data_6YH5
# 
_entry.id   6YH5 
# 
_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   6YH5         pdb_00006yh5 10.2210/pdb6yh5/pdb 
WWPDB D_1292106555 ?            ?                   
# 
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                        6YH5 
_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 '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' 343.809   1   ?       ? ? ? 
4 non-polymer syn 'BENZOIC ACID'                                                  122.121   1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                            78.133    1   ?       ? ? ? 
6 water       nat water                                                           18.015    334 ?       ? ? ? 
# 
_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 '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' E1F 
4 'BENZOIC ACID'                                                  BEZ 
5 'DIMETHYL SULFOXIDE'                                            DMS 
6 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 
ALA 'L-peptide linking' y ALANINE                                                         ? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                                                        ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                      ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                 ? 'C4 H7 N O4'          133.103 
BEZ non-polymer         . 'BENZOIC ACID'                                                  ? 'C7 H6 O2'            122.121 
CYS 'L-peptide linking' y CYSTEINE                                                        ? 'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                            ? 'C2 H6 O S'           78.133  
E1F non-polymer         . '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' ? 'C12 H10 Cl N3 O3 S2' 343.809 
GLN 'L-peptide linking' y GLUTAMINE                                                       ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                 ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                         ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                       ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                           ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                      ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                         ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                          ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                      ? 'C5 H11 N O2 S'       149.211 
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   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  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 E1F 1   302 1   E1F E18 A . 
D 4 BEZ 1   303 1   BEZ BEZ A . 
E 5 DMS 1   304 2   DMS DMS A . 
F 6 HOH 1   401 161 HOH HOH A . 
F 6 HOH 2   402 220 HOH HOH A . 
F 6 HOH 3   403 340 HOH HOH A . 
F 6 HOH 4   404 136 HOH HOH A . 
F 6 HOH 5   405 122 HOH HOH A . 
F 6 HOH 6   406 79  HOH HOH A . 
F 6 HOH 7   407 274 HOH HOH A . 
F 6 HOH 8   408 53  HOH HOH A . 
F 6 HOH 9   409 20  HOH HOH A . 
F 6 HOH 10  410 153 HOH HOH A . 
F 6 HOH 11  411 279 HOH HOH A . 
F 6 HOH 12  412 38  HOH HOH A . 
F 6 HOH 13  413 143 HOH HOH A . 
F 6 HOH 14  414 168 HOH HOH A . 
F 6 HOH 15  415 130 HOH HOH A . 
F 6 HOH 16  416 209 HOH HOH A . 
F 6 HOH 17  417 25  HOH HOH A . 
F 6 HOH 18  418 252 HOH HOH A . 
F 6 HOH 19  419 241 HOH HOH A . 
F 6 HOH 20  420 233 HOH HOH A . 
F 6 HOH 21  421 169 HOH HOH A . 
F 6 HOH 22  422 246 HOH HOH A . 
F 6 HOH 23  423 163 HOH HOH A . 
F 6 HOH 24  424 164 HOH HOH A . 
F 6 HOH 25  425 105 HOH HOH A . 
F 6 HOH 26  426 144 HOH HOH A . 
F 6 HOH 27  427 14  HOH HOH A . 
F 6 HOH 28  428 322 HOH HOH A . 
F 6 HOH 29  429 267 HOH HOH A . 
F 6 HOH 30  430 306 HOH HOH A . 
F 6 HOH 31  431 226 HOH HOH A . 
F 6 HOH 32  432 59  HOH HOH A . 
F 6 HOH 33  433 56  HOH HOH A . 
F 6 HOH 34  434 36  HOH HOH A . 
F 6 HOH 35  435 227 HOH HOH A . 
F 6 HOH 36  436 75  HOH HOH A . 
F 6 HOH 37  437 296 HOH HOH A . 
F 6 HOH 38  438 307 HOH HOH A . 
F 6 HOH 39  439 133 HOH HOH A . 
F 6 HOH 40  440 188 HOH HOH A . 
F 6 HOH 41  441 134 HOH HOH A . 
F 6 HOH 42  442 240 HOH HOH A . 
F 6 HOH 43  443 176 HOH HOH A . 
F 6 HOH 44  444 152 HOH HOH A . 
F 6 HOH 45  445 127 HOH HOH A . 
F 6 HOH 46  446 89  HOH HOH A . 
F 6 HOH 47  447 251 HOH HOH A . 
F 6 HOH 48  448 11  HOH HOH A . 
F 6 HOH 49  449 16  HOH HOH A . 
F 6 HOH 50  450 191 HOH HOH A . 
F 6 HOH 51  451 273 HOH HOH A . 
F 6 HOH 52  452 115 HOH HOH A . 
F 6 HOH 53  453 293 HOH HOH A . 
F 6 HOH 54  454 330 HOH HOH A . 
F 6 HOH 55  455 107 HOH HOH A . 
F 6 HOH 56  456 50  HOH HOH A . 
F 6 HOH 57  457 271 HOH HOH A . 
F 6 HOH 58  458 303 HOH HOH A . 
F 6 HOH 59  459 113 HOH HOH A . 
F 6 HOH 60  460 142 HOH HOH A . 
F 6 HOH 61  461 8   HOH HOH A . 
F 6 HOH 62  462 309 HOH HOH A . 
F 6 HOH 63  463 123 HOH HOH A . 
F 6 HOH 64  464 63  HOH HOH A . 
F 6 HOH 65  465 24  HOH HOH A . 
F 6 HOH 66  466 27  HOH HOH A . 
F 6 HOH 67  467 190 HOH HOH A . 
F 6 HOH 68  468 250 HOH HOH A . 
F 6 HOH 69  469 201 HOH HOH A . 
F 6 HOH 70  470 31  HOH HOH A . 
F 6 HOH 71  471 114 HOH HOH A . 
F 6 HOH 72  472 77  HOH HOH A . 
F 6 HOH 73  473 253 HOH HOH A . 
F 6 HOH 74  474 189 HOH HOH A . 
F 6 HOH 75  475 338 HOH HOH A . 
F 6 HOH 76  476 71  HOH HOH A . 
F 6 HOH 77  477 119 HOH HOH A . 
F 6 HOH 78  478 160 HOH HOH A . 
F 6 HOH 79  479 156 HOH HOH A . 
F 6 HOH 80  480 51  HOH HOH A . 
F 6 HOH 81  481 35  HOH HOH A . 
F 6 HOH 82  482 132 HOH HOH A . 
F 6 HOH 83  483 85  HOH HOH A . 
F 6 HOH 84  484 7   HOH HOH A . 
F 6 HOH 85  485 325 HOH HOH A . 
F 6 HOH 86  486 276 HOH HOH A . 
F 6 HOH 87  487 6   HOH HOH A . 
F 6 HOH 88  488 177 HOH HOH A . 
F 6 HOH 89  489 82  HOH HOH A . 
F 6 HOH 90  490 117 HOH HOH A . 
F 6 HOH 91  491 13  HOH HOH A . 
F 6 HOH 92  492 181 HOH HOH A . 
F 6 HOH 93  493 32  HOH HOH A . 
F 6 HOH 94  494 194 HOH HOH A . 
F 6 HOH 95  495 235 HOH HOH A . 
F 6 HOH 96  496 96  HOH HOH A . 
F 6 HOH 97  497 49  HOH HOH A . 
F 6 HOH 98  498 242 HOH HOH A . 
F 6 HOH 99  499 155 HOH HOH A . 
F 6 HOH 100 500 69  HOH HOH A . 
F 6 HOH 101 501 245 HOH HOH A . 
F 6 HOH 102 502 106 HOH HOH A . 
F 6 HOH 103 503 179 HOH HOH A . 
F 6 HOH 104 504 58  HOH HOH A . 
F 6 HOH 105 505 3   HOH HOH A . 
F 6 HOH 106 506 9   HOH HOH A . 
F 6 HOH 107 507 18  HOH HOH A . 
F 6 HOH 108 508 2   HOH HOH A . 
F 6 HOH 109 509 46  HOH HOH A . 
F 6 HOH 110 510 213 HOH HOH A . 
F 6 HOH 111 511 98  HOH HOH A . 
F 6 HOH 112 512 10  HOH HOH A . 
F 6 HOH 113 513 90  HOH HOH A . 
F 6 HOH 114 514 1   HOH HOH A . 
F 6 HOH 115 515 55  HOH HOH A . 
F 6 HOH 116 516 33  HOH HOH A . 
F 6 HOH 117 517 183 HOH HOH A . 
F 6 HOH 118 518 182 HOH HOH A . 
F 6 HOH 119 519 67  HOH HOH A . 
F 6 HOH 120 520 215 HOH HOH A . 
F 6 HOH 121 521 185 HOH HOH A . 
F 6 HOH 122 522 57  HOH HOH A . 
F 6 HOH 123 523 310 HOH HOH A . 
F 6 HOH 124 524 30  HOH HOH A . 
F 6 HOH 125 525 4   HOH HOH A . 
F 6 HOH 126 526 205 HOH HOH A . 
F 6 HOH 127 527 280 HOH HOH A . 
F 6 HOH 128 528 187 HOH HOH A . 
F 6 HOH 129 529 261 HOH HOH A . 
F 6 HOH 130 530 12  HOH HOH A . 
F 6 HOH 131 531 81  HOH HOH A . 
F 6 HOH 132 532 74  HOH HOH A . 
F 6 HOH 133 533 192 HOH HOH A . 
F 6 HOH 134 534 15  HOH HOH A . 
F 6 HOH 135 535 195 HOH HOH A . 
F 6 HOH 136 536 88  HOH HOH A . 
F 6 HOH 137 537 29  HOH HOH A . 
F 6 HOH 138 538 339 HOH HOH A . 
F 6 HOH 139 539 180 HOH HOH A . 
F 6 HOH 140 540 5   HOH HOH A . 
F 6 HOH 141 541 299 HOH HOH A . 
F 6 HOH 142 542 224 HOH HOH A . 
F 6 HOH 143 543 332 HOH HOH A . 
F 6 HOH 144 544 43  HOH HOH A . 
F 6 HOH 145 545 19  HOH HOH A . 
F 6 HOH 146 546 76  HOH HOH A . 
F 6 HOH 147 547 222 HOH HOH A . 
F 6 HOH 148 548 128 HOH HOH A . 
F 6 HOH 149 549 193 HOH HOH A . 
F 6 HOH 150 550 28  HOH HOH A . 
F 6 HOH 151 551 131 HOH HOH A . 
F 6 HOH 152 552 288 HOH HOH A . 
F 6 HOH 153 553 22  HOH HOH A . 
F 6 HOH 154 554 52  HOH HOH A . 
F 6 HOH 155 555 313 HOH HOH A . 
F 6 HOH 156 556 45  HOH HOH A . 
F 6 HOH 157 557 228 HOH HOH A . 
F 6 HOH 158 558 300 HOH HOH A . 
F 6 HOH 159 559 66  HOH HOH A . 
F 6 HOH 160 560 17  HOH HOH A . 
F 6 HOH 161 561 104 HOH HOH A . 
F 6 HOH 162 562 68  HOH HOH A . 
F 6 HOH 163 563 264 HOH HOH A . 
F 6 HOH 164 564 166 HOH HOH A . 
F 6 HOH 165 565 64  HOH HOH A . 
F 6 HOH 166 566 328 HOH HOH A . 
F 6 HOH 167 567 21  HOH HOH A . 
F 6 HOH 168 568 93  HOH HOH A . 
F 6 HOH 169 569 258 HOH HOH A . 
F 6 HOH 170 570 60  HOH HOH A . 
F 6 HOH 171 571 162 HOH HOH A . 
F 6 HOH 172 572 184 HOH HOH A . 
F 6 HOH 173 573 86  HOH HOH A . 
F 6 HOH 174 574 101 HOH HOH A . 
F 6 HOH 175 575 129 HOH HOH A . 
F 6 HOH 176 576 78  HOH HOH A . 
F 6 HOH 177 577 263 HOH HOH A . 
F 6 HOH 178 578 95  HOH HOH A . 
F 6 HOH 179 579 286 HOH HOH A . 
F 6 HOH 180 580 140 HOH HOH A . 
F 6 HOH 181 581 278 HOH HOH A . 
F 6 HOH 182 582 65  HOH HOH A . 
F 6 HOH 183 583 305 HOH HOH A . 
F 6 HOH 184 584 148 HOH HOH A . 
F 6 HOH 185 585 301 HOH HOH A . 
F 6 HOH 186 586 199 HOH HOH A . 
F 6 HOH 187 587 97  HOH HOH A . 
F 6 HOH 188 588 41  HOH HOH A . 
F 6 HOH 189 589 331 HOH HOH A . 
F 6 HOH 190 590 270 HOH HOH A . 
F 6 HOH 191 591 320 HOH HOH A . 
F 6 HOH 192 592 210 HOH HOH A . 
F 6 HOH 193 593 37  HOH HOH A . 
F 6 HOH 194 594 225 HOH HOH A . 
F 6 HOH 195 595 231 HOH HOH A . 
F 6 HOH 196 596 324 HOH HOH A . 
F 6 HOH 197 597 198 HOH HOH A . 
F 6 HOH 198 598 178 HOH HOH A . 
F 6 HOH 199 599 34  HOH HOH A . 
F 6 HOH 200 600 282 HOH HOH A . 
F 6 HOH 201 601 61  HOH HOH A . 
F 6 HOH 202 602 196 HOH HOH A . 
F 6 HOH 203 603 319 HOH HOH A . 
F 6 HOH 204 604 256 HOH HOH A . 
F 6 HOH 205 605 145 HOH HOH A . 
F 6 HOH 206 606 23  HOH HOH A . 
F 6 HOH 207 607 40  HOH HOH A . 
F 6 HOH 208 608 99  HOH HOH A . 
F 6 HOH 209 609 203 HOH HOH A . 
F 6 HOH 210 610 281 HOH HOH A . 
F 6 HOH 211 611 146 HOH HOH A . 
F 6 HOH 212 612 157 HOH HOH A . 
F 6 HOH 213 613 269 HOH HOH A . 
F 6 HOH 214 614 214 HOH HOH A . 
F 6 HOH 215 615 260 HOH HOH A . 
F 6 HOH 216 616 39  HOH HOH A . 
F 6 HOH 217 617 26  HOH HOH A . 
F 6 HOH 218 618 116 HOH HOH A . 
F 6 HOH 219 619 239 HOH HOH A . 
F 6 HOH 220 620 317 HOH HOH A . 
F 6 HOH 221 621 42  HOH HOH A . 
F 6 HOH 222 622 211 HOH HOH A . 
F 6 HOH 223 623 141 HOH HOH A . 
F 6 HOH 224 624 44  HOH HOH A . 
F 6 HOH 225 625 318 HOH HOH A . 
F 6 HOH 226 626 197 HOH HOH A . 
F 6 HOH 227 627 165 HOH HOH A . 
F 6 HOH 228 628 333 HOH HOH A . 
F 6 HOH 229 629 47  HOH HOH A . 
F 6 HOH 230 630 154 HOH HOH A . 
F 6 HOH 231 631 268 HOH HOH A . 
F 6 HOH 232 632 327 HOH HOH A . 
F 6 HOH 233 633 139 HOH HOH A . 
F 6 HOH 234 634 321 HOH HOH A . 
F 6 HOH 235 635 54  HOH HOH A . 
F 6 HOH 236 636 48  HOH HOH A . 
F 6 HOH 237 637 304 HOH HOH A . 
F 6 HOH 238 638 126 HOH HOH A . 
F 6 HOH 239 639 294 HOH HOH A . 
F 6 HOH 240 640 167 HOH HOH A . 
F 6 HOH 241 641 83  HOH HOH A . 
F 6 HOH 242 642 337 HOH HOH A . 
F 6 HOH 243 643 73  HOH HOH A . 
F 6 HOH 244 644 170 HOH HOH A . 
F 6 HOH 245 645 230 HOH HOH A . 
F 6 HOH 246 646 308 HOH HOH A . 
F 6 HOH 247 647 232 HOH HOH A . 
F 6 HOH 248 648 206 HOH HOH A . 
F 6 HOH 249 649 80  HOH HOH A . 
F 6 HOH 250 650 223 HOH HOH A . 
F 6 HOH 251 651 208 HOH HOH A . 
F 6 HOH 252 652 326 HOH HOH A . 
F 6 HOH 253 653 135 HOH HOH A . 
F 6 HOH 254 654 109 HOH HOH A . 
F 6 HOH 255 655 207 HOH HOH A . 
F 6 HOH 256 656 91  HOH HOH A . 
F 6 HOH 257 657 70  HOH HOH A . 
F 6 HOH 258 658 275 HOH HOH A . 
F 6 HOH 259 659 217 HOH HOH A . 
F 6 HOH 260 660 221 HOH HOH A . 
F 6 HOH 261 661 329 HOH HOH A . 
F 6 HOH 262 662 314 HOH HOH A . 
F 6 HOH 263 663 149 HOH HOH A . 
F 6 HOH 264 664 72  HOH HOH A . 
F 6 HOH 265 665 125 HOH HOH A . 
F 6 HOH 266 666 212 HOH HOH A . 
F 6 HOH 267 667 236 HOH HOH A . 
F 6 HOH 268 668 102 HOH HOH A . 
F 6 HOH 269 669 173 HOH HOH A . 
F 6 HOH 270 670 284 HOH HOH A . 
F 6 HOH 271 671 243 HOH HOH A . 
F 6 HOH 272 672 316 HOH HOH A . 
F 6 HOH 273 673 335 HOH HOH A . 
F 6 HOH 274 674 110 HOH HOH A . 
F 6 HOH 275 675 297 HOH HOH A . 
F 6 HOH 276 676 204 HOH HOH A . 
F 6 HOH 277 677 151 HOH HOH A . 
F 6 HOH 278 678 108 HOH HOH A . 
F 6 HOH 279 679 291 HOH HOH A . 
F 6 HOH 280 680 118 HOH HOH A . 
F 6 HOH 281 681 298 HOH HOH A . 
F 6 HOH 282 682 100 HOH HOH A . 
F 6 HOH 283 683 147 HOH HOH A . 
F 6 HOH 284 684 238 HOH HOH A . 
F 6 HOH 285 685 290 HOH HOH A . 
F 6 HOH 286 686 229 HOH HOH A . 
F 6 HOH 287 687 248 HOH HOH A . 
F 6 HOH 288 688 277 HOH HOH A . 
F 6 HOH 289 689 94  HOH HOH A . 
F 6 HOH 290 690 112 HOH HOH A . 
F 6 HOH 291 691 103 HOH HOH A . 
F 6 HOH 292 692 289 HOH HOH A . 
F 6 HOH 293 693 287 HOH HOH A . 
F 6 HOH 294 694 249 HOH HOH A . 
F 6 HOH 295 695 259 HOH HOH A . 
F 6 HOH 296 696 292 HOH HOH A . 
F 6 HOH 297 697 92  HOH HOH A . 
F 6 HOH 298 698 272 HOH HOH A . 
F 6 HOH 299 699 124 HOH HOH A . 
F 6 HOH 300 700 323 HOH HOH A . 
F 6 HOH 301 701 111 HOH HOH A . 
F 6 HOH 302 702 202 HOH HOH A . 
F 6 HOH 303 703 311 HOH HOH A . 
F 6 HOH 304 704 334 HOH HOH A . 
F 6 HOH 305 705 200 HOH HOH A . 
F 6 HOH 306 706 186 HOH HOH A . 
F 6 HOH 307 707 237 HOH HOH A . 
F 6 HOH 308 708 254 HOH HOH A . 
F 6 HOH 309 709 62  HOH HOH A . 
F 6 HOH 310 710 265 HOH HOH A . 
F 6 HOH 311 711 87  HOH HOH A . 
F 6 HOH 312 712 150 HOH HOH A . 
F 6 HOH 313 713 137 HOH HOH A . 
F 6 HOH 314 714 255 HOH HOH A . 
F 6 HOH 315 715 312 HOH HOH A . 
F 6 HOH 316 716 172 HOH HOH A . 
F 6 HOH 317 717 121 HOH HOH A . 
F 6 HOH 318 718 219 HOH HOH A . 
F 6 HOH 319 719 247 HOH HOH A . 
F 6 HOH 320 720 266 HOH HOH A . 
F 6 HOH 321 721 315 HOH HOH A . 
F 6 HOH 322 722 285 HOH HOH A . 
F 6 HOH 323 723 138 HOH HOH A . 
F 6 HOH 324 724 283 HOH HOH A . 
F 6 HOH 325 725 84  HOH HOH A . 
F 6 HOH 326 726 174 HOH HOH A . 
F 6 HOH 327 727 302 HOH HOH A . 
F 6 HOH 328 728 234 HOH HOH A . 
F 6 HOH 329 729 159 HOH HOH A . 
F 6 HOH 330 730 257 HOH HOH A . 
F 6 HOH 331 731 218 HOH HOH A . 
F 6 HOH 332 732 295 HOH HOH A . 
F 6 HOH 333 733 262 HOH HOH A . 
F 6 HOH 334 734 120 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  ? CE  ? A LYS 80  CE  
7  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
8  1 Y 1 A LYS 168 ? NZ  ? A LYS 167 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 LYS 228 ? CE  ? A LYS 227 CE  
12 1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
13 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
14 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
15 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
16 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
17 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? '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                   103.660 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YH5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.829 
_cell.length_a_esd                 ? 
_cell.length_b                     41.103 
_cell.length_b_esd                 ? 
_cell.length_c                     71.699 
_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                         6YH5 
_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                   6YH5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.05 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.99 
_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         2012-11-30 
_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   0.826605 
_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        0.826605 
_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                         6YH5 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.200 
_reflns.d_resolution_low                 69.672 
_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                       73229 
_reflns.number_obs                       73229 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.800 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.049 
_reflns.pdbx_netI_over_av_sigmaI         8.200 
_reflns.pdbx_netI_over_sigmaI            15.300 
_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                  0.057 
_reflns.pdbx_Rpim_I_all                  0.022 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         494667 
_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 
1.200 1.260  ? 2.700  68309 ? ? ? 10593 98.300 ? ? ? ? 0.292 ? ? ? ? ? ? ? ? 6.400 0.292 ? ? 4.700  0.349 0.135 ? 1  1 ? ? ? 
1.260 1.340  ? 3.400  69242 ? ? ? 10064 99.100 ? ? ? ? 0.225 ? ? ? ? ? ? ? ? 6.900 0.225 ? ? 6.200  0.266 0.100 ? 2  1 ? ? ? 
1.340 1.430  ? 4.600  63190 ? ? ? 9454  98.500 ? ? ? ? 0.166 ? ? ? ? ? ? ? ? 6.700 0.166 ? ? 7.600  0.197 0.075 ? 3  1 ? ? ? 
1.430 1.550  ? 6.500  58613 ? ? ? 8790  98.600 ? ? ? ? 0.114 ? ? ? ? ? ? ? ? 6.700 0.114 ? ? 10.300 0.137 0.052 ? 4  1 ? ? ? 
1.550 1.700  ? 8.500  56568 ? ? ? 8151  99.300 ? ? ? ? 0.085 ? ? ? ? ? ? ? ? 6.900 0.085 ? ? 14.000 0.101 0.038 ? 5  1 ? ? ? 
1.700 1.900  ? 11.000 48559 ? ? ? 7367  98.500 ? ? ? ? 0.062 ? ? ? ? ? ? ? ? 6.600 0.062 ? ? 18.600 0.075 0.029 ? 6  1 ? ? ? 
1.900 2.190  ? 13.500 46681 ? ? ? 6561  99.700 ? ? ? ? 0.048 ? ? ? ? ? ? ? ? 7.100 0.048 ? ? 26.700 0.057 0.021 ? 7  1 ? ? ? 
2.190 2.680  ? 14.800 36618 ? ? ? 5497  98.500 ? ? ? ? 0.044 ? ? ? ? ? ? ? ? 6.700 0.044 ? ? 30.000 0.052 0.020 ? 8  1 ? ? ? 
2.680 3.790  ? 16.300 30801 ? ? ? 4332  99.400 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 7.100 0.038 ? ? 37.400 0.043 0.016 ? 9  1 ? ? ? 
3.790 69.672 ? 19.800 16086 ? ? ? 2420  98.800 ? ? ? ? 0.030 ? ? ? ? ? ? ? ? 6.600 0.030 ? ? 38.900 0.035 0.013 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.4800 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.0700 
_refine.aniso_B[2][2]                            -0.2600 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.6900 
_refine.B_iso_max                                104.480 
_refine.B_iso_mean                               17.0550 
_refine.B_iso_min                                6.930 
_refine.correlation_coeff_Fo_to_Fc               0.9810 
_refine.correlation_coeff_Fo_to_Fc_free          0.9700 
_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                                 6YH5 
_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                            1.2000 
_refine.ls_d_res_low                             40.6500 
_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                     65836 
_refine.ls_number_reflns_R_free                  7367 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.6700 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1266 
_refine.ls_R_factor_R_free                       0.1590 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1230 
_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                       0.0370 
_refine.pdbx_overall_ESU_R_Free                  0.0390 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0369 
_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                       1.2000 
_refine_hist.d_res_low                        40.6500 
_refine_hist.number_atoms_solvent             339 
_refine_hist.number_atoms_total               2410 
_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       258 
_refine_hist.pdbx_B_iso_mean_ligand           24.38 
_refine_hist.pdbx_B_iso_mean_solvent          30.73 
_refine_hist.pdbx_number_atoms_protein        2036 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_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' ? 0.017  0.012  2232 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.997  1.647  3045 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.766  5.000  279  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.278 23.519 108  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.398 15.000 363  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 16.164 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.141  0.200  271  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.020  1766 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 7.963  3.000  2232 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 25.380 5.000  186  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 12.389 5.000  2315 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2000 
_refine_ls_shell.d_res_low                        1.2310 
_refine_ls_shell.number_reflns_all                5384 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             569 
_refine_ls_shell.number_reflns_R_work             4815 
_refine_ls_shell.percent_reflns_obs               98.1400 
_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                  0.1910 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1530 
_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                     6YH5 
_struct.title                        
'Crystal structure of chimeric carbonic anhydrase XII with 2-Chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]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        6YH5 
_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 ? 
# 
_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              6YH5 
_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 6YH5 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YH5 LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YH5 THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YH5 ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YH5 SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YH5 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)' 610   ? 
1 MORE         6     ? 
1 'SSA (A^2)'  11500 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? 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 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.989 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C E1F . N19 ? ? A ZN  301 A E1F 302 1_555 ? ? ? ? ? ? ? 1.963 ? ? 
# 
_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_555 102.7 ? 
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_555 112.3 ? 
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 99.6  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N19 ? C E1F .   ? A E1F 302 ? 1_555 109.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N19 ? C E1F .   ? A E1F 302 ? 1_555 116.1 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N19 ? C E1F .   ? A E1F 302 ? 1_555 115.5 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -1.21 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 6.53  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O 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 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 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 E1F 302 ? 13 'binding site for residue E1F A 302' 
AC3 Software A BEZ 303 ? 7  'binding site for residue BEZ A 303' 
AC4 Software A DMS 304 ? 3  'binding site for residue DMS A 304' 
# 
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  E1F C .   ? E1F A 302 . ? 1_555 ? 
5  AC2 13 HIS A 94  ? HIS A 94  . ? 1_555 ? 
6  AC2 13 HIS A 96  ? HIS A 96  . ? 1_555 ? 
7  AC2 13 HIS A 119 ? HIS A 119 . ? 1_555 ? 
8  AC2 13 SER A 134 ? SER A 135 . ? 1_555 ? 
9  AC2 13 VAL A 142 ? VAL A 143 . ? 1_555 ? 
10 AC2 13 LEU A 197 ? LEU A 198 . ? 1_555 ? 
11 AC2 13 THR A 198 ? THR A 199 . ? 1_555 ? 
12 AC2 13 THR A 199 ? THR A 200 . ? 1_555 ? 
13 AC2 13 PRO A 201 ? PRO A 202 . ? 1_555 ? 
14 AC2 13 TRP A 208 ? TRP A 209 . ? 1_555 ? 
15 AC2 13 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
16 AC2 13 BEZ D .   ? BEZ A 303 . ? 1_555 ? 
17 AC2 13 HOH F .   ? HOH A 475 . ? 1_555 ? 
18 AC3 7  ASN A 62  ? ASN A 62  . ? 1_555 ? 
19 AC3 7  HIS A 64  ? HIS A 64  . ? 1_555 ? 
20 AC3 7  LYS A 67  ? LYS A 67  . ? 1_555 ? 
21 AC3 7  GLN A 92  ? GLN A 92  . ? 1_555 ? 
22 AC3 7  HIS A 94  ? HIS A 94  . ? 1_555 ? 
23 AC3 7  E1F C .   ? E1F A 302 . ? 1_555 ? 
24 AC3 7  HOH F .   ? HOH A 596 . ? 1_555 ? 
25 AC4 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
26 AC4 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
27 AC4 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    89 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.85 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             4 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             4 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.416 
_pdbx_validate_rmsd_bond.bond_target_value         1.354 
_pdbx_validate_rmsd_bond.bond_deviation            0.062 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.009 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              4 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              4 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              4 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                100.72 
_pdbx_validate_rmsd_angle.angle_target_value         113.60 
_pdbx_validate_rmsd_angle.angle_deviation            -12.88 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.70 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 11  ? ? -140.45 15.13   
2  1 ARG A 27  ? ? -144.85 57.78   
3  1 LEU A 57  ? ? -120.38 -54.51  
4  1 LYS A 76  ? ? -110.92 -89.27  
5  1 GLU A 106 ? ? -91.41  -60.61  
6  1 LYS A 111 ? ? 74.37   -3.88   
7  1 PHE A 176 ? ? -155.13 80.77   
8  1 PHE A 176 ? ? -155.27 80.77   
9  1 ASN A 244 ? ? -97.51  51.99   
10 1 LYS A 252 ? ? 58.42   -137.38 
# 
_pdbx_entry_details.entry_id                 6YH5 
_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 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BEZ C    C  N N 74  
BEZ O1   O  N N 75  
BEZ O2   O  N N 76  
BEZ C1   C  Y N 77  
BEZ C2   C  Y N 78  
BEZ C3   C  Y N 79  
BEZ C4   C  Y N 80  
BEZ C5   C  Y N 81  
BEZ C6   C  Y N 82  
BEZ HO2  H  N N 83  
BEZ H2   H  N N 84  
BEZ H3   H  N N 85  
BEZ H4   H  N N 86  
BEZ H5   H  N N 87  
BEZ H6   H  N N 88  
CYS N    N  N N 89  
CYS CA   C  N R 90  
CYS C    C  N N 91  
CYS O    O  N N 92  
CYS CB   C  N N 93  
CYS SG   S  N N 94  
CYS OXT  O  N N 95  
CYS H    H  N N 96  
CYS H2   H  N N 97  
CYS HA   H  N N 98  
CYS HB2  H  N N 99  
CYS HB3  H  N N 100 
CYS HG   H  N N 101 
CYS HXT  H  N N 102 
DMS S    S  N N 103 
DMS O    O  N N 104 
DMS C1   C  N N 105 
DMS C2   C  N N 106 
DMS H11  H  N N 107 
DMS H12  H  N N 108 
DMS H13  H  N N 109 
DMS H21  H  N N 110 
DMS H22  H  N N 111 
DMS H23  H  N N 112 
E1F O18  O  N N 113 
E1F C13  C  Y N 114 
E1F C1   C  Y N 115 
E1F C2   C  Y N 116 
E1F CL1  CL N N 117 
E1F C21  C  Y N 118 
E1F C5   C  Y N 119 
E1F C4   C  Y N 120 
E1F C3   C  Y N 121 
E1F S16  S  N N 122 
E1F N19  N  N N 123 
E1F O17  O  N N 124 
E1F C6   C  N N 125 
E1F O12  O  N N 126 
E1F C7   C  N N 127 
E1F S8   S  N N 128 
E1F C9   C  Y N 129 
E1F N11  N  Y N 130 
E1F C14  C  Y N 131 
E1F C15  C  Y N 132 
E1F N10  N  Y N 133 
E1F H1   H  N N 134 
E1F H2   H  N N 135 
E1F H3   H  N N 136 
E1F H4   H  N N 137 
E1F H5   H  N N 138 
E1F H6   H  N N 139 
E1F H7   H  N N 140 
E1F H8   H  N N 141 
E1F H9   H  N N 142 
E1F H10  H  N N 143 
GLN N    N  N N 144 
GLN CA   C  N S 145 
GLN C    C  N N 146 
GLN O    O  N N 147 
GLN CB   C  N N 148 
GLN CG   C  N N 149 
GLN CD   C  N N 150 
GLN OE1  O  N N 151 
GLN NE2  N  N N 152 
GLN OXT  O  N N 153 
GLN H    H  N N 154 
GLN H2   H  N N 155 
GLN HA   H  N N 156 
GLN HB2  H  N N 157 
GLN HB3  H  N N 158 
GLN HG2  H  N N 159 
GLN HG3  H  N N 160 
GLN HE21 H  N N 161 
GLN HE22 H  N N 162 
GLN HXT  H  N N 163 
GLU N    N  N N 164 
GLU CA   C  N S 165 
GLU C    C  N N 166 
GLU O    O  N N 167 
GLU CB   C  N N 168 
GLU CG   C  N N 169 
GLU CD   C  N N 170 
GLU OE1  O  N N 171 
GLU OE2  O  N N 172 
GLU OXT  O  N N 173 
GLU H    H  N N 174 
GLU H2   H  N N 175 
GLU HA   H  N N 176 
GLU HB2  H  N N 177 
GLU HB3  H  N N 178 
GLU HG2  H  N N 179 
GLU HG3  H  N N 180 
GLU HE2  H  N N 181 
GLU HXT  H  N N 182 
GLY N    N  N N 183 
GLY CA   C  N N 184 
GLY C    C  N N 185 
GLY O    O  N N 186 
GLY OXT  O  N N 187 
GLY H    H  N N 188 
GLY H2   H  N N 189 
GLY HA2  H  N N 190 
GLY HA3  H  N N 191 
GLY HXT  H  N N 192 
HIS N    N  N N 193 
HIS CA   C  N S 194 
HIS C    C  N N 195 
HIS O    O  N N 196 
HIS CB   C  N N 197 
HIS CG   C  Y N 198 
HIS ND1  N  Y N 199 
HIS CD2  C  Y N 200 
HIS CE1  C  Y N 201 
HIS NE2  N  Y N 202 
HIS OXT  O  N N 203 
HIS H    H  N N 204 
HIS H2   H  N N 205 
HIS HA   H  N N 206 
HIS HB2  H  N N 207 
HIS HB3  H  N N 208 
HIS HD1  H  N N 209 
HIS HD2  H  N N 210 
HIS HE1  H  N N 211 
HIS HE2  H  N N 212 
HIS HXT  H  N N 213 
HOH O    O  N N 214 
HOH H1   H  N N 215 
HOH H2   H  N N 216 
ILE N    N  N N 217 
ILE CA   C  N S 218 
ILE C    C  N N 219 
ILE O    O  N N 220 
ILE CB   C  N S 221 
ILE CG1  C  N N 222 
ILE CG2  C  N N 223 
ILE CD1  C  N N 224 
ILE OXT  O  N N 225 
ILE H    H  N N 226 
ILE H2   H  N N 227 
ILE HA   H  N N 228 
ILE HB   H  N N 229 
ILE HG12 H  N N 230 
ILE HG13 H  N N 231 
ILE HG21 H  N N 232 
ILE HG22 H  N N 233 
ILE HG23 H  N N 234 
ILE HD11 H  N N 235 
ILE HD12 H  N N 236 
ILE HD13 H  N N 237 
ILE HXT  H  N N 238 
LEU N    N  N N 239 
LEU CA   C  N S 240 
LEU C    C  N N 241 
LEU O    O  N N 242 
LEU CB   C  N N 243 
LEU CG   C  N N 244 
LEU CD1  C  N N 245 
LEU CD2  C  N N 246 
LEU OXT  O  N N 247 
LEU H    H  N N 248 
LEU H2   H  N N 249 
LEU HA   H  N N 250 
LEU HB2  H  N N 251 
LEU HB3  H  N N 252 
LEU HG   H  N N 253 
LEU HD11 H  N N 254 
LEU HD12 H  N N 255 
LEU HD13 H  N N 256 
LEU HD21 H  N N 257 
LEU HD22 H  N N 258 
LEU HD23 H  N N 259 
LEU HXT  H  N N 260 
LYS N    N  N N 261 
LYS CA   C  N S 262 
LYS C    C  N N 263 
LYS O    O  N N 264 
LYS CB   C  N N 265 
LYS CG   C  N N 266 
LYS CD   C  N N 267 
LYS CE   C  N N 268 
LYS NZ   N  N N 269 
LYS OXT  O  N N 270 
LYS H    H  N N 271 
LYS H2   H  N N 272 
LYS HA   H  N N 273 
LYS HB2  H  N N 274 
LYS HB3  H  N N 275 
LYS HG2  H  N N 276 
LYS HG3  H  N N 277 
LYS HD2  H  N N 278 
LYS HD3  H  N N 279 
LYS HE2  H  N N 280 
LYS HE3  H  N N 281 
LYS HZ1  H  N N 282 
LYS HZ2  H  N N 283 
LYS HZ3  H  N N 284 
LYS HXT  H  N N 285 
MET N    N  N N 286 
MET CA   C  N S 287 
MET C    C  N N 288 
MET O    O  N N 289 
MET CB   C  N N 290 
MET CG   C  N N 291 
MET SD   S  N N 292 
MET CE   C  N N 293 
MET OXT  O  N N 294 
MET H    H  N N 295 
MET H2   H  N N 296 
MET HA   H  N N 297 
MET HB2  H  N N 298 
MET HB3  H  N N 299 
MET HG2  H  N N 300 
MET HG3  H  N N 301 
MET HE1  H  N N 302 
MET HE2  H  N N 303 
MET HE3  H  N N 304 
MET HXT  H  N N 305 
PHE N    N  N N 306 
PHE CA   C  N S 307 
PHE C    C  N N 308 
PHE O    O  N N 309 
PHE CB   C  N N 310 
PHE CG   C  Y N 311 
PHE CD1  C  Y N 312 
PHE CD2  C  Y N 313 
PHE CE1  C  Y N 314 
PHE CE2  C  Y N 315 
PHE CZ   C  Y N 316 
PHE OXT  O  N N 317 
PHE H    H  N N 318 
PHE H2   H  N N 319 
PHE HA   H  N N 320 
PHE HB2  H  N N 321 
PHE HB3  H  N N 322 
PHE HD1  H  N N 323 
PHE HD2  H  N N 324 
PHE HE1  H  N N 325 
PHE HE2  H  N N 326 
PHE HZ   H  N N 327 
PHE HXT  H  N N 328 
PRO N    N  N N 329 
PRO CA   C  N S 330 
PRO C    C  N N 331 
PRO O    O  N N 332 
PRO CB   C  N N 333 
PRO CG   C  N N 334 
PRO CD   C  N N 335 
PRO OXT  O  N N 336 
PRO H    H  N N 337 
PRO HA   H  N N 338 
PRO HB2  H  N N 339 
PRO HB3  H  N N 340 
PRO HG2  H  N N 341 
PRO HG3  H  N N 342 
PRO HD2  H  N N 343 
PRO HD3  H  N N 344 
PRO HXT  H  N N 345 
SER N    N  N N 346 
SER CA   C  N S 347 
SER C    C  N N 348 
SER O    O  N N 349 
SER CB   C  N N 350 
SER OG   O  N N 351 
SER OXT  O  N N 352 
SER H    H  N N 353 
SER H2   H  N N 354 
SER HA   H  N N 355 
SER HB2  H  N N 356 
SER HB3  H  N N 357 
SER HG   H  N N 358 
SER HXT  H  N N 359 
THR N    N  N N 360 
THR CA   C  N S 361 
THR C    C  N N 362 
THR O    O  N N 363 
THR CB   C  N R 364 
THR OG1  O  N N 365 
THR CG2  C  N N 366 
THR OXT  O  N N 367 
THR H    H  N N 368 
THR H2   H  N N 369 
THR HA   H  N N 370 
THR HB   H  N N 371 
THR HG1  H  N N 372 
THR HG21 H  N N 373 
THR HG22 H  N N 374 
THR HG23 H  N N 375 
THR HXT  H  N N 376 
TRP N    N  N N 377 
TRP CA   C  N S 378 
TRP C    C  N N 379 
TRP O    O  N N 380 
TRP CB   C  N N 381 
TRP CG   C  Y N 382 
TRP CD1  C  Y N 383 
TRP CD2  C  Y N 384 
TRP NE1  N  Y N 385 
TRP CE2  C  Y N 386 
TRP CE3  C  Y N 387 
TRP CZ2  C  Y N 388 
TRP CZ3  C  Y N 389 
TRP CH2  C  Y N 390 
TRP OXT  O  N N 391 
TRP H    H  N N 392 
TRP H2   H  N N 393 
TRP HA   H  N N 394 
TRP HB2  H  N N 395 
TRP HB3  H  N N 396 
TRP HD1  H  N N 397 
TRP HE1  H  N N 398 
TRP HE3  H  N N 399 
TRP HZ2  H  N N 400 
TRP HZ3  H  N N 401 
TRP HH2  H  N N 402 
TRP HXT  H  N N 403 
TYR N    N  N N 404 
TYR CA   C  N S 405 
TYR C    C  N N 406 
TYR O    O  N N 407 
TYR CB   C  N N 408 
TYR CG   C  Y N 409 
TYR CD1  C  Y N 410 
TYR CD2  C  Y N 411 
TYR CE1  C  Y N 412 
TYR CE2  C  Y N 413 
TYR CZ   C  Y N 414 
TYR OH   O  N N 415 
TYR OXT  O  N N 416 
TYR H    H  N N 417 
TYR H2   H  N N 418 
TYR HA   H  N N 419 
TYR HB2  H  N N 420 
TYR HB3  H  N N 421 
TYR HD1  H  N N 422 
TYR HD2  H  N N 423 
TYR HE1  H  N N 424 
TYR HE2  H  N N 425 
TYR HH   H  N N 426 
TYR HXT  H  N N 427 
VAL N    N  N N 428 
VAL CA   C  N S 429 
VAL C    C  N N 430 
VAL O    O  N N 431 
VAL CB   C  N N 432 
VAL CG1  C  N N 433 
VAL CG2  C  N N 434 
VAL OXT  O  N N 435 
VAL H    H  N N 436 
VAL H2   H  N N 437 
VAL HA   H  N N 438 
VAL HB   H  N N 439 
VAL HG11 H  N N 440 
VAL HG12 H  N N 441 
VAL HG13 H  N N 442 
VAL HG21 H  N N 443 
VAL HG22 H  N N 444 
VAL HG23 H  N N 445 
VAL HXT  H  N N 446 
ZN  ZN   ZN N N 447 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BEZ C   O1   doub N N 70  
BEZ C   O2   sing N N 71  
BEZ C   C1   sing N N 72  
BEZ O2  HO2  sing N N 73  
BEZ C1  C2   doub Y N 74  
BEZ C1  C6   sing Y N 75  
BEZ C2  C3   sing Y N 76  
BEZ C2  H2   sing N N 77  
BEZ C3  C4   doub Y N 78  
BEZ C3  H3   sing N N 79  
BEZ C4  C5   sing Y N 80  
BEZ C4  H4   sing N N 81  
BEZ C5  C6   doub Y N 82  
BEZ C5  H5   sing N N 83  
BEZ C6  H6   sing N N 84  
CYS N   CA   sing N N 85  
CYS N   H    sing N N 86  
CYS N   H2   sing N N 87  
CYS CA  C    sing N N 88  
CYS CA  CB   sing N N 89  
CYS CA  HA   sing N N 90  
CYS C   O    doub N N 91  
CYS C   OXT  sing N N 92  
CYS CB  SG   sing N N 93  
CYS CB  HB2  sing N N 94  
CYS CB  HB3  sing N N 95  
CYS SG  HG   sing N N 96  
CYS OXT HXT  sing N N 97  
DMS S   O    doub N N 98  
DMS S   C1   sing N N 99  
DMS S   C2   sing N N 100 
DMS C1  H11  sing N N 101 
DMS C1  H12  sing N N 102 
DMS C1  H13  sing N N 103 
DMS C2  H21  sing N N 104 
DMS C2  H22  sing N N 105 
DMS C2  H23  sing N N 106 
E1F S8  C9   sing N N 107 
E1F S8  C7   sing N N 108 
E1F N11 C9   doub Y N 109 
E1F N11 C14  sing Y N 110 
E1F C9  N10  sing Y N 111 
E1F C7  C6   sing N N 112 
E1F O12 C6   doub N N 113 
E1F C14 C15  doub Y N 114 
E1F C6  C1   sing N N 115 
E1F C5  C1   doub Y N 116 
E1F C5  C4   sing Y N 117 
E1F C1  C21  sing Y N 118 
E1F N10 C13  doub Y N 119 
E1F C15 C13  sing Y N 120 
E1F C4  C3   doub Y N 121 
E1F C21 C2   doub Y N 122 
E1F C3  C2   sing Y N 123 
E1F C3  S16  sing N N 124 
E1F C2  CL1  sing N N 125 
E1F N19 S16  sing N N 126 
E1F O17 S16  doub N N 127 
E1F S16 O18  doub N N 128 
E1F C13 H1   sing N N 129 
E1F C21 H2   sing N N 130 
E1F C5  H3   sing N N 131 
E1F C4  H4   sing N N 132 
E1F N19 H5   sing N N 133 
E1F N19 H6   sing N N 134 
E1F C7  H7   sing N N 135 
E1F C7  H8   sing N N 136 
E1F C14 H9   sing N N 137 
E1F C15 H10  sing N N 138 
GLN N   CA   sing N N 139 
GLN N   H    sing N N 140 
GLN N   H2   sing N N 141 
GLN CA  C    sing N N 142 
GLN CA  CB   sing N N 143 
GLN CA  HA   sing N N 144 
GLN C   O    doub N N 145 
GLN C   OXT  sing N N 146 
GLN CB  CG   sing N N 147 
GLN CB  HB2  sing N N 148 
GLN CB  HB3  sing N N 149 
GLN CG  CD   sing N N 150 
GLN CG  HG2  sing N N 151 
GLN CG  HG3  sing N N 152 
GLN CD  OE1  doub N N 153 
GLN CD  NE2  sing N N 154 
GLN NE2 HE21 sing N N 155 
GLN NE2 HE22 sing N N 156 
GLN OXT HXT  sing N N 157 
GLU N   CA   sing N N 158 
GLU N   H    sing N N 159 
GLU N   H2   sing N N 160 
GLU CA  C    sing N N 161 
GLU CA  CB   sing N N 162 
GLU CA  HA   sing N N 163 
GLU C   O    doub N N 164 
GLU C   OXT  sing N N 165 
GLU CB  CG   sing N N 166 
GLU CB  HB2  sing N N 167 
GLU CB  HB3  sing N N 168 
GLU CG  CD   sing N N 169 
GLU CG  HG2  sing N N 170 
GLU CG  HG3  sing N N 171 
GLU CD  OE1  doub N N 172 
GLU CD  OE2  sing N N 173 
GLU OE2 HE2  sing N N 174 
GLU OXT HXT  sing N N 175 
GLY N   CA   sing N N 176 
GLY N   H    sing N N 177 
GLY N   H2   sing N N 178 
GLY CA  C    sing N N 179 
GLY CA  HA2  sing N N 180 
GLY CA  HA3  sing N N 181 
GLY C   O    doub N N 182 
GLY C   OXT  sing N N 183 
GLY OXT HXT  sing N N 184 
HIS N   CA   sing N N 185 
HIS N   H    sing N N 186 
HIS N   H2   sing N N 187 
HIS CA  C    sing N N 188 
HIS CA  CB   sing N N 189 
HIS CA  HA   sing N N 190 
HIS C   O    doub N N 191 
HIS C   OXT  sing N N 192 
HIS CB  CG   sing N N 193 
HIS CB  HB2  sing N N 194 
HIS CB  HB3  sing N N 195 
HIS CG  ND1  sing Y N 196 
HIS CG  CD2  doub Y N 197 
HIS ND1 CE1  doub Y N 198 
HIS ND1 HD1  sing N N 199 
HIS CD2 NE2  sing Y N 200 
HIS CD2 HD2  sing N N 201 
HIS CE1 NE2  sing Y N 202 
HIS CE1 HE1  sing N N 203 
HIS NE2 HE2  sing N N 204 
HIS OXT HXT  sing N N 205 
HOH O   H1   sing N N 206 
HOH O   H2   sing N N 207 
ILE N   CA   sing N N 208 
ILE N   H    sing N N 209 
ILE N   H2   sing N N 210 
ILE CA  C    sing N N 211 
ILE CA  CB   sing N N 212 
ILE CA  HA   sing N N 213 
ILE C   O    doub N N 214 
ILE C   OXT  sing N N 215 
ILE CB  CG1  sing N N 216 
ILE CB  CG2  sing N N 217 
ILE CB  HB   sing N N 218 
ILE CG1 CD1  sing N N 219 
ILE CG1 HG12 sing N N 220 
ILE CG1 HG13 sing N N 221 
ILE CG2 HG21 sing N N 222 
ILE CG2 HG22 sing N N 223 
ILE CG2 HG23 sing N N 224 
ILE CD1 HD11 sing N N 225 
ILE CD1 HD12 sing N N 226 
ILE CD1 HD13 sing N N 227 
ILE OXT HXT  sing N N 228 
LEU N   CA   sing N N 229 
LEU N   H    sing N N 230 
LEU N   H2   sing N N 231 
LEU CA  C    sing N N 232 
LEU CA  CB   sing N N 233 
LEU CA  HA   sing N N 234 
LEU C   O    doub N N 235 
LEU C   OXT  sing N N 236 
LEU CB  CG   sing N N 237 
LEU CB  HB2  sing N N 238 
LEU CB  HB3  sing N N 239 
LEU CG  CD1  sing N N 240 
LEU CG  CD2  sing N N 241 
LEU CG  HG   sing N N 242 
LEU CD1 HD11 sing N N 243 
LEU CD1 HD12 sing N N 244 
LEU CD1 HD13 sing N N 245 
LEU CD2 HD21 sing N N 246 
LEU CD2 HD22 sing N N 247 
LEU CD2 HD23 sing N N 248 
LEU OXT HXT  sing N N 249 
LYS N   CA   sing N N 250 
LYS N   H    sing N N 251 
LYS N   H2   sing N N 252 
LYS CA  C    sing N N 253 
LYS CA  CB   sing N N 254 
LYS CA  HA   sing N N 255 
LYS C   O    doub N N 256 
LYS C   OXT  sing N N 257 
LYS CB  CG   sing N N 258 
LYS CB  HB2  sing N N 259 
LYS CB  HB3  sing N N 260 
LYS CG  CD   sing N N 261 
LYS CG  HG2  sing N N 262 
LYS CG  HG3  sing N N 263 
LYS CD  CE   sing N N 264 
LYS CD  HD2  sing N N 265 
LYS CD  HD3  sing N N 266 
LYS CE  NZ   sing N N 267 
LYS CE  HE2  sing N N 268 
LYS CE  HE3  sing N N 269 
LYS NZ  HZ1  sing N N 270 
LYS NZ  HZ2  sing N N 271 
LYS NZ  HZ3  sing N N 272 
LYS OXT HXT  sing N N 273 
MET N   CA   sing N N 274 
MET N   H    sing N N 275 
MET N   H2   sing N N 276 
MET CA  C    sing N N 277 
MET CA  CB   sing N N 278 
MET CA  HA   sing N N 279 
MET C   O    doub N N 280 
MET C   OXT  sing N N 281 
MET CB  CG   sing N N 282 
MET CB  HB2  sing N N 283 
MET CB  HB3  sing N N 284 
MET CG  SD   sing N N 285 
MET CG  HG2  sing N N 286 
MET CG  HG3  sing N N 287 
MET SD  CE   sing N N 288 
MET CE  HE1  sing N N 289 
MET CE  HE2  sing N N 290 
MET CE  HE3  sing N N 291 
MET OXT HXT  sing N N 292 
PHE N   CA   sing N N 293 
PHE N   H    sing N N 294 
PHE N   H2   sing N N 295 
PHE CA  C    sing N N 296 
PHE CA  CB   sing N N 297 
PHE CA  HA   sing N N 298 
PHE C   O    doub N N 299 
PHE C   OXT  sing N N 300 
PHE CB  CG   sing N N 301 
PHE CB  HB2  sing N N 302 
PHE CB  HB3  sing N N 303 
PHE CG  CD1  doub Y N 304 
PHE CG  CD2  sing Y N 305 
PHE CD1 CE1  sing Y N 306 
PHE CD1 HD1  sing N N 307 
PHE CD2 CE2  doub Y N 308 
PHE CD2 HD2  sing N N 309 
PHE CE1 CZ   doub Y N 310 
PHE CE1 HE1  sing N N 311 
PHE CE2 CZ   sing Y N 312 
PHE CE2 HE2  sing N N 313 
PHE CZ  HZ   sing N N 314 
PHE OXT HXT  sing N N 315 
PRO N   CA   sing N N 316 
PRO N   CD   sing N N 317 
PRO N   H    sing N N 318 
PRO CA  C    sing N N 319 
PRO CA  CB   sing N N 320 
PRO CA  HA   sing N N 321 
PRO C   O    doub N N 322 
PRO C   OXT  sing N N 323 
PRO CB  CG   sing N N 324 
PRO CB  HB2  sing N N 325 
PRO CB  HB3  sing N N 326 
PRO CG  CD   sing N N 327 
PRO CG  HG2  sing N N 328 
PRO CG  HG3  sing N N 329 
PRO CD  HD2  sing N N 330 
PRO CD  HD3  sing N N 331 
PRO OXT HXT  sing N N 332 
SER N   CA   sing N N 333 
SER N   H    sing N N 334 
SER N   H2   sing N N 335 
SER CA  C    sing N N 336 
SER CA  CB   sing N N 337 
SER CA  HA   sing N N 338 
SER C   O    doub N N 339 
SER C   OXT  sing N N 340 
SER CB  OG   sing N N 341 
SER CB  HB2  sing N N 342 
SER CB  HB3  sing N N 343 
SER OG  HG   sing N N 344 
SER OXT HXT  sing N N 345 
THR N   CA   sing N N 346 
THR N   H    sing N N 347 
THR N   H2   sing N N 348 
THR CA  C    sing N N 349 
THR CA  CB   sing N N 350 
THR CA  HA   sing N N 351 
THR C   O    doub N N 352 
THR C   OXT  sing N N 353 
THR CB  OG1  sing N N 354 
THR CB  CG2  sing N N 355 
THR CB  HB   sing N N 356 
THR OG1 HG1  sing N N 357 
THR CG2 HG21 sing N N 358 
THR CG2 HG22 sing N N 359 
THR CG2 HG23 sing N N 360 
THR OXT HXT  sing N N 361 
TRP N   CA   sing N N 362 
TRP N   H    sing N N 363 
TRP N   H2   sing N N 364 
TRP CA  C    sing N N 365 
TRP CA  CB   sing N N 366 
TRP CA  HA   sing N N 367 
TRP C   O    doub N N 368 
TRP C   OXT  sing N N 369 
TRP CB  CG   sing N N 370 
TRP CB  HB2  sing N N 371 
TRP CB  HB3  sing N N 372 
TRP CG  CD1  doub Y N 373 
TRP CG  CD2  sing Y N 374 
TRP CD1 NE1  sing Y N 375 
TRP CD1 HD1  sing N N 376 
TRP CD2 CE2  doub Y N 377 
TRP CD2 CE3  sing Y N 378 
TRP NE1 CE2  sing Y N 379 
TRP NE1 HE1  sing N N 380 
TRP CE2 CZ2  sing Y N 381 
TRP CE3 CZ3  doub Y N 382 
TRP CE3 HE3  sing N N 383 
TRP CZ2 CH2  doub Y N 384 
TRP CZ2 HZ2  sing N N 385 
TRP CZ3 CH2  sing Y N 386 
TRP CZ3 HZ3  sing N N 387 
TRP CH2 HH2  sing N N 388 
TRP OXT HXT  sing N N 389 
TYR N   CA   sing N N 390 
TYR N   H    sing N N 391 
TYR N   H2   sing N N 392 
TYR CA  C    sing N N 393 
TYR CA  CB   sing N N 394 
TYR CA  HA   sing N N 395 
TYR C   O    doub N N 396 
TYR C   OXT  sing N N 397 
TYR CB  CG   sing N N 398 
TYR CB  HB2  sing N N 399 
TYR CB  HB3  sing N N 400 
TYR CG  CD1  doub Y N 401 
TYR CG  CD2  sing Y N 402 
TYR CD1 CE1  sing Y N 403 
TYR CD1 HD1  sing N N 404 
TYR CD2 CE2  doub Y N 405 
TYR CD2 HD2  sing N N 406 
TYR CE1 CZ   doub Y N 407 
TYR CE1 HE1  sing N N 408 
TYR CE2 CZ   sing Y N 409 
TYR CE2 HE2  sing N N 410 
TYR CZ  OH   sing N N 411 
TYR OH  HH   sing N N 412 
TYR OXT HXT  sing N N 413 
VAL N   CA   sing N N 414 
VAL N   H    sing N N 415 
VAL N   H2   sing N N 416 
VAL CA  C    sing N N 417 
VAL CA  CB   sing N N 418 
VAL CA  HA   sing N N 419 
VAL C   O    doub N N 420 
VAL C   OXT  sing N N 421 
VAL CB  CG1  sing N N 422 
VAL CB  CG2  sing N N 423 
VAL CB  HB   sing N N 424 
VAL CG1 HG11 sing N N 425 
VAL CG1 HG12 sing N N 426 
VAL CG1 HG13 sing N N 427 
VAL CG2 HG21 sing N N 428 
VAL CG2 HG22 sing N N 429 
VAL CG2 HG23 sing N N 430 
VAL OXT HXT  sing N N 431 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        E1F 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   E1F 
_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                    6YH5 
_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]   0.023907 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005808 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024329 
_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]   0.014353 
_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  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 3   ? 14.188  0.244   6.492   1.00 30.42  ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 13.807  -0.884  7.384   1.00 37.36  ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 12.669  -0.442  8.312   1.00 40.31  ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 12.908  -0.186  9.527   1.00 41.20  ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 15.030  -1.404  8.137   1.00 30.78  ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 14.731  -2.616  8.944   1.00 30.20  ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 14.333  -2.525  10.262  1.00 33.48  ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 14.731  -3.930  8.614   1.00 27.95  ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 14.180  -3.756  10.739  1.00 34.63  ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 14.364  -4.644  9.721   1.00 34.30  ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 11.470  -0.381  7.762   1.00 38.14  ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 10.358  0.096   8.516   1.00 39.10  ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 9.650   -1.029  9.231   1.00 27.52  ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 9.927   -2.210  8.980   1.00 28.31  ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 9.421   0.733   7.572   1.00 25.21  ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 9.150   1.983   8.262   1.00 12.23  ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 9.953   2.619   9.133   1.00 32.00  ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 7.837   2.486   8.431   1.00 16.15  ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 9.279   3.644   9.667   1.00 44.36  ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 7.983   3.599   9.229   1.00 47.41  ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.711   -0.636  10.108  1.00 23.33  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 8.105   -1.566  11.042  1.00 17.27  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 7.132   -2.461  10.282  1.00 15.45  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.524   -2.075  9.247   1.00 19.05  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.401   -0.854  12.204  1.00 18.16  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 6.170   -0.089  11.835  1.00 15.99  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 6.077   1.201   11.401  1.00 19.89  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.831   -0.610  11.828  1.00 14.58  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.760   1.541   11.222  1.00 18.58  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.970   0.469   11.480  1.00 15.12  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 4.278   -1.861  12.157  1.00 13.72  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.582   0.316   11.420  1.00 15.96  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.905   -1.987  12.128  1.00 14.39  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 2.078   -0.912  11.748  1.00 15.29  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.861   -3.655  10.818  1.00 14.06  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.840   -4.559  10.288  1.00 14.78  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.517   -5.613  11.326  1.00 13.05  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.561   -5.356  12.527  1.00 12.27  ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 5.244   -6.817  10.848  1.00 13.64  ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.823   -7.950  11.675  1.00 13.95  ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.704   -9.166  11.457  1.00 16.37  ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 5.415   -10.227 12.031  1.00 21.51  ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 3.350   -8.303  11.378  1.00 14.21  ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 2.446   -7.198  11.880  1.00 12.29  ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 2.030   -7.142  13.215  1.00 11.73  ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.969   -6.206  11.024  1.00 12.50  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 1.192   -6.138  13.686  1.00 11.38  ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 1.139   -5.204  11.462  1.00 12.19  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.745   -5.182  12.796  1.00 10.79  ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.088  -4.193  13.162  1.00 12.28  ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.847   -8.974  10.780  1.00 15.74  ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.762   -10.094 10.502  1.00 19.33  ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.763   -10.338 11.633  1.00 18.24  ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.861   -9.600  12.617  1.00 17.51  ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.613   -11.339 11.410  1.00 18.89  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.622  -11.688 12.391  1.00 19.91  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.604  -10.545 12.663  1.00 15.84  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 12.093  -10.423 13.796  1.00 16.61  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 11.422  -12.865 11.846  1.00 22.96  ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 12.577  -13.251 12.748  1.00 30.37  ? 9   LYS A CG  1 
ATOM   61   N  N   . HIS A 1 10  ? 11.934  -9.755  11.646  1.00 16.20  ? 10  HIS A N   1 
ATOM   62   C  CA  . HIS A 1 10  ? 13.013  -8.763  11.826  1.00 15.67  ? 10  HIS A CA  1 
ATOM   63   C  C   . HIS A 1 10  ? 12.472  -7.365  12.023  1.00 14.49  ? 10  HIS A C   1 
ATOM   64   O  O   . HIS A 1 10  ? 13.293  -6.467  12.370  1.00 16.09  ? 10  HIS A O   1 
ATOM   65   C  CB  . HIS A 1 10  ? 13.968  -8.750  10.652  1.00 16.69  ? 10  HIS A CB  1 
ATOM   66   C  CG  . HIS A 1 10  ? 14.593  -10.079 10.528  1.00 16.29  ? 10  HIS A CG  1 
ATOM   67   N  ND1 . HIS A 1 10  ? 15.651  -10.506 11.334  1.00 19.63  ? 10  HIS A ND1 1 
ATOM   68   C  CD2 . HIS A 1 10  ? 14.310  -11.090 9.705   1.00 17.49  ? 10  HIS A CD2 1 
ATOM   69   C  CE1 . HIS A 1 10  ? 15.967  -11.744 11.024  1.00 19.50  ? 10  HIS A CE1 1 
ATOM   70   N  NE2 . HIS A 1 10  ? 15.173  -12.105 9.974   1.00 18.38  ? 10  HIS A NE2 1 
ATOM   71   N  N   . ASN A 1 11  ? 11.127  -7.175  11.901  1.00 13.91  ? 11  ASN A N   1 
ATOM   72   C  CA  . ASN A 1 11  ? 10.603  -5.815  12.086  1.00 13.57  ? 11  ASN A CA  1 
ATOM   73   C  C   . ASN A 1 11  ? 9.279   -5.801  12.858  1.00 11.81  ? 11  ASN A C   1 
ATOM   74   O  O   . ASN A 1 11  ? 8.631   -4.748  12.912  1.00 12.73  ? 11  ASN A O   1 
ATOM   75   C  CB  . ASN A 1 11  ? 10.427  -5.125  10.732  1.00 15.18  ? 11  ASN A CB  1 
ATOM   76   C  CG  . ASN A 1 11  ? 9.371   -5.795  9.871   1.00 14.86  ? 11  ASN A CG  1 
ATOM   77   O  OD1 . ASN A 1 11  ? 8.751   -6.784  10.263  1.00 17.72  ? 11  ASN A OD1 1 
ATOM   78   N  ND2 . ASN A 1 11  ? 9.079   -5.187  8.741   1.00 20.30  ? 11  ASN A ND2 1 
ATOM   79   N  N   . GLY A 1 12  ? 8.931   -6.904  13.516  1.00 11.97  ? 12  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 12  ? 7.655   -7.122  14.190  1.00 12.34  ? 12  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 12  ? 7.625   -6.541  15.575  1.00 10.67  ? 12  GLY A C   1 
ATOM   82   O  O   . GLY A 1 12  ? 8.543   -5.815  16.011  1.00 10.95  ? 12  GLY A O   1 
ATOM   83   N  N   . PRO A 1 13  ? 6.545   -6.841  16.308  1.00 10.86  ? 13  PRO A N   1 
ATOM   84   C  CA  . PRO A 1 13  ? 6.318   -6.260  17.614  1.00 10.63  ? 13  PRO A CA  1 
ATOM   85   C  C   . PRO A 1 13  ? 7.455   -6.250  18.607  1.00 10.86  ? 13  PRO A C   1 
ATOM   86   O  O   . PRO A 1 13  ? 7.595   -5.290  19.365  1.00 12.32  ? 13  PRO A O   1 
ATOM   87   C  CB  . PRO A 1 13  ? 5.117   -7.107  18.137  1.00 12.40  ? 13  PRO A CB  1 
ATOM   88   C  CG  . PRO A 1 13  ? 4.320   -7.344  16.886  1.00 11.82  ? 13  PRO A CG  1 
ATOM   89   C  CD  . PRO A 1 13  ? 5.387   -7.596  15.802  1.00 12.63  ? 13  PRO A CD  1 
ATOM   90   N  N   . GLU A 1 14  ? 8.325   -7.281  18.596  1.00 12.10  ? 14  GLU A N   1 
ATOM   91   C  CA  . GLU A 1 14  ? 9.436   -7.312  19.561  1.00 12.98  ? 14  GLU A CA  1 
ATOM   92   C  C   . GLU A 1 14  ? 10.533  -6.288  19.198  1.00 11.80  ? 14  GLU A C   1 
ATOM   93   O  O   . GLU A 1 14  ? 11.416  -6.054  20.043  1.00 13.24  ? 14  GLU A O   1 
ATOM   94   C  CB  . GLU A 1 14  ? 10.045  -8.734  19.548  1.00 15.46  ? 14  GLU A CB  1 
ATOM   95   C  CG  . GLU A 1 14  ? 9.011   -9.767  19.964  1.00 22.39  ? 14  GLU A CG  1 
ATOM   96   C  CD  . GLU A 1 14  ? 8.184   -9.420  21.196  1.00 32.57  ? 14  GLU A CD  1 
ATOM   97   O  OE1 . GLU A 1 14  ? 8.791   -8.985  22.218  1.00 38.94  ? 14  GLU A OE1 1 
ATOM   98   O  OE2 . GLU A 1 14  ? 6.901   -9.615  21.142  1.00 34.62  ? 14  GLU A OE2 1 
ATOM   99   N  N   . HIS A 1 15  ? 10.476  -5.726  18.002  1.00 10.56  ? 15  HIS A N   1 
ATOM   100  C  CA  . HIS A 1 15  ? 11.433  -4.725  17.587  1.00 11.18  ? 15  HIS A CA  1 
ATOM   101  C  C   . HIS A 1 15  ? 10.960  -3.290  17.719  1.00 10.86  ? 15  HIS A C   1 
ATOM   102  O  O   . HIS A 1 15  ? 11.767  -2.358  17.638  1.00 11.56  ? 15  HIS A O   1 
ATOM   103  C  CB  . HIS A 1 15  ? 11.784  -4.905  16.085  1.00 11.07  ? 15  HIS A CB  1 
ATOM   104  C  CG  . HIS A 1 15  ? 12.504  -6.153  15.769  1.00 11.68  ? 15  HIS A CG  1 
ATOM   105  N  ND1 . HIS A 1 15  ? 13.908  -6.216  15.793  1.00 13.59  ? 15  HIS A ND1 1 
ATOM   106  C  CD2 . HIS A 1 15  ? 12.054  -7.397  15.437  1.00 13.78  ? 15  HIS A CD2 1 
ATOM   107  C  CE1 . HIS A 1 15  ? 14.290  -7.436  15.481  1.00 14.30  ? 15  HIS A CE1 1 
ATOM   108  N  NE2 . HIS A 1 15  ? 13.184  -8.197  15.253  1.00 16.14  ? 15  HIS A NE2 1 
ATOM   109  N  N   . TRP A 1 16  ? 9.633   -3.077  17.912  1.00 10.05  ? 16  TRP A N   1 
ATOM   110  C  CA  . TRP A 1 16  ? 9.099   -1.748  17.772  1.00 10.48  ? 16  TRP A CA  1 
ATOM   111  C  C   . TRP A 1 16  ? 9.630   -0.756  18.806  1.00 10.26  ? 16  TRP A C   1 
ATOM   112  O  O   . TRP A 1 16  ? 9.708   0.443   18.497  1.00 11.38  ? 16  TRP A O   1 
ATOM   113  C  CB  . TRP A 1 16  ? 7.542   -1.802  17.889  1.00 10.37  ? 16  TRP A CB  1 
ATOM   114  C  CG  . TRP A 1 16  ? 6.887   -2.521  16.732  1.00 10.17  ? 16  TRP A CG  1 
ATOM   115  C  CD1 . TRP A 1 16  ? 7.447   -2.961  15.580  1.00 10.56  ? 16  TRP A CD1 1 
ATOM   116  C  CD2 . TRP A 1 16  ? 5.506   -2.892  16.711  1.00 9.66   ? 16  TRP A CD2 1 
ATOM   117  N  NE1 . TRP A 1 16  ? 6.472   -3.538  14.787  1.00 10.40  ? 16  TRP A NE1 1 
ATOM   118  C  CE2 . TRP A 1 16  ? 5.272   -3.522  15.474  1.00 9.80   ? 16  TRP A CE2 1 
ATOM   119  C  CE3 . TRP A 1 16  ? 4.441   -2.717  17.611  1.00 9.70   ? 16  TRP A CE3 1 
ATOM   120  C  CZ2 . TRP A 1 16  ? 4.006   -4.000  15.084  1.00 10.04  ? 16  TRP A CZ2 1 
ATOM   121  C  CZ3 . TRP A 1 16  ? 3.203   -3.213  17.262  1.00 10.70  ? 16  TRP A CZ3 1 
ATOM   122  C  CH2 . TRP A 1 16  ? 2.976   -3.840  16.027  1.00 10.43  ? 16  TRP A CH2 1 
ATOM   123  N  N   . HIS A 1 17  ? 10.038  -1.226  19.999  1.00 10.65  ? 17  HIS A N   1 
ATOM   124  C  CA  . HIS A 1 17  ? 10.499  -0.339  21.048  1.00 11.03  ? 17  HIS A CA  1 
ATOM   125  C  C   . HIS A 1 17  ? 11.730  0.427   20.602  1.00 11.43  ? 17  HIS A C   1 
ATOM   126  O  O   . HIS A 1 17  ? 12.022  1.482   21.184  1.00 12.43  ? 17  HIS A O   1 
ATOM   127  C  CB  . HIS A 1 17  ? 10.797  -1.108  22.360  1.00 11.60  ? 17  HIS A CB  1 
ATOM   128  C  CG  . HIS A 1 17  ? 12.015  -1.964  22.237  1.00 11.88  ? 17  HIS A CG  1 
ATOM   129  N  ND1 . HIS A 1 17  ? 13.228  -1.527  22.786  1.00 13.43  ? 17  HIS A ND1 1 
ATOM   130  C  CD2 . HIS A 1 17  ? 12.232  -3.162  21.652  1.00 12.87  ? 17  HIS A CD2 1 
ATOM   131  C  CE1 . HIS A 1 17  ? 14.134  -2.427  22.522  1.00 15.19  ? 17  HIS A CE1 1 
ATOM   132  N  NE2 . HIS A 1 17  ? 13.567  -3.443  21.850  1.00 14.17  ? 17  HIS A NE2 1 
ATOM   133  N  N   . LYS A 1 18  ? 12.516  -0.058  19.624  1.00 11.42  ? 18  LYS A N   1 
ATOM   134  C  CA  . LYS A 1 18  ? 13.719  0.679   19.205  1.00 12.33  ? 18  LYS A CA  1 
ATOM   135  C  C   . LYS A 1 18  ? 13.358  2.015   18.559  1.00 13.57  ? 18  LYS A C   1 
ATOM   136  O  O   . LYS A 1 18  ? 13.966  3.056   18.843  1.00 18.93  ? 18  LYS A O   1 
ATOM   137  C  CB  . LYS A 1 18  ? 14.583  -0.213  18.331  1.00 12.80  ? 18  LYS A CB  1 
ATOM   138  C  CG  . LYS A 1 18  ? 15.196  -1.434  19.051  1.00 13.58  ? 18  LYS A CG  1 
ATOM   139  C  CD  . LYS A 1 18  ? 15.945  -2.370  18.113  1.00 14.28  ? 18  LYS A CD  1 
ATOM   140  C  CE  . LYS A 1 18  ? 15.002  -3.381  17.510  1.00 12.87  ? 18  LYS A CE  1 
ATOM   141  N  NZ  . LYS A 1 18  ? 15.650  -4.125  16.394  1.00 12.92  ? 18  LYS A NZ  1 
ATOM   142  N  N   . ASP A 1 19  ? 12.370  2.022   17.686  1.00 12.79  ? 19  ASP A N   1 
ATOM   143  C  CA  . ASP A 1 19  ? 11.919  3.273   17.097  1.00 13.56  ? 19  ASP A CA  1 
ATOM   144  C  C   . ASP A 1 19  ? 10.898  4.000   17.936  1.00 12.79  ? 19  ASP A C   1 
ATOM   145  O  O   . ASP A 1 19  ? 10.797  5.208   17.851  1.00 15.06  ? 19  ASP A O   1 
ATOM   146  C  CB  . ASP A 1 19  ? 11.299  3.018   15.736  1.00 16.29  ? 19  ASP A CB  1 
ATOM   147  C  CG  . ASP A 1 19  ? 12.293  2.847   14.632  1.00 24.15  ? 19  ASP A CG  1 
ATOM   148  O  OD1 . ASP A 1 19  ? 13.316  3.592   14.612  1.00 28.66  ? 19  ASP A OD1 1 
ATOM   149  O  OD2 . ASP A 1 19  ? 12.088  1.880   13.878  1.00 44.10  ? 19  ASP A OD2 1 
ATOM   150  N  N   . PHE A 1 20  ? 10.156  3.248   18.769  1.00 11.88  ? 20  PHE A N   1 
ATOM   151  C  CA  . PHE A 1 20  ? 9.062   3.811   19.557  1.00 11.82  ? 20  PHE A CA  1 
ATOM   152  C  C   . PHE A 1 20  ? 9.176   3.326   20.996  1.00 11.61  ? 20  PHE A C   1 
ATOM   153  O  O   . PHE A 1 20  ? 8.535   2.340   21.387  1.00 11.40  ? 20  PHE A O   1 
ATOM   154  C  CB  . PHE A 1 20  ? 7.710   3.390   18.942  1.00 13.67  ? 20  PHE A CB  1 
ATOM   155  C  CG  . PHE A 1 20  ? 7.607   3.782   17.489  1.00 15.51  ? 20  PHE A CG  1 
ATOM   156  C  CD1 . PHE A 1 20  ? 7.325   5.077   17.130  1.00 20.74  ? 20  PHE A CD1 1 
ATOM   157  C  CD2 . PHE A 1 20  ? 7.931   2.846   16.502  1.00 18.89  ? 20  PHE A CD2 1 
ATOM   158  C  CE1 . PHE A 1 20  ? 7.296   5.412   15.771  1.00 21.01  ? 20  PHE A CE1 1 
ATOM   159  C  CE2 . PHE A 1 20  ? 7.937   3.179   15.158  1.00 21.09  ? 20  PHE A CE2 1 
ATOM   160  C  CZ  . PHE A 1 20  ? 7.638   4.479   14.825  1.00 21.15  ? 20  PHE A CZ  1 
ATOM   161  N  N   . PRO A 1 21  ? 10.038  3.954   21.815  1.00 12.28  ? 21  PRO A N   1 
ATOM   162  C  CA  . PRO A 1 21  ? 10.314  3.447   23.164  1.00 13.29  ? 21  PRO A CA  1 
ATOM   163  C  C   . PRO A 1 21  ? 9.099   3.369   24.068  1.00 12.74  ? 21  PRO A C   1 
ATOM   164  O  O   . PRO A 1 21  ? 9.155   2.622   25.060  1.00 13.42  ? 21  PRO A O   1 
ATOM   165  C  CB  . PRO A 1 21  ? 11.358  4.404   23.741  1.00 17.81  ? 21  PRO A CB  1 
ATOM   166  C  CG  . PRO A 1 21  ? 11.904  5.104   22.566  1.00 22.53  ? 21  PRO A CG  1 
ATOM   167  C  CD  . PRO A 1 21  ? 10.957  5.039   21.406  1.00 15.10  ? 21  PRO A CD  1 
ATOM   168  N  N   A ILE A 1 22  ? 8.011   4.082   23.708  0.50 11.89  ? 22  ILE A N   1 
ATOM   169  N  N   B ILE A 1 22  ? 7.994   4.081   23.740  0.50 12.29  ? 22  ILE A N   1 
ATOM   170  C  CA  A ILE A 1 22  ? 6.780   3.968   24.462  0.50 10.57  ? 22  ILE A CA  1 
ATOM   171  C  CA  B ILE A 1 22  ? 6.789   3.945   24.548  0.50 11.60  ? 22  ILE A CA  1 
ATOM   172  C  C   A ILE A 1 22  ? 6.166   2.565   24.379  0.50 10.24  ? 22  ILE A C   1 
ATOM   173  C  C   B ILE A 1 22  ? 6.215   2.526   24.448  0.50 10.88  ? 22  ILE A C   1 
ATOM   174  O  O   A ILE A 1 22  ? 5.257   2.258   25.159  0.50 11.58  ? 22  ILE A O   1 
ATOM   175  O  O   B ILE A 1 22  ? 5.338   2.188   25.246  0.50 12.13  ? 22  ILE A O   1 
ATOM   176  C  CB  A ILE A 1 22  ? 5.788   5.067   24.005  0.50 11.64  ? 22  ILE A CB  1 
ATOM   177  C  CB  B ILE A 1 22  ? 5.716   4.970   24.099  0.50 12.44  ? 22  ILE A CB  1 
ATOM   178  C  CG1 A ILE A 1 22  ? 4.763   5.366   25.096  0.50 10.51  ? 22  ILE A CG1 1 
ATOM   179  C  CG1 B ILE A 1 22  ? 4.662   5.249   25.176  0.50 15.46  ? 22  ILE A CG1 1 
ATOM   180  C  CG2 A ILE A 1 22  ? 5.119   4.732   22.673  0.50 10.87  ? 22  ILE A CG2 1 
ATOM   181  C  CG2 B ILE A 1 22  ? 5.077   4.522   22.792  0.50 14.01  ? 22  ILE A CG2 1 
ATOM   182  C  CD1 A ILE A 1 22  ? 3.832   6.472   24.727  0.50 12.67  ? 22  ILE A CD1 1 
ATOM   183  C  CD1 B ILE A 1 22  ? 5.173   6.011   26.370  0.50 18.33  ? 22  ILE A CD1 1 
ATOM   184  N  N   . ALA A 1 23  ? 6.711   1.708   23.516  1.00 10.79  ? 23  ALA A N   1 
ATOM   185  C  CA  . ALA A 1 23  ? 6.265   0.327   23.424  1.00 11.24  ? 23  ALA A CA  1 
ATOM   186  C  C   . ALA A 1 23  ? 6.371   -0.386  24.761  1.00 11.77  ? 23  ALA A C   1 
ATOM   187  O  O   . ALA A 1 23  ? 5.702   -1.403  24.903  1.00 13.35  ? 23  ALA A O   1 
ATOM   188  C  CB  . ALA A 1 23  ? 7.100   -0.392  22.370  1.00 11.11  ? 23  ALA A CB  1 
ATOM   189  N  N   . LYS A 1 24  ? 7.329   0.019   25.628  1.00 12.37  ? 24  LYS A N   1 
