 3TV G .   ? 0.2913 0.3269 0.4789 -0.0416 -0.0868 0.0990  306 3TV A F16 
2173 C  C5  . 3TV G .   ? 0.2838 0.3657 0.3636 0.0987  0.0108  0.0438  306 3TV A C5  
2174 S  S1  . 3TV G .   ? 0.2820 0.3632 0.4195 0.0055  0.0225  -0.0073 306 3TV A S1  
2175 O  O3  . 3TV G .   ? 0.2755 0.3273 0.3689 -0.0491 -0.0521 0.0594  306 3TV A O3  
2176 O  O4  . 3TV G .   ? 0.2258 0.3523 0.6263 0.0829  -0.1005 -0.0895 306 3TV A O4  
2177 N  N2  . 3TV G .   ? 0.2456 0.3735 0.3309 0.0683  0.0219  0.1055  306 3TV A N2  
2178 O  O   . HOH H .   ? 0.4001 0.2481 0.2906 0.1083  -0.0266 -0.0545 401 HOH A O   
2179 O  O   . HOH H .   ? 0.2730 0.3444 0.2572 0.0164  0.0378  0.0013  402 HOH A O   
2180 O  O   . HOH H .   ? 0.3369 0.2547 0.3546 -0.0245 -0.0790 0.0258  403 HOH A O   
2181 O  O   . HOH H .   ? 0.1802 0.1249 0.1571 -0.0049 -0.0388 -0.0039 404 HOH A O   
2182 O  O   . HOH H .   ? 0.3026 1.1346 0.3147 0.1218  -0.0281 0.0726  405 HOH A O   
2183 O  O   . HOH H .   ? 0.3956 0.3477 0.3714 -0.0206 0.0682  -0.1837 406 HOH A O   
2184 O  O   . HOH H .   ? 0.1822 0.2104 0.1430 0.0146  0.0301  0.0351  407 HOH A O   
2185 O  O   . HOH H .   ? 0.3183 0.4038 0.3409 0.1326  -0.0466 -0.1314 408 HOH A O   
2186 O  O   . HOH H .   ? 0.3683 0.5946 0.4397 -0.1202 0.1512  -0.0063 409 HOH A O   
2187 O  O   . HOH H .   ? 0.4253 0.5292 0.3291 0.1415  0.1559  0.0116  410 HOH A O   
2188 O  O   . HOH H .   ? 0.4595 0.2981 0.5665 -0.0219 0.0960  0.0807  411 HOH A O   
2189 O  O   . HOH H .   ? 0.2278 0.2709 0.2034 0.0601  0.0041  0.0290  412 HOH A O   
2190 O  O   . HOH H .   ? 0.6228 0.3342 0.2605 0.1649  0.1394  0.0730  413 HOH A O   
2191 O  O   . HOH H .   ? 0.6316 0.4277 0.3230 -0.0345 -0.1128 -0.1249 414 HOH A O   
2192 O  O   . HOH H .   ? 0.3611 0.3485 0.2784 -0.0749 -0.0463 -0.0248 415 HOH A O   
2193 O  O   . HOH H .   ? 0.3829 0.3797 0.3302 -0.0127 0.0223  -0.0893 416 HOH A O   
2194 O  O   . HOH H .   ? 0.3898 0.2916 0.2249 -0.0279 0.0420  -0.0190 417 HOH A O   
2195 O  O   . HOH H .   ? 0.3568 0.2827 0.3162 0.0109  -0.0473 -0.0397 418 HOH A O   
2196 O  O   . HOH H .   ? 0.3295 0.2888 0.2605 -0.0606 -0.0220 0.0801  419 HOH A O   
2197 O  O   . HOH H .   ? 0.4192 0.4020 0.2519 -0.0414 0.0286  0.0632  420 HOH A O   
2198 O  O   . HOH H .   ? 0.3044 0.3121 0.2206 0.0414  -0.0229 -0.0559 421 HOH A O   
2199 O  O   . HOH H .   ? 0.1536 0.1886 0.1474 0.0152  0.0130  -0.0201 422 HOH A O   
2200 O  O   . HOH H .   ? 0.2461 0.1698 0.4296 -0.0043 0.0146  0.0179  423 HOH A O   
2201 O  O   . HOH H .   ? 0.2939 0.5251 0.1657 -0.0923 -0.0566 0.0053  424 HOH A O   
2202 O  O   . HOH H .   ? 0.2974 0.3093 0.2378 0.0356  -0.0023 -0.0208 425 HOH A O   
2203 O  O   . HOH H .   ? 0.3219 0.4070 0.6479 -0.0004 0.0269  0.2268  426 HOH A O   
2204 O  O   . HOH H .   ? 0.5776 0.6077 0.2065 -0.0012 0.0491  0.0647  427 HOH A O   
