data_6YH6
# 
_entry.id   6YH6 
# 
_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   6YH6         pdb_00006yh6 10.2210/pdb6yh6/pdb 
WWPDB D_1292106473 ?            ?                   
# 
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                        6YH6 
_pdbx_database_status.recvd_initial_deposition_date   2020-03-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistryopen 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2191-1363 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                567 
_citation.page_last                 580 
_citation.title                     'Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/open.202100042 
_citation.pdbx_database_id_PubMed   33945229 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnoviene, J.'   1  0000-0001-5503-4775 
primary 'Smirnov, A.'       2  ?                   
primary 'Zaksauskas, A.'    3  ?                   
primary 'Zubriene, A.'      4  0000-0001-5996-1883 
primary 'Petrauskas, V.'    5  0000-0001-7983-4128 
primary 'Mickeviciute, A.'  6  ?                   
primary 'Michailoviene, V.' 7  ?                   
primary 'Capkauskaite, E.'  8  ?                   
primary 'Manakova, E.'      9  0000-0002-6027-2265 
primary 'Grazulis, S.'      10 0000-0002-7928-5218 
primary 'Baranauskiene, L.' 11 0000-0002-9924-9177 
primary 'Chen, W.Y.'        12 ?                   
primary 'Ladbury, J.E.'     13 0000-0002-6328-7200 
primary 'Matulis, D.'       14 0000-0002-6178-6276 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                  29220.879 1   4.2.1.1 
'A65S, N67K, I91T, F130A, V134S, L203N' ? ? 
2 non-polymer syn 'ZINC ION'                                              65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                    78.133    1   ?       ? ? ? 
4 non-polymer syn '2-(Cyclooctylamino)-3,5,6-trifluorobenzenesulfonamide' 336.373   1   ?       ? ? ? 
5 water       nat water                                                   18.015    207 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                              ZN  
3 'DIMETHYL SULFOXIDE'                                    DMS 
4 '2-(Cyclooctylamino)-3,5,6-trifluorobenzenesulfonamide' OQW 
5 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 
CYS 'L-peptide linking' y CYSTEINE                                                ? 'C3 H7 N O2 S'       121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                    ? 'C2 H6 O S'          78.133  
GLN 'L-peptide linking' y GLUTAMINE                                               ? 'C5 H10 N2 O3'       146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                         ? 'C5 H9 N O4'         147.129 
GLY 'peptide linking'   y GLYCINE                                                 ? 'C2 H5 N O2'         75.067  
HIS 'L-peptide linking' y HISTIDINE                                               ? 'C6 H10 N3 O2 1'     156.162 
HOH non-polymer         . WATER                                                   ? 'H2 O'               18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                              ? 'C6 H13 N O2'        131.173 
LEU 'L-peptide linking' y LEUCINE                                                 ? 'C6 H13 N O2'        131.173 
LYS 'L-peptide linking' y LYSINE                                                  ? 'C6 H15 N2 O2 1'     147.195 
MET 'L-peptide linking' y METHIONINE                                              ? 'C5 H11 N O2 S'      149.211 
OQW non-polymer         . '2-(Cyclooctylamino)-3,5,6-trifluorobenzenesulfonamide' 
'2-(cyclooctylamino)-3,5,6-tris(fluoranyl)benzenesulfonamide' 'C14 H19 F3 N2 O2 S' 336.373 
PHE 'L-peptide linking' y PHENYLALANINE                                           ? 'C9 H11 N O2'        165.189 
PRO 'L-peptide linking' y PROLINE                                                 ? 'C5 H9 N O2'         115.130 
SER 'L-peptide linking' y SERINE                                                  ? 'C3 H7 N O3'         105.093 
THR 'L-peptide linking' y THREONINE                                               ? 'C4 H9 N O3'         119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                              ? 'C11 H12 N2 O2'      204.225 
TYR 'L-peptide linking' y TYROSINE                                                ? 'C9 H11 N O3'        181.189 
VAL 'L-peptide linking' y VALINE                                                  ? 'C5 H11 N O2'        117.146 
ZN  non-polymer         . 'ZINC ION'                                              ? 'Zn 2'               65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 ALA 130 131 131 ALA ALA A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 SER 134 135 135 SER SER A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 ASN 203 204 204 ASN ASN A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 OQW 1   303 1   OQW V11 A . 
E 5 HOH 1   401 145 HOH HOH A . 
E 5 HOH 2   402 5   HOH HOH A . 
E 5 HOH 3   403 187 HOH HOH A . 
E 5 HOH 4   404 41  HOH HOH A . 
E 5 HOH 5   405 94  HOH HOH A . 
E 5 HOH 6   406 203 HOH HOH A . 
E 5 HOH 7   407 125 HOH HOH A . 