ATOM   190  C  CA  . LYS A 1 24  ? 7.508   -0.551  26.953  1.00 13.71  ? 24  LYS A CA  1 
ATOM   191  C  C   . LYS A 1 24  ? 6.904   0.356   28.020  1.00 14.80  ? 24  LYS A C   1 
ATOM   192  O  O   . LYS A 1 24  ? 7.280   0.241   29.197  1.00 16.44  ? 24  LYS A O   1 
ATOM   193  C  CB  . LYS A 1 24  ? 9.009   -0.753  27.190  1.00 16.79  ? 24  LYS A CB  1 
ATOM   194  C  CG  . LYS A 1 24  ? 9.621   -1.763  26.265  1.00 17.50  ? 24  LYS A CG  1 
ATOM   195  C  CD  . LYS A 1 24  ? 11.090  -1.948  26.630  1.00 21.30  ? 24  LYS A CD  1 
ATOM   196  C  CE  . LYS A 1 24  ? 11.780  -2.925  25.739  1.00 22.16  ? 24  LYS A CE  1 
ATOM   197  N  NZ  . LYS A 1 24  ? 11.441  -4.296  26.132  1.00 28.32  ? 24  LYS A NZ  1 
ATOM   198  N  N   . GLY A 1 25  ? 5.875   1.149   27.632  1.00 13.84  ? 25  GLY A N   1 
ATOM   199  C  CA  . GLY A 1 25  ? 5.272   2.127   28.547  1.00 15.12  ? 25  GLY A CA  1 
ATOM   200  C  C   . GLY A 1 25  ? 4.317   1.505   29.580  1.00 12.99  ? 25  GLY A C   1 
ATOM   201  O  O   . GLY A 1 25  ? 4.113   0.277   29.639  1.00 14.09  ? 25  GLY A O   1 
ATOM   202  N  N   . GLU A 1 26  ? 3.642   2.391   30.281  1.00 13.53  ? 26  GLU A N   1 
ATOM   203  C  CA  . GLU A 1 26  ? 2.799   2.028   31.399  1.00 14.58  ? 26  GLU A CA  1 
ATOM   204  C  C   . GLU A 1 26  ? 1.358   1.741   30.980  1.00 12.82  ? 26  GLU A C   1 
ATOM   205  O  O   . GLU A 1 26  ? 0.570   1.239   31.804  1.00 13.96  ? 26  GLU A O   1 
ATOM   206  C  CB  . GLU A 1 26  ? 2.810   3.150   32.454  1.00 17.71  ? 26  GLU A CB  1 
ATOM   207  C  CG  . GLU A 1 26  ? 4.209   3.321   33.051  1.00 21.64  ? 26  GLU A CG  1 
ATOM   208  C  CD  . GLU A 1 26  ? 4.824   2.035   33.615  1.00 27.30  ? 26  GLU A CD  1 
ATOM   209  O  OE1 . GLU A 1 26  ? 4.194   1.364   34.497  1.00 34.07  ? 26  GLU A OE1 1 
ATOM   210  O  OE2 . GLU A 1 26  ? 5.952   1.712   33.221  1.00 37.60  ? 26  GLU A OE2 1 
ATOM   211  N  N   . ARG A 1 27  ? 0.965   2.046   29.729  1.00 10.39  ? 27  ARG A N   1 
ATOM   212  C  CA  . ARG A 1 27  ? -0.443  1.801   29.372  1.00 10.83  ? 27  ARG A CA  1 
ATOM   213  C  C   . ARG A 1 27  ? -0.519  1.357   27.917  1.00 9.43   ? 27  ARG A C   1 
ATOM   214  O  O   . ARG A 1 27  ? -1.244  1.908   27.089  1.00 10.52  ? 27  ARG A O   1 
ATOM   215  C  CB  . ARG A 1 27  ? -1.370  2.988   29.673  1.00 12.60  ? 27  ARG A CB  1 
ATOM   216  C  CG  . ARG A 1 27  ? -0.925  4.328   29.093  1.00 12.78  ? 27  ARG A CG  1 
ATOM   217  C  CD  . ARG A 1 27  ? -1.917  5.481   29.256  1.00 13.99  ? 27  ARG A CD  1 
ATOM   218  N  NE  . ARG A 1 27  ? -3.051  5.372   28.320  1.00 12.62  ? 27  ARG A NE  1 
ATOM   219  C  CZ  . ARG A 1 27  ? -4.039  6.255   28.229  1.00 12.53  ? 27  ARG A CZ  1 
ATOM   220  N  NH1 . ARG A 1 27  ? -4.048  7.321   29.011  1.00 15.90  ? 27  ARG A NH1 1 
ATOM   221  N  NH2 . ARG A 1 27  ? -5.013  6.070   27.357  1.00 13.94  ? 27  ARG A NH2 1 
ATOM   222  N  N   . GLN A 1 28  ? 0.202   0.251   27.631  1.00 9.06   ? 28  GLN A N   1 
ATOM   223  C  CA  . GLN A 1 28  ? 0.220   -0.267  26.256  1.00 9.14   ? 28  GLN A CA  1 
ATOM   224  C  C   . GLN A 1 28  ? -0.926  -1.258  25.984  1.00 8.34   ? 28  GLN A C   1 
ATOM   225  O  O   . GLN A 1 28  ? -1.443  -1.915  26.908  1.00 10.12  ? 28  GLN A O   1 
ATOM   226  C  CB  . GLN A 1 28  ? 1.585   -0.948  26.006  1.00 10.55  ? 28  GLN A CB  1 
ATOM   227  C  CG  . GLN A 1 28  ? 2.703   0.095   25.886  1.00 10.26  ? 28  GLN A CG  1 
ATOM   228  C  CD  . GLN A 1 28  ? 2.571   0.876   24.594  1.00 10.00  ? 28  GLN A CD  1 
ATOM   229  O  OE1 . GLN A 1 28  ? 2.742   0.309   23.500  1.00 10.36  ? 28  GLN A OE1 1 
ATOM   230  N  NE2 . GLN A 1 28  ? 2.217   2.178   24.659  1.00 10.27  ? 28  GLN A NE2 1 
ATOM   231  N  N   . SER A 1 29  ? -1.300  -1.369  24.717  1.00 8.54   ? 29  SER A N   1 
ATOM   232  C  CA  . SER A 1 29  ? -2.371  -2.252  24.266  1.00 8.49   ? 29  SER A CA  1 
ATOM   233  C  C   . SER A 1 29  ? -1.831  -3.107  23.149  1.00 7.92   ? 29  SER A C   1 
ATOM   234  O  O   . SER A 1 29  ? -0.881  -2.783  22.433  1.00 9.20   ? 29  SER A O   1 
ATOM   235  C  CB  . SER A 1 29  ? -3.490  -1.359  23.706  1.00 8.69   ? 29  SER A CB  1 
ATOM   236  O  OG  . SER A 1 29  ? -4.119  -0.632  24.756  1.00 9.00   ? 29  SER A OG  1 
ATOM   237  N  N   . PRO A 1 30  ? -2.485  -4.258  22.886  1.00 8.43   ? 30  PRO A N   1 
ATOM   238  C  CA  . PRO A 1 30  ? -3.668  -4.790  23.594  1.00 8.47   ? 30  PRO A CA  1 
ATOM   239  C  C   . PRO A 1 30  ? -3.237  -5.444  24.918  1.00 8.39   ? 30  PRO A C   1 
ATOM   240  O  O   . PRO A 1 30  ? -2.053  -5.499  25.253  1.00 9.41   ? 30  PRO A O   1 
ATOM   241  C  CB  . PRO A 1 30  ? -4.173  -5.830  22.616  1.00 9.19   ? 30  PRO A CB  1 
ATOM   242  C  CG  . PRO A 1 30  ? -2.880  -6.425  22.010  1.00 8.90   ? 30  PRO A CG  1 
ATOM   243  C  CD  . PRO A 1 30  ? -1.982  -5.218  21.849  1.00 9.10   ? 30  PRO A CD  1 
ATOM   244  N  N   . VAL A 1 31  ? -4.234  -6.003  25.599  1.00 8.56   ? 31  VAL A N   1 
ATOM   245  C  CA  . VAL A 1 31  ? -4.059  -6.731  26.848  1.00 9.28   ? 31  VAL A CA  1 
ATOM   246  C  C   . VAL A 1 31  ? -4.940  -7.967  26.807  1.00 9.57   ? 31  VAL A C   1 
ATOM   247  O  O   . VAL A 1 31  ? -5.884  -8.036  26.031  1.00 9.83   ? 31  VAL A O   1 
ATOM   248  C  CB  . VAL A 1 31  ? -4.376  -5.885  28.105  1.00 9.95   ? 31  VAL A CB  1 
ATOM   249  C  CG1 . VAL A 1 31  ? -3.422  -4.705  28.196  1.00 11.44  ? 31  VAL A CG1 1 
ATOM   250  C  CG2 . VAL A 1 31  ? -5.859  -5.453  28.141  1.00 11.15  ? 31  VAL A CG2 1 
ATOM   251  N  N   . ASP A 1 32  ? -4.592  -8.951  27.646  1.00 10.24  ? 32  ASP A N   1 
ATOM   252  C  CA  . ASP A 1 32  ? -5.525  -10.027 27.980  1.00 10.22  ? 32  ASP A CA  1 
ATOM   253  C  C   . ASP A 1 32  ? -6.577  -9.497  28.935  1.00 10.75  ? 32  ASP A C   1 
ATOM   254  O  O   . ASP A 1 32  ? -6.272  -8.866  29.962  1.00 12.27  ? 32  ASP A O   1 
ATOM   255  C  CB  . ASP A 1 32  ? -4.782  -11.206 28.590  1.00 11.36  ? 32  ASP A CB  1 
ATOM   256  C  CG  . ASP A 1 32  ? -5.739  -12.367 28.887  1.00 11.95  ? 32  ASP A CG  1 
ATOM   257  O  OD1 . ASP A 1 32  ? -6.436  -12.800 27.956  1.00 12.14  ? 32  ASP A OD1 1 
ATOM   258  O  OD2 . ASP A 1 32  ? -5.798  -12.794 30.070  1.00 16.34  ? 32  ASP A OD2 1 
ATOM   259  N  N   . ILE A 1 33  ? -7.837  -9.809  28.609  1.00 10.47  ? 33  ILE A N   1 
ATOM   260  C  CA  . ILE A 1 33  ? -8.949  -9.419  29.488  1.00 10.73  ? 33  ILE A CA  1 
ATOM   261  C  C   . ILE A 1 33  ? -9.281  -10.631 30.339  1.00 10.97  ? 33  ILE A C   1 
ATOM   262  O  O   . ILE A 1 33  ? -9.799  -11.657 29.851  1.00 12.21  ? 33  ILE A O   1 
ATOM   263  C  CB  . ILE A 1 33  ? -10.150 -8.989  28.670  1.00 10.61  ? 33  ILE A CB  1 
ATOM   264  C  CG1 . ILE A 1 33  ? -9.763  -7.788  27.795  1.00 11.19  ? 33  ILE A CG1 1 
ATOM   265  C  CG2 . ILE A 1 33  ? -11.351 -8.739  29.597  1.00 12.92  ? 33  ILE A CG2 1 
ATOM   266  C  CD1 . ILE A 1 33  ? -10.790 -7.470  26.709  1.00 12.99  ? 33  ILE A CD1 1 
ATOM   267  N  N   A ASP A 1 34  ? -8.856  -10.602 31.594  0.50 11.80  ? 34  ASP A N   1 
ATOM   268  N  N   B ASP A 1 34  ? -8.911  -10.543 31.618  0.50 12.48  ? 34  ASP A N   1 
ATOM   269  C  CA  A ASP A 1 34  ? -9.164  -11.686 32.523  0.50 14.28  ? 34  ASP A CA  1 
ATOM   270  C  CA  B ASP A 1 34  ? -9.222  -11.556 32.626  0.50 13.21  ? 34  ASP A CA  1 
ATOM   271  C  C   A ASP A 1 34  ? -10.552 -11.419 33.102  0.50 14.75  ? 34  ASP A C   1 
ATOM   272  C  C   B ASP A 1 34  ? -10.650 -11.300 33.072  0.50 13.70  ? 34  ASP A C   1 
ATOM   273  O  O   A ASP A 1 34  ? -10.707 -10.552 33.958  0.50 16.72  ? 34  ASP A O   1 
ATOM   274  O  O   B ASP A 1 34  ? -10.935 -10.318 33.757  0.50 13.75  ? 34  ASP A O   1 
ATOM   275  C  CB  A ASP A 1 34  ? -8.050  -11.824 33.554  0.50 14.93  ? 34  ASP A CB  1 
ATOM   276  C  CB  B ASP A 1 34  ? -8.212  -11.527 33.771  0.50 14.86  ? 34  ASP A CB  1 
ATOM   277  C  CG  A ASP A 1 34  ? -8.301  -13.040 34.428  0.50 17.71  ? 34  ASP A CG  1 
ATOM   278  C  CG  B ASP A 1 34  ? -8.498  -12.572 34.838  0.50 17.21  ? 34  ASP A CG  1 
ATOM   279  O  OD1 A ASP A 1 34  ? -7.834  -14.113 34.052  0.50 21.67  ? 34  ASP A OD1 1 
ATOM   280  O  OD1 B ASP A 1 34  ? -9.675  -13.036 34.943  0.50 18.28  ? 34  ASP A OD1 1 
ATOM   281  O  OD2 A ASP A 1 34  ? -8.983  -12.923 35.447  0.50 19.22  ? 34  ASP A OD2 1 
ATOM   282  O  OD2 B ASP A 1 34  ? -7.558  -12.897 35.588  0.50 22.57  ? 34  ASP A OD2 1 
ATOM   283  N  N   . THR A 1 35  ? -11.561 -12.152 32.601  1.00 13.73  ? 35  THR A N   1 
ATOM   284  C  CA  . THR A 1 35  ? -12.961 -11.859 32.809  1.00 15.48  ? 35  THR A CA  1 
ATOM   285  C  C   . THR A 1 35  ? -13.337 -11.904 34.270  1.00 14.84  ? 35  THR A C   1 
ATOM   286  O  O   . THR A 1 35  ? -14.256 -11.224 34.680  1.00 17.51  ? 35  THR A O   1 
ATOM   287  C  CB  . THR A 1 35  ? -13.885 -12.754 31.977  1.00 16.82  ? 35  THR A CB  1 
ATOM   288  O  OG1 . THR A 1 35  ? -13.800 -14.089 32.459  1.00 17.49  ? 35  THR A OG1 1 
ATOM   289  C  CG2 . THR A 1 35  ? -13.664 -12.679 30.476  1.00 18.68  ? 35  THR A CG2 1 
ATOM   290  N  N   . HIS A 1 36  ? -12.693 -12.788 35.049  1.00 16.59  ? 36  HIS A N   1 
ATOM   291  C  CA  . HIS A 1 36  ? -13.026 -12.958 36.421  1.00 17.28  ? 36  HIS A CA  1 
ATOM   292  C  C   . HIS A 1 36  ? -12.502 -11.793 37.263  1.00 19.59  ? 36  HIS A C   1 
ATOM   293  O  O   . HIS A 1 36  ? -13.143 -11.513 38.277  1.00 22.64  ? 36  HIS A O   1 
ATOM   294  C  CB  . HIS A 1 36  ? -12.566 -14.348 36.868  1.00 18.94  ? 36  HIS A CB  1 
ATOM   295  C  CG  . HIS A 1 36  ? -13.432 -15.482 36.343  1.00 24.30  ? 36  HIS A CG  1 
ATOM   296  N  ND1 . HIS A 1 36  ? -14.768 -15.604 36.673  1.00 26.02  ? 36  HIS A ND1 1 
ATOM   297  C  CD2 . HIS A 1 36  ? -13.148 -16.520 35.527  1.00 26.81  ? 36  HIS A CD2 1 
ATOM   298  C  CE1 . HIS A 1 36  ? -15.269 -16.670 36.082  1.00 25.07  ? 36  HIS A CE1 1 
ATOM   299  N  NE2 . HIS A 1 36  ? -14.295 -17.249 35.373  1.00 28.69  ? 36  HIS A NE2 1 
ATOM   300  N  N   . THR A 1 37  ? -11.401 -11.134 36.839  1.00 18.74  ? 37  THR A N   1 
ATOM   301  C  CA  . THR A 1 37  ? -10.748 -10.024 37.524  1.00 18.55  ? 37  THR A CA  1 
ATOM   302  C  C   . THR A 1 37  ? -11.336 -8.658  37.156  1.00 17.15  ? 37  THR A C   1 
ATOM   303  O  O   . THR A 1 37  ? -11.218 -7.711  37.920  1.00 22.40  ? 37  THR A O   1 
ATOM   304  C  CB  . THR A 1 37  ? -9.234  -10.084 37.251  1.00 26.83  ? 37  THR A CB  1 
ATOM   305  O  OG1 . THR A 1 37  ? -8.831  -11.306 37.861  1.00 33.40  ? 37  THR A OG1 1 
ATOM   306  C  CG2 . THR A 1 37  ? -8.433  -8.965  37.902  1.00 28.07  ? 37  THR A CG2 1 
ATOM   307  N  N   . ALA A 1 38  ? -11.938 -8.556  35.984  1.00 15.61  ? 38  ALA A N   1 
ATOM   308  C  CA  . ALA A 1 38  ? -12.533 -7.287  35.585  1.00 14.48  ? 38  ALA A CA  1 
ATOM   309  C  C   . ALA A 1 38  ? -13.637 -6.955  36.569  1.00 18.92  ? 38  ALA A C   1 
ATOM   310  O  O   . ALA A 1 38  ? -14.408 -7.818  36.941  1.00 27.45  ? 38  ALA A O   1 
ATOM   311  C  CB  . ALA A 1 38  ? -13.036 -7.432  34.147  1.00 15.00  ? 38  ALA A CB  1 
ATOM   312  N  N   . LYS A 1 39  ? -13.703 -5.711  37.011  1.00 17.13  ? 39  LYS A N   1 
ATOM   313  C  CA  . LYS A 1 39  ? -14.737 -5.371  37.998  1.00 23.44  ? 39  LYS A CA  1 
ATOM   314  C  C   . LYS A 1 39  ? -15.943 -4.732  37.306  1.00 18.44  ? 39  LYS A C   1 
ATOM   315  O  O   . LYS A 1 39  ? -15.788 -3.782  36.546  1.00 16.42  ? 39  LYS A O   1 
ATOM   316  C  CB  . LYS A 1 39  ? -14.297 -4.509  39.202  1.00 36.67  ? 39  LYS A CB  1 
ATOM   317  C  CG  . LYS A 1 39  ? -14.894 -4.921  40.550  1.00 48.90  ? 39  LYS A CG  1 
ATOM   318  C  CD  . LYS A 1 39  ? -15.208 -3.789  41.537  1.00 31.11  ? 39  LYS A CD  1 
ATOM   319  C  CE  . LYS A 1 39  ? -16.070 -4.222  42.714  1.00 29.67  ? 39  LYS A CE  1 
ATOM   320  N  NZ  . LYS A 1 39  ? -16.080 -3.259  43.843  1.00 40.92  ? 39  LYS A NZ  1 
ATOM   321  N  N   . TYR A 1 40  ? -17.111 -5.229  37.694  1.00 18.91  ? 40  TYR A N   1 
ATOM   322  C  CA  . TYR A 1 40  ? -18.356 -4.674  37.239  1.00 17.02  ? 40  TYR A CA  1 
ATOM   323  C  C   . TYR A 1 40  ? -18.448 -3.280  37.843  1.00 17.22  ? 40  TYR A C   1 
ATOM   324  O  O   . TYR A 1 40  ? -18.321 -3.135  39.063  1.00 19.61  ? 40  TYR A O   1 
ATOM   325  C  CB  . TYR A 1 40  ? -19.553 -5.581  37.572  1.00 22.18  ? 40  TYR A CB  1 
ATOM   326  C  CG  . TYR A 1 40  ? -20.857 -4.841  37.446  1.00 21.28  ? 40  TYR A CG  1 
ATOM   327  C  CD1 . TYR A 1 40  ? -21.288 -4.383  36.199  1.00 19.77  ? 40  TYR A CD1 1 
ATOM   328  C  CD2 . TYR A 1 40  ? -21.724 -4.676  38.549  1.00 28.73  ? 40  TYR A CD2 1 
ATOM   329  C  CE1 . TYR A 1 40  ? -22.474 -3.678  36.066  1.00 24.25  ? 40  TYR A CE1 1 
ATOM   330  C  CE2 . TYR A 1 40  ? -22.928 -4.002  38.410  1.00 28.51  ? 40  TYR A CE2 1 
ATOM   331  C  CZ  . TYR A 1 40  ? -23.286 -3.481  37.174  1.00 31.78  ? 40  TYR A CZ  1 
ATOM   332  O  OH  . TYR A 1 40  ? -24.489 -2.852  36.985  1.00 36.78  ? 40  TYR A OH  1 
ATOM   333  N  N   . ASP A 1 41  ? -18.658 -2.280  37.021  1.00 15.71  ? 41  ASP A N   1 
ATOM   334  C  CA  . ASP A 1 41  ? -18.776 -0.901  37.479  1.00 17.01  ? 41  ASP A CA  1 
ATOM   335  C  C   . ASP A 1 41  ? -20.178 -0.381  37.198  1.00 19.80  ? 41  ASP A C   1 
ATOM   336  O  O   . ASP A 1 41  ? -20.462 -0.041  36.055  1.00 17.47  ? 41  ASP A O   1 
ATOM   337  C  CB  . ASP A 1 41  ? -17.745 0.027   36.860  1.00 20.25  ? 41  ASP A CB  1 
ATOM   338  C  CG  . ASP A 1 41  ? -17.777 1.449   37.363  1.00 23.73  ? 41  ASP A CG  1 
ATOM   339  O  OD1 . ASP A 1 41  ? -18.711 1.792   38.135  1.00 27.61  ? 41  ASP A OD1 1 
ATOM   340  O  OD2 . ASP A 1 41  ? -16.868 2.208   36.965  1.00 30.06  ? 41  ASP A OD2 1 
ATOM   341  N  N   . PRO A 1 42  ? -21.075 -0.377  38.229  1.00 24.11  ? 42  PRO A N   1 
ATOM   342  C  CA  . PRO A 1 42  ? -22.460 0.071   38.012  1.00 28.49  ? 42  PRO A CA  1 
ATOM   343  C  C   . PRO A 1 42  ? -22.521 1.544   37.600  1.00 27.77  ? 42  PRO A C   1 
ATOM   344  O  O   . PRO A 1 42  ? -23.578 2.058   37.167  1.00 35.43  ? 42  PRO A O   1 
ATOM   345  C  CB  . PRO A 1 42  ? -23.202 -0.268  39.312  1.00 34.02  ? 42  PRO A CB  1 
ATOM   346  C  CG  . PRO A 1 42  ? -22.104 -0.434  40.350  1.00 37.21  ? 42  PRO A CG  1 
ATOM   347  C  CD  . PRO A 1 42  ? -20.805 -0.794  39.633  1.00 26.15  ? 42  PRO A CD  1 
ATOM   348  N  N   . SER A 1 43  ? -21.397 2.269   37.741  1.00 25.23  ? 43  SER A N   1 
ATOM   349  C  CA  . SER A 1 43  ? -21.554 3.682   37.370  1.00 30.44  ? 43  SER A CA  1 
ATOM   350  C  C   . SER A 1 43  ? -21.315 3.900   35.872  1.00 24.09  ? 43  SER A C   1 
ATOM   351  O  O   . SER A 1 43  ? -21.512 5.032   35.376  1.00 33.16  ? 43  SER A O   1 
ATOM   352  C  CB  . SER A 1 43  ? -20.587 4.493   38.141  1.00 36.45  ? 43  SER A CB  1 
ATOM   353  O  OG  . SER A 1 43  ? -19.254 4.302   37.635  1.00 35.44  ? 43  SER A OG  1 
ATOM   354  N  N   . LEU A 1 44  ? -20.831 2.851   35.175  1.00 22.79  ? 44  LEU A N   1 
ATOM   355  C  CA  . LEU A 1 44  ? -20.572 2.968   33.729  1.00 21.90  ? 44  LEU A CA  1 
ATOM   356  C  C   . LEU A 1 44  ? -21.903 3.143   33.011  1.00 25.12  ? 44  LEU A C   1 
ATOM   357  O  O   . LEU A 1 44  ? -22.902 2.518   33.315  1.00 28.75  ? 44  LEU A O   1 
ATOM   358  C  CB  . LEU A 1 44  ? -19.845 1.760   33.133  1.00 20.77  ? 44  LEU A CB  1 
ATOM   359  C  CG  . LEU A 1 44  ? -18.348 1.718   33.416  1.00 20.03  ? 44  LEU A CG  1 
ATOM   360  C  CD1 . LEU A 1 44  ? -17.785 0.373   33.038  1.00 20.30  ? 44  LEU A CD1 1 
ATOM   361  C  CD2 . LEU A 1 44  ? -17.674 2.874   32.710  1.00 20.74  ? 44  LEU A CD2 1 
ATOM   362  N  N   . LYS A 1 45  ? -21.893 3.956   31.983  1.00 22.59  ? 45  LYS A N   1 
ATOM   363  C  CA  . LYS A 1 45  ? -23.115 4.200   31.234  1.00 22.33  ? 45  LYS A CA  1 
ATOM   364  C  C   . LYS A 1 45  ? -23.172 3.282   30.045  1.00 20.04  ? 45  LYS A C   1 
ATOM   365  O  O   . LYS A 1 45  ? -22.169 2.703   29.567  1.00 20.83  ? 45  LYS A O   1 
ATOM   366  C  CB  . LYS A 1 45  ? -23.175 5.627   30.767  1.00 21.81  ? 45  LYS A CB  1 
ATOM   367  C  CG  . LYS A 1 45  ? -23.163 6.648   31.890  1.00 27.45  ? 45  LYS A CG  1 
ATOM   368  C  CD  . LYS A 1 45  ? -23.317 8.048   31.366  1.00 35.45  ? 45  LYS A CD  1 
ATOM   369  N  N   . PRO A 1 46  ? -24.413 3.067   29.507  1.00 19.98  ? 46  PRO A N   1 
ATOM   370  C  CA  . PRO A 1 46  ? -24.501 2.386   28.218  1.00 19.25  ? 46  PRO A CA  1 
ATOM   371  C  C   . PRO A 1 46  ? -23.675 3.166   27.216  1.00 16.20  ? 46  PRO A C   1 
ATOM   372  O  O   . PRO A 1 46  ? -23.642 4.379   27.253  1.00 17.43  ? 46  PRO A O   1 
ATOM   373  C  CB  . PRO A 1 46  ? -25.991 2.437   27.865  1.00 20.53  ? 46  PRO A CB  1 
ATOM   374  C  CG  . PRO A 1 46  ? -26.677 2.637   29.167  1.00 24.58  ? 46  PRO A CG  1 
ATOM   375  C  CD  . PRO A 1 46  ? -25.734 3.508   30.020  1.00 23.42  ? 46  PRO A CD  1 
ATOM   376  N  N   . LEU A 1 47  ? -23.070 2.448   26.268  1.00 17.62  ? 47  LEU A N   1 
ATOM   377  C  CA  . LEU A 1 47  ? -22.358 3.086   25.227  1.00 15.36  ? 47  LEU A CA  1 
ATOM   378  C  C   . LEU A 1 47  ? -23.404 3.637   24.231  1.00 17.93  ? 47  LEU A C   1 
ATOM   379  O  O   . LEU A 1 47  ? -24.381 2.912   23.943  1.00 20.16  ? 47  LEU A O   1 
ATOM   380  C  CB  . LEU A 1 47  ? -21.471 1.989   24.629  1.00 22.69  ? 47  LEU A CB  1 
ATOM   381  C  CG  . LEU A 1 47  ? -20.510 2.461   23.581  1.00 24.52  ? 47  LEU A CG  1 
ATOM   382  C  CD1 . LEU A 1 47  ? -19.440 3.371   24.248  1.00 27.67  ? 47  LEU A CD1 1 
ATOM   383  C  CD2 . LEU A 1 47  ? -19.889 1.246   22.914  1.00 26.98  ? 47  LEU A CD2 1 
ATOM   384  N  N   . SER A 1 48  ? -23.212 4.859   23.746  1.00 14.34  ? 48  SER A N   1 
ATOM   385  C  CA  . SER A 1 48  ? -24.038 5.404   22.675  1.00 14.67  ? 48  SER A CA  1 
ATOM   386  C  C   . SER A 1 48  ? -23.270 5.396   21.360  1.00 13.88  ? 48  SER A C   1 
ATOM   387  O  O   . SER A 1 48  ? -22.245 6.045   21.231  1.00 15.89  ? 48  SER A O   1 
ATOM   388  C  CB  . SER A 1 48  ? -24.431 6.839   23.088  1.00 17.47  ? 48  SER A CB  1 
ATOM   389  O  OG  . SER A 1 48  ? -25.001 7.577   22.002  1.00 22.62  ? 48  SER A OG  1 
ATOM   390  N  N   . VAL A 1 49  ? -23.791 4.642   20.397  1.00 16.74  ? 49  VAL A N   1 
ATOM   391  C  CA  . VAL A 1 49  ? -23.179 4.516   19.099  1.00 16.96  ? 49  VAL A CA  1 
ATOM   392  C  C   . VAL A 1 49  ? -24.151 5.160   18.085  1.00 19.00  ? 49  VAL A C   1 
ATOM   393  O  O   . VAL A 1 49  ? -25.284 4.652   17.950  1.00 26.65  ? 49  VAL A O   1 
ATOM   394  C  CB  . VAL A 1 49  ? -22.915 3.039   18.748  1.00 20.70  ? 49  VAL A CB  1 
ATOM   395  C  CG1 . VAL A 1 49  ? -22.256 3.009   17.389  1.00 31.31  ? 49  VAL A CG1 1 
ATOM   396  C  CG2 . VAL A 1 49  ? -22.047 2.368   19.785  1.00 22.16  ? 49  VAL A CG2 1 
ATOM   397  N  N   . SER A 1 50  ? -23.815 6.309   17.468  1.00 17.08  ? 50  SER A N   1 
ATOM   398  C  CA  . SER A 1 50  ? -24.742 7.033   16.617  1.00 17.93  ? 50  SER A CA  1 
ATOM   399  C  C   . SER A 1 50  ? -24.110 7.132   15.251  1.00 15.94  ? 50  SER A C   1 
ATOM   400  O  O   . SER A 1 50  ? -23.427 8.118   14.944  1.00 16.17  ? 50  SER A O   1 
ATOM   401  C  CB  . SER A 1 50  ? -25.072 8.422   17.170  1.00 21.87  ? 50  SER A CB  1 
ATOM   402  O  OG  . SER A 1 50  ? -25.738 8.294   18.395  1.00 24.80  ? 50  SER A OG  1 
ATOM   403  N  N   . TYR A 1 51  ? -24.352 6.080   14.445  1.00 17.13  ? 51  TYR A N   1 
ATOM   404  C  CA  . TYR A 1 51  ? -23.689 5.951   13.144  1.00 15.68  ? 51  TYR A CA  1 
ATOM   405  C  C   . TYR A 1 51  ? -24.639 6.212   11.958  1.00 16.54  ? 51  TYR A C   1 
ATOM   406  O  O   . TYR A 1 51  ? -24.212 6.083   10.817  1.00 15.75  ? 51  TYR A O   1 
ATOM   407  C  CB  . TYR A 1 51  ? -23.070 4.558   12.976  1.00 15.37  ? 51  TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 51  ? -21.791 4.248   13.724  1.00 13.13  ? 51  TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 51  ? -21.085 5.214   14.426  1.00 14.25  ? 51  TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 51  ? -21.273 2.963   13.720  1.00 13.33  ? 51  TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 51  ? -19.910 4.906   15.102  1.00 13.10  ? 51  TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 51  ? -20.103 2.639   14.389  1.00 13.25  ? 51  TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 51  ? -19.411 3.613   15.087  1.00 12.64  ? 51  TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 51  ? -18.253 3.282   15.745  1.00 13.53  ? 51  TYR A OH  1 
ATOM   415  N  N   . ASP A 1 52  ? -25.874 6.685   12.238  1.00 17.57  ? 52  ASP A N   1 
ATOM   416  C  CA  . ASP A 1 52  ? -26.818 6.922   11.141  1.00 18.75  ? 52  ASP A CA  1 
ATOM   417  C  C   . ASP A 1 52  ? -26.363 7.829   9.962   1.00 17.42  ? 52  ASP A C   1 
ATOM   418  O  O   . ASP A 1 52  ? -26.758 7.598   8.791   1.00 20.86  ? 52  ASP A O   1 
ATOM   419  C  CB  . ASP A 1 52  ? -28.172 7.404   11.676  1.00 24.35  ? 52  ASP A CB  1 
ATOM   420  C  CG  . ASP A 1 52  ? -28.152 8.593   12.639  1.00 42.78  ? 52  ASP A CG  1 
ATOM   421  O  OD1 . ASP A 1 52  ? -27.508 8.490   13.777  1.00 54.76  ? 52  ASP A OD1 1 
ATOM   422  O  OD2 . ASP A 1 52  ? -28.808 9.625   12.270  1.00 66.80  ? 52  ASP A OD2 1 
ATOM   423  N  N   . GLN A 1 53  ? -25.579 8.859   10.229  1.00 16.95  ? 53  GLN A N   1 
ATOM   424  C  CA  . GLN A 1 53  ? -25.184 9.789   9.164   1.00 15.06  ? 53  GLN A CA  1 
ATOM   425  C  C   . GLN A 1 53  ? -23.734 9.540   8.755   1.00 13.58  ? 53  GLN A C   1 
ATOM   426  O  O   . GLN A 1 53  ? -23.113 10.406  8.138   1.00 14.98  ? 53  GLN A O   1 
ATOM   427  C  CB  . GLN A 1 53  ? -25.402 11.242  9.612   1.00 16.75  ? 53  GLN A CB  1 
ATOM   428  C  CG  . GLN A 1 53  ? -26.871 11.568  9.903   1.00 21.22  ? 53  GLN A CG  1 
ATOM   429  C  CD  . GLN A 1 53  ? -27.710 11.393  8.663   1.00 25.39  ? 53  GLN A CD  1 
ATOM   430  O  OE1 . GLN A 1 53  ? -28.771 10.772  8.687   1.00 33.98  ? 53  GLN A OE1 1 
ATOM   431  N  NE2 . GLN A 1 53  ? -27.219 11.901  7.519   1.00 19.68  ? 53  GLN A NE2 1 
ATOM   432  N  N   . ALA A 1 54  ? -23.179 8.360   9.044   1.00 13.92  ? 54  ALA A N   1 
ATOM   433  C  CA  . ALA A 1 54  ? -21.784 8.116   8.650   1.00 12.35  ? 54  ALA A CA  1 
ATOM   434  C  C   . ALA A 1 54  ? -21.611 8.277   7.154   1.00 13.10  ? 54  ALA A C   1 
ATOM   435  O  O   . ALA A 1 54  ? -22.450 7.850   6.331   1.00 14.60  ? 54  ALA A O   1 
ATOM   436  C  CB  . ALA A 1 54  ? -21.395 6.724   9.084   1.00 14.57  ? 54  ALA A CB  1 
ATOM   437  N  N   . THR A 1 55  ? -20.448 8.815   6.793   1.00 12.29  ? 55  THR A N   1 
ATOM   438  C  CA  . THR A 1 55  ? -20.079 9.000   5.382   1.00 11.91  ? 55  THR A CA  1 
ATOM   439  C  C   . THR A 1 55  ? -18.716 8.371   5.150   1.00 10.09  ? 55  THR A C   1 
ATOM   440  O  O   . THR A 1 55  ? -17.683 8.987   5.416   1.00 11.03  ? 55  THR A O   1 
ATOM   441  C  CB  . THR A 1 55  ? -20.007 10.510  5.015   1.00 13.33  ? 55  THR A CB  1 
ATOM   442  O  OG1 . THR A 1 55  ? -21.292 11.079  5.098   1.00 15.55  ? 55  THR A OG1 1 
ATOM   443  C  CG2 . THR A 1 55  ? -19.505 10.753  3.586   1.00 15.90  ? 55  THR A CG2 1 
ATOM   444  N  N   . SER A 1 56  ? -18.722 7.131   4.660   1.00 9.62   ? 56  SER A N   1 
ATOM   445  C  CA  . SER A 1 56  ? -17.451 6.544   4.252   1.00 9.27   ? 56  SER A CA  1 
ATOM   446  C  C   . SER A 1 56  ? -16.959 7.272   2.996   1.00 9.44   ? 56  SER A C   1 
ATOM   447  O  O   . SER A 1 56  ? -17.742 7.677   2.153   1.00 10.69  ? 56  SER A O   1 
ATOM   448  C  CB  . SER A 1 56  ? -17.581 5.021   4.093   1.00 10.15  ? 56  SER A CB  1 
ATOM   449  O  OG  . SER A 1 56  ? -18.387 4.713   2.970   1.00 10.41  ? 56  SER A OG  1 
ATOM   450  N  N   . LEU A 1 57  ? -15.616 7.303   2.819   1.00 9.82   ? 57  LEU A N   1 
ATOM   451  C  CA  . LEU A 1 57  ? -15.035 7.973   1.671   1.00 10.06  ? 57  LEU A CA  1 
ATOM   452  C  C   . LEU A 1 57  ? -14.210 7.014   0.810   1.00 9.29   ? 57  LEU A C   1 
ATOM   453  O  O   . LEU A 1 57  ? -14.379 6.984   -0.389  1.00 11.06  ? 57  LEU A O   1 
ATOM   454  C  CB  . LEU A 1 57  ? -14.144 9.141   2.100   1.00 11.28  ? 57  LEU A CB  1 
ATOM   455  C  CG  . LEU A 1 57  ? -14.960 10.307  2.634   1.00 12.83  ? 57  LEU A CG  1 
ATOM   456  C  CD1 . LEU A 1 57  ? -13.995 11.357  3.183   1.00 15.54  ? 57  LEU A CD1 1 
ATOM   457  C  CD2 . LEU A 1 57  ? -15.930 10.885  1.558   1.00 17.33  ? 57  LEU A CD2 1 
ATOM   458  N  N   . ARG A 1 58  ? -13.224 6.309   1.420   1.00 9.67   ? 58  ARG A N   1 
ATOM   459  C  CA  . ARG A 1 58  ? -12.226 5.567   0.665   1.00 9.50   ? 58  ARG A CA  1 
ATOM   460  C  C   . ARG A 1 58  ? -11.795 4.340   1.460   1.00 9.57   ? 58  ARG A C   1 
ATOM   461  O  O   . ARG A 1 58  ? -11.930 4.311   2.675   1.00 10.92  ? 58  ARG A O   1 
ATOM   462  C  CB  . ARG A 1 58  ? -11.008 6.432   0.359   1.00 11.96  ? 58  ARG A CB  1 
ATOM   463  C  CG  . ARG A 1 58  ? -11.274 7.646   -0.543  1.00 15.73  ? 58  ARG A CG  1 
ATOM   464  C  CD  . ARG A 1 58  ? -10.038 8.311   -1.095  1.00 16.59  ? 58  ARG A CD  1 
ATOM   465  N  NE  . ARG A 1 58  ? -9.268  7.362   -1.930  1.00 15.84  ? 58  ARG A NE  1 
ATOM   466  C  CZ  . ARG A 1 58  ? -9.507  7.117   -3.226  1.00 16.70  ? 58  ARG A CZ  1 
ATOM   467  N  NH1 . ARG A 1 58  ? -10.529 7.699   -3.821  1.00 19.93  ? 58  ARG A NH1 1 
ATOM   468  N  NH2 . ARG A 1 58  ? -8.723  6.293   -3.897  1.00 17.15  ? 58  ARG A NH2 1 
ATOM   469  N  N   . ILE A 1 59  ? -11.161 3.395   0.767   1.00 9.11   ? 59  ILE A N   1 
ATOM   470  C  CA  . ILE A 1 59  ? -10.562 2.212   1.386   1.00 9.12   ? 59  ILE A CA  1 
ATOM   471  C  C   . ILE A 1 59  ? -9.129  2.101   0.852   1.00 9.40   ? 59  ILE A C   1 
ATOM   472  O  O   . ILE A 1 59  ? -8.887  2.359   -0.328  1.00 10.21  ? 59  ILE A O   1 
ATOM   473  C  CB  . ILE A 1 59  ? -11.417 0.943   1.111   1.00 9.55   ? 59  ILE A CB  1 
ATOM   474  C  CG1 . ILE A 1 59  ? -10.972 -0.243  1.998   1.00 10.66  ? 59  ILE A CG1 1 
ATOM   475  C  CG2 . ILE A 1 59  ? -11.501 0.592   -0.388  1.00 10.37  ? 59  ILE A CG2 1 
ATOM   476  C  CD1 . ILE A 1 59  ? -11.889 -1.442  1.896   1.00 12.48  ? 59  ILE A CD1 1 
ATOM   477  N  N   A LEU A 1 60  ? -8.159  1.782   1.754   0.50 10.39  ? 60  LEU A N   1 
ATOM   478  N  N   B LEU A 1 60  ? -8.216  1.666   1.724   0.50 9.75   ? 60  LEU A N   1 
ATOM   479  C  CA  A LEU A 1 60  ? -6.717  1.839   1.437   0.50 9.05   ? 60  LEU A CA  1 
ATOM   480  C  CA  B LEU A 1 60  ? -6.869  1.557   1.190   0.50 10.96  ? 60  LEU A CA  1 
ATOM   481  C  C   A LEU A 1 60  ? -5.977  0.625   2.051   0.50 9.71   ? 60  LEU A C   1 
ATOM   482  C  C   B LEU A 1 60  ? -6.177  0.398   1.909   0.50 8.29   ? 60  LEU A C   1 
ATOM   483  O  O   A LEU A 1 60  ? -6.193  0.284   3.220   0.50 9.87   ? 60  LEU A O   1 
ATOM   484  O  O   B LEU A 1 60  ? -6.583  -0.071  2.974   0.50 9.04   ? 60  LEU A O   1 
ATOM   485  C  CB  A LEU A 1 60  ? -6.067  3.133   1.981   0.50 11.92  ? 60  LEU A CB  1 
ATOM   486  C  CB  B LEU A 1 60  ? -6.035  2.848   1.381   0.50 13.33  ? 60  LEU A CB  1 
ATOM   487  C  CG  A LEU A 1 60  ? -4.528  3.162   2.071   0.50 11.93  ? 60  LEU A CG  1 
ATOM   488  C  CG  B LEU A 1 60  ? -5.863  3.331   2.830   0.50 14.25  ? 60  LEU A CG  1 
ATOM   489  C  CD1 A LEU A 1 60  ? -3.905  3.331   0.693   0.50 14.64  ? 60  LEU A CD1 1 
ATOM   490  C  CD1 B LEU A 1 60  ? -5.281  4.778   2.910   0.50 15.57  ? 60  LEU A CD1 1 
ATOM   491  C  CD2 A LEU A 1 60  ? -4.119  4.268   2.992   0.50 13.82  ? 60  LEU A CD2 1 
ATOM   492  C  CD2 B LEU A 1 60  ? -7.198  3.316   3.491   0.50 25.23  ? 60  LEU A CD2 1 
ATOM   493  N  N   . ASN A 1 61  ? -5.120  -0.048  1.260   1.00 9.25   ? 61  ASN A N   1 
ATOM   494  C  CA  . ASN A 1 61  ? -4.156  -1.036  1.798   1.00 9.20   ? 61  ASN A CA  1 
ATOM   495  C  C   . ASN A 1 61  ? -2.897  -0.223  2.089   1.00 8.78   ? 61  ASN A C   1 
ATOM   496  O  O   . ASN A 1 61  ? -2.280  0.314   1.184   1.00 10.61  ? 61  ASN A O   1 
ATOM   497  C  CB  . ASN A 1 61  ? -3.904  -2.105  0.749   1.00 10.14  ? 61  ASN A CB  1 
ATOM   498  C  CG  . ASN A 1 61  ? -2.852  -3.105  1.150   1.00 10.20  ? 61  ASN A CG  1 
ATOM   499  O  OD1 . ASN A 1 61  ? -1.990  -2.838  2.038   1.00 11.36  ? 61  ASN A OD1 1 
ATOM   500  N  ND2 . ASN A 1 61  ? -2.905  -4.300  0.568   1.00 10.65  ? 61  ASN A ND2 1 
ATOM   501  N  N   . ASN A 1 62  ? -2.533  -0.121  3.370   1.00 9.72   ? 62  ASN A N   1 
ATOM   502  C  CA  . ASN A 1 62  ? -1.362  0.686   3.747   1.00 10.75  ? 62  ASN A CA  1 
ATOM   503  C  C   . ASN A 1 62  ? -0.155  -0.218  4.033   1.00 11.08  ? 62  ASN A C   1 
ATOM   504  O  O   . ASN A 1 62  ? 0.857   0.251   4.627   1.00 14.35  ? 62  ASN A O   1 
ATOM   505  C  CB  . ASN A 1 62  ? -1.640  1.599   4.939   1.00 12.72  ? 62  ASN A CB  1 
ATOM   506  C  CG  . ASN A 1 62  ? -1.995  0.842   6.208   1.00 12.44  ? 62  ASN A CG  1 
ATOM   507  O  OD1 . ASN A 1 62  ? -1.873  -0.371  6.258   1.00 11.76  ? 62  ASN A OD1 1 
ATOM   508  N  ND2 . ASN A 1 62  ? -2.467  1.545   7.213   1.00 19.89  ? 62  ASN A ND2 1 
ATOM   509  N  N   . GLY A 1 63  ? -0.228  -1.510  3.704   1.00 11.74  ? 63  GLY A N   1 
ATOM   510  C  CA  . GLY A 1 63  ? 0.899   -2.407  3.925   1.00 12.51  ? 63  GLY A CA  1 
ATOM   511  C  C   . GLY A 1 63  ? 0.897   -3.029  5.299   1.00 11.36  ? 63  GLY A C   1 
ATOM   512  O  O   . GLY A 1 63  ? 1.725   -3.916  5.536   1.00 14.11  ? 63  GLY A O   1 
ATOM   513  N  N   . HIS A 1 64  ? -0.026  -2.615  6.183   1.00 11.21  ? 64  HIS A N   1 
ATOM   514  C  CA  . HIS A 1 64  ? -0.164  -3.144  7.524   1.00 12.72  ? 64  HIS A CA  1 
ATOM   515  C  C   . HIS A 1 64  ? -1.533  -3.737  7.773   1.00 11.24  ? 64  HIS A C   1 
ATOM   516  O  O   . HIS A 1 64  ? -1.672  -4.736  8.490   1.00 16.51  ? 64  HIS A O   1 
ATOM   517  C  CB  . HIS A 1 64  ? 0.102   -2.078  8.586   1.00 13.66  ? 64  HIS A CB  1 
ATOM   518  C  CG  . HIS A 1 64  ? 1.397   -1.392  8.391   1.00 13.48  ? 64  HIS A CG  1 
ATOM   519  N  ND1 . HIS A 1 64  ? 1.611   -0.059  8.101   1.00 18.49  ? 64  HIS A ND1 1 
ATOM   520  C  CD2 . HIS A 1 64  ? 2.619   -1.961  8.526   1.00 15.34  ? 64  HIS A CD2 1 
ATOM   521  C  CE1 . HIS A 1 64  ? 2.909   0.214   8.135   1.00 17.18  ? 64  HIS A CE1 1 
ATOM   522  N  NE2 . HIS A 1 64  ? 3.562   -0.976  8.331   1.00 19.78  ? 64  HIS A NE2 1 
ATOM   523  N  N   . SER A 1 65  ? -2.546  -3.181  7.153   1.00 10.50  ? 65  SER A N   1 
ATOM   524  C  CA  . SER A 1 65  ? -3.936  -3.583  7.259   1.00 10.41  ? 65  SER A CA  1 
ATOM   525  C  C   . SER A 1 65  ? -4.636  -2.965  6.035   1.00 9.25   ? 65  SER A C   1 
ATOM   526  O  O   . SER A 1 65  ? -3.993  -2.381  5.165   1.00 10.92  ? 65  SER A O   1 
ATOM   527  C  CB  . SER A 1 65  ? -4.555  -3.018  8.577   1.00 12.94  ? 65  SER A CB  1 
ATOM   528  O  OG  . SER A 1 65  ? -5.887  -3.490  8.789   1.00 15.59  ? 65  SER A OG  1 
ATOM   529  N  N   . PHE A 1 66  ? -5.952  -3.068  6.014   1.00 10.11  ? 66  PHE A N   1 
ATOM   530  C  CA  . PHE A 1 66  ? -6.719  -2.173  5.141   1.00 10.74  ? 66  PHE A CA  1 
ATOM   531  C  C   . PHE A 1 66  ? -7.612  -1.320  6.043   1.00 9.87   ? 66  PHE A C   1 
ATOM   532  O  O   . PHE A 1 66  ? -8.072  -1.741  7.109   1.00 10.62  ? 66  PHE A O   1 
ATOM   533  C  CB  . PHE A 1 66  ? -7.530  -2.916  4.078   1.00 11.35  ? 66  PHE A CB  1 
ATOM   534  C  CG  . PHE A 1 66  ? -8.703  -3.731  4.599   1.00 10.76  ? 66  PHE A CG  1 
ATOM   535  C  CD1 . PHE A 1 66  ? -9.930  -3.103  4.749   1.00 11.64  ? 66  PHE A CD1 1 
ATOM   536  C  CD2 . PHE A 1 66  ? -8.567  -5.051  4.979   1.00 11.75  ? 66  PHE A CD2 1 
ATOM   537  C  CE1 . PHE A 1 66  ? -10.982 -3.822  5.257   1.00 12.88  ? 66  PHE A CE1 1 
ATOM   538  C  CE2 . PHE A 1 66  ? -9.643  -5.772  5.463   1.00 12.69  ? 66  PHE A CE2 1 
ATOM   539  C  CZ  . PHE A 1 66  ? -10.881 -5.159  5.613   1.00 12.81  ? 66  PHE A CZ  1 
ATOM   540  N  N   . LYS A 1 67  ? -7.906  -0.080  5.584   1.00 10.99  ? 67  LYS A N   1 
ATOM   541  C  CA  . LYS A 1 67  ? -8.671  0.837   6.395   1.00 10.90  ? 67  LYS A CA  1 
ATOM   542  C  C   . LYS A 1 67  ? -9.690  1.546   5.500   1.00 10.07  ? 67  LYS A C   1 
ATOM   543  O  O   . LYS A 1 67  ? -9.408  1.960   4.372   1.00 11.77  ? 67  LYS A O   1 
ATOM   544  C  CB  . LYS A 1 67  ? -7.751  1.807   7.088   1.00 16.26  ? 67  LYS A CB  1 
ATOM   545  C  CG  . LYS A 1 67  ? -7.018  2.879   6.356   1.00 20.64  ? 67  LYS A CG  1 
ATOM   546  C  CD  . LYS A 1 67  ? -6.511  3.944   7.466   1.00 22.80  ? 67  LYS A CD  1 
ATOM   547  C  CE  . LYS A 1 67  ? -5.485  4.784   6.739   1.00 30.50  ? 67  LYS A CE  1 
ATOM   548  N  NZ  . LYS A 1 67  ? -4.949  5.886   7.554   1.00 41.98  ? 67  LYS A NZ  1 
ATOM   549  N  N   . VAL A 1 68  ? -10.869 1.703   6.105   1.00 9.26   ? 68  VAL A N   1 
ATOM   550  C  CA  . VAL A 1 68  ? -11.953 2.497   5.528   1.00 9.25   ? 68  VAL A CA  1 
ATOM   551  C  C   . VAL A 1 68  ? -11.967 3.829   6.272   1.00 8.99   ? 68  VAL A C   1 
ATOM   552  O  O   . VAL A 1 68  ? -12.065 3.856   7.497   1.00 9.54   ? 68  VAL A O   1 
ATOM   553  C  CB  . VAL A 1 68  ? -13.294 1.781   5.675   1.00 9.86   ? 68  VAL A CB  1 
ATOM   554  C  CG1 . VAL A 1 68  ? -14.427 2.724   5.200   1.00 10.89  ? 68  VAL A CG1 1 
ATOM   555  C  CG2 . VAL A 1 68  ? -13.307 0.499   4.822   1.00 10.51  ? 68  VAL A CG2 1 
ATOM   556  N  N   . GLU A 1 69  ? -11.790 4.922   5.508   1.00 9.15   ? 69  GLU A N   1 
ATOM   557  C  CA  . GLU A 1 69  ? -11.750 6.250   6.094   1.00 9.36   ? 69  GLU A CA  1 
ATOM   558  C  C   . GLU A 1 69  ? -13.061 6.986   5.863   1.00 9.06   ? 69  GLU A C   1 
ATOM   559  O  O   . GLU A 1 69  ? -13.660 6.846   4.782   1.00 11.18  ? 69  GLU A O   1 
ATOM   560  C  CB  . GLU A 1 69  ? -10.588 7.057   5.527   1.00 12.85  ? 69  GLU A CB  1 
ATOM   561  C  CG  . GLU A 1 69  ? -9.280  6.351   5.985   1.00 16.59  ? 69  GLU A CG  1 
ATOM   562  C  CD  . GLU A 1 69  ? -7.992  7.144   5.739   1.00 16.69  ? 69  GLU A CD  1 
ATOM   563  O  OE1 . GLU A 1 69  ? -7.446  7.064   4.680   1.00 17.15  ? 69  GLU A OE1 1 
ATOM   564  O  OE2 . GLU A 1 69  ? -7.533  7.901   6.623   1.00 25.26  ? 69  GLU A OE2 1 
ATOM   565  N  N   . PHE A 1 70  ? -13.462 7.777   6.871   1.00 9.39   ? 70  PHE A N   1 
ATOM   566  C  CA  . PHE A 1 70  ? -14.735 8.492   6.903   1.00 9.67   ? 70  PHE A CA  1 
ATOM   567  C  C   . PHE A 1 70  ? -14.545 9.990   6.818   1.00 10.28  ? 70  PHE A C   1 
ATOM   568  O  O   . PHE A 1 70  ? -13.504 10.534  7.168   1.00 11.91  ? 70  PHE A O   1 
ATOM   569  C  CB  . PHE A 1 70  ? -15.507 8.164   8.191   1.00 9.98   ? 70  PHE A CB  1 
ATOM   570  C  CG  . PHE A 1 70  ? -16.052 6.759   8.176   1.00 9.75   ? 70  PHE A CG  1 
ATOM   571  C  CD1 . PHE A 1 70  ? -15.221 5.664   8.414   1.00 10.51  ? 70  PHE A CD1 1 
ATOM   572  C  CD2 . PHE A 1 70  ? -17.391 6.512   7.884   1.00 10.57  ? 70  PHE A CD2 1 
ATOM   573  C  CE1 . PHE A 1 70  ? -15.683 4.378   8.318   1.00 12.30  ? 70  PHE A CE1 1 
ATOM   574  C  CE2 . PHE A 1 70  ? -17.878 5.211   7.814   1.00 11.10  ? 70  PHE A CE2 1 
ATOM   575  C  CZ  . PHE A 1 70  ? -17.015 4.144   8.017   1.00 11.60  ? 70  PHE A CZ  1 
ATOM   576  N  N   . ASP A 1 71  ? -15.608 10.690  6.346   1.00 10.85  ? 71  ASP A N   1 
ATOM   577  C  CA  . ASP A 1 71  ? -15.637 12.142  6.459   1.00 11.45  ? 71  ASP A CA  1 
ATOM   578  C  C   . ASP A 1 71  ? -15.929 12.497  7.902   1.00 11.34  ? 71  ASP A C   1 
ATOM   579  O  O   . ASP A 1 71  ? -17.045 12.303  8.400   1.00 14.96  ? 71  ASP A O   1 
ATOM   580  C  CB  . ASP A 1 71  ? -16.747 12.674  5.545   1.00 13.97  ? 71  ASP A CB  1 
ATOM   581  C  CG  . ASP A 1 71  ? -16.754 14.214  5.529   1.00 17.01  ? 71  ASP A CG  1 
ATOM   582  O  OD1 . ASP A 1 71  ? -16.111 14.832  6.380   1.00 15.34  ? 71  ASP A OD1 1 
ATOM   583  O  OD2 . ASP A 1 71  ? -17.450 14.782  4.632   1.00 22.21  ? 71  ASP A OD2 1 
ATOM   584  N  N   . ASP A 1 72  ? -14.934 12.971  8.584   1.00 11.35  ? 72  ASP A N   1 
ATOM   585  C  CA  . ASP A 1 72  ? -15.022 13.328  10.013  1.00 11.94  ? 72  ASP A CA  1 
ATOM   586  C  C   . ASP A 1 72  ? -14.956 14.863  10.203  1.00 13.29  ? 72  ASP A C   1 
ATOM   587  O  O   . ASP A 1 72  ? -14.505 15.352  11.258  1.00 15.07  ? 72  ASP A O   1 
ATOM   588  C  CB  . ASP A 1 72  ? -13.965 12.626  10.885  1.00 11.93  ? 72  ASP A CB  1 
ATOM   589  C  CG  . ASP A 1 72  ? -12.539 12.908  10.474  1.00 13.56  ? 72  ASP A CG  1 
ATOM   590  O  OD1 . ASP A 1 72  ? -12.332 13.645  9.468   1.00 15.05  ? 72  ASP A OD1 1 
ATOM   591  O  OD2 . ASP A 1 72  ? -11.640 12.391  11.133  1.00 16.26  ? 72  ASP A OD2 1 
ATOM   592  N  N   . SER A 1 73  ? -15.322 15.621  9.157   1.00 13.89  ? 73  SER A N   1 
ATOM   593  C  CA  . SER A 1 73  ? -15.275 17.088  9.217   1.00 15.31  ? 73  SER A CA  1 
ATOM   594  C  C   . SER A 1 73  ? -16.539 17.697  9.824   1.00 17.72  ? 73  SER A C   1 
ATOM   595  O  O   . SER A 1 73  ? -16.611 18.952  9.929   1.00 20.11  ? 73  SER A O   1 
ATOM   596  C  CB  . SER A 1 73  ? -14.997 17.602  7.860   1.00 18.69  ? 73  SER A CB  1 
ATOM   597  O  OG  . SER A 1 73  ? -16.191 17.494  7.048   1.00 16.16  ? 73  SER A OG  1 
ATOM   598  N  N   . GLN A 1 74  ? -17.528 16.892  10.249  1.00 18.14  ? 74  GLN A N   1 
ATOM   599  C  CA  . GLN A 1 74  ? -18.716 17.326  10.952  1.00 21.41  ? 74  GLN A CA  1 
ATOM   600  C  C   . GLN A 1 74  ? -19.161 16.210  11.870  1.00 18.05  ? 74  GLN A C   1 
ATOM   601  O  O   . GLN A 1 74  ? -18.668 15.100  11.727  1.00 17.09  ? 74  GLN A O   1 
ATOM   602  C  CB  . GLN A 1 74  ? -19.922 17.504  9.993   1.00 33.97  ? 74  GLN A CB  1 
ATOM   603  C  CG  . GLN A 1 74  ? -19.622 18.321  8.752   1.00 44.58  ? 74  GLN A CG  1 
ATOM   604  C  CD  . GLN A 1 74  ? -20.227 17.843  7.444   1.00 47.58  ? 74  GLN A CD  1 
ATOM   605  O  OE1 . GLN A 1 74  ? -21.448 17.701  7.341   1.00 34.65  ? 74  GLN A OE1 1 
ATOM   606  N  NE2 . GLN A 1 74  ? -19.375 17.641  6.423   1.00 31.95  ? 74  GLN A NE2 1 
ATOM   607  N  N   . ASP A 1 75  ? -20.125 16.503  12.768  1.00 25.81  ? 75  ASP A N   1 
ATOM   608  C  CA  . ASP A 1 75  ? -20.633 15.502  13.683  1.00 29.23  ? 75  ASP A CA  1 
ATOM   609  C  C   . ASP A 1 75  ? -21.556 14.619  12.901  1.00 23.55  ? 75  ASP A C   1 
ATOM   610  O  O   . ASP A 1 75  ? -22.641 15.061  12.525  1.00 32.02  ? 75  ASP A O   1 
ATOM   611  C  CB  . ASP A 1 75  ? -21.497 16.042  14.825  1.00 53.47  ? 75  ASP A CB  1 
ATOM   612  C  CG  . ASP A 1 75  ? -20.720 16.278  16.109  1.00 43.29  ? 75  ASP A CG  1 
ATOM   613  O  OD1 . ASP A 1 75  ? -19.548 15.857  16.169  1.00 54.36  ? 75  ASP A OD1 1 
ATOM   614  O  OD2 . ASP A 1 75  ? -21.294 16.882  17.037  1.00 50.14  ? 75  ASP A OD2 1 
ATOM   615  N  N   . LYS A 1 76  ? -21.024 13.497  12.486  1.00 19.85  ? 76  LYS A N   1 
ATOM   616  C  CA  . LYS A 1 76  ? -21.794 12.489  11.746  1.00 23.66  ? 76  LYS A CA  1 
ATOM   617  C  C   . LYS A 1 76  ? -21.958 11.271  12.660  1.00 36.99  ? 76  LYS A C   1 
ATOM   618  O  O   . LYS A 1 76  ? -22.791 11.247  13.545  1.00 41.61  ? 76  LYS A O   1 
ATOM   619  C  CB  . LYS A 1 76  ? -21.177 12.239  10.359  1.00 25.46  ? 76  LYS A CB  1 
ATOM   620  C  CG  . LYS A 1 76  ? -21.341 13.355  9.348   1.00 29.44  ? 76  LYS A CG  1 
ATOM   621  C  CD  . LYS A 1 76  ? -20.710 13.079  8.035   1.00 21.06  ? 76  LYS A CD  1 
ATOM   622  C  CE  . LYS A 1 76  ? -21.324 14.092  7.125   1.00 36.65  ? 76  LYS A CE  1 
ATOM   623  N  NZ  . LYS A 1 76  ? -21.305 13.633  5.717   1.00 32.23  ? 76  LYS A NZ  1 
ATOM   624  N  N   . ALA A 1 77  ? -21.014 10.387  12.579  1.00 22.32  ? 77  ALA A N   1 
ATOM   625  C  CA  . ALA A 1 77  ? -20.872 9.059   13.229  1.00 15.34  ? 77  ALA A CA  1 
ATOM   626  C  C   . ALA A 1 77  ? -20.062 9.237   14.509  1.00 14.59  ? 77  ALA A C   1 
ATOM   627  O  O   . ALA A 1 77  ? -18.848 9.456   14.504  1.00 19.80  ? 77  ALA A O   1 
ATOM   628  C  CB  . ALA A 1 77  ? -20.208 8.090   12.283  1.00 17.70  ? 77  ALA A CB  1 
ATOM   629  N  N   . VAL A 1 78  ? -20.757 9.225   15.629  1.00 14.11  ? 78  VAL A N   1 
ATOM   630  C  CA  . VAL A 1 78  ? -20.135 9.563   16.891  1.00 16.07  ? 78  VAL A CA  1 
ATOM   631  C  C   . VAL A 1 78  ? -20.407 8.501   17.971  1.00 13.66  ? 78  VAL A C   1 
ATOM   632  O  O   . VAL A 1 78  ? -21.447 7.838   18.018  1.00 17.05  ? 78  VAL A O   1 
ATOM   633  C  CB  . VAL A 1 78  ? -20.446 10.968  17.380  1.00 18.70  ? 78  VAL A CB  1 
ATOM   634  C  CG1 . VAL A 1 78  ? -20.332 12.055  16.331  1.00 23.08  ? 78  VAL A CG1 1 
ATOM   635  C  CG2 . VAL A 1 78  ? -21.806 10.963  17.918  1.00 22.01  ? 78  VAL A CG2 1 
ATOM   636  N  N   . LEU A 1 79  ? -19.437 8.395   18.838  1.00 12.58  ? 79  LEU A N   1 
ATOM   637  C  CA  . LEU A 1 79  ? -19.468 7.554   20.025  1.00 12.91  ? 79  LEU A CA  1 
ATOM   638  C  C   . LEU A 1 79  ? -19.508 8.462   21.256  1.00 13.74  ? 79  LEU A C   1 
ATOM   639  O  O   . LEU A 1 79  ? -18.673 9.412   21.337  1.00 16.79  ? 79  LEU A O   1 
ATOM   640  C  CB  . LEU A 1 79  ? -18.179 6.686   19.991  1.00 16.38  ? 79  LEU A CB  1 
ATOM   641  C  CG  . LEU A 1 79  ? -18.009 5.554   20.980  1.00 15.76  ? 79  LEU A CG  1 
ATOM   642  C  CD1 . LEU A 1 79  ? -19.037 4.458   20.743  1.00 23.03  ? 79  LEU A CD1 1 
ATOM   643  C  CD2 . LEU A 1 79  ? -16.625 4.975   20.828  1.00 16.27  ? 79  LEU A CD2 1 
ATOM   644  N  N   . LYS A 1 80  ? -20.346 8.135   22.223  1.00 15.44  ? 80  LYS A N   1 
ATOM   645  C  CA  . LYS A 1 80  ? -20.309 8.834   23.503  1.00 17.51  ? 80  LYS A CA  1 
ATOM   646  C  C   . LYS A 1 80  ? -20.852 7.888   24.571  1.00 16.16  ? 80  LYS A C   1 
ATOM   647  O  O   . LYS A 1 80  ? -21.178 6.723   24.286  1.00 16.87  ? 80  LYS A O   1 
ATOM   648  C  CB  . LYS A 1 80  ? -21.099 10.118  23.468  1.00 23.72  ? 80  LYS A CB  1 
ATOM   649  C  CG  . LYS A 1 80  ? -22.580 9.955   23.263  1.00 26.68  ? 80  LYS A CG  1 
ATOM   650  C  CD  . LYS A 1 80  ? -23.157 11.346  22.939  1.00 32.81  ? 80  LYS A CD  1 
ATOM   651  N  N   . GLY A 1 81  ? -20.956 8.399   25.800  1.00 17.94  ? 81  GLY A N   1 
ATOM   652  C  CA  . GLY A 1 81  ? -21.426 7.605   26.915  1.00 18.20  ? 81  GLY A CA  1 
ATOM   653  C  C   . GLY A 1 81  ? -20.380 6.541   27.256  1.00 17.00  ? 81  GLY A C   1 
ATOM   654  O  O   . GLY A 1 81  ? -19.193 6.728   27.007  1.00 16.88  ? 81  GLY A O   1 
ATOM   655  N  N   . GLY A 1 82  ? -20.847 5.461   27.857  1.00 20.44  ? 82  GLY A N   1 
ATOM   656  C  CA  . GLY A 1 82  ? -19.923 4.425   28.258  1.00 22.03  ? 82  GLY A CA  1 
ATOM   657  C  C   . GLY A 1 82  ? -18.982 5.054   29.276  1.00 20.19  ? 82  GLY A C   1 
ATOM   658  O  O   . GLY A 1 82  ? -19.385 5.822   30.142  1.00 26.57  ? 82  GLY A O   1 
ATOM   659  N  N   . PRO A 1 83  ? -17.660 4.804   29.149  1.00 18.20  ? 83  PRO A N   1 
ATOM   660  C  CA  . PRO A 1 83  ? -16.693 5.410   30.069  1.00 18.45  ? 83  PRO A CA  1 
ATOM   661  C  C   . PRO A 1 83  ? -16.297 6.807   29.597  1.00 16.98  ? 83  PRO A C   1 
ATOM   662  O  O   . PRO A 1 83  ? -15.444 7.414   30.234  1.00 23.03  ? 83  PRO A O   1 
ATOM   663  C  CB  . PRO A 1 83  ? -15.439 4.482   29.869  1.00 18.52  ? 83  PRO A CB  1 
ATOM   664  C  CG  . PRO A 1 83  ? -15.542 4.116   28.409  1.00 16.63  ? 83  PRO A CG  1 
ATOM   665  C  CD  . PRO A 1 83  ? -17.001 3.926   28.146  1.00 18.03  ? 83  PRO A CD  1 
ATOM   666  N  N   . LEU A 1 84  ? -16.845 7.312   28.477  1.00 14.93  ? 84  LEU A N   1 
ATOM   667  C  CA  . LEU A 1 84  ? -16.268 8.505   27.874  1.00 14.33  ? 84  LEU A CA  1 
ATOM   668  C  C   . LEU A 1 84  ? -16.933 9.762   28.433  1.00 15.30  ? 84  LEU A C   1 
ATOM   669  O  O   . LEU A 1 84  ? -18.117 9.758   28.762  1.00 18.12  ? 84  LEU A O   1 
ATOM   670  C  CB  . LEU A 1 84  ? -16.594 8.455   26.377  1.00 13.47  ? 84  LEU A CB  1 
ATOM   671  C  CG  . LEU A 1 84  ? -16.031 7.231   25.660  1.00 13.05  ? 84  LEU A CG  1 
ATOM   672  C  CD1 . LEU A 1 84  ? -16.534 7.159   24.220  1.00 15.83  ? 84  LEU A CD1 1 
ATOM   673  C  CD2 . LEU A 1 84  ? -14.490 7.218   25.714  1.00 14.48  ? 84  LEU A CD2 1 
ATOM   674  N  N   . ASP A 1 85  ? -16.170 10.870  28.461  1.00 19.23  ? 85  ASP A N   1 
ATOM   675  C  CA  . ASP A 1 85  ? -16.645 12.233  28.745  1.00 21.31  ? 85  ASP A CA  1 
ATOM   676  C  C   . ASP A 1 85  ? -16.566 12.904  27.380  1.00 23.76  ? 85  ASP A C   1 
ATOM   677  O  O   . ASP A 1 85  ? -15.539 12.833  26.694  1.00 28.32  ? 85  ASP A O   1 
ATOM   678  C  CB  . ASP A 1 85  ? -15.729 12.923  29.776  1.00 29.57  ? 85  ASP A CB  1 
ATOM   679  C  CG  . ASP A 1 85  ? -15.880 12.419  31.216  1.00 47.57  ? 85  ASP A CG  1 
ATOM   680  O  OD1 . ASP A 1 85  ? -16.950 11.793  31.574  1.00 47.01  ? 85  ASP A OD1 1 
ATOM   681  O  OD2 . ASP A 1 85  ? -14.932 12.696  32.004  1.00 51.56  ? 85  ASP A OD2 1 
ATOM   682  N  N   . GLY A 1 86  ? -17.651 13.505  26.962  1.00 27.81  ? 86  GLY A N   1 
ATOM   683  C  CA  . GLY A 1 86  ? -17.749 14.185  25.688  1.00 24.95  ? 86  GLY A CA  1 
ATOM   684  C  C   . GLY A 1 86  ? -18.006 13.252  24.482  1.00 21.24  ? 86  GLY A C   1 
ATOM   685  O  O   . GLY A 1 86  ? -18.484 12.119  24.627  1.00 26.27  ? 86  GLY A O   1 
ATOM   686  N  N   . THR A 1 87  ? -17.746 13.755  23.257  1.00 19.06  ? 87  THR A N   1 
ATOM   687  C  CA  . THR A 1 87  ? -18.203 13.203  21.977  1.00 17.88  ? 87  THR A CA  1 
ATOM   688  C  C   . THR A 1 87  ? -16.961 12.829  21.149  1.00 15.75  ? 87  THR A C   1 
ATOM   689  O  O   . THR A 1 87  ? -16.028 13.624  21.061  1.00 16.33  ? 87  THR A O   1 
ATOM   690  C  CB  . THR A 1 87  ? -18.963 14.368  21.268  1.00 30.40  ? 87  THR A CB  1 
ATOM   691  O  OG1 . THR A 1 87  ? -20.173 14.506  21.968  1.00 41.91  ? 87  THR A OG1 1 
ATOM   692  C  CG2 . THR A 1 87  ? -19.340 13.990  19.834  1.00 26.67  ? 87  THR A CG2 1 
ATOM   693  N  N   . TYR A 1 88  ? -16.950 11.614  20.589  1.00 14.65  ? 88  TYR A N   1 
ATOM   694  C  CA  . TYR A 1 88  ? -15.824 11.136  19.781  1.00 13.22  ? 88  TYR A CA  1 
ATOM   695  C  C   . TYR A 1 88  ? -16.307 10.846  18.357  1.00 12.95  ? 88  TYR A C   1 
ATOM   696  O  O   . TYR A 1 88  ? -17.267 10.099  18.202  1.00 18.13  ? 88  TYR A O   1 
ATOM   697  C  CB  . TYR A 1 88  ? -15.230 9.886   20.455  1.00 13.32  ? 88  TYR A CB  1 
ATOM   698  C  CG  . TYR A 1 88  ? -14.460 10.126  21.735  1.00 11.89  ? 88  TYR A CG  1 
ATOM   699  C  CD1 . TYR A 1 88  ? -15.078 10.524  22.921  1.00 12.75  ? 88  TYR A CD1 1 
ATOM   700  C  CD2 . TYR A 1 88  ? -13.083 9.856   21.769  1.00 11.33  ? 88  TYR A CD2 1 
ATOM   701  C  CE1 . TYR A 1 88  ? -14.357 10.717  24.075  1.00 12.33  ? 88  TYR A CE1 1 
ATOM   702  C  CE2 . TYR A 1 88  ? -12.358 9.999   22.929  1.00 11.45  ? 88  TYR A CE2 1 
ATOM   703  C  CZ  . TYR A 1 88  ? -12.983 10.439  24.093  1.00 11.43  ? 88  TYR A CZ  1 
ATOM   704  O  OH  . TYR A 1 88  ? -12.301 10.520  25.271  1.00 13.13  ? 88  TYR A OH  1 
ATOM   705  N  N   A ARG A 1 89  ? -15.701 11.481  17.296  0.50 13.63  ? 89  ARG A N   1 
ATOM   706  N  N   B ARG A 1 89  ? -15.540 11.222  17.387  0.50 12.30  ? 89  ARG A N   1 
ATOM   707  C  CA  A ARG A 1 89  ? -15.957 11.322  15.846  0.50 10.94  ? 89  ARG A CA  1 
ATOM   708  C  CA  B ARG A 1 89  ? -16.142 11.052  16.106  0.50 12.28  ? 89  ARG A CA  1 
ATOM   709  C  C   A ARG A 1 89  ? -15.268 10.082  15.253  0.50 10.00  ? 89  ARG A C   1 
ATOM   710  C  C   B ARG A 1 89  ? -15.322 10.029  15.339  0.50 9.96   ? 89  ARG A C   1 
ATOM   711  O  O   A ARG A 1 89  ? -14.051 9.922   15.369  0.50 9.82   ? 89  ARG A O   1 
ATOM   712  O  O   B ARG A 1 89  ? -14.100 9.971   15.460  0.50 9.50   ? 89  ARG A O   1 
ATOM   713  C  CB  A ARG A 1 89  ? -15.463 12.514  15.003  0.50 14.05  ? 89  ARG A CB  1 
ATOM   714  C  CB  B ARG A 1 89  ? -16.001 12.454  15.561  0.50 11.15  ? 89  ARG A CB  1 
ATOM   715  C  CG  A ARG A 1 89  ? -16.318 13.779  15.116  0.50 14.03  ? 89  ARG A CG  1 
ATOM   716  C  CG  B ARG A 1 89  ? -16.575 12.565  14.181  0.50 12.21  ? 89  ARG A CG  1 
ATOM   717  C  CD  A ARG A 1 89  ? -15.977 14.810  14.072  0.50 12.30  ? 89  ARG A CD  1 
ATOM   718  C  CD  B ARG A 1 89  ? -16.376 13.963  13.631  0.50 12.14  ? 89  ARG A CD  1 
ATOM   719  N  NE  A ARG A 1 89  ? -16.673 16.078  14.368  0.50 13.30  ? 89  ARG A NE  1 
ATOM   720  N  NE  B ARG A 1 89  ? -17.107 14.907  14.454  0.50 12.84  ? 89  ARG A NE  1 
ATOM   721  C  CZ  A ARG A 1 89  ? -16.280 17.306  13.963  0.50 13.28  ? 89  ARG A CZ  1 
ATOM   722  C  CZ  B ARG A 1 89  ? -16.942 16.220  14.277  0.50 11.35  ? 89  ARG A CZ  1 
ATOM   723  N  NH1 A ARG A 1 89  ? -15.243 17.428  13.140  0.50 14.20  ? 89  ARG A NH1 1 
ATOM   724  N  NH1 B ARG A 1 89  ? -16.081 16.684  13.379  0.50 13.15  ? 89  ARG A NH1 1 
ATOM   725  N  NH2 A ARG A 1 89  ? -16.961 18.392  14.307  0.50 18.35  ? 89  ARG A NH2 1 
ATOM   726  N  NH2 B ARG A 1 89  ? -17.563 17.114  15.032  0.50 12.93  ? 89  ARG A NH2 1 
ATOM   727  N  N   . LEU A 1 90  ? -16.049 9.191   14.572  1.00 9.76   ? 90  LEU A N   1 
ATOM   728  C  CA  . LEU A 1 90  ? -15.441 8.096   13.835  1.00 9.59   ? 90  LEU A CA  1 
ATOM   729  C  C   . LEU A 1 90  ? -14.580 8.644   12.694  1.00 10.18  ? 90  LEU A C   1 
ATOM   730  O  O   . LEU A 1 90  ? -15.081 9.410   11.852  1.00 12.11  ? 90  LEU A O   1 
ATOM   731  C  CB  . LEU A 1 90  ? -16.564 7.217   13.273  1.00 10.35  ? 90  LEU A CB  1 
ATOM   732  C  CG  . LEU A 1 90  ? -16.101 6.018   12.408  1.00 10.22  ? 90  LEU A CG  1 
ATOM   733  C  CD1 . LEU A 1 90  ? -15.330 4.989   13.235  1.00 10.73  ? 90  LEU A CD1 1 
ATOM   734  C  CD2 . LEU A 1 90  ? -17.295 5.372   11.743  1.00 12.57  ? 90  LEU A CD2 1 
ATOM   735  N  N   . THR A 1 91  ? -13.328 8.190   12.609  1.00 9.60   ? 91  THR A N   1 
ATOM   736  C  CA  . THR A 1 91  ? -12.446 8.563   11.519  1.00 10.19  ? 91  THR A CA  1 
ATOM   737  C  C   . THR A 1 91  ? -12.110 7.400   10.601  1.00 9.54   ? 91  THR A C   1 
ATOM   738  O  O   . THR A 1 91  ? -11.996 7.605   9.388   1.00 10.03  ? 91  THR A O   1 
ATOM   739  C  CB  . THR A 1 91  ? -11.192 9.264   12.059  1.00 11.92  ? 91  THR A CB  1 
ATOM   740  O  OG1 . THR A 1 91  ? -10.392 9.681   10.933  1.00 16.31  ? 91  THR A OG1 1 
ATOM   741  C  CG2 . THR A 1 91  ? -10.356 8.423   12.999  1.00 12.49  ? 91  THR A CG2 1 
ATOM   742  N  N   . GLN A 1 92  ? -11.986 6.164   11.115  1.00 8.99   ? 92  GLN A N   1 
ATOM   743  C  CA  . GLN A 1 92  ? -11.623 5.021   10.251  1.00 8.73   ? 92  GLN A CA  1 
ATOM   744  C  C   . GLN A 1 92  ? -11.999 3.748   10.958  1.00 8.41   ? 92  GLN A C   1 
ATOM   745  O  O   . GLN A 1 92  ? -12.086 3.758   12.212  1.00 9.01   ? 92  GLN A O   1 
ATOM   746  C  CB  . GLN A 1 92  ? -10.119 5.032   9.881   1.00 10.21  ? 92  GLN A CB  1 
ATOM   747  C  CG  . GLN A 1 92  ? -9.228  5.107   11.118  1.00 12.37  ? 92  GLN A CG  1 
ATOM   748  C  CD  . GLN A 1 92  ? -8.297  3.962   11.198  1.00 14.58  ? 92  GLN A CD  1 
ATOM   749  O  OE1 . GLN A 1 92  ? -8.753  2.829   11.043  1.00 17.93  ? 92  GLN A OE1 1 
ATOM   750  N  NE2 . GLN A 1 92  ? -7.091  4.203   11.662  1.00 22.39  ? 92  GLN A NE2 1 
ATOM   751  N  N   . PHE A 1 93  ? -12.105 2.671   10.209  1.00 8.07   ? 93  PHE A N   1 
ATOM   752  C  CA  . PHE A 1 93  ? -11.995 1.367   10.839  1.00 8.35   ? 93  PHE A CA  1 
ATOM   753  C  C   . PHE A 1 93  ? -11.013 0.514   10.021  1.00 7.85   ? 93  PHE A C   1 
ATOM   754  O  O   . PHE A 1 93  ? -10.766 0.744   8.843   1.00 8.49   ? 93  PHE A O   1 
ATOM   755  C  CB  . PHE A 1 93  ? -13.356 0.654   11.026  1.00 8.03   ? 93  PHE A CB  1 
ATOM   756  C  CG  . PHE A 1 93  ? -14.055 0.231   9.763   1.00 8.54   ? 93  PHE A CG  1 
ATOM   757  C  CD1 . PHE A 1 93  ? -13.670 -0.917  9.073   1.00 9.06   ? 93  PHE A CD1 1 
ATOM   758  C  CD2 . PHE A 1 93  ? -15.180 0.933   9.322   1.00 8.90   ? 93  PHE A CD2 1 
ATOM   759  C  CE1 . PHE A 1 93  ? -14.339 -1.287  7.906   1.00 9.75   ? 93  PHE A CE1 1 
ATOM   760  C  CE2 . PHE A 1 93  ? -15.895 0.522   8.203   1.00 9.55   ? 93  PHE A CE2 1 
ATOM   761  C  CZ  . PHE A 1 93  ? -15.472 -0.578  7.478   1.00 10.00  ? 93  PHE A CZ  1 
ATOM   762  N  N   . HIS A 1 94  ? -10.491 -0.510  10.707  1.00 8.00   ? 94  HIS A N   1 
ATOM   763  C  CA  . HIS A 1 94  ? -9.596  -1.474  10.074  1.00 7.87   ? 94  HIS A CA  1 
ATOM   764  C  C   . HIS A 1 94  ? -9.666  -2.760  10.884  1.00 7.31   ? 94  HIS A C   1 
ATOM   765  O  O   . HIS A 1 94  ? -10.333 -2.814  11.922  1.00 8.10   ? 94  HIS A O   1 
ATOM   766  C  CB  . HIS A 1 94  ? -8.149  -0.899  10.069  1.00 8.32   ? 94  HIS A CB  1 
ATOM   767  C  CG  . HIS A 1 94  ? -7.633  -0.689  11.444  1.00 7.89   ? 94  HIS A CG  1 
ATOM   768  N  ND1 . HIS A 1 94  ? -7.746  0.532   12.109  1.00 8.52   ? 94  HIS A ND1 1 
ATOM   769  C  CD2 . HIS A 1 94  ? -7.048  -1.523  12.335  1.00 8.15   ? 94  HIS A CD2 1 
ATOM   770  C  CE1 . HIS A 1 94  ? -7.259  0.413   13.322  1.00 8.79   ? 94  HIS A CE1 1 
ATOM   771  N  NE2 . HIS A 1 94  ? -6.838  -0.890  13.534  1.00 7.94   ? 94  HIS A NE2 1 
ATOM   772  N  N   . PHE A 1 95  ? -8.945  -3.775  10.458  1.00 8.15   ? 95  PHE A N   1 
ATOM   773  C  CA  . PHE A 1 95  ? -8.972  -5.083  11.108  1.00 8.31   ? 95  PHE A CA  1 
ATOM   774  C  C   . PHE A 1 95  ? -7.549  -5.570  11.365  1.00 7.81   ? 95  PHE A C   1 
ATOM   775  O  O   . PHE A 1 95  ? -6.609  -5.167  10.700  1.00 9.15   ? 95  PHE A O   1 
ATOM   776  C  CB  . PHE A 1 95  ? -9.676  -6.126  10.209  1.00 9.52   ? 95  PHE A CB  1 
ATOM   777  C  CG  . PHE A 1 95  ? -11.158 -5.837  9.953   1.00 9.06   ? 95  PHE A CG  1 
ATOM   778  C  CD1 . PHE A 1 95  ? -11.523 -4.964  8.920   1.00 10.04  ? 95  PHE A CD1 1 
ATOM   779  C  CD2 . PHE A 1 95  ? -12.150 -6.513  10.644  1.00 9.99   ? 95  PHE A CD2 1 
ATOM   780  C  CE1 . PHE A 1 95  ? -12.868 -4.740  8.629   1.00 10.76  ? 95  PHE A CE1 1 
ATOM   781  C  CE2 . PHE A 1 95  ? -13.483 -6.315  10.317  1.00 10.54  ? 95  PHE A CE2 1 
ATOM   782  C  CZ  . PHE A 1 95  ? -13.849 -5.417  9.313   1.00 10.83  ? 95  PHE A CZ  1 
ATOM   783  N  N   . HIS A 1 96  ? -7.462  -6.543  12.255  1.00 7.99   ? 96  HIS A N   1 
ATOM   784  C  CA  . HIS A 1 96  ? -6.266  -7.369  12.426  1.00 8.17   ? 96  HIS A CA  1 
ATOM   785  C  C   . HIS A 1 96  ? -6.756  -8.801  12.351  1.00 7.96   ? 96  HIS A C   1 
ATOM   786  O  O   . HIS A 1 96  ? -7.845  -9.138  12.849  1.00 8.60   ? 96  HIS A O   1 
ATOM   787  C  CB  . HIS A 1 96  ? -5.658  -7.132  13.817  1.00 8.16   ? 96  HIS A CB  1 
ATOM   788  C  CG  . HIS A 1 96  ? -5.354  -5.685  14.080  1.00 8.11   ? 96  HIS A CG  1 
ATOM   789  N  ND1 . HIS A 1 96  ? -4.123  -5.110  13.856  1.00 9.11   ? 96  HIS A ND1 1 
ATOM   790  C  CD2 . HIS A 1 96  ? -6.142  -4.670  14.528  1.00 8.13   ? 96  HIS A CD2 1 
ATOM   791  C  CE1 . HIS A 1 96  ? -4.173  -3.802  14.175  1.00 9.35   ? 96  HIS A CE1 1 
ATOM   792  N  NE2 . HIS A 1 96  ? -5.414  -3.467  14.534  1.00 8.59   ? 96  HIS A NE2 1 
ATOM   793  N  N   . TRP A 1 97  ? -5.971  -9.707  11.726  1.00 8.06   ? 97  TRP A N   1 
ATOM   794  C  CA  . TRP A 1 97  ? -6.432  -11.083 11.543  1.00 8.06   ? 97  TRP A CA  1 
ATOM   795  C  C   . TRP A 1 97  ? -5.229  -12.025 11.439  1.00 7.98   ? 97  TRP A C   1 
ATOM   796  O  O   . TRP A 1 97  ? -4.049  -11.585 11.365  1.00 9.45   ? 97  TRP A O   1 
ATOM   797  C  CB  . TRP A 1 97  ? -7.316  -11.194 10.302  1.00 8.60   ? 97  TRP A CB  1 
ATOM   798  C  CG  . TRP A 1 97  ? -6.652  -10.852 9.001   1.00 8.08   ? 97  TRP A CG  1 
ATOM   799  C  CD1 . TRP A 1 97  ? -5.977  -11.715 8.176   1.00 9.41   ? 97  TRP A CD1 1 
ATOM   800  C  CD2 . TRP A 1 97  ? -6.568  -9.546  8.403   1.00 8.33   ? 97  TRP A CD2 1 
ATOM   801  N  NE1 . TRP A 1 97  ? -5.476  -11.038 7.083   1.00 9.46   ? 97  TRP A NE1 1 
ATOM   802  C  CE2 . TRP A 1 97  ? -5.829  -9.704  7.205   1.00 9.00   ? 97  TRP A CE2 1 
ATOM   803  C  CE3 . TRP A 1 97  ? -7.044  -8.270  8.768   1.00 8.85   ? 97  TRP A CE3 1 
ATOM   804  C  CZ2 . TRP A 1 97  ? -5.587  -8.624  6.338   1.00 9.76   ? 97  TRP A CZ2 1 
ATOM   805  C  CZ3 . TRP A 1 97  ? -6.792  -7.209  7.905   1.00 9.50   ? 97  TRP A CZ3 1 
ATOM   806  C  CH2 . TRP A 1 97  ? -6.061  -7.374  6.717   1.00 9.41   ? 97  TRP A CH2 1 
ATOM   807  N  N   . GLY A 1 98  ? -5.528  -13.308 11.449  1.00 9.07   ? 98  GLY A N   1 
ATOM   808  C  CA  . GLY A 1 98  ? -4.526  -14.357 11.529  1.00 10.05  ? 98  GLY A CA  1 
ATOM   809  C  C   . GLY A 1 98  ? -4.365  -15.100 10.228  1.00 10.01  ? 98  GLY A C   1 
ATOM   810  O  O   . GLY A 1 98  ? -5.097  -14.933 9.229   1.00 11.04  ? 98  GLY A O   1 
ATOM   811  N  N   . SER A 1 99  ? -3.345  -15.965 10.220  1.00 10.88  ? 99  SER A N   1 
ATOM   812  C  CA  . SER A 1 99  ? -3.160  -16.944 9.158   1.00 12.34  ? 99  SER A CA  1 
ATOM   813  C  C   . SER A 1 99  ? -4.094  -18.157 9.298   1.00 12.14  ? 99  SER A C   1 
ATOM   814  O  O   . SER A 1 99  ? -4.288  -18.856 8.324   1.00 16.91  ? 99  SER A O   1 
ATOM   815  C  CB  . SER A 1 99  ? -1.696  -17.384 9.136   1.00 13.99  ? 99  SER A CB  1 
ATOM   816  O  OG  . SER A 1 99  ? -1.256  -17.779 10.419  1.00 13.24  ? 99  SER A OG  1 
ATOM   817  N  N   . LEU A 1 100 ? -4.566  -18.370 10.523  1.00 12.34  ? 100 LEU A N   1 
ATOM   818  C  CA  . LEU A 1 100 ? -5.498  -19.477 10.837  1.00 16.14  ? 100 LEU A CA  1 
ATOM   819  C  C   . LEU A 1 100 ? -6.518  -19.002 11.829  1.00 12.95  ? 100 LEU A C   1 
ATOM   820  O  O   . LEU A 1 100 ? -6.290  -17.965 12.464  1.00 14.00  ? 100 LEU A O   1 
ATOM   821  C  CB  . LEU A 1 100 ? -4.699  -20.688 11.452  1.00 46.70  ? 100 LEU A CB  1 
ATOM   822  C  CG  . LEU A 1 100 ? -3.979  -21.578 10.297  1.00 104.48 ? 100 LEU A CG  1 
ATOM   823  C  CD1 . LEU A 1 100 ? -3.121  -22.673 10.912  1.00 78.05  ? 100 LEU A CD1 1 
ATOM   824  C  CD2 . LEU A 1 100 ? -5.010  -22.177 9.353   1.00 80.97  ? 100 LEU A CD2 1 
ATOM   825  N  N   . ASP A 1 101 ? -7.654  -19.727 11.965  1.00 13.25  ? 101 ASP A N   1 
ATOM   826  C  CA  . ASP A 1 101 ? -8.766  -19.102 12.681  1.00 13.01  ? 101 ASP A CA  1 
ATOM   827  C  C   . ASP A 1 101 ? -8.512  -19.011 14.176  1.00 12.91  ? 101 ASP A C   1 
ATOM   828  O  O   . ASP A 1 101 ? -9.238  -18.270 14.853  1.00 17.83  ? 101 ASP A O   1 
ATOM   829  C  CB  . ASP A 1 101 ? -10.073 -19.892 12.467  1.00 14.71  ? 101 ASP A CB  1 
ATOM   830  C  CG  . ASP A 1 101 ? -10.568 -19.935 11.025  1.00 17.74  ? 101 ASP A CG  1 
ATOM   831  O  OD1 . ASP A 1 101 ? -10.061 -19.198 10.132  1.00 18.31  ? 101 ASP A OD1 1 
ATOM   832  O  OD2 . ASP A 1 101 ? -11.475 -20.754 10.773  1.00 23.88  ? 101 ASP A OD2 1 
ATOM   833  N  N   . GLY A 1 102 ? -7.532  -19.769 14.709  1.00 14.30  ? 102 GLY A N   1 
ATOM   834  C  CA  . GLY A 1 102 ? -7.202  -19.717 16.122  1.00 14.30  ? 102 GLY A CA  1 
ATOM   835  C  C   . GLY A 1 102 ? -6.299  -18.583 16.557  1.00 13.23  ? 102 GLY A C   1 
ATOM   836  O  O   . GLY A 1 102 ? -5.881  -18.560 17.709  1.00 14.20  ? 102 GLY A O   1 
ATOM   837  N  N   . GLN A 1 103 ? -6.009  -17.632 15.677  1.00 12.31  ? 103 GLN A N   1 
ATOM   838  C  CA  . GLN A 1 103 ? -5.276  -16.451 16.094  1.00 10.86  ? 103 GLN A CA  1 
ATOM   839  C  C   . GLN A 1 103 ? -5.709  -15.314 15.183  1.00 9.54   ? 103 GLN A C   1 
ATOM   840  O  O   . GLN A 1 103 ? -6.246  -15.526 14.094  1.00 10.60  ? 103 GLN A O   1 
ATOM   841  C  CB  . GLN A 1 103 ? -3.757  -16.731 16.080  1.00 12.23  ? 103 GLN A CB  1 
ATOM   842  C  CG  . GLN A 1 103 ? -3.239  -17.019 14.679  1.00 13.06  ? 103 GLN A CG  1 
ATOM   843  C  CD  . GLN A 1 103 ? -1.844  -17.589 14.684  1.00 16.75  ? 103 GLN A CD  1 
ATOM   844  O  OE1 . GLN A 1 103 ? -0.952  -17.167 13.941  1.00 17.26  ? 103 GLN A OE1 1 
ATOM   845  N  NE2 . GLN A 1 103 ? -1.631  -18.608 15.471  1.00 27.46  ? 103 GLN A NE2 1 
ATOM   846  N  N   . GLY A 1 104 ? -5.363  -14.089 15.587  1.00 9.76   ? 104 GLY A N   1 
ATOM   847  C  CA  . GLY A 1 104 ? -5.649  -12.924 14.767  1.00 9.77   ? 104 GLY A CA  1 
ATOM   848  C  C   . GLY A 1 104 ? -6.101  -11.731 15.578  1.00 8.41   ? 104 GLY A C   1 
ATOM   849  O  O   . GLY A 1 104 ? -5.822  -10.578 15.197  1.00 10.21  ? 104 GLY A O   1 
ATOM   850  N  N   . SER A 1 105 ? -6.793  -11.969 16.714  1.00 9.02   ? 105 SER A N   1 
ATOM   851  C  CA  . SER A 1 105 ? -7.205  -10.845 17.538  1.00 9.33   ? 105 SER A CA  1 
ATOM   852  C  C   . SER A 1 105 ? -5.980  -10.287 18.286  1.00 9.37   ? 105 SER A C   1 
ATOM   853  O  O   . SER A 1 105 ? -4.966  -10.969 18.513  1.00 10.21  ? 105 SER A O   1 
ATOM   854  C  CB  . SER A 1 105 ? -8.346  -11.147 18.472  1.00 9.14   ? 105 SER A CB  1 
ATOM   855  O  OG  . SER A 1 105 ? -7.976  -12.117 19.473  1.00 9.78   ? 105 SER A OG  1 
ATOM   856  N  N   . GLU A 1 106 ? -6.115  -9.034  18.681  1.00 8.88   ? 106 GLU A N   1 
ATOM   857  C  CA  . GLU A 1 106 ? -5.098  -8.345  19.509  1.00 8.41   ? 106 GLU A CA  1 
ATOM   858  C  C   . GLU A 1 106 ? -5.431  -8.524  20.970  1.00 8.21   ? 106 GLU A C   1 
ATOM   859  O  O   . GLU A 1 106 ? -4.643  -9.071  21.757  1.00 9.69   ? 106 GLU A O   1 
ATOM   860  C  CB  . GLU A 1 106 ? -5.001  -6.902  19.038  1.00 9.21   ? 106 GLU A CB  1 
ATOM   861  C  CG  . GLU A 1 106 ? -4.537  -6.822  17.617  1.00 9.80   ? 106 GLU A CG  1 