2205 O  O   . HOH H .   ? 0.2296 0.3161 0.3829 0.0186  -0.1176 -0.1061 428 HOH A O   
2206 O  O   . HOH H .   ? 0.1807 0.1800 0.1503 0.0111  0.0048  0.0023  429 HOH A O   
2207 O  O   . HOH H .   ? 0.2913 0.2428 0.3037 0.0048  0.0677  -0.0710 430 HOH A O   
2208 O  O   . HOH H .   ? 0.2503 0.1763 0.3561 0.0068  -0.0552 0.0031  431 HOH A O   
2209 O  O   . HOH H .   ? 0.3804 0.3556 0.3101 0.0168  -0.0210 0.1018  432 HOH A O   
2210 O  O   . HOH H .   ? 0.3444 0.2543 0.2472 -0.0107 -0.0146 0.0016  433 HOH A O   
2211 O  O   . HOH H .   ? 0.3362 0.3478 0.2253 -0.0094 -0.0419 0.0348  434 HOH A O   
2212 O  O   . HOH H .   ? 0.5279 0.3958 0.2287 -0.0399 -0.0560 0.0484  435 HOH A O   
2213 O  O   . HOH H .   ? 0.2397 0.1713 0.1285 -0.0116 0.0092  -0.0182 436 HOH A O   
2214 O  O   . HOH H .   ? 0.2511 0.3007 0.2932 0.0495  -0.1239 -0.0823 437 HOH A O   
2215 O  O   . HOH H .   ? 0.3725 0.5651 0.3392 0.0859  -0.0216 0.0089  438 HOH A O   
2216 O  O   . HOH H .   ? 0.4971 0.4218 0.2888 0.0641  0.1460  -0.0139 439 HOH A O   
2217 O  O   . HOH H .   ? 0.2190 0.2202 0.2260 -0.0152 -0.0162 -0.0031 440 HOH A O   
2218 O  O   . HOH H .   ? 0.6940 0.3778 0.3062 -0.1957 0.1351  -0.0554 441 HOH A O   
2219 O  O   . HOH H .   ? 0.2303 0.4534 0.9104 0.0620  -0.1238 0.0980  442 HOH A O   
2220 O  O   . HOH H .   ? 0.3359 0.2073 0.3557 0.0075  -0.0746 0.0412  443 HOH A O   
2221 O  O   . HOH H .   ? 0.7218 0.2669 0.9108 -0.0639 -0.2034 0.1127  444 HOH A O   
2222 O  O   . HOH H .   ? 0.1958 0.2559 0.2147 0.0553  0.0328  0.0179  445 HOH A O   
2223 O  O   . HOH H .   ? 0.2052 0.2871 0.4705 -0.0679 0.0592  0.1018  446 HOH A O   
2224 O  O   . HOH H .   ? 0.5835 0.5398 0.5152 -0.1551 0.1764  -0.0495 447 HOH A O   
2225 O  O   . HOH H .   ? 0.2282 0.3603 0.2662 -0.0130 -0.0006 -0.0341 448 HOH A O   
2226 O  O   . HOH H .   ? 0.2138 0.7839 0.4784 0.0542  -0.0226 -0.3274 449 HOH A O   
2227 O  O   . HOH H .   ? 0.2276 0.1955 0.1641 0.0121  -0.0268 0.0152  450 HOH A O   
2228 O  O   . HOH H .   ? 0.1657 0.1599 0.2561 0.0134  -0.0201 -0.0707 451 HOH A O   
2229 O  O   . HOH H .   ? 0.2715 0.3229 0.2806 -0.0267 0.0233  -0.0486 452 HOH A O   
2230 O  O   . HOH H .   ? 0.3664 0.2655 0.2037 -0.0486 0.0230  0.0386  453 HOH A O   
2231 O  O   . HOH H .   ? 0.4317 0.3381 0.4544 0.0938  -0.1766 -0.1324 454 HOH A O   
2232 O  O   . HOH H .   ? 0.3413 0.2960 0.2935 0.0116  -0.0197 0.1047  455 HOH A O   
2233 O  O   . HOH H .   ? 0.5345 0.2209 0.3909 -0.0445 0.0903  -0.0681 456 HOH A O   
2234 O  O   . HOH H .   ? 0.3186 0.3571 0.1983 0.0050  0.1100  -0.0684 457 HOH A O   
2235 O  O   . HOH H .   ? 0.3276 0.2932 0.2568 0.0281  0.0719  -0.1173 458 HOH A O   
2236 O  O   . HOH H .   ? 0.2163 0.2957 0.1961 0.0820  0.0105  -0.0092 459 HOH A O   