E 5 HOH 8   408 148 HOH HOH A . 
E 5 HOH 9   409 90  HOH HOH A . 
E 5 HOH 10  410 193 HOH HOH A . 
E 5 HOH 11  411 12  HOH HOH A . 
E 5 HOH 12  412 168 HOH HOH A . 
E 5 HOH 13  413 115 HOH HOH A . 
E 5 HOH 14  414 201 HOH HOH A . 
E 5 HOH 15  415 149 HOH HOH A . 
E 5 HOH 16  416 59  HOH HOH A . 
E 5 HOH 17  417 46  HOH HOH A . 
E 5 HOH 18  418 159 HOH HOH A . 
E 5 HOH 19  419 176 HOH HOH A . 
E 5 HOH 20  420 91  HOH HOH A . 
E 5 HOH 21  421 6   HOH HOH A . 
E 5 HOH 22  422 30  HOH HOH A . 
E 5 HOH 23  423 183 HOH HOH A . 
E 5 HOH 24  424 157 HOH HOH A . 
E 5 HOH 25  425 107 HOH HOH A . 
E 5 HOH 26  426 126 HOH HOH A . 
E 5 HOH 27  427 109 HOH HOH A . 
E 5 HOH 28  428 42  HOH HOH A . 
E 5 HOH 29  429 39  HOH HOH A . 
E 5 HOH 30  430 140 HOH HOH A . 
E 5 HOH 31  431 114 HOH HOH A . 
E 5 HOH 32  432 68  HOH HOH A . 
E 5 HOH 33  433 74  HOH HOH A . 
E 5 HOH 34  434 18  HOH HOH A . 
E 5 HOH 35  435 13  HOH HOH A . 
E 5 HOH 36  436 173 HOH HOH A . 
E 5 HOH 37  437 67  HOH HOH A . 
E 5 HOH 38  438 28  HOH HOH A . 
E 5 HOH 39  439 62  HOH HOH A . 
E 5 HOH 40  440 123 HOH HOH A . 
E 5 HOH 41  441 162 HOH HOH A . 
E 5 HOH 42  442 31  HOH HOH A . 
E 5 HOH 43  443 112 HOH HOH A . 
E 5 HOH 44  444 184 HOH HOH A . 
E 5 HOH 45  445 137 HOH HOH A . 
E 5 HOH 46  446 52  HOH HOH A . 
E 5 HOH 47  447 111 HOH HOH A . 
E 5 HOH 48  448 167 HOH HOH A . 
E 5 HOH 49  449 11  HOH HOH A . 
E 5 HOH 50  450 106 HOH HOH A . 
E 5 HOH 51  451 10  HOH HOH A . 
E 5 HOH 52  452 61  HOH HOH A . 
E 5 HOH 53  453 45  HOH HOH A . 
E 5 HOH 54  454 24  HOH HOH A . 
E 5 HOH 55  455 22  HOH HOH A . 
E 5 HOH 56  456 48  HOH HOH A . 
E 5 HOH 57  457 130 HOH HOH A . 
E 5 HOH 58  458 160 HOH HOH A . 
E 5 HOH 59  459 104 HOH HOH A . 
E 5 HOH 60  460 32  HOH HOH A . 
E 5 HOH 61  461 92  HOH HOH A . 
E 5 HOH 62  462 205 HOH HOH A . 
E 5 HOH 63  463 7   HOH HOH A . 
E 5 HOH 64  464 56  HOH HOH A . 
E 5 HOH 65  465 108 HOH HOH A . 
E 5 HOH 66  466 120 HOH HOH A . 
E 5 HOH 67  467 37  HOH HOH A . 
E 5 HOH 68  468 35  HOH HOH A . 
E 5 HOH 69  469 54  HOH HOH A . 
E 5 HOH 70  470 102 HOH HOH A . 
E 5 HOH 71  471 121 HOH HOH A . 
E 5 HOH 72  472 19  HOH HOH A . 
E 5 HOH 73  473 40  HOH HOH A . 
E 5 HOH 74  474 47  HOH HOH A . 
E 5 HOH 75  475 53  HOH HOH A . 
E 5 HOH 76  476 1   HOH HOH A . 
E 5 HOH 77  477 72  HOH HOH A . 
E 5 HOH 78  478 79  HOH HOH A . 
E 5 HOH 79  479 3   HOH HOH A . 
E 5 HOH 80  480 128 HOH HOH A . 
E 5 HOH 81  481 20  HOH HOH A . 
E 5 HOH 82  482 96  HOH HOH A . 
E 5 HOH 83  483 17  HOH HOH A . 
E 5 HOH 84  484 16  HOH HOH A . 
E 5 HOH 85  485 23  HOH HOH A . 