ATOM   862  C  CD  . GLU A 1 106 ? -3.886  -5.522  17.304  1.00 9.07   ? 106 GLU A CD  1 
ATOM   863  O  OE1 . GLU A 1 106 ? -4.486  -4.443  17.523  1.00 9.98   ? 106 GLU A OE1 1 
ATOM   864  O  OE2 . GLU A 1 106 ? -2.736  -5.539  16.778  1.00 10.52  ? 106 GLU A OE2 1 
ATOM   865  N  N   . HIS A 1 107 ? -6.603  -8.045  21.399  1.00 8.30   ? 107 HIS A N   1 
ATOM   866  C  CA  . HIS A 1 107 ? -7.072  -8.413  22.715  1.00 8.73   ? 107 HIS A CA  1 
ATOM   867  C  C   . HIS A 1 107 ? -7.361  -9.925  22.745  1.00 8.64   ? 107 HIS A C   1 
ATOM   868  O  O   . HIS A 1 107 ? -7.724  -10.510 21.724  1.00 9.06   ? 107 HIS A O   1 
ATOM   869  C  CB  . HIS A 1 107 ? -8.332  -7.600  23.080  1.00 9.51   ? 107 HIS A CB  1 
ATOM   870  C  CG  . HIS A 1 107 ? -7.992  -6.158  23.239  1.00 8.72   ? 107 HIS A CG  1 
ATOM   871  N  ND1 . HIS A 1 107 ? -8.027  -5.255  22.184  1.00 9.03   ? 107 HIS A ND1 1 
ATOM   872  C  CD2 . HIS A 1 107 ? -7.543  -5.472  24.325  1.00 8.97   ? 107 HIS A CD2 1 
ATOM   873  C  CE1 . HIS A 1 107 ? -7.603  -4.080  22.617  1.00 8.79   ? 107 HIS A CE1 1 
ATOM   874  N  NE2 . HIS A 1 107 ? -7.292  -4.157  23.912  1.00 8.85   ? 107 HIS A NE2 1 
ATOM   875  N  N   . THR A 1 108 ? -7.275  -10.462 23.966  1.00 8.98   ? 108 THR A N   1 
ATOM   876  C  CA  . THR A 1 108 ? -7.660  -11.840 24.227  1.00 8.96   ? 108 THR A CA  1 
ATOM   877  C  C   . THR A 1 108 ? -8.591  -11.851 25.420  1.00 8.94   ? 108 THR A C   1 
ATOM   878  O  O   . THR A 1 108 ? -8.636  -10.876 26.197  1.00 10.03  ? 108 THR A O   1 
ATOM   879  C  CB  . THR A 1 108 ? -6.417  -12.729 24.416  1.00 10.31  ? 108 THR A CB  1 
ATOM   880  O  OG1 . THR A 1 108 ? -5.596  -12.256 25.478  1.00 10.49  ? 108 THR A OG1 1 
ATOM   881  C  CG2 . THR A 1 108 ? -5.604  -12.818 23.147  1.00 11.19  ? 108 THR A CG2 1 
ATOM   882  N  N   . VAL A 1 109 ? -9.370  -12.909 25.564  1.00 9.81   ? 109 VAL A N   1 
ATOM   883  C  CA  . VAL A 1 109 ? -10.369 -12.965 26.646  1.00 10.39  ? 109 VAL A CA  1 
ATOM   884  C  C   . VAL A 1 109 ? -10.053 -14.282 27.382  1.00 10.45  ? 109 VAL A C   1 
ATOM   885  O  O   . VAL A 1 109 ? -10.204 -15.384 26.844  1.00 11.15  ? 109 VAL A O   1 
ATOM   886  C  CB  . VAL A 1 109 ? -11.799 -13.014 26.057  1.00 10.54  ? 109 VAL A CB  1 
ATOM   887  C  CG1 . VAL A 1 109 ? -12.794 -13.143 27.202  1.00 13.00  ? 109 VAL A CG1 1 
ATOM   888  C  CG2 . VAL A 1 109 ? -12.067 -11.723 25.276  1.00 13.70  ? 109 VAL A CG2 1 
ATOM   889  N  N   . ASP A 1 110 ? -9.566  -14.198 28.620  1.00 10.84  ? 110 ASP A N   1 
ATOM   890  C  CA  . ASP A 1 110 ? -9.084  -15.388 29.339  1.00 12.84  ? 110 ASP A CA  1 
ATOM   891  C  C   . ASP A 1 110 ? -8.136  -16.218 28.458  1.00 12.81  ? 110 ASP A C   1 
ATOM   892  O  O   . ASP A 1 110 ? -8.209  -17.432 28.418  1.00 12.96  ? 110 ASP A O   1 
ATOM   893  C  CB  . ASP A 1 110 ? -10.287 -16.201 29.827  1.00 14.78  ? 110 ASP A CB  1 
ATOM   894  C  CG  . ASP A 1 110 ? -11.113 -15.451 30.833  1.00 15.18  ? 110 ASP A CG  1 
ATOM   895  O  OD1 . ASP A 1 110 ? -10.590 -14.557 31.505  1.00 16.53  ? 110 ASP A OD1 1 
ATOM   896  O  OD2 . ASP A 1 110 ? -12.311 -15.771 30.912  1.00 18.90  ? 110 ASP A OD2 1 
ATOM   897  N  N   . LYS A 1 111 ? -7.241  -15.495 27.781  1.00 11.89  ? 111 LYS A N   1 
ATOM   898  C  CA  . LYS A 1 111 ? -6.210  -16.038 26.911  1.00 11.75  ? 111 LYS A CA  1 
ATOM   899  C  C   . LYS A 1 111 ? -6.759  -16.545 25.573  1.00 12.30  ? 111 LYS A C   1 
ATOM   900  O  O   . LYS A 1 111 ? -5.954  -16.917 24.693  1.00 14.01  ? 111 LYS A O   1 
ATOM   901  C  CB  . LYS A 1 111 ? -5.321  -17.102 27.568  1.00 14.53  ? 111 LYS A CB  1 
ATOM   902  C  CG  . LYS A 1 111 ? -4.607  -16.613 28.827  1.00 19.49  ? 111 LYS A CG  1 
ATOM   903  C  CD  . LYS A 1 111 ? -3.636  -15.446 28.540  1.00 24.72  ? 111 LYS A CD  1 
ATOM   904  C  CE  . LYS A 1 111 ? -2.953  -14.871 29.780  1.00 31.59  ? 111 LYS A CE  1 
ATOM   905  N  NZ  . LYS A 1 111 ? -1.549  -15.273 29.801  1.00 34.94  ? 111 LYS A NZ  1 
ATOM   906  N  N   . LYS A 1 112 ? -8.074  -16.521 25.367  1.00 11.36  ? 112 LYS A N   1 
ATOM   907  C  CA  . LYS A 1 112 ? -8.617  -16.938 24.074  1.00 11.99  ? 112 LYS A CA  1 
ATOM   908  C  C   . LYS A 1 112 ? -8.316  -15.871 23.001  1.00 10.79  ? 112 LYS A C   1 
ATOM   909  O  O   . LYS A 1 112 ? -8.598  -14.702 23.196  1.00 10.86  ? 112 LYS A O   1 
ATOM   910  C  CB  . LYS A 1 112 ? -10.145 -17.070 24.156  1.00 14.08  ? 112 LYS A CB  1 
ATOM   911  C  CG  . LYS A 1 112 ? -10.821 -17.409 22.813  1.00 15.89  ? 112 LYS A CG  1 
ATOM   912  C  CD  . LYS A 1 112 ? -12.345 -17.433 22.892  1.00 16.75  ? 112 LYS A CD  1 
ATOM   913  C  CE  . LYS A 1 112 ? -12.928 -17.584 21.515  1.00 21.13  ? 112 LYS A CE  1 
ATOM   914  N  NZ  . LYS A 1 112 ? -12.788 -18.937 21.034  1.00 22.64  ? 112 LYS A NZ  1 
ATOM   915  N  N   A LYS A 1 113 ? -7.792  -16.336 21.874  0.50 11.16  ? 113 LYS A N   1 
ATOM   916  N  N   B LYS A 1 113 ? -7.802  -16.335 21.869  0.50 11.01  ? 113 LYS A N   1 
ATOM   917  C  CA  A LYS A 1 113 ? -7.610  -15.525 20.681  0.50 11.33  ? 113 LYS A CA  1 
ATOM   918  C  CA  B LYS A 1 113 ? -7.605  -15.528 20.673  0.50 10.69  ? 113 LYS A CA  1 
ATOM   919  C  C   A LYS A 1 113 ? -8.780  -15.762 19.739  0.50 11.75  ? 113 LYS A C   1 
ATOM   920  C  C   B LYS A 1 113 ? -8.761  -15.766 19.717  0.50 10.97  ? 113 LYS A C   1 
ATOM   921  O  O   A LYS A 1 113 ? -9.140  -16.916 19.504  0.50 15.25  ? 113 LYS A O   1 
ATOM   922  O  O   B LYS A 1 113 ? -9.088  -16.924 19.451  0.50 12.08  ? 113 LYS A O   1 
ATOM   923  C  CB  A LYS A 1 113 ? -6.300  -15.862 19.957  0.50 12.13  ? 113 LYS A CB  1 
ATOM   924  C  CB  B LYS A 1 113 ? -6.288  -15.872 19.969  0.50 12.07  ? 113 LYS A CB  1 
ATOM   925  C  CG  A LYS A 1 113 ? -5.048  -15.580 20.765  0.50 12.48  ? 113 LYS A CG  1 
ATOM   926  C  CG  B LYS A 1 113 ? -5.073  -15.577 20.823  0.50 12.71  ? 113 LYS A CG  1 
ATOM   927  C  CD  A LYS A 1 113 ? -3.835  -16.206 20.086  0.50 13.58  ? 113 LYS A CD  1 
ATOM   928  C  CD  B LYS A 1 113 ? -3.808  -16.160 20.225  0.50 14.10  ? 113 LYS A CD  1 
ATOM   929  C  CE  A LYS A 1 113 ? -2.499  -15.716 20.608  0.50 17.82  ? 113 LYS A CE  1 
ATOM   930  C  CE  B LYS A 1 113 ? -2.592  -15.622 20.946  0.50 18.11  ? 113 LYS A CE  1 
ATOM   931  N  NZ  A LYS A 1 113 ? -2.116  -16.354 21.888  0.50 15.88  ? 113 LYS A NZ  1 
ATOM   932  N  NZ  B LYS A 1 113 ? -1.368  -16.402 20.657  0.50 18.54  ? 113 LYS A NZ  1 
ATOM   933  N  N   . TYR A 1 114 ? -9.324  -14.685 19.176  1.00 9.99   ? 114 TYR A N   1 
ATOM   934  C  CA  . TYR A 1 114 ? -10.326 -14.759 18.122  1.00 10.01  ? 114 TYR A CA  1 
ATOM   935  C  C   . TYR A 1 114 ? -9.637  -14.736 16.773  1.00 9.64   ? 114 TYR A C   1 
ATOM   936  O  O   . TYR A 1 114 ? -8.422  -14.424 16.615  1.00 10.10  ? 114 TYR A O   1 
ATOM   937  C  CB  . TYR A 1 114 ? -11.366 -13.657 18.254  1.00 10.35  ? 114 TYR A CB  1 
ATOM   938  C  CG  . TYR A 1 114 ? -12.312 -13.882 19.412  1.00 9.92   ? 114 TYR A CG  1 
ATOM   939  C  CD1 . TYR A 1 114 ? -12.063 -13.452 20.713  1.00 11.75  ? 114 TYR A CD1 1 
ATOM   940  C  CD2 . TYR A 1 114 ? -13.521 -14.531 19.159  1.00 12.10  ? 114 TYR A CD2 1 
ATOM   941  C  CE1 . TYR A 1 114 ? -12.974 -13.639 21.752  1.00 13.59  ? 114 TYR A CE1 1 
ATOM   942  C  CE2 . TYR A 1 114 ? -14.463 -14.719 20.185  1.00 14.36  ? 114 TYR A CE2 1 
ATOM   943  C  CZ  . TYR A 1 114 ? -14.158 -14.277 21.471  1.00 15.48  ? 114 TYR A CZ  1 
ATOM   944  O  OH  . TYR A 1 114 ? -15.063 -14.412 22.536  1.00 20.84  ? 114 TYR A OH  1 
ATOM   945  N  N   . ALA A 1 115 ? -10.386 -15.020 15.696  1.00 9.24   ? 115 ALA A N   1 
ATOM   946  C  CA  . ALA A 1 115 ? -9.834  -15.097 14.347  1.00 9.36   ? 115 ALA A CA  1 
ATOM   947  C  C   . ALA A 1 115 ? -9.442  -13.709 13.860  1.00 9.21   ? 115 ALA A C   1 
ATOM   948  O  O   . ALA A 1 115 ? -8.584  -13.567 12.954  1.00 9.67   ? 115 ALA A O   1 
ATOM   949  C  CB  . ALA A 1 115 ? -10.858 -15.696 13.380  1.00 11.06  ? 115 ALA A CB  1 
ATOM   950  N  N   . ALA A 1 116 ? -10.106 -12.655 14.333  1.00 8.87   ? 116 ALA A N   1 
ATOM   951  C  CA  . ALA A 1 116 ? -9.792  -11.302 13.877  1.00 8.57   ? 116 ALA A CA  1 
ATOM   952  C  C   . ALA A 1 116 ? -10.370 -10.336 14.906  1.00 8.15   ? 116 ALA A C   1 
ATOM   953  O  O   . ALA A 1 116 ? -11.151 -10.706 15.781  1.00 8.79   ? 116 ALA A O   1 
ATOM   954  C  CB  . ALA A 1 116 ? -10.354 -11.063 12.469  1.00 9.42   ? 116 ALA A CB  1 
ATOM   955  N  N   . GLU A 1 117 ? -10.002 -9.046  14.727  1.00 8.53   ? 117 GLU A N   1 
ATOM   956  C  CA  . GLU A 1 117 ? -10.523 -7.979  15.566  1.00 8.22   ? 117 GLU A CA  1 
ATOM   957  C  C   . GLU A 1 117 ? -10.729 -6.756  14.693  1.00 8.31   ? 117 GLU A C   1 
ATOM   958  O  O   . GLU A 1 117 ? -9.845  -6.378  13.927  1.00 9.64   ? 117 GLU A O   1 
ATOM   959  C  CB  . GLU A 1 117 ? -9.560  -7.705  16.720  1.00 9.42   ? 117 GLU A CB  1 
ATOM   960  C  CG  . GLU A 1 117 ? -10.079 -6.784  17.806  1.00 8.99   ? 117 GLU A CG  1 
ATOM   961  C  CD  . GLU A 1 117 ? -9.193  -6.723  19.044  1.00 8.94   ? 117 GLU A CD  1 
ATOM   962  O  OE1 . GLU A 1 117 ? -8.528  -7.759  19.347  1.00 10.36  ? 117 GLU A OE1 1 
ATOM   963  O  OE2 . GLU A 1 117 ? -9.105  -5.638  19.664  1.00 10.92  ? 117 GLU A OE2 1 
ATOM   964  N  N   . LEU A 1 118 ? -11.901 -6.144  14.851  1.00 8.01   ? 118 LEU A N   1 
ATOM   965  C  CA  . LEU A 1 118 ? -12.284 -4.891  14.163  1.00 8.25   ? 118 LEU A CA  1 
ATOM   966  C  C   . LEU A 1 118 ? -12.053 -3.720  15.135  1.00 6.93   ? 118 LEU A C   1 
ATOM   967  O  O   . LEU A 1 118 ? -12.476 -3.799  16.290  1.00 8.08   ? 118 LEU A O   1 
ATOM   968  C  CB  . LEU A 1 118 ? -13.784 -4.999  13.802  1.00 8.55   ? 118 LEU A CB  1 
ATOM   969  C  CG  . LEU A 1 118 ? -14.508 -3.705  13.436  1.00 9.06   ? 118 LEU A CG  1 
ATOM   970  C  CD1 . LEU A 1 118 ? -13.888 -3.008  12.188  1.00 9.54   ? 118 LEU A CD1 1 
ATOM   971  C  CD2 . LEU A 1 118 ? -15.973 -4.012  13.178  1.00 10.63  ? 118 LEU A CD2 1 
ATOM   972  N  N   . HIS A 1 119 ? -11.386 -2.682  14.640  1.00 7.13   ? 119 HIS A N   1 
ATOM   973  C  CA  . HIS A 1 119 ? -11.161 -1.455  15.421  1.00 7.82   ? 119 HIS A CA  1 
ATOM   974  C  C   . HIS A 1 119 ? -11.846 -0.289  14.709  1.00 6.97   ? 119 HIS A C   1 
ATOM   975  O  O   . HIS A 1 119 ? -11.460 0.056   13.595  1.00 8.10   ? 119 HIS A O   1 
ATOM   976  C  CB  . HIS A 1 119 ? -9.657  -1.188  15.519  1.00 8.15   ? 119 HIS A CB  1 
ATOM   977  C  CG  . HIS A 1 119 ? -9.001  -2.181  16.435  1.00 7.87   ? 119 HIS A CG  1 
ATOM   978  N  ND1 . HIS A 1 119 ? -7.627  -2.424  16.388  1.00 7.94   ? 119 HIS A ND1 1 
ATOM   979  C  CD2 . HIS A 1 119 ? -9.552  -2.974  17.389  1.00 8.66   ? 119 HIS A CD2 1 
ATOM   980  C  CE1 . HIS A 1 119 ? -7.390  -3.333  17.345  1.00 8.00   ? 119 HIS A CE1 1 
ATOM   981  N  NE2 . HIS A 1 119 ? -8.498  -3.720  17.920  1.00 8.42   ? 119 HIS A NE2 1 
ATOM   982  N  N   . LEU A 1 120 ? -12.802 0.304   15.380  1.00 7.23   ? 120 LEU A N   1 
ATOM   983  C  CA  . LEU A 1 120 ? -13.458 1.529   14.941  1.00 7.80   ? 120 LEU A CA  1 
ATOM   984  C  C   . LEU A 1 120 ? -12.857 2.679   15.764  1.00 7.42   ? 120 LEU A C   1 
ATOM   985  O  O   . LEU A 1 120 ? -12.993 2.708   16.977  1.00 7.72   ? 120 LEU A O   1 
ATOM   986  C  CB  . LEU A 1 120 ? -14.964 1.430   15.167  1.00 9.11   ? 120 LEU A CB  1 
ATOM   987  C  CG  . LEU A 1 120 ? -15.675 0.399   14.284  1.00 8.78   ? 120 LEU A CG  1 
ATOM   988  C  CD1 . LEU A 1 120 ? -16.550 -0.521  15.130  1.00 13.29  ? 120 LEU A CD1 1 
ATOM   989  C  CD2 . LEU A 1 120 ? -16.456 1.049   13.169  1.00 11.19  ? 120 LEU A CD2 1 
ATOM   990  N  N   . VAL A 1 121 ? -12.101 3.540   15.076  1.00 8.31   ? 121 VAL A N   1 
ATOM   991  C  CA  . VAL A 1 121 ? -11.239 4.544   15.726  1.00 8.42   ? 121 VAL A CA  1 
ATOM   992  C  C   . VAL A 1 121 ? -11.952 5.907   15.722  1.00 7.86   ? 121 VAL A C   1 
ATOM   993  O  O   . VAL A 1 121 ? -12.390 6.350   14.648  1.00 9.34   ? 121 VAL A O   1 
ATOM   994  C  CB  . VAL A 1 121 ? -9.903  4.650   14.968  1.00 8.51   ? 121 VAL A CB  1 
ATOM   995  C  CG1 . VAL A 1 121 ? -9.005  5.715   15.624  1.00 9.76   ? 121 VAL A CG1 1 
ATOM   996  C  CG2 . VAL A 1 121 ? -9.196  3.303   14.888  1.00 9.65   ? 121 VAL A CG2 1 
ATOM   997  N  N   . HIS A 1 122 ? -12.061 6.503   16.907  1.00 8.38   ? 122 HIS A N   1 
ATOM   998  C  CA  . HIS A 1 122 ? -12.755 7.758   17.050  1.00 8.52   ? 122 HIS A CA  1 
ATOM   999  C  C   . HIS A 1 122 ? -11.849 8.737   17.803  1.00 9.11   ? 122 HIS A C   1 
ATOM   1000 O  O   . HIS A 1 122 ? -11.052 8.341   18.661  1.00 10.44  ? 122 HIS A O   1 
ATOM   1001 C  CB  . HIS A 1 122 ? -14.017 7.594   17.902  1.00 9.56   ? 122 HIS A CB  1 
ATOM   1002 C  CG  . HIS A 1 122 ? -14.913 6.470   17.498  1.00 9.09   ? 122 HIS A CG  1 
ATOM   1003 N  ND1 . HIS A 1 122 ? -14.586 5.149   17.733  1.00 9.04   ? 122 HIS A ND1 1 
ATOM   1004 C  CD2 . HIS A 1 122 ? -16.127 6.422   16.909  1.00 9.99   ? 122 HIS A CD2 1 
ATOM   1005 C  CE1 . HIS A 1 122 ? -15.601 4.397   17.331  1.00 10.16  ? 122 HIS A CE1 1 
ATOM   1006 N  NE2 . HIS A 1 122 ? -16.574 5.144   16.789  1.00 9.88   ? 122 HIS A NE2 1 
ATOM   1007 N  N   . TRP A 1 123 ? -12.015 10.058  17.533  1.00 9.01   ? 123 TRP A N   1 
ATOM   1008 C  CA  . TRP A 1 123 ? -11.225 11.074  18.233  1.00 9.41   ? 123 TRP A CA  1 
ATOM   1009 C  C   . TRP A 1 123 ? -12.138 12.033  18.981  1.00 9.55   ? 123 TRP A C   1 
ATOM   1010 O  O   . TRP A 1 123 ? -13.234 12.368  18.530  1.00 11.32  ? 123 TRP A O   1 
ATOM   1011 C  CB  . TRP A 1 123 ? -10.271 11.846  17.298  1.00 11.15  ? 123 TRP A CB  1 
ATOM   1012 C  CG  . TRP A 1 123 ? -10.890 12.411  16.044  1.00 11.32  ? 123 TRP A CG  1 
ATOM   1013 C  CD1 . TRP A 1 123 ? -11.062 11.799  14.835  1.00 14.40  ? 123 TRP A CD1 1 
ATOM   1014 C  CD2 . TRP A 1 123 ? -11.362 13.761  15.874  1.00 12.20  ? 123 TRP A CD2 1 
ATOM   1015 N  NE1 . TRP A 1 123 ? -11.640 12.624  13.939  1.00 14.98  ? 123 TRP A NE1 1 
ATOM   1016 C  CE2 . TRP A 1 123 ? -11.818 13.858  14.541  1.00 13.44  ? 123 TRP A CE2 1 
ATOM   1017 C  CE3 . TRP A 1 123 ? -11.442 14.880  16.727  1.00 14.11  ? 123 TRP A CE3 1 
ATOM   1018 C  CZ2 . TRP A 1 123 ? -12.356 15.039  14.018  1.00 17.63  ? 123 TRP A CZ2 1 
ATOM   1019 C  CZ3 . TRP A 1 123 ? -11.977 16.033  16.208  1.00 14.81  ? 123 TRP A CZ3 1 
ATOM   1020 C  CH2 . TRP A 1 123 ? -12.418 16.112  14.885  1.00 17.05  ? 123 TRP A CH2 1 
ATOM   1021 N  N   . ASN A 1 124 ? -11.615 12.501  20.111  1.00 10.17  ? 124 ASN A N   1 
ATOM   1022 C  CA  . ASN A 1 124 ? -12.398 13.408  20.988  1.00 11.36  ? 124 ASN A CA  1 
ATOM   1023 C  C   . ASN A 1 124 ? -12.499 14.778  20.363  1.00 11.59  ? 124 ASN A C   1 
ATOM   1024 O  O   . ASN A 1 124 ? -11.492 15.440  20.086  1.00 11.14  ? 124 ASN A O   1 
ATOM   1025 C  CB  . ASN A 1 124 ? -11.645 13.455  22.314  1.00 12.08  ? 124 ASN A CB  1 
ATOM   1026 C  CG  . ASN A 1 124 ? -12.403 14.077  23.421  1.00 12.86  ? 124 ASN A CG  1 
ATOM   1027 O  OD1 . ASN A 1 124 ? -13.196 15.008  23.187  1.00 14.31  ? 124 ASN A OD1 1 
ATOM   1028 N  ND2 . ASN A 1 124 ? -12.085 13.674  24.677  1.00 14.53  ? 124 ASN A ND2 1 
ATOM   1029 N  N   . THR A 1 125 ? -13.749 15.204  20.144  1.00 13.10  ? 125 THR A N   1 
ATOM   1030 C  CA  . THR A 1 125 ? -13.945 16.467  19.403  1.00 13.70  ? 125 THR A CA  1 
ATOM   1031 C  C   . THR A 1 125 ? -13.410 17.678  20.178  1.00 13.97  ? 125 THR A C   1 
ATOM   1032 O  O   . THR A 1 125 ? -13.221 18.717  19.568  1.00 16.07  ? 125 THR A O   1 
ATOM   1033 C  CB  . THR A 1 125 ? -15.417 16.664  19.026  1.00 16.95  ? 125 THR A CB  1 
ATOM   1034 O  OG1 . THR A 1 125 ? -16.204 16.682  20.219  1.00 19.44  ? 125 THR A OG1 1 
ATOM   1035 C  CG2 . THR A 1 125 ? -15.876 15.560  18.107  1.00 21.75  ? 125 THR A CG2 1 
ATOM   1036 N  N   . LYS A 1 126 ? -13.153 17.546  21.541  1.00 13.12  ? 127 LYS A N   1 
ATOM   1037 C  CA  . LYS A 1 126 ? -12.605 18.705  22.248  1.00 16.03  ? 127 LYS A CA  1 
ATOM   1038 C  C   . LYS A 1 126 ? -11.199 19.044  21.742  1.00 14.20  ? 127 LYS A C   1 
ATOM   1039 O  O   . LYS A 1 126 ? -10.706 20.134  22.040  1.00 18.69  ? 127 LYS A O   1 
ATOM   1040 C  CB  . LYS A 1 126 ? -12.727 18.481  23.749  1.00 20.70  ? 127 LYS A CB  1 
ATOM   1041 C  CG  . LYS A 1 126 ? -11.681 17.616  24.329  1.00 19.83  ? 127 LYS A CG  1 
ATOM   1042 C  CD  . LYS A 1 126 ? -11.990 17.471  25.799  1.00 27.91  ? 127 LYS A CD  1 
ATOM   1043 C  CE  . LYS A 1 126 ? -11.084 16.439  26.384  1.00 26.78  ? 127 LYS A CE  1 
ATOM   1044 N  NZ  . LYS A 1 126 ? -11.237 16.300  27.846  1.00 42.59  ? 127 LYS A NZ  1 
ATOM   1045 N  N   . TYR A 1 127 ? -10.536 18.135  21.016  1.00 12.37  ? 128 TYR A N   1 
ATOM   1046 C  CA  . TYR A 1 127 ? -9.193  18.389  20.520  1.00 11.90  ? 128 TYR A CA  1 
ATOM   1047 C  C   . TYR A 1 127 ? -9.174  18.760  19.020  1.00 12.03  ? 128 TYR A C   1 
ATOM   1048 O  O   . TYR A 1 127 ? -8.079  18.986  18.462  1.00 12.73  ? 128 TYR A O   1 
ATOM   1049 C  CB  . TYR A 1 127 ? -8.256  17.196  20.788  1.00 12.83  ? 128 TYR A CB  1 
ATOM   1050 C  CG  . TYR A 1 127 ? -8.187  16.909  22.265  1.00 11.82  ? 128 TYR A CG  1 
ATOM   1051 C  CD1 . TYR A 1 127 ? -7.756  17.891  23.160  1.00 14.28  ? 128 TYR A CD1 1 
ATOM   1052 C  CD2 . TYR A 1 127 ? -8.514  15.674  22.773  1.00 12.28  ? 128 TYR A CD2 1 
ATOM   1053 C  CE1 . TYR A 1 127 ? -7.711  17.669  24.517  1.00 14.57  ? 128 TYR A CE1 1 
ATOM   1054 C  CE2 . TYR A 1 127 ? -8.458  15.394  24.120  1.00 12.08  ? 128 TYR A CE2 1 
ATOM   1055 C  CZ  . TYR A 1 127 ? -8.030  16.404  25.002  1.00 14.33  ? 128 TYR A CZ  1 
ATOM   1056 O  OH  . TYR A 1 127 ? -7.965  16.207  26.345  1.00 15.77  ? 128 TYR A OH  1 
ATOM   1057 N  N   . GLY A 1 128 ? -10.351 18.844  18.381  1.00 12.46  ? 129 GLY A N   1 
ATOM   1058 C  CA  . GLY A 1 128 ? -10.421 19.496  17.076  1.00 13.59  ? 129 GLY A CA  1 
ATOM   1059 C  C   . GLY A 1 128 ? -10.014 18.644  15.868  1.00 12.72  ? 129 GLY A C   1 
ATOM   1060 O  O   . GLY A 1 128 ? -10.611 18.765  14.796  1.00 14.39  ? 129 GLY A O   1 
ATOM   1061 N  N   . ASP A 1 129 ? -8.935  17.826  15.979  1.00 13.82  ? 130 ASP A N   1 
ATOM   1062 C  CA  . ASP A 1 129 ? -8.499  16.950  14.881  1.00 14.81  ? 130 ASP A CA  1 
ATOM   1063 C  C   . ASP A 1 129 ? -7.867  15.708  15.489  1.00 14.75  ? 130 ASP A C   1 
ATOM   1064 O  O   . ASP A 1 129 ? -7.420  15.741  16.639  1.00 14.20  ? 130 ASP A O   1 
ATOM   1065 C  CB  . ASP A 1 129 ? -7.535  17.676  13.887  1.00 15.82  ? 130 ASP A CB  1 
ATOM   1066 C  CG  . ASP A 1 129 ? -6.136  18.005  14.401  1.00 18.80  ? 130 ASP A CG  1 
ATOM   1067 O  OD1 . ASP A 1 129 ? -5.273  17.128  14.498  1.00 20.29  ? 130 ASP A OD1 1 
ATOM   1068 O  OD2 . ASP A 1 129 ? -5.870  19.223  14.542  1.00 20.56  ? 130 ASP A OD2 1 
ATOM   1069 N  N   . ALA A 1 130 ? -7.778  14.658  14.698  1.00 14.19  ? 131 ALA A N   1 
ATOM   1070 C  CA  . ALA A 1 130 ? -7.309  13.372  15.139  1.00 14.70  ? 131 ALA A CA  1 
ATOM   1071 C  C   . ALA A 1 130 ? -5.835  13.433  15.550  1.00 14.88  ? 131 ALA A C   1 
ATOM   1072 O  O   . ALA A 1 130 ? -5.430  12.723  16.457  1.00 14.69  ? 131 ALA A O   1 
ATOM   1073 C  CB  . ALA A 1 130 ? -7.548  12.302  14.081  1.00 18.22  ? 131 ALA A CB  1 
ATOM   1074 N  N   . GLY A 1 131 ? -4.987  14.222  14.822  1.00 14.91  ? 132 GLY A N   1 
ATOM   1075 C  CA  . GLY A 1 131 ? -3.562  14.311  15.148  1.00 15.63  ? 132 GLY A CA  1 
ATOM   1076 C  C   . GLY A 1 131 ? -3.401  14.966  16.526  1.00 14.02  ? 132 GLY A C   1 
ATOM   1077 O  O   . GLY A 1 131 ? -2.639  14.486  17.361  1.00 16.50  ? 132 GLY A O   1 
ATOM   1078 N  N   A LYS A 1 132 ? -4.095  16.096  16.767  0.50 14.85  ? 133 LYS A N   1 
ATOM   1079 N  N   B LYS A 1 132 ? -4.079  16.099  16.799  0.50 13.49  ? 133 LYS A N   1 
ATOM   1080 C  CA  A LYS A 1 132 ? -4.011  16.719  18.073  0.50 14.36  ? 133 LYS A CA  1 
ATOM   1081 C  CA  B LYS A 1 132 ? -3.969  16.718  18.108  0.50 13.01  ? 133 LYS A CA  1 
ATOM   1082 C  C   A LYS A 1 132 ? -4.509  15.737  19.130  0.50 11.32  ? 133 LYS A C   1 
ATOM   1083 C  C   B LYS A 1 132 ? -4.573  15.809  19.180  0.50 11.94  ? 133 LYS A C   1 
ATOM   1084 O  O   A LYS A 1 132 ? -3.873  15.569  20.178  0.50 12.11  ? 133 LYS A O   1 
ATOM   1085 O  O   B LYS A 1 132 ? -4.084  15.763  20.313  0.50 13.45  ? 133 LYS A O   1 
ATOM   1086 C  CB  A LYS A 1 132 ? -4.792  18.043  18.062  0.50 16.02  ? 133 LYS A CB  1 
ATOM   1087 C  CB  B LYS A 1 132 ? -4.653  18.090  18.062  0.50 12.20  ? 133 LYS A CB  1 
ATOM   1088 C  CG  A LYS A 1 132 ? -3.924  19.281  17.925  0.50 22.67  ? 133 LYS A CG  1 
ATOM   1089 C  CG  B LYS A 1 132 ? -3.961  19.111  17.174  0.50 15.87  ? 133 LYS A CG  1 
ATOM   1090 C  CD  A LYS A 1 132 ? -3.033  19.255  16.677  0.50 22.89  ? 133 LYS A CD  1 
ATOM   1091 C  CD  B LYS A 1 132 ? -2.585  19.500  17.750  0.50 18.97  ? 133 LYS A CD  1 
ATOM   1092 C  CE  A LYS A 1 132 ? -3.683  20.058  15.568  0.50 19.47  ? 133 LYS A CE  1 
ATOM   1093 C  CE  B LYS A 1 132 ? -2.759  20.266  19.036  0.50 28.90  ? 133 LYS A CE  1 
ATOM   1094 N  NZ  A LYS A 1 132 ? -2.970  20.212  14.270  0.50 28.59  ? 133 LYS A NZ  1 
ATOM   1095 N  NZ  B LYS A 1 132 ? -1.657  21.233  19.275  0.50 31.64  ? 133 LYS A NZ  1 
ATOM   1096 N  N   . ALA A 1 133 ? -5.631  15.061  18.826  1.00 11.36  ? 134 ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 133 ? -6.218  14.169  19.821  1.00 10.72  ? 134 ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 133 ? -5.193  13.081  20.199  1.00 11.38  ? 134 ALA A C   1 
ATOM   1099 O  O   . ALA A 1 133 ? -5.163  12.646  21.370  1.00 11.94  ? 134 ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 133 ? -7.503  13.517  19.289  1.00 11.14  ? 134 ALA A CB  1 
ATOM   1101 N  N   . SER A 1 134 ? -4.366  12.616  19.248  1.00 11.77  ? 135 SER A N   1 
ATOM   1102 C  CA  . SER A 1 134 ? -3.439  11.500  19.498  1.00 12.36  ? 135 SER A CA  1 
ATOM   1103 C  C   . SER A 1 134 ? -2.351  11.899  20.507  1.00 12.36  ? 135 SER A C   1 
ATOM   1104 O  O   . SER A 1 134 ? -1.589  11.048  20.964  1.00 13.53  ? 135 SER A O   1 
ATOM   1105 C  CB  . SER A 1 134 ? -2.769  10.997  18.241  1.00 14.24  ? 135 SER A CB  1 
ATOM   1106 O  OG  . SER A 1 134 ? -1.833  11.920  17.701  1.00 18.25  ? 135 SER A OG  1 
ATOM   1107 N  N   . GLN A 1 135 ? -2.221  13.209  20.788  1.00 12.48  ? 136 GLN A N   1 
ATOM   1108 C  CA  . GLN A 1 135 ? -1.229  13.672  21.765  1.00 13.24  ? 136 GLN A CA  1 
ATOM   1109 C  C   . GLN A 1 135 ? -1.822  13.826  23.165  1.00 12.96  ? 136 GLN A C   1 
ATOM   1110 O  O   . GLN A 1 135 ? -1.159  14.357  24.081  1.00 16.26  ? 136 GLN A O   1 
ATOM   1111 C  CB  . GLN A 1 135 ? -0.680  15.030  21.303  1.00 16.86  ? 136 GLN A CB  1 
ATOM   1112 C  CG  . GLN A 1 135 ? -0.050  14.939  19.948  1.00 23.26  ? 136 GLN A CG  1 
ATOM   1113 C  CD  . GLN A 1 135 ? 1.135   14.018  19.793  1.00 36.46  ? 136 GLN A CD  1 
ATOM   1114 O  OE1 . GLN A 1 135 ? 2.181   14.202  20.419  1.00 55.65  ? 136 GLN A OE1 1 
ATOM   1115 N  NE2 . GLN A 1 135 ? 0.981   13.031  18.919  1.00 44.09  ? 136 GLN A NE2 1 
ATOM   1116 N  N   . GLN A 1 136 ? -3.060  13.347  23.407  1.00 12.63  ? 137 GLN A N   1 
ATOM   1117 C  CA  . GLN A 1 136 ? -3.752  13.547  24.675  1.00 12.16  ? 137 GLN A CA  1 
ATOM   1118 C  C   . GLN A 1 136 ? -4.063  12.201  25.269  1.00 12.44  ? 137 GLN A C   1 
ATOM   1119 O  O   . GLN A 1 136 ? -4.444  11.282  24.557  1.00 12.07  ? 137 GLN A O   1 
ATOM   1120 C  CB  . GLN A 1 136 ? -5.052  14.345  24.512  1.00 13.93  ? 137 GLN A CB  1 
ATOM   1121 C  CG  . GLN A 1 136 ? -4.888  15.602  23.650  1.00 15.66  ? 137 GLN A CG  1 
ATOM   1122 C  CD  . GLN A 1 136 ? -3.826  16.492  24.197  1.00 19.73  ? 137 GLN A CD  1 
ATOM   1123 O  OE1 . GLN A 1 136 ? -3.681  16.650  25.401  1.00 22.48  ? 137 GLN A OE1 1 
ATOM   1124 N  NE2 . GLN A 1 136 ? -3.149  17.222  23.292  1.00 32.30  ? 137 GLN A NE2 1 
ATOM   1125 N  N   . PRO A 1 137 ? -4.083  12.095  26.631  1.00 11.55  ? 138 PRO A N   1 
ATOM   1126 C  CA  . PRO A 1 137 ? -4.333  10.798  27.248  1.00 12.70  ? 138 PRO A CA  1 
ATOM   1127 C  C   . PRO A 1 137 ? -5.745  10.272  27.024  1.00 12.45  ? 138 PRO A C   1 
ATOM   1128 O  O   . PRO A 1 137 ? -5.986  9.084   27.145  1.00 17.08  ? 138 PRO A O   1 
ATOM   1129 C  CB  . PRO A 1 137 ? -4.039  10.964  28.722  1.00 17.24  ? 138 PRO A CB  1 
ATOM   1130 C  CG  . PRO A 1 137 ? -3.985  12.441  28.895  1.00 23.54  ? 138 PRO A CG  1 
ATOM   1131 C  CD  . PRO A 1 137 ? -3.574  13.090  27.608  1.00 14.81  ? 138 PRO A CD  1 
ATOM   1132 N  N   . ASP A 1 138 ? -6.681  11.207  26.788  1.00 11.77  ? 139 ASP A N   1 
ATOM   1133 C  CA  . ASP A 1 138 ? -8.086  10.906  26.505  1.00 12.76  ? 139 ASP A CA  1 
ATOM   1134 C  C   . ASP A 1 138 ? -8.448  11.332  25.078  1.00 11.28  ? 139 ASP A C   1 
ATOM   1135 O  O   . ASP A 1 138 ? -9.582  11.779  24.829  1.00 13.68  ? 139 ASP A O   1 
ATOM   1136 C  CB  . ASP A 1 138 ? -9.041  11.534  27.551  1.00 14.18  ? 139 ASP A CB  1 
ATOM   1137 C  CG  . ASP A 1 138 ? -8.949  13.043  27.549  1.00 15.69  ? 139 ASP A CG  1 
ATOM   1138 O  OD1 . ASP A 1 138 ? -7.967  13.645  27.010  1.00 16.16  ? 139 ASP A OD1 1 
ATOM   1139 O  OD2 . ASP A 1 138 ? -9.829  13.646  28.237  1.00 20.20  ? 139 ASP A OD2 1 
ATOM   1140 N  N   . GLY A 1 139 ? -7.489  11.235  24.152  1.00 10.29  ? 140 GLY A N   1 
ATOM   1141 C  CA  . GLY A 1 139 ? -7.710  11.745  22.807  1.00 11.20  ? 140 GLY A CA  1 
ATOM   1142 C  C   . GLY A 1 139 ? -8.574  10.855  21.926  1.00 8.67   ? 140 GLY A C   1 
ATOM   1143 O  O   . GLY A 1 139 ? -9.279  11.337  21.045  1.00 9.89   ? 140 GLY A O   1 
ATOM   1144 N  N   . LEU A 1 140 ? -8.349  9.512   21.986  1.00 9.53   ? 141 LEU A N   1 
ATOM   1145 C  CA  . LEU A 1 140 ? -9.003  8.570   21.076  1.00 9.07   ? 141 LEU A CA  1 
ATOM   1146 C  C   . LEU A 1 140 ? -9.846  7.572   21.852  1.00 8.81   ? 141 LEU A C   1 
ATOM   1147 O  O   . LEU A 1 140 ? -9.566  7.300   23.029  1.00 9.27   ? 141 LEU A O   1 
ATOM   1148 C  CB  . LEU A 1 140 ? -7.990  7.795   20.230  1.00 9.80   ? 141 LEU A CB  1 
ATOM   1149 C  CG  . LEU A 1 140 ? -7.046  8.599   19.358  1.00 11.83  ? 141 LEU A CG  1 
ATOM   1150 C  CD1 . LEU A 1 140 ? -6.201  7.628   18.510  1.00 12.83  ? 141 LEU A CD1 1 
ATOM   1151 C  CD2 . LEU A 1 140 ? -7.727  9.581   18.456  1.00 13.03  ? 141 LEU A CD2 1 
ATOM   1152 N  N   . ALA A 1 141 ? -10.873 7.035   21.196  1.00 8.88   ? 142 ALA A N   1 
ATOM   1153 C  CA  . ALA A 1 141 ? -11.619 5.914   21.751  1.00 9.13   ? 142 ALA A CA  1 
ATOM   1154 C  C   . ALA A 1 141 ? -11.732 4.919   20.635  1.00 8.40   ? 142 ALA A C   1 
ATOM   1155 O  O   . ALA A 1 141 ? -12.130 5.247   19.511  1.00 9.60   ? 142 ALA A O   1 
ATOM   1156 C  CB  . ALA A 1 141 ? -13.014 6.329   22.215  1.00 11.53  ? 142 ALA A CB  1 
ATOM   1157 N  N   . VAL A 1 142 ? -11.345 3.660   20.923  1.00 8.41   ? 143 VAL A N   1 
ATOM   1158 C  CA  . VAL A 1 142 ? -11.456 2.590   19.918  1.00 8.74   ? 143 VAL A CA  1 
ATOM   1159 C  C   . VAL A 1 142 ? -12.492 1.594   20.402  1.00 8.32   ? 143 VAL A C   1 
ATOM   1160 O  O   . VAL A 1 142 ? -12.360 1.118   21.543  1.00 9.39   ? 143 VAL A O   1 
ATOM   1161 C  CB  . VAL A 1 142 ? -10.084 1.919   19.624  1.00 9.63   ? 143 VAL A CB  1 
ATOM   1162 C  CG1 . VAL A 1 142 ? -10.308 0.876   18.499  1.00 11.34  ? 143 VAL A CG1 1 
ATOM   1163 C  CG2 . VAL A 1 142 ? -9.078  2.943   19.133  1.00 11.36  ? 143 VAL A CG2 1 
ATOM   1164 N  N   . LEU A 1 143 ? -13.491 1.374   19.539  1.00 8.61   ? 144 LEU A N   1 
ATOM   1165 C  CA  . LEU A 1 143 ? -14.425 0.308   19.785  1.00 8.81   ? 144 LEU A CA  1 
ATOM   1166 C  C   . LEU A 1 143 ? -13.882 -0.944  19.119  1.00 8.25   ? 144 LEU A C   1 
ATOM   1167 O  O   . LEU A 1 143 ? -13.716 -0.957  17.893  1.00 9.37   ? 144 LEU A O   1 
ATOM   1168 C  CB  . LEU A 1 143 ? -15.804 0.745   19.215  1.00 10.68  ? 144 LEU A CB  1 
ATOM   1169 C  CG  . LEU A 1 143 ? -16.953 -0.209  19.377  1.00 11.71  ? 144 LEU A CG  1 
ATOM   1170 C  CD1 . LEU A 1 143 ? -17.235 -0.446  20.853  1.00 15.64  ? 144 LEU A CD1 1 
ATOM   1171 C  CD2 . LEU A 1 143 ? -18.206 0.334   18.684  1.00 14.13  ? 144 LEU A CD2 1 
ATOM   1172 N  N   . GLY A 1 144 ? -13.566 -1.958  19.918  1.00 8.54   ? 145 GLY A N   1 
ATOM   1173 C  CA  . GLY A 1 144 ? -13.002 -3.204  19.458  1.00 8.90   ? 145 GLY A CA  1 
ATOM   1174 C  C   . GLY A 1 144 ? -14.024 -4.308  19.481  1.00 8.14   ? 145 GLY A C   1 
ATOM   1175 O  O   . GLY A 1 144 ? -14.774 -4.459  20.438  1.00 9.27   ? 145 GLY A O   1 
ATOM   1176 N  N   . ILE A 1 145 ? -14.090 -5.041  18.352  1.00 7.95   ? 146 ILE A N   1 
ATOM   1177 C  CA  . ILE A 1 145 ? -15.110 -6.069  18.168  1.00 8.24   ? 146 ILE A CA  1 
ATOM   1178 C  C   . ILE A 1 145 ? -14.386 -7.316  17.680  1.00 7.95   ? 146 ILE A C   1 
ATOM   1179 O  O   . ILE A 1 145 ? -13.647 -7.301  16.684  1.00 8.76   ? 146 ILE A O   1 
ATOM   1180 C  CB  . ILE A 1 145 ? -16.166 -5.613  17.166  1.00 8.44   ? 146 ILE A CB  1 
ATOM   1181 C  CG1 . ILE A 1 145 ? -16.849 -4.337  17.685  1.00 10.52  ? 146 ILE A CG1 1 
ATOM   1182 C  CG2 . ILE A 1 145 ? -17.213 -6.715  16.943  1.00 11.39  ? 146 ILE A CG2 1 
ATOM   1183 C  CD1 . ILE A 1 145 ? -17.896 -3.743  16.790  1.00 10.99  ? 146 ILE A CD1 1 
ATOM   1184 N  N   . PHE A 1 146 ? -14.587 -8.441  18.377  1.00 8.09   ? 147 PHE A N   1 
ATOM   1185 C  CA  . PHE A 1 146 ? -13.985 -9.718  17.970  1.00 8.38   ? 147 PHE A CA  1 
ATOM   1186 C  C   . PHE A 1 146 ? -14.755 -10.325 16.810  1.00 8.45   ? 147 PHE A C   1 
ATOM   1187 O  O   . PHE A 1 146 ? -15.986 -10.210 16.745  1.00 9.79   ? 147 PHE A O   1 
ATOM   1188 C  CB  . PHE A 1 146 ? -14.023 -10.667 19.169  1.00 9.26   ? 147 PHE A CB  1 
ATOM   1189 C  CG  . PHE A 1 146 ? -13.167 -10.220 20.316  1.00 9.06   ? 147 PHE A CG  1 
ATOM   1190 C  CD1 . PHE A 1 146 ? -11.783 -10.044 20.126  1.00 9.66   ? 147 PHE A CD1 1 
ATOM   1191 C  CD2 . PHE A 1 146 ? -13.705 -9.942  21.574  1.00 9.41   ? 147 PHE A CD2 1 
ATOM   1192 C  CE1 . PHE A 1 146 ? -10.987 -9.674  21.206  1.00 9.46   ? 147 PHE A CE1 1 
ATOM   1193 C  CE2 . PHE A 1 146 ? -12.907 -9.564  22.635  1.00 9.53   ? 147 PHE A CE2 1 
ATOM   1194 C  CZ  . PHE A 1 146 ? -11.532 -9.462  22.420  1.00 9.44   ? 147 PHE A CZ  1 
ATOM   1195 N  N   . LEU A 1 147 ? -14.031 -11.052 15.956  1.00 8.63   ? 148 LEU A N   1 
ATOM   1196 C  CA  . LEU A 1 147 ? -14.638 -11.849 14.881  1.00 9.07   ? 148 LEU A CA  1 
ATOM   1197 C  C   . LEU A 1 147 ? -14.305 -13.315 15.135  1.00 9.16   ? 148 LEU A C   1 
ATOM   1198 O  O   . LEU A 1 147 ? -13.136 -13.680 15.363  1.00 10.22  ? 148 LEU A O   1 
ATOM   1199 C  CB  . LEU A 1 147 ? -14.038 -11.480 13.507  1.00 9.21   ? 148 LEU A CB  1 
ATOM   1200 C  CG  . LEU A 1 147 ? -14.600 -10.229 12.842  1.00 9.85   ? 148 LEU A CG  1 
ATOM   1201 C  CD1 . LEU A 1 147 ? -14.416 -8.935  13.694  1.00 12.08  ? 148 LEU A CD1 1 
ATOM   1202 C  CD2 . LEU A 1 147 ? -13.949 -10.035 11.489  1.00 10.25  ? 148 LEU A CD2 1 
ATOM   1203 N  N   . LYS A 1 148 ? -15.351 -14.166 15.059  1.00 10.25  ? 149 LYS A N   1 
ATOM   1204 C  CA  . LYS A 1 148 ? -15.189 -15.633 15.061  1.00 10.81  ? 149 LYS A CA  1 
ATOM   1205 C  C   . LYS A 1 148 ? -15.691 -16.134 13.702  1.00 10.87  ? 149 LYS A C   1 
ATOM   1206 O  O   . LYS A 1 148 ? -16.472 -15.462 13.030  1.00 12.38  ? 149 LYS A O   1 
ATOM   1207 C  CB  . LYS A 1 148 ? -15.954 -16.290 16.201  1.00 13.57  ? 149 LYS A CB  1 
ATOM   1208 C  CG  . LYS A 1 148 ? -17.469 -16.132 16.184  1.00 15.08  ? 149 LYS A CG  1 
ATOM   1209 C  CD  . LYS A 1 148 ? -18.136 -16.814 17.405  1.00 20.98  ? 149 LYS A CD  1 
ATOM   1210 C  CE  . LYS A 1 148 ? -19.638 -16.809 17.316  1.00 30.31  ? 149 LYS A CE  1 
ATOM   1211 N  NZ  . LYS A 1 148 ? -20.270 -17.711 18.317  1.00 42.64  ? 149 LYS A NZ  1 
ATOM   1212 N  N   . VAL A 1 149 ? -15.219 -17.333 13.322  1.00 12.08  ? 150 VAL A N   1 
ATOM   1213 C  CA  . VAL A 1 149 ? -15.582 -17.864 12.014  1.00 11.64  ? 150 VAL A CA  1 
ATOM   1214 C  C   . VAL A 1 149 ? -16.767 -18.807 12.170  1.00 12.66  ? 150 VAL A C   1 
ATOM   1215 O  O   . VAL A 1 149 ? -16.725 -19.805 12.916  1.00 15.12  ? 150 VAL A O   1 
ATOM   1216 C  CB  . VAL A 1 149 ? -14.355 -18.534 11.358  1.00 12.88  ? 150 VAL A CB  1 
ATOM   1217 C  CG1 . VAL A 1 149 ? -14.770 -19.261 10.093  1.00 15.02  ? 150 VAL A CG1 1 
ATOM   1218 C  CG2 . VAL A 1 149 ? -13.269 -17.490 11.175  1.00 16.23  ? 150 VAL A CG2 1 
ATOM   1219 N  N   . GLY A 1 150 ? -17.801 -18.587 11.386  1.00 12.00  ? 151 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 150 ? -19.003 -19.431 11.412  1.00 13.71  ? 151 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 150 ? -19.919 -18.949 10.288  1.00 12.80  ? 151 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 150 ? -19.582 -19.027 9.127   1.00 12.54  ? 151 GLY A O   1 
ATOM   1223 N  N   A SER A 1 151 ? -21.090 -18.414 10.653  0.50 14.15  ? 152 SER A N   1 
ATOM   1224 N  N   B SER A 1 151 ? -21.051 -18.365 10.707  0.50 13.53  ? 152 SER A N   1 
ATOM   1225 C  CA  A SER A 1 151 ? -21.966 -17.847 9.626   0.50 14.71  ? 152 SER A CA  1 
ATOM   1226 C  CA  B SER A 1 151 ? -21.991 -17.725 9.790   0.50 13.68  ? 152 SER A CA  1 
ATOM   1227 C  C   A SER A 1 151 ? -21.434 -16.495 9.153   0.50 12.15  ? 152 SER A C   1 
ATOM   1228 C  C   B SER A 1 151 ? -21.355 -16.488 9.137   0.50 11.83  ? 152 SER A C   1 
ATOM   1229 O  O   A SER A 1 151 ? -20.802 -15.764 9.935   0.50 11.66  ? 152 SER A O   1 
ATOM   1230 O  O   B SER A 1 151 ? -20.480 -15.857 9.744   0.50 12.23  ? 152 SER A O   1 
ATOM   1231 C  CB  A SER A 1 151 ? -23.347 -17.643 10.149  0.50 18.10  ? 152 SER A CB  1 
ATOM   1232 C  CB  B SER A 1 151 ? -23.287 -17.392 10.510  0.50 14.75  ? 152 SER A CB  1 
ATOM   1233 O  OG  A SER A 1 151 ? -23.260 -16.840 11.297  0.50 21.13  ? 152 SER A OG  1 
ATOM   1234 O  OG  B SER A 1 151 ? -23.905 -18.582 11.011  0.50 21.02  ? 152 SER A OG  1 
ATOM   1235 N  N   . ALA A 1 152 ? -21.788 -16.157 7.900   1.00 12.06  ? 153 ALA A N   1 
ATOM   1236 C  CA  . ALA A 1 152 ? -21.355 -14.895 7.335   1.00 11.84  ? 153 ALA A CA  1 
ATOM   1237 C  C   . ALA A 1 152 ? -22.002 -13.679 7.997   1.00 11.91  ? 153 ALA A C   1 
ATOM   1238 O  O   . ALA A 1 152 ? -23.106 -13.757 8.523   1.00 13.21  ? 153 ALA A O   1 
ATOM   1239 C  CB  . ALA A 1 152 ? -21.723 -14.867 5.856   1.00 13.83  ? 153 ALA A CB  1 
ATOM   1240 N  N   . LYS A 1 153 ? -21.261 -12.558 7.932   1.00 10.83  ? 154 LYS A N   1 
ATOM   1241 C  CA  . LYS A 1 153 ? -21.824 -11.279 8.368   1.00 10.55  ? 154 LYS A CA  1 
ATOM   1242 C  C   . LYS A 1 153 ? -22.260 -10.559 7.094   1.00 10.93  ? 154 LYS A C   1 
ATOM   1243 O  O   . LYS A 1 153 ? -21.406 -10.049 6.341   1.00 10.67  ? 154 LYS A O   1 
ATOM   1244 C  CB  . LYS A 1 153 ? -20.754 -10.476 9.149   1.00 10.80  ? 154 LYS A CB  1 
ATOM   1245 C  CG  . LYS A 1 153 ? -21.322 -9.266  9.879   1.00 12.42  ? 154 LYS A CG  1 
ATOM   1246 C  CD  . LYS A 1 153 ? -22.252 -9.605  11.024  1.00 13.85  ? 154 LYS A CD  1 
ATOM   1247 C  CE  . LYS A 1 153 ? -22.497 -8.407  11.956  1.00 17.87  ? 154 LYS A CE  1 
ATOM   1248 N  NZ  . LYS A 1 153 ? -23.642 -8.722  12.859  1.00 26.87  ? 154 LYS A NZ  1 
ATOM   1249 N  N   . PRO A 1 154 ? -23.553 -10.401 6.805   1.00 11.03  ? 155 PRO A N   1 
ATOM   1250 C  CA  . PRO A 1 154 ? -23.941 -9.813  5.518   1.00 12.58  ? 155 PRO A CA  1 
ATOM   1251 C  C   . PRO A 1 154 ? -23.404 -8.393  5.367   1.00 12.36  ? 155 PRO A C   1 
ATOM   1252 O  O   . PRO A 1 154 ? -23.022 -8.007  4.261   1.00 13.04  ? 155 PRO A O   1 
ATOM   1253 C  CB  . PRO A 1 154 ? -25.484 -9.851  5.584   1.00 14.95  ? 155 PRO A CB  1 
ATOM   1254 C  CG  . PRO A 1 154 ? -25.746 -11.087 6.455   1.00 17.44  ? 155 PRO A CG  1 
ATOM   1255 C  CD  . PRO A 1 154 ? -24.712 -10.960 7.562   1.00 13.92  ? 155 PRO A CD  1 
ATOM   1256 N  N   . GLY A 1 155 ? -23.340 -7.634  6.467   1.00 11.74  ? 156 GLY A N   1 
ATOM   1257 C  CA  . GLY A 1 155 ? -22.906 -6.236  6.437   1.00 13.44  ? 156 GLY A CA  1 
ATOM   1258 C  C   . GLY A 1 155 ? -21.405 -6.086  6.155   1.00 11.59  ? 156 GLY A C   1 
ATOM   1259 O  O   . GLY A 1 155 ? -20.963 -4.959  5.906   1.00 13.74  ? 156 GLY A O   1 
ATOM   1260 N  N   . LEU A 1 156 ? -20.629 -7.169  6.213   1.00 10.49  ? 157 LEU A N   1 
ATOM   1261 C  CA  . LEU A 1 156 ? -19.224 -7.086  5.876   1.00 10.28  ? 157 LEU A CA  1 
ATOM   1262 C  C   . LEU A 1 156 ? -18.978 -7.333  4.410   1.00 9.68   ? 157 LEU A C   1 
ATOM   1263 O  O   . LEU A 1 156 ? -17.888 -7.077  3.862   1.00 10.29  ? 157 LEU A O   1 
ATOM   1264 C  CB  . LEU A 1 156 ? -18.500 -8.143  6.717   1.00 11.41  ? 157 LEU A CB  1 
ATOM   1265 C  CG  . LEU A 1 156 ? -16.974 -8.276  6.528   1.00 11.07  ? 157 LEU A CG  1 
ATOM   1266 C  CD1 . LEU A 1 156 ? -16.245 -6.973  6.878   1.00 12.36  ? 157 LEU A CD1 1 
ATOM   1267 C  CD2 . LEU A 1 156 ? -16.436 -9.450  7.386   1.00 13.32  ? 157 LEU A CD2 1 
ATOM   1268 N  N   . GLN A 1 157 ? -19.983 -7.877  3.660   1.00 10.31  ? 158 GLN A N   1 
ATOM   1269 C  CA  . GLN A 1 157 ? -19.715 -8.349  2.315   1.00 10.92  ? 158 GLN A CA  1 
ATOM   1270 C  C   . GLN A 1 157 ? -19.265 -7.225  1.391   1.00 10.06  ? 158 GLN A C   1 
ATOM   1271 O  O   . GLN A 1 157 ? -18.401 -7.456  0.555   1.00 10.88  ? 158 GLN A O   1 
ATOM   1272 C  CB  . GLN A 1 157 ? -20.921 -9.142  1.786   1.00 11.64  ? 158 GLN A CB  1 
ATOM   1273 C  CG  . GLN A 1 157 ? -20.591 -9.917  0.499   1.00 12.91  ? 158 GLN A CG  1 
ATOM   1274 C  CD  . GLN A 1 157 ? -19.564 -11.002 0.729   1.00 12.12  ? 158 GLN A CD  1 
ATOM   1275 O  OE1 . GLN A 1 157 ? -19.386 -11.515 1.871   1.00 12.77  ? 158 GLN A OE1 1 
ATOM   1276 N  NE2 . GLN A 1 157 ? -18.785 -11.269 -0.306  1.00 14.19  ? 158 GLN A NE2 1 
ATOM   1277 N  N   . LYS A 1 158 ? -19.830 -6.018  1.515   1.00 11.03  ? 159 LYS A N   1 
ATOM   1278 C  CA  . LYS A 1 158 ? -19.437 -4.931  0.632   1.00 11.58  ? 159 LYS A CA  1 
ATOM   1279 C  C   . LYS A 1 158 ? -17.912 -4.643  0.771   1.00 10.75  ? 159 LYS A C   1 
ATOM   1280 O  O   . LYS A 1 158 ? -17.247 -4.263  -0.225  1.00 12.55  ? 159 LYS A O   1 
ATOM   1281 C  CB  . LYS A 1 158 ? -20.264 -3.672  0.948   1.00 13.95  ? 159 LYS A CB  1 
ATOM   1282 C  CG  . LYS A 1 158 ? -19.951 -2.454  0.080   1.00 17.78  ? 159 LYS A CG  1 
ATOM   1283 C  CD  . LYS A 1 158 ? -20.951 -1.289  0.371   1.00 22.23  ? 159 LYS A CD  1 
ATOM   1284 C  CE  . LYS A 1 158 ? -20.641 0.044   -0.308  1.00 29.71  ? 159 LYS A CE  1 
ATOM   1285 N  NZ  . LYS A 1 158 ? -20.834 0.016   -1.805  1.00 21.77  ? 159 LYS A NZ  1 
ATOM   1286 N  N   . VAL A 1 159 ? -17.384 -4.748  2.012   1.00 10.16  ? 160 VAL A N   1 
ATOM   1287 C  CA  . VAL A 1 159 ? -15.945 -4.579  2.232   1.00 10.37  ? 160 VAL A CA  1 
ATOM   1288 C  C   . VAL A 1 159 ? -15.159 -5.702  1.544   1.00 9.57   ? 160 VAL A C   1 
ATOM   1289 O  O   . VAL A 1 159 ? -14.225 -5.439  0.777   1.00 11.10  ? 160 VAL A O   1 
ATOM   1290 C  CB  . VAL A 1 159 ? -15.637 -4.541  3.724   1.00 11.53  ? 160 VAL A CB  1 
ATOM   1291 C  CG1 . VAL A 1 159 ? -14.124 -4.637  3.948   1.00 13.91  ? 160 VAL A CG1 1 
ATOM   1292 C  CG2 . VAL A 1 159 ? -16.206 -3.295  4.361   1.00 14.58  ? 160 VAL A CG2 1 
ATOM   1293 N  N   . VAL A 1 160 ? -15.529 -6.955  1.834   1.00 9.83   ? 161 VAL A N   1 
ATOM   1294 C  CA  . VAL A 1 160 ? -14.698 -8.032  1.309   1.00 12.38  ? 161 VAL A CA  1 
ATOM   1295 C  C   . VAL A 1 160 ? -14.704 -8.042  -0.204  1.00 10.26  ? 161 VAL A C   1 
ATOM   1296 O  O   . VAL A 1 160 ? -13.669 -8.396  -0.828  1.00 11.44  ? 161 VAL A O   1 
ATOM   1297 C  CB  . VAL A 1 160 ? -14.786 -9.377  2.040   1.00 15.04  ? 161 VAL A CB  1 
ATOM   1298 C  CG1 . VAL A 1 160 ? -14.472 -9.319  3.522   1.00 18.97  ? 161 VAL A CG1 1 
ATOM   1299 C  CG2 . VAL A 1 160 ? -16.157 -9.820  1.849   1.00 16.53  ? 161 VAL A CG2 1 
ATOM   1300 N  N   . ASP A 1 161 ? -15.806 -7.670  -0.865  1.00 10.46  ? 162 ASP A N   1 
ATOM   1301 C  CA  . ASP A 1 161 ? -15.893 -7.727  -2.314  1.00 11.93  ? 162 ASP A CA  1 
ATOM   1302 C  C   . ASP A 1 161 ? -15.042 -6.700  -3.015  1.00 11.71  ? 162 ASP A C   1 
ATOM   1303 O  O   . ASP A 1 161 ? -14.795 -6.867  -4.189  1.00 16.10  ? 162 ASP A O   1 
ATOM   1304 C  CB  . ASP A 1 161 ? -17.325 -7.623  -2.756  1.00 13.98  ? 162 ASP A CB  1 
ATOM   1305 C  CG  . ASP A 1 161 ? -18.056 -8.959  -2.642  1.00 14.59  ? 162 ASP A CG  1 
ATOM   1306 O  OD1 . ASP A 1 161 ? -17.409 -10.045 -2.719  1.00 17.97  ? 162 ASP A OD1 1 
ATOM   1307 O  OD2 . ASP A 1 161 ? -19.304 -8.943  -2.569  1.00 17.38  ? 162 ASP A OD2 1 
ATOM   1308 N  N   . VAL A 1 162 ? -14.516 -5.673  -2.334  1.00 11.65  ? 163 VAL A N   1 
ATOM   1309 C  CA  . VAL A 1 162 ? -13.644 -4.730  -3.023  1.00 12.61  ? 163 VAL A CA  1 
ATOM   1310 C  C   . VAL A 1 162 ? -12.177 -4.971  -2.704  1.00 11.56  ? 163 VAL A C   1 
ATOM   1311 O  O   . VAL A 1 162 ? -11.300 -4.302  -3.264  1.00 11.61  ? 163 VAL A O   1 
ATOM   1312 C  CB  . VAL A 1 162 ? -14.008 -3.305  -2.686  1.00 16.52  ? 163 VAL A CB  1 
ATOM   1313 C  CG1 . VAL A 1 162 ? -15.460 -3.000  -3.019  1.00 20.76  ? 163 VAL A CG1 1 
ATOM   1314 C  CG2 . VAL A 1 162 ? -13.710 -2.976  -1.231  1.00 15.00  ? 163 VAL A CG2 1 
ATOM   1315 N  N   . LEU A 1 163 ? -11.854 -5.962  -1.889  1.00 11.03  ? 164 LEU A N   1 
ATOM   1316 C  CA  . LEU A 1 163 ? -10.467 -6.141  -1.502  1.00 10.88  ? 164 LEU A CA  1 
ATOM   1317 C  C   . LEU A 1 163 ? -9.561  -6.543  -2.655  1.00 11.57  ? 164 LEU A C   1 
ATOM   1318 O  O   . LEU A 1 163 ? -8.385  -6.179  -2.660  1.00 11.51  ? 164 LEU A O   1 
ATOM   1319 C  CB  . LEU A 1 163 ? -10.325 -7.125  -0.352  1.00 10.58  ? 164 LEU A CB  1 
ATOM   1320 C  CG  . LEU A 1 163 ? -10.979 -6.689  0.980   1.00 10.17  ? 164 LEU A CG  1 
ATOM   1321 C  CD1 . LEU A 1 163 ? -10.822 -7.795  2.043   1.00 12.43  ? 164 LEU A CD1 1 
ATOM   1322 C  CD2 . LEU A 1 163 ? -10.409 -5.383  1.478   1.00 12.23  ? 164 LEU A CD2 1 
ATOM   1323 N  N   . ASP A 1 164 ? -10.099 -7.221  -3.655  1.00 11.83  ? 165 ASP A N   1 
ATOM   1324 C  CA  . ASP A 1 164 ? -9.288  -7.552  -4.822  1.00 14.56  ? 165 ASP A CA  1 
ATOM   1325 C  C   . ASP A 1 164 ? -8.785  -6.304  -5.551  1.00 13.35  ? 165 ASP A C   1 
ATOM   1326 O  O   . ASP A 1 164 ? -7.786  -6.397  -6.292  1.00 17.34  ? 165 ASP A O   1 
ATOM   1327 C  CB  . ASP A 1 164 ? -10.064 -8.396  -5.844  1.00 18.11  ? 165 ASP A CB  1 
ATOM   1328 C  CG  . ASP A 1 164 ? -11.090 -7.540  -6.583  1.00 23.10  ? 165 ASP A CG  1 
ATOM   1329 O  OD1 . ASP A 1 164 ? -12.069 -7.118  -5.925  1.00 24.38  ? 165 ASP A OD1 1 
ATOM   1330 O  OD2 . ASP A 1 164 ? -10.897 -7.288  -7.841  1.00 32.24  ? 165 ASP A OD2 1 
ATOM   1331 N  N   . SER A 1 165 ? -9.434  -5.135  -5.337  1.00 12.13  ? 166 SER A N   1 
ATOM   1332 C  CA  . SER A 1 165 ? -8.983  -3.912  -6.000  1.00 12.42  ? 166 SER A CA  1 
ATOM   1333 C  C   . SER A 1 165 ? -7.886  -3.191  -5.215  1.00 11.69  ? 166 SER A C   1 
ATOM   1334 O  O   . SER A 1 165 ? -7.340  -2.214  -5.736  1.00 13.39  ? 166 SER A O   1 
ATOM   1335 C  CB  . SER A 1 165 ? -10.141 -2.996  -6.237  1.00 15.50  ? 166 SER A CB  1 
ATOM   1336 O  OG  . SER A 1 165 ? -10.577 -2.391  -5.042  1.00 14.62  ? 166 SER A OG  1 
ATOM   1337 N  N   . ILE A 1 166 ? -7.580  -3.619  -3.996  1.00 10.31  ? 167 ILE A N   1 
ATOM   1338 C  CA  . ILE A 1 166 ? -6.529  -3.006  -3.184  1.00 10.82  ? 167 ILE A CA  1 
ATOM   1339 C  C   . ILE A 1 166 ? -5.597  -4.087  -2.663  1.00 9.70   ? 167 ILE A C   1 
ATOM   1340 O  O   . ILE A 1 166 ? -5.180  -4.096  -1.491  1.00 10.70  ? 167 ILE A O   1 
ATOM   1341 C  CB  . ILE A 1 166 ? -7.126  -2.167  -2.039  1.00 10.16  ? 167 ILE A CB  1 
ATOM   1342 C  CG1 . ILE A 1 166 ? -8.056  -2.956  -1.121  1.00 10.43  ? 167 ILE A CG1 1 
ATOM   1343 C  CG2 . ILE A 1 166 ? -7.842  -0.927  -2.628  1.00 12.38  ? 167 ILE A CG2 1 
ATOM   1344 C  CD1 . ILE A 1 166 ? -8.193  -2.289  0.238   1.00 11.00  ? 167 ILE A CD1 1 
ATOM   1345 N  N   . LYS A 1 167 ? -5.137  -4.987  -3.557  1.00 11.18  ? 168 LYS A N   1 
ATOM   1346 C  CA  . LYS A 1 167 ? -4.430  -6.189  -3.102  1.00 11.25  ? 168 LYS A CA  1 
ATOM   1347 C  C   . LYS A 1 167 ? -3.106  -5.849  -2.432  1.00 11.19  ? 168 LYS A C   1 
ATOM   1348 O  O   . LYS A 1 167 ? -2.702  -6.515  -1.469  1.00 12.74  ? 168 LYS A O   1 
ATOM   1349 C  CB  . LYS A 1 167 ? -4.172  -7.124  -4.299  1.00 13.93  ? 168 LYS A CB  1 
ATOM   1350 C  CG  . LYS A 1 167 ? -3.478  -8.430  -3.910  1.00 15.73  ? 168 LYS A CG  1 
ATOM   1351 C  CD  . LYS A 1 167 ? -3.195  -9.370  -5.080  1.00 20.88  ? 168 LYS A CD  1 
ATOM   1352 C  CE  . LYS A 1 167 ? -2.159  -10.430 -4.839  1.00 34.54  ? 168 LYS A CE  1 
ATOM   1353 N  N   . THR A 1 168 ? -2.399  -4.847  -2.987  1.00 11.62  ? 169 THR A N   1 
ATOM   1354 C  CA  . THR A 1 168 ? -1.005  -4.571  -2.542  1.00 12.07  ? 169 THR A CA  1 
ATOM   1355 C  C   . THR A 1 168 ? -0.913  -3.207  -1.895  1.00 10.95  ? 169 THR A C   1 
ATOM   1356 O  O   . THR A 1 168 ? -1.759  -2.287  -2.025  1.00 11.69  ? 169 THR A O   1 
ATOM   1357 C  CB  . THR A 1 168 ? -0.039  -4.705  -3.722  1.00 13.00  ? 169 THR A CB  1 
ATOM   1358 O  OG1 . THR A 1 168 ? -0.587  -3.924  -4.791  1.00 14.02  ? 169 THR A OG1 1 
ATOM   1359 C  CG2 . THR A 1 168 ? 0.125   -6.135  -4.186  1.00 14.68  ? 169 THR A CG2 1 
ATOM   1360 N  N   . LYS A 1 169 ? 0.174   -3.048  -1.148  1.00 12.00  ? 170 LYS A N   1 
ATOM   1361 C  CA  . LYS A 1 169 ? 0.449   -1.834  -0.391  1.00 10.80  ? 170 LYS A CA  1 
ATOM   1362 C  C   . LYS A 1 169 ? 0.423   -0.636  -1.296  1.00 11.15  ? 170 LYS A C   1 
ATOM   1363 O  O   . LYS A 1 169 ? 1.057   -0.602  -2.372  1.00 13.36  ? 170 LYS A O   1 
ATOM   1364 C  CB  . LYS A 1 169 ? 1.827   -1.935  0.266   1.00 12.86  ? 170 LYS A CB  1 
ATOM   1365 C  CG  . LYS A 1 169 ? 2.276   -0.680  0.984   1.00 13.61  ? 170 LYS A CG  1 
ATOM   1366 C  CD  . LYS A 1 169 ? 3.656   -0.861  1.657   1.00 16.65  ? 170 LYS A CD  1 
ATOM   1367 C  CE  . LYS A 1 169 ? 4.069   0.489   2.217   1.00 29.93  ? 170 LYS A CE  1 
ATOM   1368 N  NZ  . LYS A 1 169 ? 5.491   0.455   2.670   1.00 40.98  ? 170 LYS A NZ  1 
ATOM   1369 N  N   . GLY A 1 170 ? -0.310  0.409   -0.834  1.00 10.60  ? 171 GLY A N   1 
ATOM   1370 C  CA  . GLY A 1 170 ? -0.423  1.691   -1.504  1.00 12.91  ? 171 GLY A CA  1 
ATOM   1371 C  C   . GLY A 1 170 ? -1.627  1.776   -2.435  1.00 13.02  ? 171 GLY A C   1 
ATOM   1372 O  O   . GLY A 1 170 ? -1.869  2.882   -2.959  1.00 14.79  ? 171 GLY A O   1 
ATOM   1373 N  N   . LYS A 1 171 ? -2.390  0.716   -2.629  1.00 10.87  ? 172 LYS A N   1 
ATOM   1374 C  CA  . LYS A 1 171 ? -3.587  0.826   -3.473  1.00 10.78  ? 172 LYS A CA  1 
ATOM   1375 C  C   . LYS A 1 171 ? -4.757  1.329   -2.639  1.00 10.80  ? 172 LYS A C   1 
ATOM   1376 O  O   . LYS A 1 171 ? -4.938  0.950   -1.507  1.00 12.35  ? 172 LYS A O   1 
ATOM   1377 C  CB  . LYS A 1 171 ? -3.911  -0.510  -4.092  1.00 11.94  ? 172 LYS A CB  1 
ATOM   1378 C  CG  . LYS A 1 171 ? -2.907  -0.964  -5.131  1.00 15.86  ? 172 LYS A CG  1 
ATOM   1379 C  CD  . LYS A 1 171 ? -3.351  -2.073  -6.036  1.00 18.91  ? 172 LYS A CD  1 
ATOM   1380 C  CE  . LYS A 1 171 ? -4.208  -1.489  -7.154  1.00 28.16  ? 172 LYS A CE  1 
ATOM   1381 N  NZ  . LYS A 1 171 ? -4.793  -2.593  -8.135  1.00 43.14  ? 172 LYS A NZ  1 
ATOM   1382 N  N   . SER A 1 172 ? -5.593  2.172   -3.267  1.00 10.29  ? 173 SER A N   1 
ATOM   1383 C  CA  . SER A 1 172 ? -6.789  2.673   -2.615  1.00 10.40  ? 173 SER A CA  1 
ATOM   1384 C  C   . SER A 1 172 ? -7.908  2.718   -3.655  1.00 9.55   ? 173 SER A C   1 
ATOM   1385 O  O   . SER A 1 172 ? -7.688  2.679   -4.867  1.00 12.18  ? 173 SER A O   1 
ATOM   1386 C  CB  . SER A 1 172 ? -6.546  4.018   -1.941  1.00 11.93  ? 173 SER A CB  1 
ATOM   1387 O  OG  . SER A 1 172 ? -6.281  5.089   -2.854  1.00 14.26  ? 173 SER A OG  1 
ATOM   1388 N  N   . ALA A 1 173 ? -9.161  2.925   -3.136  1.00 10.84  ? 174 ALA A N   1 
ATOM   1389 C  CA  . ALA A 1 173 ? -10.295 3.078   -4.021  1.00 11.75  ? 174 ALA A CA  1 
ATOM   1390 C  C   . ALA A 1 173 ? -11.335 3.926   -3.301  1.00 11.00  ? 174 ALA A C   1 
ATOM   1391 O  O   . ALA A 1 173 ? -11.404 3.941   -2.079  1.00 10.70  ? 174 ALA A O   1 
ATOM   1392 C  CB  . ALA A 1 173 ? -10.901 1.711   -4.298  1.00 13.05  ? 174 ALA A CB  1 
ATOM   1393 N  N   A ASP A 1 174 ? -12.249 4.446   -4.094  0.50 12.40  ? 175 ASP A N   1 
ATOM   1394 N  N   B ASP A 1 174 ? -12.175 4.659   -4.038  0.50 11.54  ? 175 ASP A N   1 
ATOM   1395 C  CA  A ASP A 1 174 ? -13.410 5.131   -3.570  0.50 12.32  ? 175 ASP A CA  1 
ATOM   1396 C  CA  B ASP A 1 174 ? -13.358 5.285   -3.440  0.50 11.81  ? 175 ASP A CA  1 
ATOM   1397 C  C   A ASP A 1 174 ? -14.278 4.088   -2.863  0.50 12.23  ? 175 ASP A C   1 
ATOM   1398 C  C   B ASP A 1 174 ? -14.239 4.175   -2.879  0.50 11.34  ? 175 ASP A C   1 
ATOM   1399 O  O   A ASP A 1 174 ? -14.359 2.924   -3.230  0.50 12.78  ? 175 ASP A O   1 
ATOM   1400 O  O   B ASP A 1 174 ? -14.328 3.082   -3.427  0.50 13.01  ? 175 ASP A O   1 
ATOM   1401 C  CB  A ASP A 1 174 ? -14.091 5.905   -4.718  0.50 15.48  ? 175 ASP A CB  1 
ATOM   1402 C  CB  B ASP A 1 174 ? -14.210 6.145   -4.412  0.50 13.34  ? 175 ASP A CB  1 
ATOM   1403 C  CG  A ASP A 1 174 ? -13.308 7.113   -5.215  0.50 19.92  ? 175 ASP A CG  1 
ATOM   1404 C  CG  B ASP A 1 174 ? -14.911 5.370   -5.537  0.50 15.76  ? 175 ASP A CG  1 
ATOM   1405 O  OD1 A ASP A 1 174 ? -12.993 7.935   -4.392  0.50 23.78  ? 175 ASP A OD1 1 
ATOM   1406 O  OD1 B ASP A 1 174 ? -14.245 5.046   -6.540  0.50 24.96  ? 175 ASP A OD1 1 
ATOM   1407 O  OD2 A ASP A 1 174 ? -13.053 7.249   -6.454  0.50 24.40  ? 175 ASP A OD2 1 
ATOM   1408 O  OD2 B ASP A 1 174 ? -16.136 5.144   -5.418  0.50 20.72  ? 175 ASP A OD2 1 
ATOM   1409 N  N   . PHE A 1 175 ? -14.908 4.486   -1.764  1.00 10.52  ? 176 PHE A N   1 
ATOM   1410 C  CA  . PHE A 1 175 ? -15.691 3.495   -1.024  1.00 10.79  ? 176 PHE A CA  1 
ATOM   1411 C  C   . PHE A 1 175 ? -16.775 4.248   -0.234  1.00 10.67  ? 176 PHE A C   1 
ATOM   1412 O  O   . PHE A 1 175 ? -16.594 4.508   0.935   1.00 11.64  ? 176 PHE A O   1 
ATOM   1413 C  CB  . PHE A 1 175 ? -14.773 2.684   -0.090  1.00 11.42  ? 176 PHE A CB  1 
ATOM   1414 C  CG  . PHE A 1 175 ? -15.424 1.457   0.481   1.00 10.67  ? 176 PHE A CG  1 
ATOM   1415 C  CD1 . PHE A 1 175 ? -15.776 0.390   -0.357  1.00 12.98  ? 176 PHE A CD1 1 
ATOM   1416 C  CD2 . PHE A 1 175 ? -15.721 1.344   1.833   1.00 11.73  ? 176 PHE A CD2 1 
ATOM   1417 C  CE1 . PHE A 1 175 ? -16.374 -0.774  0.130   1.00 13.74  ? 176 PHE A CE1 1 
ATOM   1418 C  CE2 . PHE A 1 175 ? -16.326 0.181   2.313   1.00 12.57  ? 176 PHE A CE2 1 
ATOM   1419 C  CZ  . PHE A 1 175 ? -16.650 -0.848  1.472   1.00 13.24  ? 176 PHE A CZ  1 
ATOM   1420 N  N   . THR A 1 176 ? -17.851 4.592   -0.931  1.00 11.34  ? 177 THR A N   1 
ATOM   1421 C  CA  . THR A 1 176 ? -18.880 5.448   -0.363  1.00 11.08  ? 177 THR A CA  1 
ATOM   1422 C  C   . THR A 1 176 ? -20.058 4.596   0.069   1.00 10.01  ? 177 THR A C   1 
ATOM   1423 O  O   . THR A 1 176 ? -20.259 3.436   -0.349  1.00 11.79  ? 177 THR A O   1 
ATOM   1424 C  CB  . THR A 1 176 ? -19.351 6.526   -1.340  1.00 13.39  ? 177 THR A CB  1 
ATOM   1425 O  OG1 . THR A 1 176 ? -19.767 5.936   -2.576  1.00 15.49  ? 177 THR A OG1 1 
ATOM   1426 C  CG2 . THR A 1 176 ? -18.267 7.561   -1.576  1.00 19.93  ? 177 THR A CG2 1 
ATOM   1427 N  N   . ASN A 1 177 ? -20.882 5.179   0.937   1.00 10.34  ? 178 ASN A N   1 
ATOM   1428 C  CA  . ASN A 1 177 ? -22.161 4.619   1.393   1.00 11.59  ? 178 ASN A CA  1 
ATOM   1429 C  C   . ASN A 1 177 ? -21.987 3.294   2.122   1.00 12.35  ? 178 ASN A C   1 
ATOM   1430 O  O   . ASN A 1 177 ? -22.923 2.488   2.138   1.00 16.54  ? 178 ASN A O   1 
ATOM   1431 C  CB  . ASN A 1 177 ? -23.189 4.491   0.251   1.00 12.20  ? 178 ASN A CB  1 
ATOM   1432 C  CG  . ASN A 1 177 ? -23.496 5.883   -0.285  1.00 12.90  ? 178 ASN A CG  1 
ATOM   1433 O  OD1 . ASN A 1 177 ? -24.199 6.648   0.344   1.00 15.88  ? 178 ASN A OD1 1 
ATOM   1434 N  ND2 . ASN A 1 177 ? -22.963 6.144   -1.455  1.00 13.61  ? 178 ASN A ND2 1 
ATOM   1435 N  N   . PHE A 1 178 ? -20.856 3.044   2.777   1.00 10.69  ? 179 PHE A N   1 
ATOM   1436 C  CA  . PHE A 1 178 ? -20.722 1.855   3.599   1.00 10.05  ? 179 PHE A CA  1 
ATOM   1437 C  C   . PHE A 1 178 ? -21.270 2.183   4.980   1.00 10.88  ? 179 PHE A C   1 
ATOM   1438 O  O   . PHE A 1 178 ? -20.863 3.179   5.588   1.00 12.30  ? 179 PHE A O   1 
ATOM   1439 C  CB  . PHE A 1 178 ? -19.255 1.414   3.705   1.00 11.28  ? 179 PHE A CB  1 
ATOM   1440 C  CG  . PHE A 1 178 ? -19.214 0.185   4.570   1.00 10.66  ? 179 PHE A CG  1 
ATOM   1441 C  CD1 . PHE A 1 178 ? -19.604 -1.071  4.052   1.00 12.02  ? 179 PHE A CD1 1 
ATOM   1442 C  CD2 . PHE A 1 178 ? -18.811 0.271   5.916   1.00 11.01  ? 179 PHE A CD2 1 
ATOM   1443 C  CE1 . PHE A 1 178 ? -19.683 -2.180  4.884   1.00 11.97  ? 179 PHE A CE1 1 
ATOM   1444 C  CE2 . PHE A 1 178 ? -18.879 -0.876  6.726   1.00 11.21  ? 179 PHE A CE2 1 
ATOM   1445 C  CZ  . PHE A 1 178 ? -19.313 -2.063  6.219   1.00 10.54  ? 179 PHE A CZ  1 
ATOM   1446 N  N   . ASP A 1 179 ? -22.166 1.324   5.472   1.00 10.79  ? 180 ASP A N   1 
ATOM   1447 C  CA  . ASP A 1 179 ? -22.820 1.587   6.759   1.00 11.09  ? 180 ASP A CA  1 
ATOM   1448 C  C   . ASP A 1 179 ? -22.151 0.747   7.839   1.00 10.12  ? 180 ASP A C   1 
ATOM   1449 O  O   . ASP A 1 179 ? -22.362 -0.483  7.936   1.00 10.84  ? 180 ASP A O   1 
ATOM   1450 C  CB  . ASP A 1 179 ? -24.298 1.221   6.671   1.00 13.23  ? 180 ASP A CB  1 
ATOM   1451 C  CG  . ASP A 1 179 ? -25.107 1.573   7.897   1.00 14.76  ? 180 ASP A CG  1 
ATOM   1452 O  OD1 . ASP A 1 179 ? -24.534 1.879   8.945   1.00 13.47  ? 180 ASP A OD1 1 
ATOM   1453 O  OD2 . ASP A 1 179 ? -26.342 1.547   7.803   1.00 22.71  ? 180 ASP A OD2 1 
ATOM   1454 N  N   . PRO A 1 180 ? -21.372 1.326   8.777   1.00 9.94   ? 181 PRO A N   1 
ATOM   1455 C  CA  . PRO A 1 180 ? -20.696 0.517   9.799   1.00 11.03  ? 181 PRO A CA  1 
ATOM   1456 C  C   . PRO A 1 180 ? -21.638 -0.095  10.818  1.00 10.16  ? 181 PRO A C   1 
ATOM   1457 O  O   . PRO A 1 180 ? -21.177 -0.960  11.589  1.00 11.69  ? 181 PRO A O   1 
ATOM   1458 C  CB  . PRO A 1 180 ? -19.675 1.494   10.382  1.00 12.82  ? 181 PRO A CB  1 
ATOM   1459 C  CG  . PRO A 1 180 ? -20.322 2.860   10.187  1.00 12.40  ? 181 PRO A CG  1 
ATOM   1460 C  CD  . PRO A 1 180 ? -21.017 2.756   8.844   1.00 11.48  ? 181 PRO A CD  1 
ATOM   1461 N  N   . ARG A 1 181 ? -22.905 0.328   10.862  1.00 11.13  ? 182 ARG A N   1 
ATOM   1462 C  CA  . ARG A 1 181 ? -23.836 -0.341  11.746  1.00 10.51  ? 182 ARG A CA  1 
ATOM   1463 C  C   . ARG A 1 181 ? -23.941 -1.829  11.415  1.00 11.05  ? 182 ARG A C   1 
ATOM   1464 O  O   . ARG A 1 181 ? -24.316 -2.636  12.283  1.00 12.31  ? 182 ARG A O   1 
ATOM   1465 C  CB  . ARG A 1 181 ? -25.225 0.299   11.671  1.00 11.87  ? 182 ARG A CB  1 
ATOM   1466 C  CG  . ARG A 1 181 ? -25.240 1.723   12.210  1.00 14.04  ? 182 ARG A CG  1 
ATOM   1467 C  CD  . ARG A 1 181 ? -26.563 2.452   12.141  1.00 15.77  ? 182 ARG A CD  1 
ATOM   1468 N  NE  . ARG A 1 181 ? -26.850 2.640   10.729  1.00 15.61  ? 182 ARG A NE  1 
ATOM   1469 C  CZ  . ARG A 1 181 ? -27.885 3.378   10.342  1.00 16.69  ? 182 ARG A CZ  1 
ATOM   1470 N  NH1 . ARG A 1 181 ? -28.673 3.944   11.245  1.00 23.07  ? 182 ARG A NH1 1 
ATOM   1471 N  NH2 . ARG A 1 181 ? -28.108 3.559   9.041   1.00 20.40  ? 182 ARG A NH2 1 
ATOM   1472 N  N   . GLY A 1 182 ? -23.679 -2.204  10.165  1.00 11.24  ? 183 GLY A N   1 
ATOM   1473 C  CA  . GLY A 1 182 ? -23.811 -3.622  9.796   1.00 12.18  ? 183 GLY A CA  1 
ATOM   1474 C  C   . GLY A 1 182 ? -22.670 -4.484  10.300  1.00 12.31  ? 183 GLY A C   1 
ATOM   1475 O  O   . GLY A 1 182 ? -22.653 -5.669  9.986   1.00 13.17  ? 183 GLY A O   1 
ATOM   1476 N  N   . LEU A 1 183 ? -21.691 -3.912  11.054  1.00 11.77  ? 184 LEU A N   1 
ATOM   1477 C  CA  . LEU A 1 183 ? -20.591 -4.682  11.633  1.00 11.62  ? 184 LEU A CA  1 
ATOM   1478 C  C   . LEU A 1 183 ? -20.778 -4.890  13.118  1.00 11.62  ? 184 LEU A C   1 
ATOM   1479 O  O   . LEU A 1 183 ? -19.881 -5.476  13.740  1.00 12.26  ? 184 LEU A O   1 
ATOM   1480 C  CB  . LEU A 1 183 ? -19.295 -3.938  11.346  1.00 11.50  ? 184 LEU A CB  1 
ATOM   1481 C  CG  . LEU A 1 183 ? -18.910 -3.781  9.886   1.00 12.15  ? 184 LEU A CG  1 
ATOM   1482 C  CD1 . LEU A 1 183 ? -17.643 -2.936  9.781   1.00 15.00  ? 184 LEU A CD1 1 
ATOM   1483 C  CD2 . LEU A 1 183 ? -18.795 -5.115  9.170   1.00 15.28  ? 184 LEU A CD2 1 
ATOM   1484 N  N   . LEU A 1 184 ? -21.887 -4.414  13.706  1.00 11.06  ? 185 LEU A N   1 
ATOM   1485 C  CA  . LEU A 1 184 ? -21.985 -4.465  15.165  1.00 11.48  ? 185 LEU A CA  1 
ATOM   1486 C  C   . LEU A 1 184 ? -22.772 -5.689  15.651  1.00 11.59  ? 185 LEU A C   1 
ATOM   1487 O  O   . LEU A 1 184 ? -23.772 -6.037  15.047  1.00 15.05  ? 185 LEU A O   1 
ATOM   1488 C  CB  . LEU A 1 184 ? -22.734 -3.192  15.647  1.00 11.45  ? 185 LEU A CB  1 
ATOM   1489 C  CG  . LEU A 1 184 ? -22.113 -1.832  15.227  1.00 12.56  ? 185 LEU A CG  1 
ATOM   1490 C  CD1 . LEU A 1 184 ? -22.961 -0.681  15.738  1.00 14.27  ? 185 LEU A CD1 1 
ATOM   1491 C  CD2 . LEU A 1 184 ? -20.669 -1.750  15.721  1.00 15.54  ? 185 LEU A CD2 1 
ATOM   1492 N  N   . PRO A 1 185 ? -22.383 -6.283  16.790  1.00 11.07  ? 186 PRO A N   1 
ATOM   1493 C  CA  . PRO A 1 185 ? -23.161 -7.393  17.376  1.00 11.31  ? 186 PRO A CA  1 
ATOM   1494 C  C   . PRO A 1 185 ? -24.426 -6.829  18.035  1.00 9.73   ? 186 PRO A C   1 
ATOM   1495 O  O   . PRO A 1 185 ? -24.596 -5.607  18.134  1.00 12.02  ? 186 PRO A O   1 
ATOM   1496 C  CB  . PRO A 1 185 ? -22.207 -7.985  18.422  1.00 13.27  ? 186 PRO A CB  1 
ATOM   1497 C  CG  . PRO A 1 185 ? -21.421 -6.758  18.874  1.00 11.36  ? 186 PRO A CG  1 
ATOM   1498 C  CD  . PRO A 1 185 ? -21.235 -5.901  17.616  1.00 10.97  ? 186 PRO A CD  1 
ATOM   1499 N  N   . GLU A 1 186 ? -25.279 -7.717  18.541  1.00 11.84  ? 187 GLU A N   1 
ATOM   1500 C  CA  . GLU A 1 186 ? -26.518 -7.283  19.178  1.00 12.03  ? 187 GLU A CA  1 
ATOM   1501 C  C   . GLU A 1 186 ? -26.222 -6.472  20.415  1.00 11.26  ? 187 GLU A C   1 
ATOM   1502 O  O   . GLU A 1 186 ? -26.818 -5.419  20.607  1.00 13.75  ? 187 GLU A O   1 
ATOM   1503 C  CB  . GLU A 1 186 ? -27.359 -8.482  19.613  1.00 15.43  ? 187 GLU A CB  1 
ATOM   1504 C  CG  . GLU A 1 186 ? -27.992 -9.244  18.505  1.00 17.80  ? 187 GLU A CG  1 
ATOM   1505 C  CD  . GLU A 1 186 ? -28.725 -10.518 18.985  1.00 16.96  ? 187 GLU A CD  1 
ATOM   1506 O  OE1 . GLU A 1 186 ? -28.787 -10.781 20.201  1.00 20.28  ? 187 GLU A OE1 1 
ATOM   1507 O  OE2 . GLU A 1 186 ? -29.240 -11.223 18.126  1.00 24.09  ? 187 GLU A OE2 1 
ATOM   1508 N  N   . SER A 1 187 ? -25.387 -6.999  21.331  1.00 12.45  ? 188 SER A N   1 
ATOM   1509 C  CA  . SER A 1 187 ? -25.129 -6.401  22.630  1.00 13.31  ? 188 SER A CA  1 
ATOM   1510 C  C   . SER A 1 187 ? -24.006 -5.359  22.559  1.00 12.41  ? 188 SER A C   1 
ATOM   1511 O  O   . SER A 1 187 ? -23.005 -5.586  21.889  1.00 13.40  ? 188 SER A O   1 
ATOM   1512 C  CB  . SER A 1 187 ? -24.766 -7.457  23.616  1.00 14.51  ? 188 SER A CB  1 
ATOM   1513 O  OG  . SER A 1 187 ? -24.472 -6.901  24.898  1.00 15.19  ? 188 SER A OG  1 
ATOM   1514 N  N   . LEU A 1 188 ? -24.160 -4.274  23.314  1.00 12.86  ? 189 LEU A N   1 
ATOM   1515 C  CA  . LEU A 1 188 ? -23.088 -3.305  23.505  1.00 12.64  ? 189 LEU A CA  1 
ATOM   1516 C  C   . LEU A 1 188 ? -22.481 -3.453  24.903  1.00 13.01  ? 189 LEU A C   1 
ATOM   1517 O  O   . LEU A 1 188 ? -21.760 -2.573  25.347  1.00 15.35  ? 189 LEU A O   1 
ATOM   1518 C  CB  . LEU A 1 188 ? -23.615 -1.865  23.285  1.00 14.48  ? 189 LEU A CB  1 
ATOM   1519 C  CG  . LEU A 1 188 ? -23.979 -1.472  21.847  1.00 13.86  ? 189 LEU A CG  1 
ATOM   1520 C  CD1 . LEU A 1 188 ? -24.491 -0.031  21.806  1.00 17.88  ? 189 LEU A CD1 1 
ATOM   1521 C  CD2 . LEU A 1 188 ? -22.858 -1.696  20.837  1.00 16.82  ? 189 LEU A CD2 1 
ATOM   1522 N  N   . ASP A 1 189 ? -22.620 -4.608  25.559  1.00 12.91  ? 190 ASP A N   1 
ATOM   1523 C  CA  . ASP A 1 189 ? -21.877 -4.823  26.795  1.00 12.59  ? 190 ASP A CA  1 
ATOM   1524 C  C   . ASP A 1 189 ? -20.380 -4.849  26.481  1.00 11.41  ? 190 ASP A C   1 
ATOM   1525 O  O   . ASP A 1 189 ? -19.931 -5.389  25.470  1.00 11.27  ? 190 ASP A O   1 
ATOM   1526 C  CB  . ASP A 1 189 ? -22.266 -6.144  27.385  1.00 16.62  ? 190 ASP A CB  1 
ATOM   1527 C  CG  . ASP A 1 189 ? -23.664 -6.148  28.022  1.00 19.87  ? 190 ASP A CG  1 
ATOM   1528 O  OD1 . ASP A 1 189 ? -24.312 -5.067  28.018  1.00 30.36  ? 190 ASP A OD1 1 
ATOM   1529 O  OD2 . ASP A 1 189 ? -24.103 -7.227  28.396  1.00 28.63  ? 190 ASP A OD2 1 
ATOM   1530 N  N   . TYR A 1 190 ? -19.573 -4.273  27.390  1.00 11.28  ? 191 TYR A N   1 
ATOM   1531 C  CA  . TYR A 1 190 ? -18.164 -4.048  27.052  1.00 10.46  ? 191 TYR A CA  1 
ATOM   1532 C  C   . TYR A 1 190 ? -17.292 -4.105  28.304  1.00 9.67   ? 191 TYR A C   1 