2237 O  O   . HOH H .   ? 0.2505 0.2245 0.2316 -0.0094 0.0208  0.0063  460 HOH A O   
2238 O  O   . HOH H .   ? 0.3089 0.4354 0.2117 -0.0334 0.0362  -0.0428 461 HOH A O   
2239 O  O   . HOH H .   ? 0.1573 0.1682 0.1710 0.0060  -0.0167 0.0005  462 HOH A O   
2240 O  O   . HOH H .   ? 0.4986 0.2914 0.2289 -0.0591 0.0402  0.0578  463 HOH A O   
2241 O  O   . HOH H .   ? 0.2071 0.2583 0.4325 0.0080  -0.0026 0.0209  464 HOH A O   
2242 O  O   . HOH H .   ? 0.1725 0.2138 0.1571 0.0381  0.0166  0.0259  465 HOH A O   
2243 O  O   . HOH H .   ? 0.1917 0.2411 0.2083 0.0384  -0.0300 0.0384  466 HOH A O   
2244 O  O   . HOH H .   ? 0.2406 0.2931 0.1465 -0.0152 0.0337  -0.0241 467 HOH A O   
2245 O  O   . HOH H .   ? 0.2142 0.1996 0.2465 0.0087  -0.0138 0.0027  468 HOH A O   
2246 O  O   . HOH H .   ? 0.2284 0.3180 0.2906 0.0507  -0.0111 -0.0873 469 HOH A O   
2247 O  O   . HOH H .   ? 0.2669 0.4709 0.3100 -0.0348 0.0423  -0.0061 470 HOH A O   
2248 O  O   . HOH H .   ? 0.4056 0.5966 0.3078 0.1606  0.0200  0.0272  471 HOH A O   
2249 O  O   . HOH H .   ? 0.2831 0.4034 0.2393 -0.0932 0.0736  -0.0276 472 HOH A O   
2250 O  O   . HOH H .   ? 0.5010 0.5450 0.1450 -0.0741 0.0401  -0.0864 473 HOH A O   
2251 O  O   . HOH H .   ? 0.5001 0.4791 0.4849 -0.1903 0.0110  0.0773  474 HOH A O   
2252 O  O   . HOH H .   ? 0.3582 0.3420 0.2195 0.0369  0.0079  -0.0917 475 HOH A O   
2253 O  O   . HOH H .   ? 0.3873 0.3179 0.2705 0.0012  0.0708  0.0873  476 HOH A O   
2254 O  O   . HOH H .   ? 0.4419 0.4375 0.4024 -0.0454 0.1250  0.0125  477 HOH A O   
2255 O  O   . HOH H .   ? 0.3861 0.5256 0.2389 -0.0803 0.0414  -0.1194 478 HOH A O   
2256 O  O   . HOH H .   ? 0.4271 0.3082 0.1950 -0.0721 -0.0279 -0.0401 479 HOH A O   
2257 O  O   . HOH H .   ? 0.4562 0.7756 0.4041 0.2427  -0.0480 0.0196  480 HOH A O   
2258 O  O   . HOH H .   ? 0.3212 0.3104 0.5413 0.1005  0.1529  0.1628  481 HOH A O   
2259 O  O   . HOH H .   ? 0.1987 0.2789 0.1747 -0.0304 0.0363  -0.0769 482 HOH A O   
2260 O  O   . HOH H .   ? 0.1703 0.3301 0.2155 -0.0410 0.0125  0.0079  483 HOH A O   
2261 O  O   . HOH H .   ? 0.3229 0.4318 0.3365 -0.0504 -0.0900 0.0296  484 HOH A O   
2262 O  O   . HOH H .   ? 0.2278 0.3990 0.5049 -0.0016 0.0078  -0.1451 485 HOH A O   
2263 O  O   . HOH H .   ? 0.1797 0.3094 0.1591 0.0351  0.0183  -0.0425 486 HOH A O   
2264 O  O   . HOH H .   ? 0.1536 0.1754 0.1835 0.0052  -0.0002 0.0062  487 HOH A O   
2265 O  O   . HOH H .   ? 0.3531 0.3973 0.4490 -0.0212 -0.1186 0.0256  488 HOH A O   
2266 O  O   . HOH H .   ? 0.4771 0.4293 0.3445 0.0882  0.0727  -0.0512 489 HOH A O   
2267 O  O   . HOH H .   ? 0.2827 0.5811 0.4487 0.0891  0.0072  0.0495  490 HOH A O   
2268 O  O   . HOH H .   ? 0.1458 0.1691 0.1213 0.0073  0.0208  0.0040  491 HOH A O   
2269 O  O   . HOH H .   ? 0.2413 0.2198 0.3552 -0.0275 -0.0665 0.0359  492 HOH A O   