E 5 HOH 86  486 78  HOH HOH A . 
E 5 HOH 87  487 182 HOH HOH A . 
E 5 HOH 88  488 84  HOH HOH A . 
E 5 HOH 89  489 113 HOH HOH A . 
E 5 HOH 90  490 146 HOH HOH A . 
E 5 HOH 91  491 4   HOH HOH A . 
E 5 HOH 92  492 127 HOH HOH A . 
E 5 HOH 93  493 2   HOH HOH A . 
E 5 HOH 94  494 8   HOH HOH A . 
E 5 HOH 95  495 34  HOH HOH A . 
E 5 HOH 96  496 36  HOH HOH A . 
E 5 HOH 97  497 55  HOH HOH A . 
E 5 HOH 98  498 124 HOH HOH A . 
E 5 HOH 99  499 131 HOH HOH A . 
E 5 HOH 100 500 73  HOH HOH A . 
E 5 HOH 101 501 164 HOH HOH A . 
E 5 HOH 102 502 88  HOH HOH A . 
E 5 HOH 103 503 117 HOH HOH A . 
E 5 HOH 104 504 71  HOH HOH A . 
E 5 HOH 105 505 163 HOH HOH A . 
E 5 HOH 106 506 129 HOH HOH A . 
E 5 HOH 107 507 81  HOH HOH A . 
E 5 HOH 108 508 105 HOH HOH A . 
E 5 HOH 109 509 181 HOH HOH A . 
E 5 HOH 110 510 133 HOH HOH A . 
E 5 HOH 111 511 206 HOH HOH A . 
E 5 HOH 112 512 136 HOH HOH A . 
E 5 HOH 113 513 155 HOH HOH A . 
E 5 HOH 114 514 141 HOH HOH A . 
E 5 HOH 115 515 95  HOH HOH A . 
E 5 HOH 116 516 97  HOH HOH A . 
E 5 HOH 117 517 33  HOH HOH A . 
E 5 HOH 118 518 192 HOH HOH A . 
E 5 HOH 119 519 93  HOH HOH A . 
E 5 HOH 120 520 134 HOH HOH A . 
E 5 HOH 121 521 15  HOH HOH A . 
E 5 HOH 122 522 26  HOH HOH A . 
E 5 HOH 123 523 66  HOH HOH A . 
E 5 HOH 124 524 64  HOH HOH A . 
E 5 HOH 125 525 51  HOH HOH A . 
E 5 HOH 126 526 151 HOH HOH A . 
E 5 HOH 127 527 87  HOH HOH A . 
E 5 HOH 128 528 110 HOH HOH A . 
E 5 HOH 129 529 172 HOH HOH A . 
E 5 HOH 130 530 75  HOH HOH A . 
E 5 HOH 131 531 80  HOH HOH A . 
E 5 HOH 132 532 132 HOH HOH A . 
E 5 HOH 133 533 63  HOH HOH A . 
E 5 HOH 134 534 135 HOH HOH A . 
E 5 HOH 135 535 58  HOH HOH A . 
E 5 HOH 136 536 85  HOH HOH A . 
E 5 HOH 137 537 200 HOH HOH A . 
E 5 HOH 138 538 150 HOH HOH A . 
E 5 HOH 139 539 21  HOH HOH A . 
E 5 HOH 140 540 69  HOH HOH A . 
E 5 HOH 141 541 169 HOH HOH A . 
E 5 HOH 142 542 101 HOH HOH A . 
E 5 HOH 143 543 100 HOH HOH A . 
E 5 HOH 144 544 118 HOH HOH A . 
E 5 HOH 145 545 198 HOH HOH A . 
E 5 HOH 146 546 57  HOH HOH A . 
E 5 HOH 147 547 98  HOH HOH A . 
E 5 HOH 148 548 122 HOH HOH A . 
E 5 HOH 149 549 43  HOH HOH A . 
E 5 HOH 150 550 49  HOH HOH A . 
E 5 HOH 151 551 14  HOH HOH A . 
E 5 HOH 152 552 199 HOH HOH A . 
E 5 HOH 153 553 152 HOH HOH A . 
E 5 HOH 154 554 76  HOH HOH A . 
E 5 HOH 155 555 65  HOH HOH A . 
E 5 HOH 156 556 29  HOH HOH A . 
E 5 HOH 157 557 185 HOH HOH A . 
E 5 HOH 158 558 50  HOH HOH A . 
E 5 HOH 159 559 207 HOH HOH A . 
E 5 HOH 160 560 119 HOH HOH A . 
E 5 HOH 161 561 70  HOH HOH A . 
E 5 HOH 162 562 44  HOH HOH A . 
E 5 HOH 163 563 138 HOH HOH A . 