ATOM   1533 O  O   . TYR A 1 190 ? -17.739 -3.973  29.441  1.00 11.66  ? 191 TYR A O   1 
ATOM   1534 C  CB  . TYR A 1 190 ? -17.988 -2.669  26.394  1.00 11.23  ? 191 TYR A CB  1 
ATOM   1535 C  CG  . TYR A 1 190 ? -18.396 -1.484  27.251  1.00 10.50  ? 191 TYR A CG  1 
ATOM   1536 C  CD1 . TYR A 1 190 ? -17.467 -0.875  28.103  1.00 12.38  ? 191 TYR A CD1 1 
ATOM   1537 C  CD2 . TYR A 1 190 ? -19.669 -0.931  27.222  1.00 11.59  ? 191 TYR A CD2 1 
ATOM   1538 C  CE1 . TYR A 1 190 ? -17.841 0.200   28.913  1.00 12.41  ? 191 TYR A CE1 1 
ATOM   1539 C  CE2 . TYR A 1 190 ? -20.059 0.135   28.020  1.00 12.64  ? 191 TYR A CE2 1 
ATOM   1540 C  CZ  . TYR A 1 190 ? -19.134 0.711   28.885  1.00 13.48  ? 191 TYR A CZ  1 
ATOM   1541 O  OH  . TYR A 1 190 ? -19.473 1.741   29.700  1.00 15.58  ? 191 TYR A OH  1 
ATOM   1542 N  N   . TRP A 1 191 ? -16.000 -4.275  27.984  1.00 9.32   ? 192 TRP A N   1 
ATOM   1543 C  CA  . TRP A 1 191 ? -14.925 -3.996  28.928  1.00 9.34   ? 192 TRP A CA  1 
ATOM   1544 C  C   . TRP A 1 191 ? -14.209 -2.694  28.529  1.00 9.05   ? 192 TRP A C   1 
ATOM   1545 O  O   . TRP A 1 191 ? -14.145 -2.402  27.345  1.00 10.83  ? 192 TRP A O   1 
ATOM   1546 C  CB  . TRP A 1 191 ? -13.903 -5.119  28.930  1.00 10.02  ? 192 TRP A CB  1 
ATOM   1547 C  CG  . TRP A 1 191 ? -14.444 -6.464  29.366  1.00 10.44  ? 192 TRP A CG  1 
ATOM   1548 C  CD1 . TRP A 1 191 ? -14.659 -6.885  30.683  1.00 11.77  ? 192 TRP A CD1 1 
ATOM   1549 C  CD2 . TRP A 1 191 ? -14.720 -7.595  28.498  1.00 10.96  ? 192 TRP A CD2 1 
ATOM   1550 N  NE1 . TRP A 1 191 ? -15.122 -8.183  30.631  1.00 12.86  ? 192 TRP A NE1 1 
ATOM   1551 C  CE2 . TRP A 1 191 ? -15.138 -8.663  29.341  1.00 12.17  ? 192 TRP A CE2 1 
ATOM   1552 C  CE3 . TRP A 1 191 ? -14.623 -7.787  27.098  1.00 11.64  ? 192 TRP A CE3 1 
ATOM   1553 C  CZ2 . TRP A 1 191 ? -15.501 -9.917  28.811  1.00 12.36  ? 192 TRP A CZ2 1 
ATOM   1554 C  CZ3 . TRP A 1 191 ? -14.913 -9.035  26.591  1.00 12.38  ? 192 TRP A CZ3 1 
ATOM   1555 C  CH2 . TRP A 1 191 ? -15.314 -10.061 27.437  1.00 12.87  ? 192 TRP A CH2 1 
ATOM   1556 N  N   . THR A 1 192 ? -13.636 -1.995  29.498  1.00 9.49   ? 193 THR A N   1 
ATOM   1557 C  CA  . THR A 1 192 ? -12.906 -0.797  29.142  1.00 9.00   ? 193 THR A CA  1 
ATOM   1558 C  C   . THR A 1 192 ? -11.680 -0.620  30.027  1.00 9.25   ? 193 THR A C   1 
ATOM   1559 O  O   . THR A 1 192 ? -11.655 -1.024  31.172  1.00 10.16  ? 193 THR A O   1 
ATOM   1560 C  CB  . THR A 1 192 ? -13.842 0.435   29.245  1.00 9.80   ? 193 THR A CB  1 
ATOM   1561 O  OG1 . THR A 1 192 ? -13.152 1.623   28.826  1.00 10.76  ? 193 THR A OG1 1 
ATOM   1562 C  CG2 . THR A 1 192 ? -14.393 0.675   30.640  1.00 11.73  ? 193 THR A CG2 1 
ATOM   1563 N  N   . TYR A 1 193 ? -10.635 -0.015  29.420  1.00 9.17   ? 194 TYR A N   1 
ATOM   1564 C  CA  . TYR A 1 193 ? -9.417  0.279   30.164  1.00 9.35   ? 194 TYR A CA  1 
ATOM   1565 C  C   . TYR A 1 193 ? -8.629  1.344   29.382  1.00 8.53   ? 194 TYR A C   1 
ATOM   1566 O  O   . TYR A 1 193 ? -8.838  1.506   28.185  1.00 9.02   ? 194 TYR A O   1 
ATOM   1567 C  CB  . TYR A 1 193 ? -8.548  -0.988  30.367  1.00 10.13  ? 194 TYR A CB  1 
ATOM   1568 C  CG  . TYR A 1 193 ? -7.876  -1.494  29.121  1.00 9.57   ? 194 TYR A CG  1 
ATOM   1569 C  CD1 . TYR A 1 193 ? -8.593  -2.234  28.151  1.00 9.99   ? 194 TYR A CD1 1 
ATOM   1570 C  CD2 . TYR A 1 193 ? -6.566  -1.136  28.851  1.00 9.62   ? 194 TYR A CD2 1 
ATOM   1571 C  CE1 . TYR A 1 193 ? -7.971  -2.594  26.952  1.00 9.62   ? 194 TYR A CE1 1 
ATOM   1572 C  CE2 . TYR A 1 193 ? -5.932  -1.523  27.674  1.00 9.34   ? 194 TYR A CE2 1 
ATOM   1573 C  CZ  . TYR A 1 193 ? -6.643  -2.229  26.706  1.00 8.52   ? 194 TYR A CZ  1 
ATOM   1574 O  OH  . TYR A 1 193 ? -5.988  -2.533  25.554  1.00 9.36   ? 194 TYR A OH  1 
ATOM   1575 N  N   . PRO A 1 194 ? -7.705  2.042   30.069  1.00 9.48   ? 195 PRO A N   1 
ATOM   1576 C  CA  . PRO A 1 194 ? -6.857  3.019   29.373  1.00 9.36   ? 195 PRO A CA  1 
ATOM   1577 C  C   . PRO A 1 194 ? -5.672  2.352   28.687  1.00 8.86   ? 195 PRO A C   1 
ATOM   1578 O  O   . PRO A 1 194 ? -4.931  1.591   29.354  1.00 9.80   ? 195 PRO A O   1 
ATOM   1579 C  CB  . PRO A 1 194 ? -6.378  3.921   30.520  1.00 11.22  ? 195 PRO A CB  1 
ATOM   1580 C  CG  . PRO A 1 194 ? -6.388  3.034   31.773  1.00 12.38  ? 195 PRO A CG  1 
ATOM   1581 C  CD  . PRO A 1 194 ? -7.538  2.067   31.556  1.00 11.32  ? 195 PRO A CD  1 
ATOM   1582 N  N   . GLY A 1 195 ? -5.454  2.648   27.422  1.00 8.43   ? 196 GLY A N   1 
ATOM   1583 C  CA  . GLY A 1 195 ? -4.380  1.983   26.713  1.00 9.19   ? 196 GLY A CA  1 
ATOM   1584 C  C   . GLY A 1 195 ? -3.806  2.865   25.617  1.00 8.81   ? 196 GLY A C   1 
ATOM   1585 O  O   . GLY A 1 195 ? -3.638  4.094   25.745  1.00 8.64   ? 196 GLY A O   1 
ATOM   1586 N  N   . SER A 1 196 ? -3.416  2.216   24.518  1.00 8.24   ? 197 SER A N   1 
ATOM   1587 C  CA  . SER A 1 196 ? -2.586  2.828   23.482  1.00 8.85   ? 197 SER A CA  1 
ATOM   1588 C  C   . SER A 1 196 ? -3.032  2.408   22.089  1.00 7.76   ? 197 SER A C   1 
ATOM   1589 O  O   . SER A 1 196 ? -3.783  1.438   21.938  1.00 8.65   ? 197 SER A O   1 
ATOM   1590 C  CB  . SER A 1 196 ? -1.091  2.456   23.667  1.00 9.31   ? 197 SER A CB  1 
ATOM   1591 O  OG  . SER A 1 196 ? -0.848  1.110   23.314  1.00 9.09   ? 197 SER A OG  1 
ATOM   1592 N  N   . LEU A 1 197 ? -2.458  3.064   21.072  1.00 8.49   ? 198 LEU A N   1 
ATOM   1593 C  CA  . LEU A 1 197 ? -2.446  2.466   19.737  1.00 8.44   ? 198 LEU A CA  1 
ATOM   1594 C  C   . LEU A 1 197 ? -1.758  1.098   19.830  1.00 8.75   ? 198 LEU A C   1 
ATOM   1595 O  O   . LEU A 1 197 ? -0.768  0.938   20.548  1.00 9.51   ? 198 LEU A O   1 
ATOM   1596 C  CB  . LEU A 1 197 ? -1.594  3.341   18.819  1.00 10.14  ? 198 LEU A CB  1 
ATOM   1597 C  CG  . LEU A 1 197 ? -2.317  4.339   17.962  1.00 12.56  ? 198 LEU A CG  1 
ATOM   1598 C  CD1 . LEU A 1 197 ? -3.102  5.364   18.784  1.00 13.18  ? 198 LEU A CD1 1 
ATOM   1599 C  CD2 . LEU A 1 197 ? -1.342  4.987   16.994  1.00 14.69  ? 198 LEU A CD2 1 
ATOM   1600 N  N   . THR A 1 198 ? -2.211  0.142   19.008  1.00 9.22   ? 199 THR A N   1 
ATOM   1601 C  CA  . THR A 1 198 ? -1.567  -1.180  18.956  1.00 8.87   ? 199 THR A CA  1 
ATOM   1602 C  C   . THR A 1 198 ? -0.552  -1.262  17.847  1.00 8.62   ? 199 THR A C   1 
ATOM   1603 O  O   . THR A 1 198 ? 0.087   -2.309  17.676  1.00 10.13  ? 199 THR A O   1 
ATOM   1604 C  CB  . THR A 1 198 ? -2.583  -2.320  18.843  1.00 8.15   ? 199 THR A CB  1 
ATOM   1605 O  OG1 . THR A 1 198 ? -3.117  -2.241  17.540  1.00 8.71   ? 199 THR A OG1 1 
ATOM   1606 C  CG2 . THR A 1 198 ? -3.627  -2.277  19.926  1.00 9.55   ? 199 THR A CG2 1 
ATOM   1607 N  N   . THR A 1 199 ? -0.415  -0.195  17.037  1.00 9.57   ? 200 THR A N   1 
ATOM   1608 C  CA  . THR A 1 199 ? 0.596   -0.116  15.989  1.00 9.41   ? 200 THR A CA  1 
ATOM   1609 C  C   . THR A 1 199 ? 1.474   1.086   16.304  1.00 10.34  ? 200 THR A C   1 
ATOM   1610 O  O   . THR A 1 199 ? 1.016   2.072   16.920  1.00 10.64  ? 200 THR A O   1 
ATOM   1611 C  CB  . THR A 1 199 ? 0.007   0.090   14.569  1.00 11.35  ? 200 THR A CB  1 
ATOM   1612 O  OG1 . THR A 1 199 ? -0.665  1.354   14.530  1.00 14.81  ? 200 THR A OG1 1 
ATOM   1613 C  CG2 . THR A 1 199 ? -0.962  -1.001  14.209  1.00 12.58  ? 200 THR A CG2 1 
ATOM   1614 N  N   . PRO A 1 200 ? 2.729   1.115   15.793  1.00 10.65  ? 201 PRO A N   1 
ATOM   1615 C  CA  . PRO A 1 200 ? 3.487   2.357   15.834  1.00 10.92  ? 201 PRO A CA  1 
ATOM   1616 C  C   . PRO A 1 200 ? 2.620   3.508   15.323  1.00 11.41  ? 201 PRO A C   1 
ATOM   1617 O  O   . PRO A 1 200 ? 1.853   3.308   14.345  1.00 12.61  ? 201 PRO A O   1 
ATOM   1618 C  CB  . PRO A 1 200 ? 4.655   2.018   14.885  1.00 12.00  ? 201 PRO A CB  1 
ATOM   1619 C  CG  . PRO A 1 200 ? 4.910   0.555   15.144  1.00 12.75  ? 201 PRO A CG  1 
ATOM   1620 C  CD  . PRO A 1 200 ? 3.466   -0.006  15.178  1.00 11.37  ? 201 PRO A CD  1 
ATOM   1621 N  N   . PRO A 1 201 ? 2.710   4.709   15.913  1.00 11.62  ? 202 PRO A N   1 
ATOM   1622 C  CA  . PRO A 1 201 ? 3.668   5.119   16.953  1.00 11.44  ? 202 PRO A CA  1 
ATOM   1623 C  C   . PRO A 1 201 ? 3.335   4.736   18.389  1.00 10.36  ? 202 PRO A C   1 
ATOM   1624 O  O   . PRO A 1 201 ? 4.051   5.133   19.321  1.00 11.64  ? 202 PRO A O   1 
ATOM   1625 C  CB  . PRO A 1 201 ? 3.785   6.617   16.767  1.00 13.58  ? 202 PRO A CB  1 
ATOM   1626 C  CG  . PRO A 1 201 ? 2.393   6.981   16.216  1.00 18.15  ? 202 PRO A CG  1 
ATOM   1627 C  CD  . PRO A 1 201 ? 1.951   5.845   15.361  1.00 13.61  ? 202 PRO A CD  1 
ATOM   1628 N  N   . LEU A 1 202 ? 2.284   3.934   18.616  1.00 10.08  ? 203 LEU A N   1 
ATOM   1629 C  CA  . LEU A 1 202 ? 2.018   3.338   19.941  1.00 9.42   ? 203 LEU A CA  1 
ATOM   1630 C  C   . LEU A 1 202 ? 1.615   4.386   20.986  1.00 9.72   ? 203 LEU A C   1 
ATOM   1631 O  O   . LEU A 1 202 ? 1.692   4.123   22.200  1.00 9.69   ? 203 LEU A O   1 
ATOM   1632 C  CB  . LEU A 1 202 ? 3.171   2.446   20.457  1.00 10.43  ? 203 LEU A CB  1 
ATOM   1633 C  CG  . LEU A 1 202 ? 3.514   1.292   19.509  1.00 9.98   ? 203 LEU A CG  1 
ATOM   1634 C  CD1 . LEU A 1 202 ? 4.810   0.631   20.014  1.00 12.21  ? 203 LEU A CD1 1 
ATOM   1635 C  CD2 . LEU A 1 202 ? 2.398   0.269   19.476  1.00 10.74  ? 203 LEU A CD2 1 
ATOM   1636 N  N   . ASN A 1 203 ? 1.105   5.543   20.560  1.00 10.23  ? 204 ASN A N   1 
ATOM   1637 C  CA  . ASN A 1 203 ? 0.763   6.633   21.466  1.00 10.44  ? 204 ASN A CA  1 
ATOM   1638 C  C   . ASN A 1 203 ? -0.215  6.144   22.532  1.00 9.64   ? 204 ASN A C   1 
ATOM   1639 O  O   . ASN A 1 203 ? -1.188  5.421   22.277  1.00 9.88   ? 204 ASN A O   1 
ATOM   1640 C  CB  . ASN A 1 203 ? 0.054   7.754   20.704  1.00 11.55  ? 204 ASN A CB  1 
ATOM   1641 C  CG  . ASN A 1 203 ? 0.975   8.485   19.759  1.00 13.58  ? 204 ASN A CG  1 
ATOM   1642 O  OD1 . ASN A 1 203 ? 1.982   7.968   19.317  1.00 19.14  ? 204 ASN A OD1 1 
ATOM   1643 N  ND2 . ASN A 1 203 ? 0.677   9.716   19.428  1.00 16.41  ? 204 ASN A ND2 1 
ATOM   1644 N  N   . GLU A 1 204 ? -0.010  6.621   23.752  1.00 10.34  ? 205 GLU A N   1 
ATOM   1645 C  CA  . GLU A 1 204 ? -0.817  6.288   24.920  1.00 9.86   ? 205 GLU A CA  1 
ATOM   1646 C  C   . GLU A 1 204 ? -2.008  7.235   25.041  1.00 9.83   ? 205 GLU A C   1 
ATOM   1647 O  O   . GLU A 1 204 ? -2.111  8.000   26.015  1.00 12.73  ? 205 GLU A O   1 
ATOM   1648 C  CB  . GLU A 1 204 ? 0.069   6.187   26.154  1.00 11.14  ? 205 GLU A CB  1 
ATOM   1649 C  CG  . GLU A 1 204 ? 0.924   4.923   26.055  1.00 11.39  ? 205 GLU A CG  1 
ATOM   1650 C  CD  . GLU A 1 204 ? 1.803   4.619   27.283  1.00 11.97  ? 205 GLU A CD  1 
ATOM   1651 O  OE1 . GLU A 1 204 ? 2.158   5.590   28.009  1.00 14.63  ? 205 GLU A OE1 1 
ATOM   1652 O  OE2 . GLU A 1 204 ? 2.200   3.433   27.458  1.00 12.89  ? 205 GLU A OE2 1 
ATOM   1653 N  N   . CYS A 1 205 ? -2.916  7.138   24.083  1.00 9.53   ? 206 CYS A N   1 
ATOM   1654 C  CA  . CYS A 1 205 ? -3.960  8.155   23.945  1.00 9.44   ? 206 CYS A CA  1 
ATOM   1655 C  C   . CYS A 1 205 ? -5.349  7.506   23.816  1.00 9.79   ? 206 CYS A C   1 
ATOM   1656 O  O   . CYS A 1 205 ? -6.296  8.225   23.476  1.00 11.96  ? 206 CYS A O   1 
ATOM   1657 C  CB  . CYS A 1 205 ? -3.714  9.036   22.719  1.00 10.70  ? 206 CYS A CB  1 
ATOM   1658 S  SG  . CYS A 1 205 ? -3.601  8.081   21.176  1.00 11.38  ? 206 CYS A SG  1 
ATOM   1659 N  N   . VAL A 1 206 ? -5.482  6.193   24.071  1.00 9.36   ? 207 VAL A N   1 
ATOM   1660 C  CA  . VAL A 1 206 ? -6.723  5.497   23.735  1.00 8.69   ? 207 VAL A CA  1 
ATOM   1661 C  C   . VAL A 1 206 ? -7.494  5.046   24.962  1.00 8.70   ? 207 VAL A C   1 
ATOM   1662 O  O   . VAL A 1 206 ? -6.949  4.392   25.834  1.00 10.84  ? 207 VAL A O   1 
ATOM   1663 C  CB  . VAL A 1 206 ? -6.417  4.272   22.857  1.00 9.36   ? 207 VAL A CB  1 
ATOM   1664 C  CG1 . VAL A 1 206 ? -7.745  3.534   22.538  1.00 10.29  ? 207 VAL A CG1 1 
ATOM   1665 C  CG2 . VAL A 1 206 ? -5.674  4.628   21.583  1.00 10.56  ? 207 VAL A CG2 1 
ATOM   1666 N  N   . THR A 1 207 ? -8.812  5.360   25.004  1.00 8.75   ? 208 THR A N   1 
ATOM   1667 C  CA  . THR A 1 207 ? -9.733  4.649   25.884  1.00 9.56   ? 208 THR A CA  1 
ATOM   1668 C  C   . THR A 1 207 ? -10.281 3.475   25.067  1.00 8.75   ? 208 THR A C   1 
ATOM   1669 O  O   . THR A 1 207 ? -10.920 3.650   24.026  1.00 9.46   ? 208 THR A O   1 
ATOM   1670 C  CB  . THR A 1 207 ? -10.923 5.526   26.318  1.00 10.63  ? 208 THR A CB  1 
ATOM   1671 O  OG1 . THR A 1 207 ? -10.387 6.657   27.026  1.00 11.80  ? 208 THR A OG1 1 
ATOM   1672 C  CG2 . THR A 1 207 ? -11.849 4.731   27.228  1.00 12.02  ? 208 THR A CG2 1 
ATOM   1673 N  N   . TRP A 1 208 ? -9.931  2.247   25.495  1.00 8.40   ? 209 TRP A N   1 
ATOM   1674 C  CA  . TRP A 1 208 ? -10.401 1.048   24.809  1.00 8.04   ? 209 TRP A CA  1 
ATOM   1675 C  C   . TRP A 1 208 ? -11.774 0.644   25.316  1.00 7.89   ? 209 TRP A C   1 
ATOM   1676 O  O   . TRP A 1 208 ? -12.013 0.624   26.523  1.00 8.90   ? 209 TRP A O   1 
ATOM   1677 C  CB  . TRP A 1 208 ? -9.403  -0.122  25.019  1.00 8.56   ? 209 TRP A CB  1 
ATOM   1678 C  CG  . TRP A 1 208 ? -8.264  -0.021  24.058  1.00 8.38   ? 209 TRP A CG  1 
ATOM   1679 C  CD1 . TRP A 1 208 ? -7.042  0.614   24.209  1.00 9.17   ? 209 TRP A CD1 1 
ATOM   1680 C  CD2 . TRP A 1 208 ? -8.313  -0.431  22.696  1.00 7.97   ? 209 TRP A CD2 1 
ATOM   1681 N  NE1 . TRP A 1 208 ? -6.344  0.556   23.042  1.00 9.38   ? 209 TRP A NE1 1 
ATOM   1682 C  CE2 . TRP A 1 208 ? -7.110  -0.080  22.065  1.00 8.55   ? 209 TRP A CE2 1 
ATOM   1683 C  CE3 . TRP A 1 208 ? -9.291  -1.094  21.922  1.00 8.32   ? 209 TRP A CE3 1 
ATOM   1684 C  CZ2 . TRP A 1 208 ? -6.852  -0.322  20.721  1.00 9.45   ? 209 TRP A CZ2 1 
ATOM   1685 C  CZ3 . TRP A 1 208 ? -9.025  -1.391  20.611  1.00 9.21   ? 209 TRP A CZ3 1 
ATOM   1686 C  CH2 . TRP A 1 208 ? -7.812  -1.005  19.998  1.00 9.51   ? 209 TRP A CH2 1 
ATOM   1687 N  N   . ILE A 1 209 ? -12.641 0.287   24.357  1.00 8.47   ? 210 ILE A N   1 
ATOM   1688 C  CA  . ILE A 1 209 ? -13.986 -0.204  24.662  1.00 8.71   ? 210 ILE A CA  1 
ATOM   1689 C  C   . ILE A 1 209 ? -14.082 -1.483  23.827  1.00 8.06   ? 210 ILE A C   1 
ATOM   1690 O  O   . ILE A 1 209 ? -14.235 -1.417  22.610  1.00 9.49   ? 210 ILE A O   1 
ATOM   1691 C  CB  . ILE A 1 209 ? -15.053 0.832   24.279  1.00 9.14   ? 210 ILE A CB  1 
ATOM   1692 C  CG1 . ILE A 1 209 ? -14.823 2.148   25.056  1.00 11.12  ? 210 ILE A CG1 1 
ATOM   1693 C  CG2 . ILE A 1 209 ? -16.462 0.232   24.532  1.00 11.66  ? 210 ILE A CG2 1 
ATOM   1694 C  CD1 . ILE A 1 209 ? -15.623 3.320   24.522  1.00 14.85  ? 210 ILE A CD1 1 
ATOM   1695 N  N   . VAL A 1 210 ? -14.018 -2.637  24.499  1.00 8.52   ? 211 VAL A N   1 
ATOM   1696 C  CA  . VAL A 1 210 ? -13.972 -3.924  23.782  1.00 8.41   ? 211 VAL A CA  1 
ATOM   1697 C  C   . VAL A 1 210 ? -15.287 -4.630  24.055  1.00 8.48   ? 211 VAL A C   1 
ATOM   1698 O  O   . VAL A 1 210 ? -15.666 -4.892  25.200  1.00 9.25   ? 211 VAL A O   1 
ATOM   1699 C  CB  . VAL A 1 210 ? -12.776 -4.785  24.266  1.00 8.93   ? 211 VAL A CB  1 
ATOM   1700 C  CG1 . VAL A 1 210 ? -12.777 -6.166  23.605  1.00 10.30  ? 211 VAL A CG1 1 
ATOM   1701 C  CG2 . VAL A 1 210 ? -11.488 -4.070  23.953  1.00 10.65  ? 211 VAL A CG2 1 
ATOM   1702 N  N   . LEU A 1 211 ? -16.043 -4.902  22.986  1.00 9.10   ? 212 LEU A N   1 
ATOM   1703 C  CA  . LEU A 1 211 ? -17.363 -5.548  23.185  1.00 9.19   ? 212 LEU A CA  1 
ATOM   1704 C  C   . LEU A 1 211 ? -17.193 -7.016  23.569  1.00 9.77   ? 212 LEU A C   1 
ATOM   1705 O  O   . LEU A 1 211 ? -16.350 -7.739  23.020  1.00 10.04  ? 212 LEU A O   1 
ATOM   1706 C  CB  . LEU A 1 211 ? -18.180 -5.439  21.891  1.00 9.87   ? 212 LEU A CB  1 
ATOM   1707 C  CG  . LEU A 1 211 ? -18.547 -4.022  21.470  1.00 10.11  ? 212 LEU A CG  1 
ATOM   1708 C  CD1 . LEU A 1 211 ? -19.578 -4.082  20.306  1.00 12.36  ? 212 LEU A CD1 1 
ATOM   1709 C  CD2 . LEU A 1 211 ? -19.107 -3.179  22.613  1.00 12.12  ? 212 LEU A CD2 1 
ATOM   1710 N  N   . LYS A 1 212 ? -18.065 -7.451  24.472  1.00 10.20  ? 213 LYS A N   1 
ATOM   1711 C  CA  . LYS A 1 212 ? -18.015 -8.846  24.893  1.00 11.75  ? 213 LYS A CA  1 
ATOM   1712 C  C   . LYS A 1 212 ? -18.517 -9.795  23.808  1.00 11.16  ? 213 LYS A C   1 
ATOM   1713 O  O   . LYS A 1 212 ? -18.013 -10.924 23.685  1.00 13.89  ? 213 LYS A O   1 
ATOM   1714 C  CB  . LYS A 1 212 ? -18.884 -9.034  26.123  1.00 14.93  ? 213 LYS A CB  1 
ATOM   1715 C  CG  . LYS A 1 212 ? -18.997 -10.492 26.554  1.00 22.03  ? 213 LYS A CG  1 
ATOM   1716 C  CD  . LYS A 1 212 ? -19.757 -10.668 27.843  1.00 34.33  ? 213 LYS A CD  1 
ATOM   1717 C  CE  . LYS A 1 212 ? -19.668 -12.116 28.301  1.00 41.01  ? 213 LYS A CE  1 
ATOM   1718 N  NZ  . LYS A 1 212 ? -20.573 -12.392 29.446  1.00 44.17  ? 213 LYS A NZ  1 
ATOM   1719 N  N   . GLU A 1 213 ? -19.519 -9.396  23.019  1.00 10.55  ? 214 GLU A N   1 
ATOM   1720 C  CA  . GLU A 1 213 ? -20.115 -10.332 22.046  1.00 10.42  ? 214 GLU A CA  1 
ATOM   1721 C  C   . GLU A 1 213 ? -19.358 -10.222 20.725  1.00 10.11  ? 214 GLU A C   1 
ATOM   1722 O  O   . GLU A 1 213 ? -19.279 -9.136  20.143  1.00 10.33  ? 214 GLU A O   1 
ATOM   1723 C  CB  . GLU A 1 213 ? -21.577 -9.917  21.814  1.00 11.60  ? 214 GLU A CB  1 
ATOM   1724 C  CG  . GLU A 1 213 ? -22.327 -10.840 20.851  1.00 14.58  ? 214 GLU A CG  1 
ATOM   1725 C  CD  . GLU A 1 213 ? -23.791 -10.385 20.572  1.00 16.34  ? 214 GLU A CD  1 
ATOM   1726 O  OE1 . GLU A 1 213 ? -24.370 -9.736  21.398  1.00 17.21  ? 214 GLU A OE1 1 
ATOM   1727 O  OE2 . GLU A 1 213 ? -24.334 -10.528 19.394  1.00 22.49  ? 214 GLU A OE2 1 
ATOM   1728 N  N   . PRO A 1 214 ? -18.801 -11.335 20.228  1.00 10.56  ? 215 PRO A N   1 
ATOM   1729 C  CA  . PRO A 1 214 ? -18.183 -11.324 18.910  1.00 9.90   ? 215 PRO A CA  1 
ATOM   1730 C  C   . PRO A 1 214 ? -19.212 -11.233 17.796  1.00 10.30  ? 215 PRO A C   1 
ATOM   1731 O  O   . PRO A 1 214 ? -20.355 -11.653 18.016  1.00 13.10  ? 215 PRO A O   1 
ATOM   1732 C  CB  . PRO A 1 214 ? -17.416 -12.641 18.808  1.00 11.68  ? 215 PRO A CB  1 
ATOM   1733 C  CG  . PRO A 1 214 ? -18.248 -13.566 19.668  1.00 17.41  ? 215 PRO A CG  1 
ATOM   1734 C  CD  . PRO A 1 214 ? -18.760 -12.690 20.859  1.00 13.03  ? 215 PRO A CD  1 
ATOM   1735 N  N   . ILE A 1 215 ? -18.802 -10.802 16.612  1.00 9.98   ? 216 ILE A N   1 
ATOM   1736 C  CA  . ILE A 1 215 ? -19.575 -11.073 15.402  1.00 10.26  ? 216 ILE A CA  1 
ATOM   1737 C  C   . ILE A 1 215 ? -19.048 -12.348 14.775  1.00 10.43  ? 216 ILE A C   1 
ATOM   1738 O  O   . ILE A 1 215 ? -17.868 -12.673 14.878  1.00 11.97  ? 216 ILE A O   1 
ATOM   1739 C  CB  . ILE A 1 215 ? -19.598 -9.871  14.425  1.00 11.17  ? 216 ILE A CB  1 
ATOM   1740 C  CG1 . ILE A 1 215 ? -18.188 -9.522  13.932  1.00 11.30  ? 216 ILE A CG1 1 
ATOM   1741 C  CG2 . ILE A 1 215 ? -20.237 -8.669  15.108  1.00 11.69  ? 216 ILE A CG2 1 
ATOM   1742 C  CD1 . ILE A 1 215 ? -18.208 -8.564  12.732  1.00 13.11  ? 216 ILE A CD1 1 
ATOM   1743 N  N   . SER A 1 216 ? -19.926 -13.024 14.009  1.00 11.14  ? 217 SER A N   1 
ATOM   1744 C  CA  A SER A 1 216 ? -19.518 -14.174 13.203  0.50 11.52  ? 217 SER A CA  1 
ATOM   1745 C  CA  B SER A 1 216 ? -19.538 -14.172 13.212  0.50 11.50  ? 217 SER A CA  1 
ATOM   1746 C  C   . SER A 1 216 ? -19.305 -13.701 11.783  1.00 10.39  ? 217 SER A C   1 
ATOM   1747 O  O   . SER A 1 216 ? -20.145 -12.942 11.252  1.00 11.41  ? 217 SER A O   1 
ATOM   1748 C  CB  A SER A 1 216 ? -20.590 -15.267 13.184  0.50 12.71  ? 217 SER A CB  1 
ATOM   1749 C  CB  B SER A 1 216 ? -20.671 -15.190 13.269  0.50 14.89  ? 217 SER A CB  1 
ATOM   1750 O  OG  A SER A 1 216 ? -20.651 -15.874 14.444  0.50 14.30  ? 217 SER A OG  1 
ATOM   1751 O  OG  B SER A 1 216 ? -20.252 -16.338 12.602  0.50 14.19  ? 217 SER A OG  1 
ATOM   1752 N  N   . VAL A 1 217 ? -18.234 -14.170 11.178  1.00 10.07  ? 218 VAL A N   1 
ATOM   1753 C  CA  . VAL A 1 217 ? -17.990 -13.976 9.758   1.00 10.64  ? 218 VAL A CA  1 
ATOM   1754 C  C   . VAL A 1 217 ? -17.738 -15.342 9.145   1.00 9.87   ? 218 VAL A C   1 
ATOM   1755 O  O   . VAL A 1 217 ? -17.369 -16.309 9.852   1.00 11.48  ? 218 VAL A O   1 
ATOM   1756 C  CB  . VAL A 1 217 ? -16.778 -13.043 9.517   1.00 11.94  ? 218 VAL A CB  1 
ATOM   1757 C  CG1 . VAL A 1 217 ? -17.007 -11.673 10.189  1.00 12.31  ? 218 VAL A CG1 1 
ATOM   1758 C  CG2 . VAL A 1 217 ? -15.447 -13.675 10.039  1.00 13.03  ? 218 VAL A CG2 1 
ATOM   1759 N  N   . SER A 1 218 ? -17.915 -15.476 7.837   1.00 9.83   ? 219 SER A N   1 
ATOM   1760 C  CA  . SER A 1 218 ? -17.700 -16.828 7.270   1.00 10.60  ? 219 SER A CA  1 
ATOM   1761 C  C   . SER A 1 218 ? -16.232 -17.067 6.918   1.00 10.28  ? 219 SER A C   1 
ATOM   1762 O  O   . SER A 1 218 ? -15.428 -16.131 6.731   1.00 11.20  ? 219 SER A O   1 
ATOM   1763 C  CB  . SER A 1 218 ? -18.572 -17.010 6.030   1.00 10.40  ? 219 SER A CB  1 
ATOM   1764 O  OG  . SER A 1 218 ? -18.140 -16.096 5.035   1.00 11.39  ? 219 SER A OG  1 
ATOM   1765 N  N   . SER A 1 219 ? -15.907 -18.341 6.704   1.00 11.07  ? 220 SER A N   1 
ATOM   1766 C  CA  . SER A 1 219 ? -14.584 -18.708 6.224   1.00 12.05  ? 220 SER A CA  1 
ATOM   1767 C  C   . SER A 1 219 ? -14.283 -18.002 4.914   1.00 11.75  ? 220 SER A C   1 
ATOM   1768 O  O   . SER A 1 219 ? -13.165 -17.588 4.662   1.00 12.60  ? 220 SER A O   1 
ATOM   1769 C  CB  . SER A 1 219 ? -14.481 -20.200 6.148   1.00 14.14  ? 220 SER A CB  1 
ATOM   1770 O  OG  . SER A 1 219 ? -15.466 -20.780 5.245   1.00 15.22  ? 220 SER A OG  1 
ATOM   1771 N  N   . GLU A 1 220 ? -15.267 -17.904 3.992   1.00 11.25  ? 221 GLU A N   1 
ATOM   1772 C  CA  . GLU A 1 220 ? -15.030 -17.243 2.727   1.00 12.00  ? 221 GLU A CA  1 
ATOM   1773 C  C   . GLU A 1 220 ? -14.700 -15.748 2.911   1.00 10.44  ? 221 GLU A C   1 
ATOM   1774 O  O   . GLU A 1 220 ? -13.873 -15.213 2.174   1.00 12.72  ? 221 GLU A O   1 
ATOM   1775 C  CB  . GLU A 1 220 ? -16.195 -17.359 1.733   1.00 13.61  ? 221 GLU A CB  1 
ATOM   1776 C  CG  . GLU A 1 220 ? -16.534 -18.773 1.271   1.00 16.98  ? 221 GLU A CG  1 
ATOM   1777 C  CD  . GLU A 1 220 ? -17.528 -19.528 2.130   1.00 21.32  ? 221 GLU A CD  1 
ATOM   1778 O  OE1 . GLU A 1 220 ? -17.848 -19.105 3.258   1.00 18.07  ? 221 GLU A OE1 1 
ATOM   1779 O  OE2 . GLU A 1 220 ? -17.996 -20.594 1.666   1.00 29.72  ? 221 GLU A OE2 1 
ATOM   1780 N  N   . GLN A 1 221 ? -15.353 -15.079 3.880   1.00 10.18  ? 222 GLN A N   1 
ATOM   1781 C  CA  . GLN A 1 221 ? -15.034 -13.706 4.138   1.00 10.39  ? 222 GLN A CA  1 
ATOM   1782 C  C   . GLN A 1 221 ? -13.598 -13.536 4.646   1.00 10.68  ? 222 GLN A C   1 
ATOM   1783 O  O   . GLN A 1 221 ? -12.836 -12.674 4.159   1.00 10.81  ? 222 GLN A O   1 
ATOM   1784 C  CB  . GLN A 1 221 ? -16.040 -13.091 5.100   1.00 9.93   ? 222 GLN A CB  1 
ATOM   1785 C  CG  . GLN A 1 221 ? -17.425 -12.989 4.422   1.00 9.99   ? 222 GLN A CG  1 
ATOM   1786 C  CD  . GLN A 1 221 ? -18.487 -12.438 5.333   1.00 9.69   ? 222 GLN A CD  1 
ATOM   1787 O  OE1 . GLN A 1 221 ? -18.608 -12.801 6.536   1.00 10.37  ? 222 GLN A OE1 1 
ATOM   1788 N  NE2 . GLN A 1 221 ? -19.319 -11.540 4.800   1.00 10.90  ? 222 GLN A NE2 1 
ATOM   1789 N  N   A VAL A 1 222 ? -13.196 -14.328 5.637   0.50 10.52  ? 223 VAL A N   1 
ATOM   1790 N  N   B VAL A 1 222 ? -13.181 -14.352 5.623   0.50 11.59  ? 223 VAL A N   1 
ATOM   1791 C  CA  A VAL A 1 222 ? -11.861 -14.158 6.169   0.50 11.61  ? 223 VAL A CA  1 
ATOM   1792 C  CA  B VAL A 1 222 ? -11.835 -14.277 6.175   0.50 12.57  ? 223 VAL A CA  1 
ATOM   1793 C  C   A VAL A 1 222 ? -10.810 -14.647 5.155   0.50 10.89  ? 223 VAL A C   1 
ATOM   1794 C  C   B VAL A 1 222 ? -10.775 -14.630 5.134   0.50 11.40  ? 223 VAL A C   1 
ATOM   1795 O  O   A VAL A 1 222 ? -9.706  -14.106 5.111   0.50 11.90  ? 223 VAL A O   1 
ATOM   1796 O  O   B VAL A 1 222 ? -9.691  -14.054 5.130   0.50 12.03  ? 223 VAL A O   1 
ATOM   1797 C  CB  A VAL A 1 222 ? -11.732 -14.776 7.583   0.50 14.74  ? 223 VAL A CB  1 
ATOM   1798 C  CB  B VAL A 1 222 ? -11.684 -15.152 7.433   0.50 14.83  ? 223 VAL A CB  1 
ATOM   1799 C  CG1 A VAL A 1 222 ? -11.693 -16.299 7.477   0.50 15.21  ? 223 VAL A CG1 1 
ATOM   1800 C  CG1 B VAL A 1 222 ? -10.216 -15.255 7.846   0.50 21.59  ? 223 VAL A CG1 1 
ATOM   1801 C  CG2 A VAL A 1 222 ? -10.514 -14.177 8.324   0.50 17.45  ? 223 VAL A CG2 1 
ATOM   1802 C  CG2 B VAL A 1 222 ? -12.563 -14.623 8.528   0.50 15.45  ? 223 VAL A CG2 1 
ATOM   1803 N  N   A LEU A 1 223 ? -11.169 -15.600 4.275   0.50 12.71  ? 224 LEU A N   1 
ATOM   1804 N  N   B LEU A 1 223 ? -11.073 -15.598 4.266   0.50 12.79  ? 224 LEU A N   1 
ATOM   1805 C  CA  A LEU A 1 223 ? -10.244 -15.985 3.199   0.50 14.00  ? 224 LEU A CA  1 
ATOM   1806 C  CA  B LEU A 1 223 ? -10.079 -15.944 3.253   0.50 13.81  ? 224 LEU A CA  1 
ATOM   1807 C  C   A LEU A 1 223 ? -9.848  -14.766 2.371   0.50 12.50  ? 224 LEU A C   1 
ATOM   1808 C  C   B LEU A 1 223 ? -9.820  -14.757 2.326   0.50 12.95  ? 224 LEU A C   1 
ATOM   1809 O  O   A LEU A 1 223 ? -8.697  -14.643 1.927   0.50 15.15  ? 224 LEU A O   1 
ATOM   1810 O  O   B LEU A 1 223 ? -8.691  -14.598 1.838   0.50 12.67  ? 224 LEU A O   1 
ATOM   1811 C  CB  A LEU A 1 223 ? -10.883 -17.088 2.324   0.50 17.78  ? 224 LEU A CB  1 
ATOM   1812 C  CB  B LEU A 1 223 ? -10.508 -17.223 2.517   0.50 17.63  ? 224 LEU A CB  1 
ATOM   1813 C  CG  A LEU A 1 223 ? -10.084 -17.566 1.115   0.50 22.64  ? 224 LEU A CG  1 
ATOM   1814 C  CG  B LEU A 1 223 ? -10.489 -18.494 3.374   0.50 19.50  ? 224 LEU A CG  1 
ATOM   1815 N  N   . LYS A 1 224 ? -10.811 -13.883 2.097   1.00 12.04  ? 225 LYS A N   1 
ATOM   1816 C  CA  . LYS A 1 224 ? -10.527 -12.694 1.297   1.00 12.57  ? 225 LYS A CA  1 
ATOM   1817 C  C   . LYS A 1 224 ? -9.604  -11.716 2.020   1.00 11.04  ? 225 LYS A C   1 
ATOM   1818 O  O   . LYS A 1 224 ? -8.738  -11.116 1.364   1.00 11.94  ? 225 LYS A O   1 
ATOM   1819 C  CB  . LYS A 1 224 ? -11.851 -12.011 0.882   1.00 15.36  ? 225 LYS A CB  1 
ATOM   1820 C  CG  . LYS A 1 224 ? -12.617 -12.863 -0.095  1.00 18.48  ? 225 LYS A CG  1 
ATOM   1821 C  CD  . LYS A 1 224 ? -13.941 -12.151 -0.597  1.00 31.48  ? 225 LYS A CD  1 
ATOM   1822 C  CE  . LYS A 1 224 ? -14.450 -12.532 -1.976  1.00 34.94  ? 225 LYS A CE  1 
ATOM   1823 N  NZ  . LYS A 1 224 ? -14.807 -13.977 -2.039  1.00 51.30  ? 225 LYS A NZ  1 
ATOM   1824 N  N   . PHE A 1 225 ? -9.709  -11.580 3.345   1.00 10.04  ? 226 PHE A N   1 
ATOM   1825 C  CA  . PHE A 1 225 ? -8.704  -10.804 4.076   1.00 10.33  ? 226 PHE A CA  1 
ATOM   1826 C  C   . PHE A 1 225 ? -7.312  -11.395 3.826   1.00 10.18  ? 226 PHE A C   1 
ATOM   1827 O  O   . PHE A 1 225 ? -6.363  -10.624 3.622   1.00 10.80  ? 226 PHE A O   1 
ATOM   1828 C  CB  . PHE A 1 225 ? -8.961  -10.852 5.576   1.00 11.30  ? 226 PHE A CB  1 
ATOM   1829 C  CG  . PHE A 1 225 ? -10.106 -10.061 6.169   1.00 10.51  ? 226 PHE A CG  1 
ATOM   1830 C  CD1 . PHE A 1 225 ? -11.068 -9.485  5.355   1.00 13.46  ? 226 PHE A CD1 1 
ATOM   1831 C  CD2 . PHE A 1 225 ? -10.218 -9.895  7.540   1.00 13.41  ? 226 PHE A CD2 1 
ATOM   1832 C  CE1 . PHE A 1 225 ? -12.117 -8.760  5.900   1.00 14.31  ? 226 PHE A CE1 1 
ATOM   1833 C  CE2 . PHE A 1 225 ? -11.267 -9.170  8.083   1.00 16.32  ? 226 PHE A CE2 1 
ATOM   1834 C  CZ  . PHE A 1 225 ? -12.214 -8.604  7.262   1.00 14.14  ? 226 PHE A CZ  1 
ATOM   1835 N  N   . ARG A 1 226 ? -7.195  -12.711 3.867   1.00 10.32  ? 227 ARG A N   1 
ATOM   1836 C  CA  . ARG A 1 226 ? -5.899  -13.394 3.777   1.00 11.12  ? 227 ARG A CA  1 
ATOM   1837 C  C   . ARG A 1 226 ? -5.291  -13.362 2.376   1.00 11.08  ? 227 ARG A C   1 
ATOM   1838 O  O   . ARG A 1 226 ? -4.140  -13.800 2.247   1.00 13.34  ? 227 ARG A O   1 
ATOM   1839 C  CB  . ARG A 1 226 ? -6.059  -14.811 4.299   1.00 11.15  ? 227 ARG A CB  1 
ATOM   1840 C  CG  . ARG A 1 226 ? -6.425  -14.913 5.778   1.00 10.99  ? 227 ARG A CG  1 
ATOM   1841 C  CD  . ARG A 1 226 ? -6.486  -16.379 6.209   1.00 13.22  ? 227 ARG A CD  1 
ATOM   1842 N  NE  . ARG A 1 226 ? -6.916  -16.496 7.588   1.00 11.29  ? 227 ARG A NE  1 
ATOM   1843 C  CZ  . ARG A 1 226 ? -7.674  -17.459 8.078   1.00 12.83  ? 227 ARG A CZ  1 
ATOM   1844 N  NH1 . ARG A 1 226 ? -8.096  -18.482 7.333   1.00 16.09  ? 227 ARG A NH1 1 
ATOM   1845 N  NH2 . ARG A 1 226 ? -8.013  -17.415 9.335   1.00 15.23  ? 227 ARG A NH2 1 
ATOM   1846 N  N   . LYS A 1 227 ? -6.023  -12.886 1.348   1.00 11.31  ? 228 LYS A N   1 
ATOM   1847 C  CA  . LYS A 1 227 ? -5.476  -12.750 0.015   1.00 12.14  ? 228 LYS A CA  1 
ATOM   1848 C  C   . LYS A 1 227 ? -4.809  -11.393 -0.196  1.00 11.50  ? 228 LYS A C   1 
ATOM   1849 O  O   . LYS A 1 227 ? -4.141  -11.203 -1.212  1.00 13.83  ? 228 LYS A O   1 
ATOM   1850 C  CB  . LYS A 1 227 ? -6.604  -12.897 -1.019  1.00 14.99  ? 228 LYS A CB  1 
ATOM   1851 C  CG  . LYS A 1 227 ? -7.084  -14.301 -1.192  1.00 19.98  ? 228 LYS A CG  1 
ATOM   1852 C  CD  . LYS A 1 227 ? -8.161  -14.414 -2.300  1.00 25.78  ? 228 LYS A CD  1 
ATOM   1853 N  N   . LEU A 1 228 ? -4.990  -10.463 0.752   1.00 10.67  ? 229 LEU A N   1 
ATOM   1854 C  CA  . LEU A 1 228 ? -4.260  -9.218  0.667   1.00 10.47  ? 229 LEU A CA  1 
ATOM   1855 C  C   . LEU A 1 228 ? -2.768  -9.469  0.809   1.00 11.11  ? 229 LEU A C   1 
ATOM   1856 O  O   . LEU A 1 228 ? -2.347  -10.528 1.293   1.00 11.68  ? 229 LEU A O   1 
ATOM   1857 C  CB  . LEU A 1 228 ? -4.781  -8.258  1.769   1.00 11.13  ? 229 LEU A CB  1 
ATOM   1858 C  CG  . LEU A 1 228 ? -6.212  -7.752  1.562   1.00 10.88  ? 229 LEU A CG  1 
ATOM   1859 C  CD1 . LEU A 1 228 ? -6.663  -7.099  2.858   1.00 11.23  ? 229 LEU A CD1 1 
ATOM   1860 C  CD2 . LEU A 1 228 ? -6.269  -6.728  0.386   1.00 13.16  ? 229 LEU A CD2 1 
ATOM   1861 N  N   . ASN A 1 229 ? -1.988  -8.496  0.383   1.00 11.31  ? 230 ASN A N   1 
ATOM   1862 C  CA  . ASN A 1 229 ? -0.511  -8.589  0.435   1.00 11.24  ? 230 ASN A CA  1 
ATOM   1863 C  C   . ASN A 1 229 ? 0.049   -7.457  1.289   1.00 10.41  ? 230 ASN A C   1 
ATOM   1864 O  O   . ASN A 1 229 ? -0.440  -6.305  1.231   1.00 11.52  ? 230 ASN A O   1 
ATOM   1865 C  CB  . ASN A 1 229 ? 0.115   -8.407  -0.931  1.00 12.46  ? 230 ASN A CB  1 
ATOM   1866 C  CG  . ASN A 1 229 ? -0.000  -9.554  -1.897  1.00 13.64  ? 230 ASN A CG  1 
ATOM   1867 O  OD1 . ASN A 1 229 ? 0.549   -9.427  -2.979  1.00 19.15  ? 230 ASN A OD1 1 
ATOM   1868 N  ND2 . ASN A 1 229 ? -0.735  -10.614 -1.557  1.00 16.60  ? 230 ASN A ND2 1 
ATOM   1869 N  N   . PHE A 1 230 ? 1.062   -7.763  2.097   1.00 10.71  ? 231 PHE A N   1 
ATOM   1870 C  CA  . PHE A 1 230 ? 1.835   -6.740  2.794   1.00 11.40  ? 231 PHE A CA  1 
ATOM   1871 C  C   . PHE A 1 230 ? 2.642   -5.897  1.834   1.00 11.34  ? 231 PHE A C   1 
ATOM   1872 O  O   . PHE A 1 230 ? 2.904   -4.718  2.051   1.00 12.05  ? 231 PHE A O   1 
ATOM   1873 C  CB  . PHE A 1 230 ? 2.831   -7.344  3.816   1.00 12.29  ? 231 PHE A CB  1 
ATOM   1874 C  CG  . PHE A 1 230 ? 2.281   -7.912  5.103   1.00 10.45  ? 231 PHE A CG  1 
ATOM   1875 C  CD1 . PHE A 1 230 ? 1.517   -7.108  5.951   1.00 12.26  ? 231 PHE A CD1 1 
ATOM   1876 C  CD2 . PHE A 1 230 ? 2.558   -9.222  5.508   1.00 12.18  ? 231 PHE A CD2 1 
ATOM   1877 C  CE1 . PHE A 1 230 ? 1.111   -7.564  7.211   1.00 11.96  ? 231 PHE A CE1 1 
ATOM   1878 C  CE2 . PHE A 1 230 ? 2.120   -9.682  6.745   1.00 12.22  ? 231 PHE A CE2 1 
ATOM   1879 C  CZ  . PHE A 1 230 ? 1.398   -8.874  7.607   1.00 12.54  ? 231 PHE A CZ  1 
ATOM   1880 N  N   . ASN A 1 231 ? 3.189   -6.546  0.821   1.00 11.34  ? 232 ASN A N   1 
ATOM   1881 C  CA  . ASN A 1 231 ? 4.125   -5.954  -0.114  1.00 11.76  ? 232 ASN A CA  1 
ATOM   1882 C  C   . ASN A 1 231 ? 3.440   -5.040  -1.125  1.00 11.94  ? 232 ASN A C   1 
ATOM   1883 O  O   . ASN A 1 231 ? 2.243   -5.165  -1.406  1.00 12.49  ? 232 ASN A O   1 
ATOM   1884 C  CB  . ASN A 1 231 ? 4.867   -7.061  -0.890  1.00 13.33  ? 232 ASN A CB  1 
ATOM   1885 C  CG  . ASN A 1 231 ? 3.868   -7.982  -1.571  1.00 12.47  ? 232 ASN A CG  1 
ATOM   1886 O  OD1 . ASN A 1 231 ? 3.291   -8.856  -0.909  1.00 13.64  ? 232 ASN A OD1 1 
ATOM   1887 N  ND2 . ASN A 1 231 ? 3.645   -7.836  -2.882  1.00 15.97  ? 232 ASN A ND2 1 
ATOM   1888 N  N   . GLY A 1 232 ? 4.245   -4.127  -1.683  1.00 12.44  ? 233 GLY A N   1 
ATOM   1889 C  CA  . GLY A 1 232 ? 3.824   -3.405  -2.873  1.00 13.44  ? 233 GLY A CA  1 
ATOM   1890 C  C   . GLY A 1 232 ? 3.871   -4.276  -4.123  1.00 14.19  ? 233 GLY A C   1 
ATOM   1891 O  O   . GLY A 1 232 ? 4.557   -5.322  -4.155  1.00 15.03  ? 233 GLY A O   1 
ATOM   1892 N  N   . GLU A 1 233 ? 3.125   -3.871  -5.147  1.00 15.52  ? 234 GLU A N   1 
ATOM   1893 C  CA  . GLU A 1 233 ? 3.171   -4.616  -6.397  1.00 18.18  ? 234 GLU A CA  1 
ATOM   1894 C  C   . GLU A 1 233 ? 4.613   -4.677  -6.906  1.00 19.13  ? 234 GLU A C   1 
ATOM   1895 O  O   . GLU A 1 233 ? 5.343   -3.680  -6.838  1.00 19.44  ? 234 GLU A O   1 
ATOM   1896 C  CB  . GLU A 1 233 ? 2.219   -3.968  -7.398  1.00 20.46  ? 234 GLU A CB  1 
ATOM   1897 C  CG  . GLU A 1 233 ? 2.136   -4.692  -8.745  1.00 24.59  ? 234 GLU A CG  1 
ATOM   1898 C  CD  . GLU A 1 233 ? 0.918   -4.212  -9.528  1.00 33.27  ? 234 GLU A CD  1 
ATOM   1899 O  OE1 . GLU A 1 233 ? 0.229   -3.226  -9.113  1.00 44.25  ? 234 GLU A OE1 1 
ATOM   1900 O  OE2 . GLU A 1 233 ? 0.712   -4.726  -10.615 1.00 58.35  ? 234 GLU A OE2 1 
ATOM   1901 N  N   . GLY A 1 234 ? 5.031   -5.863  -7.388  1.00 22.29  ? 235 GLY A N   1 
ATOM   1902 C  CA  . GLY A 1 234 ? 6.337   -6.092  -7.997  1.00 25.10  ? 235 GLY A CA  1 
ATOM   1903 C  C   . GLY A 1 234 ? 7.378   -6.548  -6.983  1.00 24.37  ? 235 GLY A C   1 
ATOM   1904 O  O   . GLY A 1 234 ? 8.447   -6.966  -7.390  1.00 41.29  ? 235 GLY A O   1 
ATOM   1905 N  N   . GLU A 1 235 ? 7.102   -6.388  -5.679  1.00 18.64  ? 236 GLU A N   1 
ATOM   1906 C  CA  . GLU A 1 235 ? 7.976   -6.933  -4.645  1.00 16.94  ? 236 GLU A CA  1 
ATOM   1907 C  C   . GLU A 1 235 ? 7.612   -8.371  -4.374  1.00 17.22  ? 236 GLU A C   1 
ATOM   1908 O  O   . GLU A 1 235 ? 6.466   -8.781  -4.665  1.00 18.43  ? 236 GLU A O   1 
ATOM   1909 C  CB  . GLU A 1 235 ? 7.810   -6.116  -3.374  1.00 18.89  ? 236 GLU A CB  1 
ATOM   1910 C  CG  . GLU A 1 235 ? 8.068   -4.615  -3.539  1.00 22.06  ? 236 GLU A CG  1 
ATOM   1911 C  CD  . GLU A 1 235 ? 7.687   -3.754  -2.317  1.00 24.58  ? 236 GLU A CD  1 
ATOM   1912 O  OE1 . GLU A 1 235 ? 7.149   -4.318  -1.343  1.00 23.80  ? 236 GLU A OE1 1 
ATOM   1913 O  OE2 . GLU A 1 235 ? 7.934   -2.532  -2.356  1.00 36.18  ? 236 GLU A OE2 1 
ATOM   1914 N  N   . PRO A 1 236 ? 8.495   -9.181  -3.723  1.00 16.75  ? 237 PRO A N   1 
ATOM   1915 C  CA  . PRO A 1 236 ? 8.117   -10.563 -3.425  1.00 15.84  ? 237 PRO A CA  1 
ATOM   1916 C  C   . PRO A 1 236 ? 6.805   -10.593 -2.639  1.00 13.75  ? 237 PRO A C   1 
ATOM   1917 O  O   . PRO A 1 236 ? 6.531   -9.777  -1.727  1.00 15.14  ? 237 PRO A O   1 
ATOM   1918 C  CB  . PRO A 1 236 ? 9.324   -11.058 -2.589  1.00 18.03  ? 237 PRO A CB  1 
ATOM   1919 C  CG  . PRO A 1 236 ? 10.475  -10.235 -3.181  1.00 20.36  ? 237 PRO A CG  1 
ATOM   1920 C  CD  . PRO A 1 236 ? 9.878   -8.846  -3.305  1.00 19.57  ? 237 PRO A CD  1 
ATOM   1921 N  N   . GLU A 1 237 ? 5.992   -11.585 -2.924  1.00 14.13  ? 238 GLU A N   1 
ATOM   1922 C  CA  . GLU A 1 237 ? 4.641   -11.656 -2.401  1.00 14.01  ? 238 GLU A CA  1 
ATOM   1923 C  C   . GLU A 1 237 ? 4.672   -12.208 -0.972  1.00 13.60  ? 238 GLU A C   1 
ATOM   1924 O  O   . GLU A 1 237 ? 5.113   -13.360 -0.744  1.00 14.10  ? 238 GLU A O   1 
ATOM   1925 C  CB  . GLU A 1 237 ? 3.864   -12.527 -3.391  1.00 17.07  ? 238 GLU A CB  1 
ATOM   1926 C  CG  . GLU A 1 237 ? 2.425   -12.772 -2.987  1.00 20.03  ? 238 GLU A CG  1 
ATOM   1927 C  CD  . GLU A 1 237 ? 1.726   -13.702 -4.016  1.00 30.56  ? 238 GLU A CD  1 
ATOM   1928 O  OE1 . GLU A 1 237 ? 2.221   -13.864 -5.151  1.00 39.69  ? 238 GLU A OE1 1 
ATOM   1929 O  OE2 . GLU A 1 237 ? 0.727   -14.325 -3.681  1.00 36.93  ? 238 GLU A OE2 1 
ATOM   1930 N  N   . GLU A 1 238 ? 4.116   -11.437 -0.047  1.00 12.28  ? 239 GLU A N   1 
ATOM   1931 C  CA  . GLU A 1 238 ? 3.981   -11.868 1.343   1.00 12.18  ? 239 GLU A CA  1 
ATOM   1932 C  C   . GLU A 1 238 ? 2.532   -11.583 1.712   1.00 10.99  ? 239 GLU A C   1 
ATOM   1933 O  O   . GLU A 1 238 ? 2.087   -10.418 1.741   1.00 13.98  ? 239 GLU A O   1 
ATOM   1934 C  CB  . GLU A 1 238 ? 4.884   -11.059 2.262   1.00 15.50  ? 239 GLU A CB  1 
ATOM   1935 C  CG  . GLU A 1 238 ? 6.351   -11.374 2.016   1.00 16.96  ? 239 GLU A CG  1 
ATOM   1936 C  CD  . GLU A 1 238 ? 7.258   -10.656 2.985   1.00 17.02  ? 239 GLU A CD  1 
ATOM   1937 O  OE1 . GLU A 1 238 ? 7.286   -10.997 4.186   1.00 22.06  ? 239 GLU A OE1 1 
ATOM   1938 O  OE2 . GLU A 1 238 ? 7.960   -9.739  2.562   1.00 19.64  ? 239 GLU A OE2 1 
ATOM   1939 N  N   A LEU A 1 239 ? 1.763   -12.653 1.966   0.50 11.01  ? 240 LEU A N   1 
ATOM   1940 N  N   B LEU A 1 239 ? 1.806   -12.662 1.993   0.50 11.23  ? 240 LEU A N   1 
ATOM   1941 C  CA  A LEU A 1 239 ? 0.344   -12.450 2.255   0.50 11.43  ? 240 LEU A CA  1 
ATOM   1942 C  CA  B LEU A 1 239 ? 0.405   -12.480 2.335   0.50 10.76  ? 240 LEU A CA  1 
ATOM   1943 C  C   A LEU A 1 239 ? 0.194   -11.720 3.579   0.50 9.48   ? 240 LEU A C   1 
ATOM   1944 C  C   B LEU A 1 239 ? 0.300   -11.601 3.571   0.50 10.25  ? 240 LEU A C   1 
ATOM   1945 O  O   A LEU A 1 239 ? 0.859   -12.023 4.572   0.50 10.70  ? 240 LEU A O   1 
ATOM   1946 O  O   B LEU A 1 239 ? 1.081   -11.713 4.524   0.50 10.45  ? 240 LEU A O   1 
ATOM   1947 C  CB  A LEU A 1 239 ? -0.386  -13.792 2.323   0.50 12.70  ? 240 LEU A CB  1 
ATOM   1948 C  CB  B LEU A 1 239 ? -0.166  -13.857 2.633   0.50 14.37  ? 240 LEU A CB  1 
ATOM   1949 C  CG  A LEU A 1 239 ? -0.374  -14.586 1.026   0.50 15.80  ? 240 LEU A CG  1 
ATOM   1950 C  CG  B LEU A 1 239 ? -0.598  -14.696 1.440   0.50 14.36  ? 240 LEU A CG  1 
ATOM   1951 C  CD1 A LEU A 1 239 ? -0.877  -15.984 1.227   0.50 20.92  ? 240 LEU A CD1 1 
ATOM   1952 C  CD1 B LEU A 1 239 ? 0.544   -15.102 0.467   0.50 14.44  ? 240 LEU A CD1 1 
ATOM   1953 C  CD2 A LEU A 1 239 ? -1.249  -13.863 0.066   0.50 11.93  ? 240 LEU A CD2 1 
ATOM   1954 C  CD2 B LEU A 1 239 ? -1.345  -15.853 2.039   0.50 13.00  ? 240 LEU A CD2 1 
ATOM   1955 N  N   . MET A 1 240 ? -0.770  -10.804 3.597   1.00 10.89  ? 241 MET A N   1 
ATOM   1956 C  CA  . MET A 1 240 ? -1.100  -9.987  4.781   1.00 10.51  ? 241 MET A CA  1 
ATOM   1957 C  C   . MET A 1 240 ? -1.935  -10.845 5.725   1.00 10.43  ? 241 MET A C   1 
ATOM   1958 O  O   . MET A 1 240 ? -3.130  -10.972 5.585   1.00 11.03  ? 241 MET A O   1 
ATOM   1959 C  CB  . MET A 1 240 ? -1.884  -8.728  4.345   1.00 11.25  ? 241 MET A CB  1 
ATOM   1960 C  CG  . MET A 1 240 ? -2.209  -7.796  5.515   1.00 10.92  ? 241 MET A CG  1 
ATOM   1961 S  SD  . MET A 1 240 ? -3.109  -6.341  5.032   1.00 12.29  ? 241 MET A SD  1 
ATOM   1962 C  CE  . MET A 1 240 ? -1.804  -5.359  4.262   1.00 12.83  ? 241 MET A CE  1 
ATOM   1963 N  N   . VAL A 1 241 ? -1.199  -11.466 6.664   1.00 10.36  ? 242 VAL A N   1 
ATOM   1964 C  CA  . VAL A 1 241 ? -1.799  -12.323 7.695   1.00 10.24  ? 242 VAL A CA  1 
ATOM   1965 C  C   . VAL A 1 241 ? -0.977  -12.100 8.962   1.00 8.80   ? 242 VAL A C   1 
ATOM   1966 O  O   . VAL A 1 241 ? 0.215   -11.704 8.888   1.00 10.52  ? 242 VAL A O   1 
ATOM   1967 C  CB  . VAL A 1 241 ? -1.782  -13.834 7.334   1.00 10.55  ? 242 VAL A CB  1 
ATOM   1968 C  CG1 . VAL A 1 241 ? -2.710  -14.065 6.129   1.00 12.49  ? 242 VAL A CG1 1 
ATOM   1969 C  CG2 . VAL A 1 241 ? -0.372  -14.377 7.060   1.00 12.17  ? 242 VAL A CG2 1 
ATOM   1970 N  N   . ASP A 1 242 ? -1.570  -12.358 10.115  1.00 9.12   ? 243 ASP A N   1 
ATOM   1971 C  CA  . ASP A 1 242 ? -0.896  -12.235 11.393  1.00 9.06   ? 243 ASP A CA  1 
ATOM   1972 C  C   . ASP A 1 242 ? -0.372  -10.825 11.605  1.00 9.05   ? 243 ASP A C   1 
ATOM   1973 O  O   . ASP A 1 242 ? 0.715   -10.577 12.158  1.00 11.20  ? 243 ASP A O   1 
ATOM   1974 C  CB  . ASP A 1 242 ? 0.190   -13.320 11.616  1.00 10.51  ? 243 ASP A CB  1 
ATOM   1975 C  CG  . ASP A 1 242 ? -0.444  -14.685 11.674  1.00 10.34  ? 243 ASP A CG  1 
ATOM   1976 O  OD1 . ASP A 1 242 ? -1.483  -14.828 12.374  1.00 10.73  ? 243 ASP A OD1 1 
ATOM   1977 O  OD2 . ASP A 1 242 ? 0.159   -15.643 11.085  1.00 13.01  ? 243 ASP A OD2 1 
ATOM   1978 N  N   . ASN A 1 243 ? -1.243  -9.843  11.327  1.00 8.59   ? 244 ASN A N   1 
ATOM   1979 C  CA  . ASN A 1 243 ? -0.959  -8.425  11.516  1.00 8.09   ? 244 ASN A CA  1 
ATOM   1980 C  C   . ASN A 1 243 ? -1.542  -7.964  12.850  1.00 8.19   ? 244 ASN A C   1 
ATOM   1981 O  O   . ASN A 1 243 ? -2.221  -6.930  12.950  1.00 9.93   ? 244 ASN A O   1 
ATOM   1982 C  CB  . ASN A 1 243 ? -1.459  -7.573  10.329  1.00 9.00   ? 244 ASN A CB  1 
ATOM   1983 C  CG  . ASN A 1 243 ? -2.938  -7.719  10.090  1.00 9.04   ? 244 ASN A CG  1 
ATOM   1984 O  OD1 . ASN A 1 243 ? -3.579  -8.592  10.647  1.00 9.94   ? 244 ASN A OD1 1 
ATOM   1985 N  ND2 . ASN A 1 243 ? -3.500  -6.833  9.257   1.00 10.94  ? 244 ASN A ND2 1 
ATOM   1986 N  N   . TRP A 1 244 ? -1.212  -8.682  13.921  1.00 8.70   ? 245 TRP A N   1 
ATOM   1987 C  CA  . TRP A 1 244 ? -1.681  -8.407  15.273  1.00 9.14   ? 245 TRP A CA  1 
ATOM   1988 C  C   . TRP A 1 244 ? -0.496  -8.292  16.241  1.00 8.84   ? 245 TRP A C   1 
ATOM   1989 O  O   . TRP A 1 244 ? 0.492   -9.048  16.099  1.00 10.35  ? 245 TRP A O   1 
ATOM   1990 C  CB  . TRP A 1 244 ? -2.679  -9.476  15.775  1.00 9.23   ? 245 TRP A CB  1 
ATOM   1991 C  CG  . TRP A 1 244 ? -2.203  -10.896 15.604  1.00 9.11   ? 245 TRP A CG  1 
ATOM   1992 C  CD1 . TRP A 1 244 ? -2.329  -11.653 14.475  1.00 9.07   ? 245 TRP A CD1 1 
ATOM   1993 C  CD2 . TRP A 1 244 ? -1.603  -11.753 16.611  1.00 9.56   ? 245 TRP A CD2 1 
ATOM   1994 N  NE1 . TRP A 1 244 ? -1.839  -12.926 14.691  1.00 9.45   ? 245 TRP A NE1 1 
ATOM   1995 C  CE2 . TRP A 1 244 ? -1.370  -12.991 15.987  1.00 9.87   ? 245 TRP A CE2 1 
ATOM   1996 C  CE3 . TRP A 1 244 ? -1.275  -11.597 17.970  1.00 10.49  ? 245 TRP A CE3 1 
ATOM   1997 C  CZ2 . TRP A 1 244 ? -0.798  -14.077 16.654  1.00 11.16  ? 245 TRP A CZ2 1 
ATOM   1998 C  CZ3 . TRP A 1 244 ? -0.768  -12.670 18.657  1.00 12.03  ? 245 TRP A CZ3 1 
ATOM   1999 C  CH2 . TRP A 1 244 ? -0.502  -13.904 17.999  1.00 11.85  ? 245 TRP A CH2 1 
ATOM   2000 N  N   . ARG A 1 245 ? -0.587  -7.338  17.161  1.00 9.38   ? 246 ARG A N   1 
ATOM   2001 C  CA  . ARG A 1 245 ? 0.356   -7.243  18.278  1.00 8.56   ? 246 ARG A CA  1 
ATOM   2002 C  C   . ARG A 1 245 ? -0.152  -8.150  19.386  1.00 9.29   ? 246 ARG A C   1 
ATOM   2003 O  O   . ARG A 1 245 ? -1.326  -8.136  19.730  1.00 10.77  ? 246 ARG A O   1 
ATOM   2004 C  CB  . ARG A 1 245 ? 0.381   -5.768  18.765  1.00 9.29   ? 246 ARG A CB  1 
ATOM   2005 C  CG  . ARG A 1 245 ? 1.509   -5.535  19.796  1.00 9.53   ? 246 ARG A CG  1 
ATOM   2006 C  CD  . ARG A 1 245 ? 1.403   -4.172  20.402  1.00 9.77   ? 246 ARG A CD  1 
ATOM   2007 N  NE  . ARG A 1 245 ? 2.650   -3.853  21.123  1.00 9.81   ? 246 ARG A NE  1 
ATOM   2008 C  CZ  . ARG A 1 245 ? 2.830   -2.814  21.911  1.00 9.89   ? 246 ARG A CZ  1 
ATOM   2009 N  NH1 . ARG A 1 245 ? 1.844   -2.020  22.281  1.00 11.16  ? 246 ARG A NH1 1 
ATOM   2010 N  NH2 . ARG A 1 245 ? 4.077   -2.527  22.351  1.00 11.38  ? 246 ARG A NH2 1 
ATOM   2011 N  N   . PRO A 1 246 ? 0.738   -8.918  20.039  1.00 10.07  ? 247 PRO A N   1 
ATOM   2012 C  CA  . PRO A 1 246 ? 0.311   -9.763  21.167  1.00 10.90  ? 247 PRO A CA  1 
ATOM   2013 C  C   . PRO A 1 246 ? -0.036  -8.907  22.404  1.00 9.90   ? 247 PRO A C   1 
ATOM   2014 O  O   . PRO A 1 246 ? 0.319   -7.721  22.519  1.00 10.81  ? 247 PRO A O   1 
ATOM   2015 C  CB  . PRO A 1 246 ? 1.521   -10.651 21.446  1.00 13.58  ? 247 PRO A CB  1 
ATOM   2016 C  CG  . PRO A 1 246 ? 2.431   -10.485 20.253  1.00 22.19  ? 247 PRO A CG  1 
ATOM   2017 C  CD  . PRO A 1 246 ? 2.156   -9.124  19.680  1.00 12.22  ? 247 PRO A CD  1 
ATOM   2018 N  N   . ALA A 1 247 ? -0.687  -9.552  23.365  1.00 10.95  ? 248 ALA A N   1 
ATOM   2019 C  CA  . ALA A 1 247 ? -1.027  -8.903  24.642  1.00 11.02  ? 248 ALA A CA  1 
ATOM   2020 C  C   . ALA A 1 247 ? 0.246   -8.382  25.336  1.00 10.78  ? 248 ALA A C   1 
ATOM   2021 O  O   . ALA A 1 247 ? 1.276   -9.054  25.401  1.00 12.28  ? 248 ALA A O   1 
ATOM   2022 C  CB  . ALA A 1 247 ? -1.778  -9.901  25.540  1.00 13.23  ? 248 ALA A CB  1 
ATOM   2023 N  N   . GLN A 1 248 ? 0.080   -7.201  25.923  1.00 10.27  ? 249 GLN A N   1 
ATOM   2024 C  CA  . GLN A 1 248 ? 1.131   -6.469  26.623  1.00 10.96  ? 249 GLN A CA  1 
ATOM   2025 C  C   . GLN A 1 248 ? 0.842   -6.467  28.118  1.00 11.81  ? 249 GLN A C   1 
ATOM   2026 O  O   . GLN A 1 248 ? -0.298  -6.671  28.559  1.00 12.24  ? 249 GLN A O   1 
ATOM   2027 C  CB  . GLN A 1 248 ? 1.170   -5.022  26.085  1.00 11.54  ? 249 GLN A CB  1 
ATOM   2028 C  CG  . GLN A 1 248 ? 1.467   -4.966  24.581  1.00 11.26  ? 249 GLN A CG  1 
ATOM   2029 C  CD  . GLN A 1 248 ? 2.795   -5.622  24.278  1.00 13.22  ? 249 GLN A CD  1 
ATOM   2030 O  OE1 . GLN A 1 248 ? 3.823   -5.270  24.838  1.00 14.53  ? 249 GLN A OE1 1 
ATOM   2031 N  NE2 . GLN A 1 248 ? 2.763   -6.594  23.361  1.00 13.35  ? 249 GLN A NE2 1 
ATOM   2032 N  N   . PRO A 1 249 ? 1.838   -6.139  28.970  1.00 12.52  ? 250 PRO A N   1 
ATOM   2033 C  CA  . PRO A 1 249 ? 1.642   -6.163  30.424  1.00 14.22  ? 250 PRO A CA  1 
ATOM   2034 C  C   . PRO A 1 249 ? 0.553   -5.185  30.852  1.00 12.34  ? 250 PRO A C   1 
ATOM   2035 O  O   . PRO A 1 249 ? 0.565   -4.002  30.498  1.00 12.67  ? 250 PRO A O   1 
ATOM   2036 C  CB  . PRO A 1 249 ? 3.034   -5.794  30.972  1.00 19.63  ? 250 PRO A CB  1 
ATOM   2037 C  CG  . PRO A 1 249 ? 4.002   -6.103  29.890  1.00 20.18  ? 250 PRO A CG  1 
ATOM   2038 C  CD  . PRO A 1 249 ? 3.256   -5.904  28.588  1.00 15.71  ? 250 PRO A CD  1 
ATOM   2039 N  N   . LEU A 1 250 ? -0.310  -5.668  31.755  1.00 12.43  ? 251 LEU A N   1 
ATOM   2040 C  CA  . LEU A 1 250 ? -1.364  -4.814  32.247  1.00 12.40  ? 251 LEU A CA  1 
ATOM   2041 C  C   . LEU A 1 250 ? -0.836  -3.715  33.162  1.00 12.00  ? 251 LEU A C   1 
ATOM   2042 O  O   . LEU A 1 250 ? -1.418  -2.610  33.250  1.00 12.68  ? 251 LEU A O   1 
ATOM   2043 C  CB  . LEU A 1 250 ? -2.381  -5.668  32.999  1.00 14.86  ? 251 LEU A CB  1 
ATOM   2044 C  CG  . LEU A 1 250 ? -3.702  -4.960  33.411  1.00 16.22  ? 251 LEU A CG  1 
ATOM   2045 C  CD1 . LEU A 1 250 ? -4.489  -4.407  32.172  1.00 16.08  ? 251 LEU A CD1 1 
ATOM   2046 C  CD2 . LEU A 1 250 ? -4.608  -5.939  34.205  1.00 21.15  ? 251 LEU A CD2 1 
ATOM   2047 N  N   . LYS A 1 251 ? 0.212   -3.996  33.926  1.00 13.15  ? 252 LYS A N   1 
ATOM   2048 C  CA  . LYS A 1 251 ? 0.831   -2.980  34.797  1.00 14.65  ? 252 LYS A CA  1 
ATOM   2049 C  C   . LYS A 1 251 ? -0.219  -2.432  35.792  1.00 14.40  ? 252 LYS A C   1 
ATOM   2050 O  O   . LYS A 1 251 ? -1.046  -3.203  36.291  1.00 18.10  ? 252 LYS A O   1 
ATOM   2051 C  CB  . LYS A 1 251 ? 1.699   -1.956  34.052  1.00 16.74  ? 252 LYS A CB  1 
ATOM   2052 C  CG  . LYS A 1 251 ? 2.834   -2.611  33.258  1.00 19.43  ? 252 LYS A CG  1 
ATOM   2053 C  CD  . LYS A 1 251 ? 3.753   -1.696  32.549  1.00 21.43  ? 252 LYS A CD  1 
ATOM   2054 C  CE  . LYS A 1 251 ? 4.976   -2.374  31.989  1.00 23.96  ? 252 LYS A CE  1 
ATOM   2055 N  NZ  . LYS A 1 251 ? 5.841   -1.365  31.304  1.00 28.82  ? 252 LYS A NZ  1 
ATOM   2056 N  N   . ASN A 1 252 ? -0.219  -1.119  35.994  1.00 14.30  ? 253 ASN A N   1 
ATOM   2057 C  CA  . ASN A 1 252 ? -1.045  -0.625  37.064  1.00 21.82  ? 253 ASN A CA  1 
ATOM   2058 C  C   . ASN A 1 252 ? -2.355  -0.191  36.423  1.00 24.14  ? 253 ASN A C   1 
ATOM   2059 O  O   . ASN A 1 252 ? -2.572  1.088   36.440  1.00 23.23  ? 253 ASN A O   1 
ATOM   2060 C  CB  . ASN A 1 252 ? -0.283  0.477   37.821  1.00 25.65  ? 253 ASN A CB  1 
ATOM   2061 C  CG  . ASN A 1 252 ? -1.060  1.113   38.966  1.00 27.00  ? 253 ASN A CG  1 
ATOM   2062 O  OD1 . ASN A 1 252 ? -1.638  0.431   39.806  1.00 46.65  ? 253 ASN A OD1 1 
ATOM   2063 N  ND2 . ASN A 1 252 ? -1.146  2.433   38.957  1.00 28.42  ? 253 ASN A ND2 1 
ATOM   2064 N  N   . ARG A 1 253 ? -3.150  -1.239  35.873  1.00 17.00  ? 254 ARG A N   1 
ATOM   2065 C  CA  . ARG A 1 253 ? -4.445  -0.879  35.299  1.00 12.48  ? 254 ARG A CA  1 
ATOM   2066 C  C   . ARG A 1 253 ? -5.488  -1.854  35.768  1.00 13.94  ? 254 ARG A C   1 
ATOM   2067 O  O   . ARG A 1 253 ? -5.219  -3.028  35.972  1.00 20.21  ? 254 ARG A O   1 
ATOM   2068 C  CB  . ARG A 1 253 ? -4.386  -0.897  33.789  1.00 12.14  ? 254 ARG A CB  1 
ATOM   2069 C  CG  . ARG A 1 253 ? -3.476  0.246   33.299  1.00 11.85  ? 254 ARG A CG  1 
ATOM   2070 C  CD  . ARG A 1 253 ? -3.380  0.246   31.775  1.00 11.16  ? 254 ARG A CD  1 
ATOM   2071 N  NE  . ARG A 1 253 ? -2.552  -0.895  31.303  1.00 9.90   ? 254 ARG A NE  1 
ATOM   2072 C  CZ  . ARG A 1 253 ? -2.300  -1.121  30.026  1.00 8.29   ? 254 ARG A CZ  1 
ATOM   2073 N  NH1 . ARG A 1 253 ? -2.915  -0.460  29.044  1.00 9.33   ? 254 ARG A NH1 1 
ATOM   2074 N  NH2 . ARG A 1 253 ? -1.506  -2.124  29.725  1.00 9.61   ? 254 ARG A NH2 1 
ATOM   2075 N  N   . GLN A 1 254 ? -6.705  -1.332  35.844  1.00 14.20  ? 255 GLN A N   1 
ATOM   2076 C  CA  . GLN A 1 254 ? -7.895  -2.116  36.091  1.00 14.67  ? 255 GLN A CA  1 
ATOM   2077 C  C   . GLN A 1 254 ? -8.767  -2.098  34.839  1.00 13.66  ? 255 GLN A C   1 
ATOM   2078 O  O   . GLN A 1 254 ? -8.984  -1.057  34.187  1.00 17.60  ? 255 GLN A O   1 
ATOM   2079 C  CB  . GLN A 1 254 ? -8.700  -1.514  37.231  1.00 21.72  ? 255 GLN A CB  1 
ATOM   2080 C  CG  . GLN A 1 254 ? -7.990  -1.767  38.578  1.00 23.98  ? 255 GLN A CG  1 
ATOM   2081 N  N   . ILE A 1 255 ? -9.280  -3.293  34.478  1.00 12.05  ? 256 ILE A N   1 
ATOM   2082 C  CA  . ILE A 1 255 ? -10.277 -3.415  33.417  1.00 11.51  ? 256 ILE A CA  1 
ATOM   2083 C  C   . ILE A 1 255 ? -11.639 -3.430  34.079  1.00 11.60  ? 256 ILE A C   1 
ATOM   2084 O  O   . ILE A 1 255 ? -11.859 -4.136  35.082  1.00 13.41  ? 256 ILE A O   1 
ATOM   2085 C  CB  . ILE A 1 255 ? -10.008 -4.676  32.587  1.00 11.75  ? 256 ILE A CB  1 
ATOM   2086 C  CG1 . ILE A 1 255 ? -8.550  -4.681  32.026  1.00 13.03  ? 256 ILE A CG1 1 
ATOM   2087 C  CG2 . ILE A 1 255 ? -11.057 -4.751  31.471  1.00 13.66  ? 256 ILE A CG2 1 
ATOM   2088 C  CD1 . ILE A 1 255 ? -8.235  -5.892  31.174  1.00 14.89  ? 256 ILE A CD1 1 
ATOM   2089 N  N   . LYS A 1 256 ? -12.527 -2.542  33.592  1.00 11.09  ? 257 LYS A N   1 
ATOM   2090 C  CA  . LYS A 1 256 ? -13.862 -2.437  34.105  1.00 11.55  ? 257 LYS A CA  1 
ATOM   2091 C  C   . LYS A 1 256 ? -14.839 -3.072  33.162  1.00 12.51  ? 257 LYS A C   1 
ATOM   2092 O  O   . LYS A 1 256 ? -14.675 -2.995  31.965  1.00 13.96  ? 257 LYS A O   1 
ATOM   2093 C  CB  . LYS A 1 256 ? -14.197 -0.965  34.339  1.00 14.38  ? 257 LYS A CB  1 
ATOM   2094 C  CG  . LYS A 1 256 ? -13.294 -0.356  35.441  1.00 19.77  ? 257 LYS A CG  1 
ATOM   2095 C  CD  . LYS A 1 256 ? -13.432 1.095   35.672  1.00 31.80  ? 257 LYS A CD  1 
ATOM   2096 C  CE  . LYS A 1 256 ? -12.391 1.611   36.647  1.00 46.76  ? 257 LYS A CE  1 
ATOM   2097 N  NZ  . LYS A 1 256 ? -12.417 3.098   36.724  1.00 46.64  ? 257 LYS A NZ  1 
ATOM   2098 N  N   . ALA A 1 257 ? -15.889 -3.694  33.704  1.00 12.34  ? 258 ALA A N   1 
ATOM   2099 C  CA  . ALA A 1 257 ? -16.964 -4.294  32.895  1.00 12.75  ? 258 ALA A CA  1 
ATOM   2100 C  C   . ALA A 1 257 ? -18.230 -3.473  33.054  1.00 11.65  ? 258 ALA A C   1 
ATOM   2101 O  O   . ALA A 1 257 ? -18.581 -3.061  34.156  1.00 13.34  ? 258 ALA A O   1 
ATOM   2102 C  CB  . ALA A 1 257 ? -17.246 -5.742  33.309  1.00 14.89  ? 258 ALA A CB  1 
ATOM   2103 N  N   . SER A 1 258 ? -18.970 -3.337  31.928  1.00 12.28  ? 259 SER A N   1 
ATOM   2104 C  CA  . SER A 1 258 ? -20.244 -2.602  31.970  1.00 13.84  ? 259 SER A CA  1 
ATOM   2105 C  C   . SER A 1 258 ? -21.408 -3.515  32.402  1.00 14.72  ? 259 SER A C   1 
ATOM   2106 O  O   . SER A 1 258 ? -22.539 -3.020  32.488  1.00 19.42  ? 259 SER A O   1 
ATOM   2107 C  CB  . SER A 1 258 ? -20.574 -2.030  30.638  1.00 14.69  ? 259 SER A CB  1 
ATOM   2108 O  OG  . SER A 1 258 ? -20.942 -3.057  29.703  1.00 13.43  ? 259 SER A OG  1 
ATOM   2109 N  N   . PHE A 1 259 ? -21.134 -4.797  32.649  1.00 15.29  ? 260 PHE A N   1 
ATOM   2110 C  CA  . PHE A 1 259 ? -22.150 -5.833  32.799  1.00 18.04  ? 260 PHE A CA  1 
ATOM   2111 C  C   . PHE A 1 259 ? -21.701 -6.759  33.939  1.00 21.02  ? 260 PHE A C   1 
ATOM   2112 O  O   . PHE A 1 259 ? -20.510 -6.892  34.229  1.00 20.02  ? 260 PHE A O   1 
ATOM   2113 C  CB  . PHE A 1 259 ? -22.383 -6.584  31.486  1.00 17.39  ? 260 PHE A CB  1 
ATOM   2114 C  CG  . PHE A 1 259 ? -21.112 -7.302  31.073  1.00 15.59  ? 260 PHE A CG  1 
ATOM   2115 C  CD1 . PHE A 1 259 ? -20.139 -6.615  30.383  1.00 14.94  ? 260 PHE A CD1 1 
ATOM   2116 C  CD2 . PHE A 1 259 ? -20.912 -8.652  31.424  1.00 19.06  ? 260 PHE A CD2 1 
ATOM   2117 C  CE1 . PHE A 1 259 ? -18.938 -7.287  30.062  1.00 18.33  ? 260 PHE A CE1 1 
ATOM   2118 C  CE2 . PHE A 1 259 ? -19.731 -9.319  31.100  1.00 21.88  ? 260 PHE A CE2 1 
ATOM   2119 C  CZ  . PHE A 1 259 ? -18.759 -8.627  30.386  1.00 20.40  ? 260 PHE A CZ  1 
ATOM   2120 N  N   . LYS A 1 260 ? -22.727 -7.434  34.482  1.00 30.10  ? 261 LYS A N   1 
ATOM   2121 C  CA  . LYS A 1 260 ? -22.597 -8.544  35.464  1.00 42.41  ? 261 LYS A CA  1 
ATOM   2122 C  C   . LYS A 1 260 ? -22.869 -8.072  36.890  1.00 52.00  ? 261 LYS A C   1 
ATOM   2123 O  O   . LYS A 1 260 ? -23.890 -7.484  37.292  1.00 61.38  ? 261 LYS A O   1 
ATOM   2124 C  CB  . LYS A 1 260 ? -21.208 -9.182  35.361  1.00 55.05  ? 261 LYS A CB  1 
ATOM   2125 C  CG  . LYS A 1 260 ? -21.148 -10.489 34.581  1.00 55.00  ? 261 LYS A CG  1 
ATOM   2126 C  CD  . LYS A 1 260 ? -22.447 -10.829 33.881  1.00 50.32  ? 261 LYS A CD  1 
ATOM   2127 O  OXT . LYS A 1 260 ? -21.979 -8.284  37.703  1.00 85.00  ? 261 LYS A OXT 1 
HETATM 2128 ZN ZN  . ZN  B 2 .   ? -6.141  -1.733  15.195  1.00 7.94   ? 301 ZN  A ZN  1 
HETATM 2129 O  O18 . E1F C 3 .   ? -4.882  0.965   18.062  1.00 8.54   ? 302 E1F A O18 1 
HETATM 2130 C  C13 . E1F C 3 .   ? -1.020  8.558   15.921  1.00 28.07  ? 302 E1F A C13 1 
HETATM 2131 C  C1  . E1F C 3 .   ? -3.826  4.216   14.216  1.00 16.50  ? 302 E1F A C1  1 
HETATM 2132 C  C2  . E1F C 3 .   ? -5.271  3.451   16.041  1.00 11.13  ? 302 E1F A C2  1 
HETATM 2133 CL CL1 . E1F C 3 .   ? -6.257  3.841   17.367  1.00 14.15  ? 302 E1F A CL1 1 
HETATM 2134 C  C21 . E1F C 3 .   ? -4.755  4.518   15.245  1.00 13.67  ? 302 E1F A C21 1 
HETATM 2135 C  C5  . E1F C 3 .   ? -3.462  2.909   13.955  1.00 18.17  ? 302 E1F A C5  1 
HETATM 2136 C  C4  . E1F C 3 .   ? -4.002  1.893   14.699  1.00 13.53  ? 302 E1F A C4  1 
HETATM 2137 C  C3  . E1F C 3 .   ? -4.859  2.142   15.771  1.00 10.18  ? 302 E1F A C3  1 
HETATM 2138 S  S16 . E1F C 3 .   ? -5.443  0.780   16.738  1.00 8.79   ? 302 E1F A S16 1 
HETATM 2139 N  N19 . E1F C 3 .   ? -4.854  -0.530  16.061  1.00 8.89   ? 302 E1F A N19 1 
HETATM 2140 O  O17 . E1F C 3 .   ? -6.894  0.821   16.608  1.00 9.76   ? 302 E1F A O17 1 
HETATM 2141 C  C6  . E1F C 3 .   ? -3.177  5.367   13.462  1.00 22.91  ? 302 E1F A C6  1 
HETATM 2142 O  O12 . E1F C 3 .   ? -3.780  6.436   13.415  1.00 28.72  ? 302 E1F A O12 1 
HETATM 2143 C  C7  . E1F C 3 .   ? -1.714  5.265   13.085  1.00 25.06  ? 302 E1F A C7  1 
HETATM 2144 S  S8  . E1F C 3 .   ? -0.952  6.705   12.343  1.00 29.20  ? 302 E1F A S8  1 
HETATM 2145 C  C9  . E1F C 3 .   ? -0.716  7.880   13.651  1.00 27.12  ? 302 E1F A C9  1 
HETATM 2146 N  N11 . E1F C 3 .   ? -0.025  9.019   13.359  1.00 34.89  ? 302 E1F A N11 1 
HETATM 2147 C  C14 . E1F C 3 .   ? 0.157   9.932   14.354  1.00 28.80  ? 302 E1F A C14 1 
HETATM 2148 C  C15 . E1F C 3 .   ? -0.355  9.717   15.656  1.00 26.85  ? 302 E1F A C15 1 
HETATM 2149 N  N10 . E1F C 3 .   ? -1.170  7.640   14.907  1.00 26.32  ? 302 E1F A N10 1 
HETATM 2150 C  C   . BEZ D 4 .   ? -3.020  3.885   10.150  1.00 33.42  ? 303 BEZ A C   1 
HETATM 2151 O  O1  . BEZ D 4 .   ? -1.878  4.438   9.921   1.00 41.23  ? 303 BEZ A O1  1 
HETATM 2152 O  O2  . BEZ D 4 .   ? -4.112  4.452   10.107  1.00 45.33  ? 303 BEZ A O2  1 
HETATM 2153 C  C1  . BEZ D 4 .   ? -3.012  2.416   10.409  1.00 31.38  ? 303 BEZ A C1  1 
HETATM 2154 C  C2  . BEZ D 4 .   ? -1.789  1.733   10.433  1.00 39.17  ? 303 BEZ A C2  1 
HETATM 2155 C  C3  . BEZ D 4 .   ? -1.751  0.361   10.643  1.00 29.56  ? 303 BEZ A C3  1 
HETATM 2156 C  C4  . BEZ D 4 .   ? -2.929  -0.335  10.826  1.00 30.64  ? 303 BEZ A C4  1 
HETATM 2157 C  C5  . BEZ D 4 .   ? -4.150  0.337   10.812  1.00 28.79  ? 303 BEZ A C5  1 
HETATM 2158 C  C6  . BEZ D 4 .   ? -4.202  1.700   10.566  1.00 33.77  ? 303 BEZ A C6  1 
HETATM 2159 S  S   . DMS E 5 .   ? 1.759   -11.706 14.971  1.00 25.64  ? 304 DMS A S   1 
HETATM 2160 O  O   . DMS E 5 .   ? 2.274   -13.130 14.489  1.00 36.30  ? 304 DMS A O   1 
HETATM 2161 C  C1  . DMS E 5 .   ? 3.029   -10.537 14.555  1.00 37.53  ? 304 DMS A C1  1 
HETATM 2162 C  C2  . DMS E 5 .   ? 2.103   -11.583 16.685  1.00 21.49  ? 304 DMS A C2  1 
HETATM 2163 O  O   . HOH F 6 .   ? -14.921 19.250  13.016  1.00 23.95  ? 401 HOH A O   1 
HETATM 2164 O  O   . HOH F 6 .   ? -25.248 -10.453 17.385  1.00 27.90  ? 402 HOH A O   1 
HETATM 2165 O  O   . HOH F 6 .   ? -3.778  -1.349  37.990  1.00 35.37  ? 403 HOH A O   1 
HETATM 2166 O  O   . HOH F 6 .   ? -18.115 20.215  14.790  1.00 29.97  ? 404 HOH A O   1 
HETATM 2167 O  O   . HOH F 6 .   ? -10.486 13.255  8.301   1.00 23.84  ? 405 HOH A O   1 
HETATM 2168 O  O   . HOH F 6 .   ? -15.809 -15.035 32.686  1.00 45.45  ? 406 HOH A O   1 
HETATM 2169 O  O   . HOH F 6 .   ? -12.698 9.688   -3.020  1.00 33.85  ? 407 HOH A O   1 
HETATM 2170 O  O   . HOH F 6 .   ? -0.934  -12.766 -3.426  1.00 48.00  ? 408 HOH A O   1 
HETATM 2171 O  O   . HOH F 6 .   ? -17.426 19.072  5.908   1.00 11.09  ? 409 HOH A O   1 
HETATM 2172 O  O   . HOH F 6 .   ? -12.846 -22.425 11.733  1.00 35.53  ? 410 HOH A O   1 
HETATM 2173 O  O   . HOH F 6 .   ? -18.855 12.537  12.785  1.00 48.10  ? 411 HOH A O   1 
HETATM 2174 O  O   . HOH F 6 .   ? -24.563 9.770   12.894  1.00 32.61  ? 412 HOH A O   1 
HETATM 2175 O  O   . HOH F 6 .   ? -3.336  -19.812 6.340   1.00 27.25  ? 413 HOH A O   1 
HETATM 2176 O  O   . HOH F 6 .   ? -9.445  15.575  29.650  1.00 42.74  ? 414 HOH A O   1 
HETATM 2177 O  O   . HOH F 6 .   ? -10.148 -5.591  38.419  1.00 27.58  ? 415 HOH A O   1 
HETATM 2178 O  O   . HOH F 6 .   ? -10.713 -15.110 34.208  1.00 29.38  ? 416 HOH A O   1 
HETATM 2179 O  O   . HOH F 6 .   ? -28.118 11.592  5.266   1.00 15.33  ? 417 HOH A O   1 
HETATM 2180 O  O   . HOH F 6 .   ? 7.939   -1.373  -4.529  1.00 37.67  ? 418 HOH A O   1 
HETATM 2181 O  O   . HOH F 6 .   ? -0.947  -16.135 -3.434  1.00 32.96  ? 419 HOH A O   1 
HETATM 2182 O  O   . HOH F 6 .   ? 1.865   -9.411  -5.090  1.00 31.90  ? 420 HOH A O   1 
HETATM 2183 O  O   . HOH F 6 .   ? -11.957 12.676  29.138  1.00 27.26  ? 421 HOH A O   1 
HETATM 2184 O  O   . HOH F 6 .   ? -19.956 8.620   30.032  1.00 30.36  ? 422 HOH A O   1 
HETATM 2185 O  O   . HOH F 6 .   ? -20.455 18.978  13.070  1.00 58.91  ? 423 HOH A O   1 
HETATM 2186 O  O   . HOH F 6 .   ? -15.441 -11.933 39.231  1.00 29.84  ? 424 HOH A O   1 
HETATM 2187 O  O   . HOH F 6 .   ? -25.836 13.772  6.522   1.00 20.02  ? 425 HOH A O   1 
HETATM 2188 O  O   . HOH F 6 .   ? -5.670  9.677   6.553   1.00 37.87  ? 426 HOH A O   1 
HETATM 2189 O  O   . HOH F 6 .   ? -14.003 -16.394 29.068  1.00 24.43  ? 427 HOH A O   1 
HETATM 2190 O  O   . HOH F 6 .   ? -11.894 4.147   -7.134  1.00 34.60  ? 428 HOH A O   1 
HETATM 2191 O  O   . HOH F 6 .   ? -15.295 -10.072 37.854  1.00 38.21  ? 429 HOH A O   1 
HETATM 2192 O  O   . HOH F 6 .   ? -26.701 -10.605 22.132  1.00 55.29  ? 430 HOH A O   1 
HETATM 2193 O  O   . HOH F 6 .   ? -23.706 -2.793  29.114  1.00 47.80  ? 431 HOH A O   1 