2270 O  O   . HOH H .   ? 0.2924 0.2063 0.3231 0.0003  0.0619  -0.0449 493 HOH A O   
2271 O  O   . HOH H .   ? 0.2588 0.2674 0.1474 -0.0484 -0.0021 0.0009  494 HOH A O   
2272 O  O   . HOH H .   ? 0.2105 0.3204 0.3283 0.0611  -0.0146 0.0391  495 HOH A O   
2273 O  O   . HOH H .   ? 0.1973 0.1849 0.2463 -0.0016 0.0104  -0.0291 496 HOH A O   
2274 O  O   . HOH H .   ? 0.1634 0.2398 0.1932 -0.0214 0.0037  -0.0001 497 HOH A O   
2275 O  O   . HOH H .   ? 0.3406 0.3376 0.5123 0.0290  0.0032  -0.2141 498 HOH A O   
2276 O  O   . HOH H .   ? 0.1614 0.1953 0.1937 0.0093  0.0104  0.0353  499 HOH A O   
2277 O  O   . HOH H .   ? 0.2636 0.2640 0.4469 -0.0352 0.1090  -0.0113 500 HOH A O   
2278 O  O   . HOH H .   ? 0.4099 0.5564 0.3007 0.0610  0.0498  0.0642  501 HOH A O   
2279 O  O   . HOH H .   ? 0.1846 0.1302 0.1875 -0.0068 -0.0176 -0.0018 502 HOH A O   
2280 O  O   . HOH H .   ? 0.3819 0.4374 0.1632 -0.0211 0.0891  -0.0581 503 HOH A O   
2281 O  O   . HOH H .   ? 0.2323 0.3683 0.1706 0.0214  -0.0215 0.0208  504 HOH A O   
2282 O  O   . HOH H .   ? 0.3589 0.4877 0.2709 -0.2537 0.0076  0.0283  505 HOH A O   
2283 O  O   . HOH H .   ? 0.2615 0.2511 0.1887 0.0454  0.0553  0.0502  506 HOH A O   
2284 O  O   . HOH H .   ? 0.6179 0.3129 0.1890 0.0912  -0.0451 0.0961  507 HOH A O   
2285 O  O   . HOH H .   ? 0.2023 0.2805 0.1793 -0.0071 -0.0058 0.0326  508 HOH A O   
2286 O  O   . HOH H .   ? 0.3970 0.3187 0.2873 0.0230  0.0270  -0.0973 509 HOH A O   
2287 O  O   . HOH H .   ? 0.5456 0.5730 0.4404 0.1306  0.1271  -0.0901 510 HOH A O   
2288 O  O   . HOH H .   ? 0.2737 0.2809 0.2647 -0.0097 0.0267  0.0144  511 HOH A O   
2289 O  O   . HOH H .   ? 0.4067 0.5654 0.4767 0.1254  -0.0589 -0.2241 512 HOH A O   
2290 O  O   . HOH H .   ? 0.3079 0.4264 0.3995 0.0531  0.0227  0.0387  513 HOH A O   
2291 O  O   . HOH H .   ? 0.1987 0.1624 0.1320 0.0283  -0.0110 0.0067  514 HOH A O   
2292 O  O   . HOH H .   ? 0.1558 0.1833 0.1858 0.0065  0.0036  -0.0308 515 HOH A O   
2293 O  O   . HOH H .   ? 0.4372 0.3861 0.2353 0.0561  0.0386  0.0242  516 HOH A O   
2294 O  O   . HOH H .   ? 0.1377 0.2659 0.2112 0.0212  0.0144  -0.0325 517 HOH A O   
2295 O  O   . HOH H .   ? 0.4093 0.3726 0.3074 0.0388  -0.0758 -0.0652 518 HOH A O   
2296 O  O   . HOH H .   ? 0.3401 0.3395 0.5131 -0.0723 0.0670  -0.0128 519 HOH A O   
2297 O  O   . HOH H .   ? 0.5013 0.2235 0.3730 0.0898  -0.1309 -0.1002 520 HOH A O   
2298 O  O   . HOH H .   ? 0.3758 0.2204 0.3233 0.0744  -0.0565 0.0156  521 HOH A O   
2299 O  O   . HOH H .   ? 0.3863 0.3313 0.4082 0.1005  0.1347  0.0533  522 HOH A O   
2300 O  O   . HOH H .   ? 0.2303 0.2429 0.1821 0.0282  0.0550  0.0333  523 HOH A O   
2301 O  O   . HOH H .   ? 0.5854 0.2425 0.3722 0.0353  0.1526  0.0706  524 HOH A O   
2302 O  O   . HOH H .   ? 0.2048 0.3380 0.2828 0.0017  -0.0048 0.0375  525 HOH A O   
2303 O  O   . HOH H .   ? 0.3028 0.3057 0.3060 0.0414  0.0517  0.0220  526 HOH A O   
2304 O  O   . HOH H .   ? 0.3985 0.4116 0.2137 -0.0325 0.0859  -0.0760 527 HOH A O   
2305 O  O   . HOH H .   ? 0.4331 0.3244 0.5679 -0.0244 0.0659  0.1931  528 HOH A O   
2306 O  O   . HOH H .   ? 0.4281 0.3542 0.2601 0.0066  0.0237  0.0822  529 HOH A O   
2307 O  O   . HOH H .   ? 0.2368 0.2418 0.1702 0.0499  0.0187  0.0139  530 HOH A O   
2308 O  O   . HOH H .   ? 0.3312 0.3416 0.2208 0.0403  0.0401  0.0355  531 HOH A O   
2309 O  O   . HOH H .   ? 0.3919 0.4307 0.3535 0.0178  0.0011  0.2092  532 HOH A O   
2310 O  O   . HOH H .   ? 0.3295 0.4503 0.4785 0.0781  0.0844  0.0829  533 HOH A O   
2311 O  O   . HOH H .   ? 0.6473 0.3398 0.5539 0.1265  -0.0436 -0.0270 534 HOH A O   
2312 O  O   . HOH H .   ? 0.4446 0.2523 0.5393 -0.0091 -0.1877 -0.0501 535 HOH A O   
2313 O  O   . HOH H .   ? 0.3040 0.3154 0.3507 0.1294  -0.0647 -0.0788 536 HOH A O   
2314 O  O   . HOH H .   ? 0.2770 0.4824 0.2787 -0.0829 -0.0823 0.0653  537 HOH A O   
2315 O  O   . HOH H .   ? 0.2587 0.4823 0.7228 -0.1208 -0.1116 0.0460  538 HOH A O   
2316 O  O   . HOH H .   ? 0.3125 0.6012 0.1736 -0.0284 0.0260  -0.0615 539 HOH A O   
2317 O  O   . HOH H .   ? 0.3025 0.2364 0.2788 -0.0497 -0.0422 -0.0728 540 HOH A O   
2318 O  O   . HOH H .   ? 0.3595 0.2637 0.3466 0.0429  -0.1256 0.0218  541 HOH A O   
2319 O  O   . HOH H .   ? 0.2910 0.3450 0.3908 0.0741  0.0138  -0.1298 542 HOH A O   
2320 O  O   . HOH H .   ? 0.2479 0.3313 0.4551 -0.1304 0.0823  -0.1958 543 HOH A O   
2321 O  O   . HOH H .   ? 0.2076 0.3154 0.2509 0.0183  0.0305  0.0209  544 HOH A O   
2322 O  O   . HOH H .   ? 0.2989 0.4307 0.3825 -0.0314 0.0740  0.0817  545 HOH A O   
2323 O  O   . HOH H .   ? 0.3186 0.2817 0.3315 0.0109  0.0759  0.1267  546 HOH A O   
2324 O  O   . HOH H .   ? 0.2475 0.2892 0.3380 0.0885  -0.0370 0.0533  547 HOH A O   
2325 O  O   . HOH H .   ? 0.3055 0.4383 0.8036 -0.0183 0.2196  -0.0560 548 HOH A O   
2326 O  O   . HOH H .   ? 0.2224 0.3104 0.2593 0.0328  0.0729  0.0175  549 HOH A O   
2327 O  O   . HOH H .   ? 0.5991 0.4289 0.6512 -0.0609 0.0512  -0.2612 550 HOH A O   
2328 O  O   . HOH H .   ? 0.3212 0.3292 0.2803 0.0628  0.0053  0.1191  551 HOH A O   
2329 O  O   . HOH H .   ? 0.3883 0.4243 0.2802 0.0469  0.1188  -0.0929 552 HOH A O   
2330 O  O   . HOH H .   ? 0.6093 0.4286 0.4131 0.0722  0.0336  0.1708  553 HOH A O   
2331 O  O   . HOH H .   ? 0.2629 0.2924 0.2702 0.0160  0.0989  0.1081  554 HOH A O   
2332 O  O   . HOH H .   ? 0.3258 0.6718 0.2398 0.1713  -0.1479 -0.1472 555 HOH A O   
2333 O  O   . HOH H .   ? 0.2995 0.5757 0.3349 -0.0008 -0.0340 0.0194  556 HOH A O   
2334 O  O   . HOH H .   ? 0.2364 0.3035 0.3899 0.0389  -0.0268 -0.0561 557 HOH A O   