HETATM 2194 O  O   . HOH F 6 .   ? -23.629 8.714   20.112  1.00 20.91  ? 432 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? -13.494 14.370  27.153  1.00 29.04  ? 433 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? -6.318  -20.331 19.562  1.00 16.78  ? 434 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? -10.190 21.599  19.954  1.00 28.30  ? 435 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? -10.133 -18.303 17.296  1.00 17.47  ? 436 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? -14.476 0.371   -3.722  1.00 30.46  ? 437 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? -24.474 -10.882 23.744  1.00 39.82  ? 438 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? -7.829  7.862   9.225   1.00 43.18  ? 439 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? 4.608   -3.368  26.470  1.00 21.44  ? 440 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? -12.391 13.365  31.916  1.00 34.60  ? 441 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? -17.470 14.003  2.117   1.00 47.65  ? 442 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? -0.767  -4.149  15.717  1.00 11.42  ? 443 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? 2.200   8.224   28.134  1.00 32.38  ? 444 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? -23.721 -17.508 6.704   1.00 51.41  ? 445 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? -14.080 -21.188 3.030   1.00 33.71  ? 446 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? 3.251   9.839   17.942  1.00 45.26  ? 447 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? 4.061   5.141   29.792  1.00 18.99  ? 448 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? -10.119 8.748   25.413  1.00 13.75  ? 449 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? 1.766   -6.113  34.332  1.00 29.87  ? 450 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? -21.107 19.532  17.142  1.00 40.98  ? 451 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? -4.657  2.302   37.563  1.00 30.06  ? 452 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? -23.611 0.075   1.236   1.00 41.51  ? 453 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? 5.876   -11.244 19.294  1.00 41.35  ? 454 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? -21.648 -18.419 13.522  1.00 26.31  ? 455 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? -19.090 -20.818 4.886   1.00 20.61  ? 456 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? -22.562 15.388  18.856  1.00 44.20  ? 457 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? 9.980   -8.483  3.786   1.00 38.18  ? 458 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? -24.351 4.633   8.571   1.00 31.97  ? 459 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? -22.979 -11.054 17.143  1.00 25.88  ? 460 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? 1.057   -1.808  -4.800  1.00 15.43  ? 461 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? -26.816 -7.352  26.120  1.00 34.06  ? 462 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? -9.181  13.030  10.273  1.00 21.44  ? 463 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? -5.558  -4.926  -6.554  1.00 18.11  ? 464 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? -0.612  9.219   27.879  1.00 23.82  ? 465 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? -20.625 -6.632  -2.180  1.00 31.06  ? 466 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? -4.398  -11.850 32.165  1.00 23.18  ? 467 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? -12.115 -21.875 8.410   1.00 35.01  ? 468 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? -6.635  -14.775 31.692  1.00 23.65  ? 469 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? -19.897 -16.625 3.058   1.00 22.71  ? 470 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? -31.072 -10.837 16.177  1.00 19.11  ? 471 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? -19.519 -4.179  41.253  1.00 34.59  ? 472 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? -24.966 -1.225  34.874  1.00 46.44  ? 473 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? 8.274   -8.674  0.032   1.00 19.33  ? 474 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? -6.201  6.892   12.278  1.00 46.25  ? 475 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? -3.654  -13.172 -3.016  1.00 24.31  ? 476 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? -5.446  17.381  27.331  1.00 37.61  ? 477 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? -9.839  -12.434 40.118  1.00 29.62  ? 478 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? -25.816 -7.305  30.505  1.00 38.89  ? 479 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? 0.445   1.195   34.519  1.00 23.52  ? 480 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? -13.319 10.499  27.792  1.00 19.69  ? 481 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? -21.475 -14.040 18.680  1.00 37.92  ? 482 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? -8.464  6.032   28.844  1.00 29.32  ? 483 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? -7.602  -15.639 11.485  1.00 12.03  ? 484 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? 11.671  -3.723  7.522   1.00 38.18  ? 485 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? 1.911   2.721   5.144   1.00 35.04  ? 486 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? -4.121  -13.538 18.086  1.00 10.90  ? 487 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? -2.085  -8.673  29.112  1.00 13.40  ? 488 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? -25.483 6.395   27.021  1.00 25.30  ? 489 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? 12.008  -0.239  15.917  1.00 21.77  ? 490 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? -18.038 3.818   -3.956  1.00 39.32  ? 491 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? 8.996   -3.702  21.107  1.00 13.36  ? 492 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? 5.476   7.258   20.312  1.00 17.11  ? 493 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? 2.265   -15.814 9.334   1.00 21.44  ? 494 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? 6.269   -0.659  -1.228  1.00 37.14  ? 495 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? -19.795 10.904  26.716  1.00 21.35  ? 496 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? 13.717  0.560   24.512  1.00 17.14  ? 497 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? -25.027 14.404  11.318  1.00 35.81  ? 498 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? -22.466 -14.791 16.209  1.00 45.41  ? 499 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? -17.074 -16.218 22.003  1.00 24.73  ? 500 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? -20.142 2.023   -3.561  1.00 38.82  ? 501 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? -12.474 10.238  -5.814  1.00 41.72  ? 502 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? -3.096  -11.194 20.923  1.00 11.33  ? 503 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? -14.562 20.130  17.615  1.00 23.53  ? 504 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? -20.468 7.818   1.755   1.00 12.10  ? 505 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? -22.545 -5.866  2.588   1.00 18.21  ? 506 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? -17.458 10.647  11.189  1.00 16.34  ? 507 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? -16.581 -8.311  20.329  1.00 9.90   ? 508 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? -15.728 16.065  23.515  1.00 24.40  ? 509 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? -3.840  -8.452  31.215  1.00 23.94  ? 510 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? -10.955 10.279  8.229   1.00 23.62  ? 511 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? -17.524 20.588  7.884   1.00 13.89  ? 512 HOH A O   1 
HETATM 2275 O  O   . HOH F 6 .   ? -7.787  0.395   -6.569  1.00 24.29  ? 513 HOH A O   1 
HETATM 2276 O  O   . HOH F 6 .   ? -21.221 5.753   4.609   1.00 11.83  ? 514 HOH A O   1 
HETATM 2277 O  O   . HOH F 6 .   ? -26.222 -2.323  14.283  1.00 15.12  ? 515 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? -12.507 -9.032  -3.274  1.00 16.39  ? 516 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? -3.390  -15.860 24.472  1.00 15.03  ? 517 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? -2.998  -13.228 25.258  1.00 13.34  ? 518 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? -12.772 -0.865  -5.817  1.00 21.37  ? 519 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? -16.739 -13.911 37.673  1.00 28.56  ? 520 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? -2.063  -3.459  11.342  1.00 17.48  ? 521 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? -22.912 -13.246 11.310  1.00 19.99  ? 522 HOH A O   1 
HETATM 2285 O  O   . HOH F 6 .   ? -29.150 -9.499  22.646  1.00 38.62  ? 523 HOH A O   1 
HETATM 2286 O  O   . HOH F 6 .   ? -15.715 -12.326 24.409  1.00 16.53  ? 524 HOH A O   1 
HETATM 2287 O  O   . HOH F 6 .   ? -21.135 -6.987  23.529  1.00 13.09  ? 525 HOH A O   1 
HETATM 2288 O  O   . HOH F 6 .   ? 8.470   -6.194  0.246   1.00 34.80  ? 526 HOH A O   1 
HETATM 2289 O  O   . HOH F 6 .   ? 0.287   -20.074 10.799  1.00 56.86  ? 527 HOH A O   1 
HETATM 2290 O  O   . HOH F 6 .   ? 3.210   -4.592  7.804   1.00 20.87  ? 528 HOH A O   1 
HETATM 2291 O  O   . HOH F 6 .   ? 9.672   7.599   18.760  1.00 35.55  ? 529 HOH A O   1 
HETATM 2292 O  O   . HOH F 6 .   ? -18.640 10.028  8.705   1.00 12.59  ? 530 HOH A O   1 
HETATM 2293 O  O   . HOH F 6 .   ? -18.448 -4.272  -2.750  1.00 21.62  ? 531 HOH A O   1 
HETATM 2294 O  O   . HOH F 6 .   ? -18.971 -12.254 -3.432  1.00 16.85  ? 532 HOH A O   1 
HETATM 2295 O  O   . HOH F 6 .   ? 10.935  -9.224  9.082   1.00 26.48  ? 533 HOH A O   1 
HETATM 2296 O  O   . HOH F 6 .   ? -12.633 -16.770 26.642  1.00 17.40  ? 534 HOH A O   1 
HETATM 2297 O  O   . HOH F 6 .   ? -6.986  -8.582  32.659  1.00 18.50  ? 535 HOH A O   1 
HETATM 2298 O  O   . HOH F 6 .   ? -25.701 3.437   15.453  1.00 33.11  ? 536 HOH A O   1 
HETATM 2299 O  O   . HOH F 6 .   ? -1.178  -5.280  -7.178  1.00 27.54  ? 537 HOH A O   1 
HETATM 2300 O  O   . HOH F 6 .   ? -7.611  9.417   11.224  1.00 46.03  ? 538 HOH A O   1 
HETATM 2301 O  O   . HOH F 6 .   ? 5.363   -4.887  21.025  1.00 13.41  ? 539 HOH A O   1 
HETATM 2302 O  O   . HOH F 6 .   ? -22.804 -2.860  6.498   1.00 17.87  ? 540 HOH A O   1 
HETATM 2303 O  O   . HOH F 6 .   ? 4.925   -1.348  -5.319  1.00 29.74  ? 541 HOH A O   1 
HETATM 2304 O  O   . HOH F 6 .   ? -22.877 -0.079  34.401  1.00 34.58  ? 542 HOH A O   1 
HETATM 2305 O  O   . HOH F 6 .   ? -16.627 -11.369 36.191  1.00 41.27  ? 543 HOH A O   1 
HETATM 2306 O  O   . HOH F 6 .   ? -24.284 12.016  6.145   1.00 19.39  ? 544 HOH A O   1 
HETATM 2307 O  O   . HOH F 6 .   ? -3.471  5.276   -2.937  1.00 18.32  ? 545 HOH A O   1 
HETATM 2308 O  O   . HOH F 6 .   ? -14.336 -18.475 18.723  1.00 19.16  ? 546 HOH A O   1 
HETATM 2309 O  O   . HOH F 6 .   ? 4.783   -2.372  28.889  1.00 26.53  ? 547 HOH A O   1 
HETATM 2310 O  O   . HOH F 6 .   ? -14.202 6.475   32.589  1.00 43.01  ? 548 HOH A O   1 
HETATM 2311 O  O   . HOH F 6 .   ? -8.752  5.379   2.822   1.00 19.17  ? 549 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? -24.557 -7.643  9.020   1.00 16.39  ? 550 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? -13.565 -16.047 -0.511  1.00 30.85  ? 551 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? -16.384 18.921  21.941  1.00 51.05  ? 552 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? 11.604  1.576   26.022  1.00 20.90  ? 553 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? -13.052 -18.572 14.663  1.00 21.53  ? 554 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? -0.523  -5.990  36.484  1.00 28.72  ? 555 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? -11.552 2.861   30.829  1.00 21.00  ? 556 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? -0.939  -17.773 18.199  1.00 33.44  ? 557 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? 10.390  -2.155  -0.955  1.00 48.58  ? 558 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? -8.193  -22.183 10.616  1.00 19.30  ? 559 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? -23.175 -0.737  3.774   1.00 19.55  ? 560 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? -15.175 9.004   -2.250  1.00 24.65  ? 561 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? -0.189  10.694  23.433  1.00 24.25  ? 562 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? 9.930   0.076   14.408  1.00 31.14  ? 563 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? -4.437  -16.081 0.538   1.00 26.15  ? 564 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? -7.705  6.392   0.270   1.00 16.15  ? 565 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? 4.399   4.343   10.716  1.00 37.36  ? 566 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? -26.231 -3.743  25.230  1.00 19.75  ? 567 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? -6.953  -16.795 1.169   1.00 21.78  ? 568 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? 8.081   -2.808  -6.841  1.00 38.90  ? 569 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? -16.010 -9.786  32.914  1.00 18.84  ? 570 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? -14.620 2.507   38.732  1.00 38.31  ? 571 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? 1.642   -1.446  29.453  1.00 16.55  ? 572 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? -7.534  -19.099 30.664  1.00 32.63  ? 573 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? -4.833  15.554  12.124  1.00 36.86  ? 574 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? 8.585   3.286   27.810  1.00 30.13  ? 575 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? -12.317 7.960   28.738  1.00 26.77  ? 576 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? 2.041   12.566  22.798  1.00 38.92  ? 577 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? -6.459  -8.790  -7.224  1.00 27.62  ? 578 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? -2.150  -19.246 21.907  1.00 41.86  ? 579 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? 9.812   0.231   30.595  1.00 54.45  ? 580 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? 4.683   -4.048  4.240   1.00 41.45  ? 581 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? -25.583 -6.213  12.786  1.00 24.68  ? 582 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? -24.914 6.266   3.134   1.00 32.90  ? 583 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? -25.351 8.008   6.223   1.00 24.26  ? 584 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? 9.924   -4.526  -7.960  1.00 45.08  ? 585 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? -0.133  -8.470  32.542  1.00 23.70  ? 586 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? -8.695  10.558  6.936   1.00 41.14  ? 587 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? -8.697  -5.726  35.979  1.00 20.25  ? 588 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? 7.372   -3.394  29.868  1.00 38.56  ? 589 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? -25.505 12.306  13.313  1.00 37.04  ? 590 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? 8.525   -9.333  16.524  1.00 19.69  ? 591 HOH A O   1 
HETATM 2354 O  O   . HOH F 6 .   ? 5.482   -7.355  22.336  1.00 28.58  ? 592 HOH A O   1 
HETATM 2355 O  O   . HOH F 6 .   ? -8.781  -10.102 -1.381  1.00 24.78  ? 593 HOH A O   1 
HETATM 2356 O  O   . HOH F 6 .   ? -10.658 1.216   33.413  1.00 27.12  ? 594 HOH A O   1 
HETATM 2357 O  O   . HOH F 6 .   ? -27.320 -11.996 16.053  1.00 37.28  ? 595 HOH A O   1 
HETATM 2358 O  O   . HOH F 6 .   ? -2.251  4.453   6.883   1.00 33.75  ? 596 HOH A O   1 
HETATM 2359 O  O   . HOH F 6 .   ? 4.764   -7.009  7.954   1.00 25.00  ? 597 HOH A O   1 
HETATM 2360 O  O   . HOH F 6 .   ? -1.655  -12.295 22.932  1.00 12.35  ? 598 HOH A O   1 
HETATM 2361 O  O   . HOH F 6 .   ? 1.908   8.851   23.819  1.00 16.67  ? 599 HOH A O   1 
HETATM 2362 O  O   . HOH F 6 .   ? 0.291   -20.827 15.682  1.00 59.66  ? 600 HOH A O   1 
HETATM 2363 O  O   . HOH F 6 .   ? -8.718  15.047  11.935  1.00 21.54  ? 601 HOH A O   1 
HETATM 2364 O  O   . HOH F 6 .   ? 1.824   -11.938 25.145  1.00 27.39  ? 602 HOH A O   1 
HETATM 2365 O  O   . HOH F 6 .   ? 13.307  -3.643  13.216  1.00 24.37  ? 603 HOH A O   1 
HETATM 2366 O  O   . HOH F 6 .   ? 6.214   -3.624  6.755   1.00 35.78  ? 604 HOH A O   1 
HETATM 2367 O  O   . HOH F 6 .   ? -17.255 17.678  4.100   1.00 30.77  ? 605 HOH A O   1 
HETATM 2368 O  O   . HOH F 6 .   ? -13.222 20.151  14.889  1.00 26.32  ? 606 HOH A O   1 
HETATM 2369 O  O   . HOH F 6 .   ? -20.952 -19.611 6.568   1.00 21.88  ? 607 HOH A O   1 
HETATM 2370 O  O   . HOH F 6 .   ? -23.526 -0.515  26.554  1.00 17.51  ? 608 HOH A O   1 
HETATM 2371 O  O   . HOH F 6 .   ? -11.802 12.820  6.321   1.00 31.41  ? 609 HOH A O   1 
HETATM 2372 O  O   . HOH F 6 .   ? 1.942   -17.841 13.783  1.00 39.08  ? 610 HOH A O   1 
HETATM 2373 O  O   . HOH F 6 .   ? -19.608 14.158  29.120  1.00 51.34  ? 611 HOH A O   1 
HETATM 2374 O  O   . HOH F 6 .   ? -0.259  2.900   -5.480  1.00 37.49  ? 612 HOH A O   1 
HETATM 2375 O  O   . HOH F 6 .   ? -29.294 9.569   5.998   1.00 31.34  ? 613 HOH A O   1 
HETATM 2376 O  O   . HOH F 6 .   ? -5.877  -19.819 23.929  1.00 29.58  ? 614 HOH A O   1 
HETATM 2377 O  O   . HOH F 6 .   ? 10.758  6.839   15.329  1.00 40.07  ? 615 HOH A O   1 
HETATM 2378 O  O   . HOH F 6 .   ? -9.186  -7.904  34.128  1.00 22.99  ? 616 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? -4.624  3.101   -5.956  1.00 17.84  ? 617 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? -6.596  1.598   35.180  1.00 25.63  ? 618 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? -14.696 -15.829 25.182  1.00 32.85  ? 619 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? 9.125   -13.042 8.959   1.00 43.51  ? 620 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? -7.787  -19.367 21.704  1.00 22.02  ? 621 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? 15.207  -10.316 14.455  1.00 25.73  ? 622 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? -16.064 5.899   -8.831  1.00 30.15  ? 623 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? 7.823   6.256   21.579  1.00 16.01  ? 624 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? 10.636  -2.507  13.458  1.00 23.71  ? 625 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? 0.179   -14.312 22.267  1.00 23.46  ? 626 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? -23.310 -0.009  31.638  1.00 51.66  ? 627 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? -18.663 17.631  18.663  1.00 39.52  ? 628 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? -22.726 -11.777 13.895  1.00 26.86  ? 629 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? -8.950  -21.367 8.238   1.00 27.97  ? 630 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? -18.259 -9.004  34.541  1.00 32.35  ? 631 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? 4.148   -0.867  5.141   1.00 51.88  ? 632 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? -10.150 20.722  25.041  1.00 26.93  ? 633 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? -10.004 5.740   -6.683  1.00 45.14  ? 634 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? -24.630 -9.423  1.965   1.00 21.20  ? 635 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? -26.615 3.289   20.873  1.00 35.89  ? 636 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? 6.971   -2.628  1.333   1.00 39.99  ? 637 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? -6.464  5.289   -6.319  1.00 28.52  ? 638 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? -25.047 3.693   4.249   1.00 49.66  ? 639 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? 14.161  6.284   18.794  1.00 40.32  ? 640 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? -6.876  -9.048  -2.500  1.00 29.00  ? 641 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? 2.238   -2.742  37.412  1.00 56.27  ? 642 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? -0.960  11.488  25.856  1.00 29.49  ? 643 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? -12.535 -17.186 16.885  1.00 16.72  ? 644 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? -10.359 -23.581 12.064  1.00 24.50  ? 645 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? -22.390 -9.447  25.251  1.00 28.85  ? 646 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? 11.995  -6.450  7.800   1.00 44.41  ? 647 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? -0.947  -13.176 27.284  1.00 27.52  ? 648 HOH A O   1 
HETATM 2411 O  O   . HOH F 6 .   ? 14.789  0.167   14.882  1.00 22.87  ? 649 HOH A O   1 
HETATM 2412 O  O   . HOH F 6 .   ? -24.645 11.272  19.601  1.00 33.17  ? 650 HOH A O   1 
HETATM 2413 O  O   . HOH F 6 .   ? -8.019  -17.438 34.838  1.00 28.97  ? 651 HOH A O   1 
HETATM 2414 O  O   . HOH F 6 .   ? 8.707   -8.437  7.266   1.00 51.20  ? 652 HOH A O   1 
HETATM 2415 O  O   . HOH F 6 .   ? -26.172 -6.171  5.178   1.00 34.84  ? 653 HOH A O   1 
HETATM 2416 O  O   . HOH F 6 .   ? -28.045 15.178  6.838   1.00 28.72  ? 654 HOH A O   1 
HETATM 2417 O  O   . HOH F 6 .   ? 9.010   -4.516  23.676  1.00 31.16  ? 655 HOH A O   1 
HETATM 2418 O  O   . HOH F 6 .   ? -26.217 10.156  4.681   1.00 24.48  ? 656 HOH A O   1 
HETATM 2419 O  O   . HOH F 6 .   ? -17.380 19.907  17.466  1.00 25.04  ? 657 HOH A O   1 
HETATM 2420 O  O   . HOH F 6 .   ? -9.187  10.086  -6.061  1.00 29.81  ? 658 HOH A O   1 
HETATM 2421 O  O   . HOH F 6 .   ? 0.925   2.491   1.779   1.00 29.49  ? 659 HOH A O   1 
HETATM 2422 O  O   . HOH F 6 .   ? -17.638 -5.057  -5.351  1.00 30.21  ? 660 HOH A O   1 
HETATM 2423 O  O   . HOH F 6 .   ? 6.727   -10.896 15.283  1.00 46.51  ? 661 HOH A O   1 
HETATM 2424 O  O   . HOH F 6 .   ? 0.518   -2.678  39.489  1.00 43.71  ? 662 HOH A O   1 
HETATM 2425 O  O   . HOH F 6 .   ? -24.605 8.792   26.118  1.00 36.93  ? 663 HOH A O   1 
HETATM 2426 O  O   . HOH F 6 .   ? 4.189   8.938   22.123  1.00 23.22  ? 664 HOH A O   1 
HETATM 2427 O  O   . HOH F 6 .   ? -17.565 -11.963 31.614  1.00 32.85  ? 665 HOH A O   1 
HETATM 2428 O  O   . HOH F 6 .   ? -3.522  -6.116  -8.048  1.00 33.09  ? 666 HOH A O   1 
HETATM 2429 O  O   . HOH F 6 .   ? 10.651  5.611   12.917  1.00 36.64  ? 667 HOH A O   1 
HETATM 2430 O  O   . HOH F 6 .   ? -26.754 -6.753  7.762   1.00 40.33  ? 668 HOH A O   1 
HETATM 2431 O  O   . HOH F 6 .   ? -2.450  -17.595 5.267   1.00 30.45  ? 669 HOH A O   1 
HETATM 2432 O  O   . HOH F 6 .   ? -6.858  -17.291 32.197  1.00 44.47  ? 670 HOH A O   1 
HETATM 2433 O  O   . HOH F 6 .   ? -1.701  -11.891 31.571  1.00 37.12  ? 671 HOH A O   1 
HETATM 2434 O  O   . HOH F 6 .   ? 5.858   -8.921  7.082   1.00 40.22  ? 672 HOH A O   1 
HETATM 2435 O  O   . HOH F 6 .   ? -16.350 -17.525 24.405  1.00 50.64  ? 673 HOH A O   1 
HETATM 2436 O  O   . HOH F 6 .   ? -29.804 -6.894  22.550  1.00 29.40  ? 674 HOH A O   1 
HETATM 2437 O  O   . HOH F 6 .   ? -17.128 0.304   -3.832  1.00 33.32  ? 675 HOH A O   1 
HETATM 2438 O  O   . HOH F 6 .   ? -1.614  -17.356 25.596  1.00 33.91  ? 676 HOH A O   1 
HETATM 2439 O  O   . HOH F 6 .   ? -10.043 5.068   30.725  1.00 29.45  ? 677 HOH A O   1 
HETATM 2440 O  O   . HOH F 6 .   ? 8.487   7.933   23.723  1.00 40.33  ? 678 HOH A O   1 
HETATM 2441 O  O   . HOH F 6 .   ? -3.510  10.745  13.173  1.00 56.64  ? 679 HOH A O   1 
HETATM 2442 O  O   . HOH F 6 .   ? -16.528 -18.105 20.277  1.00 30.30  ? 680 HOH A O   1 
HETATM 2443 O  O   . HOH F 6 .   ? -5.432  1.603   -7.872  1.00 42.19  ? 681 HOH A O   1 
HETATM 2444 O  O   . HOH F 6 .   ? -5.599  7.982   -5.591  1.00 26.01  ? 682 HOH A O   1 
HETATM 2445 O  O   . HOH F 6 .   ? -19.715 -23.269 4.032   1.00 23.55  ? 683 HOH A O   1 
HETATM 2446 O  O   . HOH F 6 .   ? -11.669 -24.554 9.659   1.00 38.49  ? 684 HOH A O   1 
HETATM 2447 O  O   . HOH F 6 .   ? -4.584  12.882  11.112  1.00 38.42  ? 685 HOH A O   1 
HETATM 2448 O  O   . HOH F 6 .   ? 4.530   -11.781 23.489  1.00 48.53  ? 686 HOH A O   1 
HETATM 2449 O  O   . HOH F 6 .   ? -14.098 -2.745  -6.912  1.00 41.71  ? 687 HOH A O   1 
HETATM 2450 O  O   . HOH F 6 .   ? 3.002   2.661   -0.369  1.00 36.42  ? 688 HOH A O   1 
HETATM 2451 O  O   . HOH F 6 .   ? 14.826  2.984   23.680  1.00 22.47  ? 689 HOH A O   1 
HETATM 2452 O  O   . HOH F 6 .   ? 0.930   0.046   -6.839  1.00 31.07  ? 690 HOH A O   1 
HETATM 2453 O  O   . HOH F 6 .   ? -16.519 -13.986 26.290  1.00 25.92  ? 691 HOH A O   1 
HETATM 2454 O  O   . HOH F 6 .   ? -1.944  15.612  12.433  1.00 30.51  ? 692 HOH A O   1 
HETATM 2455 O  O   . HOH F 6 .   ? -14.943 21.029  22.807  1.00 38.78  ? 693 HOH A O   1 
HETATM 2456 O  O   . HOH F 6 .   ? -6.813  11.609  10.147  1.00 30.75  ? 694 HOH A O   1 
HETATM 2457 O  O   . HOH F 6 .   ? -4.200  -9.592  33.484  1.00 33.76  ? 695 HOH A O   1 
HETATM 2458 O  O   . HOH F 6 .   ? -26.384 -7.529  1.868   1.00 44.99  ? 696 HOH A O   1 
HETATM 2459 O  O   . HOH F 6 .   ? -28.420 -5.619  24.657  1.00 24.27  ? 697 HOH A O   1 
HETATM 2460 O  O   . HOH F 6 .   ? -23.976 13.570  20.494  1.00 43.41  ? 698 HOH A O   1 
HETATM 2461 O  O   . HOH F 6 .   ? -10.842 -11.313 -3.092  1.00 27.31  ? 699 HOH A O   1 
HETATM 2462 O  O   . HOH F 6 .   ? -21.985 -12.244 24.883  1.00 37.82  ? 700 HOH A O   1 
HETATM 2463 O  O   . HOH F 6 .   ? -6.770  16.549  10.573  1.00 22.99  ? 701 HOH A O   1 
HETATM 2464 O  O   . HOH F 6 .   ? 11.198  -9.116  -0.120  1.00 27.61  ? 702 HOH A O   1 
HETATM 2465 O  O   . HOH F 6 .   ? -10.708 -15.788 -1.745  1.00 53.79  ? 703 HOH A O   1 
HETATM 2466 O  O   . HOH F 6 .   ? 0.461   -7.610  -7.450  1.00 40.89  ? 704 HOH A O   1 
HETATM 2467 O  O   . HOH F 6 .   ? 2.387   -14.266 20.734  1.00 29.74  ? 705 HOH A O   1 
HETATM 2468 O  O   . HOH F 6 .   ? -0.731  -11.056 29.116  1.00 20.68  ? 706 HOH A O   1 
HETATM 2469 O  O   . HOH F 6 .   ? -1.935  2.954   -7.315  1.00 29.60  ? 707 HOH A O   1 
HETATM 2470 O  O   . HOH F 6 .   ? -20.625 20.710  14.756  1.00 41.58  ? 708 HOH A O   1 
HETATM 2471 O  O   . HOH F 6 .   ? -3.095  7.045   -5.121  1.00 16.76  ? 709 HOH A O   1 
HETATM 2472 O  O   . HOH F 6 .   ? 12.473  4.457   27.278  1.00 40.78  ? 710 HOH A O   1 
HETATM 2473 O  O   . HOH F 6 .   ? -23.783 -7.237  0.003   1.00 42.16  ? 711 HOH A O   1 
HETATM 2474 O  O   . HOH F 6 .   ? -25.270 -3.117  5.926   1.00 43.84  ? 712 HOH A O   1 
HETATM 2475 O  O   . HOH F 6 .   ? -10.709 15.309  32.252  1.00 23.11  ? 713 HOH A O   1 
HETATM 2476 O  O   . HOH F 6 .   ? -16.264 -14.588 28.779  1.00 39.77  ? 714 HOH A O   1 
HETATM 2477 O  O   . HOH F 6 .   ? -6.885  -10.500 -4.674  1.00 36.78  ? 715 HOH A O   1 
HETATM 2478 O  O   . HOH F 6 .   ? -8.726  5.294   32.988  1.00 26.81  ? 716 HOH A O   1 
HETATM 2479 O  O   . HOH F 6 .   ? 2.754   9.691   26.283  1.00 34.69  ? 717 HOH A O   1 
HETATM 2480 O  O   . HOH F 6 .   ? -15.843 17.530  26.079  1.00 45.06  ? 718 HOH A O   1 
HETATM 2481 O  O   . HOH F 6 .   ? -5.164  -12.817 -5.305  1.00 35.16  ? 719 HOH A O   1 
HETATM 2482 O  O   . HOH F 6 .   ? 6.778   5.511   29.011  1.00 39.10  ? 720 HOH A O   1 
HETATM 2483 O  O   . HOH F 6 .   ? 12.645  -8.510  7.246   1.00 39.92  ? 721 HOH A O   1 
HETATM 2484 O  O   . HOH F 6 .   ? -4.443  -20.669 21.576  1.00 28.60  ? 722 HOH A O   1 
HETATM 2485 O  O   . HOH F 6 .   ? -3.591  -15.707 -2.185  1.00 27.22  ? 723 HOH A O   1 
HETATM 2486 O  O   . HOH F 6 .   ? -2.973  -20.012 26.550  1.00 50.24  ? 724 HOH A O   1 
HETATM 2487 O  O   . HOH F 6 .   ? -26.257 -1.002  26.038  1.00 18.97  ? 725 HOH A O   1 
HETATM 2488 O  O   . HOH F 6 .   ? -12.453 21.686  26.234  1.00 27.59  ? 726 HOH A O   1 
HETATM 2489 O  O   . HOH F 6 .   ? 11.900  -6.533  -1.428  1.00 38.30  ? 727 HOH A O   1 
HETATM 2490 O  O   . HOH F 6 .   ? 12.170  0.810   28.709  1.00 34.89  ? 728 HOH A O   1 
HETATM 2491 O  O   . HOH F 6 .   ? -27.470 -1.255  28.518  1.00 29.24  ? 729 HOH A O   1 
HETATM 2492 O  O   . HOH F 6 .   ? 5.735   8.781   26.509  1.00 59.32  ? 730 HOH A O   1 
HETATM 2493 O  O   . HOH F 6 .   ? -8.209  21.299  26.735  1.00 30.54  ? 731 HOH A O   1 
HETATM 2494 O  O   . HOH F 6 .   ? -17.240 -2.678  -6.803  1.00 38.87  ? 732 HOH A O   1 
HETATM 2495 O  O   . HOH F 6 .   ? 6.166   9.516   23.658  1.00 47.72  ? 733 HOH A O   1 
HETATM 2496 O  O   . HOH F 6 .   ? 14.414  5.261   25.359  1.00 25.65  ? 734 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 3   ? 0.2548 0.4672 0.4340 0.0253  -0.0249 -0.0941 3   HIS A N   
2    C  CA  . HIS A 3   ? 0.4777 0.4700 0.4719 0.0791  -0.0361 0.0069  3   HIS A CA  
3    C  C   . HIS A 3   ? 0.5465 0.5473 0.4378 -0.1018 -0.0026 -0.0133 3   HIS A C   
4    O  O   . HIS A 3   ? 0.6598 0.4877 0.4180 -0.0822 -0.0623 -0.0607 3   HIS A O   
5    C  CB  . HIS A 3   ? 0.2972 0.3090 0.5633 -0.0885 -0.0055 0.0478  3   HIS A CB  
6    C  CG  . HIS A 3   ? 0.3243 0.3909 0.4324 -0.0917 -0.0281 0.0085  3   HIS A CG  
7    N  ND1 . HIS A 3   ? 0.4061 0.4140 0.4520 0.0665  0.1263  0.0736  3   HIS A ND1 
8    C  CD2 . HIS A 3   ? 0.2455 0.3220 0.4945 0.0342  0.0085  0.0284  3   HIS A CD2 
9    C  CE1 . HIS A 3   ? 0.4554 0.4197 0.4406 0.0088  0.0775  0.0510  3   HIS A CE1 
10   N  NE2 . HIS A 3   ? 0.3581 0.4540 0.4910 0.0352  0.0188  0.0518  3   HIS A NE2 
11   N  N   . HIS A 4   ? 0.4071 0.4640 0.5781 -0.0149 0.1430  0.2172  4   HIS A N   
12   C  CA  . HIS A 4   ? 0.3238 0.4854 0.6763 0.0753  0.1074  0.2599  4   HIS A CA  
13   C  C   . HIS A 4   ? 0.2560 0.4724 0.3173 0.0579  0.0165  0.1269  4   HIS A C   
14   O  O   . HIS A 4   ? 0.3398 0.3615 0.3744 -0.1608 -0.0520 0.0844  4   HIS A O   
15   C  CB  . HIS A 4   ? 0.2992 0.1745 0.4840 0.0276  0.1179  0.0632  4   HIS A CB  
16   C  CG  . HIS A 4   ? 0.1335 0.1533 0.1777 0.0321  0.0277  0.0886  4   HIS A CG  
17   N  ND1 . HIS A 4   ? 0.3553 0.4352 0.4252 0.0910  -0.0583 -0.0179 4   HIS A ND1 
18   C  CD2 . HIS A 4   ? 0.1903 0.2143 0.2091 0.0306  0.0212  0.0511  4   HIS A CD2 
19   C  CE1 . HIS A 4   ? 0.5769 0.5631 0.5453 0.1617  0.0287  -0.0886 4   HIS A CE1 
20   N  NE2 . HIS A 4   ? 0.6516 0.5565 0.5931 0.0346  0.0979  -0.2392 4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1856 0.2824 0.4186 0.0004  0.0555  0.1390  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1346 0.2445 0.2770 -0.0326 0.0080  0.0629  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1134 0.2526 0.2208 0.0037  0.0168  0.0308  5   TRP A C   
24   O  O   . TRP A 5   ? 0.1601 0.3260 0.2377 0.0367  0.0086  0.0734  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1513 0.2530 0.2857 -0.0395 0.0082  0.0631  5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1808 0.1913 0.2354 -0.0355 0.0190  0.0357  5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.2143 0.2486 0.2927 -0.0245 0.0145  0.0999  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1587 0.1902 0.2052 0.0025  0.0072  -0.0067 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.2312 0.2041 0.2703 0.0106  -0.0111 0.0221  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1890 0.2236 0.1619 0.0147  -0.0093 0.0099  5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1421 0.2274 0.1517 -0.0298 -0.0062 -0.0178 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1932 0.2557 0.1575 0.0432  -0.0172 -0.0262 5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1544 0.2509 0.1414 -0.0139 -0.0094 -0.0308 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1623 0.2703 0.1483 0.0156  -0.0198 -0.0532 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1362 0.2064 0.1917 -0.0004 0.0284  -0.0059 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1590 0.2013 0.2010 0.0013  -0.0044 -0.0001 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1067 0.2238 0.1654 -0.0059 0.0083  -0.0100 6   GLY A C   
38   O  O   . GLY A 6   ? 0.1244 0.1948 0.1468 0.0149  0.0038  -0.0176 6   GLY A O   
39   N  N   . TYR A 7   ? 0.1292 0.2262 0.1628 -0.0114 0.0065  -0.0406 7   TYR A N   
40   C  CA  . TYR A 7   ? 0.1279 0.1697 0.2323 -0.0152 0.0152  -0.0453 7   TYR A CA  
41   C  C   . TYR A 7   ? 0.1339 0.2075 0.2804 0.0047  0.0136  -0.0472 7   TYR A C   
42   O  O   . TYR A 7   ? 0.1894 0.2121 0.4159 -0.0062 0.0518  -0.0465 7   TYR A O   
43   C  CB  . TYR A 7   ? 0.1168 0.2052 0.2179 -0.0033 0.0033  -0.0615 7   TYR A CB  
44   C  CG  . TYR A 7   ? 0.1136 0.1835 0.1698 -0.0148 -0.0083 -0.0414 7   TYR A CG  
45   C  CD1 . TYR A 7   ? 0.1046 0.1747 0.1662 -0.0116 -0.0019 -0.0440 7   TYR A CD1 
46   C  CD2 . TYR A 7   ? 0.1235 0.1978 0.1536 -0.0255 -0.0013 -0.0309 7   TYR A CD2 
47   C  CE1 . TYR A 7   ? 0.1210 0.1289 0.1824 -0.0092 -0.0289 -0.0291 7   TYR A CE1 
48   C  CE2 . TYR A 7   ? 0.1307 0.1766 0.1557 -0.0219 0.0115  -0.0039 7   TYR A CE2 
49   C  CZ  . TYR A 7   ? 0.1084 0.1493 0.1521 -0.0149 0.0003  -0.0225 7   TYR A CZ  
50   O  OH  . TYR A 7   ? 0.1697 0.1423 0.1544 0.0053  -0.0050 -0.0181 7   TYR A OH  
51   N  N   . GLY A 8   ? 0.1297 0.2297 0.2386 0.0261  0.0130  -0.0697 8   GLY A N   
52   C  CA  . GLY A 8   ? 0.1518 0.2533 0.3292 0.0439  0.0268  -0.1076 8   GLY A CA  
53   C  C   . GLY A 8   ? 0.1423 0.2107 0.3399 0.0177  0.0453  -0.0585 8   GLY A C   
54   O  O   . GLY A 8   ? 0.1472 0.2315 0.2864 -0.0025 0.0453  -0.0387 8   GLY A O   
55   N  N   . LYS A 9   ? 0.1481 0.2322 0.3373 0.0367  0.0256  -0.0678 9   LYS A N   
56   C  CA  . LYS A 9   ? 0.1872 0.1872 0.3820 0.0239  0.0070  -0.0490 9   LYS A CA  
57   C  C   . LYS A 9   ? 0.1611 0.1964 0.2444 0.0030  0.0245  -0.0251 9   LYS A C   
58   O  O   . LYS A 9   ? 0.1738 0.1855 0.2716 -0.0062 0.0057  0.0066  9   LYS A O   
59   C  CB  . LYS A 9   ? 0.2273 0.2035 0.4415 0.0407  0.0039  -0.0605 9   LYS A CB  
60   C  CG  . LYS A 9   ? 0.3990 0.2282 0.5269 0.1201  -0.0759 -0.0403 9   LYS A CG  
61   N  N   . HIS A 10  ? 0.1553 0.2156 0.2445 0.0430  0.0428  0.0084  10  HIS A N   
62   C  CA  . HIS A 10  ? 0.1479 0.2002 0.2470 0.0307  0.0738  0.0080  10  HIS A CA  
63   C  C   . HIS A 10  ? 0.1439 0.1851 0.2214 0.0278  0.0331  -0.0043 10  HIS A C   
64   O  O   . HIS A 10  ? 0.1461 0.2032 0.2621 0.0190  0.0352  -0.0055 10  HIS A O   
65   C  CB  . HIS A 10  ? 0.1890 0.2398 0.2052 0.0615  0.0671  -0.0173 10  HIS A CB  
66   C  CG  . HIS A 10  ? 0.1702 0.2068 0.2416 0.0146  0.0644  0.0083  10  HIS A CG  
67   N  ND1 . HIS A 10  ? 0.2068 0.2429 0.2962 0.0510  0.0069  -0.0354 10  HIS A ND1 
68   C  CD2 . HIS A 10  ? 0.2154 0.2061 0.2431 0.0229  0.0807  -0.0199 10  HIS A CD2 
69   C  CE1 . HIS A 10  ? 0.2694 0.2068 0.2645 0.0265  0.0310  -0.0146 10  HIS A CE1 
70   N  NE2 . HIS A 10  ? 0.2142 0.2089 0.2754 0.0221  0.0562  -0.0298 10  HIS A NE2 
71   N  N   . ASN A 11  ? 0.1306 0.1745 0.2235 0.0329  0.0392  0.0206  11  ASN A N   
72   C  CA  . ASN A 11  ? 0.1615 0.1804 0.1737 0.0175  0.0275  -0.0138 11  ASN A CA  
73   C  C   . ASN A 11  ? 0.1206 0.1729 0.1551 0.0178  0.0154  -0.0011 11  ASN A C   
74   O  O   . ASN A 11  ? 0.1420 0.1811 0.1605 0.0231  0.0006  -0.0138 11  ASN A O   
75   C  CB  . ASN A 11  ? 0.1499 0.2437 0.1830 0.0267  0.0154  0.0005  11  ASN A CB  
76   C  CG  . ASN A 11  ? 0.1763 0.2314 0.1569 0.0111  0.0205  -0.0029 11  ASN A CG  
77   O  OD1 . ASN A 11  ? 0.2085 0.2503 0.2145 0.0127  -0.0168 -0.0084 11  ASN A OD1 
78   N  ND2 . ASN A 11  ? 0.2391 0.3719 0.1603 0.0252  0.0172  0.0175  11  ASN A ND2 
79   N  N   . GLY A 12  ? 0.1298 0.1647 0.1604 0.0051  0.0241  -0.0046 12  GLY A N   
80   C  CA  . GLY A 12  ? 0.1357 0.2107 0.1224 0.0117  0.0296  -0.0171 12  GLY A CA  
81   C  C   . GLY A 12  ? 0.1086 0.1590 0.1377 0.0135  0.0107  -0.0013 12  GLY A C   
82   O  O   . GLY A 12  ? 0.1040 0.1557 0.1562 0.0021  -0.0031 0.0027  12  GLY A O   
83   N  N   . PRO A 13  ? 0.0994 0.1564 0.1568 0.0024  0.0134  -0.0219 13  PRO A N   
84   C  CA  . PRO A 13  ? 0.1332 0.1472 0.1234 0.0046  0.0110  -0.0075 13  PRO A CA  
85   C  C   . PRO A 13  ? 0.1337 0.1156 0.1632 -0.0082 0.0047  0.0233  13  PRO A C   
86   O  O   . PRO A 13  ? 0.1344 0.1517 0.1819 -0.0165 -0.0042 -0.0193 13  PRO A O   
87   C  CB  . PRO A 13  ? 0.1253 0.1493 0.1966 -0.0119 0.0075  -0.0135 13  PRO A CB  
88   C  CG  . PRO A 13  ? 0.1266 0.1507 0.1719 -0.0203 0.0187  -0.0271 13  PRO A CG  
89   C  CD  . PRO A 13  ? 0.1029 0.1734 0.2032 -0.0111 0.0118  -0.0368 13  PRO A CD  
90   N  N   . GLU A 14  ? 0.1414 0.1349 0.1831 0.0079  -0.0094 0.0107  14  GLU A N   
91   C  CA  . GLU A 14  ? 0.1574 0.1483 0.1874 -0.0024 -0.0131 0.0362  14  GLU A CA  
92   C  C   . GLU A 14  ? 0.1400 0.1258 0.1824 0.0181  -0.0122 0.0236  14  GLU A C   
93   O  O   . GLU A 14  ? 0.1585 0.1533 0.1910 0.0131  -0.0319 0.0130  14  GLU A O   
94   C  CB  . GLU A 14  ? 0.1761 0.1468 0.2643 0.0058  -0.0333 0.0617  14  GLU A CB  
95   C  CG  . GLU A 14  ? 0.3415 0.1769 0.3324 -0.0661 -0.0257 0.0885  14  GLU A CG  
96   C  CD  . GLU A 14  ? 0.5536 0.3001 0.3837 -0.1269 0.0490  0.0030  14  GLU A CD  
97   O  OE1 . GLU A 14  ? 0.5793 0.5435 0.3569 -0.2001 -0.0368 0.1169  14  GLU A OE1 
98   O  OE2 . GLU A 14  ? 0.5675 0.4380 0.3098 -0.0401 0.0718  0.0333  14  GLU A OE2 
99   N  N   . HIS A 15  ? 0.1142 0.1278 0.1594 0.0070  0.0022  0.0005  15  HIS A N   
100  C  CA  . HIS A 15  ? 0.1197 0.1206 0.1845 -0.0021 0.0167  0.0067  15  HIS A CA  
101  C  C   . HIS A 15  ? 0.1102 0.1429 0.1594 0.0074  0.0149  0.0163  15  HIS A C   
102  O  O   . HIS A 15  ? 0.0928 0.1549 0.1913 -0.0042 -0.0009 -0.0096 15  HIS A O   
103  C  CB  . HIS A 15  ? 0.1104 0.1450 0.1651 0.0151  0.0030  0.0052  15  HIS A CB  
104  C  CG  . HIS A 15  ? 0.1235 0.1515 0.1684 0.0157  0.0059  0.0027  15  HIS A CG  
105  N  ND1 . HIS A 15  ? 0.1382 0.1701 0.2081 0.0222  0.0033  -0.0055 15  HIS A ND1 
106  C  CD2 . HIS A 15  ? 0.1773 0.1497 0.1964 0.0293  -0.0105 -0.0032 15  HIS A CD2 
107  C  CE1 . HIS A 15  ? 0.1678 0.1880 0.1874 0.0565  -0.0111 -0.0165 15  HIS A CE1 
108  N  NE2 . HIS A 15  ? 0.1862 0.1804 0.2466 0.0445  -0.0102 -0.0171 15  HIS A NE2 
109  N  N   . TRP A 16  ? 0.1055 0.1377 0.1386 0.0152  0.0071  -0.0044 16  TRP A N   
110  C  CA  . TRP A 16  ? 0.0994 0.1267 0.1720 0.0055  -0.0116 -0.0102 16  TRP A CA  
111  C  C   . TRP A 16  ? 0.0980 0.1330 0.1587 -0.0064 -0.0125 -0.0163 16  TRP A C   
112  O  O   . TRP A 16  ? 0.1199 0.1221 0.1902 -0.0094 -0.0094 0.0103  16  TRP A O   
113  C  CB  . TRP A 16  ? 0.0935 0.1604 0.1400 -0.0002 -0.0024 -0.0044 16  TRP A CB  
114  C  CG  . TRP A 16  ? 0.1100 0.1254 0.1511 -0.0001 -0.0034 -0.0074 16  TRP A CG  
115  C  CD1 . TRP A 16  ? 0.1122 0.1312 0.1576 0.0118  0.0004  -0.0048 16  TRP A CD1 
116  C  CD2 . TRP A 16  ? 0.1090 0.1183 0.1398 0.0089  0.0006  0.0033  16  TRP A CD2 
117  N  NE1 . TRP A 16  ? 0.1082 0.1515 0.1353 0.0139  0.0073  -0.0121 16  TRP A NE1 
118  C  CE2 . TRP A 16  ? 0.1092 0.1259 0.1371 0.0058  -0.0041 0.0011  16  TRP A CE2 
119  C  CE3 . TRP A 16  ? 0.1049 0.1165 0.1470 0.0148  -0.0027 -0.0032 16  TRP A CE3 
120  C  CZ2 . TRP A 16  ? 0.1097 0.1260 0.1456 0.0063  -0.0034 -0.0042 16  TRP A CZ2 
121  C  CZ3 . TRP A 16  ? 0.1147 0.1421 0.1496 0.0020  0.0030  -0.0074 16  TRP A CZ3 
122  C  CH2 . TRP A 16  ? 0.1170 0.1483 0.1309 -0.0002 -0.0063 0.0023  16  TRP A CH2 
123  N  N   . HIS A 17  ? 0.1009 0.1506 0.1529 0.0033  -0.0078 -0.0034 17  HIS A N   
124  C  CA  . HIS A 17  ? 0.1196 0.1676 0.1319 -0.0206 -0.0195 0.0036  17  HIS A CA  
125  C  C   . HIS A 17  ? 0.1079 0.1603 0.1662 -0.0082 0.0023  -0.0024 17  HIS A C   
126  O  O   . HIS A 17  ? 0.1289 0.1630 0.1802 -0.0134 -0.0052 -0.0182 17  HIS A O   
127  C  CB  . HIS A 17  ? 0.1259 0.1758 0.1392 0.0124  0.0013  0.0068  17  HIS A CB  
128  C  CG  . HIS A 17  ? 0.1311 0.1676 0.1526 0.0060  -0.0057 0.0135  17  HIS A CG  
129  N  ND1 . HIS A 17  ? 0.1321 0.2251 0.1531 0.0027  -0.0133 0.0147  17  HIS A ND1 
130  C  CD2 . HIS A 17  ? 0.1474 0.1644 0.1770 0.0252  -0.0108 0.0241  17  HIS A CD2 
131  C  CE1 . HIS A 17  ? 0.1323 0.2407 0.2039 0.0303  0.0089  -0.0027 17  HIS A CE1 
132  N  NE2 . HIS A 17  ? 0.1427 0.1910 0.2046 0.0390  0.0120  0.0332  17  HIS A NE2 
133  N  N   . LYS A 18  ? 0.1005 0.1738 0.1593 -0.0080 0.0074  0.0104  18  LYS A N   
134  C  CA  . LYS A 18  ? 0.0957 0.1770 0.1956 0.0005  0.0149  0.0148  18  LYS A CA  
135  C  C   . LYS A 18  ? 0.1479 0.1581 0.2096 -0.0109 -0.0188 0.0034  18  LYS A C   
136  O  O   . LYS A 18  ? 0.1937 0.1848 0.3406 -0.0714 -0.0629 0.0713  18  LYS A O   
137  C  CB  . LYS A 18  ? 0.1046 0.2064 0.1754 0.0171  0.0018  0.0079  18  LYS A CB  
138  C  CG  . LYS A 18  ? 0.1242 0.1852 0.2064 0.0395  -0.0115 0.0044  18  LYS A CG  
139  C  CD  . LYS A 18  ? 0.1234 0.1978 0.2211 0.0271  0.0042  -0.0140 18  LYS A CD  
140  C  CE  . LYS A 18  ? 0.1196 0.1705 0.1989 0.0080  0.0099  0.0122  18  LYS A CE  
141  N  NZ  . LYS A 18  ? 0.1270 0.1709 0.1930 0.0285  0.0199  0.0304  18  LYS A NZ  
142  N  N   . ASP A 19  ? 0.1266 0.1865 0.1729 0.0174  -0.0044 0.0222  19  ASP A N   
143  C  CA  . ASP A 19  ? 0.1400 0.1610 0.2140 0.0011  -0.0009 0.0027  19  ASP A CA  
144  C  C   . ASP A 19  ? 0.1461 0.1362 0.2035 0.0035  0.0021  -0.0075 19  ASP A C   
145  O  O   . ASP A 19  ? 0.1755 0.1389 0.2580 -0.0263 0.0323  0.0141  19  ASP A O   
146  C  CB  . ASP A 19  ? 0.1697 0.2762 0.1729 0.0280  0.0030  0.0122  19  ASP A CB  
147  C  CG  . ASP A 19  ? 0.1608 0.4693 0.2875 0.0478  0.0388  -0.0751 19  ASP A CG  
148  O  OD1 . ASP A 19  ? 0.2709 0.4222 0.3958 0.0302  0.0889  -0.0122 19  ASP A OD1 
149  O  OD2 . ASP A 19  ? 0.3775 0.7488 0.5493 -0.1602 0.0947  -0.2897 19  ASP A OD2 
150  N  N   . PHE A 20  ? 0.1287 0.1556 0.1672 0.0024  0.0074  0.0052  20  PHE A N   
151  C  CA  . PHE A 20  ? 0.1346 0.1400 0.1744 -0.0084 0.0120  -0.0003 20  PHE A CA  
152  C  C   . PHE A 20  ? 0.1225 0.1406 0.1780 -0.0034 0.0117  0.0050  20  PHE A C   
153  O  O   . PHE A 20  ? 0.1323 0.1364 0.1641 -0.0043 0.0154  0.0111  20  PHE A O   
154  C  CB  . PHE A 20  ? 0.1567 0.1793 0.1835 -0.0309 -0.0289 0.0333  20  PHE A CB  
155  C  CG  . PHE A 20  ? 0.1116 0.2843 0.1932 -0.0133 0.0024  0.0705  20  PHE A CG  
156  C  CD1 . PHE A 20  ? 0.1623 0.3397 0.2859 -0.0458 -0.0221 0.1514  20  PHE A CD1 
157  C  CD2 . PHE A 20  ? 0.1311 0.3815 0.2050 -0.0580 0.0192  0.0425  20  PHE A CD2 
158  C  CE1 . PHE A 20  ? 0.2050 0.3400 0.2532 -0.0361 -0.0299 0.0747  20  PHE A CE1 
159  C  CE2 . PHE A 20  ? 0.1691 0.4045 0.2276 -0.0871 0.0209  0.0599  20  PHE A CE2 
160  C  CZ  . PHE A 20  ? 0.1867 0.4036 0.2133 -0.0763 -0.0373 0.0952  20  PHE A CZ  
161  N  N   . PRO A 21  ? 0.1291 0.1574 0.1801 -0.0131 0.0044  -0.0048 21  PRO A N   
162  C  CA  . PRO A 21  ? 0.1278 0.1995 0.1775 -0.0290 -0.0118 -0.0018 21  PRO A CA  
163  C  C   . PRO A 21  ? 0.1287 0.1914 0.1641 -0.0182 -0.0192 -0.0249 21  PRO A C   
164  O  O   . PRO A 21  ? 0.1298 0.2046 0.1754 -0.0062 -0.0181 0.0003  21  PRO A O   
165  C  CB  . PRO A 21  ? 0.1366 0.2902 0.2498 -0.0767 -0.0100 -0.0248 21  PRO A CB  
166  C  CG  . PRO A 21  ? 0.2929 0.2950 0.2683 -0.1301 -0.0656 0.0337  21  PRO A CG  
167  C  CD  . PRO A 21  ? 0.1675 0.1845 0.2215 -0.0565 0.0092  0.0109  21  PRO A CD  
168  N  N   A ILE A 22  ? 0.1266 0.1607 0.1644 -0.0170 -0.0067 -0.0239 22  ILE A N   
169  N  N   B ILE A 22  ? 0.1270 0.1693 0.1705 -0.0146 -0.0068 -0.0184 22  ILE A N   
170  C  CA  A ILE A 22  ? 0.1254 0.1312 0.1452 -0.0063 -0.0128 -0.0055 22  ILE A CA  
171  C  CA  B ILE A 22  ? 0.1111 0.1373 0.1923 -0.0303 -0.0163 0.0178  22  ILE A CA  
172  C  C   A ILE A 22  ? 0.1119 0.1428 0.1342 -0.0023 -0.0048 -0.0120 22  ILE A C   
173  C  C   B ILE A 22  ? 0.1297 0.1260 0.1578 -0.0027 -0.0034 -0.0140 22  ILE A C   
174  O  O   A ILE A 22  ? 0.1385 0.1521 0.1495 -0.0021 0.0109  0.0066  22  ILE A O   
175  O  O   B ILE A 22  ? 0.1171 0.1571 0.1865 -0.0164 -0.0029 -0.0076 22  ILE A O   
176  C  CB  A ILE A 22  ? 0.1429 0.1571 0.1423 0.0255  -0.0153 -0.0253 22  ILE A CB  
177  C  CB  B ILE A 22  ? 0.1348 0.1331 0.2046 -0.0084 -0.0026 0.0019  22  ILE A CB  
178  C  CG1 A ILE A 22  ? 0.1310 0.1045 0.1640 -0.0136 -0.0019 -0.0242 22  ILE A CG1 
179  C  CG1 B ILE A 22  ? 0.1711 0.1811 0.2353 0.0143  0.0182  -0.0315 22  ILE A CG1 
180  C  CG2 A ILE A 22  ? 0.1544 0.1400 0.1185 -0.0644 0.0211  -0.0241 22  ILE A CG2 
181  C  CG2 B ILE A 22  ? 0.1453 0.1949 0.1919 0.0106  -0.0436 0.0343  22  ILE A CG2 
182  C  CD1 A ILE A 22  ? 0.1417 0.1215 0.2183 0.0117  0.0122  0.0013  22  ILE A CD1 
183  C  CD1 B ILE A 22  ? 0.2438 0.2017 0.2508 -0.0573 0.0271  -0.0242 22  ILE A CD1 
184  N  N   . ALA A 23  ? 0.1232 0.1291 0.1576 0.0009  -0.0100 -0.0099 23  ALA A N   
185  C  CA  . ALA A 23  ? 0.1359 0.1180 0.1732 0.0107  -0.0052 -0.0113 23  ALA A CA  
186  C  C   . ALA A 23  ? 0.1251 0.1363 0.1859 0.0181  -0.0020 -0.0125 23  ALA A C   
187  O  O   . ALA A 23  ? 0.1535 0.1395 0.2143 -0.0093 0.0129  0.0051  23  ALA A O   
188  C  CB  . ALA A 23  ? 0.1132 0.1418 0.1671 0.0110  -0.0032 -0.0234 23  ALA A CB  
189  N  N   . LYS A 24  ? 0.1403 0.1737 0.1560 0.0182  -0.0044 0.0000  24  LYS A N   
190  C  CA  . LYS A 24  ? 0.1479 0.2084 0.1646 0.0326  -0.0085 0.0236  24  LYS A CA  
191  C  C   . LYS A 24  ? 0.1529 0.2526 0.1565 0.0006  -0.0109 -0.0085 24  LYS A C   
192  O  O   . LYS A 24  ? 0.1799 0.2615 0.1831 -0.0086 -0.0369 0.0092  24  LYS A O   
193  C  CB  . LYS A 24  ? 0.1535 0.2793 0.2053 0.0446  -0.0182 0.0117  24  LYS A CB  
194  C  CG  . LYS A 24  ? 0.1761 0.2719 0.2169 0.0717  0.0233  0.0142  24  LYS A CG  
195  C  CD  . LYS A 24  ? 0.2129 0.2915 0.3048 0.0844  -0.0025 0.0219  24  LYS A CD  
196  C  CE  . LYS A 24  ? 0.2276 0.2912 0.3231 0.0601  0.0570  0.0364  24  LYS A CE  
197  N  NZ  . LYS A 24  ? 0.3982 0.2802 0.3975 -0.0275 0.0629  -0.0802 24  LYS A NZ  
198  N  N   . GLY A 25  ? 0.1479 0.2063 0.1714 0.0221  0.0114  -0.0165 25  GLY A N   
199  C  CA  . GLY A 25  ? 0.1823 0.2175 0.1747 0.0088  0.0306  -0.0280 25  GLY A CA  
200  C  C   . GLY A 25  ? 0.1404 0.2036 0.1496 0.0031  -0.0238 -0.0257 25  GLY A C   
201  O  O   . GLY A 25  ? 0.1763 0.2089 0.1500 0.0052  -0.0042 -0.0196 25  GLY A O   
202  N  N   . GLU A 26  ? 0.1270 0.2406 0.1463 -0.0033 -0.0115 -0.0430 26  GLU A N   
203  C  CA  . GLU A 26  ? 0.1472 0.2798 0.1268 -0.0232 -0.0083 -0.0469 26  GLU A CA  
204  C  C   . GLU A 26  ? 0.1515 0.2045 0.1309 -0.0030 -0.0115 -0.0095 26  GLU A C   
205  O  O   . GLU A 26  ? 0.1831 0.2190 0.1283 -0.0262 -0.0088 0.0133  26  GLU A O   
206  C  CB  . GLU A 26  ? 0.1838 0.3272 0.1618 -0.0722 0.0058  -0.0933 26  GLU A CB  
207  C  CG  . GLU A 26  ? 0.2251 0.3808 0.2163 -0.0304 -0.0631 -0.0396 26  GLU A CG  
208  C  CD  . GLU A 26  ? 0.2763 0.4488 0.3121 -0.0018 -0.0721 0.0245  26  GLU A CD  
209  O  OE1 . GLU A 26  ? 0.3998 0.5906 0.3041 -0.0988 -0.0930 0.0354  26  GLU A OE1 
210  O  OE2 . GLU A 26  ? 0.3128 0.5478 0.5682 0.1358  -0.0750 -0.0405 26  GLU A OE2 
211  N  N   . ARG A 27  ? 0.1436 0.1363 0.1147 -0.0065 -0.0188 -0.0205 27  ARG A N   
212  C  CA  . ARG A 27  ? 0.1482 0.1359 0.1275 -0.0108 -0.0151 -0.0172 27  ARG A CA  
213  C  C   . ARG A 27  ? 0.1181 0.1201 0.1201 -0.0110 -0.0181 -0.0063 27  ARG A C   
214  O  O   . ARG A 27  ? 0.1262 0.1366 0.1371 0.0134  -0.0129 -0.0042 27  ARG A O   
215  C  CB  . ARG A 27  ? 0.1899 0.1360 0.1526 0.0051  -0.0132 -0.0283 27  ARG A CB  
216  C  CG  . ARG A 27  ? 0.1870 0.1544 0.1443 0.0029  0.0023  -0.0200 27  ARG A CG  
217  C  CD  . ARG A 27  ? 0.2224 0.1622 0.1470 0.0073  -0.0124 -0.0072 27  ARG A CD  
218  N  NE  . ARG A 27  ? 0.2273 0.1220 0.1303 0.0047  -0.0051 -0.0102 27  ARG A NE  
219  C  CZ  . ARG A 27  ? 0.1937 0.1298 0.1525 0.0110  0.0053  -0.0054 27  ARG A CZ  
220  N  NH1 . ARG A 27  ? 0.2357 0.1647 0.2036 0.0309  0.0034  -0.0520 27  ARG A NH1 
221  N  NH2 . ARG A 27  ? 0.1806 0.1540 0.1948 -0.0016 -0.0003 -0.0305 27  ARG A NH2 
222  N  N   . GLN A 28  ? 0.1183 0.1178 0.1082 -0.0082 -0.0013 -0.0099 28  GLN A N   
223  C  CA  . GLN A 28  ? 0.1292 0.0967 0.1212 -0.0011 -0.0015 -0.0179 28  GLN A CA  
224  C  C   . GLN A 28  ? 0.1190 0.0973 0.1005 0.0069  -0.0076 0.0106  28  GLN A C   
225  O  O   . GLN A 28  ? 0.1459 0.1336 0.1050 -0.0193 -0.0033 0.0095  28  GLN A O   
226  C  CB  . GLN A 28  ? 0.1214 0.1165 0.1628 0.0040  0.0046  -0.0110 28  GLN A CB  
227  C  CG  . GLN A 28  ? 0.1280 0.1339 0.1276 -0.0201 -0.0051 -0.0072 28  GLN A CG  
228  C  CD  . GLN A 28  ? 0.1320 0.1298 0.1181 -0.0148 -0.0064 -0.0116 28  GLN A CD  
229  O  OE1 . GLN A 28  ? 0.1309 0.1238 0.1389 -0.0223 -0.0032 -0.0027 28  GLN A OE1 
230  N  NE2 . GLN A 28  ? 0.1045 0.1201 0.1655 -0.0039 -0.0076 -0.0124 28  GLN A NE2 
231  N  N   . SER A 29  ? 0.1224 0.0993 0.1029 0.0040  -0.0082 -0.0012 29  SER A N   
232  C  CA  . SER A 29  ? 0.1133 0.0813 0.1279 0.0032  -0.0023 -0.0110 29  SER A CA  
233  C  C   . SER A 29  ? 0.0996 0.1012 0.1002 0.0050  -0.0018 0.0078  29  SER A C   
234  O  O   . SER A 29  ? 0.1122 0.1250 0.1125 0.0054  0.0132  -0.0100 29  SER A O   
235  C  CB  . SER A 29  ? 0.1192 0.0937 0.1172 0.0167  -0.0016 -0.0170 29  SER A CB  
236  O  OG  . SER A 29  ? 0.1208 0.0946 0.1266 0.0027  0.0058  -0.0144 29  SER A OG  
237  N  N   . PRO A 30  ? 0.1180 0.0905 0.1119 0.0050  0.0000  0.0059  30  PRO A N   
238  C  CA  . PRO A 30  ? 0.1190 0.1020 0.1009 -0.0094 -0.0040 0.0013  30  PRO A CA  
239  C  C   . PRO A 30  ? 0.1231 0.0851 0.1104 0.0075  -0.0080 -0.0050 30  PRO A C   
240  O  O   . PRO A 30  ? 0.1170 0.1083 0.1321 0.0072  -0.0136 -0.0016 30  PRO A O   
241  C  CB  . PRO A 30  ? 0.1213 0.1201 0.1075 0.0158  -0.0067 -0.0313 30  PRO A CB  
242  C  CG  . PRO A 30  ? 0.1146 0.0982 0.1252 0.0004  0.0151  -0.0034 30  PRO A CG  
243  C  CD  . PRO A 30  ? 0.1295 0.0885 0.1276 0.0110  0.0102  -0.0109 30  PRO A CD  
244  N  N   . VAL A 31  ? 0.1252 0.0935 0.1065 0.0052  0.0023  0.0025  31  VAL A N   
245  C  CA  . VAL A 31  ? 0.1460 0.1063 0.1003 0.0115  0.0087  0.0048  31  VAL A CA  
246  C  C   . VAL A 31  ? 0.1302 0.1090 0.1244 0.0185  -0.0046 0.0033  31  VAL A C   
247  O  O   . VAL A 31  ? 0.1300 0.1061 0.1373 -0.0006 -0.0044 0.0221  31  VAL A O   
248  C  CB  . VAL A 31  ? 0.1478 0.1286 0.1018 0.0068  0.0067  -0.0060 31  VAL A CB  
249  C  CG1 . VAL A 31  ? 0.1769 0.1141 0.1438 -0.0040 0.0002  -0.0179 31  VAL A CG1 
250  C  CG2 . VAL A 31  ? 0.1551 0.1126 0.1560 0.0105  0.0136  -0.0098 31  VAL A CG2 
251  N  N   . ASP A 32  ? 0.1526 0.1029 0.1333 0.0042  -0.0074 0.0206  32  ASP A N   
252  C  CA  . ASP A 32  ? 0.1558 0.0973 0.1353 0.0037  0.0023  0.0197  32  ASP A CA  
253  C  C   . ASP A 32  ? 0.1643 0.1436 0.1005 0.0177  0.0026  0.0168  32  ASP A C   
254  O  O   . ASP A 32  ? 0.1626 0.1820 0.1214 0.0062  -0.0006 -0.0158 32  ASP A O   
255  C  CB  . ASP A 32  ? 0.1669 0.1172 0.1475 0.0133  0.0023  0.0264  32  ASP A CB  
256  C  CG  . ASP A 32  ? 0.1686 0.1215 0.1641 0.0178  -0.0025 0.0281  32  ASP A CG  
257  O  OD1 . ASP A 32  ? 0.1860 0.1212 0.1539 0.0037  -0.0034 0.0208  32  ASP A OD1 
258  O  OD2 . ASP A 32  ? 0.2952 0.1499 0.1759 -0.0172 -0.0059 0.0317  32  ASP A OD2 
259  N  N   . ILE A 33  ? 0.1429 0.1253 0.1297 0.0136  0.0030  -0.0032 33  ILE A N   
260  C  CA  . ILE A 33  ? 0.1450 0.1294 0.1331 0.0099  0.0040  0.0176  33  ILE A CA  
261  C  C   . ILE A 33  ? 0.1802 0.1099 0.1268 0.0129  0.0261  -0.0009 33  ILE A C   
262  O  O   . ILE A 33  ? 0.1977 0.1160 0.1502 0.0111  0.0120  0.0000  33  ILE A O   
263  C  CB  . ILE A 33  ? 0.1413 0.1212 0.1407 0.0130  0.0171  0.0136  33  ILE A CB  
264  C  CG1 . ILE A 33  ? 0.1400 0.1317 0.1533 -0.0070 -0.0039 0.0314  33  ILE A CG1 
265  C  CG2 . ILE A 33  ? 0.1630 0.1614 0.1664 0.0187  0.0356  0.0059  33  ILE A CG2 
266  C  CD1 . ILE A 33  ? 0.1612 0.1644 0.1676 0.0049  -0.0122 0.0433  33  ILE A CD1 
267  N  N   A ASP A 34  ? 0.2096 0.1080 0.1307 0.0236  0.0148  0.0176  34  ASP A N   
268  N  N   B ASP A 34  ? 0.2111 0.1467 0.1161 0.0047  0.0392  0.0150  34  ASP A N   
269  C  CA  A ASP A 34  ? 0.2499 0.1686 0.1239 0.0249  0.0162  0.0488  34  ASP A CA  
270  C  CA  B ASP A 34  ? 0.2226 0.1568 0.1226 0.0136  0.0321  0.0225  34  ASP A CA  
271  C  C   A ASP A 34  ? 0.2441 0.1443 0.1720 0.0392  0.0254  0.0230  34  ASP A C   
272  C  C   B ASP A 34  ? 0.2226 0.1820 0.1158 0.0447  0.0336  0.0194  34  ASP A C   
273  O  O   A ASP A 34  ? 0.2599 0.1673 0.2078 0.0035  0.0361  0.0066  34  ASP A O   
274  O  O   B ASP A 34  ? 0.2477 0.1842 0.0903 0.0631  0.0445  0.0465  34  ASP A O   
275  C  CB  A ASP A 34  ? 0.2988 0.1254 0.1429 0.0584  -0.0196 0.0184  34  ASP A CB  
276  C  CB  B ASP A 34  ? 0.2346 0.2023 0.1278 0.0339  0.0214  0.0329  34  ASP A CB  
277  C  CG  A ASP A 34  ? 0.2945 0.1805 0.1980 0.0267  0.0400  0.0523  34  ASP A CG  
278  C  CG  B ASP A 34  ? 0.2294 0.2741 0.1504 0.0340  0.0369  0.0672  34  ASP A CG  
279  O  OD1 A ASP A 34  ? 0.3801 0.2160 0.2273 0.1261  0.0270  0.0905  34  ASP A OD1 
280  O  OD1 B ASP A 34  ? 0.2226 0.3352 0.1367 0.0391  0.0047  0.0789  34  ASP A OD1 
281  O  OD2 A ASP A 34  ? 0.3620 0.1751 0.1932 0.0163  0.0361  0.0239  34  ASP A OD2 
282  O  OD2 B ASP A 34  ? 0.3052 0.3123 0.2402 0.0048  -0.0370 0.1065  34  ASP A OD2 
283  N  N   . THR A 35  ? 0.2170 0.1813 0.1234 0.0479  0.0161  0.0383  35  THR A N   
284  C  CA  . THR A 35  ? 0.2438 0.1921 0.1522 0.0621  0.0386  0.0629  35  THR A CA  
285  C  C   . THR A 35  ? 0.2311 0.1743 0.1586 0.0460  0.0466  0.0692  35  THR A C   
286  O  O   . THR A 35  ? 0.2626 0.2271 0.1756 0.0798  0.0385  0.0398  35  THR A O   
287  C  CB  . THR A 35  ? 0.2103 0.2341 0.1944 0.0299  0.0326  0.0518  35  THR A CB  
288  O  OG1 . THR A 35  ? 0.2463 0.1966 0.2214 0.0145  0.0450  0.0546  35  THR A OG1 
289  C  CG2 . THR A 35  ? 0.2853 0.2714 0.1531 0.0787  0.0315  0.0416  35  THR A CG2 
290  N  N   . HIS A 36  ? 0.2982 0.1993 0.1328 0.0781  0.0576  0.0560  36  HIS A N   
291  C  CA  . HIS A 36  ? 0.3370 0.1978 0.1215 0.0541  0.0379  0.0746  36  HIS A CA  
292  C  C   . HIS A 36  ? 0.2968 0.3156 0.1321 0.0168  -0.0065 0.0137  36  HIS A C   
293  O  O   . HIS A 36  ? 0.3467 0.3617 0.1517 0.0693  0.0052  0.0030  36  HIS A O   
294  C  CB  . HIS A 36  ? 0.3525 0.2145 0.1525 0.0276  0.0343  0.1050  36  HIS A CB  
295  C  CG  . HIS A 36  ? 0.5116 0.1867 0.2249 0.0141  0.0003  0.0340  36  HIS A CG  
296  N  ND1 . HIS A 36  ? 0.5455 0.2066 0.2365 -0.0995 -0.0499 0.0462  36  HIS A ND1 
297  C  CD2 . HIS A 36  ? 0.4474 0.3165 0.2548 0.0631  -0.1257 -0.0252 36  HIS A CD2 
298  C  CE1 . HIS A 36  ? 0.4811 0.2468 0.2244 -0.0728 -0.0807 0.0230  36  HIS A CE1 
299  N  NE2 . HIS A 36  ? 0.5075 0.2361 0.3464 0.0531  -0.0221 -0.0069 36  HIS A NE2 
300  N  N   . THR A 37  ? 0.3129 0.2179 0.1813 0.0876  0.0179  0.0000  37  THR A N   
301  C  CA  . THR A 37  ? 0.3586 0.1876 0.1587 0.0639  -0.0040 0.0556  37  THR A CA  
302  C  C   . THR A 37  ? 0.2928 0.1993 0.1594 0.0766  -0.0055 0.0343  37  THR A C   
303  O  O   . THR A 37  ? 0.4279 0.2172 0.2060 0.0779  -0.0357 0.0055  37  THR A O   
304  C  CB  . THR A 37  ? 0.3307 0.2916 0.3973 0.0562  -0.1008 0.0296  37  THR A CB  
305  O  OG1 . THR A 37  ? 0.4532 0.3419 0.4738 0.1056  -0.0497 0.0653  37  THR A OG1 
306  C  CG2 . THR A 37  ? 0.3745 0.3430 0.3492 0.0655  -0.0841 0.0985  37  THR A CG2 
307  N  N   . ALA A 38  ? 0.2659 0.1854 0.1418 0.0593  0.0061  0.0380  38  ALA A N   
308  C  CA  . ALA A 38  ? 0.2483 0.1662 0.1353 0.0562  0.0257  0.0396  38  ALA A CA  
309  C  C   . ALA A 38  ? 0.2744 0.2043 0.2401 0.0375  0.0662  0.0438  38  ALA A C   
310  O  O   . ALA A 38  ? 0.3861 0.1946 0.4622 0.0350  0.2260  0.0082  38  ALA A O   
311  C  CB  . ALA A 38  ? 0.2483 0.1770 0.1447 0.0554  0.0018  0.0311  38  ALA A CB  
312  N  N   . LYS A 39  ? 0.2573 0.2350 0.1587 0.0760  0.0013  -0.0055 39  LYS A N   
313  C  CA  . LYS A 39  ? 0.3158 0.3768 0.1982 0.1963  0.0356  0.0121  39  LYS A CA  
314  C  C   . LYS A 39  ? 0.2425 0.3348 0.1233 0.1130  0.0655  0.0152  39  LYS A C   
315  O  O   . LYS A 39  ? 0.2109 0.2974 0.1156 0.0773  -0.0010 0.0205  39  LYS A O   
316  C  CB  . LYS A 39  ? 0.4707 0.5396 0.3829 0.1341  -0.0527 -0.1882 39  LYS A CB  
317  C  CG  . LYS A 39  ? 0.7490 0.6072 0.5017 -0.0088 -0.0688 -0.0836 39  LYS A CG  
318  C  CD  . LYS A 39  ? 0.3468 0.4793 0.3559 -0.1193 -0.0723 0.1377  39  LYS A CD  
319  C  CE  . LYS A 39  ? 0.2594 0.5730 0.2948 0.0804  -0.0160 0.0784  39  LYS A CE  
320  N  NZ  . LYS A 39  ? 0.4735 0.5294 0.5519 0.1657  -0.2060 -0.0336 39  LYS A NZ  
321  N  N   . TYR A 40  ? 0.2896 0.2797 0.1493 0.0593  0.0284  0.0155  40  TYR A N   
322  C  CA  . TYR A 40  ? 0.2469 0.2477 0.1521 0.0183  0.0151  0.0179  40  TYR A CA  
323  C  C   . TYR A 40  ? 0.2609 0.2606 0.1329 0.0489  0.0266  0.0115  40  TYR A C   
324  O  O   . TYR A 40  ? 0.2761 0.3366 0.1324 0.0824  0.0029  0.0030  40  TYR A O   
325  C  CB  . TYR A 40  ? 0.2943 0.3246 0.2240 -0.0321 0.0672  0.0757  40  TYR A CB  
326  C  CG  . TYR A 40  ? 0.2829 0.3379 0.1877 -0.0194 0.0629  0.0337  40  TYR A CG  
327  C  CD1 . TYR A 40  ? 0.2425 0.3154 0.1932 -0.0628 0.0070  -0.0019 40  TYR A CD1 
328  C  CD2 . TYR A 40  ? 0.3503 0.4465 0.2947 -0.0358 0.1382  -0.0057 40  TYR A CD2 
329  C  CE1 . TYR A 40  ? 0.2305 0.4835 0.2071 -0.0345 -0.0013 -0.0204 40  TYR A CE1 
330  C  CE2 . TYR A 40  ? 0.4048 0.4890 0.1892 0.0281  0.1341  -0.0060 40  TYR A CE2 
331  C  CZ  . TYR A 40  ? 0.2452 0.7300 0.2322 0.0414  0.0111  -0.0027 40  TYR A CZ  
332  O  OH  . TYR A 40  ? 0.2283 0.8207 0.3484 0.1340  0.0776  -0.0290 40  TYR A OH  
333  N  N   . ASP A 41  ? 0.1981 0.2381 0.1605 0.0384  0.0328  0.0044  41  ASP A N   
334  C  CA  . ASP A 41  ? 0.2370 0.2165 0.1927 0.0038  -0.0519 0.0037  41  ASP A CA  
335  C  C   . ASP A 41  ? 0.2823 0.3204 0.1495 0.0883  -0.0079 -0.0143 41  ASP A C   
336  O  O   . ASP A 41  ? 0.2190 0.2618 0.1827 0.0430  -0.0111 -0.0178 41  ASP A O   
337  C  CB  . ASP A 41  ? 0.3208 0.2168 0.2317 -0.0384 -0.0566 -0.0210 41  ASP A CB  
338  C  CG  . ASP A 41  ? 0.3953 0.2056 0.3007 -0.0423 -0.0935 -0.0370 41  ASP A CG  
339  O  OD1 . ASP A 41  ? 0.4951 0.3007 0.2531 0.0401  -0.0826 -0.0899 41  ASP A OD1 
340  O  OD2 . ASP A 41  ? 0.4599 0.3103 0.3721 -0.1505 -0.1172 0.0451  41  ASP A OD2 
341  N  N   . PRO A 42  ? 0.2505 0.4637 0.2020 0.0850  0.0171  0.0071  42  PRO A N   
342  C  CA  . PRO A 42  ? 0.2603 0.5007 0.3215 0.1106  0.0403  0.1185  42  PRO A CA  
343  C  C   . PRO A 42  ? 0.3522 0.4284 0.2745 0.1021  0.0643  0.0208  42  PRO A C   
344  O  O   . PRO A 42  ? 0.3358 0.5956 0.4149 0.1707  0.0374  0.0516  42  PRO A O   
345  C  CB  . PRO A 42  ? 0.3162 0.6329 0.3434 0.0524  0.1381  -0.0006 42  PRO A CB  
346  C  CG  . PRO A 42  ? 0.3727 0.7562 0.2850 0.1932  0.1621  0.0410  42  PRO A CG  
347  C  CD  . PRO A 42  ? 0.3095 0.4639 0.2200 0.1337  0.0866  0.0876  42  PRO A CD  
348  N  N   . SER A 43  ? 0.3458 0.3904 0.2225 0.1384  0.0669  -0.0249 43  SER A N   
349  C  CA  . SER A 43  ? 0.5543 0.3640 0.2384 0.1177  -0.0135 -0.0208 43  SER A CA  
350  C  C   . SER A 43  ? 0.3819 0.2803 0.2532 0.1318  -0.0243 -0.0129 43  SER A C   
351  O  O   . SER A 43  ? 0.5492 0.2812 0.4294 0.1582  -0.0770 -0.0013 43  SER A O   
352  C  CB  . SER A 43  ? 0.6196 0.4361 0.3294 0.0872  -0.0955 -0.0647 43  SER A CB  
353  O  OG  . SER A 43  ? 0.6021 0.4559 0.2886 -0.0861 -0.1082 -0.0531 43  SER A OG  
354  N  N   . LEU A 44  ? 0.3805 0.2717 0.2138 0.1091  -0.0268 0.0004  44  LEU A N   
355  C  CA  . LEU A 44  ? 0.2953 0.3183 0.2186 0.0727  -0.0550 0.0058  44  LEU A CA  
356  C  C   . LEU A 44  ? 0.2548 0.3881 0.3116 -0.0013 -0.0370 0.0706  44  LEU A C   
357  O  O   . LEU A 44  ? 0.2477 0.5480 0.2965 -0.0556 -0.0087 0.1293  44  LEU A O   
358  C  CB  . LEU A 44  ? 0.2370 0.3458 0.2064 -0.0099 -0.0352 -0.0381 44  LEU A CB  
359  C  CG  . LEU A 44  ? 0.2311 0.3118 0.2181 -0.0076 -0.0069 0.0164  44  LEU A CG  
360  C  CD1 . LEU A 44  ? 0.2789 0.3033 0.1891 -0.0054 -0.0179 -0.0034 44  LEU A CD1 
361  C  CD2 . LEU A 44  ? 0.2785 0.2440 0.2655 -0.0219 -0.0365 0.0181  44  LEU A CD2 
362  N  N   . LYS A 45  ? 0.2779 0.3169 0.2637 -0.0070 -0.0820 0.0023  45  LYS A N   
363  C  CA  . LYS A 45  ? 0.2667 0.2495 0.3320 -0.0317 -0.0863 -0.0065 45  LYS A CA  
364  C  C   . LYS A 45  ? 0.2244 0.3414 0.1955 0.0663  -0.0031 0.0133  45  LYS A C   
365  O  O   . LYS A 45  ? 0.1985 0.3032 0.2899 0.0006  0.0201  -0.0208 45  LYS A O   
366  C  CB  . LYS A 45  ? 0.2787 0.2248 0.3250 0.0480  0.0029  -0.0431 45  LYS A CB  
367  C  CG  . LYS A 45  ? 0.4206 0.3021 0.3204 0.0305  -0.0649 -0.0866 45  LYS A CG  
368  C  CD  . LYS A 45  ? 0.4903 0.3072 0.5493 -0.0449 0.1311  0.0144  45  LYS A CD  
369  N  N   . PRO A 46  ? 0.2071 0.3177 0.2341 -0.0588 0.0043  0.0041  46  PRO A N   
370  C  CA  . PRO A 46  ? 0.1863 0.3299 0.2151 -0.0562 -0.0025 0.0019  46  PRO A CA  
371  C  C   . PRO A 46  ? 0.1999 0.2254 0.1902 0.0047  0.0147  0.0126  46  PRO A C   
372  O  O   . PRO A 46  ? 0.1781 0.2585 0.2256 -0.0052 0.0006  0.0168  46  PRO A O   
373  C  CB  . PRO A 46  ? 0.1910 0.3136 0.2754 -0.0359 -0.0147 -0.0240 46  PRO A CB  
374  C  CG  . PRO A 46  ? 0.1974 0.4192 0.3173 0.0076  0.0269  -0.0996 46  PRO A CG  
375  C  CD  . PRO A 46  ? 0.2724 0.3877 0.2296 0.0313  -0.0333 -0.0279 46  PRO A CD  
376  N  N   . LEU A 47  ? 0.1881 0.2438 0.2373 -0.0147 -0.0105 0.0118  47  LEU A N   
377  C  CA  . LEU A 47  ? 0.1571 0.2337 0.1928 -0.0221 0.0003  -0.0126 47  LEU A CA  
378  C  C   . LEU A 47  ? 0.1463 0.2362 0.2986 -0.0400 -0.0445 0.0196  47  LEU A C   
379  O  O   . LEU A 47  ? 0.1659 0.2343 0.3657 -0.0325 -0.0551 0.0270  47  LEU A O   
380  C  CB  . LEU A 47  ? 0.2115 0.2570 0.3935 0.0097  -0.0270 -0.0370 47  LEU A CB  
381  C  CG  . LEU A 47  ? 0.1312 0.3234 0.4772 -0.0293 -0.0594 -0.0869 47  LEU A CG  
382  C  CD1 . LEU A 47  ? 0.1873 0.3834 0.4806 -0.0678 -0.0769 -0.1506 47  LEU A CD1 
383  C  CD2 . LEU A 47  ? 0.2025 0.3830 0.4397 0.0181  -0.0972 -0.1954 47  LEU A CD2 
384  N  N   . SER A 48  ? 0.1518 0.2145 0.1787 -0.0272 -0.0174 -0.0061 48  SER A N   