2335 O  O   . HOH H .   ? 0.5210 0.4368 0.6673 -0.0446 0.3128  -0.2145 558 HOH A O   
2336 O  O   . HOH H .   ? 0.3690 0.1547 0.3330 0.0201  -0.0479 -0.0019 559 HOH A O   
2337 O  O   . HOH H .   ? 0.1923 0.1706 0.1718 0.0102  0.0030  0.0272  560 HOH A O   
2338 O  O   . HOH H .   ? 0.5314 0.5123 0.3811 0.2106  -0.0085 -0.1094 561 HOH A O   
2339 O  O   . HOH H .   ? 0.1858 0.3355 0.1521 0.0207  -0.0329 0.0277  562 HOH A O   
2340 O  O   . HOH H .   ? 0.8725 0.4296 0.4641 0.2485  0.1599  0.2144  563 HOH A O   
2341 O  O   . HOH H .   ? 0.1822 0.3042 0.2841 0.0192  -0.0122 0.0011  564 HOH A O   
2342 O  O   . HOH H .   ? 0.3664 0.2914 0.3729 0.0662  -0.0113 -0.0528 565 HOH A O   
2343 O  O   . HOH H .   ? 0.5054 0.5297 0.5344 -0.2828 -0.0118 0.0695  566 HOH A O   
2344 O  O   . HOH H .   ? 0.2528 0.4268 0.2040 0.0068  0.1148  0.1054  567 HOH A O   
2345 O  O   . HOH H .   ? 0.4250 0.3758 0.3794 0.0705  0.0494  -0.0388 568 HOH A O   
2346 O  O   . HOH H .   ? 0.4300 0.2661 0.3367 0.0288  0.0594  0.0442  569 HOH A O   
2347 O  O   . HOH H .   ? 0.2850 0.2590 0.3129 -0.0419 0.1174  -0.0425 570 HOH A O   
2348 O  O   . HOH H .   ? 0.3899 0.3818 0.3502 -0.1150 -0.1139 -0.0241 571 HOH A O   
2349 O  O   . HOH H .   ? 0.4485 0.4049 0.5400 0.2334  0.2156  0.1016  572 HOH A O   
2350 O  O   . HOH H .   ? 0.4997 0.2367 0.4910 -0.0502 0.0661  -0.0603 573 HOH A O   
2351 O  O   . HOH H .   ? 0.4376 0.6230 0.2018 0.2306  0.0387  0.0329  574 HOH A O   
2352 O  O   . HOH H .   ? 0.2477 0.2608 0.2093 0.0532  0.0387  0.0257  575 HOH A O   
2353 O  O   . HOH H .   ? 0.4325 0.4685 0.3191 -0.0003 0.1164  0.1533  576 HOH A O   
2354 O  O   . HOH H .   ? 0.4117 0.3076 0.3251 0.0551  0.0357  -0.0637 577 HOH A O   
2355 O  O   . HOH H .   ? 0.4764 0.6120 0.3525 0.0597  -0.0405 -0.0528 578 HOH A O   
2356 O  O   . HOH H .   ? 0.2859 0.3502 0.2152 0.0268  -0.0218 -0.0497 579 HOH A O   
2357 O  O   . HOH H .   ? 0.4537 0.7291 0.4235 -0.0655 -0.0413 -0.1500 580 HOH A O   
2358 O  O   . HOH H .   ? 0.3380 0.6467 0.3455 -0.0734 -0.0047 0.0082  581 HOH A O   
2359 O  O   . HOH H .   ? 0.2627 0.2605 0.2512 0.0190  -0.0044 -0.0150 582 HOH A O   
2360 O  O   . HOH H .   ? 0.5870 0.4325 0.2212 0.1107  -0.1180 -0.0102 583 HOH A O   
2361 O  O   . HOH H .   ? 0.1745 0.2278 0.2569 0.0075  0.0234  0.0089  584 HOH A O   
2362 O  O   . HOH H .   ? 0.4020 0.3474 0.5074 0.0693  0.1449  -0.0052 585 HOH A O   
2363 O  O   . HOH H .   ? 0.3732 0.3288 0.6224 0.0757  0.1280  0.0342  586 HOH A O   
2364 O  O   . HOH H .   ? 0.3676 0.3638 0.4002 -0.0655 -0.0364 0.0960  587 HOH A O   
2365 O  O   . HOH H .   ? 0.5299 0.3536 0.2717 0.1246  -0.0182 0.0573  588 HOH A O   
2366 O  O   . HOH H .   ? 0.5177 0.4019 0.5735 0.0776  0.0302  -0.0873 589 HOH A O   
2367 O  O   . HOH H .   ? 0.3075 0.2849 0.5181 0.1008  0.0080  0.0361  590 HOH A O   