385  C  CA  . SER A 48  ? 0.1791 0.2455 0.1328 -0.0044 -0.0012 -0.0329 48  SER A CA  
386  C  C   . SER A 48  ? 0.1465 0.2246 0.1562 -0.0185 -0.0019 -0.0044 48  SER A C   
387  O  O   . SER A 48  ? 0.1684 0.2134 0.2221 -0.0389 0.0181  -0.0397 48  SER A O   
388  C  CB  . SER A 48  ? 0.2188 0.2296 0.2154 -0.0076 -0.0024 -0.0328 48  SER A CB  
389  O  OG  . SER A 48  ? 0.2604 0.3339 0.2651 0.0622  0.0307  0.0149  48  SER A OG  
390  N  N   . VAL A 49  ? 0.1987 0.3084 0.1291 -0.0769 -0.0042 -0.0047 49  VAL A N   
391  C  CA  . VAL A 49  ? 0.2643 0.2354 0.1447 -0.0675 0.0223  -0.0466 49  VAL A CA  
392  C  C   . VAL A 49  ? 0.2423 0.3071 0.1725 -0.1045 -0.0149 -0.0175 49  VAL A C   
393  O  O   . VAL A 49  ? 0.2970 0.4901 0.2255 -0.2118 -0.0132 0.0071  49  VAL A O   
394  C  CB  . VAL A 49  ? 0.3308 0.2531 0.2027 -0.0861 0.0534  -0.0783 49  VAL A CB  
395  C  CG1 . VAL A 49  ? 0.6038 0.3185 0.2673 -0.1122 0.1708  -0.0258 49  VAL A CG1 
396  C  CG2 . VAL A 49  ? 0.2764 0.2573 0.3082 -0.0581 0.0791  -0.0467 49  VAL A CG2 
397  N  N   . SER A 50  ? 0.2023 0.2902 0.1564 -0.0702 0.0137  -0.0290 50  SER A N   
398  C  CA  . SER A 50  ? 0.1725 0.2924 0.2164 -0.0579 -0.0003 -0.0540 50  SER A CA  
399  C  C   . SER A 50  ? 0.1282 0.2608 0.2168 -0.0186 0.0003  -0.0439 50  SER A C   
400  O  O   . SER A 50  ? 0.1686 0.2480 0.1975 -0.0200 -0.0173 -0.0152 50  SER A O   
401  C  CB  . SER A 50  ? 0.2321 0.3177 0.2810 -0.0089 0.0716  -0.0629 50  SER A CB  
402  O  OG  . SER A 50  ? 0.2802 0.3667 0.2952 -0.0369 0.0240  -0.0697 50  SER A OG  
403  N  N   . TYR A 51  ? 0.1610 0.2790 0.2110 -0.0210 -0.0026 -0.0652 51  TYR A N   
404  C  CA  . TYR A 51  ? 0.1903 0.2170 0.1884 -0.0155 0.0054  -0.0483 51  TYR A CA  
405  C  C   . TYR A 51  ? 0.1662 0.2497 0.2125 -0.0167 0.0076  -0.0145 51  TYR A C   
406  O  O   . TYR A 51  ? 0.1696 0.2138 0.2150 0.0006  -0.0249 -0.0003 51  TYR A O   
407  C  CB  . TYR A 51  ? 0.1590 0.2230 0.2018 -0.0161 -0.0172 -0.0334 51  TYR A CB  
408  C  CG  . TYR A 51  ? 0.1508 0.1966 0.1514 -0.0487 0.0117  -0.0093 51  TYR A CG  
409  C  CD1 . TYR A 51  ? 0.1434 0.1854 0.2125 -0.0129 -0.0173 -0.0325 51  TYR A CD1 
410  C  CD2 . TYR A 51  ? 0.1583 0.1723 0.1759 -0.0395 -0.0054 -0.0022 51  TYR A CD2 
411  C  CE1 . TYR A 51  ? 0.1748 0.1614 0.1614 -0.0179 -0.0107 0.0042  51  TYR A CE1 
412  C  CE2 . TYR A 51  ? 0.1680 0.1684 0.1669 -0.0491 -0.0149 -0.0179 51  TYR A CE2 
413  C  CZ  . TYR A 51  ? 0.1709 0.1411 0.1682 -0.0480 -0.0200 0.0030  51  TYR A CZ  
414  O  OH  . TYR A 51  ? 0.1626 0.1644 0.1872 -0.0165 -0.0242 -0.0274 51  TYR A OH  
415  N  N   . ASP A 52  ? 0.1468 0.2621 0.2585 -0.0108 0.0038  -0.0018 52  ASP A N   
416  C  CA  . ASP A 52  ? 0.1571 0.2682 0.2872 -0.0194 0.0132  0.0829  52  ASP A CA  
417  C  C   . ASP A 52  ? 0.1657 0.2450 0.2513 0.0139  -0.0206 0.0272  52  ASP A C   
418  O  O   . ASP A 52  ? 0.2611 0.2825 0.2490 -0.0058 -0.0556 0.0537  52  ASP A O   
419  C  CB  . ASP A 52  ? 0.1765 0.4038 0.3448 0.0153  0.0397  0.0704  52  ASP A CB  
420  C  CG  . ASP A 52  ? 0.3879 0.5157 0.7218 -0.0788 0.1726  -0.0480 52  ASP A CG  
421  O  OD1 . ASP A 52  ? 0.3885 0.8143 0.8777 -0.0241 0.0961  -0.2653 52  ASP A OD1 
422  O  OD2 . ASP A 52  ? 0.6944 0.7868 1.0570 0.0571  0.1885  0.2224  52  ASP A OD2 
423  N  N   . GLN A 53  ? 0.1398 0.1996 0.3047 0.0118  0.0340  0.0080  53  GLN A N   
424  C  CA  . GLN A 53  ? 0.1744 0.1892 0.2088 0.0184  0.0377  -0.0077 53  GLN A CA  
425  C  C   . GLN A 53  ? 0.1856 0.1705 0.1597 0.0252  0.0072  0.0022  53  GLN A C   
426  O  O   . GLN A 53  ? 0.1863 0.1917 0.1910 0.0348  0.0011  0.0241  53  GLN A O   
427  C  CB  . GLN A 53  ? 0.2082 0.2089 0.2194 0.0795  0.0299  -0.0258 53  GLN A CB  
428  C  CG  . GLN A 53  ? 0.2146 0.2949 0.2969 0.0745  0.0562  -0.0688 53  GLN A CG  
429  C  CD  . GLN A 53  ? 0.2323 0.3881 0.3441 0.0075  0.0370  0.0482  53  GLN A CD  
430  O  OE1 . GLN A 53  ? 0.2830 0.4328 0.5753 -0.0542 0.0798  0.0498  53  GLN A OE1 
431  N  NE2 . GLN A 53  ? 0.2091 0.2366 0.3021 0.0436  -0.0058 0.0234  53  GLN A NE2 
432  N  N   . ALA A 54  ? 0.1664 0.1745 0.1880 0.0262  0.0163  0.0047  54  ALA A N   
433  C  CA  . ALA A 54  ? 0.1574 0.1439 0.1680 0.0192  0.0083  -0.0069 54  ALA A CA  
434  C  C   . ALA A 54  ? 0.1727 0.1547 0.1704 0.0144  0.0003  -0.0181 54  ALA A C   
435  O  O   . ALA A 54  ? 0.1704 0.2197 0.1647 -0.0039 0.0043  -0.0343 54  ALA A O   
436  C  CB  . ALA A 54  ? 0.1745 0.1553 0.2237 0.0194  0.0152  0.0160  54  ALA A CB  
437  N  N   . THR A 55  ? 0.1646 0.1316 0.1705 0.0378  0.0186  -0.0072 55  THR A N   
438  C  CA  . THR A 55  ? 0.1737 0.1264 0.1524 0.0458  0.0039  0.0102  55  THR A CA  
439  C  C   . THR A 55  ? 0.1565 0.1046 0.1221 0.0223  -0.0153 0.0055  55  THR A C   
440  O  O   . THR A 55  ? 0.1726 0.1023 0.1439 0.0091  -0.0190 0.0029  55  THR A O   
441  C  CB  . THR A 55  ? 0.1745 0.1450 0.1867 0.0414  -0.0055 0.0251  55  THR A CB  
442  O  OG1 . THR A 55  ? 0.1863 0.1747 0.2298 0.0409  0.0062  -0.0074 55  THR A OG1 
443  C  CG2 . THR A 55  ? 0.2316 0.1705 0.2021 0.0126  -0.0346 0.0497  55  THR A CG2 
444  N  N   . SER A 56  ? 0.1417 0.1021 0.1216 0.0089  0.0010  0.0091  56  SER A N   
445  C  CA  . SER A 56  ? 0.1428 0.0964 0.1129 0.0094  0.0118  -0.0027 56  SER A CA  
446  C  C   . SER A 56  ? 0.1402 0.1018 0.1167 0.0069  -0.0130 0.0156  56  SER A C   
447  O  O   . SER A 56  ? 0.1483 0.1234 0.1342 0.0138  -0.0234 0.0209  56  SER A O   
448  C  CB  . SER A 56  ? 0.1648 0.1000 0.1206 0.0001  -0.0149 0.0119  56  SER A CB  
449  O  OG  . SER A 56  ? 0.1436 0.1036 0.1485 0.0021  -0.0182 0.0043  56  SER A OG  
450  N  N   . LEU A 57  ? 0.1382 0.1002 0.1346 0.0036  0.0208  0.0068  57  LEU A N   
451  C  CA  . LEU A 57  ? 0.1640 0.0916 0.1268 0.0023  0.0296  0.0102  57  LEU A CA  
452  C  C   . LEU A 57  ? 0.1425 0.0980 0.1122 0.0032  0.0120  0.0216  57  LEU A C   
453  O  O   . LEU A 57  ? 0.1873 0.1160 0.1169 0.0091  0.0034  0.0157  57  LEU A O   
454  C  CB  . LEU A 57  ? 0.1702 0.1061 0.1521 0.0037  0.0273  -0.0036 57  LEU A CB  
455  C  CG  . LEU A 57  ? 0.2014 0.1067 0.1791 0.0155  0.0086  -0.0115 57  LEU A CG  
456  C  CD1 . LEU A 57  ? 0.2197 0.1282 0.2425 -0.0178 0.0401  -0.0469 57  LEU A CD1 
457  C  CD2 . LEU A 57  ? 0.2775 0.1280 0.2530 0.0468  -0.0250 0.0190  57  LEU A CD2 
458  N  N   . ARG A 58  ? 0.1363 0.0976 0.1336 0.0019  0.0047  0.0208  58  ARG A N   
459  C  CA  . ARG A 58  ? 0.1355 0.0905 0.1350 0.0008  0.0152  0.0168  58  ARG A CA  
460  C  C   . ARG A 58  ? 0.1493 0.1052 0.1090 0.0070  0.0021  0.0129  58  ARG A C   
461  O  O   . ARG A 58  ? 0.1840 0.1241 0.1068 0.0264  0.0067  0.0034  58  ARG A O   
462  C  CB  . ARG A 58  ? 0.1684 0.1011 0.1849 -0.0051 0.0350  0.0253  58  ARG A CB  
463  C  CG  . ARG A 58  ? 0.2189 0.1146 0.2640 -0.0274 0.0446  0.0577  58  ARG A CG  
464  C  CD  . ARG A 58  ? 0.2315 0.1201 0.2788 -0.0212 0.0898  0.0359  58  ARG A CD  
465  N  NE  . ARG A 58  ? 0.2346 0.1508 0.2164 -0.0321 0.0424  0.0223  58  ARG A NE  
466  C  CZ  . ARG A 58  ? 0.2560 0.1623 0.2163 -0.0268 0.0521  0.0691  58  ARG A CZ  
467  N  NH1 . ARG A 58  ? 0.2915 0.1987 0.2671 0.0347  0.0526  0.0873  58  ARG A NH1 
468  N  NH2 . ARG A 58  ? 0.2488 0.1819 0.2211 -0.0088 0.0458  0.0359  58  ARG A NH2 
469  N  N   . ILE A 59  ? 0.1265 0.0932 0.1263 0.0063  0.0011  0.0086  59  ILE A N   
470  C  CA  . ILE A 59  ? 0.1302 0.0926 0.1235 0.0049  0.0106  0.0187  59  ILE A CA  
471  C  C   . ILE A 59  ? 0.1431 0.1101 0.1041 0.0140  0.0054  0.0048  59  ILE A C   
472  O  O   . ILE A 59  ? 0.1362 0.1450 0.1067 0.0061  0.0005  0.0171  59  ILE A O   
473  C  CB  . ILE A 59  ? 0.1617 0.1011 0.1000 -0.0041 -0.0027 0.0209  59  ILE A CB  
474  C  CG1 . ILE A 59  ? 0.1902 0.0980 0.1167 0.0001  -0.0043 0.0287  59  ILE A CG1 
475  C  CG2 . ILE A 59  ? 0.1686 0.1282 0.0971 0.0046  0.0017  0.0118  59  ILE A CG2 
476  C  CD1 . ILE A 59  ? 0.2057 0.0937 0.1745 0.0087  -0.0011 0.0211  59  ILE A CD1 
477  N  N   A LEU A 60  ? 0.1350 0.1450 0.1147 0.0155  0.0006  0.0008  60  LEU A N   
478  N  N   B LEU A 60  ? 0.1393 0.1074 0.1239 0.0093  0.0012  0.0170  60  LEU A N   
479  C  CA  A LEU A 60  ? 0.1375 0.1110 0.0953 0.0034  0.0043  0.0087  60  LEU A CA  
480  C  CA  B LEU A 60  ? 0.1366 0.1025 0.1770 0.0051  0.0038  0.0036  60  LEU A CA  
481  C  C   A LEU A 60  ? 0.1102 0.1256 0.1331 0.0159  0.0078  0.0119  60  LEU A C   
482  C  C   B LEU A 60  ? 0.1388 0.1163 0.0597 -0.0008 -0.0146 -0.0212 60  LEU A C   
483  O  O   A LEU A 60  ? 0.1229 0.1307 0.1214 0.0003  0.0116  -0.0188 60  LEU A O   
484  O  O   B LEU A 60  ? 0.1212 0.1346 0.0874 -0.0033 -0.0072 0.0049  60  LEU A O   
485  C  CB  A LEU A 60  ? 0.1375 0.1474 0.1679 -0.0531 0.0097  -0.0050 60  LEU A CB  
486  C  CB  B LEU A 60  ? 0.1905 0.1093 0.2064 -0.0186 -0.0137 0.0179  60  LEU A CB  
487  C  CG  A LEU A 60  ? 0.1536 0.1082 0.1914 -0.0300 0.0142  -0.0018 60  LEU A CG  
488  C  CG  B LEU A 60  ? 0.2588 0.0785 0.2039 0.0334  -0.0150 0.0238  60  LEU A CG  
489  C  CD1 A LEU A 60  ? 0.2018 0.1536 0.2007 0.0049  0.0094  0.0512  60  LEU A CD1 
490  C  CD1 B LEU A 60  ? 0.2481 0.1409 0.2025 -0.0282 0.0139  0.0130  60  LEU A CD1 
491  C  CD2 A LEU A 60  ? 0.1648 0.1032 0.2570 0.0055  -0.0632 -0.0044 60  LEU A CD2 
492  C  CD2 B LEU A 60  ? 0.3492 0.3574 0.2519 -0.0143 0.0269  0.0061  60  LEU A CD2 
493  N  N   . ASN A 61  ? 0.1208 0.1070 0.1235 0.0060  0.0082  -0.0082 61  ASN A N   
494  C  CA  . ASN A 61  ? 0.1117 0.1050 0.1328 -0.0019 0.0135  0.0019  61  ASN A CA  
495  C  C   . ASN A 61  ? 0.1119 0.1061 0.1156 0.0027  0.0024  0.0039  61  ASN A C   
496  O  O   . ASN A 61  ? 0.1382 0.1286 0.1360 -0.0032 0.0164  0.0077  61  ASN A O   
497  C  CB  . ASN A 61  ? 0.1400 0.1059 0.1393 0.0192  0.0163  0.0018  61  ASN A CB  
498  C  CG  . ASN A 61  ? 0.1392 0.1099 0.1385 0.0157  0.0037  0.0015  61  ASN A CG  
499  O  OD1 . ASN A 61  ? 0.1432 0.1280 0.1605 0.0105  -0.0087 -0.0082 61  ASN A OD1 
500  N  ND2 . ASN A 61  ? 0.1493 0.1104 0.1449 0.0122  0.0120  -0.0048 61  ASN A ND2 
501  N  N   . ASN A 62  ? 0.1405 0.1132 0.1158 -0.0227 -0.0035 0.0118  62  ASN A N   
502  C  CA  . ASN A 62  ? 0.1407 0.1254 0.1421 -0.0227 0.0040  -0.0048 62  ASN A CA  
503  C  C   . ASN A 62  ? 0.1612 0.1407 0.1190 -0.0013 0.0120  0.0037  62  ASN A C   
504  O  O   . ASN A 62  ? 0.1557 0.1813 0.2084 -0.0283 -0.0024 -0.0233 62  ASN A O   
505  C  CB  . ASN A 62  ? 0.1856 0.1497 0.1478 -0.0253 -0.0023 -0.0100 62  ASN A CB  
506  C  CG  . ASN A 62  ? 0.2059 0.1514 0.1155 0.0073  -0.0183 -0.0141 62  ASN A CG  
507  O  OD1 . ASN A 62  ? 0.1617 0.1467 0.1382 -0.0059 0.0128  -0.0089 62  ASN A OD1 
508  N  ND2 . ASN A 62  ? 0.3533 0.2379 0.1646 0.0376  0.0465  -0.0267 62  ASN A ND2 
509  N  N   . GLY A 63  ? 0.1485 0.1350 0.1623 0.0026  0.0008  0.0108  63  GLY A N   
510  C  CA  . GLY A 63  ? 0.1500 0.1775 0.1478 0.0184  0.0127  0.0144  63  GLY A CA  
511  C  C   . GLY A 63  ? 0.1644 0.1228 0.1446 0.0109  0.0039  0.0027  63  GLY A C   
512  O  O   . GLY A 63  ? 0.1826 0.1659 0.1877 0.0384  -0.0077 0.0058  63  GLY A O   
513  N  N   . HIS A 64  ? 0.1313 0.1629 0.1318 -0.0305 -0.0083 0.0167  64  HIS A N   
514  C  CA  . HIS A 64  ? 0.1550 0.1957 0.1327 -0.0199 0.0019  0.0160  64  HIS A CA  
515  C  C   . HIS A 64  ? 0.1319 0.1183 0.1766 -0.0104 -0.0044 0.0271  64  HIS A C   
516  O  O   . HIS A 64  ? 0.1596 0.1758 0.2919 -0.0179 -0.0469 0.0968  64  HIS A O   
517  C  CB  . HIS A 64  ? 0.1586 0.1988 0.1615 -0.0221 -0.0167 -0.0054 64  HIS A CB  
518  C  CG  . HIS A 64  ? 0.1854 0.1862 0.1405 -0.0284 -0.0320 -0.0050 64  HIS A CG  
519  N  ND1 . HIS A 64  ? 0.2269 0.2563 0.2192 -0.0296 -0.0247 0.0081  64  HIS A ND1 
520  C  CD2 . HIS A 64  ? 0.1734 0.2451 0.1643 -0.0299 -0.0406 0.0129  64  HIS A CD2 
521  C  CE1 . HIS A 64  ? 0.1921 0.2433 0.2172 -0.0476 0.0136  -0.0011 64  HIS A CE1 
522  N  NE2 . HIS A 64  ? 0.1852 0.3096 0.2568 -0.0522 0.0015  -0.0170 64  HIS A NE2 
523  N  N   . SER A 65  ? 0.1298 0.1303 0.1389 -0.0086 -0.0037 0.0230  65  SER A N   
524  C  CA  . SER A 65  ? 0.1246 0.1331 0.1377 -0.0093 -0.0047 0.0178  65  SER A CA  
525  C  C   . SER A 65  ? 0.1298 0.1221 0.0996 0.0034  0.0092  -0.0073 65  SER A C   
526  O  O   . SER A 65  ? 0.1350 0.1529 0.1268 0.0153  0.0022  0.0163  65  SER A O   
527  C  CB  . SER A 65  ? 0.1575 0.2139 0.1201 -0.0381 0.0000  0.0414  65  SER A CB  
528  O  OG  . SER A 65  ? 0.1759 0.2533 0.1630 -0.0126 -0.0084 0.0584  65  SER A OG  
529  N  N   . PHE A 66  ? 0.1288 0.1234 0.1321 0.0198  -0.0177 0.0020  66  PHE A N   
530  C  CA  . PHE A 66  ? 0.1284 0.1707 0.1089 0.0412  0.0006  -0.0034 66  PHE A CA  
531  C  C   . PHE A 66  ? 0.1177 0.1439 0.1132 0.0159  0.0026  -0.0086 66  PHE A C   
532  O  O   . PHE A 66  ? 0.1456 0.1416 0.1163 0.0151  0.0115  0.0005  66  PHE A O   
533  C  CB  . PHE A 66  ? 0.1607 0.1507 0.1197 0.0212  -0.0131 -0.0085 66  PHE A CB  
534  C  CG  . PHE A 66  ? 0.1532 0.1447 0.1109 0.0179  -0.0189 -0.0203 66  PHE A CG  
535  C  CD1 . PHE A 66  ? 0.1349 0.1542 0.1531 0.0046  -0.0304 -0.0218 66  PHE A CD1 
536  C  CD2 . PHE A 66  ? 0.1655 0.1289 0.1518 0.0178  -0.0248 -0.0328 66  PHE A CD2 
537  C  CE1 . PHE A 66  ? 0.1535 0.1475 0.1881 0.0063  -0.0350 0.0143  66  PHE A CE1 
538  C  CE2 . PHE A 66  ? 0.1906 0.1206 0.1709 0.0122  -0.0254 -0.0245 66  PHE A CE2 
539  C  CZ  . PHE A 66  ? 0.1869 0.1328 0.1671 0.0154  -0.0330 -0.0297 66  PHE A CZ  
540  N  N   . LYS A 67  ? 0.1508 0.1542 0.1124 0.0529  0.0095  0.0142  67  LYS A N   
541  C  CA  . LYS A 67  ? 0.1377 0.1565 0.1197 0.0439  -0.0089 -0.0030 67  LYS A CA  
542  C  C   . LYS A 67  ? 0.1554 0.1335 0.0935 0.0394  -0.0064 -0.0022 67  LYS A C   
543  O  O   . LYS A 67  ? 0.1399 0.2078 0.0995 0.0414  0.0072  0.0145  67  LYS A O   
544  C  CB  . LYS A 67  ? 0.2370 0.1862 0.1946 0.0206  -0.0759 0.0012  67  LYS A CB  
545  C  CG  . LYS A 67  ? 0.2711 0.2344 0.2788 0.0035  -0.0729 0.0164  67  LYS A CG  
546  C  CD  . LYS A 67  ? 0.2790 0.1935 0.3938 -0.0629 -0.1024 -0.0194 67  LYS A CD  
547  C  CE  . LYS A 67  ? 0.3413 0.2664 0.5511 -0.0314 -0.0617 0.0110  67  LYS A CE  
548  N  NZ  . LYS A 67  ? 0.4608 0.3003 0.8341 0.0788  -0.1847 -0.2675 67  LYS A NZ  
549  N  N   . VAL A 68  ? 0.1461 0.0933 0.1122 0.0205  0.0081  0.0087  68  VAL A N   
550  C  CA  . VAL A 68  ? 0.1402 0.0811 0.1300 0.0128  0.0039  0.0059  68  VAL A CA  
551  C  C   . VAL A 68  ? 0.1413 0.0873 0.1129 0.0124  0.0103  0.0179  68  VAL A C   
552  O  O   . VAL A 68  ? 0.1581 0.0919 0.1122 0.0079  0.0022  0.0155  68  VAL A O   
553  C  CB  . VAL A 68  ? 0.1442 0.0898 0.1405 0.0057  0.0160  -0.0016 68  VAL A CB  
554  C  CG1 . VAL A 68  ? 0.1465 0.1257 0.1413 0.0152  0.0015  0.0009  68  VAL A CG1 
555  C  CG2 . VAL A 68  ? 0.1539 0.1039 0.1417 -0.0037 0.0154  -0.0030 68  VAL A CG2 
556  N  N   . GLU A 69  ? 0.1332 0.0858 0.1286 0.0084  0.0043  0.0173  69  GLU A N   
557  C  CA  . GLU A 69  ? 0.1389 0.0917 0.1249 0.0093  -0.0011 0.0141  69  GLU A CA  
558  C  C   . GLU A 69  ? 0.1436 0.0869 0.1136 0.0152  -0.0099 0.0210  69  GLU A C   
559  O  O   . GLU A 69  ? 0.1697 0.1226 0.1324 0.0406  -0.0309 0.0061  69  GLU A O   
560  C  CB  . GLU A 69  ? 0.1528 0.0989 0.2363 -0.0051 0.0385  0.0196  69  GLU A CB  
561  C  CG  . GLU A 69  ? 0.1636 0.2049 0.2620 -0.0022 0.0436  0.0265  69  GLU A CG  
562  C  CD  . GLU A 69  ? 0.2279 0.1971 0.2089 -0.0473 0.0458  0.0250  69  GLU A CD  
563  O  OE1 . GLU A 69  ? 0.2078 0.2236 0.2203 -0.0122 0.0424  0.0420  69  GLU A OE1 
564  O  OE2 . GLU A 69  ? 0.2942 0.3543 0.3113 -0.0749 0.0079  -0.0344 69  GLU A OE2 
565  N  N   . PHE A 70  ? 0.1360 0.0885 0.1321 0.0134  0.0032  0.0033  70  PHE A N   
566  C  CA  . PHE A 70  ? 0.1382 0.0948 0.1344 0.0154  0.0005  0.0055  70  PHE A CA  
567  C  C   . PHE A 70  ? 0.1447 0.1048 0.1411 -0.0050 -0.0049 -0.0017 70  PHE A C   
568  O  O   . PHE A 70  ? 0.1592 0.0983 0.1951 0.0087  -0.0161 -0.0052 70  PHE A O   
569  C  CB  . PHE A 70  ? 0.1529 0.1040 0.1221 0.0020  -0.0057 0.0078  70  PHE A CB  
570  C  CG  . PHE A 70  ? 0.1544 0.0946 0.1214 0.0187  0.0005  0.0089  70  PHE A CG  
571  C  CD1 . PHE A 70  ? 0.1817 0.0876 0.1301 0.0199  0.0292  0.0227  70  PHE A CD1 
572  C  CD2 . PHE A 70  ? 0.1571 0.1230 0.1213 -0.0025 0.0070  0.0120  70  PHE A CD2 
573  C  CE1 . PHE A 70  ? 0.1824 0.0996 0.1852 0.0152  0.0340  0.0287  70  PHE A CE1 
574  C  CE2 . PHE A 70  ? 0.1779 0.1040 0.1400 0.0057  0.0247  0.0223  70  PHE A CE2 
575  C  CZ  . PHE A 70  ? 0.1808 0.1170 0.1428 0.0054  0.0344  0.0102  70  PHE A CZ  
576  N  N   . ASP A 71  ? 0.1687 0.0966 0.1470 0.0140  -0.0095 -0.0044 71  ASP A N   
577  C  CA  . ASP A 71  ? 0.1759 0.0873 0.1718 0.0122  -0.0012 0.0105  71  ASP A CA  
578  C  C   . ASP A 71  ? 0.1675 0.0811 0.1820 -0.0140 0.0193  0.0100  71  ASP A C   
579  O  O   . ASP A 71  ? 0.1969 0.1655 0.2059 -0.0324 0.0326  -0.0266 71  ASP A O   
580  C  CB  . ASP A 71  ? 0.2028 0.1183 0.2097 0.0223  -0.0499 0.0080  71  ASP A CB  
581  C  CG  . ASP A 71  ? 0.2286 0.1427 0.2750 0.0125  -0.0836 -0.0006 71  ASP A CG  
582  O  OD1 . ASP A 71  ? 0.2513 0.1156 0.2158 0.0326  -0.0356 0.0050  71  ASP A OD1 
583  O  OD2 . ASP A 71  ? 0.3258 0.1845 0.3333 0.0331  -0.1102 0.0026  71  ASP A OD2 
584  N  N   . ASP A 72  ? 0.1831 0.0985 0.1495 -0.0015 -0.0063 0.0179  72  ASP A N   
585  C  CA  . ASP A 72  ? 0.2049 0.0847 0.1641 -0.0175 -0.0105 0.0093  72  ASP A CA  
586  C  C   . ASP A 72  ? 0.2201 0.0910 0.1937 -0.0027 -0.0153 0.0275  72  ASP A C   
587  O  O   . ASP A 72  ? 0.2732 0.1059 0.1934 0.0088  -0.0146 0.0087  72  ASP A O   
588  C  CB  . ASP A 72  ? 0.2176 0.0955 0.1400 0.0208  -0.0033 0.0181  72  ASP A CB  
589  C  CG  . ASP A 72  ? 0.2309 0.1062 0.1781 -0.0144 -0.0188 0.0087  72  ASP A CG  
590  O  OD1 . ASP A 72  ? 0.2323 0.1425 0.1971 -0.0231 -0.0306 0.0336  72  ASP A OD1 
591  O  OD2 . ASP A 72  ? 0.2557 0.1752 0.1867 0.0048  -0.0527 0.0335  72  ASP A OD2 
592  N  N   . SER A 73  ? 0.2328 0.0941 0.2009 0.0201  -0.0234 0.0179  73  SER A N   
593  C  CA  . SER A 73  ? 0.2944 0.0991 0.1880 -0.0196 -0.0650 0.0100  73  SER A CA  
594  C  C   . SER A 73  ? 0.3604 0.0748 0.2382 0.0288  -0.0476 -0.0073 73  SER A C   
595  O  O   . SER A 73  ? 0.4368 0.0862 0.2412 0.0221  -0.0978 -0.0147 73  SER A O   
596  C  CB  . SER A 73  ? 0.3782 0.1364 0.1953 -0.0489 -0.0807 0.0436  73  SER A CB  
597  O  OG  . SER A 73  ? 0.3044 0.0991 0.2106 0.0254  -0.0240 0.0198  73  SER A OG  
598  N  N   . GLN A 74  ? 0.2789 0.1313 0.2791 0.0295  0.0030  -0.0122 74  GLN A N   
599  C  CA  . GLN A 74  ? 0.3587 0.1741 0.2806 0.1152  0.0361  -0.0185 74  GLN A CA  
600  C  C   . GLN A 74  ? 0.2899 0.2081 0.1880 0.0145  -0.0660 -0.0770 74  GLN A C   
601  O  O   . GLN A 74  ? 0.2304 0.1781 0.2408 0.0019  -0.0324 -0.0183 74  GLN A O   
602  C  CB  . GLN A 74  ? 0.3278 0.5248 0.4381 0.1964  0.0272  0.1249  74  GLN A CB  
603  C  CG  . GLN A 74  ? 0.6883 0.4260 0.5794 -0.0818 0.0992  0.1011  74  GLN A CG  
604  C  CD  . GLN A 74  ? 0.4162 0.5577 0.8340 -0.1288 -0.0135 -0.0505 74  GLN A CD  
605  O  OE1 . GLN A 74  ? 0.3540 0.3626 0.6001 0.0323  -0.1106 0.1400  74  GLN A OE1 
606  N  NE2 . GLN A 74  ? 0.3646 0.3389 0.5103 -0.1357 -0.2039 0.2164  74  GLN A NE2 
607  N  N   . ASP A 75  ? 0.3509 0.3075 0.3222 -0.0661 0.0348  -0.1029 75  ASP A N   
608  C  CA  . ASP A 75  ? 0.3219 0.3466 0.4421 -0.1725 -0.0771 -0.0544 75  ASP A CA  
609  C  C   . ASP A 75  ? 0.2225 0.3076 0.3647 0.0033  -0.1027 -0.1223 75  ASP A C   
610  O  O   . ASP A 75  ? 0.3927 0.1852 0.6388 0.0558  -0.2141 0.0064  75  ASP A O   
611  C  CB  . ASP A 75  ? 0.2988 0.8801 0.8527 0.2492  0.1300  -0.2050 75  ASP A CB  
612  C  CG  . ASP A 75  ? 0.4079 0.5655 0.6714 0.3021  0.1812  0.0248  75  ASP A CG  
613  O  OD1 . ASP A 75  ? 0.6621 0.9558 0.4476 0.3062  0.0201  -0.0911 75  ASP A OD1 
614  O  OD2 . ASP A 75  ? 0.5482 0.4451 0.9118 -0.0021 0.3491  -0.0864 75  ASP A OD2 
615  N  N   . LYS A 76  ? 0.2219 0.2400 0.2922 0.0105  -0.0583 0.0576  76  LYS A N   
616  C  CA  . LYS A 76  ? 0.2761 0.1492 0.4737 -0.0170 0.0080  -0.0120 76  LYS A CA  
617  C  C   . LYS A 76  ? 0.5047 0.3518 0.5488 0.2104  0.0598  0.1772  76  LYS A C   
618  O  O   . LYS A 76  ? 0.2251 0.7723 0.5837 -0.0047 0.0015  -0.0374 76  LYS A O   
619  C  CB  . LYS A 76  ? 0.3960 0.2265 0.3447 0.0813  -0.1870 -0.0093 76  LYS A CB  
620  C  CG  . LYS A 76  ? 0.5932 0.2136 0.3116 -0.0974 0.0406  -0.0292 76  LYS A CG  
621  C  CD  . LYS A 76  ? 0.3598 0.1906 0.2498 -0.0813 -0.0477 -0.0057 76  LYS A CD  
622  C  CE  . LYS A 76  ? 0.5088 0.4321 0.4518 0.1297  -0.2228 -0.0067 76  LYS A CE  
623  N  NZ  . LYS A 76  ? 0.6073 0.1576 0.4596 -0.0539 -0.1859 -0.0804 76  LYS A NZ  
624  N  N   . ALA A 77  ? 0.2287 0.2720 0.3473 0.0566  -0.1053 0.0750  77  ALA A N   
625  C  CA  . ALA A 77  ? 0.1970 0.1865 0.1993 0.0477  -0.0412 0.0082  77  ALA A CA  
626  C  C   . ALA A 77  ? 0.1691 0.1381 0.2470 0.0302  -0.0425 -0.0199 77  ALA A C   
627  O  O   . ALA A 77  ? 0.1556 0.2359 0.3609 0.0281  -0.0341 -0.0817 77  ALA A O   
628  C  CB  . ALA A 77  ? 0.2606 0.1737 0.2383 0.0283  -0.0249 -0.0241 77  ALA A CB  
629  N  N   . VAL A 78  ? 0.1931 0.1575 0.1855 -0.0076 -0.0381 0.0072  78  VAL A N   
630  C  CA  . VAL A 78  ? 0.2358 0.1590 0.2157 -0.0197 -0.0719 0.0105  78  VAL A CA  
631  C  C   . VAL A 78  ? 0.1917 0.1273 0.2000 -0.0176 -0.0523 -0.0214 78  VAL A C   
632  O  O   . VAL A 78  ? 0.1914 0.1592 0.2973 -0.0351 -0.0787 0.0067  78  VAL A O   
633  C  CB  . VAL A 78  ? 0.2694 0.2283 0.2129 0.0135  -0.0326 -0.0080 78  VAL A CB  
634  C  CG1 . VAL A 78  ? 0.4264 0.0977 0.3529 0.0017  -0.0829 -0.0051 78  VAL A CG1 
635  C  CG2 . VAL A 78  ? 0.2809 0.1795 0.3759 0.0126  0.0935  -0.0477 78  VAL A CG2 
636  N  N   . LEU A 79  ? 0.1704 0.1386 0.1691 -0.0054 -0.0303 -0.0091 79  LEU A N   
637  C  CA  . LEU A 79  ? 0.1689 0.1503 0.1712 -0.0135 0.0102  -0.0148 79  LEU A CA  
638  C  C   . LEU A 79  ? 0.1837 0.1743 0.1641 -0.0128 -0.0067 -0.0203 79  LEU A C   
639  O  O   . LEU A 79  ? 0.2312 0.2108 0.1959 -0.0662 0.0264  -0.0561 79  LEU A O   
640  C  CB  . LEU A 79  ? 0.1732 0.2176 0.2315 0.0030  -0.0255 0.0460  79  LEU A CB  
641  C  CG  . LEU A 79  ? 0.2032 0.2000 0.1955 0.0052  0.0002  0.0135  79  LEU A CG  
642  C  CD1 . LEU A 79  ? 0.1903 0.2006 0.4841 -0.0256 0.0523  0.0425  79  LEU A CD1 
643  C  CD2 . LEU A 79  ? 0.2067 0.1920 0.2194 0.0354  0.0226  -0.0057 79  LEU A CD2 
644  N  N   . LYS A 80  ? 0.1970 0.2326 0.1569 -0.0227 0.0022  -0.0170 80  LYS A N   
645  C  CA  . LYS A 80  ? 0.2751 0.2077 0.1826 -0.0210 0.0275  -0.0261 80  LYS A CA  
646  C  C   . LYS A 80  ? 0.2034 0.2190 0.1916 -0.0253 0.0342  -0.0291 80  LYS A C   
647  O  O   . LYS A 80  ? 0.2002 0.2228 0.2181 -0.0445 -0.0106 -0.0287 80  LYS A O   
648  C  CB  . LYS A 80  ? 0.3218 0.2196 0.3598 -0.0059 0.0176  -0.0054 80  LYS A CB  
649  C  CG  . LYS A 80  ? 0.3421 0.2604 0.4111 0.0605  -0.0271 -0.0620 80  LYS A CG  
650  C  CD  . LYS A 80  ? 0.3371 0.2473 0.6621 0.0172  -0.0763 0.0150  80  LYS A CD  
651  N  N   . GLY A 81  ? 0.2400 0.2352 0.2063 -0.0055 0.0384  -0.0457 81  GLY A N   
652  C  CA  . GLY A 81  ? 0.2164 0.2231 0.2522 0.0260  0.0248  -0.0100 81  GLY A CA  
653  C  C   . GLY A 81  ? 0.1729 0.1964 0.2766 0.0012  0.0418  -0.0234 81  GLY A C   
654  O  O   . GLY A 81  ? 0.1700 0.2542 0.2172 -0.0340 0.0136  -0.0414 81  GLY A O   
655  N  N   . GLY A 82  ? 0.1953 0.1820 0.3993 0.0055  0.0403  0.0134  82  GLY A N   
656  C  CA  . GLY A 82  ? 0.1989 0.1975 0.4405 0.0220  0.0228  0.0130  82  GLY A CA  
657  C  C   . GLY A 82  ? 0.2179 0.2473 0.3017 0.0756  0.0217  0.0239  82  GLY A C   
658  O  O   . GLY A 82  ? 0.3017 0.3761 0.3318 0.0996  0.1279  0.0340  82  GLY A O   
659  N  N   . PRO A 83  ? 0.1980 0.1795 0.3138 0.0307  0.0567  0.0065  83  PRO A N   
660  C  CA  . PRO A 83  ? 0.2340 0.1996 0.2674 0.0460  0.0387  0.0009  83  PRO A CA  
661  C  C   . PRO A 83  ? 0.1989 0.2091 0.2371 0.0379  0.0157  -0.0308 83  PRO A C   
662  O  O   . PRO A 83  ? 0.3029 0.2964 0.2757 -0.0019 -0.0601 0.0011  83  PRO A O   
663  C  CB  . PRO A 83  ? 0.2000 0.2898 0.2136 0.0480  0.0139  -0.0044 83  PRO A CB  
664  C  CG  . PRO A 83  ? 0.1998 0.2107 0.2212 0.0489  -0.0003 0.0008  83  PRO A CG  
665  C  CD  . PRO A 83  ? 0.1842 0.1665 0.3344 0.0348  0.0288  -0.0259 83  PRO A CD  
666  N  N   . LEU A 84  ? 0.1734 0.1657 0.2280 0.0263  0.0372  -0.0313 84  LEU A N   
667  C  CA  . LEU A 84  ? 0.1723 0.1528 0.2194 0.0220  -0.0027 -0.0597 84  LEU A CA  
668  C  C   . LEU A 84  ? 0.1862 0.1714 0.2237 0.0210  -0.0044 -0.0638 84  LEU A C   
669  O  O   . LEU A 84  ? 0.1935 0.1993 0.2958 0.0200  0.0208  -0.0807 84  LEU A O   
670  C  CB  . LEU A 84  ? 0.1849 0.1291 0.1975 0.0283  0.0218  -0.0295 84  LEU A CB  
671  C  CG  . LEU A 84  ? 0.1529 0.1456 0.1971 0.0302  0.0188  -0.0422 84  LEU A CG  
672  C  CD1 . LEU A 84  ? 0.2274 0.1916 0.1824 0.0185  0.0081  -0.0453 84  LEU A CD1 
673  C  CD2 . LEU A 84  ? 0.1576 0.1557 0.2370 0.0036  0.0341  -0.0491 84  LEU A CD2 
674  N  N   . ASP A 85  ? 0.2592 0.1529 0.3187 -0.0087 0.0556  -0.1091 85  ASP A N   
675  C  CA  . ASP A 85  ? 0.2952 0.1319 0.3825 0.0060  0.0266  -0.0813 85  ASP A CA  
676  C  C   . ASP A 85  ? 0.2887 0.1277 0.4864 0.0193  0.0807  -0.0357 85  ASP A C   
677  O  O   . ASP A 85  ? 0.3409 0.3374 0.3978 0.0670  0.0630  -0.0597 85  ASP A O   
678  C  CB  . ASP A 85  ? 0.4064 0.3592 0.3579 0.0133  -0.1110 0.0357  85  ASP A CB  
679  C  CG  . ASP A 85  ? 0.6366 0.6799 0.4910 -0.0364 -0.0290 0.0846  85  ASP A CG  
680  O  OD1 . ASP A 85  ? 0.7218 0.8565 0.2077 -0.1276 0.0251  -0.0315 85  ASP A OD1 
681  O  OD2 . ASP A 85  ? 0.4301 0.5000 1.0290 -0.0314 -0.0557 -0.2249 85  ASP A OD2 
682  N  N   . GLY A 86  ? 0.2724 0.3034 0.4809 -0.0127 0.0556  -0.0167 86  GLY A N   
683  C  CA  . GLY A 86  ? 0.3402 0.2407 0.3672 -0.1133 0.0823  -0.0818 86  GLY A CA  
684  C  C   . GLY A 86  ? 0.2681 0.2011 0.3380 -0.0553 -0.0731 -0.0293 86  GLY A C   
685  O  O   . GLY A 86  ? 0.3653 0.2706 0.3623 -0.1341 -0.0438 0.0109  86  GLY A O   
686  N  N   . THR A 87  ? 0.2437 0.2034 0.2772 0.0555  -0.0098 -0.0752 87  THR A N   
687  C  CA  . THR A 87  ? 0.1797 0.2102 0.2894 -0.0137 0.0400  -0.1001 87  THR A CA  
688  C  C   . THR A 87  ? 0.1558 0.1249 0.3177 0.0132  0.0114  -0.0597 87  THR A C   
689  O  O   . THR A 87  ? 0.1859 0.1129 0.3215 0.0128  0.0010  -0.0634 87  THR A O   
690  C  CB  . THR A 87  ? 0.4291 0.4818 0.2442 0.0512  -0.0530 0.0443  87  THR A CB  
691  O  OG1 . THR A 87  ? 0.5630 0.5677 0.4615 -0.0401 -0.1085 0.0097  87  THR A OG1 
692  C  CG2 . THR A 87  ? 0.2989 0.3404 0.3740 0.0582  0.0048  0.0013  87  THR A CG2 
693  N  N   . TYR A 88  ? 0.1594 0.1266 0.2706 0.0119  0.0051  -0.0527 88  TYR A N   
694  C  CA  . TYR A 88  ? 0.1496 0.1405 0.2121 0.0115  -0.0188 -0.0390 88  TYR A CA  
695  C  C   . TYR A 88  ? 0.1496 0.1138 0.2287 0.0164  -0.0342 -0.0388 88  TYR A C   
696  O  O   . TYR A 88  ? 0.2131 0.1948 0.2809 -0.0581 -0.0825 0.0205  88  TYR A O   
697  C  CB  . TYR A 88  ? 0.1672 0.1283 0.2104 0.0451  -0.0106 -0.0543 88  TYR A CB  
698  C  CG  . TYR A 88  ? 0.1619 0.0912 0.1984 0.0057  0.0075  -0.0386 88  TYR A CG  
699  C  CD1 . TYR A 88  ? 0.1651 0.1207 0.1987 0.0068  -0.0051 -0.0514 88  TYR A CD1 
700  C  CD2 . TYR A 88  ? 0.1580 0.0870 0.1852 0.0128  0.0040  -0.0189 88  TYR A CD2 
701  C  CE1 . TYR A 88  ? 0.1673 0.1129 0.1883 0.0034  -0.0089 -0.0289 88  TYR A CE1 
702  C  CE2 . TYR A 88  ? 0.1644 0.0876 0.1826 0.0113  -0.0087 -0.0351 88  TYR A CE2 
703  C  CZ  . TYR A 88  ? 0.1641 0.0937 0.1763 0.0054  -0.0144 -0.0480 88  TYR A CZ  
704  O  OH  . TYR A 88  ? 0.1730 0.1583 0.1673 0.0023  0.0033  -0.0446 88  TYR A OH  
705  N  N   A ARG A 89  ? 0.1536 0.1669 0.1974 0.0399  -0.0117 -0.0770 89  ARG A N   
706  N  N   B ARG A 89  ? 0.1532 0.0876 0.2264 0.0477  -0.0298 -0.0529 89  ARG A N   
707  C  CA  A ARG A 89  ? 0.1194 0.1068 0.1895 0.0232  -0.0305 0.0009  89  ARG A CA  
708  C  CA  B ARG A 89  ? 0.1858 0.0761 0.2046 0.0300  -0.0376 -0.0278 89  ARG A CA  
709  C  C   A ARG A 89  ? 0.1243 0.0772 0.1786 -0.0012 -0.0092 0.0046  89  ARG A C   
710  C  C   B ARG A 89  ? 0.1486 0.0881 0.1416 0.0340  -0.0400 -0.0077 89  ARG A C   
711  O  O   A ARG A 89  ? 0.1297 0.1009 0.1425 0.0074  -0.0207 0.0055  89  ARG A O   
712  O  O   B ARG A 89  ? 0.1489 0.0757 0.1364 0.0048  -0.0270 -0.0016 89  ARG A O   
713  C  CB  A ARG A 89  ? 0.1956 0.1082 0.2300 0.0102  0.0346  0.0041  89  ARG A CB  
714  C  CB  B ARG A 89  ? 0.1311 0.1183 0.1743 -0.0024 -0.0410 0.0184  89  ARG A CB  
715  C  CG  A ARG A 89  ? 0.1874 0.1330 0.2125 0.0212  0.0268  0.0217  89  ARG A CG  
716  C  CG  B ARG A 89  ? 0.2580 0.0700 0.1357 0.0271  -0.0355 0.0093  89  ARG A CG  
717  C  CD  A ARG A 89  ? 0.2043 0.0673 0.1955 0.0121  -0.0064 0.0054  89  ARG A CD  
718  C  CD  B ARG A 89  ? 0.2368 0.0779 0.1465 0.0264  -0.0233 0.0212  89  ARG A CD  
719  N  NE  A ARG A 89  ? 0.2153 0.0851 0.2050 0.0381  -0.0438 0.0000  89  ARG A NE  
720  N  NE  B ARG A 89  ? 0.2588 0.0694 0.1596 -0.0149 -0.0234 0.0067  89  ARG A NE  
721  C  CZ  A ARG A 89  ? 0.2332 0.1065 0.1650 0.0013  -0.0076 -0.0085 89  ARG A CZ  
722  C  CZ  B ARG A 89  ? 0.2183 0.0627 0.1500 -0.0111 -0.0185 -0.0064 89  ARG A CZ  
723  N  NH1 A ARG A 89  ? 0.2532 0.1235 0.1629 -0.0511 -0.0003 0.0422  89  ARG A NH1 
724  N  NH1 B ARG A 89  ? 0.2327 0.0901 0.1766 0.0109  0.0083  0.0248  89  ARG A NH1 
725  N  NH2 A ARG A 89  ? 0.3265 0.1070 0.2637 0.0416  -0.0414 -0.0287 89  ARG A NH2 
726  N  NH2 B ARG A 89  ? 0.2476 0.0612 0.1824 0.0065  0.0103  -0.0008 89  ARG A NH2 
727  N  N   . LEU A 90  ? 0.1515 0.0797 0.1393 0.0108  -0.0143 -0.0074 90  LEU A N   
728  C  CA  . LEU A 90  ? 0.1392 0.0826 0.1425 0.0156  -0.0100 0.0049  90  LEU A CA  
729  C  C   . LEU A 90  ? 0.1450 0.0993 0.1425 -0.0032 -0.0160 0.0148  90  LEU A C   
730  O  O   . LEU A 90  ? 0.1791 0.1192 0.1615 0.0027  -0.0241 0.0318  90  LEU A O   
731  C  CB  . LEU A 90  ? 0.1514 0.0979 0.1439 0.0086  -0.0229 -0.0194 90  LEU A CB  
732  C  CG  . LEU A 90  ? 0.1607 0.0883 0.1393 -0.0022 -0.0002 0.0016  90  LEU A CG  
733  C  CD1 . LEU A 90  ? 0.1826 0.0837 0.1411 0.0091  0.0066  0.0068  90  LEU A CD1 
734  C  CD2 . LEU A 90  ? 0.1939 0.1468 0.1368 -0.0341 -0.0114 -0.0129 90  LEU A CD2 
735  N  N   . THR A 91  ? 0.1514 0.0761 0.1371 0.0033  0.0040  -0.0145 91  THR A N   
736  C  CA  . THR A 91  ? 0.1705 0.0898 0.1268 -0.0051 -0.0067 -0.0049 91  THR A CA  
737  C  C   . THR A 91  ? 0.1626 0.0756 0.1241 0.0111  -0.0111 0.0070  91  THR A C   
738  O  O   . THR A 91  ? 0.1622 0.0982 0.1205 0.0036  -0.0167 0.0227  91  THR A O   
739  C  CB  . THR A 91  ? 0.1802 0.1180 0.1546 -0.0335 -0.0194 0.0063  91  THR A CB  
740  O  OG1 . THR A 91  ? 0.2408 0.2071 0.1716 -0.0967 -0.0270 0.0375  91  THR A OG1 
741  C  CG2 . THR A 91  ? 0.1880 0.1027 0.1838 -0.0095 -0.0337 -0.0046 91  THR A CG2 
742  N  N   . GLN A 92  ? 0.1424 0.0650 0.1341 0.0022  -0.0011 0.0048  92  GLN A N   
743  C  CA  . GLN A 92  ? 0.1486 0.0633 0.1197 0.0070  0.0181  0.0087  92  GLN A CA  
744  C  C   . GLN A 92  ? 0.1425 0.0743 0.1025 0.0070  -0.0054 0.0143  92  GLN A C   
745  O  O   . GLN A 92  ? 0.1650 0.0775 0.0996 0.0113  0.0027  0.0004  92  GLN A O   
746  C  CB  . GLN A 92  ? 0.1465 0.1215 0.1199 0.0054  0.0176  0.0035  92  GLN A CB  
747  C  CG  . GLN A 92  ? 0.1852 0.1490 0.1357 0.0139  -0.0038 -0.0106 92  GLN A CG  
748  C  CD  . GLN A 92  ? 0.2733 0.1054 0.1752 -0.0025 -0.0367 0.0033  92  GLN A CD  
749  O  OE1 . GLN A 92  ? 0.3632 0.1235 0.1944 0.0234  -0.1003 0.0168  92  GLN A OE1 
750  N  NE2 . GLN A 92  ? 0.2228 0.3265 0.3013 0.0496  -0.0433 -0.0425 92  GLN A NE2 
751  N  N   . PHE A 93  ? 0.1231 0.0560 0.1275 0.0000  -0.0068 0.0072  93  PHE A N   
752  C  CA  . PHE A 93  ? 0.1241 0.0538 0.1393 0.0079  0.0072  0.0106  93  PHE A CA  
753  C  C   . PHE A 93  ? 0.1284 0.0734 0.0964 0.0065  -0.0110 0.0042  93  PHE A C   
754  O  O   . PHE A 93  ? 0.1465 0.0818 0.0942 0.0148  -0.0002 0.0117  93  PHE A O   
755  C  CB  . PHE A 93  ? 0.1194 0.0826 0.1032 0.0076  -0.0006 0.0081  93  PHE A CB  
756  C  CG  . PHE A 93  ? 0.1183 0.0777 0.1286 -0.0004 0.0040  0.0172  93  PHE A CG  
757  C  CD1 . PHE A 93  ? 0.1226 0.0826 0.1389 0.0022  0.0031  0.0075  93  PHE A CD1 
758  C  CD2 . PHE A 93  ? 0.1165 0.1020 0.1196 0.0037  -0.0016 0.0264  93  PHE A CD2 
759  C  CE1 . PHE A 93  ? 0.1522 0.0925 0.1256 0.0002  -0.0125 0.0031  93  PHE A CE1 
760  C  CE2 . PHE A 93  ? 0.1265 0.1003 0.1360 0.0012  -0.0039 0.0080  93  PHE A CE2 
761  C  CZ  . PHE A 93  ? 0.1385 0.0772 0.1641 0.0063  0.0108  0.0128  93  PHE A CZ  
762  N  N   . HIS A 94  ? 0.1124 0.0838 0.1076 0.0075  -0.0140 0.0059  94  HIS A N   
763  C  CA  . HIS A 94  ? 0.1224 0.0741 0.1023 0.0079  0.0046  0.0079  94  HIS A CA  
764  C  C   . HIS A 94  ? 0.1104 0.0831 0.0840 0.0094  -0.0093 -0.0009 94  HIS A C   
765  O  O   . HIS A 94  ? 0.1259 0.0824 0.0991 0.0119  0.0079  0.0098  94  HIS A O   
766  C  CB  . HIS A 94  ? 0.1261 0.0967 0.0933 -0.0067 -0.0136 0.0174  94  HIS A CB  
767  C  CG  . HIS A 94  ? 0.1327 0.0949 0.0721 0.0049  0.0044  0.0001  94  HIS A CG  
768  N  ND1 . HIS A 94  ? 0.1339 0.0948 0.0949 -0.0029 -0.0108 0.0020  94  HIS A ND1 
769  C  CD2 . HIS A 94  ? 0.1108 0.1294 0.0693 -0.0061 -0.0062 0.0075  94  HIS A CD2 
770  C  CE1 . HIS A 94  ? 0.1346 0.0948 0.1043 0.0178  -0.0125 -0.0054 94  HIS A CE1 
771  N  NE2 . HIS A 94  ? 0.1159 0.1111 0.0745 0.0013  -0.0066 -0.0068 94  HIS A NE2 
772  N  N   . PHE A 95  ? 0.1310 0.0678 0.1109 0.0145  -0.0053 -0.0019 95  PHE A N   
773  C  CA  . PHE A 95  ? 0.1149 0.0551 0.1459 0.0096  -0.0121 -0.0035 95  PHE A CA  
774  C  C   . PHE A 95  ? 0.1064 0.0844 0.1059 0.0100  -0.0041 -0.0077 95  PHE A C   
775  O  O   . PHE A 95  ? 0.1256 0.1061 0.1160 0.0102  0.0089  0.0071  95  PHE A O   
776  C  CB  . PHE A 95  ? 0.1169 0.1025 0.1423 0.0070  -0.0211 -0.0185 95  PHE A CB  
777  C  CG  . PHE A 95  ? 0.1231 0.1007 0.1204 0.0137  -0.0184 -0.0111 95  PHE A CG  
778  C  CD1 . PHE A 95  ? 0.1596 0.1076 0.1144 0.0038  -0.0337 -0.0156 95  PHE A CD1 
779  C  CD2 . PHE A 95  ? 0.1223 0.1160 0.1414 0.0036  -0.0049 -0.0277 95  PHE A CD2 
780  C  CE1 . PHE A 95  ? 0.1483 0.1204 0.1402 0.0149  -0.0234 -0.0157 95  PHE A CE1 
781  C  CE2 . PHE A 95  ? 0.1311 0.1274 0.1420 0.0047  0.0020  -0.0385 95  PHE A CE2 
782  C  CZ  . PHE A 95  ? 0.1364 0.1239 0.1511 0.0139  -0.0165 -0.0517 95  PHE A CZ  
783  N  N   . HIS A 96  ? 0.1161 0.0772 0.1102 0.0120  -0.0008 -0.0009 96  HIS A N   
784  C  CA  . HIS A 96  ? 0.1210 0.0680 0.1214 0.0197  -0.0119 -0.0011 96  HIS A CA  
785  C  C   . HIS A 96  ? 0.1104 0.0851 0.1068 0.0107  -0.0024 -0.0044 96  HIS A C   
786  O  O   . HIS A 96  ? 0.1187 0.0828 0.1251 0.0070  0.0111  -0.0049 96  HIS A O   
787  C  CB  . HIS A 96  ? 0.1186 0.0784 0.1129 0.0170  -0.0004 -0.0074 96  HIS A CB  
788  C  CG  . HIS A 96  ? 0.1058 0.0822 0.1201 0.0024  -0.0033 0.0019  96  HIS A CG  
789  N  ND1 . HIS A 96  ? 0.1192 0.0752 0.1517 0.0075  -0.0043 -0.0039 96  HIS A ND1 
790  C  CD2 . HIS A 96  ? 0.1391 0.0548 0.1149 0.0032  -0.0011 0.0061  96  HIS A CD2 
791  C  CE1 . HIS A 96  ? 0.1303 0.0750 0.1497 0.0130  -0.0021 -0.0111 96  HIS A CE1 
792  N  NE2 . HIS A 96  ? 0.1075 0.0991 0.1197 0.0005  0.0018  0.0193  96  HIS A NE2 
793  N  N   . TRP A 97  ? 0.1235 0.0785 0.1041 0.0136  -0.0068 -0.0084 97  TRP A N   
794  C  CA  . TRP A 97  ? 0.1159 0.0739 0.1164 0.0115  -0.0092 -0.0198 97  TRP A CA  
795  C  C   . TRP A 97  ? 0.1252 0.0758 0.1021 0.0161  0.0136  -0.0121 97  TRP A C   
796  O  O   . TRP A 97  ? 0.1242 0.0973 0.1377 0.0183  0.0103  -0.0062 97  TRP A O   
797  C  CB  . TRP A 97  ? 0.1252 0.0890 0.1126 0.0131  -0.0037 -0.0072 97  TRP A CB  
798  C  CG  . TRP A 97  ? 0.1232 0.0824 0.1014 0.0006  -0.0067 -0.0198 97  TRP A CG  
799  C  CD1 . TRP A 97  ? 0.1270 0.1221 0.1084 0.0064  0.0133  -0.0196 97  TRP A CD1 
800  C  CD2 . TRP A 97  ? 0.1188 0.1016 0.0961 0.0058  -0.0002 -0.0016 97  TRP A CD2 
801  N  NE1 . TRP A 97  ? 0.1445 0.0871 0.1279 0.0183  -0.0010 -0.0061 97  TRP A NE1 
802  C  CE2 . TRP A 97  ? 0.1300 0.0993 0.1127 0.0223  0.0022  -0.0034 97  TRP A CE2 
803  C  CE3 . TRP A 97  ? 0.1289 0.0802 0.1270 0.0104  -0.0150 -0.0084 97  TRP A CE3 
804  C  CZ2 . TRP A 97  ? 0.1405 0.1003 0.1298 0.0064  -0.0096 -0.0051 97  TRP A CZ2 
805  C  CZ3 . TRP A 97  ? 0.1276 0.1208 0.1122 0.0060  -0.0025 -0.0010 97  TRP A CZ3 
806  C  CH2 . TRP A 97  ? 0.1492 0.0921 0.1161 0.0093  -0.0066 -0.0051 97  TRP A CH2 
807  N  N   . GLY A 98  ? 0.1511 0.0698 0.1234 0.0200  -0.0036 -0.0116 98  GLY A N   
808  C  CA  . GLY A 98  ? 0.1684 0.0763 0.1370 0.0298  -0.0126 -0.0206 98  GLY A CA  
809  C  C   . GLY A 98  ? 0.1600 0.0882 0.1322 0.0134  -0.0034 -0.0139 98  GLY A C   
810  O  O   . GLY A 98  ? 0.1788 0.0980 0.1425 0.0247  -0.0122 -0.0168 98  GLY A O   
811  N  N   . SER A 99  ? 0.1693 0.0856 0.1583 0.0353  -0.0074 -0.0225 99  SER A N   
812  C  CA  . SER A 99  ? 0.1939 0.1014 0.1733 0.0405  0.0137  -0.0373 99  SER A CA  
813  C  C   . SER A 99  ? 0.2030 0.0964 0.1617 0.0314  -0.0080 -0.0453 99  SER A C   
814  O  O   . SER A 99  ? 0.2843 0.1644 0.1935 0.0006  -0.0438 -0.0594 99  SER A O   
815  C  CB  . SER A 99  ? 0.1883 0.1655 0.1776 0.0555  -0.0167 -0.0590 99  SER A CB  
816  O  OG  . SER A 99  ? 0.1912 0.1081 0.2036 0.0361  -0.0145 -0.0251 99  SER A OG  
817  N  N   . LEU A 100 ? 0.1682 0.0903 0.2103 0.0275  0.0058  -0.0270 100 LEU A N   
818  C  CA  . LEU A 100 ? 0.1993 0.0824 0.3314 0.0145  0.0262  -0.0298 100 LEU A CA  
819  C  C   . LEU A 100 ? 0.1870 0.0934 0.2116 0.0140  0.0051  -0.0002 100 LEU A C   
820  O  O   . LEU A 100 ? 0.1998 0.0837 0.2486 0.0134  0.0176  -0.0234 100 LEU A O   
821  C  CB  . LEU A 100 ? 0.8988 0.1393 0.7364 -0.1126 -0.1508 0.3082  100 LEU A CB  
822  C  CG  . LEU A 100 ? 0.5295 2.1992 1.2409 -0.2972 0.7510  -0.9891 100 LEU A CG  
823  C  CD1 . LEU A 100 ? 0.6650 0.5748 1.7257 0.1248  -0.1870 0.4147  100 LEU A CD1 
824  C  CD2 . LEU A 100 ? 0.8326 1.1323 1.1115 0.4709  0.4967  0.5462  100 LEU A CD2 
825  N  N   . ASP A 101 ? 0.1743 0.1002 0.2289 0.0139  -0.0074 -0.0103 101 ASP A N   
826  C  CA  . ASP A 101 ? 0.1750 0.0895 0.2297 0.0168  0.0065  0.0089  101 ASP A CA  
827  C  C   . ASP A 101 ? 0.1867 0.0980 0.2056 0.0027  0.0073  0.0496  101 ASP A C   
828  O  O   . ASP A 101 ? 0.2514 0.1352 0.2907 0.0535  0.0019  0.0249  101 ASP A O   
829  C  CB  . ASP A 101 ? 0.1989 0.1099 0.2501 -0.0100 -0.0476 0.0333  101 ASP A CB  
830  C  CG  . ASP A 101 ? 0.2317 0.1302 0.3120 0.0087  -0.0500 0.0370  101 ASP A CG  
831  O  OD1 . ASP A 101 ? 0.2206 0.1619 0.3133 -0.0178 -0.0320 0.0483  101 ASP A OD1 
832  O  OD2 . ASP A 101 ? 0.2787 0.2032 0.4254 -0.0549 -0.0967 0.0563  101 ASP A OD2 
833  N  N   . GLY A 102 ? 0.1831 0.1119 0.2481 -0.0057 -0.0259 0.0434  102 GLY A N   
834  C  CA  . GLY A 102 ? 0.1776 0.1140 0.2516 -0.0008 -0.0097 0.0316  102 GLY A CA  
835  C  C   . GLY A 102 ? 0.1951 0.0968 0.2109 0.0072  -0.0020 0.0166  102 GLY A C   
836  O  O   . GLY A 102 ? 0.2061 0.1254 0.2079 0.0161  -0.0119 0.0254  102 GLY A O   
837  N  N   . GLN A 103 ? 0.1704 0.0958 0.2014 0.0071  0.0177  0.0128  103 GLN A N   
838  C  CA  . GLN A 103 ? 0.1524 0.1043 0.1561 0.0089  -0.0004 0.0098  103 GLN A CA  
839  C  C   . GLN A 103 ? 0.1478 0.0880 0.1268 0.0043  0.0058  0.0044  103 GLN A C   
840  O  O   . GLN A 103 ? 0.1594 0.0974 0.1457 0.0069  -0.0060 -0.0161 103 GLN A O   
841  C  CB  . GLN A 103 ? 0.1659 0.1377 0.1610 0.0258  0.0048  -0.0001 103 GLN A CB  
842  C  CG  . GLN A 103 ? 0.1885 0.1346 0.1729 0.0447  0.0339  0.0037  103 GLN A CG  
843  C  CD  . GLN A 103 ? 0.2343 0.1923 0.2098 0.0982  0.0526  0.0363  103 GLN A CD  
844  O  OE1 . GLN A 103 ? 0.2282 0.2152 0.2122 0.0590  0.0345  0.0525  103 GLN A OE1 
845  N  NE2 . GLN A 103 ? 0.3291 0.3492 0.3652 0.1381  0.1439  0.1720  103 GLN A NE2 
846  N  N   . GLY A 104 ? 0.1289 0.0820 0.1599 0.0210  0.0163  0.0016  104 GLY A N   
847  C  CA  . GLY A 104 ? 0.1389 0.0869 0.1454 0.0332  -0.0079 -0.0083 104 GLY A CA  
848  C  C   . GLY A 104 ? 0.1215 0.0842 0.1138 -0.0006 -0.0022 -0.0096 104 GLY A C   
849  O  O   . GLY A 104 ? 0.1436 0.1005 0.1436 0.0001  -0.0065 0.0043  104 GLY A O   
850  N  N   . SER A 105 ? 0.1217 0.0991 0.1219 0.0146  0.0055  -0.0096 105 SER A N   
851  C  CA  . SER A 105 ? 0.1120 0.1030 0.1393 0.0199  0.0015  -0.0168 105 SER A CA  
852  C  C   . SER A 105 ? 0.1436 0.0817 0.1307 0.0135  -0.0081 0.0110  105 SER A C   
853  O  O   . SER A 105 ? 0.1461 0.0939 0.1479 0.0092  -0.0176 -0.0089 105 SER A O   
854  C  CB  . SER A 105 ? 0.1235 0.0921 0.1316 0.0053  0.0063  0.0140  105 SER A CB  
855  O  OG  . SER A 105 ? 0.1477 0.0763 0.1474 -0.0041 0.0043  0.0068  105 SER A OG  
856  N  N   . GLU A 106 ? 0.1307 0.0807 0.1259 0.0016  0.0044  -0.0017 106 GLU A N   
857  C  CA  . GLU A 106 ? 0.1177 0.0903 0.1113 0.0079  -0.0013 -0.0111 106 GLU A CA  
858  C  C   . GLU A 106 ? 0.1165 0.0932 0.1020 0.0042  0.0035  -0.0154 106 GLU A C   
859  O  O   . GLU A 106 ? 0.1214 0.1016 0.1452 0.0168  -0.0190 0.0065  106 GLU A O   
860  C  CB  . GLU A 106 ? 0.1539 0.0898 0.1064 -0.0069 0.0062  -0.0006 106 GLU A CB  
861  C  CG  . GLU A 106 ? 0.1520 0.1091 0.1113 -0.0160 0.0222  0.0034  106 GLU A CG  
862  C  CD  . GLU A 106 ? 0.1234 0.1050 0.1164 0.0154  0.0034  -0.0199 106 GLU A CD  
863  O  OE1 . GLU A 106 ? 0.1210 0.0977 0.1604 0.0042  0.0034  -0.0190 106 GLU A OE1 
864  O  OE2 . GLU A 106 ? 0.1226 0.1242 0.1529 0.0116  0.0189  -0.0002 106 GLU A OE2 
865  N  N   . HIS A 107 ? 0.1230 0.0684 0.1240 0.0072  0.0084  -0.0004 107 HIS A N   
866  C  CA  . HIS A 107 ? 0.1288 0.0831 0.1197 0.0019  0.0170  -0.0023 107 HIS A CA  
867  C  C   . HIS A 107 ? 0.1271 0.0955 0.1055 0.0181  -0.0073 -0.0027 107 HIS A C   
868  O  O   . HIS A 107 ? 0.1257 0.0973 0.1210 0.0013  -0.0122 0.0067  107 HIS A O   
869  C  CB  . HIS A 107 ? 0.1374 0.0860 0.1381 -0.0015 0.0023  -0.0087 107 HIS A CB  
870  C  CG  . HIS A 107 ? 0.1275 0.0910 0.1128 0.0163  0.0070  -0.0036 107 HIS A CG  
871  N  ND1 . HIS A 107 ? 0.1353 0.0824 0.1254 0.0002  -0.0005 0.0042  107 HIS A ND1 
872  C  CD2 . HIS A 107 ? 0.1214 0.0820 0.1373 0.0115  0.0122  -0.0174 107 HIS A CD2 
873  C  CE1 . HIS A 107 ? 0.1418 0.0788 0.1134 0.0189  -0.0163 -0.0071 107 HIS A CE1 
874  N  NE2 . HIS A 107 ? 0.1210 0.0900 0.1253 0.0161  -0.0156 -0.0119 107 HIS A NE2 
875  N  N   . THR A 108 ? 0.1441 0.0872 0.1100 0.0073  -0.0065 0.0049  108 THR A N   
876  C  CA  . THR A 108 ? 0.1425 0.0657 0.1320 0.0076  -0.0012 0.0027  108 THR A CA  
877  C  C   . THR A 108 ? 0.1253 0.0941 0.1204 0.0029  -0.0024 0.0057  108 THR A C   
878  O  O   . THR A 108 ? 0.1553 0.1020 0.1239 0.0027  -0.0008 0.0008  108 THR A O   
879  C  CB  . THR A 108 ? 0.1557 0.1032 0.1329 0.0223  -0.0196 0.0040  108 THR A CB  
880  O  OG1 . THR A 108 ? 0.1568 0.1034 0.1384 0.0089  -0.0205 0.0052  108 THR A OG1 
881  C  CG2 . THR A 108 ? 0.1580 0.1286 0.1385 0.0157  0.0038  0.0024  108 THR A CG2 
882  N  N   . VAL A 109 ? 0.1500 0.0982 0.1243 -0.0072 0.0208  0.0074  109 VAL A N   
883  C  CA  . VAL A 109 ? 0.1515 0.1133 0.1298 0.0015  0.0146  0.0296  109 VAL A CA  
884  C  C   . VAL A 109 ? 0.1676 0.0903 0.1393 -0.0043 0.0116  0.0121  109 VAL A C   
885  O  O   . VAL A 109 ? 0.1714 0.0953 0.1571 0.0023  0.0024  0.0076  109 VAL A O   
886  C  CB  . VAL A 109 ? 0.1597 0.1119 0.1288 -0.0040 0.0025  0.0232  109 VAL A CB  
887  C  CG1 . VAL A 109 ? 0.1694 0.1410 0.1837 -0.0129 0.0182  0.0387  109 VAL A CG1 
888  C  CG2 . VAL A 109 ? 0.1885 0.1311 0.2009 0.0124  -0.0115 0.0454  109 VAL A CG2 
889  N  N   . ASP A 110 ? 0.1852 0.1104 0.1162 0.0124  0.0009  0.0309  110 ASP A N   
890  C  CA  . ASP A 110 ? 0.2002 0.1093 0.1781 0.0284  0.0240  0.0491  110 ASP A CA  
891  C  C   . ASP A 110 ? 0.2117 0.1034 0.1716 0.0214  0.0060  0.0178  110 ASP A C   
892  O  O   . ASP A 110 ? 0.2262 0.1047 0.1615 0.0127  0.0054  0.0319  110 ASP A O   
893  C  CB  . ASP A 110 ? 0.2548 0.1280 0.1787 0.0003  0.0328  0.0558  110 ASP A CB  
894  C  CG  . ASP A 110 ? 0.2565 0.1547 0.1655 0.0092  0.0245  0.0453  110 ASP A CG  
895  O  OD1 . ASP A 110 ? 0.2570 0.1589 0.2120 0.0175  0.0438  0.0353  110 ASP A OD1 
896  O  OD2 . ASP A 110 ? 0.2603 0.2154 0.2424 0.0176  0.0521  0.0641  110 ASP A OD2 
897  N  N   . LYS A 111 ? 0.1641 0.1342 0.1535 0.0133  0.0093  0.0182  111 LYS A N   
898  C  CA  . LYS A 111 ? 0.1686 0.1192 0.1587 0.0203  -0.0080 0.0190  111 LYS A CA  
899  C  C   . LYS A 111 ? 0.1801 0.1174 0.1698 0.0296  -0.0172 0.0107  111 LYS A C   
900  O  O   . LYS A 111 ? 0.1957 0.1309 0.2056 0.0380  0.0149  -0.0006 111 LYS A O   
901  C  CB  . LYS A 111 ? 0.2238 0.1625 0.1658 0.0618  -0.0100 0.0331  111 LYS A CB  
902  C  CG  . LYS A 111 ? 0.2606 0.2890 0.1910 0.0756  -0.0398 0.0300  111 LYS A CG  
903  C  CD  . LYS A 111 ? 0.2861 0.3400 0.3131 0.0188  -0.0802 -0.0610 111 LYS A CD  
904  C  CE  . LYS A 111 ? 0.3953 0.4625 0.3423 0.1447  -0.1211 -0.1242 111 LYS A CE  
905  N  NZ  . LYS A 111 ? 0.3296 0.5399 0.4579 0.0185  -0.0121 0.1375  111 LYS A NZ  
906  N  N   . LYS A 112 ? 0.1729 0.0960 0.1628 -0.0050 -0.0008 0.0163  112 LYS A N   
907  C  CA  . LYS A 112 ? 0.1837 0.1231 0.1488 -0.0049 0.0111  0.0208  112 LYS A CA  
908  C  C   . LYS A 112 ? 0.1678 0.0978 0.1443 0.0173  0.0003  0.0131  112 LYS A C   
909  O  O   . LYS A 112 ? 0.1689 0.0971 0.1467 0.0150  -0.0021 0.0046  112 LYS A O   
910  C  CB  . LYS A 112 ? 0.1826 0.1550 0.1973 -0.0252 -0.0100 -0.0037 112 LYS A CB  
911  C  CG  . LYS A 112 ? 0.2066 0.1867 0.2103 -0.0172 -0.0055 -0.0440 112 LYS A CG  
912  C  CD  . LYS A 112 ? 0.2013 0.2133 0.2220 0.0254  -0.0168 0.0032  112 LYS A CD  
913  C  CE  . LYS A 112 ? 0.2627 0.2906 0.2497 0.0242  -0.0348 -0.0487 112 LYS A CE  
914  N  NZ  . LYS A 112 ? 0.2717 0.2305 0.3579 0.0066  -0.0735 0.0282  112 LYS A NZ  
915  N  N   A LYS A 113 ? 0.1650 0.1265 0.1323 0.0357  -0.0015 0.0105  113 LYS A N   
916  N  N   B LYS A 113 ? 0.1740 0.1117 0.1327 0.0292  -0.0043 0.0057  113 LYS A N   
917  C  CA  A LYS A 113 ? 0.1845 0.1231 0.1230 0.0255  -0.0022 -0.0003 113 LYS A CA  
918  C  CA  B LYS A 113 ? 0.1658 0.1222 0.1180 0.0212  -0.0094 -0.0034 113 LYS A CA  
919  C  C   A LYS A 113 ? 0.1768 0.0807 0.1887 0.0095  -0.0143 0.0100  113 LYS A C   
920  C  C   B LYS A 113 ? 0.1612 0.0811 0.1745 -0.0039 -0.0208 0.0129  113 LYS A C   
921  O  O   A LYS A 113 ? 0.2499 0.0759 0.2534 0.0002  -0.0653 0.0173  113 LYS A O   
922  O  O   B LYS A 113 ? 0.1939 0.0750 0.1901 0.0053  -0.0425 0.0052  113 LYS A O   
923  C  CB  A LYS A 113 ? 0.1761 0.1382 0.1467 0.0284  -0.0048 -0.0120 113 LYS A CB  
924  C  CB  B LYS A 113 ? 0.1594 0.1413 0.1580 0.0242  -0.0096 -0.0257 113 LYS A CB  
925  C  CG  A LYS A 113 ? 0.1655 0.1854 0.1232 0.0164  0.0005  -0.0170 113 LYS A CG  
926  C  CG  B LYS A 113 ? 0.1330 0.1786 0.1715 0.0093  -0.0027 -0.0262 113 LYS A CG  
927  C  CD  A LYS A 113 ? 0.1777 0.1356 0.2025 0.0141  0.0279  -0.0062 113 LYS A CD  
928  C  CD  B LYS A 113 ? 0.1583 0.1873 0.1899 0.0324  0.0026  -0.0308 113 LYS A CD  
929  C  CE  A LYS A 113 ? 0.2298 0.2495 0.1978 0.0001  -0.0460 0.0081  113 LYS A CE  
930  C  CE  B LYS A 113 ? 0.1945 0.2452 0.2484 -0.0032 -0.0424 0.0034  113 LYS A CE  
931  N  NZ  A LYS A 113 ? 0.1995 0.2122 0.1914 0.0502  -0.0391 -0.0274 113 LYS A NZ  
932  N  NZ  B LYS A 113 ? 0.2231 0.2085 0.2728 -0.0021 0.0042  -0.0212 113 LYS A NZ  
933  N  N   . TYR A 114 ? 0.1485 0.0910 0.1402 0.0127  0.0000  0.0065  114 TYR A N   
934  C  CA  . TYR A 114 ? 0.1575 0.0824 0.1402 0.0050  -0.0062 0.0000  114 TYR A CA  
935  C  C   . TYR A 114 ? 0.1465 0.0840 0.1355 0.0072  -0.0047 -0.0119 114 TYR A C   
936  O  O   . TYR A 114 ? 0.1434 0.0869 0.1533 0.0025  -0.0013 -0.0001 114 TYR A O   
937  C  CB  . TYR A 114 ? 0.1288 0.0937 0.1708 0.0122  0.0115  -0.0096 114 TYR A CB  
938  C  CG  . TYR A 114 ? 0.1585 0.0874 0.1309 0.0074  -0.0006 0.0084  114 TYR A CG  
939  C  CD1 . TYR A 114 ? 0.1937 0.1048 0.1479 0.0128  0.0074  0.0236  114 TYR A CD1 
940  C  CD2 . TYR A 114 ? 0.1497 0.0937 0.2161 0.0073  0.0186  0.0063  114 TYR A CD2 
941  C  CE1 . TYR A 114 ? 0.2255 0.1254 0.1653 0.0324  0.0212  0.0186  114 TYR A CE1 
942  C  CE2 . TYR A 114 ? 0.1701 0.1439 0.2316 0.0248  0.0434  0.0020  114 TYR A CE2 
943  C  CZ  . TYR A 114 ? 0.2020 0.1562 0.2297 0.0064  0.0605  0.0220  114 TYR A CZ  
944  O  OH  . TYR A 114 ? 0.2610 0.2568 0.2739 0.0188  0.0946  0.0078  114 TYR A OH  
945  N  N   . ALA A 115 ? 0.1441 0.0709 0.1362 0.0006  -0.0067 -0.0034 115 ALA A N   
946  C  CA  . ALA A 115 ? 0.1381 0.0810 0.1366 -0.0038 -0.0079 -0.0111 115 ALA A CA  
947  C  C   . ALA A 115 ? 0.1348 0.0801 0.1350 0.0252  -0.0048 -0.0059 115 ALA A C   
948  O  O   . ALA A 115 ? 0.1382 0.0774 0.1517 0.0075  0.0083  -0.0117 115 ALA A O   
949  C  CB  . ALA A 115 ? 0.1540 0.1025 0.1636 0.0069  -0.0339 -0.0133 115 ALA A CB  
950  N  N   . ALA A 116 ? 0.1360 0.0653 0.1353 0.0088  0.0004  -0.0096 116 ALA A N   
951  C  CA  . ALA A 116 ? 0.1385 0.0700 0.1172 0.0005  0.0053  -0.0116 116 ALA A CA  
952  C  C   . ALA A 116 ? 0.1090 0.0806 0.1199 0.0062  -0.0072 0.0024  116 ALA A C   
953  O  O   . ALA A 116 ? 0.1268 0.0793 0.1280 0.0065  0.0071  0.0024  116 ALA A O   
954  C  CB  . ALA A 116 ? 0.1312 0.1228 0.1038 0.0177  0.0089  0.0004  116 ALA A CB  
955  N  N   . GLU A 117 ? 0.1312 0.0646 0.1280 0.0166  -0.0018 -0.0032 117 GLU A N   
956  C  CA  . GLU A 117 ? 0.1291 0.0661 0.1170 0.0205  0.0013  -0.0044 117 GLU A CA  
957  C  C   . GLU A 117 ? 0.1149 0.0847 0.1162 -0.0009 0.0073  0.0013  117 GLU A C   
958  O  O   . GLU A 117 ? 0.1316 0.0837 0.1510 0.0209  0.0309  0.0201  117 GLU A O   
959  C  CB  . GLU A 117 ? 0.1641 0.0973 0.0964 0.0173  -0.0108 -0.0103 117 GLU A CB  
960  C  CG  . GLU A 117 ? 0.1407 0.0888 0.1122 0.0132  -0.0030 -0.0002 117 GLU A CG  
961  C  CD  . GLU A 117 ? 0.1293 0.0908 0.1194 0.0064  -0.0002 -0.0100 117 GLU A CD  
962  O  OE1 . GLU A 117 ? 0.1282 0.1186 0.1468 0.0208  -0.0190 -0.0067 117 GLU A OE1 
963  O  OE2 . GLU A 117 ? 0.1866 0.1016 0.1265 0.0067  -0.0282 -0.0088 117 GLU A OE2 
964  N  N   . LEU A 118 ? 0.1210 0.0612 0.1220 0.0138  0.0040  -0.0035 118 LEU A N   
965  C  CA  . LEU A 118 ? 0.1318 0.0536 0.1279 -0.0018 -0.0046 -0.0051 118 LEU A CA  
966  C  C   . LEU A 118 ? 0.1151 0.0714 0.0768 0.0059  -0.0061 0.0029  118 LEU A C   
967  O  O   . LEU A 118 ? 0.1398 0.0741 0.0930 0.0138  0.0099  0.0052  118 LEU A O   
968  C  CB  . LEU A 118 ? 0.1226 0.0609 0.1411 0.0039  -0.0018 -0.0069 118 LEU A CB  
969  C  CG  . LEU A 118 ? 0.1271 0.0907 0.1265 0.0190  -0.0031 0.0146  118 LEU A CG  
970  C  CD1 . LEU A 118 ? 0.1441 0.0792 0.1393 0.0055  -0.0038 0.0124  118 LEU A CD1 
971  C  CD2 . LEU A 118 ? 0.1197 0.1352 0.1489 0.0052  -0.0079 0.0134  118 LEU A CD2 
972  N  N   . HIS A 119 ? 0.1058 0.0551 0.1100 0.0069  -0.0079 0.0074  119 HIS A N   
973  C  CA  . HIS A 119 ? 0.1181 0.0584 0.1207 0.0060  -0.0039 0.0041  119 HIS A CA  
974  C  C   . HIS A 119 ? 0.1063 0.0684 0.0903 0.0130  -0.0003 -0.0064 119 HIS A C   
975  O  O   . HIS A 119 ? 0.1303 0.0793 0.0980 0.0142  0.0060  -0.0004 119 HIS A O   
976  C  CB  . HIS A 119 ? 0.0980 0.0709 0.1404 0.0089  -0.0040 0.0088  119 HIS A CB  
977  C  CG  . HIS A 119 ? 0.1156 0.0797 0.1034 0.0154  0.0008  -0.0054 119 HIS A CG  
978  N  ND1 . HIS A 119 ? 0.1186 0.0837 0.0991 0.0122  0.0029  -0.0042 119 HIS A ND1 
979  C  CD2 . HIS A 119 ? 0.1220 0.0948 0.1122 0.0022  -0.0043 0.0127  119 HIS A CD2 
980  C  CE1 . HIS A 119 ? 0.1168 0.1038 0.0833 0.0105  0.0016  -0.0043 119 HIS A CE1 
981  N  NE2 . HIS A 119 ? 0.1149 0.0919 0.1132 0.0148  0.0006  -0.0055 119 HIS A NE2 
982  N  N   . LEU A 120 ? 0.1049 0.0727 0.0971 0.0189  -0.0006 -0.0092 120 LEU A N   
983  C  CA  . LEU A 120 ? 0.1134 0.0603 0.1226 0.0148  -0.0037 -0.0049 120 LEU A CA  
984  C  C   . LEU A 120 ? 0.1235 0.0691 0.0894 0.0163  -0.0155 0.0026  120 LEU A C   
985  O  O   . LEU A 120 ? 0.1266 0.0743 0.0923 0.0035  -0.0079 0.0029  120 LEU A O   
986  C  CB  . LEU A 120 ? 0.1244 0.0905 0.1314 0.0152  -0.0040 -0.0182 120 LEU A CB  
987  C  CG  . LEU A 120 ? 0.1223 0.0953 0.1160 0.0006  -0.0122 -0.0072 120 LEU A CG  
988  C  CD1 . LEU A 120 ? 0.2294 0.1247 0.1508 -0.0590 0.0072  -0.0104 120 LEU A CD1 
989  C  CD2 . LEU A 120 ? 0.1486 0.1267 0.1497 0.0218  -0.0245 -0.0209 120 LEU A CD2 
990  N  N   . VAL A 121 ? 0.1244 0.0664 0.1249 0.0008  -0.0018 -0.0026 121 VAL A N   
991  C  CA  . VAL A 121 ? 0.1279 0.0696 0.1223 0.0021  0.0081  -0.0089 121 VAL A CA  
992  C  C   . VAL A 121 ? 0.1315 0.0668 0.1003 -0.0117 -0.0011 -0.0009 121 VAL A C   
993  O  O   . VAL A 121 ? 0.1550 0.0856 0.1140 0.0093  -0.0047 0.0050  121 VAL A O   
994  C  CB  . VAL A 121 ? 0.1223 0.0827 0.1181 -0.0034 0.0078  -0.0114 121 VAL A CB  
995  C  CG1 . VAL A 121 ? 0.1403 0.0880 0.1425 -0.0043 0.0013  -0.0062 121 VAL A CG1 
996  C  CG2 . VAL A 121 ? 0.1461 0.0985 0.1222 0.0146  0.0110  -0.0096 121 VAL A CG2 
997  N  N   . HIS A 122 ? 0.1301 0.0653 0.1229 0.0017  -0.0046 -0.0136 122 HIS A N   
998  C  CA  . HIS A 122 ? 0.1329 0.0632 0.1275 0.0081  -0.0092 -0.0254 122 HIS A CA  
999  C  C   . HIS A 122 ? 0.1414 0.0688 0.1360 -0.0046 -0.0214 -0.0160 122 HIS A C   
1000 O  O   . HIS A 122 ? 0.1580 0.0885 0.1500 -0.0108 -0.0379 0.0023  122 HIS A O   
1001 C  CB  . HIS A 122 ? 0.1359 0.0725 0.1547 0.0124  -0.0024 -0.0137 122 HIS A CB  
1002 C  CG  . HIS A 122 ? 0.1384 0.0691 0.1378 0.0125  -0.0132 -0.0220 122 HIS A CG  
1003 N  ND1 . HIS A 122 ? 0.1213 0.0727 0.1496 0.0129  0.0049  -0.0156 122 HIS A ND1 
1004 C  CD2 . HIS A 122 ? 0.1352 0.0917 0.1526 -0.0015 -0.0006 -0.0131 122 HIS A CD2 
1005 C  CE1 . HIS A 122 ? 0.1164 0.1214 0.1481 0.0114  0.0005  -0.0199 122 HIS A CE1 
1006 N  NE2 . HIS A 122 ? 0.1270 0.1142 0.1342 -0.0201 -0.0154 -0.0107 122 HIS A NE2 
1007 N  N   . TRP A 123 ? 0.1524 0.0662 0.1235 0.0013  -0.0172 -0.0172 123 TRP A N   
1008 C  CA  . TRP A 123 ? 0.1396 0.0677 0.1503 -0.0016 -0.0151 -0.0250 123 TRP A CA  
1009 C  C   . TRP A 123 ? 0.1406 0.0723 0.1500 0.0038  -0.0227 -0.0044 123 TRP A C   
1010 O  O   . TRP A 123 ? 0.1456 0.0888 0.1957 0.0109  -0.0330 -0.0291 123 TRP A O   
1011 C  CB  . TRP A 123 ? 0.1712 0.0983 0.1540 -0.0198 -0.0250 0.0104  123 TRP A CB  
1012 C  CG  . TRP A 123 ? 0.2021 0.0758 0.1521 -0.0321 -0.0263 0.0109  123 TRP A CG  
1013 C  CD1 . TRP A 123 ? 0.2782 0.1225 0.1461 -0.0168 -0.0652 -0.0004 123 TRP A CD1 
1014 C  CD2 . TRP A 123 ? 0.2434 0.0792 0.1409 -0.0190 -0.0405 0.0150  123 TRP A CD2 
1015 N  NE1 . TRP A 123 ? 0.3066 0.0754 0.1873 -0.0268 -0.0752 -0.0032 123 TRP A NE1 
1016 C  CE2 . TRP A 123 ? 0.2584 0.0817 0.1704 -0.0161 -0.0814 0.0016  123 TRP A CE2 
1017 C  CE3 . TRP A 123 ? 0.2591 0.0691 0.2079 -0.0237 -0.0282 0.0064  123 TRP A CE3 
1018 C  CZ2 . TRP A 123 ? 0.3762 0.0754 0.2181 -0.0061 -0.0797 0.0117  123 TRP A CZ2 
1019 C  CZ3 . TRP A 123 ? 0.3166 0.0625 0.1837 -0.0156 -0.0486 0.0054  123 TRP A CZ3 
1020 C  CH2 . TRP A 123 ? 0.3747 0.0829 0.1903 -0.0276 -0.0851 0.0225  123 TRP A CH2 
1021 N  N   . ASN A 124 ? 0.1625 0.0714 0.1525 0.0032  -0.0167 -0.0341 124 ASN A N   
1022 C  CA  . ASN A 124 ? 0.1770 0.0802 0.1741 0.0071  -0.0200 -0.0491 124 ASN A CA  
1023 C  C   . ASN A 124 ? 0.1729 0.0935 0.1738 0.0146  -0.0245 -0.0444 124 ASN A C   
1024 O  O   . ASN A 124 ? 0.1747 0.0878 0.1605 0.0081  -0.0226 -0.0334 124 ASN A O   
1025 C  CB  . ASN A 124 ? 0.1956 0.1014 0.1618 -0.0022 -0.0120 -0.0450 124 ASN A CB  
1026 C  CG  . ASN A 124 ? 0.2059 0.1079 0.1748 -0.0223 0.0043  -0.0377 124 ASN A CG  
1027 O  OD1 . ASN A 124 ? 0.2014 0.1324 0.2097 0.0054  0.0230  -0.0408 124 ASN A OD1 
1028 N  ND2 . ASN A 124 ? 0.2488 0.1149 0.1883 0.0013  0.0231  -0.0447 124 ASN A ND2 
1029 N  N   . THR A 125 ? 0.1745 0.1004 0.2229 0.0257  -0.0237 -0.0454 125 THR A N   
1030 C  CA  . THR A 125 ? 0.1932 0.0891 0.2384 0.0168  -0.0310 -0.0282 125 THR A CA  
1031 C  C   . THR A 125 ? 0.1819 0.0939 0.2551 0.0278  0.0184  -0.0367 125 THR A C   
1032 O  O   . THR A 125 ? 0.2108 0.1113 0.2885 0.0260  -0.0098 -0.0262 125 THR A O   
1033 C  CB  . THR A 125 ? 0.1985 0.1506 0.2947 0.0163  -0.0487 -0.0173 125 THR A CB  
1034 O  OG1 . THR A 125 ? 0.2187 0.1791 0.3406 0.0619  -0.0058 -0.0594 125 THR A OG1 
1035 C  CG2 . THR A 125 ? 0.2546 0.2212 0.3504 0.0287  -0.1174 -0.0684 125 THR A CG2 
1036 N  N   . LYS A 126 ? 0.1817 0.0910 0.2257 0.0087  0.0146  -0.0566 127 LYS A N   
1037 C  CA  . LYS A 126 ? 0.2201 0.1367 0.2522 -0.0125 0.0171  -0.0886 127 LYS A CA  
1038 C  C   . LYS A 126 ? 0.2213 0.1063 0.2120 -0.0098 0.0043  -0.0544 127 LYS A C   
1039 O  O   . LYS A 126 ? 0.2363 0.1097 0.3643 -0.0087 0.0299  -0.0919 127 LYS A O   
1040 C  CB  . LYS A 126 ? 0.3226 0.2122 0.2517 -0.0275 -0.0260 -0.0793 127 LYS A CB  
1041 C  CG  . LYS A 126 ? 0.2868 0.2176 0.2490 -0.0190 -0.0124 -0.0721 127 LYS A CG  
1042 C  CD  . LYS A 126 ? 0.3509 0.4220 0.2876 -0.0468 0.0826  -0.0290 127 LYS A CD  
1043 C  CE  . LYS A 126 ? 0.2739 0.4992 0.2445 -0.0295 0.0381  -0.0403 127 LYS A CE  
1044 N  NZ  . LYS A 126 ? 0.5965 0.7639 0.2578 0.1481  0.0515  0.2108  127 LYS A NZ  
1045 N  N   . TYR A 127 ? 0.2016 0.0991 0.1693 0.0144  -0.0075 -0.0287 128 TYR A N   
1046 C  CA  . TYR A 127 ? 0.1860 0.0898 0.1763 0.0122  -0.0282 -0.0307 128 TYR A CA  
1047 C  C   . TYR A 127 ? 0.1841 0.0941 0.1790 -0.0044 -0.0115 -0.0275 128 TYR A C   
1048 O  O   . TYR A 127 ? 0.1798 0.1104 0.1935 0.0065  -0.0038 -0.0080 128 TYR A O   
1049 C  CB  . TYR A 127 ? 0.1987 0.1092 0.1795 0.0189  0.0006  -0.0034 128 TYR A CB  
1050 C  CG  . TYR A 127 ? 0.1870 0.0935 0.1684 -0.0049 -0.0120 -0.0264 128 TYR A CG  
1051 C  CD1 . TYR A 127 ? 0.2387 0.1356 0.1680 -0.0055 -0.0278 -0.0354 128 TYR A CD1 
1052 C  CD2 . TYR A 127 ? 0.2054 0.1164 0.1449 0.0008  -0.0096 -0.0240 128 TYR A CD2 
1053 C  CE1 . TYR A 127 ? 0.2693 0.1104 0.1738 0.0196  -0.0443 -0.0532 128 TYR A CE1 
1054 C  CE2 . TYR A 127 ? 0.1935 0.1257 0.1396 0.0139  -0.0006 -0.0324 128 TYR A CE2 
1055 C  CZ  . TYR A 127 ? 0.2666 0.1349 0.1428 0.0198  -0.0018 -0.0510 128 TYR A CZ  
1056 O  OH  . TYR A 127 ? 0.2898 0.1431 0.1661 0.0216  -0.0141 -0.0407 128 TYR A OH  
1057 N  N   . GLY A 128 ? 0.1999 0.0891 0.1842 0.0147  -0.0335 -0.0122 129 GLY A N   
1058 C  CA  . GLY A 128 ? 0.2257 0.1038 0.1869 -0.0044 0.0039  0.0119  129 GLY A CA  
1059 C  C   . GLY A 128 ? 0.2188 0.1081 0.1565 0.0150  -0.0157 0.0178  129 GLY A C   
1060 O  O   . GLY A 128 ? 0.2514 0.1097 0.1856 0.0074  -0.0329 0.0323  129 GLY A O   
1061 N  N   . ASP A 129 ? 0.2301 0.1086 0.1862 0.0365  -0.0113 -0.0073 130 ASP A N   
1062 C  CA  . ASP A 129 ? 0.2993 0.1095 0.1539 0.0390  -0.0199 -0.0037 130 ASP A CA  
1063 C  C   . ASP A 129 ? 0.2731 0.1186 0.1687 0.0333  -0.0296 -0.0152 130 ASP A C   
1064 O  O   . ASP A 129 ? 0.2427 0.1344 0.1625 0.0505  -0.0190 -0.0073 130 ASP A O   
1065 C  CB  . ASP A 129 ? 0.2713 0.1474 0.1823 0.0390  -0.0215 0.0192  130 ASP A CB  
1066 C  CG  . ASP A 129 ? 0.3045 0.1554 0.2542 0.0664  -0.0334 -0.0073 130 ASP A CG  
1067 O  OD1 . ASP A 129 ? 0.3294 0.1870 0.2545 0.0824  -0.0103 0.0269  130 ASP A OD1 
1068 O  OD2 . ASP A 129 ? 0.2599 0.1806 0.3405 0.0546  -0.0197 0.0108  130 ASP A OD2 
1069 N  N   . ALA A 130 ? 0.2741 0.1179 0.1471 0.0345  -0.0066 0.0094  131 ALA A N   
1070 C  CA  . ALA A 130 ? 0.2879 0.1091 0.1615 0.0499  -0.0333 -0.0059 131 ALA A CA  
1071 C  C   . ALA A 130 ? 0.2502 0.1156 0.1996 0.0335  0.0021  0.0072  131 ALA A C   
1072 O  O   . ALA A 130 ? 0.2450 0.1199 0.1932 0.0303  -0.0168 0.0161  131 ALA A O   
1073 C  CB  . ALA A 130 ? 0.3652 0.1120 0.2150 0.0196  -0.0124 -0.0313 131 ALA A CB  
1074 N  N   . GLY A 131 ? 0.2621 0.1106 0.1939 0.0201  0.0039  0.0243  132 GLY A N   
1075 C  CA  . GLY A 131 ? 0.2416 0.1557 0.1966 0.0186  0.0209  0.0193  132 GLY A CA  
1076 C  C   . GLY A 131 ? 0.1858 0.1385 0.2082 0.0113  0.0451  0.0144  132 GLY A C   
1077 O  O   . GLY A 131 ? 0.2279 0.1453 0.2539 0.0274  0.0200  0.0149  132 GLY A O   
1078 N  N   A LYS A 132 ? 0.2451 0.1178 0.2011 0.0223  0.0487  0.0168  133 LYS A N   
1079 N  N   B LYS A 132 ? 0.2088 0.1201 0.1834 0.0116  0.0403  0.0093  133 LYS A N   
1080 C  CA  A LYS A 132 ? 0.2404 0.0860 0.2190 0.0111  0.0166  0.0272  133 LYS A CA  
1081 C  CA  B LYS A 132 ? 0.1780 0.1099 0.2064 -0.0068 0.0128  0.0121  133 LYS A CA  
1082 C  C   A LYS A 132 ? 0.1738 0.0730 0.1833 0.0097  0.0024  -0.0009 133 LYS A C   
1083 C  C   B LYS A 132 ? 0.1599 0.1095 0.1841 0.0032  0.0208  -0.0055 133 LYS A C   
1084 O  O   A LYS A 132 ? 0.1788 0.0851 0.1960 0.0030  -0.0203 -0.0069 133 LYS A O   
1085 O  O   B LYS A 132 ? 0.1975 0.1342 0.1791 -0.0063 0.0151  -0.0200 133 LYS A O   
1086 C  CB  A LYS A 132 ? 0.2830 0.1254 0.2002 0.0496  0.0262  0.0358  133 LYS A CB  
1087 C  CB  B LYS A 132 ? 0.1593 0.1298 0.1744 0.0015  0.0032  -0.0065 133 LYS A CB  
1088 C  CG  A LYS A 132 ? 0.3551 0.2027 0.3037 -0.0161 0.0660  0.0414  133 LYS A CG  
1089 C  CG  B LYS A 132 ? 0.1722 0.1948 0.2361 -0.0146 0.0369  0.0139  133 LYS A CG  
1090 C  CD  A LYS A 132 ? 0.4056 0.3051 0.1590 -0.0804 -0.0132 0.0650  133 LYS A CD  
1091 C  CD  B LYS A 132 ? 0.1924 0.1633 0.3647 -0.0603 0.0230  0.0672  133 LYS A CD  
1092 C  CE  A LYS A 132 ? 0.3235 0.2075 0.2086 0.0038  0.0468  0.0644  133 LYS A CE  
1093 C  CE  B LYS A 132 ? 0.3424 0.4000 0.3557 -0.0341 -0.1976 -0.0483 133 LYS A CE  
1094 N  NZ  A LYS A 132 ? 0.3816 0.4643 0.2404 -0.1736 0.0512  -0.0037 133 LYS A NZ  
1095 N  NZ  B LYS A 132 ? 0.4003 0.3046 0.4972 -0.0162 -0.0815 -0.1465 133 LYS A NZ  
1096 N  N   . ALA A 133 ? 0.1720 0.0934 0.1661 0.0039  0.0146  -0.0046 134 ALA A N   
1097 C  CA  . ALA A 133 ? 0.1583 0.1168 0.1323 -0.0094 -0.0022 0.0048  134 ALA A CA  
1098 C  C   . ALA A 133 ? 0.1860 0.1128 0.1335 -0.0240 0.0127  -0.0033 134 ALA A C   
1099 O  O   . ALA A 133 ? 0.1680 0.1375 0.1479 -0.0087 0.0013  -0.0002 134 ALA A O   
1100 C  CB  . ALA A 133 ? 0.1784 0.1101 0.1346 -0.0130 -0.0283 -0.0210 134 ALA A CB  
1101 N  N   . SER A 134 ? 0.1849 0.1016 0.1605 0.0038  -0.0026 -0.0022 135 SER A N   
1102 C  CA  . SER A 134 ? 0.2046 0.1135 0.1514 0.0149  -0.0013 0.0034  135 SER A CA  
1103 C  C   . SER A 134 ? 0.1813 0.1179 0.1702 -0.0059 0.0055  0.0149  135 SER A C   
1104 O  O   . SER A 134 ? 0.1712 0.1416 0.2011 0.0154  0.0127  0.0211  135 SER A O   
1105 C  CB  . SER A 134 ? 0.2404 0.1314 0.1691 0.0199  0.0051  -0.0195 135 SER A CB  
1106 O  OG  . SER A 134 ? 0.2885 0.1888 0.2161 0.0603  0.0438  0.0329  135 SER A OG  
1107 N  N   . GLN A 135 ? 0.1896 0.1286 0.1558 -0.0079 0.0065  -0.0083 136 GLN A N   
1108 C  CA  . GLN A 135 ? 0.1794 0.1350 0.1887 -0.0032 -0.0089 -0.0122 136 GLN A CA  
1109 C  C   . GLN A 135 ? 0.1694 0.1247 0.1982 0.0030  -0.0103 -0.0307 136 GLN A C   
1110 O  O   . GLN A 135 ? 0.1948 0.2064 0.2165 -0.0455 -0.0271 -0.0353 136 GLN A O   
1111 C  CB  . GLN A 135 ? 0.1880 0.1831 0.2693 -0.0665 -0.0088 0.0059  136 GLN A CB  
1112 C  CG  . GLN A 135 ? 0.3197 0.2703 0.2938 -0.1257 0.0533  0.0387  136 GLN A CG  
1113 C  CD  . GLN A 135 ? 0.4176 0.4745 0.4931 -0.0514 0.1805  0.0571  136 GLN A CD  
1114 O  OE1 . GLN A 135 ? 0.6334 0.7799 0.7012 0.0239  -0.0262 -0.1175 136 GLN A OE1 
1115 N  NE2 . GLN A 135 ? 0.6804 0.4591 0.5359 -0.1273 0.1550  0.0614  136 GLN A NE2 
1116 N  N   . GLN A 136 ? 0.1734 0.1316 0.1745 -0.0042 0.0148  0.0000  137 GLN A N   
1117 C  CA  . GLN A 136 ? 0.1946 0.1330 0.1344 -0.0098 -0.0168 -0.0207 137 GLN A CA  
1118 C  C   . GLN A 136 ? 0.1966 0.1269 0.1492 -0.0107 -0.0151 -0.0361 137 GLN A C   
1119 O  O   . GLN A 136 ? 0.1916 0.1293 0.1377 -0.0124 -0.0050 -0.0141 137 GLN A O   
1120 C  CB  . GLN A 136 ? 0.2240 0.1264 0.1788 0.0267  -0.0262 0.0004  137 GLN A CB  
1121 C  CG  . GLN A 136 ? 0.2591 0.1544 0.1813 0.0124  0.0067  0.0197  137 GLN A CG  
1122 C  CD  . GLN A 136 ? 0.2769 0.1104 0.3625 -0.0006 0.0225  0.0356  137 GLN A CD  
1123 O  OE1 . GLN A 136 ? 0.2904 0.2174 0.3462 -0.0070 -0.0233 -0.1366 137 GLN A OE1 
1124 N  NE2 . GLN A 136 ? 0.4438 0.2859 0.4976 -0.0659 0.0510  0.1911  137 GLN A NE2 
1125 N  N   . PRO A 137 ? 0.1655 0.1380 0.1353 -0.0006 -0.0093 -0.0266 138 PRO A N   
1126 C  CA  . PRO A 137 ? 0.1932 0.1687 0.1207 0.0032  -0.0231 -0.0016 138 PRO A CA  
1127 C  C   . PRO A 137 ? 0.1860 0.1470 0.1400 0.0023  0.0038  0.0030  138 PRO A C   
1128 O  O   . PRO A 137 ? 0.2190 0.1482 0.2815 0.0174  -0.0116 0.0288  138 PRO A O   
1129 C  CB  . PRO A 137 ? 0.2917 0.2430 0.1201 -0.0158 -0.0396 0.0174  138 PRO A CB  
1130 C  CG  . PRO A 137 ? 0.4377 0.2787 0.1781 -0.0641 -0.0425 -0.0205 138 PRO A CG  
1131 C  CD  . PRO A 137 ? 0.2176 0.1910 0.1540 -0.0133 -0.0260 -0.0551 138 PRO A CD  
1132 N  N   . ASP A 138 ? 0.1859 0.1353 0.1258 0.0085  -0.0103 -0.0125 139 ASP A N   
1133 C  CA  . ASP A 138 ? 0.1718 0.1829 0.1302 0.0203  -0.0002 0.0115  139 ASP A CA  
1134 C  C   . ASP A 138 ? 0.1578 0.1352 0.1355 -0.0119 0.0036  0.0086  139 ASP A C   
1135 O  O   . ASP A 138 ? 0.1647 0.1791 0.1759 0.0193  -0.0171 -0.0044 139 ASP A O   
1136 C  CB  . ASP A 138 ? 0.2006 0.1920 0.1463 0.0008  0.0127  -0.0108 139 ASP A CB  
1137 C  CG  . ASP A 138 ? 0.2011 0.2231 0.1718 0.0052  -0.0212 -0.0074 139 ASP A CG  
1138 O  OD1 . ASP A 138 ? 0.2505 0.1497 0.2139 0.0303  -0.0053 -0.0307 139 ASP A OD1 
1139 O  OD2 . ASP A 138 ? 0.2828 0.2546 0.2301 0.0419  0.0058  -0.0901 139 ASP A OD2 
1140 N  N   . GLY A 139 ? 0.1719 0.1100 0.1089 -0.0069 -0.0026 -0.0189 140 GLY A N   
1141 C  CA  . GLY A 139 ? 0.1919 0.1095 0.1240 -0.0084 -0.0359 -0.0128 140 GLY A CA  
1142 C  C   . GLY A 139 ? 0.1463 0.0824 0.1009 -0.0054 -0.0076 0.0005  140 GLY A C   
1143 O  O   . GLY A 139 ? 0.1622 0.0856 0.1278 0.0026  -0.0173 -0.0034 140 GLY A O   
1144 N  N   . LEU A 140 ? 0.1386 0.0802 0.1432 0.0035  -0.0070 -0.0153 141 LEU A N   
1145 C  CA  . LEU A 140 ? 0.1346 0.0718 0.1378 -0.0023 -0.0067 -0.0148 141 LEU A CA  
1146 C  C   . LEU A 140 ? 0.1302 0.0831 0.1215 0.0122  -0.0001 -0.0179 141 LEU A C   
1147 O  O   . LEU A 140 ? 0.1389 0.0916 0.1216 0.0010  -0.0100 -0.0077 141 LEU A O   
1148 C  CB  . LEU A 140 ? 0.1399 0.0919 0.1407 0.0157  -0.0013 -0.0100 141 LEU A CB  
1149 C  CG  . LEU A 140 ? 0.1643 0.0983 0.1869 0.0250  0.0273  0.0013  141 LEU A CG  
1150 C  CD1 . LEU A 140 ? 0.1860 0.1086 0.1927 0.0418  0.0253  0.0046  141 LEU A CD1 
1151 C  CD2 . LEU A 140 ? 0.1896 0.1366 0.1687 0.0212  0.0188  -0.0043 141 LEU A CD2 
1152 N  N   . ALA A 141 ? 0.1221 0.0758 0.1395 -0.0026 -0.0080 -0.0212 142 ALA A N   
1153 C  CA  . ALA A 141 ? 0.1392 0.0732 0.1344 -0.0077 -0.0060 -0.0190 142 ALA A CA  
1154 C  C   . ALA A 141 ? 0.1229 0.0842 0.1118 -0.0031 -0.0140 -0.0020 142 ALA A C   
1155 O  O   . ALA A 141 ? 0.1701 0.0732 0.1213 0.0038  -0.0125 -0.0001 142 ALA A O   
1156 C  CB  . ALA A 141 ? 0.1508 0.1147 0.1725 0.0001  0.0152  -0.0315 142 ALA A CB  
1157 N  N   . VAL A 142 ? 0.1453 0.0761 0.0980 -0.0013 0.0012  -0.0022 143 VAL A N   
1158 C  CA  . VAL A 142 ? 0.1400 0.0930 0.0989 0.0122  0.0100  -0.0155 143 VAL A CA  
1159 C  C   . VAL A 142 ? 0.1423 0.0712 0.1025 0.0125  0.0053  -0.0054 143 VAL A C   
1160 O  O   . VAL A 142 ? 0.1546 0.0974 0.1045 -0.0009 -0.0107 -0.0111 143 VAL A O   
1161 C  CB  . VAL A 142 ? 0.1414 0.0989 0.1256 0.0251  0.0060  -0.0124 143 VAL A CB  
1162 C  CG1 . VAL A 142 ? 0.1630 0.1562 0.1118 0.0527  -0.0016 -0.0303 143 VAL A CG1 
1163 C  CG2 . VAL A 142 ? 0.1324 0.1856 0.1135 0.0192  0.0031  0.0078  143 VAL A CG2 
1164 N  N   . LEU A 143 ? 0.1273 0.0781 0.1219 0.0052  0.0006  -0.0100 144 LEU A N   
1165 C  CA  . LEU A 143 ? 0.1323 0.0734 0.1292 0.0026  0.0037  -0.0012 144 LEU A CA  
1166 C  C   . LEU A 143 ? 0.1381 0.0761 0.0991 -0.0103 0.0060  -0.0016 144 LEU A C   
1167 O  O   . LEU A 143 ? 0.1637 0.0880 0.1043 -0.0128 0.0076  -0.0006 144 LEU A O   
1168 C  CB  . LEU A 143 ? 0.1540 0.1176 0.1341 -0.0070 -0.0058 0.0091  144 LEU A CB  
1169 C  CG  . LEU A 143 ? 0.1551 0.1324 0.1572 -0.0161 0.0064  -0.0062 144 LEU A CG  
1170 C  CD1 . LEU A 143 ? 0.1927 0.2235 0.1779 -0.0189 -0.0046 0.0509  144 LEU A CD1 
1171 C  CD2 . LEU A 143 ? 0.1400 0.1827 0.2139 0.0152  -0.0032 -0.0032 144 LEU A CD2 
1172 N  N   . GLY A 144 ? 0.1364 0.0680 0.1199 -0.0136 0.0058  0.0025  145 GLY A N   
1173 C  CA  . GLY A 144 ? 0.1250 0.0790 0.1342 0.0008  0.0021  -0.0059 145 GLY A CA  
1174 C  C   . GLY A 144 ? 0.1248 0.0826 0.1018 -0.0020 0.0098  0.0010  145 GLY A C   
1175 O  O   . GLY A 144 ? 0.1443 0.0946 0.1129 -0.0091 0.0198  -0.0013 145 GLY A O   
1176 N  N   . ILE A 145 ? 0.1186 0.0786 0.1047 0.0021  0.0054  -0.0099 146 ILE A N   
1177 C  CA  . ILE A 145 ? 0.1137 0.0851 0.1141 -0.0027 0.0076  -0.0044 146 ILE A CA  
1178 C  C   . ILE A 145 ? 0.1092 0.0815 0.1111 -0.0024 -0.0019 0.0006  146 ILE A C   
1179 O  O   . ILE A 145 ? 0.1250 0.0858 0.1222 0.0003  0.0163  -0.0015 146 ILE A O   
1180 C  CB  . ILE A 145 ? 0.1113 0.0925 0.1165 0.0044  0.0037  0.0071  146 ILE A CB  
1181 C  CG1 . ILE A 145 ? 0.1420 0.1181 0.1398 0.0348  0.0020  -0.0015 146 ILE A CG1 
1182 C  CG2 . ILE A 145 ? 0.1298 0.1054 0.1974 -0.0059 -0.0261 -0.0010 146 ILE A CG2 
1183 C  CD1 . ILE A 145 ? 0.1457 0.1025 0.1691 0.0212  -0.0091 0.0081  146 ILE A CD1 
1184 N  N   . PHE A 146 ? 0.1237 0.0732 0.1102 0.0044  -0.0019 0.0020  147 PHE A N   
1185 C  CA  . PHE A 146 ? 0.1168 0.0743 0.1272 0.0176  0.0042  0.0015  147 PHE A CA  
1186 C  C   . PHE A 146 ? 0.1168 0.0709 0.1335 -0.0038 0.0015  0.0006  147 PHE A C   
1187 O  O   . PHE A 146 ? 0.1206 0.1025 0.1488 0.0048  0.0002  -0.0092 147 PHE A O   
1188 C  CB  . PHE A 146 ? 0.1452 0.0707 0.1360 0.0122  -0.0004 0.0121  147 PHE A CB  
1189 C  CG  . PHE A 146 ? 0.1320 0.0835 0.1289 0.0066  -0.0003 0.0138  147 PHE A CG  
1190 C  CD1 . PHE A 146 ? 0.1296 0.0967 0.1407 0.0237  -0.0030 -0.0054 147 PHE A CD1 
1191 C  CD2 . PHE A 146 ? 0.1452 0.0791 0.1332 0.0154  -0.0030 0.0158  147 PHE A CD2 
1192 C  CE1 . PHE A 146 ? 0.1443 0.1090 0.1059 0.0064  0.0000  -0.0018 147 PHE A CE1 
1193 C  CE2 . PHE A 146 ? 0.1461 0.0856 0.1303 0.0164  0.0004  0.0064  147 PHE A CE2 
1194 C  CZ  . PHE A 146 ? 0.1429 0.0971 0.1187 -0.0052 0.0093  0.0122  147 PHE A CZ  
1195 N  N   . LEU A 147 ? 0.1286 0.0767 0.1226 0.0036  0.0022  -0.0120 148 LEU A N   
1196 C  CA  . LEU A 147 ? 0.1502 0.0750 0.1192 0.0021  -0.0074 -0.0089 148 LEU A CA  
1197 C  C   . LEU A 147 ? 0.1301 0.0824 0.1355 0.0019  0.0034  -0.0070 148 LEU A C   
1198 O  O   . LEU A 147 ? 0.1319 0.0880 0.1684 0.0111  -0.0086 0.0030  148 LEU A O   
1199 C  CB  . LEU A 147 ? 0.1283 0.0888 0.1327 0.0206  0.0098  -0.0109 148 LEU A CB  
1200 C  CG  . LEU A 147 ? 0.1654 0.0772 0.1316 0.0009  -0.0059 -0.0087 148 LEU A CG  
1201 C  CD1 . LEU A 147 ? 0.2179 0.0844 0.1565 0.0172  -0.0203 -0.0221 148 LEU A CD1 
1202 C  CD2 . LEU A 147 ? 0.1510 0.1011 0.1374 -0.0010 -0.0024 0.0044  148 LEU A CD2 
1203 N  N   . LYS A 148 ? 0.1474 0.0786 0.1632 -0.0158 -0.0082 0.0057  149 LYS A N   
1204 C  CA  . LYS A 148 ? 0.1799 0.0815 0.1493 -0.0008 -0.0211 -0.0027 149 LYS A CA  
1205 C  C   . LYS A 148 ? 0.1388 0.1093 0.1647 0.0135  -0.0328 0.0047  149 LYS A C   
1206 O  O   . LYS A 148 ? 0.1741 0.1269 0.1694 0.0356  -0.0439 -0.0076 149 LYS A O   
1207 C  CB  . LYS A 148 ? 0.2059 0.1303 0.1793 -0.0296 -0.0317 0.0342  149 LYS A CB  
1208 C  CG  . LYS A 148 ? 0.2183 0.1754 0.1791 -0.0237 -0.0348 0.0397  149 LYS A CG  
1209 C  CD  . LYS A 148 ? 0.3072 0.2276 0.2625 -0.0576 0.0221  0.0447  149 LYS A CD  
1210 C  CE  . LYS A 148 ? 0.3431 0.5238 0.2846 -0.1518 0.0039  0.1054  149 LYS A CE  
1211 N  NZ  . LYS A 148 ? 0.4850 0.6190 0.5159 -0.2800 0.1335  0.1892  149 LYS A NZ  
1212 N  N   . VAL A 149 ? 0.1953 0.0891 0.1744 0.0221  -0.0391 -0.0074 150 VAL A N   
1213 C  CA  . VAL A 149 ? 0.1888 0.0923 0.1612 0.0091  -0.0290 -0.0100 150 VAL A CA  
1214 C  C   . VAL A 149 ? 0.2175 0.0788 0.1848 0.0031  -0.0555 0.0041  150 VAL A C   
1215 O  O   . VAL A 149 ? 0.2537 0.0979 0.2229 -0.0078 -0.0657 0.0082  150 VAL A O   
1216 C  CB  . VAL A 149 ? 0.1989 0.1149 0.1756 0.0315  -0.0299 -0.0100 150 VAL A CB  
1217 C  CG1 . VAL A 149 ? 0.2330 0.1754 0.1623 0.0274  -0.0439 -0.0261 150 VAL A CG1 
1218 C  CG2 . VAL A 149 ? 0.1977 0.1902 0.2287 -0.0066 -0.0091 -0.0051 150 VAL A CG2 
1219 N  N   . GLY A 150 ? 0.1856 0.0951 0.1751 0.0025  -0.0453 -0.0070 151 GLY A N   
1220 C  CA  . GLY A 150 ? 0.2104 0.1164 0.1939 -0.0267 -0.0573 0.0181  151 GLY A CA  
1221 C  C   . GLY A 150 ? 0.2063 0.1093 0.1705 -0.0302 -0.0362 0.0025  151 GLY A C   
1222 O  O   . GLY A 150 ? 0.1747 0.1172 0.1847 -0.0195 -0.0271 0.0071  151 GLY A O   
1223 N  N   A SER A 151 ? 0.1963 0.1413 0.1999 -0.0053 -0.0252 0.0023  152 SER A N   
1224 N  N   B SER A 151 ? 0.1874 0.1357 0.1906 -0.0164 -0.0375 -0.0152 152 SER A N   
1225 C  CA  A SER A 151 ? 0.1637 0.1485 0.2467 -0.0365 -0.0297 0.0154  152 SER A CA  
1226 C  CA  B SER A 151 ? 0.1773 0.1368 0.2055 -0.0318 -0.0221 -0.0100 152 SER A CA  
1227 C  C   A SER A 151 ? 0.1797 0.1165 0.1653 -0.0185 -0.0079 -0.0294 152 SER A C   
1228 C  C   B SER A 151 ? 0.1560 0.1265 0.1669 -0.0049 0.0059  -0.0227 152 SER A C   
1229 O  O   A SER A 151 ? 0.1691 0.1279 0.1461 -0.0392 -0.0353 0.0098  152 SER A O   
1230 O  O   B SER A 151 ? 0.1630 0.1254 0.1763 0.0029  -0.0055 -0.0403 152 SER A O   
1231 C  CB  A SER A 151 ? 0.2017 0.2222 0.2637 -0.0511 0.0188  -0.0429 152 SER A CB  
1232 C  CB  B SER A 151 ? 0.1934 0.1201 0.2468 -0.0050 -0.0160 -0.0381 152 SER A CB  
1233 O  OG  A SER A 151 ? 0.2759 0.2631 0.2640 -0.0400 0.0167  -0.0538 152 SER A OG  
1234 O  OG  B SER A 151 ? 0.2056 0.2533 0.3397 -0.0359 0.0036  0.0805  152 SER A OG  
1235 N  N   . ALA A 152 ? 0.1758 0.1129 0.1694 -0.0075 -0.0261 -0.0316 153 ALA A N   
1236 C  CA  . ALA A 152 ? 0.1676 0.1088 0.1736 0.0005  -0.0268 -0.0110 153 ALA A CA  
1237 C  C   . ALA A 152 ? 0.1436 0.1249 0.1841 0.0088  -0.0240 -0.0031 153 ALA A C   
1238 O  O   . ALA A 152 ? 0.1565 0.1267 0.2186 -0.0225 0.0029  -0.0208 153 ALA A O   
1239 C  CB  . ALA A 152 ? 0.2165 0.1243 0.1845 0.0140  -0.0394 -0.0160 153 ALA A CB  
1240 N  N   . LYS A 153 ? 0.1359 0.1000 0.1757 0.0086  -0.0217 0.0060  154 LYS A N   
1241 C  CA  . LYS A 153 ? 0.1363 0.1059 0.1586 0.0131  -0.0107 -0.0003 154 LYS A CA  
1242 C  C   . LYS A 153 ? 0.1423 0.1179 0.1550 0.0271  -0.0053 -0.0164 154 LYS A C   
1243 O  O   . LYS A 153 ? 0.1384 0.1153 0.1518 0.0068  -0.0120 -0.0077 154 LYS A O   
1244 C  CB  . LYS A 153 ? 0.1517 0.0858 0.1729 0.0026  -0.0199 0.0092  154 LYS A CB  
1245 C  CG  . LYS A 153 ? 0.1816 0.1156 0.1745 0.0236  0.0001  -0.0042 154 LYS A CG  
1246 C  CD  . LYS A 153 ? 0.2113 0.1443 0.1707 0.0052  0.0275  -0.0168 154 LYS A CD  
1247 C  CE  . LYS A 153 ? 0.3363 0.1404 0.2020 0.0533  0.0366  0.0008  154 LYS A CE  
1248 N  NZ  . LYS A 153 ? 0.5186 0.2246 0.2778 0.0174  0.1745  -0.0284 154 LYS A NZ  
1249 N  N   . PRO A 154 ? 0.1362 0.1239 0.1587 -0.0015 -0.0100 0.0034  155 PRO A N   
1250 C  CA  . PRO A 154 ? 0.1368 0.1730 0.1678 -0.0031 -0.0178 0.0179  155 PRO A CA  
1251 C  C   . PRO A 154 ? 0.1326 0.1751 0.1619 0.0211  -0.0027 0.0185  155 PRO A C   
1252 O  O   . PRO A 154 ? 0.1490 0.1842 0.1622 0.0254  -0.0115 0.0149  155 PRO A O   
1253 C  CB  . PRO A 154 ? 0.1251 0.2108 0.2322 -0.0190 -0.0269 0.0391  155 PRO A CB  
1254 C  CG  . PRO A 154 ? 0.1863 0.2328 0.2437 -0.0038 -0.0411 0.0530  155 PRO A CG  
1255 C  CD  . PRO A 154 ? 0.1540 0.1777 0.1969 -0.0050 -0.0108 0.0490  155 PRO A CD  
1256 N  N   . GLY A 155 ? 0.1260 0.1267 0.1932 0.0143  0.0091  0.0048  156 GLY A N   
1257 C  CA  . GLY A 155 ? 0.1614 0.1269 0.2224 0.0013  0.0283  0.0408  156 GLY A CA  
1258 C  C   . GLY A 155 ? 0.1402 0.1080 0.1923 0.0030  0.0077  0.0047  156 GLY A C   
1259 O  O   . GLY A 155 ? 0.1579 0.1128 0.2514 0.0151  0.0212  0.0215  156 GLY A O   
1260 N  N   . LEU A 156 ? 0.1353 0.1000 0.1630 0.0091  0.0077  -0.0063 157 LEU A N   
1261 C  CA  . LEU A 156 ? 0.1375 0.1183 0.1349 0.0037  0.0110  0.0008  157 LEU A CA  
1262 C  C   . LEU A 156 ? 0.1386 0.1038 0.1252 0.0051  -0.0002 0.0020  157 LEU A C   
1263 O  O   . LEU A 156 ? 0.1300 0.1204 0.1404 -0.0035 -0.0052 0.0100  157 LEU A O   
1264 C  CB  . LEU A 156 ? 0.1414 0.1370 0.1551 0.0166  -0.0135 0.0005  157 LEU A CB  
1265 C  CG  . LEU A 156 ? 0.1382 0.1307 0.1514 -0.0006 -0.0161 0.0083  157 LEU A CG  
1266 C  CD1 . LEU A 156 ? 0.1639 0.1416 0.1643 -0.0178 -0.0141 0.0065  157 LEU A CD1 
1267 C  CD2 . LEU A 156 ? 0.1766 0.1587 0.1708 0.0190  -0.0294 0.0024  157 LEU A CD2 
1268 N  N   . GLN A 157 ? 0.1403 0.1120 0.1395 0.0071  -0.0165 -0.0012 158 GLN A N   
1269 C  CA  . GLN A 157 ? 0.1377 0.1230 0.1540 -0.0275 0.0077  -0.0072 158 GLN A CA  
1270 C  C   . GLN A 157 ? 0.1160 0.1163 0.1500 0.0027  -0.0071 -0.0072 158 GLN A C   
1271 O  O   . GLN A 157 ? 0.1224 0.1443 0.1465 -0.0027 -0.0051 -0.0065 158 GLN A O   
1272 C  CB  . GLN A 157 ? 0.1279 0.1553 0.1589 -0.0114 -0.0178 -0.0226 158 GLN A CB  
1273 C  CG  . GLN A 157 ? 0.1817 0.1454 0.1632 -0.0027 -0.0303 -0.0214 158 GLN A CG  
1274 C  CD  . GLN A 157 ? 0.1894 0.1442 0.1270 0.0027  -0.0135 -0.0087 158 GLN A CD  
1275 O  OE1 . GLN A 157 ? 0.2138 0.1371 0.1344 -0.0117 -0.0171 -0.0083 158 GLN A OE1 
1276 N  NE2 . GLN A 157 ? 0.2050 0.1812 0.1526 -0.0418 0.0012  -0.0168 158 GLN A NE2 
1277 N  N   . LYS A 158 ? 0.1421 0.1208 0.1560 0.0128  -0.0217 0.0059  159 LYS A N   
1278 C  CA  . LYS A 158 ? 0.1395 0.1144 0.1858 -0.0035 -0.0201 0.0109  159 LYS A CA  
1279 C  C   . LYS A 158 ? 0.1529 0.1037 0.1517 0.0061  -0.0111 0.0005  159 LYS A C   
1280 O  O   . LYS A 158 ? 0.1736 0.1511 0.1522 -0.0177 -0.0271 0.0228  159 LYS A O   
1281 C  CB  . LYS A 158 ? 0.1826 0.1342 0.2129 0.0347  -0.0405 0.0154  159 LYS A CB  
1282 C  CG  . LYS A 158 ? 0.2917 0.1395 0.2445 0.0266  -0.0509 0.0075  159 LYS A CG  
1283 C  CD  . LYS A 158 ? 0.3668 0.2610 0.2167 0.1195  -0.0422 0.0098  159 LYS A CD  
1284 C  CE  . LYS A 158 ? 0.4432 0.3544 0.3312 -0.0403 -0.0890 0.0856  159 LYS A CE  
1285 N  NZ  . LYS A 158 ? 0.2614 0.2896 0.2762 0.0460  0.0152  0.0692  159 LYS A NZ  
1286 N  N   . VAL A 159 ? 0.1393 0.1029 0.1439 0.0161  -0.0211 -0.0128 160 VAL A N   
1287 C  CA  . VAL A 159 ? 0.1363 0.1004 0.1574 -0.0031 -0.0192 -0.0074 160 VAL A CA  
1288 C  C   . VAL A 159 ? 0.1208 0.0971 0.1454 -0.0115 -0.0226 0.0086  160 VAL A C   
1289 O  O   . VAL A 159 ? 0.1424 0.1138 0.1655 -0.0108 0.0001  0.0081  160 VAL A O   
1290 C  CB  . VAL A 159 ? 0.1544 0.1181 0.1657 0.0089  -0.0419 -0.0009 160 VAL A CB  
1291 C  CG1 . VAL A 159 ? 0.1549 0.1608 0.2128 -0.0252 -0.0584 0.0238  160 VAL A CG1 
1292 C  CG2 . VAL A 159 ? 0.2244 0.1360 0.1932 0.0472  -0.0551 -0.0413 160 VAL A CG2 
1293 N  N   . VAL A 160 ? 0.1474 0.0781 0.1479 0.0012  -0.0160 0.0006  161 VAL A N   
1294 C  CA  . VAL A 160 ? 0.1881 0.0977 0.1845 0.0260  0.0217  0.0001  161 VAL A CA  
1295 C  C   . VAL A 160 ? 0.1377 0.0840 0.1680 -0.0134 0.0098  -0.0059 161 VAL A C   
1296 O  O   . VAL A 160 ? 0.1536 0.1154 0.1655 -0.0002 0.0257  -0.0034 161 VAL A O   
1297 C  CB  . VAL A 160 ? 0.2409 0.1120 0.2186 0.0302  0.0019  -0.0205 161 VAL A CB  
1298 C  CG1 . VAL A 160 ? 0.3388 0.1999 0.1820 0.0365  0.0499  0.0493  161 VAL A CG1 
1299 C  CG2 . VAL A 160 ? 0.1765 0.1817 0.2697 0.0681  0.0037  -0.0499 161 VAL A CG2 
1300 N  N   . ASP A 161 ? 0.1417 0.1174 0.1385 -0.0207 0.0030  -0.0114 162 ASP A N   
1301 C  CA  . ASP A 161 ? 0.1463 0.1605 0.1461 -0.0379 0.0038  0.0055  162 ASP A CA  
1302 C  C   . ASP A 161 ? 0.1284 0.1612 0.1551 -0.0306 0.0204  -0.0100 162 ASP A C   
1303 O  O   . ASP A 161 ? 0.2073 0.2361 0.1684 -0.0638 0.0365  -0.0091 162 ASP A O   
1304 C  CB  . ASP A 161 ? 0.1680 0.1745 0.1883 -0.0378 -0.0116 0.0037  162 ASP A CB  
1305 C  CG  . ASP A 161 ? 0.1770 0.1644 0.2129 -0.0230 -0.0026 -0.0068 162 ASP A CG  
1306 O  OD1 . ASP A 161 ? 0.2414 0.1730 0.2681 -0.0359 -0.0179 -0.0148 162 ASP A OD1 
1307 O  OD2 . ASP A 161 ? 0.1975 0.2556 0.2074 -0.0527 -0.0152 -0.0255 162 ASP A OD2 
1308 N  N   . VAL A 162 ? 0.1367 0.1318 0.1741 -0.0355 -0.0231 0.0150  163 VAL A N   
1309 C  CA  . VAL A 162 ? 0.1542 0.1259 0.1989 -0.0281 -0.0228 0.0293  163 VAL A CA  
1310 C  C   . VAL A 162 ? 0.1339 0.1460 0.1594 -0.0263 -0.0038 0.0295  163 VAL A C   
1311 O  O   . VAL A 162 ? 0.1479 0.1496 0.1436 -0.0257 0.0032  0.0099  163 VAL A O   
1312 C  CB  . VAL A 162 ? 0.1984 0.1364 0.2928 -0.0174 -0.0665 0.0513  163 VAL A CB  
1313 C  CG1 . VAL A 162 ? 0.1694 0.2237 0.3957 0.0079  -0.0168 0.0174  163 VAL A CG1 
1314 C  CG2 . VAL A 162 ? 0.2074 0.0926 0.2701 -0.0189 0.0217  0.0127  163 VAL A CG2 
1315 N  N   . LEU A 163 ? 0.1331 0.1370 0.1490 -0.0161 -0.0118 0.0138  164 LEU A N   
1316 C  CA  . LEU A 163 ? 0.1515 0.1016 0.1601 -0.0097 0.0032  0.0081  164 LEU A CA  
1317 C  C   . LEU A 163 ? 0.1526 0.1324 0.1546 0.0130  -0.0119 -0.0127 164 LEU A C   
1318 O  O   . LEU A 163 ? 0.1536 0.1427 0.1410 -0.0004 0.0021  -0.0010 164 LEU A O   
1319 C  CB  . LEU A 163 ? 0.1497 0.1062 0.1459 0.0030  0.0095  0.0156  164 LEU A CB  
1320 C  CG  . LEU A 163 ? 0.1488 0.1098 0.1280 -0.0001 0.0160  0.0171  164 LEU A CG  
1321 C  CD1 . LEU A 163 ? 0.1560 0.1352 0.1812 0.0061  0.0170  0.0458  164 LEU A CD1 
1322 C  CD2 . LEU A 163 ? 0.1720 0.1298 0.1626 -0.0128 -0.0026 0.0017  164 LEU A CD2 
1323 N  N   . ASP A 164 ? 0.1971 0.1185 0.1338 -0.0229 0.0109  -0.0118 165 ASP A N   
1324 C  CA  . ASP A 164 ? 0.2240 0.1614 0.1679 -0.0333 0.0449  -0.0301 165 ASP A CA  
1325 C  C   . ASP A 164 ? 0.1863 0.1793 0.1417 -0.0089 0.0148  0.0083  165 ASP A C   
1326 O  O   . ASP A 164 ? 0.2538 0.1957 0.2093 -0.0044 0.0675  -0.0044 165 ASP A O   
1327 C  CB  . ASP A 164 ? 0.2837 0.1738 0.2305 -0.0552 0.0397  -0.0718 165 ASP A CB  
1328 C  CG  . ASP A 164 ? 0.2689 0.3091 0.2998 -0.0425 0.0080  -0.0642 165 ASP A CG  
1329 O  OD1 . ASP A 164 ? 0.2690 0.3840 0.2735 -0.1049 0.0305  -0.0278 165 ASP A OD1 
1330 O  OD2 . ASP A 164 ? 0.4146 0.5335 0.2767 -0.1675 0.0784  -0.1235 165 ASP A OD2 
1331 N  N   . SER A 165 ? 0.1580 0.1745 0.1283 -0.0177 -0.0088 0.0134  166 SER A N   
1332 C  CA  . SER A 165 ? 0.1526 0.1729 0.1464 -0.0276 0.0018  0.0072  166 SER A CA  
1333 C  C   . SER A 165 ? 0.1413 0.1736 0.1293 -0.0187 0.0194  -0.0062 166 SER A C   
1334 O  O   . SER A 165 ? 0.1791 0.1658 0.1639 -0.0381 0.0016  0.0278  166 SER A O   
1335 C  CB  . SER A 165 ? 0.1813 0.2314 0.1763 0.0323  0.0055  0.0048  166 SER A CB  
1336 O  OG  . SER A 165 ? 0.1758 0.1960 0.1835 -0.0071 0.0049  0.0324  166 SER A OG  
1337 N  N   . ILE A 166 ? 0.1303 0.1520 0.1095 -0.0127 0.0089  0.0005  167 ILE A N   
1338 C  CA  . ILE A 166 ? 0.1508 0.1332 0.1269 -0.0068 -0.0037 -0.0027 167 ILE A CA  
1339 C  C   . ILE A 166 ? 0.1256 0.1125 0.1303 -0.0061 0.0193  -0.0027 167 ILE A C   
1340 O  O   . ILE A 166 ? 0.1522 0.1254 0.1286 -0.0084 0.0092  -0.0037 167 ILE A O   
1341 C  CB  . ILE A 166 ? 0.1373 0.1224 0.1262 -0.0114 0.0142  0.0049  167 ILE A CB  
1342 C  CG1 . ILE A 166 ? 0.1363 0.1488 0.1111 -0.0193 0.0070  -0.0030 167 ILE A CG1 
1343 C  CG2 . ILE A 166 ? 0.1658 0.1298 0.1747 -0.0034 -0.0134 0.0051  167 ILE A CG2 
1344 C  CD1 . ILE A 166 ? 0.1576 0.1392 0.1210 -0.0106 0.0069  -0.0104 167 ILE A CD1 
1345 N  N   . LYS A 167 ? 0.1461 0.1158 0.1628 0.0110  0.0157  -0.0074 168 LYS A N   
1346 C  CA  . LYS A 167 ? 0.1601 0.1346 0.1326 0.0176  -0.0053 -0.0127 168 LYS A CA  
1347 C  C   . LYS A 167 ? 0.1587 0.1244 0.1420 0.0096  0.0179  -0.0148 168 LYS A C   
1348 O  O   . LYS A 167 ? 0.1490 0.1720 0.1628 0.0095  -0.0039 0.0093  168 LYS A O   
1349 C  CB  . LYS A 167 ? 0.2239 0.1481 0.1572 0.0239  -0.0126 -0.0500 168 LYS A CB  
1350 C  CG  . LYS A 167 ? 0.2440 0.1360 0.2176 0.0337  -0.0120 -0.0440 168 LYS A CG  
1351 C  CD  . LYS A 167 ? 0.3425 0.1939 0.2570 0.0562  -0.0955 -0.1038 168 LYS A CD  
1352 C  CE  . LYS A 167 ? 0.4698 0.3215 0.5210 0.1411  -0.0908 -0.0146 168 LYS A CE  
1353 N  N   . THR A 168 ? 0.1447 0.1328 0.1637 -0.0003 0.0067  -0.0031 169 THR A N   
1354 C  CA  . THR A 168 ? 0.1644 0.1352 0.1589 -0.0052 0.0179  0.0023  169 THR A CA  
1355 C  C   . THR A 168 ? 0.1421 0.1267 0.1470 -0.0086 0.0247  0.0104  169 THR A C   
1356 O  O   . THR A 168 ? 0.1525 0.1286 0.1630 0.0041  0.0165  -0.0036 169 THR A O   
1357 C  CB  . THR A 168 ? 0.1715 0.1457 0.1765 0.0207  0.0365  0.0168  169 THR A CB  
1358 O  OG1 . THR A 168 ? 0.1668 0.2073 0.1586 0.0120  0.0223  0.0125  169 THR A OG1 
1359 C  CG2 . THR A 168 ? 0.1862 0.1691 0.2024 0.0211  0.0286  -0.0361 169 THR A CG2 
1360 N  N   . LYS A 169 ? 0.1355 0.1456 0.1750 -0.0036 0.0009  -0.0078 170 LYS A N   
1361 C  CA  . LYS A 169 ? 0.1348 0.1212 0.1542 -0.0111 0.0129  0.0053  170 LYS A CA  
1362 C  C   . LYS A 169 ? 0.1201 0.1470 0.1562 -0.0048 0.0277  0.0168  170 LYS A C   
1363 O  O   . LYS A 169 ? 0.1610 0.1794 0.1671 -0.0086 0.0461  0.0254  170 LYS A O   
1364 C  CB  . LYS A 169 ? 0.1399 0.1694 0.1794 0.0002  -0.0093 -0.0088 170 LYS A CB  
1365 C  CG  . LYS A 169 ? 0.1589 0.1475 0.2108 -0.0003 -0.0026 -0.0022 170 LYS A CG  
1366 C  CD  . LYS A 169 ? 0.1791 0.2152 0.2382 0.0121  -0.0285 0.0215  170 LYS A CD  
1367 C  CE  . LYS A 169 ? 0.3175 0.3414 0.4782 -0.1081 -0.1430 -0.0598 170 LYS A CE  
1368 N  NZ  . LYS A 169 ? 0.3144 0.6190 0.6236 0.0115  -0.0973 -0.1454 170 LYS A NZ  
1369 N  N   . GLY A 170 ? 0.1324 0.1201 0.1499 -0.0029 0.0074  0.0041  171 GLY A N   
1370 C  CA  . GLY A 170 ? 0.1544 0.1187 0.2176 -0.0187 -0.0097 0.0249  171 GLY A CA  
1371 C  C   . GLY A 170 ? 0.2125 0.1198 0.1625 -0.0265 -0.0075 0.0256  171 GLY A C   
1372 O  O   . GLY A 170 ? 0.2011 0.1256 0.2350 -0.0316 -0.0244 0.0458  171 GLY A O   
1373 N  N   . LYS A 171 ? 0.1522 0.1151 0.1456 -0.0023 0.0060  0.0158  172 LYS A N   
1374 C  CA  . LYS A 171 ? 0.1368 0.1217 0.1511 -0.0216 0.0152  0.0277  172 LYS A CA  
1375 C  C   . LYS A 171 ? 0.1385 0.1341 0.1378 -0.0216 0.0212  0.0358  172 LYS A C   
1376 O  O   . LYS A 171 ? 0.1582 0.1702 0.1407 0.0159  0.0262  0.0284  172 LYS A O   
1377 C  CB  . LYS A 171 ? 0.1671 0.1338 0.1529 -0.0094 -0.0019 -0.0029 172 LYS A CB  
1378 C  CG  . LYS A 171 ? 0.1714 0.1849 0.2463 0.0068  0.0250  -0.0574 172 LYS A CG  
1379 C  CD  . LYS A 171 ? 0.2398 0.2341 0.2445 -0.0024 0.0203  -0.0432 172 LYS A CD  
1380 C  CE  . LYS A 171 ? 0.3514 0.3176 0.4008 0.0531  -0.0353 0.0684  172 LYS A CE  
1381 N  NZ  . LYS A 171 ? 0.9479 0.3194 0.3718 -0.1066 0.1395  -0.0746 172 LYS A NZ  
1382 N  N   . SER A 172 ? 0.1381 0.1089 0.1441 -0.0120 0.0129  0.0171  173 SER A N   
1383 C  CA  . SER A 172 ? 0.1392 0.1170 0.1389 -0.0003 0.0044  0.0298  173 SER A CA  
1384 C  C   . SER A 172 ? 0.1560 0.1095 0.0971 -0.0069 0.0062  0.0271  173 SER A C   
1385 O  O   . SER A 172 ? 0.1648 0.1745 0.1232 0.0070  0.0223  0.0249  173 SER A O   
1386 C  CB  . SER A 172 ? 0.1831 0.1117 0.1586 -0.0252 0.0223  0.0301  173 SER A CB  
1387 O  OG  . SER A 172 ? 0.1975 0.1352 0.2091 -0.0243 0.0159  0.0387  173 SER A OG  
1388 N  N   . ALA A 173 ? 0.1381 0.1436 0.1303 0.0076  0.0041  0.0190  174 ALA A N   
1389 C  CA  . ALA A 173 ? 0.1481 0.1704 0.1279 0.0205  -0.0096 -0.0051 174 ALA A CA  
1390 C  C   . ALA A 173 ? 0.1508 0.1617 0.1055 0.0049  0.0143  0.0309  174 ALA A C   
1391 O  O   . ALA A 173 ? 0.1745 0.1226 0.1093 0.0188  0.0103  0.0232  174 ALA A O   
1392 C  CB  . ALA A 173 ? 0.1702 0.1629 0.1625 -0.0039 -0.0073 -0.0173 174 ALA A CB  
1393 N  N   A ASP A 174 ? 0.1777 0.1583 0.1350 0.0522  0.0074  0.0317  175 ASP A N   
1394 N  N   B ASP A 174 ? 0.1711 0.1456 0.1217 0.0159  -0.0029 0.0170  175 ASP A N   
1395 C  CA  A ASP A 174 ? 0.1479 0.1772 0.1428 0.0332  0.0053  0.0328  175 ASP A CA  
1396 C  CA  B ASP A 174 ? 0.1532 0.1597 0.1356 -0.0051 0.0125  0.0259  175 ASP A CA  
1397 C  C   A ASP A 174 ? 0.1763 0.1500 0.1381 0.0147  0.0046  -0.0072 175 ASP A C   
1398 C  C   B ASP A 174 ? 0.1787 0.1228 0.1293 0.0031  0.0069  0.0122  175 ASP A C   
1399 O  O   A ASP A 174 ? 0.1765 0.1558 0.1531 0.0170  0.0134  -0.0126 175 ASP A O   
1400 O  O   B ASP A 174 ? 0.1806 0.1661 0.1477 -0.0086 -0.0236 -0.0212 175 ASP A O   
1401 C  CB  A ASP A 174 ? 0.1486 0.2624 0.1770 0.0724  -0.0359 0.0223  175 ASP A CB  
1402 C  CB  B ASP A 174 ? 0.2139 0.1838 0.1090 -0.0124 0.0223  0.0436  175 ASP A CB  
1403 C  CG  A ASP A 174 ? 0.2258 0.2481 0.2829 0.0328  -0.0490 0.0219  175 ASP A CG  
1404 C  CG  B ASP A 174 ? 0.2275 0.1806 0.1908 -0.0127 0.0326  -0.0312 175 ASP A CG  
1405 O  OD1 A ASP A 174 ? 0.3084 0.2834 0.3116 0.0098  0.0571  -0.0326 175 ASP A OD1 
1406 O  OD1 B ASP A 174 ? 0.3411 0.3913 0.2160 0.0002  0.1203  0.0252  175 ASP A OD1 
1407 O  OD2 A ASP A 174 ? 0.3454 0.2706 0.3112 0.0232  -0.0366 -0.0400 175 ASP A OD2 
1408 O  OD2 B ASP A 174 ? 0.2339 0.3625 0.1909 -0.0364 -0.0350 0.0741  175 ASP A OD2 
1409 N  N   . PHE A 175 ? 0.1574 0.1274 0.1150 0.0086  0.0006  0.0106  176 PHE A N   
1410 C  CA  . PHE A 175 ? 0.1612 0.1147 0.1342 -0.0040 -0.0140 0.0040  176 PHE A CA  
1411 C  C   . PHE A 175 ? 0.1680 0.1029 0.1346 -0.0215 -0.0237 0.0162  176 PHE A C   
1412 O  O   . PHE A 175 ? 0.1759 0.1338 0.1326 0.0262  -0.0245 -0.0039 176 PHE A O   
1413 C  CB  . PHE A 175 ? 0.1576 0.1393 0.1368 -0.0118 -0.0073 0.0340  176 PHE A CB  
1414 C  CG  . PHE A 175 ? 0.1303 0.1279 0.1472 0.0051  0.0073  0.0009  176 PHE A CG  
1415 C  CD1 . PHE A 175 ? 0.2196 0.1129 0.1607 0.0178  0.0128  0.0064  176 PHE A CD1 
1416 C  CD2 . PHE A 175 ? 0.1693 0.1360 0.1402 0.0145  -0.0052 0.0389  176 PHE A CD2 
1417 C  CE1 . PHE A 175 ? 0.2075 0.1336 0.1806 0.0013  0.0019  0.0130  176 PHE A CE1 
1418 C  CE2 . PHE A 175 ? 0.1802 0.1113 0.1860 0.0110  -0.0220 0.0211  176 PHE A CE2 
1419 C  CZ  . PHE A 175 ? 0.1955 0.1098 0.1975 0.0220  -0.0134 0.0162  176 PHE A CZ  
1420 N  N   . THR A 176 ? 0.1520 0.1538 0.1251 -0.0032 -0.0168 0.0134  177 THR A N   
1421 C  CA  . THR A 176 ? 0.1465 0.1341 0.1402 0.0036  0.0009  0.0389  177 THR A CA  
1422 C  C   . THR A 176 ? 0.1449 0.1058 0.1295 0.0065  -0.0355 0.0267  177 THR A C   
1423 O  O   . THR A 176 ? 0.1842 0.1167 0.1472 0.0031  -0.0160 0.0133  177 THR A O   
1424 C  CB  . THR A 176 ? 0.1896 0.1865 0.1324 -0.0164 -0.0385 0.0700  177 THR A CB  
1425 O  OG1 . THR A 176 ? 0.2402 0.2068 0.1414 0.0130  -0.0394 0.0608  177 THR A OG1 
1426 C  CG2 . THR A 176 ? 0.2358 0.2532 0.2684 -0.0806 -0.0438 0.1340  177 THR A CG2 
1427 N  N   . ASN A 177 ? 0.1411 0.1160 0.1359 0.0036  -0.0142 0.0146  178 ASN A N   
1428 C  CA  . ASN A 177 ? 0.1497 0.1357 0.1550 -0.0137 -0.0312 0.0337  178 ASN A CA  
1429 C  C   . ASN A 177 ? 0.1766 0.1215 0.1712 -0.0215 -0.0372 0.0376  178 ASN A C   
1430 O  O   . ASN A 177 ? 0.1964 0.1877 0.2441 -0.0496 -0.0709 0.1012  178 ASN A O   
1431 C  CB  . ASN A 177 ? 0.1558 0.1542 0.1535 0.0040  -0.0337 0.0441  178 ASN A CB  
1432 C  CG  . ASN A 177 ? 0.1788 0.1576 0.1533 0.0313  -0.0467 -0.0005 178 ASN A CG  
1433 O  OD1 . ASN A 177 ? 0.1944 0.1715 0.2373 0.0271  0.0234  0.0324  178 ASN A OD1 
1434 N  ND2 . ASN A 177 ? 0.2280 0.1411 0.1479 0.0098  -0.0538 0.0228  178 ASN A ND2 
1435 N  N   . PHE A 178 ? 0.1682 0.1050 0.1328 0.0048  -0.0157 0.0252  179 PHE A N   
1436 C  CA  . PHE A 178 ? 0.1644 0.1071 0.1102 0.0049  -0.0132 0.0298  179 PHE A CA  
1437 C  C   . PHE A 178 ? 0.1811 0.0978 0.1345 -0.0006 -0.0029 0.0242  179 PHE A C   
1438 O  O   . PHE A 178 ? 0.2057 0.1190 0.1427 -0.0134 -0.0106 0.0119  179 PHE A O   
1439 C  CB  . PHE A 178 ? 0.1520 0.1355 0.1411 0.0128  0.0083  0.0522  179 PHE A CB  
1440 C  CG  . PHE A 178 ? 0.1532 0.0944 0.1576 0.0042  0.0037  0.0308  179 PHE A CG  
1441 C  CD1 . PHE A 178 ? 0.2177 0.1117 0.1272 0.0075  -0.0067 0.0226  179 PHE A CD1 
1442 C  CD2 . PHE A 178 ? 0.1368 0.1248 0.1568 0.0116  -0.0088 0.0305  179 PHE A CD2 
1443 C  CE1 . PHE A 178 ? 0.2002 0.1022 0.1524 0.0188  0.0002  0.0294  179 PHE A CE1 
1444 C  CE2 . PHE A 178 ? 0.1446 0.1152 0.1662 0.0124  0.0064  0.0253  179 PHE A CE2 
1445 C  CZ  . PHE A 178 ? 0.1410 0.1208 0.1386 0.0076  0.0193  0.0334  179 PHE A CZ  
1446 N  N   . ASP A 179 ? 0.1391 0.1352 0.1355 0.0070  -0.0005 0.0369  180 ASP A N   
1447 C  CA  . ASP A 179 ? 0.1402 0.1338 0.1474 0.0039  -0.0003 0.0223  180 ASP A CA  
1448 C  C   . ASP A 179 ? 0.1429 0.1268 0.1150 0.0001  0.0216  0.0091  180 ASP A C   
1449 O  O   . ASP A 179 ? 0.1672 0.1208 0.1235 0.0063  0.0002  -0.0001 180 ASP A O   
1450 C  CB  . ASP A 179 ? 0.1421 0.1665 0.1941 -0.0106 0.0017  0.0155  180 ASP A CB  
1451 C  CG  . ASP A 179 ? 0.1633 0.2046 0.1926 0.0314  0.0009  0.0060  180 ASP A CG  
1452 O  OD1 . ASP A 179 ? 0.1716 0.1569 0.1833 0.0336  0.0190  0.0248  180 ASP A OD1 
1453 O  OD2 . ASP A 179 ? 0.1650 0.3877 0.3100 0.0138  0.0200  -0.0613 180 ASP A OD2 
1454 N  N   . PRO A 180 ? 0.1504 0.1088 0.1183 0.0026  -0.0021 0.0168  181 PRO A N   
1455 C  CA  . PRO A 180 ? 0.1558 0.1370 0.1261 -0.0006 -0.0070 0.0151  181 PRO A CA  
1456 C  C   . PRO A 180 ? 0.1274 0.1483 0.1104 0.0043  -0.0075 0.0044  181 PRO A C   
1457 O  O   . PRO A 180 ? 0.1599 0.1544 0.1296 0.0201  -0.0019 0.0138  181 PRO A O   
1458 C  CB  . PRO A 180 ? 0.1470 0.1500 0.1899 -0.0010 -0.0137 0.0100  181 PRO A CB  
1459 C  CG  . PRO A 180 ? 0.1787 0.1402 0.1521 -0.0145 -0.0186 0.0126  181 PRO A CG  
1460 C  CD  . PRO A 180 ? 0.1791 0.1217 0.1353 -0.0139 -0.0096 0.0148  181 PRO A CD  
1461 N  N   . ARG A 181 ? 0.1344 0.1459 0.1425 0.0115  0.0117  0.0079  182 ARG A N   
1462 C  CA  . ARG A 181 ? 0.1429 0.1277 0.1287 0.0181  0.0155  0.0075  182 ARG A CA  
1463 C  C   . ARG A 181 ? 0.1603 0.1199 0.1395 0.0319  0.0005  0.0216  182 ARG A C   
1464 O  O   . ARG A 181 ? 0.1632 0.1307 0.1736 0.0110  0.0124  0.0201  182 ARG A O   
1465 C  CB  . ARG A 181 ? 0.1452 0.1151 0.1908 0.0242  0.0243  -0.0118 182 ARG A CB  
1466 C  CG  . ARG A 181 ? 0.2063 0.1303 0.1969 0.0357  0.0608  -0.0075 182 ARG A CG  
1467 C  CD  . ARG A 181 ? 0.2185 0.1327 0.2479 0.0476  0.0936  0.0298  182 ARG A CD  
1468 N  NE  . ARG A 181 ? 0.1970 0.1366 0.2594 0.0209  0.0466  0.0291  182 ARG A NE  
1469 C  CZ  . ARG A 181 ? 0.1923 0.1637 0.2780 0.0363  0.0544  0.0369  182 ARG A CZ  
1470 N  NH1 . ARG A 181 ? 0.2381 0.2649 0.3734 0.0719  0.1027  0.0263  182 ARG A NH1 
1471 N  NH2 . ARG A 181 ? 0.2467 0.2147 0.3136 0.0567  -0.0084 0.0575  182 ARG A NH2 
1472 N  N   . GLY A 182 ? 0.1639 0.1287 0.1345 0.0198  -0.0064 -0.0046 183 GLY A N   
1473 C  CA  . GLY A 182 ? 0.1824 0.1288 0.1514 0.0373  0.0041  -0.0018 183 GLY A CA  
1474 C  C   . GLY A 182 ? 0.1970 0.1253 0.1456 0.0469  0.0106  0.0135  183 GLY A C   
1475 O  O   . GLY A 182 ? 0.1987 0.1327 0.1689 0.0131  -0.0100 0.0121  183 GLY A O   
1476 N  N   . LEU A 183 ? 0.1567 0.1431 0.1474 0.0301  0.0089  0.0165  184 LEU A N   
1477 C  CA  . LEU A 183 ? 0.1611 0.1243 0.1562 0.0161  0.0116  0.0297  184 LEU A CA  
1478 C  C   . LEU A 183 ? 0.1522 0.1364 0.1528 0.0194  0.0158  0.0259  184 LEU A C   
1479 O  O   . LEU A 183 ? 0.1629 0.1418 0.1612 0.0336  0.0109  0.0269  184 LEU A O   
1480 C  CB  . LEU A 183 ? 0.1471 0.1524 0.1375 0.0271  0.0016  0.0396  184 LEU A CB  
1481 C  CG  . LEU A 183 ? 0.1569 0.1682 0.1363 0.0436  0.0030  0.0294  184 LEU A CG  
1482 C  CD1 . LEU A 183 ? 0.1626 0.2368 0.1705 0.0029  -0.0057 0.0748  184 LEU A CD1 
1483 C  CD2 . LEU A 183 ? 0.2287 0.1640 0.1878 0.0757  0.0281  0.0021  184 LEU A CD2 
1484 N  N   . LEU A 184 ? 0.1504 0.1418 0.1279 0.0063  0.0141  0.0126  185 LEU A N   
1485 C  CA  . LEU A 184 ? 0.1824 0.1289 0.1244 0.0035  0.0185  0.0018  185 LEU A CA  
1486 C  C   . LEU A 184 ? 0.1741 0.1481 0.1180 -0.0081 -0.0064 0.0037  185 LEU A C   
1487 O  O   . LEU A 184 ? 0.2264 0.1654 0.1799 -0.0419 -0.0605 0.0300  185 LEU A O   
1488 C  CB  . LEU A 184 ? 0.1608 0.1201 0.1540 -0.0083 0.0270  0.0047  185 LEU A CB  
1489 C  CG  . LEU A 184 ? 0.1212 0.1524 0.2036 -0.0013 0.0132  0.0190  185 LEU A CG  
1490 C  CD1 . LEU A 184 ? 0.1653 0.1215 0.2552 -0.0099 0.0356  0.0075  185 LEU A CD1 
1491 C  CD2 . LEU A 184 ? 0.1514 0.1526 0.2863 -0.0058 -0.0422 0.0353  185 LEU A CD2 
1492 N  N   . PRO A 185 ? 0.1474 0.1384 0.1346 0.0227  -0.0019 0.0067  186 PRO A N   
1493 C  CA  . PRO A 185 ? 0.1593 0.1296 0.1407 0.0091  0.0129  0.0209  186 PRO A CA  
1494 C  C   . PRO A 185 ? 0.1330 0.1127 0.1239 0.0037  -0.0118 0.0098  186 PRO A C   
1495 O  O   . PRO A 185 ? 0.1411 0.1120 0.2034 0.0141  -0.0105 0.0167  186 PRO A O   
1496 C  CB  . PRO A 185 ? 0.1511 0.1443 0.2088 0.0130  -0.0193 0.0222  186 PRO A CB  
1497 C  CG  . PRO A 185 ? 0.1396 0.1409 0.1511 0.0178  -0.0100 0.0100  186 PRO A CG  
1498 C  CD  . PRO A 185 ? 0.1418 0.1515 0.1235 0.0181  -0.0011 -0.0021 186 PRO A CD  
1499 N  N   . GLU A 186 ? 0.1550 0.1424 0.1524 -0.0111 0.0005  0.0179  187 GLU A N   
1500 C  CA  . GLU A 186 ? 0.1423 0.1597 0.1547 -0.0187 0.0013  0.0117  187 GLU A CA  
1501 C  C   . GLU A 186 ? 0.1210 0.1544 0.1524 -0.0008 0.0039  0.0117  187 GLU A C   
1502 O  O   . GLU A 186 ? 0.1356 0.1793 0.2077 0.0219  -0.0016 -0.0092 187 GLU A O   
1503 C  CB  . GLU A 186 ? 0.1772 0.1763 0.2326 -0.0524 -0.0138 0.0348  187 GLU A CB  
1504 C  CG  . GLU A 186 ? 0.2109 0.2055 0.2598 -0.0463 -0.0555 0.0341  187 GLU A CG  
1505 C  CD  . GLU A 186 ? 0.2093 0.1927 0.2423 -0.0063 -0.0008 0.0212  187 GLU A CD  
1506 O  OE1 . GLU A 186 ? 0.2210 0.2251 0.3242 -0.0491 -0.0291 0.0717  187 GLU A OE1 
1507 O  OE2 . GLU A 186 ? 0.2934 0.2337 0.3883 -0.0443 -0.0790 -0.0113 187 GLU A OE2 
1508 N  N   . SER A 187 ? 0.1228 0.1820 0.1682 -0.0129 -0.0183 0.0241  188 SER A N   
1509 C  CA  . SER A 187 ? 0.1583 0.1802 0.1673 -0.0284 -0.0282 0.0168  188 SER A CA  
1510 C  C   . SER A 187 ? 0.1138 0.1835 0.1743 -0.0006 -0.0096 0.0015  188 SER A C   
1511 O  O   . SER A 187 ? 0.1256 0.2050 0.1784 0.0000  0.0020  -0.0222 188 SER A O   
1512 C  CB  . SER A 187 ? 0.1604 0.2269 0.1641 -0.0077 -0.0269 0.0389  188 SER A CB  
1513 O  OG  . SER A 187 ? 0.1650 0.2351 0.1769 -0.0302 -0.0223 0.0302  188 SER A OG  
1514 N  N   . LEU A 188 ? 0.1414 0.1655 0.1815 -0.0043 0.0013  -0.0055 189 LEU A N   
1515 C  CA  . LEU A 188 ? 0.1459 0.1571 0.1770 -0.0134 -0.0266 -0.0238 189 LEU A CA  
1516 C  C   . LEU A 188 ? 0.1267 0.1939 0.1738 -0.0127 0.0055  -0.0324 189 LEU A C   
1517 O  O   . LEU A 188 ? 0.1562 0.2297 0.1974 -0.0267 -0.0221 -0.0466 189 LEU A O   
1518 C  CB  . LEU A 188 ? 0.1630 0.1747 0.2121 -0.0024 -0.0265 -0.0328 189 LEU A CB  
1519 C  CG  . LEU A 188 ? 0.1556 0.1740 0.1969 -0.0185 -0.0182 -0.0078 189 LEU A CG  
1520 C  CD1 . LEU A 188 ? 0.1908 0.1633 0.3251 -0.0011 -0.0511 -0.0077 189 LEU A CD1 
1521 C  CD2 . LEU A 188 ? 0.1747 0.2624 0.2018 -0.0431 0.0175  0.0162  189 LEU A CD2 
1522 N  N   . ASP A 189 ? 0.1270 0.2225 0.1411 0.0108  0.0035  -0.0161 190 ASP A N   
1523 C  CA  . ASP A 189 ? 0.1167 0.2348 0.1270 -0.0405 0.0053  -0.0071 190 ASP A CA  
1524 C  C   . ASP A 189 ? 0.1303 0.1805 0.1226 -0.0100 0.0129  0.0020  190 ASP A C   
1525 O  O   . ASP A 189 ? 0.1254 0.1689 0.1339 -0.0054 0.0036  -0.0124 190 ASP A O   
1526 C  CB  . ASP A 189 ? 0.1741 0.3166 0.1407 -0.1096 0.0313  0.0220  190 ASP A CB  
1527 C  CG  . ASP A 189 ? 0.1757 0.3774 0.2018 -0.0965 0.0216  -0.0127 190 ASP A CG  
1528 O  OD1 . ASP A 189 ? 0.2914 0.5168 0.3455 -0.0941 0.0791  -0.0754 190 ASP A OD1 
1529 O  OD2 . ASP A 189 ? 0.2827 0.5225 0.2825 -0.1448 -0.0388 0.1326  190 ASP A OD2 
1530 N  N   . TYR A 190 ? 0.1208 0.1840 0.1237 -0.0207 0.0099  0.0037  191 TYR A N   
1531 C  CA  . TYR A 190 ? 0.1278 0.1662 0.1034 -0.0221 0.0069  0.0080  191 TYR A CA  
1532 C  C   . TYR A 190 ? 0.1263 0.1424 0.0989 0.0044  0.0148  0.0116  191 TYR A C   
1533 O  O   . TYR A 190 ? 0.1425 0.1955 0.1049 -0.0130 0.0198  -0.0064 191 TYR A O   
1534 C  CB  . TYR A 190 ? 0.1432 0.1482 0.1350 -0.0055 0.0107  0.0049  191 TYR A CB  
1535 C  CG  . TYR A 190 ? 0.1197 0.1432 0.1357 0.0019  0.0135  0.0125  191 TYR A CG  
1536 C  CD1 . TYR A 190 ? 0.1529 0.1650 0.1522 -0.0116 -0.0006 -0.0018 191 TYR A CD1 
1537 C  CD2 . TYR A 190 ? 0.1414 0.1673 0.1316 0.0215  0.0272  0.0139  191 TYR A CD2 
1538 C  CE1 . TYR A 190 ? 0.1539 0.1676 0.1500 -0.0037 -0.0151 0.0017  191 TYR A CE1 
1539 C  CE2 . TYR A 190 ? 0.1502 0.1816 0.1486 0.0042  0.0037  -0.0168 191 TYR A CE2 
1540 C  CZ  . TYR A 190 ? 0.1693 0.1888 0.1540 0.0078  -0.0038 -0.0190 191 TYR A CZ  
1541 O  OH  . TYR A 190 ? 0.2039 0.1883 0.1996 0.0261  -0.0113 -0.0328 191 TYR A OH  
1542 N  N   . TRP A 191 ? 0.1189 0.1271 0.1081 0.0064  0.0004  -0.0044 192 TRP A N   
1543 C  CA  . TRP A 191 ? 0.1293 0.1362 0.0892 0.0016  0.0009  -0.0071 192 TRP A CA  
1544 C  C   . TRP A 191 ? 0.1307 0.1438 0.0693 0.0068  -0.0009 -0.0096 192 TRP A C   
1545 O  O   . TRP A 191 ? 0.1725 0.1580 0.0811 -0.0278 -0.0013 -0.0080 192 TRP A O   
1546 C  CB  . TRP A 191 ? 0.1296 0.1235 0.1275 -0.0047 0.0041  -0.0108 192 TRP A CB  
1547 C  CG  . TRP A 191 ? 0.1445 0.1242 0.1280 0.0111  -0.0079 0.0116  192 TRP A CG  
1548 C  CD1 . TRP A 191 ? 0.1750 0.1288 0.1432 0.0249  -0.0029 0.0145  192 TRP A CD1 
1549 C  CD2 . TRP A 191 ? 0.1262 0.1421 0.1482 0.0081  -0.0021 0.0092  192 TRP A CD2 
1550 N  NE1 . TRP A 191 ? 0.1931 0.1357 0.1599 0.0117  0.0125  0.0204  192 TRP A NE1 
1551 C  CE2 . TRP A 191 ? 0.1733 0.1314 0.1578 0.0108  0.0013  0.0070  192 TRP A CE2 
1552 C  CE3 . TRP A 191 ? 0.1503 0.1434 0.1486 0.0100  -0.0044 -0.0147 192 TRP A CE3 
1553 C  CZ2 . TRP A 191 ? 0.1653 0.1305 0.1738 0.0051  -0.0125 0.0118  192 TRP A CZ2 
1554 C  CZ3 . TRP A 191 ? 0.1490 0.1518 0.1694 -0.0013 0.0155  -0.0139 192 TRP A CZ3 
1555 C  CH2 . TRP A 191 ? 0.1447 0.1630 0.1811 0.0000  -0.0068 0.0029  192 TRP A CH2 
1556 N  N   . THR A 192 ? 0.1199 0.1416 0.0988 -0.0062 -0.0042 -0.0129 193 THR A N   
1557 C  CA  . THR A 192 ? 0.1219 0.1306 0.0895 -0.0042 -0.0027 -0.0047 193 THR A CA  
1558 C  C   . THR A 192 ? 0.1421 0.1274 0.0819 0.0020  0.0069  -0.0091 193 THR A C   
1559 O  O   . THR A 192 ? 0.1362 0.1589 0.0910 0.0001  0.0066  -0.0037 193 THR A O   
1560 C  CB  . THR A 192 ? 0.1291 0.1243 0.1189 0.0015  0.0230  -0.0060 193 THR A CB  
1561 O  OG1 . THR A 192 ? 0.1400 0.1259 0.1428 0.0073  0.0017  -0.0130 193 THR A OG1 
1562 C  CG2 . THR A 192 ? 0.1798 0.1576 0.1082 0.0271  0.0143  -0.0081 193 THR A CG2 
1563 N  N   . TYR A 193 ? 0.1258 0.1223 0.1002 -0.0015 -0.0055 -0.0084 194 TYR A N   
1564 C  CA  . TYR A 193 ? 0.1267 0.1277 0.1007 0.0020  -0.0036 0.0026  194 TYR A CA  
1565 C  C   . TYR A 193 ? 0.1199 0.1120 0.0919 0.0212  -0.0089 -0.0042 194 TYR A C   
1566 O  O   . TYR A 193 ? 0.1238 0.1244 0.0944 0.0087  -0.0081 -0.0069 194 TYR A O   
1567 C  CB  . TYR A 193 ? 0.1267 0.1360 0.1220 0.0098  0.0032  0.0067  194 TYR A CB  
1568 C  CG  . TYR A 193 ? 0.1181 0.1243 0.1210 0.0196  -0.0082 0.0008  194 TYR A CG  
1569 C  CD1 . TYR A 193 ? 0.1411 0.1248 0.1137 0.0117  -0.0005 0.0041  194 TYR A CD1 
1570 C  CD2 . TYR A 193 ? 0.1203 0.1253 0.1198 0.0237  -0.0019 -0.0054 194 TYR A CD2 
1571 C  CE1 . TYR A 193 ? 0.1331 0.1156 0.1165 0.0086  0.0079  0.0129  194 TYR A CE1 
1572 C  CE2 . TYR A 193 ? 0.1345 0.1040 0.1165 0.0110  -0.0080 -0.0070 194 TYR A CE2 
1573 C  CZ  . TYR A 193 ? 0.1244 0.0937 0.1054 0.0102  0.0029  0.0019  194 TYR A CZ  
1574 O  OH  . TYR A 193 ? 0.1258 0.1016 0.1282 0.0033  0.0099  -0.0083 194 TYR A OH  
1575 N  N   . PRO A 194 ? 0.1226 0.1265 0.1111 0.0023  -0.0149 -0.0203 195 PRO A N   
1576 C  CA  . PRO A 194 ? 0.1199 0.1155 0.1204 0.0042  0.0070  -0.0271 195 PRO A CA  
1577 C  C   . PRO A 194 ? 0.1409 0.0937 0.1018 0.0177  -0.0082 -0.0214 195 PRO A C   
1578 O  O   . PRO A 194 ? 0.1488 0.1226 0.1007 0.0087  -0.0078 0.0016  195 PRO A O   
1579 C  CB  . PRO A 194 ? 0.1590 0.1371 0.1302 -0.0078 0.0027  -0.0299 195 PRO A CB  
1580 C  CG  . PRO A 194 ? 0.1795 0.1632 0.1277 -0.0339 -0.0122 -0.0149 195 PRO A CG  
1581 C  CD  . PRO A 194 ? 0.1707 0.1632 0.0962 -0.0161 -0.0219 -0.0402 195 PRO A CD  
1582 N  N   . GLY A 195 ? 0.1213 0.0958 0.1031 -0.0020 -0.0016 -0.0168 196 GLY A N   
1583 C  CA  . GLY A 195 ? 0.1267 0.1077 0.1146 0.0115  0.0152  -0.0005 196 GLY A CA  
1584 C  C   . GLY A 195 ? 0.1375 0.0930 0.1041 -0.0062 -0.0013 -0.0075 196 GLY A C   
1585 O  O   . GLY A 195 ? 0.1339 0.0957 0.0988 0.0041  -0.0030 -0.0115 196 GLY A O   
1586 N  N   . SER A 196 ? 0.1172 0.1037 0.0923 -0.0006 -0.0009 -0.0025 197 SER A N   
1587 C  CA  . SER A 196 ? 0.1101 0.1192 0.1070 -0.0119 0.0001  0.0029  197 SER A CA  
1588 C  C   . SER A 196 ? 0.1041 0.0905 0.1002 0.0093  -0.0050 -0.0052 197 SER A C   
1589 O  O   . SER A 196 ? 0.1113 0.0987 0.1185 -0.0005 -0.0099 -0.0122 197 SER A O   
1590 C  CB  . SER A 196 ? 0.1251 0.0914 0.1373 0.0122  -0.0098 -0.0206 197 SER A CB  
1591 O  OG  . SER A 196 ? 0.1172 0.0951 0.1329 -0.0024 -0.0077 -0.0016 197 SER A OG  
1592 N  N   . LEU A 197 ? 0.1156 0.1080 0.0989 0.0023  0.0020  -0.0057 198 LEU A N   
1593 C  CA  . LEU A 197 ? 0.1250 0.1077 0.0879 -0.0003 0.0041  -0.0085 198 LEU A CA  
1594 C  C   . LEU A 197 ? 0.1168 0.1014 0.1142 -0.0075 -0.0070 -0.0186 198 LEU A C   
1595 O  O   . LEU A 197 ? 0.1259 0.1122 0.1233 0.0032  -0.0084 -0.0114 198 LEU A O   
1596 C  CB  . LEU A 197 ? 0.1375 0.1046 0.1431 -0.0019 0.0144  0.0066  198 LEU A CB  
1597 C  CG  . LEU A 197 ? 0.1311 0.1367 0.2093 0.0111  0.0179  0.0229  198 LEU A CG  
1598 C  CD1 . LEU A 197 ? 0.1752 0.1263 0.1991 0.0209  0.0052  -0.0003 198 LEU A CD1 
1599 C  CD2 . LEU A 197 ? 0.1696 0.1892 0.1992 0.0068  0.0309  0.0612  198 LEU A CD2 
1600 N  N   . THR A 198 ? 0.1298 0.0959 0.1244 0.0025  -0.0041 -0.0208 199 THR A N   
1601 C  CA  . THR A 198 ? 0.1306 0.0912 0.1152 0.0039  0.0011  -0.0247 199 THR A CA  
1602 C  C   . THR A 198 ? 0.1188 0.1013 0.1074 0.0000  -0.0042 -0.0132 199 THR A C   
1603 O  O   . THR A 198 ? 0.1243 0.1149 0.1457 0.0110  -0.0006 -0.0113 199 THR A O   
1604 C  CB  . THR A 198 ? 0.1203 0.1036 0.0856 0.0026  -0.0127 -0.0069 199 THR A CB  
1605 O  OG1 . THR A 198 ? 0.1208 0.1005 0.1097 0.0030  -0.0139 0.0043  199 THR A OG1 
1606 C  CG2 . THR A 198 ? 0.1350 0.1177 0.1102 0.0053  0.0073  -0.0002 199 THR A CG2 
1607 N  N   . THR A 199 ? 0.1180 0.1229 0.1229 -0.0048 0.0096  0.0001  200 THR A N   
1608 C  CA  . THR A 199 ? 0.1272 0.1164 0.1140 -0.0070 0.0105  -0.0073 200 THR A CA  
1609 C  C   . THR A 199 ? 0.1342 0.1262 0.1324 -0.0073 0.0013  -0.0018 200 THR A C   
1610 O  O   . THR A 199 ? 0.1331 0.1312 0.1398 -0.0134 0.0005  -0.0204 200 THR A O   
1611 C  CB  . THR A 199 ? 0.1725 0.1304 0.1282 -0.0011 -0.0200 -0.0234 200 THR A CB  
1612 O  OG1 . THR A 199 ? 0.2240 0.1508 0.1878 0.0175  -0.0509 0.0005  200 THR A OG1 
1613 C  CG2 . THR A 199 ? 0.1647 0.1461 0.1672 -0.0262 -0.0133 -0.0177 200 THR A CG2 
1614 N  N   . PRO A 200 ? 0.1259 0.1490 0.1298 -0.0037 0.0020  -0.0037 201 PRO A N   
1615 C  CA  . PRO A 200 ? 0.1265 0.1322 0.1562 -0.0217 0.0036  0.0220  201 PRO A CA  
1616 C  C   . PRO A 200 ? 0.1557 0.1363 0.1414 -0.0147 -0.0047 0.0073  201 PRO A C   
1617 O  O   . PRO A 200 ? 0.1851 0.1544 0.1396 0.0062  -0.0197 -0.0021 201 PRO A O   
1618 C  CB  . PRO A 200 ? 0.1269 0.1615 0.1676 -0.0094 0.0157  0.0047  201 PRO A CB  
1619 C  CG  . PRO A 200 ? 0.1423 0.1475 0.1946 -0.0199 0.0018  -0.0050 201 PRO A CG  
1620 C  CD  . PRO A 200 ? 0.1146 0.1533 0.1640 0.0003  0.0089  -0.0237 201 PRO A CD  
1621 N  N   . PRO A 201 ? 0.1503 0.1326 0.1587 -0.0030 -0.0086 0.0195  202 PRO A N   
1622 C  CA  . PRO A 201 ? 0.1702 0.1252 0.1392 -0.0350 0.0001  0.0010  202 PRO A CA  
1623 C  C   . PRO A 201 ? 0.1210 0.1243 0.1483 0.0128  -0.0053 0.0011  202 PRO A C   
1624 O  O   . PRO A 201 ? 0.1404 0.1235 0.1783 -0.0100 -0.0148 -0.0111 202 PRO A O   
1625 C  CB  . PRO A 201 ? 0.1701 0.1207 0.2253 -0.0149 -0.0027 0.0089  202 PRO A CB  
1626 C  CG  . PRO A 201 ? 0.2555 0.1903 0.2437 0.0013  -0.0781 -0.0049 202 PRO A CG  
1627 C  CD  . PRO A 201 ? 0.1781 0.1436 0.1953 -0.0019 -0.0001 0.0397  202 PRO A CD  
1628 N  N   . LEU A 202 ? 0.1244 0.1171 0.1413 -0.0033 0.0178  0.0102  203 LEU A N   
1629 C  CA  . LEU A 202 ? 0.1228 0.1004 0.1348 0.0059  0.0041  -0.0126 203 LEU A CA  
1630 C  C   . LEU A 202 ? 0.1279 0.1109 0.1307 0.0027  0.0012  -0.0096 203 LEU A C   
1631 O  O   . LEU A 202 ? 0.1250 0.1075 0.1357 -0.0053 -0.0041 -0.0151 203 LEU A O   
1632 C  CB  . LEU A 202 ? 0.1349 0.1226 0.1386 0.0251  -0.0093 -0.0183 203 LEU A CB  
1633 C  CG  . LEU A 202 ? 0.1176 0.1066 0.1549 0.0091  0.0052  -0.0068 203 LEU A CG  
1634 C  CD1 . LEU A 202 ? 0.1370 0.1360 0.1906 0.0147  -0.0301 -0.0036 203 LEU A CD1 
1635 C  CD2 . LEU A 202 ? 0.1360 0.1093 0.1626 -0.0049 0.0055  -0.0178 203 LEU A CD2 
1636 N  N   . ASN A 203 ? 0.1294 0.0926 0.1666 -0.0098 -0.0025 -0.0086 204 ASN A N   
1637 C  CA  . ASN A 203 ? 0.1303 0.1039 0.1623 -0.0002 0.0025  -0.0094 204 ASN A CA  
1638 C  C   . ASN A 203 ? 0.1371 0.0962 0.1327 -0.0053 -0.0067 -0.0036 204 ASN A C   
1639 O  O   . ASN A 203 ? 0.1300 0.0998 0.1456 -0.0065 -0.0116 -0.0064 204 ASN A O   
1640 C  CB  . ASN A 203 ? 0.1518 0.1061 0.1811 0.0116  0.0100  0.0150  204 ASN A CB  
1641 C  CG  . ASN A 203 ? 0.2056 0.1274 0.1829 0.0172  0.0384  0.0021  204 ASN A CG  
1642 O  OD1 . ASN A 203 ? 0.2617 0.1758 0.2899 0.0147  0.1051  0.0195  204 ASN A OD1 
1643 N  ND2 . ASN A 203 ? 0.2470 0.1436 0.2327 0.0038  0.0181  0.0105  204 ASN A ND2 
1644 N  N   . GLU A 204 ? 0.1479 0.1071 0.1375 -0.0106 0.0011  -0.0126 205 GLU A N   
1645 C  CA  . GLU A 204 ? 0.1392 0.1307 0.1048 -0.0021 -0.0016 -0.0315 205 GLU A CA  
1646 C  C   . GLU A 204 ? 0.1565 0.0982 0.1188 -0.0111 -0.0047 -0.0111 205 GLU A C   
1647 O  O   . GLU A 204 ? 0.1729 0.1683 0.1424 0.0232  -0.0293 -0.0356 205 GLU A O   
1648 C  CB  . GLU A 204 ? 0.1619 0.1147 0.1464 0.0127  -0.0374 -0.0226 205 GLU A CB  
1649 C  CG  . GLU A 204 ? 0.1434 0.1520 0.1373 0.0219  -0.0049 -0.0354 205 GLU A CG  
1650 C  CD  . GLU A 204 ? 0.1683 0.1474 0.1391 0.0139  -0.0035 -0.0258 205 GLU A CD  
1651 O  OE1 . GLU A 204 ? 0.1856 0.1730 0.1971 -0.0053 -0.0488 -0.0312 205 GLU A OE1 
1652 O  OE2 . GLU A 204 ? 0.1694 0.1479 0.1725 -0.0027 -0.0267 -0.0044 205 GLU A OE2 
1653 N  N   . CYS A 205 ? 0.1210 0.0882 0.1528 -0.0075 -0.0187 -0.0059 206 CYS A N   
1654 C  CA  . CYS A 205 ? 0.1349 0.1104 0.1134 0.0042  -0.0055 -0.0063 206 CYS A CA  
1655 C  C   . CYS A 205 ? 0.1353 0.0974 0.1393 -0.0005 -0.0292 -0.0063 206 CYS A C   
1656 O  O   . CYS A 205 ? 0.1510 0.0846 0.2187 -0.0002 -0.0447 0.0005  206 CYS A O   
1657 C  CB  . CYS A 205 ? 0.1542 0.1150 0.1373 0.0032  0.0032  0.0010  206 CYS A CB  
1658 S  SG  . CYS A 205 ? 0.1740 0.1131 0.1450 0.0064  -0.0196 -0.0107 206 CYS A SG  
1659 N  N   . VAL A 206 ? 0.1285 0.0879 0.1393 -0.0095 -0.0094 -0.0001 207 VAL A N   
1660 C  CA  . VAL A 206 ? 0.1224 0.0766 0.1311 -0.0004 0.0022  -0.0012 207 VAL A CA  
1661 C  C   . VAL A 206 ? 0.1292 0.0820 0.1194 0.0047  -0.0087 -0.0124 207 VAL A C   
1662 O  O   . VAL A 206 ? 0.1524 0.1192 0.1402 0.0078  -0.0266 0.0081  207 VAL A O   
1663 C  CB  . VAL A 206 ? 0.1134 0.0928 0.1492 0.0073  0.0147  -0.0159 207 VAL A CB  
1664 C  CG1 . VAL A 206 ? 0.1400 0.1067 0.1442 -0.0040 -0.0254 -0.0206 207 VAL A CG1 
1665 C  CG2 . VAL A 206 ? 0.1414 0.1221 0.1375 0.0151  0.0111  -0.0077 207 VAL A CG2 
1666 N  N   . THR A 207 ? 0.1133 0.0815 0.1375 0.0000  0.0017  -0.0085 208 THR A N   
1667 C  CA  . THR A 207 ? 0.1264 0.1116 0.1253 -0.0087 -0.0017 -0.0136 208 THR A CA  
1668 C  C   . THR A 207 ? 0.1261 0.0885 0.1179 -0.0082 -0.0097 -0.0066 208 THR A C   
1669 O  O   . THR A 207 ? 0.1399 0.1099 0.1095 0.0059  -0.0105 -0.0127 208 THR A O   
1670 C  CB  . THR A 207 ? 0.1317 0.1014 0.1705 -0.0030 0.0033  -0.0132 208 THR A CB  
1671 O  OG1 . THR A 207 ? 0.1640 0.1115 0.1727 0.0000  -0.0011 -0.0298 208 THR A OG1 
1672 C  CG2 . THR A 207 ? 0.1551 0.1371 0.1644 -0.0265 0.0096  -0.0129 208 THR A CG2 
1673 N  N   . TRP A 208 ? 0.1229 0.0853 0.1109 -0.0021 -0.0030 -0.0002 209 TRP A N   
1674 C  CA  . TRP A 208 ? 0.1201 0.0791 0.1061 0.0027  0.0106  0.0001  209 TRP A CA  
1675 C  C   . TRP A 208 ? 0.1228 0.0856 0.0912 0.0164  0.0099  0.0061  209 TRP A C   
1676 O  O   . TRP A 208 ? 0.1339 0.1153 0.0889 -0.0010 0.0089  0.0017  209 TRP A O   
1677 C  CB  . TRP A 208 ? 0.1268 0.0996 0.0988 0.0188  0.0005  0.0001  209 TRP A CB  
1678 C  CG  . TRP A 208 ? 0.1263 0.0901 0.1020 0.0070  0.0002  -0.0068 209 TRP A CG  
1679 C  CD1 . TRP A 208 ? 0.1268 0.0935 0.1280 0.0111  0.0013  -0.0110 209 TRP A CD1 
1680 C  CD2 . TRP A 208 ? 0.1220 0.0804 0.1005 0.0069  0.0003  -0.0026 209 TRP A CD2 
1681 N  NE1 . TRP A 208 ? 0.1254 0.0980 0.1329 0.0147  -0.0051 -0.0099 209 TRP A NE1 
1682 C  CE2 . TRP A 208 ? 0.1301 0.0813 0.1135 0.0068  0.0100  0.0054  209 TRP A CE2 
1683 C  CE3 . TRP A 208 ? 0.1230 0.0879 0.1052 0.0126  -0.0158 0.0048  209 TRP A CE3 
1684 C  CZ2 . TRP A 208 ? 0.1391 0.0976 0.1222 0.0243  0.0122  0.0019  209 TRP A CZ2 
1685 C  CZ3 . TRP A 208 ? 0.1582 0.0734 0.1183 0.0218  0.0153  0.0026  209 TRP A CZ3 
1686 C  CH2 . TRP A 208 ? 0.1460 0.0883 0.1272 0.0356  0.0122  -0.0111 209 TRP A CH2 
1687 N  N   . ILE A 209 ? 0.1198 0.1055 0.0964 0.0033  -0.0003 -0.0025 210 ILE A N   
1688 C  CA  . ILE A 209 ? 0.1232 0.0763 0.1313 0.0061  0.0102  -0.0071 210 ILE A CA  
1689 C  C   . ILE A 209 ? 0.1146 0.0903 0.1011 0.0118  0.0152  -0.0010 210 ILE A C   
1690 O  O   . ILE A 209 ? 0.1666 0.0944 0.0995 0.0010  0.0113  0.0027  210 ILE A O   
1691 C  CB  . ILE A 209 ? 0.1192 0.0953 0.1327 0.0144  0.0133  -0.0085 210 ILE A CB  
1692 C  CG1 . ILE A 209 ? 0.1382 0.0804 0.2036 0.0239  -0.0135 -0.0266 210 ILE A CG1 
1693 C  CG2 . ILE A 209 ? 0.1208 0.1506 0.1718 0.0086  0.0097  0.0082  210 ILE A CG2 
1694 C  CD1 . ILE A 209 ? 0.1899 0.1044 0.2701 0.0561  -0.0249 -0.0266 210 ILE A CD1 
1695 N  N   . VAL A 210 ? 0.1283 0.0743 0.1208 -0.0006 0.0104  0.0060  211 VAL A N   
1696 C  CA  . VAL A 210 ? 0.1238 0.0718 0.1237 -0.0001 0.0084  -0.0003 211 VAL A CA  
1697 C  C   . VAL A 210 ? 0.1204 0.0991 0.1027 0.0071  0.0116  0.0061  211 VAL A C   
1698 O  O   . VAL A 210 ? 0.1335 0.1137 0.1041 -0.0038 0.0102  -0.0011 211 VAL A O   
1699 C  CB  . VAL A 210 ? 0.1145 0.0822 0.1427 0.0034  0.0059  0.0064  211 VAL A CB  
1700 C  CG1 . VAL A 210 ? 0.1447 0.0966 0.1500 -0.0004 0.0096  -0.0177 211 VAL A CG1 
1701 C  CG2 . VAL A 210 ? 0.1400 0.0889 0.1758 -0.0085 0.0027  0.0024  211 VAL A CG2 
1702 N  N   . LEU A 211 ? 0.1167 0.1064 0.1226 0.0011  0.0020  -0.0018 212 LEU A N   
1703 C  CA  . LEU A 211 ? 0.1207 0.1205 0.1079 -0.0170 0.0039  0.0029  212 LEU A CA  
1704 C  C   . LEU A 211 ? 0.1244 0.1180 0.1289 -0.0025 -0.0006 -0.0013 212 LEU A C   
1705 O  O   . LEU A 211 ? 0.1289 0.1258 0.1265 -0.0083 -0.0084 0.0033  212 LEU A O   
1706 C  CB  . LEU A 211 ? 0.1425 0.1179 0.1144 -0.0111 -0.0083 0.0070  212 LEU A CB  
1707 C  CG  . LEU A 211 ? 0.1363 0.1221 0.1256 0.0044  -0.0136 -0.0051 212 LEU A CG  
1708 C  CD1 . LEU A 211 ? 0.1646 0.1769 0.1280 -0.0076 -0.0443 0.0253  212 LEU A CD1 
1709 C  CD2 . LEU A 211 ? 0.1729 0.1442 0.1434 0.0245  0.0102  -0.0011 212 LEU A CD2 
1710 N  N   . LYS A 212 ? 0.1252 0.1269 0.1355 -0.0199 -0.0091 0.0151  213 LYS A N   
1711 C  CA  . LYS A 212 ? 0.1802 0.1442 0.1221 -0.0178 -0.0137 0.0345  213 LYS A CA  
1712 C  C   . LYS A 212 ? 0.1538 0.1155 0.1546 -0.0209 0.0054  0.0177  213 LYS A C   
1713 O  O   . LYS A 212 ? 0.1683 0.1342 0.2250 -0.0055 -0.0337 0.0405  213 LYS A O   
1714 C  CB  . LYS A 212 ? 0.2276 0.2078 0.1319 -0.0703 -0.0100 0.0289  213 LYS A CB  
1715 C  CG  . LYS A 212 ? 0.3771 0.2608 0.1993 -0.0598 -0.0297 0.0663  213 LYS A CG  
1716 C  CD  . LYS A 212 ? 0.5427 0.4773 0.2843 -0.1155 0.0929  0.0067  213 LYS A CD  
1717 C  CE  . LYS A 212 ? 0.6556 0.4414 0.4612 -0.0288 0.0460  0.0102  213 LYS A CE  
1718 N  NZ  . LYS A 212 ? 0.4950 0.5910 0.5922 -0.1371 0.0242  0.0509  213 LYS A NZ  
1719 N  N   . GLU A 213 ? 0.1296 0.1239 0.1472 -0.0251 -0.0097 0.0106  214 GLU A N   
1720 C  CA  . GLU A 213 ? 0.1292 0.1225 0.1443 -0.0143 0.0054  0.0093  214 GLU A CA  
1721 C  C   . GLU A 213 ? 0.1485 0.1058 0.1297 0.0059  -0.0087 0.0203  214 GLU A C   
1722 O  O   . GLU A 213 ? 0.1332 0.1134 0.1457 -0.0031 -0.0017 0.0236  214 GLU A O   
1723 C  CB  . GLU A 213 ? 0.1284 0.1459 0.1664 -0.0114 -0.0085 0.0031  214 GLU A CB  
1724 C  CG  . GLU A 213 ? 0.1698 0.1870 0.1970 -0.0218 -0.0212 -0.0193 214 GLU A CG  
1725 C  CD  . GLU A 213 ? 0.1618 0.2380 0.2208 -0.0475 -0.0186 0.0116  214 GLU A CD  
1726 O  OE1 . GLU A 213 ? 0.1752 0.2020 0.2766 0.0127  -0.0219 0.0257  214 GLU A OE1 
1727 O  OE2 . GLU A 213 ? 0.2219 0.3644 0.2681 0.0032  -0.0428 -0.0184 214 GLU A OE2 
1728 N  N   . PRO A 214 ? 0.1510 0.1120 0.1384 -0.0042 0.0082  0.0181  215 PRO A N   
1729 C  CA  . PRO A 214 ? 0.1436 0.0988 0.1337 0.0080  0.0004  -0.0128 215 PRO A CA  
1730 C  C   . PRO A 214 ? 0.1382 0.1039 0.1492 0.0042  -0.0012 0.0054  215 PRO A C   
1731 O  O   . PRO A 214 ? 0.1490 0.1568 0.1920 -0.0295 -0.0122 0.0133  215 PRO A O   
1732 C  CB  . PRO A 214 ? 0.1632 0.0993 0.1812 0.0142  0.0146  0.0064  215 PRO A CB  
1733 C  CG  . PRO A 214 ? 0.2339 0.1852 0.2425 0.0089  0.0547  0.0325  215 PRO A CG  
1734 C  CD  . PRO A 214 ? 0.1834 0.0919 0.2197 0.0057  0.0242  0.0350  215 PRO A CD  
1735 N  N   . ILE A 215 ? 0.1414 0.1104 0.1271 0.0239  -0.0088 -0.0009 216 ILE A N   
1736 C  CA  . ILE A 215 ? 0.1377 0.1137 0.1385 0.0172  -0.0153 -0.0085 216 ILE A CA  
1737 C  C   . ILE A 215 ? 0.1421 0.1201 0.1338 0.0153  -0.0093 -0.0070 216 ILE A C   
1738 O  O   . ILE A 215 ? 0.1392 0.1134 0.2020 0.0190  -0.0134 -0.0137 216 ILE A O   
1739 C  CB  . ILE A 215 ? 0.1324 0.0998 0.1923 0.0220  0.0128  0.0044  216 ILE A CB  
1740 C  CG1 . ILE A 215 ? 0.1465 0.1268 0.1560 0.0084  0.0190  0.0077  216 ILE A CG1 
1741 C  CG2 . ILE A 215 ? 0.1360 0.1172 0.1908 0.0283  0.0186  -0.0036 216 ILE A CG2 
1742 C  CD1 . ILE A 215 ? 0.1867 0.1493 0.1621 0.0117  0.0015  0.0211  216 ILE A CD1 
1743 N  N   . SER A 216 ? 0.1705 0.1118 0.1410 0.0166  -0.0283 -0.0057 217 SER A N   
1744 C  CA  A SER A 216 ? 0.1655 0.1110 0.1612 0.0155  -0.0019 -0.0141 217 SER A CA  
1745 C  CA  B SER A 216 ? 0.1675 0.1059 0.1636 0.0186  -0.0077 -0.0103 217 SER A CA  
1746 C  C   . SER A 216 ? 0.1551 0.0883 0.1513 0.0071  -0.0258 -0.0149 217 SER A C   
1747 O  O   . SER A 216 ? 0.1582 0.1167 0.1586 0.0050  -0.0234 0.0027  217 SER A O   
1748 C  CB  A SER A 216 ? 0.2477 0.0702 0.1648 -0.0051 -0.0041 -0.0456 217 SER A CB  
1749 C  CB  B SER A 216 ? 0.2596 0.1180 0.1883 -0.0377 -0.0044 0.0106  217 SER A CB  
1750 O  OG  A SER A 216 ? 0.2016 0.1587 0.1830 -0.0040 -0.0421 0.0022  217 SER A OG  
1751 O  OG  B SER A 216 ? 0.2097 0.1648 0.1646 -0.0168 -0.0047 0.0067  217 SER A OG  
1752 N  N   . VAL A 217 ? 0.1551 0.0901 0.1371 -0.0082 -0.0060 -0.0294 218 VAL A N   
1753 C  CA  . VAL A 217 ? 0.1619 0.0804 0.1618 0.0013  -0.0241 -0.0190 218 VAL A CA  
1754 C  C   . VAL A 217 ? 0.1486 0.0777 0.1485 -0.0161 -0.0064 -0.0013 218 VAL A C   
1755 O  O   . VAL A 217 ? 0.1895 0.0838 0.1628 -0.0121 -0.0303 -0.0035 218 VAL A O   
1756 C  CB  . VAL A 217 ? 0.1608 0.0820 0.2109 0.0084  -0.0365 -0.0088 218 VAL A CB  
1757 C  CG1 . VAL A 217 ? 0.1806 0.0924 0.1946 -0.0066 -0.0341 -0.0231 218 VAL A CG1 
1758 C  CG2 . VAL A 217 ? 0.1547 0.1118 0.2283 0.0107  -0.0412 -0.0201 218 VAL A CG2 
1759 N  N   . SER A 218 ? 0.1542 0.0785 0.1407 -0.0036 -0.0199 -0.0073 219 SER A N   
1760 C  CA  . SER A 218 ? 0.1603 0.0874 0.1551 -0.0067 -0.0137 -0.0223 219 SER A CA  
1761 C  C   . SER A 218 ? 0.1544 0.0831 0.1532 -0.0004 -0.0282 0.0021  219 SER A C   
1762 O  O   . SER A 218 ? 0.1576 0.0874 0.1805 -0.0017 -0.0289 0.0075  219 SER A O   
1763 C  CB  . SER A 218 ? 0.1562 0.0905 0.1483 -0.0109 -0.0029 0.0047  219 SER A CB  
1764 O  OG  . SER A 218 ? 0.1543 0.1185 0.1599 -0.0132 -0.0179 -0.0047 219 SER A OG  
1765 N  N   . SER A 219 ? 0.1813 0.0797 0.1594 0.0019  -0.0190 0.0012  220 SER A N   
1766 C  CA  . SER A 219 ? 0.1734 0.0856 0.1987 0.0073  -0.0059 0.0100  220 SER A CA  
1767 C  C   . SER A 219 ? 0.1565 0.0804 0.2093 0.0157  -0.0143 0.0124  220 SER A C   
1768 O  O   . SER A 219 ? 0.1374 0.1129 0.2285 0.0057  0.0013  0.0111  220 SER A O   
1769 C  CB  . SER A 219 ? 0.1946 0.0845 0.2583 -0.0208 0.0119  -0.0122 220 SER A CB  
1770 O  OG  . SER A 219 ? 0.2238 0.0888 0.2658 0.0059  -0.0118 -0.0200 220 SER A OG  
1771 N  N   . GLU A 220 ? 0.1621 0.0969 0.1684 0.0211  -0.0120 -0.0079 221 GLU A N   
1772 C  CA  . GLU A 220 ? 0.1934 0.1040 0.1586 0.0154  -0.0295 -0.0113 221 GLU A CA  
1773 C  C   . GLU A 220 ? 0.1342 0.1029 0.1594 0.0122  -0.0071 -0.0019 221 GLU A C   
1774 O  O   . GLU A 220 ? 0.1741 0.1499 0.1590 0.0084  0.0181  -0.0132 221 GLU A O   
1775 C  CB  . GLU A 220 ? 0.1787 0.1495 0.1890 0.0104  -0.0314 -0.0469 221 GLU A CB  
1776 C  CG  . GLU A 220 ? 0.2420 0.1576 0.2456 -0.0015 -0.0168 -0.0653 221 GLU A CG  
1777 C  CD  . GLU A 220 ? 0.3525 0.1461 0.3116 -0.0433 -0.0256 -0.0097 221 GLU A CD  
1778 O  OE1 . GLU A 220 ? 0.1975 0.1768 0.3120 -0.0514 -0.0288 -0.0102 221 GLU A OE1 
1779 O  OE2 . GLU A 220 ? 0.3533 0.1969 0.5792 -0.1268 -0.0359 -0.0935 221 GLU A OE2 
1780 N  N   . GLN A 221 ? 0.1475 0.0845 0.1547 0.0122  -0.0078 -0.0059 222 GLN A N   
1781 C  CA  . GLN A 221 ? 0.1313 0.0822 0.1813 -0.0105 -0.0024 -0.0115 222 GLN A CA  
1782 C  C   . GLN A 221 ? 0.1302 0.0993 0.1762 0.0121  -0.0145 -0.0057 222 GLN A C   
1783 O  O   . GLN A 221 ? 0.1356 0.0996 0.1756 -0.0012 -0.0103 0.0043  222 GLN A O   
1784 C  CB  . GLN A 221 ? 0.1392 0.1125 0.1257 0.0038  -0.0125 0.0003  222 GLN A CB  
1785 C  CG  . GLN A 221 ? 0.1407 0.1003 0.1384 -0.0057 -0.0072 0.0025  222 GLN A CG  
1786 C  CD  . GLN A 221 ? 0.1453 0.0822 0.1406 -0.0036 -0.0065 -0.0017 222 GLN A CD  
1787 O  OE1 . GLN A 221 ? 0.1431 0.0964 0.1544 0.0130  -0.0013 -0.0077 222 GLN A OE1 
1788 N  NE2 . GLN A 221 ? 0.1518 0.1208 0.1414 0.0058  -0.0124 0.0151  222 GLN A NE2 
1789 N  N   A VAL A 222 ? 0.1197 0.0952 0.1849 0.0100  -0.0187 0.0008  223 VAL A N   
1790 N  N   B VAL A 222 ? 0.1411 0.1243 0.1748 0.0122  -0.0142 0.0113  223 VAL A N   
1791 C  CA  A VAL A 222 ? 0.1109 0.1360 0.1942 0.0379  -0.0236 0.0302  223 VAL A CA  
1792 C  CA  B VAL A 222 ? 0.1427 0.1619 0.1729 -0.0069 -0.0067 0.0248  223 VAL A CA  