2368 O  O   . HOH H .   ? 0.4985 0.4009 0.4014 -0.1556 0.1417  -0.0284 591 HOH A O   
2369 O  O   . HOH H .   ? 0.4590 0.3398 0.6396 -0.0688 -0.1070 -0.0659 592 HOH A O   
2370 O  O   . HOH H .   ? 0.4741 0.3769 0.3420 0.0761  0.1190  -0.1165 593 HOH A O   
2371 O  O   . HOH H .   ? 0.4582 0.3880 0.5493 -0.0129 -0.0066 -0.1159 594 HOH A O   
2372 O  O   . HOH H .   ? 0.3147 0.3991 0.3212 -0.0125 -0.0466 -0.0307 595 HOH A O   
2373 O  O   . HOH H .   ? 0.4370 0.3435 0.8019 -0.1778 0.2549  -0.1162 596 HOH A O   
2374 O  O   . HOH H .   ? 0.3183 0.3617 0.7744 0.0926  0.1001  -0.0110 597 HOH A O   
2375 O  O   . HOH H .   ? 0.3615 0.4643 0.6979 -0.1071 -0.0671 0.1326  598 HOH A O   
2376 O  O   . HOH H .   ? 0.4977 0.5357 0.4446 0.1841  0.1177  0.1726  599 HOH A O   
2377 O  O   . HOH H .   ? 0.2864 0.6039 0.5265 -0.0355 -0.0264 -0.1335 600 HOH A O   
2378 O  O   . HOH H .   ? 0.2787 0.6125 0.8846 0.0106  -0.0856 0.1207  601 HOH A O   
2379 O  O   . HOH H .   ? 0.3039 0.4824 0.6558 -0.0099 0.0569  0.1588  602 HOH A O   
2380 O  O   . HOH H .   ? 0.3899 0.3435 0.6019 0.1091  -0.1184 -0.1632 603 HOH A O   
2381 O  O   . HOH H .   ? 0.6007 0.4388 0.3459 -0.1288 0.0287  -0.0952 604 HOH A O   
2382 O  O   . HOH H .   ? 0.2373 0.2609 0.2990 -0.0240 -0.0215 -0.0273 605 HOH A O   
2383 O  O   . HOH H .   ? 0.5105 0.3419 0.3836 -0.0924 -0.1365 0.0974  606 HOH A O   
2384 O  O   . HOH H .   ? 0.5317 0.3570 0.3385 0.0188  -0.0337 -0.0567 607 HOH A O   
2385 O  O   . HOH H .   ? 0.3042 0.5737 0.4031 0.0425  -0.0670 -0.0656 608 HOH A O   
2386 O  O   . HOH H .   ? 0.5066 0.4803 0.5570 -0.1649 0.0223  0.0619  609 HOH A O   
2387 O  O   . HOH H .   ? 0.5370 0.7802 0.4153 0.0747  -0.2294 -0.0228 610 HOH A O   
2388 O  O   . HOH H .   ? 0.4469 0.7122 0.2057 0.2218  0.0321  0.0616  611 HOH A O   
2389 O  O   . HOH H .   ? 0.5127 0.3733 0.2533 -0.1136 0.0911  0.0272  612 HOH A O   
2390 O  O   . HOH H .   ? 0.5736 0.2970 0.8510 0.0151  0.1746  -0.0066 613 HOH A O   
2391 O  O   . HOH H .   ? 0.2911 0.5137 0.5832 0.0439  -0.0688 -0.0033 614 HOH A O   
2392 O  O   . HOH H .   ? 0.4252 0.5851 0.5230 -0.0361 -0.0022 0.1829  615 HOH A O   
2393 O  O   . HOH H .   ? 0.6294 0.2530 0.4309 -0.0648 0.1107  -0.0770 616 HOH A O   
2394 O  O   . HOH H .   ? 0.5575 0.4408 0.2764 -0.2922 -0.0917 0.0227  617 HOH A O   
2395 O  O   . HOH H .   ? 0.6879 0.3143 0.3567 -0.0888 -0.0184 0.1135  618 HOH A O   
2396 O  O   . HOH H .   ? 0.4223 0.3736 0.2587 -0.0155 -0.0729 0.0665  619 HOH A O   
2397 O  O   . HOH H .   ? 0.4713 0.3895 0.4508 0.1168  0.1018  0.0803  620 HOH A O   
2398 O  O   . HOH H .   ? 0.3226 0.3243 0.4936 0.1030  -0.1067 0.0476  621 HOH A O   
2399 O  O   . HOH H .   ? 0.5671 0.2659 0.8634 0.1161  0.1465  -0.0455 622 HOH A O   