1793 C  C   A VAL A 222 ? 0.1181 0.1129 0.1824 0.0131  -0.0057 0.0309  223 VAL A C   
1794 C  C   B VAL A 222 ? 0.1431 0.1127 0.1775 0.0016  -0.0070 0.0161  223 VAL A C   
1795 O  O   A VAL A 222 ? 0.1306 0.1253 0.1962 -0.0104 0.0126  0.0257  223 VAL A O   
1796 O  O   B VAL A 222 ? 0.1353 0.1424 0.1791 -0.0078 -0.0109 0.0260  223 VAL A O   
1797 C  CB  A VAL A 222 ? 0.1704 0.2011 0.1885 0.0121  -0.0555 0.0340  223 VAL A CB  
1798 C  CB  B VAL A 222 ? 0.1628 0.2282 0.1723 0.0212  -0.0039 0.0465  223 VAL A CB  
1799 C  CG1 A VAL A 222 ? 0.1593 0.1957 0.2230 -0.0559 -0.0329 0.0288  223 VAL A CG1 
1800 C  CG1 B VAL A 222 ? 0.1445 0.4144 0.2613 0.0630  0.0156  0.1222  223 VAL A CG1 
1801 C  CG2 A VAL A 222 ? 0.2409 0.2472 0.1751 -0.0252 -0.0939 0.0550  223 VAL A CG2 
1802 C  CG2 B VAL A 222 ? 0.1780 0.2652 0.1438 0.0265  -0.0096 0.0108  223 VAL A CG2 
1803 N  N   A LEU A 223 ? 0.1601 0.1150 0.2078 0.0420  -0.0114 -0.0011 224 LEU A N   
1804 N  N   B LEU A 223 ? 0.1659 0.1238 0.1962 -0.0196 0.0155  -0.0072 224 LEU A N   
1805 C  CA  A LEU A 223 ? 0.1740 0.1456 0.2122 -0.0034 0.0033  0.0037  224 LEU A CA  
1806 C  CA  B LEU A 223 ? 0.1644 0.0966 0.2638 -0.0010 0.0343  -0.0066 224 LEU A CA  
1807 C  C   A LEU A 223 ? 0.1410 0.1310 0.2029 0.0002  0.0027  -0.0077 224 LEU A C   
1808 C  C   B LEU A 223 ? 0.1592 0.0917 0.2413 0.0006  0.0217  -0.0119 224 LEU A C   
1809 O  O   A LEU A 223 ? 0.1456 0.2078 0.2222 -0.0070 0.0081  0.0024  224 LEU A O   
1810 O  O   B LEU A 223 ? 0.1630 0.1163 0.2020 0.0153  0.0273  -0.0181 224 LEU A O   
1811 C  CB  A LEU A 223 ? 0.1709 0.0982 0.4064 -0.0021 0.0359  -0.0770 224 LEU A CB  
1812 C  CB  B LEU A 223 ? 0.2244 0.1129 0.3326 0.0133  0.0657  -0.0749 224 LEU A CB  
1813 C  CG  A LEU A 223 ? 0.2311 0.2796 0.3496 0.0179  0.0633  -0.0214 224 LEU A CG  
1814 C  CG  B LEU A 223 ? 0.2934 0.1424 0.3052 -0.0502 0.0798  -0.0638 224 LEU A CG  
1815 N  N   . LYS A 224 ? 0.1526 0.1324 0.1722 0.0103  -0.0033 0.0132  225 LYS A N   
1816 C  CA  . LYS A 224 ? 0.1597 0.1459 0.1720 -0.0001 -0.0156 0.0076  225 LYS A CA  
1817 C  C   . LYS A 224 ? 0.1483 0.1450 0.1261 0.0190  -0.0027 -0.0046 225 LYS A C   
1818 O  O   . LYS A 224 ? 0.1490 0.1608 0.1438 0.0051  0.0079  0.0103  225 LYS A O   
1819 C  CB  . LYS A 224 ? 0.1862 0.2071 0.1903 0.0250  -0.0440 0.0341  225 LYS A CB  
1820 C  CG  . LYS A 224 ? 0.1834 0.2899 0.2290 -0.0461 -0.0316 0.0174  225 LYS A CG  
1821 C  CD  . LYS A 224 ? 0.2695 0.5127 0.4139 0.0563  -0.0121 0.0751  225 LYS A CD  
1822 C  CE  . LYS A 224 ? 0.3511 0.5457 0.4307 0.1218  -0.1626 0.0597  225 LYS A CE  
1823 N  NZ  . LYS A 224 ? 0.7574 0.4667 0.7251 0.0597  0.1002  -0.0710 225 LYS A NZ  
1824 N  N   . PHE A 225 ? 0.1536 0.1059 0.1220 0.0223  0.0136  -0.0003 226 PHE A N   
1825 C  CA  . PHE A 225 ? 0.1400 0.1216 0.1307 0.0258  0.0017  -0.0107 226 PHE A CA  
1826 C  C   . PHE A 225 ? 0.1508 0.1110 0.1250 0.0122  0.0003  0.0011  226 PHE A C   
1827 O  O   . PHE A 225 ? 0.1479 0.1222 0.1402 0.0077  0.0062  -0.0013 226 PHE A O   
1828 C  CB  . PHE A 225 ? 0.1464 0.1141 0.1690 0.0132  0.0352  0.0000  226 PHE A CB  
1829 C  CG  . PHE A 225 ? 0.1357 0.0982 0.1655 0.0049  0.0199  -0.0122 226 PHE A CG  
1830 C  CD1 . PHE A 225 ? 0.1802 0.1518 0.1791 0.0489  0.0099  0.0114  226 PHE A CD1 
1831 C  CD2 . PHE A 225 ? 0.1666 0.1797 0.1630 0.0223  0.0142  -0.0398 226 PHE A CD2 
1832 C  CE1 . PHE A 225 ? 0.1784 0.1795 0.1859 0.0337  0.0368  0.0154  226 PHE A CE1 
1833 C  CE2 . PHE A 225 ? 0.1633 0.2164 0.2401 0.0432  0.0005  -0.0606 226 PHE A CE2 
1834 C  CZ  . PHE A 225 ? 0.1676 0.1493 0.2203 0.0032  0.0006  -0.0425 226 PHE A CZ  
1835 N  N   . ARG A 226 ? 0.1461 0.1090 0.1368 0.0302  0.0120  -0.0147 227 ARG A N   
1836 C  CA  . ARG A 226 ? 0.1508 0.1137 0.1579 0.0329  0.0220  0.0005  227 ARG A CA  
1837 C  C   . ARG A 226 ? 0.1442 0.1239 0.1529 0.0099  0.0155  -0.0049 227 ARG A C   
1838 O  O   . ARG A 226 ? 0.1585 0.1553 0.1928 0.0398  0.0341  -0.0116 227 ARG A O   
1839 C  CB  . ARG A 226 ? 0.1632 0.1169 0.1435 0.0364  0.0087  -0.0003 227 ARG A CB  
1840 C  CG  . ARG A 226 ? 0.1617 0.1187 0.1370 0.0249  0.0076  -0.0046 227 ARG A CG  
1841 C  CD  . ARG A 226 ? 0.2294 0.1180 0.1549 0.0294  -0.0066 -0.0011 227 ARG A CD  
1842 N  NE  . ARG A 226 ? 0.1784 0.1156 0.1348 0.0111  -0.0138 0.0009  227 ARG A NE  
1843 C  CZ  . ARG A 226 ? 0.2090 0.1190 0.1594 -0.0221 -0.0060 -0.0150 227 ARG A CZ  
1844 N  NH1 . ARG A 226 ? 0.2278 0.1700 0.2134 -0.0445 -0.0313 -0.0520 227 ARG A NH1 
1845 N  NH2 . ARG A 226 ? 0.2397 0.1662 0.1726 -0.0275 0.0145  -0.0157 227 ARG A NH2 
1846 N  N   . LYS A 227 ? 0.1704 0.1371 0.1221 0.0006  -0.0013 -0.0267 228 LYS A N   
1847 C  CA  . LYS A 227 ? 0.1905 0.1375 0.1331 -0.0079 0.0131  -0.0440 228 LYS A CA  
1848 C  C   . LYS A 227 ? 0.1788 0.1417 0.1164 0.0094  0.0091  -0.0223 228 LYS A C   
1849 O  O   . LYS A 227 ? 0.2093 0.1960 0.1199 0.0104  0.0312  -0.0247 228 LYS A O   
1850 C  CB  . LYS A 227 ? 0.2016 0.1957 0.1723 -0.0139 -0.0212 -0.0439 228 LYS A CB  
1851 C  CG  . LYS A 227 ? 0.2721 0.2427 0.2445 -0.0850 -0.0217 -0.0373 228 LYS A CG  
1852 C  CD  . LYS A 227 ? 0.2680 0.3367 0.3747 -0.0826 -0.0708 0.0013  228 LYS A CD  
1853 N  N   . LEU A 228 ? 0.1374 0.1289 0.1391 0.0016  0.0006  -0.0302 229 LEU A N   
1854 C  CA  . LEU A 228 ? 0.1286 0.1432 0.1260 0.0006  0.0046  -0.0245 229 LEU A CA  
1855 C  C   . LEU A 228 ? 0.1421 0.1363 0.1436 0.0153  -0.0046 -0.0160 229 LEU A C   
1856 O  O   . LEU A 228 ? 0.1493 0.1418 0.1528 0.0305  0.0032  0.0047  229 LEU A O   
1857 C  CB  . LEU A 228 ? 0.1411 0.1420 0.1398 0.0372  0.0041  -0.0120 229 LEU A CB  
1858 C  CG  . LEU A 228 ? 0.1443 0.1597 0.1093 0.0419  0.0023  0.0069  229 LEU A CG  
1859 C  CD1 . LEU A 228 ? 0.1428 0.1641 0.1198 0.0192  0.0027  -0.0067 229 LEU A CD1 
1860 C  CD2 . LEU A 228 ? 0.1830 0.1838 0.1331 0.0324  0.0061  0.0298  229 LEU A CD2 
1861 N  N   . ASN A 229 ? 0.1217 0.1429 0.1650 0.0089  -0.0023 0.0021  230 ASN A N   
1862 C  CA  . ASN A 229 ? 0.1247 0.1725 0.1297 0.0026  0.0218  -0.0274 230 ASN A CA  
1863 C  C   . ASN A 229 ? 0.1248 0.1414 0.1293 0.0186  0.0203  -0.0006 230 ASN A C   
1864 O  O   . ASN A 229 ? 0.1508 0.1326 0.1543 0.0225  0.0041  -0.0039 230 ASN A O   
1865 C  CB  . ASN A 229 ? 0.1414 0.1969 0.1350 0.0104  0.0312  -0.0147 230 ASN A CB  
1866 C  CG  . ASN A 229 ? 0.1949 0.1884 0.1349 0.0391  0.0322  -0.0208 230 ASN A CG  
1867 O  OD1 . ASN A 229 ? 0.3240 0.2256 0.1781 0.0428  0.0982  -0.0226 230 ASN A OD1 
1868 N  ND2 . ASN A 229 ? 0.2006 0.1799 0.2502 0.0431  0.0099  -0.0531 230 ASN A ND2 
1869 N  N   . PHE A 230 ? 0.1226 0.1277 0.1565 0.0165  0.0176  0.0051  231 PHE A N   
1870 C  CA  . PHE A 230 ? 0.1373 0.1508 0.1450 -0.0036 0.0158  0.0075  231 PHE A CA  
1871 C  C   . PHE A 230 ? 0.1472 0.1268 0.1568 -0.0009 0.0174  -0.0088 231 PHE A C   
1872 O  O   . PHE A 230 ? 0.1707 0.1315 0.1554 -0.0033 0.0174  -0.0003 231 PHE A O   
1873 C  CB  . PHE A 230 ? 0.1518 0.1931 0.1221 0.0233  0.0086  0.0067  231 PHE A CB  
1874 C  CG  . PHE A 230 ? 0.1244 0.1493 0.1232 -0.0111 0.0091  -0.0009 231 PHE A CG  
1875 C  CD1 . PHE A 230 ? 0.1439 0.1851 0.1370 -0.0046 0.0144  -0.0212 231 PHE A CD1 
1876 C  CD2 . PHE A 230 ? 0.1303 0.1636 0.1690 0.0000  -0.0046 0.0179  231 PHE A CD2 
1877 C  CE1 . PHE A 230 ? 0.1528 0.1668 0.1348 -0.0199 0.0004  -0.0259 231 PHE A CE1 
1878 C  CE2 . PHE A 230 ? 0.1601 0.1689 0.1353 0.0200  -0.0032 -0.0086 231 PHE A CE2 
1879 C  CZ  . PHE A 230 ? 0.1625 0.1391 0.1747 0.0024  -0.0026 -0.0292 231 PHE A CZ  
1880 N  N   . ASN A 231 ? 0.1375 0.1506 0.1427 0.0096  0.0258  -0.0079 232 ASN A N   
1881 C  CA  . ASN A 231 ? 0.1381 0.1456 0.1630 0.0173  0.0353  0.0147  232 ASN A CA  
1882 C  C   . ASN A 231 ? 0.1544 0.1434 0.1558 0.0175  0.0347  0.0138  232 ASN A C   
1883 O  O   . ASN A 231 ? 0.1546 0.1364 0.1835 0.0304  0.0241  0.0003  232 ASN A O   
1884 C  CB  . ASN A 231 ? 0.1729 0.1499 0.1837 0.0212  0.0170  -0.0142 232 ASN A CB  
1885 C  CG  . ASN A 231 ? 0.1626 0.1248 0.1862 0.0240  0.0214  -0.0021 232 ASN A CG  
1886 O  OD1 . ASN A 231 ? 0.1648 0.1307 0.2225 0.0358  0.0402  0.0047  232 ASN A OD1 
1887 N  ND2 . ASN A 231 ? 0.2559 0.1504 0.2003 0.0512  0.0016  -0.0122 232 ASN A ND2 
1888 N  N   . GLY A 232 ? 0.1697 0.1554 0.1475 0.0005  0.0215  0.0034  233 GLY A N   
1889 C  CA  . GLY A 232 ? 0.2056 0.1601 0.1450 0.0222  0.0347  0.0099  233 GLY A CA  
1890 C  C   . GLY A 232 ? 0.2588 0.1317 0.1483 0.0162  0.0228  0.0051  233 GLY A C   
1891 O  O   . GLY A 232 ? 0.2617 0.1364 0.1729 0.0181  0.0499  0.0116  233 GLY A O   
1892 N  N   . GLU A 233 ? 0.2256 0.2221 0.1420 -0.0140 0.0392  0.0155  234 GLU A N   
1893 C  CA  . GLU A 233 ? 0.2939 0.2791 0.1176 -0.0016 0.0281  0.0040  234 GLU A CA  
1894 C  C   . GLU A 233 ? 0.3431 0.2300 0.1539 0.0116  0.0565  -0.0186 234 GLU A C   
1895 O  O   . GLU A 233 ? 0.3073 0.2032 0.2279 0.0166  0.0790  0.0216  234 GLU A O   
1896 C  CB  . GLU A 233 ? 0.3085 0.3066 0.1622 -0.0185 0.0277  0.0133  234 GLU A CB  
1897 C  CG  . GLU A 233 ? 0.4683 0.2914 0.1745 -0.0916 0.0204  0.0288  234 GLU A CG  
1898 C  CD  . GLU A 233 ? 0.4985 0.3739 0.3917 -0.1133 -0.0514 -0.0176 234 GLU A CD  
1899 O  OE1 . GLU A 233 ? 0.4117 0.7684 0.5010 0.0680  0.0379  0.0164  234 GLU A OE1 
1900 O  OE2 . GLU A 233 ? 0.8860 1.0175 0.3134 -0.0981 -0.0381 -0.0590 234 GLU A OE2 
1901 N  N   . GLY A 234 ? 0.3951 0.2574 0.1945 0.0882  0.0554  0.0005  235 GLY A N   
1902 C  CA  . GLY A 234 ? 0.4263 0.3116 0.2158 0.1056  0.0935  -0.0034 235 GLY A CA  
1903 C  C   . GLY A 234 ? 0.3981 0.3701 0.1579 -0.0493 0.0639  0.0409  235 GLY A C   
1904 O  O   . GLY A 234 ? 0.4243 0.6379 0.5068 0.1779  -0.0485 0.0329  235 GLY A O   
1905 N  N   . GLU A 235 ? 0.3363 0.1991 0.1729 0.0353  0.0508  0.0290  236 GLU A N   
1906 C  CA  . GLU A 235 ? 0.2606 0.2086 0.1743 0.0120  0.0771  0.0204  236 GLU A CA  
1907 C  C   . GLU A 235 ? 0.2379 0.2290 0.1872 0.0245  0.0560  0.0241  236 GLU A C   
1908 O  O   . GLU A 235 ? 0.2588 0.2177 0.2237 0.0740  0.0228  0.0034  236 GLU A O   
1909 C  CB  . GLU A 235 ? 0.3380 0.1750 0.2046 -0.0348 0.0640  0.0038  236 GLU A CB  
1910 C  CG  . GLU A 235 ? 0.3363 0.1736 0.3282 -0.0841 0.1254  -0.0305 236 GLU A CG  
1911 C  CD  . GLU A 235 ? 0.3568 0.2485 0.3288 -0.0298 0.0628  -0.0501 236 GLU A CD  
1912 O  OE1 . GLU A 235 ? 0.2179 0.2409 0.4453 -0.0015 -0.0011 0.0952  236 GLU A OE1 
1913 O  OE2 . GLU A 235 ? 0.6258 0.2452 0.5037 -0.0326 0.2347  0.0200  236 GLU A OE2 
1914 N  N   . PRO A 236 ? 0.2194 0.1942 0.2230 0.0295  0.0405  0.0081  237 PRO A N   
1915 C  CA  . PRO A 236 ? 0.2011 0.1824 0.2182 0.0201  0.0413  0.0278  237 PRO A CA  
1916 C  C   . PRO A 236 ? 0.1912 0.1294 0.2020 0.0219  0.0487  -0.0005 237 PRO A C   
1917 O  O   . PRO A 236 ? 0.1939 0.1791 0.2020 0.0158  0.0370  -0.0273 237 PRO A O   
1918 C  CB  . PRO A 236 ? 0.1586 0.2311 0.2955 0.0316  0.0405  0.0222  237 PRO A CB  
1919 C  CG  . PRO A 236 ? 0.1852 0.2228 0.3654 0.0598  0.0853  0.0701  237 PRO A CG  
1920 C  CD  . PRO A 236 ? 0.2515 0.1811 0.3110 0.0336  0.0228  0.0157  237 PRO A CD  
1921 N  N   . GLU A 237 ? 0.2027 0.1317 0.2023 0.0309  0.0484  0.0034  238 GLU A N   
1922 C  CA  . GLU A 237 ? 0.1863 0.1538 0.1921 0.0136  0.0488  -0.0186 238 GLU A CA  
1923 C  C   . GLU A 237 ? 0.1841 0.1238 0.2089 0.0265  0.0150  -0.0242 238 GLU A C   
1924 O  O   . GLU A 237 ? 0.1992 0.1324 0.2041 0.0199  -0.0019 -0.0215 238 GLU A O   
1925 C  CB  . GLU A 237 ? 0.2258 0.1734 0.2494 0.0239  -0.0284 -0.0125 238 GLU A CB  
1926 C  CG  . GLU A 237 ? 0.2495 0.1852 0.3264 -0.0250 -0.0054 0.0283  238 GLU A CG  
1927 C  CD  . GLU A 237 ? 0.3228 0.5060 0.3322 -0.1403 -0.1366 0.0710  238 GLU A CD  
1928 O  OE1 . GLU A 237 ? 0.5653 0.5442 0.3986 -0.2299 -0.0366 0.0149  238 GLU A OE1 
1929 O  OE2 . GLU A 237 ? 0.3783 0.5491 0.4756 -0.1720 -0.0323 0.0682  238 GLU A OE2 
1930 N  N   . GLU A 238 ? 0.1535 0.1400 0.1729 0.0164  0.0387  -0.0042 239 GLU A N   
1931 C  CA  . GLU A 238 ? 0.1447 0.1443 0.1738 0.0091  0.0399  0.0035  239 GLU A CA  
1932 C  C   . GLU A 238 ? 0.1386 0.1181 0.1607 0.0204  0.0483  0.0019  239 GLU A C   
1933 O  O   . GLU A 238 ? 0.1714 0.1291 0.2305 0.0403  0.0333  0.0140  239 GLU A O   
1934 C  CB  . GLU A 238 ? 0.1421 0.1876 0.2591 -0.0125 0.0398  -0.0313 239 GLU A CB  
1935 C  CG  . GLU A 238 ? 0.1671 0.2179 0.2595 0.0237  0.0189  -0.0592 239 GLU A CG  
1936 C  CD  . GLU A 238 ? 0.2186 0.2176 0.2106 -0.0138 0.0370  -0.0573 239 GLU A CD  
1937 O  OE1 . GLU A 238 ? 0.2969 0.3489 0.1921 -0.0520 0.0178  -0.0647 239 GLU A OE1 
1938 O  OE2 . GLU A 238 ? 0.2544 0.2518 0.2402 -0.0512 0.0117  -0.0192 239 GLU A OE2 
1939 N  N   A LEU A 239 ? 0.1337 0.1338 0.1510 0.0179  0.0313  0.0000  240 LEU A N   
1940 N  N   B LEU A 239 ? 0.1364 0.1418 0.1482 0.0083  0.0240  0.0085  240 LEU A N   
1941 C  CA  A LEU A 239 ? 0.1367 0.1630 0.1346 0.0306  0.0337  0.0042  240 LEU A CA  
1942 C  CA  B LEU A 239 ? 0.1414 0.1364 0.1309 0.0018  0.0344  0.0018  240 LEU A CA  
1943 C  C   A LEU A 239 ? 0.1314 0.1155 0.1133 0.0047  0.0358  0.0277  240 LEU A C   
1944 C  C   B LEU A 239 ? 0.1223 0.1467 0.1205 0.0175  0.0077  -0.0082 240 LEU A C   
1945 O  O   A LEU A 239 ? 0.1291 0.1185 0.1590 -0.0064 0.0070  0.0374  240 LEU A O   
1946 O  O   B LEU A 239 ? 0.1375 0.1395 0.1198 0.0321  0.0035  -0.0260 240 LEU A O   
1947 C  CB  A LEU A 239 ? 0.1479 0.1619 0.1727 0.0229  -0.0085 -0.0221 240 LEU A CB  
1948 C  CB  B LEU A 239 ? 0.1525 0.1646 0.2287 -0.0435 0.0104  0.0117  240 LEU A CB  
1949 C  CG  A LEU A 239 ? 0.1561 0.2244 0.2197 0.0807  0.0170  -0.0831 240 LEU A CG  
1950 C  CG  B LEU A 239 ? 0.1228 0.1747 0.2483 -0.0421 0.0074  0.0117  240 LEU A CG  
1951 C  CD1 A LEU A 239 ? 0.2393 0.2986 0.2570 0.0480  0.0165  -0.0373 240 LEU A CD1 
1952 C  CD1 B LEU A 239 ? 0.1866 0.1012 0.2610 -0.0174 -0.0118 0.0081  240 LEU A CD1 
1953 C  CD2 A LEU A 239 ? 0.1898 0.1181 0.1453 0.0188  0.0127  -0.0726 240 LEU A CD2 
1954 C  CD2 B LEU A 239 ? 0.1479 0.1064 0.2397 0.0147  0.0631  -0.0170 240 LEU A CD2 
1955 N  N   . MET A 240 ? 0.1284 0.1432 0.1423 0.0282  0.0340  -0.0017 241 MET A N   
1956 C  CA  . MET A 240 ? 0.1386 0.1551 0.1053 0.0295  0.0160  0.0042  241 MET A CA  
1957 C  C   . MET A 240 ? 0.1196 0.1664 0.1102 0.0214  0.0212  -0.0094 241 MET A C   
1958 O  O   . MET A 240 ? 0.1313 0.1492 0.1384 0.0248  0.0027  -0.0096 241 MET A O   
1959 C  CB  . MET A 240 ? 0.1447 0.1348 0.1479 0.0294  0.0305  0.0049  241 MET A CB  
1960 C  CG  . MET A 240 ? 0.1454 0.1232 0.1461 0.0120  0.0119  -0.0207 241 MET A CG  
1961 S  SD  . MET A 240 ? 0.1526 0.1349 0.1795 0.0087  0.0313  -0.0013 241 MET A SD  
1962 C  CE  . MET A 240 ? 0.1590 0.1604 0.1679 -0.0024 0.0050  0.0190  241 MET A CE  
1963 N  N   . VAL A 241 ? 0.1411 0.1190 0.1335 0.0210  -0.0019 -0.0058 242 VAL A N   
1964 C  CA  . VAL A 241 ? 0.1513 0.1141 0.1235 0.0154  -0.0030 -0.0086 242 VAL A CA  
1965 C  C   . VAL A 241 ? 0.1311 0.0831 0.1201 0.0337  -0.0055 -0.0122 242 VAL A C   
1966 O  O   . VAL A 241 ? 0.1292 0.1257 0.1447 0.0179  0.0078  -0.0171 242 VAL A O   
1967 C  CB  . VAL A 241 ? 0.1499 0.1163 0.1346 0.0148  0.0046  -0.0262 242 VAL A CB  
1968 C  CG1 . VAL A 241 ? 0.1763 0.1210 0.1770 0.0020  -0.0228 -0.0252 242 VAL A CG1 
1969 C  CG2 . VAL A 241 ? 0.1641 0.1272 0.1711 0.0452  0.0260  -0.0225 242 VAL A CG2 
1970 N  N   . ASP A 242 ? 0.1368 0.1016 0.1081 0.0179  0.0026  -0.0177 243 ASP A N   
1971 C  CA  . ASP A 242 ? 0.1335 0.0869 0.1237 0.0225  -0.0004 -0.0083 243 ASP A CA  
1972 C  C   . ASP A 242 ? 0.1307 0.0873 0.1257 0.0214  0.0037  -0.0194 243 ASP A C   
1973 O  O   . ASP A 242 ? 0.1353 0.1174 0.1729 0.0212  -0.0308 -0.0265 243 ASP A O   
1974 C  CB  . ASP A 242 ? 0.1353 0.0952 0.1687 0.0302  -0.0089 -0.0167 243 ASP A CB  
1975 C  CG  . ASP A 242 ? 0.1446 0.0980 0.1502 0.0376  -0.0030 -0.0152 243 ASP A CG  
1976 O  OD1 . ASP A 242 ? 0.1594 0.1038 0.1443 0.0397  0.0029  -0.0161 243 ASP A OD1 
1977 O  OD2 . ASP A 242 ? 0.1831 0.1199 0.1914 0.0376  0.0164  -0.0348 243 ASP A OD2 
1978 N  N   . ASN A 243 ? 0.1169 0.0888 0.1205 0.0187  0.0109  -0.0228 244 ASN A N   
1979 C  CA  . ASN A 243 ? 0.1116 0.0901 0.1055 0.0074  0.0017  -0.0083 244 ASN A CA  
1980 C  C   . ASN A 243 ? 0.0995 0.1045 0.1071 0.0088  -0.0002 -0.0087 244 ASN A C   
1981 O  O   . ASN A 243 ? 0.1264 0.1151 0.1357 0.0354  0.0051  -0.0129 244 ASN A O   
1982 C  CB  . ASN A 243 ? 0.1057 0.1106 0.1256 0.0116  -0.0032 0.0017  244 ASN A CB  
1983 C  CG  . ASN A 243 ? 0.1117 0.1147 0.1170 -0.0030 0.0136  0.0113  244 ASN A CG  
1984 O  OD1 . ASN A 243 ? 0.1140 0.1216 0.1421 0.0092  0.0109  0.0233  244 ASN A OD1 
1985 N  ND2 . ASN A 243 ? 0.1353 0.1459 0.1346 -0.0018 -0.0160 0.0424  244 ASN A ND2 
1986 N  N   . TRP A 244 ? 0.1244 0.1111 0.0951 0.0006  -0.0144 -0.0054 245 TRP A N   
1987 C  CA  . TRP A 244 ? 0.1357 0.1111 0.1004 0.0018  -0.0071 -0.0085 245 TRP A CA  
1988 C  C   . TRP A 244 ? 0.1268 0.1104 0.0987 0.0046  0.0070  -0.0144 245 TRP A C   
1989 O  O   . TRP A 244 ? 0.1225 0.1324 0.1382 0.0222  0.0031  -0.0244 245 TRP A O   
1990 C  CB  . TRP A 244 ? 0.1496 0.0889 0.1122 0.0141  -0.0032 -0.0093 245 TRP A CB  
1991 C  CG  . TRP A 244 ? 0.1215 0.0930 0.1316 0.0096  0.0066  0.0069  245 TRP A CG  
1992 C  CD1 . TRP A 244 ? 0.1238 0.0766 0.1443 0.0022  -0.0063 -0.0055 245 TRP A CD1 
1993 C  CD2 . TRP A 244 ? 0.1330 0.1049 0.1254 0.0089  -0.0010 -0.0042 245 TRP A CD2 
1994 N  NE1 . TRP A 244 ? 0.1307 0.0977 0.1304 0.0103  -0.0052 -0.0058 245 TRP A NE1 
1995 C  CE2 . TRP A 244 ? 0.1410 0.0919 0.1421 0.0175  -0.0071 0.0116  245 TRP A CE2 
1996 C  CE3 . TRP A 244 ? 0.1496 0.1250 0.1239 0.0109  -0.0013 0.0172  245 TRP A CE3 
1997 C  CZ2 . TRP A 244 ? 0.1582 0.1170 0.1490 0.0217  -0.0179 0.0293  245 TRP A CZ2 
1998 C  CZ3 . TRP A 244 ? 0.1783 0.1159 0.1629 0.0230  -0.0048 0.0129  245 TRP A CZ3 
1999 C  CH2 . TRP A 244 ? 0.1673 0.1243 0.1586 0.0407  0.0001  0.0221  245 TRP A CH2 
2000 N  N   . ARG A 245 ? 0.1280 0.1207 0.1077 0.0037  0.0065  -0.0186 246 ARG A N   
2001 C  CA  . ARG A 245 ? 0.1152 0.1059 0.1040 -0.0020 -0.0018 -0.0176 246 ARG A CA  
2002 C  C   . ARG A 245 ? 0.1221 0.0987 0.1321 0.0005  0.0053  -0.0118 246 ARG A C   
2003 O  O   . ARG A 245 ? 0.1314 0.1267 0.1511 0.0031  0.0250  -0.0170 246 ARG A O   
2004 C  CB  . ARG A 245 ? 0.1317 0.1083 0.1128 0.0010  -0.0039 -0.0207 246 ARG A CB  
2005 C  CG  . ARG A 245 ? 0.1272 0.1102 0.1248 -0.0111 -0.0083 -0.0152 246 ARG A CG  
2006 C  CD  . ARG A 245 ? 0.1329 0.1083 0.1300 -0.0060 -0.0091 -0.0230 246 ARG A CD  
2007 N  NE  . ARG A 245 ? 0.1164 0.1233 0.1332 -0.0167 -0.0030 -0.0170 246 ARG A NE  
2008 C  CZ  . ARG A 245 ? 0.1219 0.1403 0.1137 -0.0186 0.0030  -0.0201 246 ARG A CZ  
2009 N  NH1 . ARG A 245 ? 0.1329 0.1356 0.1556 -0.0043 0.0272  -0.0149 246 ARG A NH1 
2010 N  NH2 . ARG A 245 ? 0.1307 0.1526 0.1492 -0.0323 -0.0093 -0.0322 246 ARG A NH2 
2011 N  N   . PRO A 246 ? 0.1477 0.1125 0.1225 0.0100  0.0134  -0.0016 247 PRO A N   
2012 C  CA  . PRO A 246 ? 0.1612 0.1237 0.1293 0.0100  0.0055  0.0066  247 PRO A CA  
2013 C  C   . PRO A 246 ? 0.1399 0.1155 0.1208 0.0120  -0.0011 0.0016  247 PRO A C   
2014 O  O   . PRO A 246 ? 0.1526 0.1203 0.1378 0.0078  -0.0177 -0.0062 247 PRO A O   
2015 C  CB  . PRO A 246 ? 0.2054 0.1536 0.1569 0.0569  -0.0034 0.0210  247 PRO A CB  
2016 C  CG  . PRO A 246 ? 0.2402 0.2619 0.3412 0.0706  0.0731  0.1577  247 PRO A CG  
2017 C  CD  . PRO A 246 ? 0.1414 0.1601 0.1628 0.0396  0.0006  0.0204  247 PRO A CD  
2018 N  N   . ALA A 247 ? 0.1528 0.1282 0.1349 0.0165  0.0088  0.0119  248 ALA A N   
2019 C  CA  . ALA A 247 ? 0.1672 0.1285 0.1229 0.0042  0.0108  -0.0006 248 ALA A CA  
2020 C  C   . ALA A 247 ? 0.1493 0.1201 0.1400 0.0357  -0.0053 0.0088  248 ALA A C   
2021 O  O   . ALA A 247 ? 0.1635 0.1277 0.1755 0.0345  -0.0138 0.0113  248 ALA A O   
2022 C  CB  . ALA A 247 ? 0.2092 0.1540 0.1393 -0.0190 0.0373  0.0022  248 ALA A CB  
2023 N  N   . GLN A 248 ? 0.1330 0.1206 0.1364 0.0049  -0.0026 0.0089  249 GLN A N   
2024 C  CA  . GLN A 248 ? 0.1346 0.1427 0.1389 0.0228  -0.0138 -0.0096 249 GLN A CA  
2025 C  C   . GLN A 248 ? 0.1515 0.1471 0.1500 0.0240  -0.0137 0.0010  249 GLN A C   
2026 O  O   . GLN A 248 ? 0.1662 0.1472 0.1515 0.0201  0.0005  0.0087  249 GLN A O   
2027 C  CB  . GLN A 248 ? 0.1665 0.1307 0.1413 0.0027  -0.0017 -0.0061 249 GLN A CB  
2028 C  CG  . GLN A 248 ? 0.1574 0.1364 0.1339 -0.0034 0.0032  -0.0034 249 GLN A CG  
2029 C  CD  . GLN A 248 ? 0.1445 0.1738 0.1840 -0.0111 0.0100  -0.0077 249 GLN A CD  
2030 O  OE1 . GLN A 248 ? 0.1562 0.2188 0.1770 -0.0322 0.0050  -0.0228 249 GLN A OE1 
2031 N  NE2 . GLN A 248 ? 0.1842 0.1805 0.1424 0.0157  -0.0039 -0.0078 249 GLN A NE2 
2032 N  N   . PRO A 249 ? 0.1669 0.1686 0.1402 0.0239  -0.0087 -0.0089 250 PRO A N   
2033 C  CA  . PRO A 249 ? 0.2011 0.2043 0.1348 0.0557  -0.0071 0.0006  250 PRO A CA  
2034 C  C   . PRO A 249 ? 0.1942 0.1443 0.1302 0.0313  -0.0219 0.0086  250 PRO A C   
2035 O  O   . PRO A 249 ? 0.1678 0.1662 0.1474 0.0335  -0.0156 0.0087  250 PRO A O   
2036 C  CB  . PRO A 249 ? 0.2032 0.3676 0.1748 0.1050  -0.0702 -0.0754 250 PRO A CB  
2037 C  CG  . PRO A 249 ? 0.2276 0.3750 0.1641 -0.0223 -0.0443 -0.0177 250 PRO A CG  
2038 C  CD  . PRO A 249 ? 0.1493 0.2984 0.1490 0.0260  -0.0247 -0.0312 250 PRO A CD  
2039 N  N   . LEU A 250 ? 0.2041 0.1457 0.1224 0.0342  -0.0049 0.0120  251 LEU A N   
2040 C  CA  . LEU A 250 ? 0.1654 0.1544 0.1513 0.0134  -0.0058 0.0092  251 LEU A CA  
2041 C  C   . LEU A 250 ? 0.1831 0.1607 0.1120 0.0257  -0.0194 0.0087  251 LEU A C   
2042 O  O   . LEU A 250 ? 0.1734 0.1431 0.1650 0.0282  -0.0387 0.0012  251 LEU A O   
2043 C  CB  . LEU A 250 ? 0.1960 0.1619 0.2068 -0.0066 0.0070  0.0186  251 LEU A CB  
2044 C  CG  . LEU A 250 ? 0.2068 0.2165 0.1930 0.0034  0.0212  -0.0099 251 LEU A CG  
2045 C  CD1 . LEU A 250 ? 0.1955 0.2612 0.1543 -0.0398 -0.0109 -0.0223 251 LEU A CD1 
2046 C  CD2 . LEU A 250 ? 0.3436 0.2133 0.2466 -0.0668 0.0086  0.0097  251 LEU A CD2 
2047 N  N   . LYS A 251 ? 0.1877 0.1716 0.1403 0.0342  -0.0391 0.0048  252 LYS A N   
2048 C  CA  . LYS A 251 ? 0.1698 0.2481 0.1388 0.0077  -0.0302 -0.0299 252 LYS A CA  
2049 C  C   . LYS A 251 ? 0.1788 0.2034 0.1648 0.0337  -0.0359 -0.0111 252 LYS A C   
2050 O  O   . LYS A 251 ? 0.2357 0.2606 0.1913 -0.0100 0.0031  -0.0053 252 LYS A O   
2051 C  CB  . LYS A 251 ? 0.1932 0.2402 0.2027 -0.0240 -0.0188 -0.0592 252 LYS A CB  
2052 C  CG  . LYS A 251 ? 0.2645 0.2708 0.2029 -0.0041 0.0587  -0.0383 252 LYS A CG  
2053 C  CD  . LYS A 251 ? 0.3009 0.2960 0.2175 0.0156  0.0344  0.0229  252 LYS A CD  
2054 C  CE  . LYS A 251 ? 0.2427 0.3039 0.3636 0.0116  0.0129  -0.0201 252 LYS A CE  
2055 N  NZ  . LYS A 251 ? 0.2204 0.3843 0.4905 0.0238  0.0031  0.1024  252 LYS A NZ  
2056 N  N   . ASN A 252 ? 0.2242 0.1975 0.1216 0.0199  -0.0174 -0.0055 253 ASN A N   
2057 C  CA  . ASN A 252 ? 0.2687 0.4068 0.1533 0.0413  -0.0577 -0.0954 253 ASN A CA  
2058 C  C   . ASN A 252 ? 0.2787 0.2916 0.3470 0.0971  -0.0640 -0.0968 253 ASN A C   
2059 O  O   . ASN A 252 ? 0.3204 0.2807 0.2815 0.0670  -0.0049 -0.0552 253 ASN A O   
2060 C  CB  . ASN A 252 ? 0.2705 0.4447 0.2593 -0.0094 -0.0446 -0.1555 253 ASN A CB  
2061 C  CG  . ASN A 252 ? 0.3754 0.3704 0.2802 -0.0373 0.0365  -0.0910 253 ASN A CG  
2062 O  OD1 . ASN A 252 ? 0.6432 0.7056 0.4235 -0.2426 0.1157  0.0201  253 ASN A OD1 
2063 N  ND2 . ASN A 252 ? 0.3141 0.3738 0.3921 -0.0318 0.0633  -0.1096 253 ASN A ND2 
2064 N  N   . ARG A 253 ? 0.1844 0.3217 0.1396 0.0245  -0.0159 0.0385  254 ARG A N   
2065 C  CA  . ARG A 253 ? 0.1668 0.2032 0.1041 0.0255  0.0059  0.0080  254 ARG A CA  
2066 C  C   . ARG A 253 ? 0.2269 0.1641 0.1384 0.0259  0.0555  -0.0119 254 ARG A C   
2067 O  O   . ARG A 253 ? 0.3019 0.1975 0.2681 0.0546  0.1111  0.0525  254 ARG A O   
2068 C  CB  . ARG A 253 ? 0.1939 0.1630 0.1044 -0.0079 -0.0063 -0.0020 254 ARG A CB  
2069 C  CG  . ARG A 253 ? 0.1890 0.1389 0.1222 -0.0103 -0.0148 -0.0042 254 ARG A CG  
2070 C  CD  . ARG A 253 ? 0.1658 0.1353 0.1229 0.0160  0.0089  -0.0190 254 ARG A CD  
2071 N  NE  . ARG A 253 ? 0.1395 0.1223 0.1141 0.0087  -0.0023 0.0017  254 ARG A NE  
2072 C  CZ  . ARG A 253 ? 0.1177 0.1071 0.0901 -0.0040 0.0039  0.0010  254 ARG A CZ  
2073 N  NH1 . ARG A 253 ? 0.1152 0.1318 0.1075 -0.0072 -0.0141 0.0179  254 ARG A NH1 
2074 N  NH2 . ARG A 253 ? 0.1381 0.1129 0.1142 0.0018  -0.0064 -0.0022 254 ARG A NH2 
2075 N  N   . GLN A 254 ? 0.1730 0.2140 0.1522 0.0157  -0.0027 -0.0535 255 GLN A N   
2076 C  CA  . GLN A 254 ? 0.1870 0.2157 0.1546 -0.0143 -0.0150 -0.0273 255 GLN A CA  
2077 C  C   . GLN A 254 ? 0.1949 0.1698 0.1543 -0.0047 -0.0190 -0.0070 255 GLN A C   
2078 O  O   . GLN A 254 ? 0.2888 0.1619 0.2179 -0.0263 -0.0581 -0.0124 255 GLN A O   
2079 C  CB  . GLN A 254 ? 0.2770 0.3992 0.1489 -0.0520 0.0118  -0.0996 255 GLN A CB  
2080 C  CG  . GLN A 254 ? 0.3222 0.3475 0.2415 -0.0331 0.0243  -0.0299 255 GLN A CG  
2081 N  N   . ILE A 255 ? 0.1628 0.1654 0.1297 -0.0066 -0.0043 -0.0023 256 ILE A N   
2082 C  CA  . ILE A 255 ? 0.1571 0.1474 0.1327 0.0108  -0.0029 0.0043  256 ILE A CA  
2083 C  C   . ILE A 255 ? 0.1579 0.1526 0.1303 -0.0036 0.0021  0.0060  256 ILE A C   
2084 O  O   . ILE A 255 ? 0.1977 0.1621 0.1496 0.0113  0.0173  0.0207  256 ILE A O   
2085 C  CB  . ILE A 255 ? 0.1687 0.1629 0.1149 -0.0021 -0.0081 -0.0155 256 ILE A CB  
2086 C  CG1 . ILE A 255 ? 0.1691 0.1737 0.1522 0.0402  -0.0010 -0.0153 256 ILE A CG1 
2087 C  CG2 . ILE A 255 ? 0.1974 0.1842 0.1374 0.0188  -0.0301 -0.0309 256 ILE A CG2 
2088 C  CD1 . ILE A 255 ? 0.2215 0.1508 0.1932 0.0029  0.0126  -0.0272 256 ILE A CD1 
2089 N  N   . LYS A 256 ? 0.1403 0.1671 0.1141 0.0036  -0.0041 -0.0069 257 LYS A N   
2090 C  CA  . LYS A 256 ? 0.1542 0.1883 0.0962 0.0127  0.0114  -0.0046 257 LYS A CA  
2091 C  C   . LYS A 256 ? 0.1597 0.2150 0.1004 -0.0153 0.0092  0.0210  257 LYS A C   
2092 O  O   . LYS A 256 ? 0.2010 0.2383 0.0910 -0.0575 0.0067  0.0049  257 LYS A O   
2093 C  CB  . LYS A 256 ? 0.1835 0.1928 0.1701 0.0125  -0.0029 -0.0326 257 LYS A CB  
2094 C  CG  . LYS A 256 ? 0.2284 0.2662 0.2565 -0.0215 0.0011  -0.0829 257 LYS A CG  
2095 C  CD  . LYS A 256 ? 0.3983 0.3547 0.4551 -0.0403 0.0469  -0.1819 257 LYS A CD  
2096 C  CE  . LYS A 256 ? 0.5271 0.6463 0.6032 -0.1963 -0.0174 -0.2870 257 LYS A CE  
2097 N  NZ  . LYS A 256 ? 0.4601 0.5978 0.7142 -0.1206 0.1520  -0.0956 257 LYS A NZ  
2098 N  N   . ALA A 257 ? 0.1336 0.2046 0.1307 -0.0096 0.0126  0.0209  258 ALA A N   
2099 C  CA  . ALA A 257 ? 0.1574 0.1967 0.1302 0.0092  -0.0019 -0.0076 258 ALA A CA  
2100 C  C   . ALA A 257 ? 0.1564 0.1880 0.0980 -0.0052 0.0217  -0.0186 258 ALA A C   
2101 O  O   . ALA A 257 ? 0.1747 0.2309 0.1013 0.0072  0.0133  -0.0100 258 ALA A O   
2102 C  CB  . ALA A 257 ? 0.1766 0.1964 0.1928 -0.0026 0.0146  0.0290  258 ALA A CB  
2103 N  N   . SER A 258 ? 0.1402 0.1964 0.1298 -0.0041 0.0116  -0.0076 259 SER A N   
2104 C  CA  . SER A 258 ? 0.1571 0.2050 0.1635 0.0168  0.0093  0.0081  259 SER A CA  
2105 C  C   . SER A 258 ? 0.1637 0.2409 0.1546 -0.0085 0.0386  -0.0114 259 SER A C   
2106 O  O   . SER A 258 ? 0.1834 0.3359 0.2185 0.0454  0.0535  0.0118  259 SER A O   
2107 C  CB  . SER A 258 ? 0.1924 0.2327 0.1331 0.0125  -0.0233 -0.0130 259 SER A CB  
2108 O  OG  . SER A 258 ? 0.1565 0.2375 0.1162 0.0158  0.0163  0.0025  259 SER A OG  
2109 N  N   . PHE A 259 ? 0.1723 0.2559 0.1528 -0.0411 0.0225  0.0000  260 PHE A N   
2110 C  CA  . PHE A 259 ? 0.2215 0.2646 0.1993 -0.0876 0.0153  0.0074  260 PHE A CA  
2111 C  C   . PHE A 259 ? 0.2688 0.3535 0.1765 -0.0692 0.0278  0.0109  260 PHE A C   
2112 O  O   . PHE A 259 ? 0.3116 0.2405 0.2085 -0.0715 -0.0136 0.0451  260 PHE A O   
2113 C  CB  . PHE A 259 ? 0.1827 0.2488 0.2289 -0.0519 0.0077  -0.0212 260 PHE A CB  
2114 C  CG  . PHE A 259 ? 0.1763 0.2300 0.1858 -0.0214 -0.0244 0.0237  260 PHE A CG  
2115 C  CD1 . PHE A 259 ? 0.1583 0.2533 0.1558 -0.0318 -0.0043 -0.0047 260 PHE A CD1 
2116 C  CD2 . PHE A 259 ? 0.2409 0.2296 0.2537 -0.0162 -0.0122 0.0242  260 PHE A CD2 
2117 C  CE1 . PHE A 259 ? 0.2061 0.2357 0.2545 -0.0163 -0.0283 -0.0527 260 PHE A CE1 
2118 C  CE2 . PHE A 259 ? 0.2491 0.2463 0.3359 -0.0179 0.0067  0.0501  260 PHE A CE2 
2119 C  CZ  . PHE A 259 ? 0.2217 0.2722 0.2812 -0.0103 0.0111  -0.0027 260 PHE A CZ  
2120 N  N   . LYS A 260 ? 0.4378 0.4511 0.2549 -0.1760 0.0740  0.0632  261 LYS A N   
2121 C  CA  . LYS A 260 ? 0.6680 0.6271 0.3161 -0.0343 0.0310  0.2046  261 LYS A CA  
2122 C  C   . LYS A 260 ? 0.7496 0.7993 0.4270 -0.0620 0.1101  0.1187  261 LYS A C   
2123 O  O   . LYS A 260 ? 0.4287 1.1571 0.7463 -0.0736 0.0125  0.1625  261 LYS A O   
2124 C  CB  . LYS A 260 ? 0.8450 0.7810 0.4656 0.0160  0.2277  0.0900  261 LYS A CB  
2125 C  CG  . LYS A 260 ? 0.6939 0.7346 0.6610 -0.0824 0.0571  0.1614  261 LYS A CG  
2126 C  CD  . LYS A 260 ? 0.5579 0.5704 0.7837 -0.0565 0.2475  -0.0282 261 LYS A CD  
2127 O  OXT . LYS A 260 ? 0.9416 1.1463 1.1417 -0.1223 -0.2548 0.1574  261 LYS A OXT 
2128 ZN ZN  . ZN  B .   ? 0.1140 0.0815 0.1063 0.0079  -0.0052 -0.0059 301 ZN  A ZN  
2129 O  O18 . E1F C .   ? 0.1122 0.1046 0.1076 0.0134  -0.0151 0.0006  302 E1F A O18 
2130 C  C13 . E1F C .   ? 0.4068 0.2239 0.4360 0.0222  0.0358  -0.0597 302 E1F A C13 
2131 C  C1  . E1F C .   ? 0.2546 0.1834 0.1888 -0.0326 -0.0158 0.0550  302 E1F A C1  
2132 C  C2  . E1F C .   ? 0.1481 0.0908 0.1838 -0.0047 -0.0240 0.0066  302 E1F A C2  
2133 CL CL1 . E1F C .   ? 0.1579 0.1020 0.2779 0.0085  -0.0063 -0.0392 302 E1F A CL1 
2134 C  C21 . E1F C .   ? 0.2050 0.1088 0.2056 -0.0215 -0.0315 0.0272  302 E1F A C21 
2135 C  C5  . E1F C .   ? 0.2897 0.1899 0.2109 -0.0375 0.0565  0.0378  302 E1F A C5  
2136 C  C4  . E1F C .   ? 0.2054 0.1648 0.1438 -0.0226 0.0133  0.0058  302 E1F A C4  
2137 C  C3  . E1F C .   ? 0.1396 0.0899 0.1572 -0.0071 -0.0102 -0.0015 302 E1F A C3  
2138 S  S16 . E1F C .   ? 0.1217 0.0901 0.1221 0.0066  -0.0117 -0.0079 302 E1F A S16 
2139 N  N19 . E1F C .   ? 0.1143 0.0680 0.1556 -0.0122 -0.0012 -0.0091 302 E1F A N19 
2140 O  O17 . E1F C .   ? 0.1178 0.0949 0.1580 0.0150  -0.0081 -0.0158 302 E1F A O17 
2141 C  C6  . E1F C .   ? 0.3257 0.2160 0.3289 -0.0460 0.0624  0.0848  302 E1F A C6  
2142 O  O12 . E1F C .   ? 0.3458 0.2762 0.4692 0.0043  0.0314  0.1305  302 E1F A O12 
2143 C  C7  . E1F C .   ? 0.3470 0.2505 0.3547 -0.0591 0.0569  0.0603  302 E1F A C7  
2144 S  S8  . E1F C .   ? 0.4401 0.2986 0.3707 -0.1083 0.0523  0.0086  302 E1F A S8  
2145 C  C9  . E1F C .   ? 0.4536 0.2384 0.3382 -0.0644 0.0303  -0.0017 302 E1F A C9  
2146 N  N11 . E1F C .   ? 0.6179 0.2763 0.4312 -0.1537 0.0895  -0.0443 302 E1F A N11 
2147 C  C14 . E1F C .   ? 0.3850 0.2623 0.4468 0.0031  0.0629  -0.0675 302 E1F A C14 
2148 C  C15 . E1F C .   ? 0.3771 0.2201 0.4230 0.0223  0.0780  -0.0444 302 E1F A C15 
2149 N  N10 . E1F C .   ? 0.4067 0.2462 0.3473 0.0883  0.0362  0.0234  302 E1F A N10 
2150 C  C   . BEZ D .   ? 0.3503 0.4017 0.5177 -0.0473 0.1005  -0.2185 303 BEZ A C   
2151 O  O1  . BEZ D .   ? 0.4194 0.5577 0.5894 -0.1807 0.1115  -0.2258 303 BEZ A O1  
2152 O  O2  . BEZ D .   ? 0.3558 0.6400 0.7267 0.0081  0.0901  -0.3032 303 BEZ A O2  
2153 C  C1  . BEZ D .   ? 0.4005 0.4374 0.3544 -0.0445 0.0552  -0.1361 303 BEZ A C1  
2154 C  C2  . BEZ D .   ? 0.4691 0.5678 0.4514 0.0930  0.1747  -0.0998 303 BEZ A C2  
2155 C  C3  . BEZ D .   ? 0.3697 0.5653 0.1880 0.1732  -0.0560 -0.0988 303 BEZ A C3  
2156 C  C4  . BEZ D .   ? 0.3588 0.5396 0.2657 0.1258  -0.0889 -0.1351 303 BEZ A C4  
2157 C  C5  . BEZ D .   ? 0.2715 0.5119 0.3106 0.0336  0.0294  -0.0945 303 BEZ A C5  
2158 C  C6  . BEZ D .   ? 0.4301 0.5205 0.3324 -0.0948 -0.0356 -0.0841 303 BEZ A C6  
2159 S  S   . DMS E .   ? 0.2812 0.3553 0.3376 -0.0111 0.0273  -0.0555 304 DMS A S   
2160 O  O   . DMS E .   ? 0.4192 0.5212 0.4390 0.0729  0.0695  -0.2328 304 DMS A O   
2161 C  C1  . DMS E .   ? 0.4647 0.2947 0.6664 -0.0604 0.0770  -0.0145 304 DMS A C1  
2162 C  C2  . DMS E .   ? 0.2700 0.2802 0.2664 0.1124  -0.0391 -0.0640 304 DMS A C2  
2163 O  O   . HOH F .   ? 0.3352 0.1998 0.3750 0.0688  -0.0820 0.0170  401 HOH A O   
2164 O  O   . HOH F .   ? 0.3380 0.2186 0.5035 -0.0211 0.0311  -0.0936 402 HOH A O   
2165 O  O   . HOH F .   ? 0.4542 0.5575 0.3323 0.0165  -0.1127 0.0950  403 HOH A O   
2166 O  O   . HOH F .   ? 0.4114 0.3851 0.3424 -0.0675 -0.0480 0.1511  404 HOH A O   
2167 O  O   . HOH F .   ? 0.2262 0.3915 0.2881 -0.0864 0.0559  -0.0022 405 HOH A O   
2168 O  O   . HOH F .   ? 0.5034 0.5707 0.6528 0.0969  -0.0715 -0.0162 406 HOH A O   
2169 O  O   . HOH F .   ? 0.4070 0.3850 0.4941 0.1309  0.1680  0.1653  407 HOH A O   
2170 O  O   . HOH F .   ? 0.8124 0.3547 0.6564 -0.0841 0.1050  -0.0793 408 HOH A O   
2171 O  O   . HOH F .   ? 0.1630 0.0740 0.1842 0.0053  -0.0287 -0.0039 409 HOH A O   
2172 O  O   . HOH F .   ? 0.4134 0.3438 0.5928 -0.0934 0.0774  -0.1024 410 HOH A O   
2173 O  O   . HOH F .   ? 0.5235 0.6028 0.7013 0.2207  0.0879  0.0070  411 HOH A O   
2174 O  O   . HOH F .   ? 0.4373 0.3064 0.4954 0.0297  -0.1627 0.0683  412 HOH A O   
2175 O  O   . HOH F .   ? 0.4342 0.2870 0.3142 0.0867  0.0785  -0.0507 413 HOH A O   
2176 O  O   . HOH F .   ? 0.4979 0.5335 0.5924 -0.1220 0.1791  -0.0908 414 HOH A O   
2177 O  O   . HOH F .   ? 0.3041 0.3537 0.3901 -0.0189 0.0374  -0.0501 415 HOH A O   
2178 O  O   . HOH F .   ? 0.4164 0.4040 0.2960 0.0778  -0.0562 0.0315  416 HOH A O   
2179 O  O   . HOH F .   ? 0.1898 0.2118 0.1806 0.0147  0.0016  0.0455  417 HOH A O   
2180 O  O   . HOH F .   ? 0.6235 0.2897 0.5179 0.0122  -0.0054 -0.0237 418 HOH A O   
2181 O  O   . HOH F .   ? 0.3249 0.4675 0.4601 0.0489  0.0763  -0.0454 419 HOH A O   
2182 O  O   . HOH F .   ? 0.3953 0.4183 0.3985 0.1108  0.2135  0.0392  420 HOH A O   
2183 O  O   . HOH F .   ? 0.2807 0.4049 0.3501 -0.0526 0.0443  -0.1411 421 HOH A O   
2184 O  O   . HOH F .   ? 0.3549 0.4002 0.3985 -0.0773 0.1065  -0.1243 422 HOH A O   
2185 O  O   . HOH F .   ? 0.6355 0.6456 0.9572 -0.2963 -0.0026 0.0579  423 HOH A O   
2186 O  O   . HOH F .   ? 0.3442 0.3555 0.4340 -0.0182 -0.0586 0.1085  424 HOH A O   
2187 O  O   . HOH F .   ? 0.2574 0.2724 0.2307 0.0339  -0.0289 0.0033  425 HOH A O   
2188 O  O   . HOH F .   ? 0.5386 0.4754 0.4247 -0.1804 -0.0425 0.0440  426 HOH A O   
2189 O  O   . HOH F .   ? 0.2882 0.4021 0.2380 -0.0706 0.0593  0.0205  427 HOH A O   
2190 O  O   . HOH F .   ? 0.5088 0.5755 0.2303 0.2317  0.0320  0.0507  428 HOH A O   
2191 O  O   . HOH F .   ? 0.4750 0.3815 0.5952 -0.1166 -0.1937 0.1780  429 HOH A O   
2192 O  O   . HOH F .   ? 0.5036 0.8631 0.7339 0.1016  -0.1907 0.1147  430 HOH A O   
2193 O  O   . HOH F .   ? 0.4953 0.7536 0.5674 0.1231  0.0359  -0.1039 431 HOH A O   
2194 O  O   . HOH F .   ? 0.2945 0.2619 0.2382 -0.0119 -0.0532 -0.0392 432 HOH A O   
2195 O  O   . HOH F .   ? 0.4524 0.3617 0.2893 -0.1331 0.1345  -0.1363 433 HOH A O   
2196 O  O   . HOH F .   ? 0.2303 0.1966 0.2104 0.0240  0.0055  0.0120  434 HOH A O   
2197 O  O   . HOH F .   ? 0.4064 0.2217 0.4470 -0.0157 0.0638  -0.0195 435 HOH A O   
2198 O  O   . HOH F .   ? 0.2462 0.1253 0.2924 0.0104  -0.0323 -0.0072 436 HOH A O   
2199 O  O   . HOH F .   ? 0.3424 0.2756 0.5392 -0.0249 0.0914  -0.1164 437 HOH A O   
2200 O  O   . HOH F .   ? 0.6657 0.1971 0.6501 -0.0579 0.2804  -0.0286 438 HOH A O   
2201 O  O   . HOH F .   ? 0.5960 0.6351 0.4096 -0.0693 -0.1452 0.0507  439 HOH A O   
2202 O  O   . HOH F .   ? 0.3716 0.2437 0.1993 -0.0930 -0.0167 0.0043  440 HOH A O   
2203 O  O   . HOH F .   ? 0.4720 0.4218 0.4209 -0.1776 0.1140  -0.1544 441 HOH A O   
2204 O  O   . HOH F .   ? 0.9716 0.4067 0.4321 0.2845  -0.1216 0.0768  442 HOH A O   
2205 O  O   . HOH F .   ? 0.1565 0.1244 0.1529 0.0167  0.0047  -0.0144 443 HOH A O   
2206 O  O   . HOH F .   ? 0.6434 0.1928 0.3940 -0.0461 -0.1731 -0.0303 444 HOH A O   
2207 O  O   . HOH F .   ? 0.7537 0.8418 0.3580 -0.1512 -0.0458 0.2879  445 HOH A O   
2208 O  O   . HOH F .   ? 0.3940 0.5049 0.3820 0.0659  0.1265  -0.0845 446 HOH A O   
2209 O  O   . HOH F .   ? 0.5669 0.5208 0.6318 -0.0617 0.1177  -0.0029 447 HOH A O   
2210 O  O   . HOH F .   ? 0.2452 0.2103 0.2660 -0.0195 -0.1054 -0.0052 448 HOH A O   
2211 O  O   . HOH F .   ? 0.2150 0.1233 0.1842 -0.0109 -0.0027 -0.0151 449 HOH A O   
2212 O  O   . HOH F .   ? 0.5559 0.3446 0.2346 0.2125  -0.0366 -0.0435 450 HOH A O   
2213 O  O   . HOH F .   ? 0.5845 0.4703 0.5023 0.0675  -0.0127 0.1265  451 HOH A O   
2214 O  O   . HOH F .   ? 0.3215 0.2667 0.5540 0.0121  -0.0297 -0.1802 452 HOH A O   
2215 O  O   . HOH F .   ? 0.6939 0.3972 0.4861 0.1289  -0.2420 -0.0053 453 HOH A O   
2216 O  O   . HOH F .   ? 0.2901 0.3968 0.8843 -0.1675 0.1951  -0.0946 454 HOH A O   
2217 O  O   . HOH F .   ? 0.4860 0.2460 0.2675 -0.0882 0.0597  -0.0005 455 HOH A O   
2218 O  O   . HOH F .   ? 0.2703 0.1312 0.3816 -0.0414 -0.0585 0.0167  456 HOH A O   
2219 O  O   . HOH F .   ? 0.3337 0.3680 0.9778 0.1047  -0.0167 -0.0419 457 HOH A O   
2220 O  O   . HOH F .   ? 0.3654 0.5279 0.5575 -0.0769 0.0080  -0.2041 458 HOH A O   
2221 O  O   . HOH F .   ? 0.6324 0.2483 0.3342 -0.0837 0.0042  -0.0218 459 HOH A O   
2222 O  O   . HOH F .   ? 0.2755 0.3984 0.3096 -0.0278 -0.0559 0.0060  460 HOH A O   
2223 O  O   . HOH F .   ? 0.2060 0.1817 0.1985 -0.0083 0.0387  0.0291  461 HOH A O   
2224 O  O   . HOH F .   ? 0.2649 0.4737 0.5554 -0.1202 0.1363  -0.0265 462 HOH A O   
2225 O  O   . HOH F .   ? 0.3247 0.2622 0.2279 -0.0212 0.0043  -0.0362 463 HOH A O   
2226 O  O   . HOH F .   ? 0.2657 0.2549 0.1673 0.0111  0.0016  0.0158  464 HOH A O   
2227 O  O   . HOH F .   ? 0.3001 0.2732 0.3319 0.0390  -0.0806 -0.1525 465 HOH A O   
2228 O  O   . HOH F .   ? 0.3410 0.2846 0.5546 0.0428  -0.1420 -0.1518 466 HOH A O   
2229 O  O   . HOH F .   ? 0.4050 0.2598 0.2158 -0.0785 -0.0555 0.0395  467 HOH A O   
2230 O  O   . HOH F .   ? 0.4711 0.3646 0.4945 0.0797  -0.1578 -0.0297 468 HOH A O   
2231 O  O   . HOH F .   ? 0.4386 0.2117 0.2484 -0.0652 0.0226  0.0568  469 HOH A O   
2232 O  O   . HOH F .   ? 0.2124 0.4833 0.1669 -0.1163 -0.0388 0.0208  470 HOH A O   
2233 O  O   . HOH F .   ? 0.1877 0.1896 0.3488 0.0070  0.0250  -0.0032 471 HOH A O   
2234 O  O   . HOH F .   ? 0.6384 0.4380 0.2379 -0.1068 0.0089  0.0835  472 HOH A O   
2235 O  O   . HOH F .   ? 0.4768 0.9577 0.3299 -0.0039 -0.0553 0.1083  473 HOH A O   
2236 O  O   . HOH F .   ? 0.2254 0.2272 0.2817 -0.0357 0.0120  0.0046  474 HOH A O   
2237 O  O   . HOH F .   ? 0.4698 0.3252 0.9623 -0.3562 -0.0044 -0.1937 475 HOH A O   
2238 O  O   . HOH F .   ? 0.3263 0.3077 0.2895 0.0274  0.0761  -0.1133 476 HOH A O   
2239 O  O   . HOH F .   ? 0.3994 0.6157 0.4140 -0.0515 0.0150  -0.0886 477 HOH A O   
2240 O  O   . HOH F .   ? 0.4613 0.3116 0.3525 -0.0135 0.0827  -0.0275 478 HOH A O   
2241 O  O   . HOH F .   ? 0.2893 0.8021 0.3862 -0.1314 0.0416  0.1005  479 HOH A O   
2242 O  O   . HOH F .   ? 0.4978 0.2185 0.1773 -0.0212 -0.0002 -0.0069 480 HOH A O   
2243 O  O   . HOH F .   ? 0.2266 0.2911 0.2305 0.0107  0.0562  -0.0641 481 HOH A O   
2244 O  O   . HOH F .   ? 0.4366 0.4533 0.5509 0.0613  -0.0160 -0.0079 482 HOH A O   
2245 O  O   . HOH F .   ? 0.3915 0.3745 0.3481 0.2000  -0.1683 -0.1659 483 HOH A O   
2246 O  O   . HOH F .   ? 0.1571 0.1188 0.1809 0.0057  0.0133  -0.0407 484 HOH A O   
2247 O  O   . HOH F .   ? 0.5114 0.5028 0.4364 -0.1978 0.0234  0.0813  485 HOH A O   
2248 O  O   . HOH F .   ? 0.4221 0.2932 0.6160 -0.1756 -0.1571 0.0501  486 HOH A O   
2249 O  O   . HOH F .   ? 0.1650 0.1117 0.1375 0.0205  -0.0183 -0.0118 487 HOH A O   
2250 O  O   . HOH F .   ? 0.1641 0.1820 0.1629 -0.0030 -0.0236 0.0326  488 HOH A O   
2251 O  O   . HOH F .   ? 0.2488 0.2539 0.4584 0.0384  -0.0096 0.0027  489 HOH A O   
2252 O  O   . HOH F .   ? 0.2310 0.3191 0.2769 0.0223  0.0361  0.0221  490 HOH A O   
2253 O  O   . HOH F .   ? 0.3923 0.6368 0.4648 0.1344  0.1715  -0.0436 491 HOH A O   
2254 O  O   . HOH F .   ? 0.1626 0.1615 0.1831 -0.0277 -0.0083 0.0132  492 HOH A O   
2255 O  O   . HOH F .   ? 0.2100 0.1612 0.2789 -0.0408 -0.0507 0.0013  493 HOH A O   
2256 O  O   . HOH F .   ? 0.2222 0.3283 0.2641 0.0516  0.0292  -0.0440 494 HOH A O   
2257 O  O   . HOH F .   ? 0.3623 0.4837 0.5651 -0.0630 0.0996  0.0745  495 HOH A O   
2258 O  O   . HOH F .   ? 0.2315 0.2416 0.3381 -0.0098 -0.0209 -0.0850 496 HOH A O   
2259 O  O   . HOH F .   ? 0.1578 0.2497 0.2438 -0.0178 -0.0137 0.0013  497 HOH A O   
2260 O  O   . HOH F .   ? 0.4579 0.4128 0.4899 0.1127  -0.1060 -0.1203 498 HOH A O   
2261 O  O   . HOH F .   ? 0.7199 0.5165 0.4889 -0.0617 0.2403  -0.1051 499 HOH A O   
2262 O  O   . HOH F .   ? 0.3239 0.2640 0.3516 -0.0679 0.0592  0.0607  500 HOH A O   
2263 O  O   . HOH F .   ? 0.3899 0.2865 0.7984 0.0343  0.1516  -0.0127 501 HOH A O   
2264 O  O   . HOH F .   ? 0.2629 0.7356 0.5865 -0.1393 -0.0421 0.2506  502 HOH A O   
2265 O  O   . HOH F .   ? 0.1423 0.1468 0.1411 0.0339  -0.0052 -0.0058 503 HOH A O   
2266 O  O   . HOH F .   ? 0.3097 0.3690 0.2153 -0.0496 -0.0185 -0.0560 504 HOH A O   
2267 O  O   . HOH F .   ? 0.1655 0.1146 0.1794 0.0136  -0.0263 0.0006  505 HOH A O   
2268 O  O   . HOH F .   ? 0.1844 0.2380 0.2696 0.0582  0.0455  0.0558  506 HOH A O   
2269 O  O   . HOH F .   ? 0.2190 0.2009 0.2007 0.0188  -0.0573 0.0046  507 HOH A O   
2270 O  O   . HOH F .   ? 0.1346 0.1154 0.1262 0.0052  0.0273  -0.0006 508 HOH A O   
2271 O  O   . HOH F .   ? 0.2522 0.1935 0.4815 -0.0212 0.1090  -0.1015 509 HOH A O   
2272 O  O   . HOH F .   ? 0.2466 0.4114 0.2515 0.0464  -0.0088 -0.0908 510 HOH A O   
2273 O  O   . HOH F .   ? 0.1942 0.3820 0.3210 -0.0012 -0.0106 0.1587  511 HOH A O   
2274 O  O   . HOH F .   ? 0.2043 0.1095 0.2140 -0.0321 -0.0336 0.0032  512 HOH A O   
2275 O  O   . HOH F .   ? 0.4672 0.2084 0.2472 -0.0125 0.0328  0.0401  513 HOH A O   
2276 O  O   . HOH F .   ? 0.1500 0.1235 0.1759 0.0002  0.0047  0.0057  514 HOH A O   
2277 O  O   . HOH F .   ? 0.1626 0.2139 0.1980 0.0228  0.0280  0.0464  515 HOH A O   
2278 O  O   . HOH F .   ? 0.2029 0.2081 0.2117 -0.0211 0.0321  -0.0277 516 HOH A O   
2279 O  O   . HOH F .   ? 0.1984 0.1560 0.2165 0.0288  0.0000  0.0088  517 HOH A O   
2280 O  O   . HOH F .   ? 0.1614 0.1452 0.2002 0.0089  -0.0203 0.0157  518 HOH A O   
2281 O  O   . HOH F .   ? 0.2476 0.1766 0.3877 0.0385  0.0008  -0.0178 519 HOH A O   
2282 O  O   . HOH F .   ? 0.4201 0.3356 0.3296 0.0053  -0.0431 0.0844  520 HOH A O   
2283 O  O   . HOH F .   ? 0.1873 0.2952 0.1815 0.0269  -0.0125 0.0055  521 HOH A O   
2284 O  O   . HOH F .   ? 0.2264 0.2968 0.2363 0.0190  -0.0311 0.0003  522 HOH A O   
2285 O  O   . HOH F .   ? 0.6328 0.3301 0.5044 0.0385  0.0495  0.0888  523 HOH A O   
2286 O  O   . HOH F .   ? 0.1996 0.2059 0.2226 0.0410  -0.0231 0.0177  524 HOH A O   
2287 O  O   . HOH F .   ? 0.1309 0.1806 0.1858 0.0158  -0.0067 -0.0419 525 HOH A O   
2288 O  O   . HOH F .   ? 0.6353 0.2283 0.4586 -0.0102 -0.2428 -0.0230 526 HOH A O   
2289 O  O   . HOH F .   ? 1.0753 0.4018 0.6835 0.0069  -0.1434 -0.2713 527 HOH A O   
2290 O  O   . HOH F .   ? 0.2717 0.2372 0.2842 -0.0161 -0.0787 -0.0069 528 HOH A O   
2291 O  O   . HOH F .   ? 0.4039 0.2322 0.7145 0.0599  0.0021  -0.0827 529 HOH A O   
2292 O  O   . HOH F .   ? 0.1790 0.1327 0.1666 0.0244  -0.0201 -0.0034 530 HOH A O   
2293 O  O   . HOH F .   ? 0.2663 0.3414 0.2139 0.0632  -0.0566 0.0089  531 HOH A O   
2294 O  O   . HOH F .   ? 0.2287 0.1799 0.2315 -0.0423 -0.0383 0.0032  532 HOH A O   
2295 O  O   . HOH F .   ? 0.2414 0.4964 0.2682 0.0057  -0.0142 -0.0445 533 HOH A O   
2296 O  O   . HOH F .   ? 0.2363 0.1571 0.2678 -0.0145 0.0390  -0.0318 534 HOH A O   
2297 O  O   . HOH F .   ? 0.2834 0.2335 0.1859 -0.0262 0.0082  -0.0092 535 HOH A O   
2298 O  O   . HOH F .   ? 0.2592 0.7543 0.2447 -0.0471 0.0286  -0.1056 536 HOH A O   
2299 O  O   . HOH F .   ? 0.4563 0.3490 0.2409 -0.0242 -0.0576 -0.0147 537 HOH A O   
2300 O  O   . HOH F .   ? 0.4020 0.9238 0.4230 -0.2002 0.1992  0.0374  538 HOH A O   
2301 O  O   . HOH F .   ? 0.1254 0.2124 0.1716 0.0163  -0.0042 -0.0174 539 HOH A O   
2302 O  O   . HOH F .   ? 0.2430 0.1483 0.2877 0.0103  0.0166  -0.0355 540 HOH A O   
2303 O  O   . HOH F .   ? 0.4041 0.4080 0.3177 -0.1347 0.0855  -0.0029 541 HOH A O   
2304 O  O   . HOH F .   ? 0.2832 0.7079 0.3227 -0.0207 -0.0508 0.1231  542 HOH A O   
2305 O  O   . HOH F .   ? 0.4950 0.6262 0.4470 0.1798  0.0983  0.2356  543 HOH A O   
2306 O  O   . HOH F .   ? 0.2511 0.2809 0.2046 -0.0073 0.0122  0.0682  544 HOH A O   
2307 O  O   . HOH F .   ? 0.1930 0.1557 0.3473 -0.0217 0.0449  0.0670  545 HOH A O   
2308 O  O   . HOH F .   ? 0.2701 0.1960 0.2619 0.0061  -0.0242 0.0265  546 HOH A O   
2309 O  O   . HOH F .   ? 0.4207 0.2396 0.3477 -0.0813 0.0973  -0.0745 547 HOH A O   
2310 O  O   . HOH F .   ? 0.8267 0.3993 0.4082 0.2599  -0.0842 -0.0510 548 HOH A O   
2311 O  O   . HOH F .   ? 0.2282 0.2426 0.2576 0.0163  0.0096  -0.0170 549 HOH A O   
2312 O  O   . HOH F .   ? 0.1905 0.2089 0.2232 0.0447  0.0428  0.0443  550 HOH A O   
2313 O  O   . HOH F .   ? 0.4277 0.4651 0.2793 -0.0033 0.1028  -0.1624 551 HOH A O   
2314 O  O   . HOH F .   ? 0.3591 0.8888 0.6918 0.0458  0.0748  -0.1368 552 HOH A O   
2315 O  O   . HOH F .   ? 0.1759 0.3305 0.2877 0.0331  0.0109  0.0759  553 HOH A O   
2316 O  O   . HOH F .   ? 0.2973 0.2200 0.3009 0.0967  -0.1091 -0.0638 554 HOH A O   
2317 O  O   . HOH F .   ? 0.5184 0.2307 0.3422 0.0300  -0.0401 0.0559  555 HOH A O   
2318 O  O   . HOH F .   ? 0.2966 0.2242 0.2772 0.0357  -0.0754 -0.0862 556 HOH A O   
2319 O  O   . HOH F .   ? 0.4765 0.4145 0.3795 0.1804  -0.1365 -0.0776 557 HOH A O   
2320 O  O   . HOH F .   ? 0.4266 0.4979 0.9213 -0.0968 -0.0734 0.0754  558 HOH A O   
2321 O  O   . HOH F .   ? 0.3093 0.1671 0.2569 0.0036  -0.0458 -0.0532 559 HOH A O   
2322 O  O   . HOH F .   ? 0.3262 0.1978 0.2188 -0.0563 -0.0295 -0.0462 560 HOH A O   
2323 O  O   . HOH F .   ? 0.4623 0.2212 0.2531 0.0498  -0.0111 0.0945  561 HOH A O   
2324 O  O   . HOH F .   ? 0.3388 0.2427 0.3398 0.0898  -0.1237 -0.0242 562 HOH A O   
2325 O  O   . HOH F .   ? 0.4087 0.3221 0.4522 0.1104  -0.1630 -0.0794 563 HOH A O   
2326 O  O   . HOH F .   ? 0.3324 0.2717 0.3895 0.0363  -0.0002 -0.1117 564 HOH A O   
2327 O  O   . HOH F .   ? 0.1905 0.2054 0.2178 -0.0259 0.0307  -0.0064 565 HOH A O   
2328 O  O   . HOH F .   ? 0.4357 0.3521 0.6317 0.1393  0.1042  0.2703  566 HOH A O   
2329 O  O   . HOH F .   ? 0.2046 0.2691 0.2766 0.0529  0.0447  0.0304  567 HOH A O   
2330 O  O   . HOH F .   ? 0.2829 0.1791 0.3654 0.0267  0.0486  -0.0281 568 HOH A O   
2331 O  O   . HOH F .   ? 0.2925 0.3938 0.7916 -0.0402 0.0796  -0.1418 569 HOH A O   
2332 O  O   . HOH F .   ? 0.2568 0.2067 0.2524 0.0048  0.0189  0.0978  570 HOH A O   
2333 O  O   . HOH F .   ? 0.4613 0.6156 0.3787 -0.0221 -0.0323 -0.2242 571 HOH A O   
2334 O  O   . HOH F .   ? 0.1729 0.2640 0.1917 -0.0204 -0.0414 0.0653  572 HOH A O   
2335 O  O   . HOH F .   ? 0.6144 0.3928 0.2327 0.0507  -0.0209 0.0900  573 HOH A O   
2336 O  O   . HOH F .   ? 0.5481 0.5078 0.3445 0.2524  0.1087  0.1088  574 HOH A O   
2337 O  O   . HOH F .   ? 0.2758 0.5730 0.2960 -0.0548 -0.0010 -0.0086 575 HOH A O   
2338 O  O   . HOH F .   ? 0.2523 0.2588 0.5059 0.0562  0.0555  -0.0704 576 HOH A O   
2339 O  O   . HOH F .   ? 0.3657 0.4530 0.6600 -0.1143 -0.0370 0.1751  577 HOH A O   
2340 O  O   . HOH F .   ? 0.3013 0.3245 0.4238 0.0227  0.0119  -0.0862 578 HOH A O   
2341 O  O   . HOH F .   ? 0.5572 0.3139 0.7195 0.0430  -0.2453 0.0091  579 HOH A O   
2342 O  O   . HOH F .   ? 0.7819 0.8262 0.4608 -0.1736 -0.3796 0.0785  580 HOH A O   
2343 O  O   . HOH F .   ? 0.4191 0.3829 0.7729 0.0231  -0.3772 0.1048  581 HOH A O   
2344 O  O   . HOH F .   ? 0.2691 0.4069 0.2619 0.0710  -0.0131 -0.0017 582 HOH A O   
2345 O  O   . HOH F .   ? 0.4444 0.3033 0.5024 -0.0347 0.0309  -0.0594 583 HOH A O   
2346 O  O   . HOH F .   ? 0.3672 0.2577 0.2967 0.0241  -0.0321 0.0614  584 HOH A O   
2347 O  O   . HOH F .   ? 0.4782 0.2975 0.9373 0.0730  0.2867  0.0769  585 HOH A O   
2348 O  O   . HOH F .   ? 0.3762 0.1935 0.3307 0.0598  0.0177  0.0682  586 HOH A O   
2349 O  O   . HOH F .   ? 0.3717 0.6828 0.5086 0.0406  0.0617  0.2118  587 HOH A O   
2350 O  O   . HOH F .   ? 0.2929 0.2224 0.2542 0.0560  -0.0116 0.0586  588 HOH A O   
2351 O  O   . HOH F .   ? 0.4547 0.4093 0.6012 0.1300  -0.0858 -0.0825 589 HOH A O   
2352 O  O   . HOH F .   ? 0.6092 0.3240 0.4743 0.0444  -0.0917 -0.0798 590 HOH A O   
2353 O  O   . HOH F .   ? 0.2371 0.1762 0.3349 0.0557  -0.0577 -0.0515 591 HOH A O   
2354 O  O   . HOH F .   ? 0.3604 0.3187 0.4069 0.0754  0.0934  0.0744  592 HOH A O   
2355 O  O   . HOH F .   ? 0.4627 0.2061 0.2726 0.1112  -0.0068 0.0013  593 HOH A O   
2356 O  O   . HOH F .   ? 0.4038 0.3118 0.3147 -0.0295 0.0999  -0.0036 594 HOH A O   
2357 O  O   . HOH F .   ? 0.3114 0.4730 0.6320 0.0120  0.0111  -0.1147 595 HOH A O   
2358 O  O   . HOH F .   ? 0.6427 0.2286 0.4111 0.0357  -0.0195 -0.0471 596 HOH A O   
2359 O  O   . HOH F .   ? 0.2630 0.4623 0.2244 0.0730  -0.0473 -0.0691 597 HOH A O   
2360 O  O   . HOH F .   ? 0.1776 0.1125 0.1793 0.0042  -0.0127 0.0053  598 HOH A O   
2361 O  O   . HOH F .   ? 0.2132 0.1615 0.2587 -0.0587 0.0021  -0.0603 599 HOH A O   
2362 O  O   . HOH F .   ? 0.9036 0.7244 0.6388 0.1606  0.0444  -0.1546 600 HOH A O   
2363 O  O   . HOH F .   ? 0.4191 0.2013 0.1981 0.0558  -0.0723 -0.0094 601 HOH A O   
2364 O  O   . HOH F .   ? 0.4615 0.2297 0.3495 0.1040  -0.0956 -0.0122 602 HOH A O   
2365 O  O   . HOH F .   ? 0.2561 0.2645 0.4052 -0.0478 0.0130  -0.0139 603 HOH A O   
2366 O  O   . HOH F .   ? 0.4131 0.6217 0.3245 -0.1445 -0.0261 0.0752  604 HOH A O   
2367 O  O   . HOH F .   ? 0.4098 0.4281 0.3313 0.1008  -0.1059 -0.0936 605 HOH A O   
2368 O  O   . HOH F .   ? 0.2922 0.1352 0.5726 0.0051  -0.1487 0.0124  606 HOH A O   
2369 O  O   . HOH F .   ? 0.2821 0.1982 0.3511 -0.0104 -0.0618 0.0174  607 HOH A O   
2370 O  O   . HOH F .   ? 0.1679 0.2523 0.2450 0.0241  0.0039  -0.0252 608 HOH A O   
2371 O  O   . HOH F .   ? 0.4804 0.4174 0.2955 -0.1976 0.0081  0.0126  609 HOH A O   
2372 O  O   . HOH F .   ? 0.3252 0.5212 0.6386 0.0414  0.0505  0.0465  610 HOH A O   
2373 O  O   . HOH F .   ? 0.6646 0.6305 0.6554 0.1539  0.3547  -0.0587 611 HOH A O   
2374 O  O   . HOH F .   ? 0.4017 0.5192 0.5036 0.0099  -0.0097 0.1042  612 HOH A O   
2375 O  O   . HOH F .   ? 0.4107 0.3828 0.3971 -0.1081 0.0080  0.0245  613 HOH A O   
2376 O  O   . HOH F .   ? 0.5005 0.1969 0.4264 0.0929  -0.1481 -0.0533 614 HOH A O   
2377 O  O   . HOH F .   ? 0.5400 0.4734 0.5090 -0.1793 -0.1465 0.1812  615 HOH A O   
2378 O  O   . HOH F .   ? 0.3529 0.2072 0.3136 0.0245  0.0621  0.0264  616 HOH A O   
2379 O  O   . HOH F .   ? 0.2178 0.2717 0.1884 -0.0168 0.0412  0.0726  617 HOH A O   
2380 O  O   . HOH F .   ? 0.3388 0.2238 0.4111 0.0190  0.0622  0.0282  618 HOH A O   
2381 O  O   . HOH F .   ? 0.4051 0.4550 0.3882 0.1788  -0.0696 -0.0515 619 HOH A O   
2382 O  O   . HOH F .   ? 0.4209 0.6648 0.5675 0.0565  -0.0326 -0.2288 620 HOH A O   
2383 O  O   . HOH F .   ? 0.3271 0.1313 0.3782 0.0311  -0.0384 -0.0383 621 HOH A O   
2384 O  O   . HOH F .   ? 0.2723 0.3046 0.4009 0.1112  -0.0548 -0.1089 622 HOH A O   
2385 O  O   . HOH F .   ? 0.5177 0.2154 0.4124 0.0059  0.0678  0.0642  623 HOH A O   
2386 O  O   . HOH F .   ? 0.1676 0.1714 0.2693 -0.0111 0.0207  -0.0051 624 HOH A O   
2387 O  O   . HOH F .   ? 0.2827 0.2053 0.4128 -0.0197 -0.0537 0.0201  625 HOH A O   
2388 O  O   . HOH F .   ? 0.2474 0.2344 0.4095 0.0839  -0.0460 -0.0189 626 HOH A O   
2389 O  O   . HOH F .   ? 0.9847 0.4251 0.5529 -0.1638 0.3783  -0.1096 627 HOH A O   
2390 O  O   . HOH F .   ? 0.3128 0.5841 0.6048 0.1497  0.0000  -0.0826 628 HOH A O   
2391 O  O   . HOH F .   ? 0.2240 0.5026 0.2938 0.0680  -0.0377 0.0292  629 HOH A O   
2392 O  O   . HOH F .   ? 0.4911 0.1981 0.3734 -0.0058 -0.0377 0.0621  630 HOH A O   
2393 O  O   . HOH F .   ? 0.4502 0.3423 0.4365 0.0773  0.1305  0.0883  631 HOH A O   
2394 O  O   . HOH F .   ? 0.7440 0.6991 0.5281 -0.2073 -0.2834 0.1312  632 HOH A O   
2395 O  O   . HOH F .   ? 0.4400 0.1878 0.3952 0.0167  -0.0354 -0.0549 633 HOH A O   
2396 O  O   . HOH F .   ? 0.7286 0.6309 0.3556 0.0100  0.0902  0.0653  634 HOH A O   
2397 O  O   . HOH F .   ? 0.2352 0.3438 0.2264 0.0013  -0.0244 -0.0118 635 HOH A O   
2398 O  O   . HOH F .   ? 0.4878 0.6065 0.2693 -0.2822 0.0271  0.0252  636 HOH A O   
2399 O  O   . HOH F .   ? 0.4078 0.4029 0.7086 -0.0960 -0.0712 -0.1033 637 HOH A O   
2400 O  O   . HOH F .   ? 0.3767 0.2893 0.4177 0.0564  -0.0523 0.0516  638 HOH A O   
2401 O  O   . HOH F .   ? 0.5809 0.7208 0.5852 0.0677  0.2004  0.2791  639 HOH A O   
2402 O  O   . HOH F .   ? 0.3730 0.2962 0.8629 -0.2603 0.1125  0.0331  640 HOH A O   
2403 O  O   . HOH F .   ? 0.3450 0.4988 0.2579 -0.0831 -0.0420 0.0756  641 HOH A O   
2404 O  O   . HOH F .   ? 0.9188 0.5916 0.6276 0.0267  -0.1170 -0.2340 642 HOH A O   
2405 O  O   . HOH F .   ? 0.2990 0.4258 0.3955 0.0992  0.0581  0.0939  643 HOH A O   
2406 O  O   . HOH F .   ? 0.2511 0.1636 0.2206 -0.0344 -0.0525 0.0214  644 HOH A O   
2407 O  O   . HOH F .   ? 0.3723 0.1657 0.3928 0.0021  -0.0980 0.0510  645 HOH A O   
2408 O  O   . HOH F .   ? 0.3102 0.4307 0.3553 -0.1038 -0.0145 0.0688  646 HOH A O   
2409 O  O   . HOH F .   ? 0.6468 0.3435 0.6972 0.0400  0.2063  -0.1307 647 HOH A O   
2410 O  O   . HOH F .   ? 0.4145 0.2174 0.4138 0.0588  -0.2533 -0.0419 648 HOH A O   
2411 O  O   . HOH F .   ? 0.3265 0.2685 0.2740 0.0405  0.1044  0.0355  649 HOH A O   
2412 O  O   . HOH F .   ? 0.3876 0.3942 0.4784 0.1364  0.0591  0.0731  650 HOH A O   
2413 O  O   . HOH F .   ? 0.4603 0.3319 0.3087 -0.0911 -0.0089 0.1074  651 HOH A O   
2414 O  O   . HOH F .   ? 0.7792 0.6205 0.5456 -0.0279 0.0185  -0.0388 652 HOH A O   
2415 O  O   . HOH F .   ? 0.2890 0.4374 0.5974 0.0629  -0.0067 0.0776  653 HOH A O   
2416 O  O   . HOH F .   ? 0.4164 0.3190 0.3559 -0.0164 0.0520  -0.0635 654 HOH A O   
2417 O  O   . HOH F .   ? 0.4478 0.4822 0.2540 -0.1669 -0.0447 0.0434  655 HOH A O   
2418 O  O   . HOH F .   ? 0.3353 0.2937 0.3010 0.0476  0.0218  0.1000  656 HOH A O   
2419 O  O   . HOH F .   ? 0.3203 0.3036 0.3274 -0.0168 -0.0332 0.0523  657 HOH A O   
2420 O  O   . HOH F .   ? 0.3109 0.3837 0.4379 -0.0307 -0.0666 0.0890  658 HOH A O   
2421 O  O   . HOH F .   ? 0.3871 0.3620 0.3715 -0.0192 0.1367  0.0743  659 HOH A O   
2422 O  O   . HOH F .   ? 0.5630 0.2979 0.2868 -0.0411 -0.0756 0.0718  660 HOH A O   
2423 O  O   . HOH F .   ? 0.3303 0.3026 1.1344 0.1866  -0.2169 0.0826  661 HOH A O   
2424 O  O   . HOH F .   ? 0.4691 0.8510 0.3405 0.1571  -0.0475 -0.0325 662 HOH A O   
2425 O  O   . HOH F .   ? 0.2616 0.4578 0.6836 0.0508  0.0502  0.0491  663 HOH A O   
2426 O  O   . HOH F .   ? 0.2952 0.2657 0.3215 -0.0842 0.0582  -0.0732 664 HOH A O   
2427 O  O   . HOH F .   ? 0.3235 0.2850 0.6397 0.0086  0.0037  0.0714  665 HOH A O   
2428 O  O   . HOH F .   ? 0.3772 0.5572 0.3228 0.0230  0.0000  -0.1246 666 HOH A O   
2429 O  O   . HOH F .   ? 0.3374 0.5227 0.5321 -0.0392 0.1023  0.1446  667 HOH A O   
2430 O  O   . HOH F .   ? 0.3096 0.6954 0.5273 0.0943  0.0386  0.1766  668 HOH A O   
2431 O  O   . HOH F .   ? 0.4205 0.3215 0.4150 0.0864  -0.1181 -0.1071 669 HOH A O   
2432 O  O   . HOH F .   ? 0.9714 0.3300 0.3882 0.1592  -0.0055 -0.0634 670 HOH A O   
2433 O  O   . HOH F .   ? 0.3493 0.6409 0.4202 0.0609  0.0081  0.1060  671 HOH A O   
2434 O  O   . HOH F .   ? 0.2867 0.5485 0.6931 -0.1041 -0.0762 0.0461  672 HOH A O   
2435 O  O   . HOH F .   ? 0.4034 0.6321 0.8887 0.0228  -0.1145 0.0142  673 HOH A O   
2436 O  O   . HOH F .   ? 0.5547 0.3183 0.2438 0.0582  -0.0704 0.0627  674 HOH A O   
2437 O  O   . HOH F .   ? 0.2768 0.4524 0.5367 0.0927  -0.0537 0.1703  675 HOH A O   
2438 O  O   . HOH F .   ? 0.3887 0.3792 0.5204 0.1356  -0.1104 -0.0421 676 HOH A O   
2439 O  O   . HOH F .   ? 0.3727 0.2825 0.4637 -0.0294 -0.0723 -0.0597 677 HOH A O   
2440 O  O   . HOH F .   ? 0.4886 0.4342 0.6097 -0.1040 -0.1368 -0.0810 678 HOH A O   
2441 O  O   . HOH F .   ? 0.6585 0.6804 0.8130 0.2244  -0.2180 -0.1196 679 HOH A O   
2442 O  O   . HOH F .   ? 0.2774 0.4398 0.4339 -0.0464 0.0390  0.0034  680 HOH A O   
2443 O  O   . HOH F .   ? 0.6275 0.5449 0.4306 -0.0788 0.0469  -0.0027 681 HOH A O   
2444 O  O   . HOH F .   ? 0.2538 0.4689 0.2657 0.0659  -0.0053 -0.0086 682 HOH A O   
2445 O  O   . HOH F .   ? 0.3341 0.2655 0.2953 -0.0815 0.0096  -0.0567 683 HOH A O   
2446 O  O   . HOH F .   ? 0.3259 0.3302 0.8062 -0.0472 0.0425  0.0649  684 HOH A O   
2447 O  O   . HOH F .   ? 0.5625 0.5420 0.3551 0.1207  0.1168  0.0000  685 HOH A O   
2448 O  O   . HOH F .   ? 0.5183 0.6695 0.6560 0.4786  -0.1664 0.2029  686 HOH A O   
2449 O  O   . HOH F .   ? 0.5410 0.4449 0.5987 0.0333  -0.1889 -0.1476 687 HOH A O   
2450 O  O   . HOH F .   ? 0.3371 0.4348 0.6117 0.0912  0.1365  0.2044  688 HOH A O   
2451 O  O   . HOH F .   ? 0.2286 0.2672 0.3580 0.0232  0.0336  0.0644  689 HOH A O   
2452 O  O   . HOH F .   ? 0.3855 0.4383 0.3567 -0.0167 0.0713  0.1932  690 HOH A O   
2453 O  O   . HOH F .   ? 0.2808 0.3233 0.3807 0.0483  0.0013  0.1036  691 HOH A O   
2454 O  O   . HOH F .   ? 0.4371 0.3297 0.3926 0.0182  0.0423  0.0387  692 HOH A O   
2455 O  O   . HOH F .   ? 0.4117 0.3388 0.7231 0.0376  0.1298  0.0299  693 HOH A O   
2456 O  O   . HOH F .   ? 0.4043 0.3648 0.3992 0.0183  0.0528  0.0153  694 HOH A O   
2457 O  O   . HOH F .   ? 0.6797 0.3022 0.3009 0.0032  -0.0403 -0.0498 695 HOH A O   
2458 O  O   . HOH F .   ? 0.7693 0.4227 0.5176 0.0075  0.1474  -0.0409 696 HOH A O   
2459 O  O   . HOH F .   ? 0.2758 0.3001 0.3464 0.0285  0.0505  0.0375  697 HOH A O   
2460 O  O   . HOH F .   ? 0.5666 0.3814 0.7014 0.1154  -0.0174 -0.0597 698 HOH A O   
2461 O  O   . HOH F .   ? 0.3733 0.3296 0.3347 0.0201  -0.0576 0.0681  699 HOH A O   
2462 O  O   . HOH F .   ? 0.6075 0.3389 0.4904 -0.0547 0.0313  0.0708  700 HOH A O   
2463 O  O   . HOH F .   ? 0.4070 0.2339 0.2325 0.0917  0.0237  -0.0100 701 HOH A O   
2464 O  O   . HOH F .   ? 0.3153 0.3695 0.3643 0.0257  -0.0022 -0.0324 702 HOH A O   
2465 O  O   . HOH F .   ? 0.7296 0.5384 0.7758 -0.2537 0.0134  -0.3259 703 HOH A O   
2466 O  O   . HOH F .   ? 0.7965 0.5179 0.2394 -0.0298 0.1268  -0.0771 704 HOH A O   
2467 O  O   . HOH F .   ? 0.3088 0.3920 0.4293 0.0076  0.0254  0.0585  705 HOH A O   
2468 O  O   . HOH F .   ? 0.2824 0.1827 0.3206 0.0366  -0.0820 0.0016  706 HOH A O   
2469 O  O   . HOH F .   ? 0.3796 0.3512 0.3939 -0.0203 0.0869  0.0480  707 HOH A O   
2470 O  O   . HOH F .   ? 0.5502 0.2448 0.7849 -0.0431 -0.0329 0.1219  708 HOH A O   
2471 O  O   . HOH F .   ? 0.1953 0.2381 0.2032 -0.0685 0.0111  0.0013  709 HOH A O   
2472 O  O   . HOH F .   ? 0.4458 0.6942 0.4095 -0.1820 0.0038  -0.0366 710 HOH A O   
2473 O  O   . HOH F .   ? 0.7318 0.3608 0.5092 -0.1899 -0.1189 0.2508  711 HOH A O   
2474 O  O   . HOH F .   ? 0.3739 0.4657 0.8261 0.0438  -0.1576 -0.0974 712 HOH A O   
2475 O  O   . HOH F .   ? 0.2802 0.3271 0.2708 -0.0358 0.0073  -0.0414 713 HOH A O   
2476 O  O   . HOH F .   ? 0.3500 0.7748 0.3861 -0.0714 -0.0436 0.2379  714 HOH A O   
2477 O  O   . HOH F .   ? 0.5104 0.2487 0.6384 0.0227  0.0093  0.0614  715 HOH A O   
2478 O  O   . HOH F .   ? 0.3369 0.2848 0.3970 0.0030  -0.0133 -0.1119 716 HOH A O   
2479 O  O   . HOH F .   ? 0.5657 0.3808 0.3716 -0.0563 -0.0534 -0.0085 717 HOH A O   
2480 O  O   . HOH F .   ? 0.4209 0.6037 0.6875 0.0418  0.1233  -0.4019 718 HOH A O   
2481 O  O   . HOH F .   ? 0.5362 0.3153 0.4844 0.0569  -0.0021 -0.0417 719 HOH A O   
2482 O  O   . HOH F .   ? 0.2262 0.5215 0.7379 -0.1305 -0.1047 0.0632  720 HOH A O   
2483 O  O   . HOH F .   ? 0.6808 0.3996 0.4362 -0.0366 -0.2132 0.1053  721 HOH A O   
2484 O  O   . HOH F .   ? 0.3461 0.2266 0.5141 -0.0006 -0.1439 0.0198  722 HOH A O   
2485 O  O   . HOH F .   ? 0.3199 0.3549 0.3593 0.0501  0.0147  -0.1127 723 HOH A O   
2486 O  O   . HOH F .   ? 0.5792 0.5028 0.8268 0.1174  -0.1382 -0.0124 724 HOH A O   
2487 O  O   . HOH F .   ? 0.2078 0.2720 0.2409 0.0185  -0.0322 0.0063  725 HOH A O   
2488 O  O   . HOH F .   ? 0.3669 0.1307 0.5507 0.0044  0.1209  -0.0015 726 HOH A O   
2489 O  O   . HOH F .   ? 0.7127 0.3205 0.4222 -0.0269 -0.0203 -0.1064 727 HOH A O   
2490 O  O   . HOH F .   ? 0.3418 0.4831 0.5008 -0.0797 -0.0420 -0.1132 728 HOH A O   
2491 O  O   . HOH F .   ? 0.3091 0.4684 0.3333 0.0142  0.0422  0.0326  729 HOH A O   
2492 O  O   . HOH F .   ? 0.5171 0.8385 0.8983 -0.2009 0.1707  -0.2110 730 HOH A O   
2493 O  O   . HOH F .   ? 0.6147 0.2157 0.3301 -0.0095 -0.0267 0.0008  731 HOH A O   
2494 O  O   . HOH F .   ? 0.4826 0.5881 0.4061 -0.1016 -0.1490 0.1763  732 HOH A O   
2495 O  O   . HOH F .   ? 0.5338 0.5746 0.7047 0.0658  0.0806  -0.1745 733 HOH A O   
2496 O  O   . HOH F .   ? 0.2235 0.3802 0.3707 -0.0721 -0.0732 0.0421  734 HOH A O   
# 