2400 O  O   . HOH H .   ? 0.2956 0.2741 0.3714 0.0566  -0.0704 -0.0088 623 HOH A O   
2401 O  O   . HOH H .   ? 0.2475 0.2963 0.2500 -0.0203 -0.0488 0.0186  624 HOH A O   
2402 O  O   . HOH H .   ? 0.4692 0.6393 0.6927 -0.0872 0.0749  -0.3307 625 HOH A O   
2403 O  O   . HOH H .   ? 0.4340 0.2484 0.5648 -0.0390 0.0116  -0.0423 626 HOH A O   
2404 O  O   . HOH H .   ? 0.3385 0.3948 0.2541 0.0100  0.1181  -0.0351 627 HOH A O   
2405 O  O   . HOH H .   ? 0.2564 0.3743 0.7638 -0.0886 0.1438  -0.1668 628 HOH A O   
2406 O  O   . HOH H .   ? 0.2831 0.7589 0.4900 0.0457  0.0251  -0.0838 629 HOH A O   
2407 O  O   . HOH H .   ? 0.2784 0.3492 0.3908 0.0889  -0.0364 -0.0703 630 HOH A O   
2408 O  O   . HOH H .   ? 0.4587 0.5259 0.4433 0.1756  -0.0140 0.0148  631 HOH A O   
2409 O  O   . HOH H .   ? 0.2602 0.5321 0.3075 0.0550  0.0538  -0.1105 632 HOH A O   
2410 O  O   . HOH H .   ? 0.5036 0.8695 0.2458 0.2633  0.0461  -0.0805 633 HOH A O   
2411 O  O   . HOH H .   ? 0.6246 0.3315 0.3098 -0.0172 -0.0366 -0.0498 634 HOH A O   
2412 O  O   . HOH H .   ? 0.2350 0.4273 0.2425 0.0345  0.0107  0.0210  635 HOH A O   
2413 O  O   . HOH H .   ? 0.5328 0.6271 0.3394 0.1877  0.0809  0.0067  636 HOH A O   
2414 O  O   . HOH H .   ? 0.4771 0.4386 0.3352 -0.1687 -0.1004 0.0172  637 HOH A O   
2415 O  O   . HOH H .   ? 0.2958 0.3595 0.6707 0.0476  0.0283  0.0531  638 HOH A O   
2416 O  O   . HOH H .   ? 0.3334 0.3729 0.6141 -0.0265 0.1060  -0.1525 639 HOH A O   
2417 O  O   . HOH H .   ? 0.6272 0.5753 0.5809 0.2177  -0.0025 -0.0493 640 HOH A O   
2418 O  O   . HOH H .   ? 0.4411 0.3938 0.5026 0.0132  -0.0079 0.0233  641 HOH A O   
2419 O  O   . HOH H .   ? 0.5074 0.3380 0.4460 0.0178  0.0965  0.1020  642 HOH A O   
2420 O  O   . HOH H .   ? 0.2629 0.6092 0.6527 -0.0933 -0.1237 -0.0559 643 HOH A O   
2421 O  O   . HOH H .   ? 0.5064 0.5610 0.6009 -0.0068 0.2186  -0.2529 644 HOH A O   
2422 O  O   . HOH H .   ? 0.3766 0.4048 0.3783 0.0458  0.0357  -0.1258 645 HOH A O   
2423 O  O   . HOH H .   ? 0.3021 0.3794 0.5571 0.0593  0.1560  -0.0792 646 HOH A O   
2424 O  O   . HOH H .   ? 0.3184 0.3542 0.8071 0.1329  0.0154  0.1027  647 HOH A O   
2425 O  O   . HOH H .   ? 0.6894 0.5820 0.3995 0.0344  -0.1333 -0.2797 648 HOH A O   
2426 O  O   . HOH H .   ? 0.4120 0.4625 0.6694 0.1102  -0.0285 0.0609  649 HOH A O   
2427 O  O   . HOH H .   ? 0.3424 0.7750 0.2751 0.0273  0.0407  0.0183  650 HOH A O   
2428 O  O   . HOH H .   ? 0.3310 0.2649 0.7235 0.0424  0.0678  0.0949  651 HOH A O   
2429 O  O   . HOH H .   ? 0.2169 0.4659 0.6140 -0.0670 -0.0971 0.0855  652 HOH A O   
2430 O  O   . HOH H .   ? 0.3037 0.4497 0.3140 0.0553  0.0453  -0.0403 653 HOH A O   
2431 O  O   . HOH H .   ? 0.4480 0.3219 0.6302 -0.0541 0.1349  -0.1705 654 HOH A O   
2432 O  O   . HOH H .   ? 0.6302 0.2911 0.8498 -0.1750 -0.2691 0.0811  655 HOH A O   
# 