E 5 HOH 164 564 103 HOH HOH A . 
E 5 HOH 165 565 86  HOH HOH A . 
E 5 HOH 166 566 25  HOH HOH A . 
E 5 HOH 167 567 99  HOH HOH A . 
E 5 HOH 168 568 89  HOH HOH A . 
E 5 HOH 169 569 143 HOH HOH A . 
E 5 HOH 170 570 116 HOH HOH A . 
E 5 HOH 171 571 38  HOH HOH A . 
E 5 HOH 172 572 77  HOH HOH A . 
E 5 HOH 173 573 27  HOH HOH A . 
E 5 HOH 174 574 142 HOH HOH A . 
E 5 HOH 175 575 156 HOH HOH A . 
E 5 HOH 176 576 166 HOH HOH A . 
E 5 HOH 177 577 202 HOH HOH A . 
E 5 HOH 178 578 9   HOH HOH A . 
E 5 HOH 179 579 189 HOH HOH A . 
E 5 HOH 180 580 158 HOH HOH A . 
E 5 HOH 181 581 153 HOH HOH A . 
E 5 HOH 182 582 190 HOH HOH A . 
E 5 HOH 183 583 144 HOH HOH A . 
E 5 HOH 184 584 179 HOH HOH A . 
E 5 HOH 185 585 188 HOH HOH A . 
E 5 HOH 186 586 186 HOH HOH A . 
E 5 HOH 187 587 165 HOH HOH A . 
E 5 HOH 188 588 178 HOH HOH A . 
E 5 HOH 189 589 177 HOH HOH A . 
E 5 HOH 190 590 191 HOH HOH A . 
E 5 HOH 191 591 171 HOH HOH A . 
E 5 HOH 192 592 194 HOH HOH A . 
E 5 HOH 193 593 83  HOH HOH A . 
E 5 HOH 194 594 161 HOH HOH A . 
E 5 HOH 195 595 82  HOH HOH A . 
E 5 HOH 196 596 196 HOH HOH A . 
E 5 HOH 197 597 180 HOH HOH A . 
E 5 HOH 198 598 174 HOH HOH A . 
E 5 HOH 199 599 175 HOH HOH A . 
E 5 HOH 200 600 204 HOH HOH A . 
E 5 HOH 201 601 60  HOH HOH A . 
E 5 HOH 202 602 154 HOH HOH A . 
E 5 HOH 203 603 170 HOH HOH A . 
E 5 HOH 204 604 139 HOH HOH A . 
E 5 HOH 205 605 147 HOH HOH A . 
E 5 HOH 206 606 195 HOH HOH A . 
E 5 HOH 207 607 197 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
2  1 Y 1 A LYS 39  ? CD  ? A LYS 39  CD  
3  1 Y 1 A LYS 39  ? CE  ? A LYS 39  CE  
4  1 Y 1 A LYS 39  ? NZ  ? A LYS 39  NZ  
5  1 Y 1 A LYS 45  ? CD  ? A LYS 45  CD  
6  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
7  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
8  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
9  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
10 1 Y 1 A LYS 111 ? CE  ? A LYS 111 CE  
11 1 Y 1 A LYS 111 ? NZ  ? A LYS 111 NZ  
12 1 Y 1 A LEU 224 ? CD1 ? A LEU 223 CD1 
13 1 Y 1 A LEU 224 ? CD2 ? A LEU 223 CD2 
14 1 Y 1 A LYS 228 ? CE  ? A LYS 227 CE  
15 1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
16 1 Y 1 A GLU 234 ? CD  ? A GLU 233 CD  
17 1 Y 1 A GLU 234 ? OE1 ? A GLU 233 OE1 
18 1 Y 1 A GLU 234 ? OE2 ? A GLU 233 OE2 
19 1 Y 1 A ASN 253 ? CG  ? A ASN 252 CG  
20 1 Y 1 A ASN 253 ? OD1 ? A ASN 252 OD1 
21 1 Y 1 A ASN 253 ? ND2 ? A ASN 252 ND2 
22 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
23 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
24 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
25 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
26 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
27 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                   104.370 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YH6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.773 
_cell.length_a_esd                 ? 
_cell.length_b                     40.746 
_cell.length_b_esd                 ? 
_cell.length_c                     69.423 
_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                         6YH6 
_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                   6YH6 
_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            1.96 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         37.20 
_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 a
nd 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-23 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976300 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976300 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6YH6 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.400 
_reflns.d_resolution_low                 40.746 
_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                       44452 
_reflns.number_obs                       44452 
_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             99.300 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  5.000 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.064 
_reflns.pdbx_netI_over_av_sigmaI         6.200 
_reflns.pdbx_netI_over_sigmaI            11.500 
_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                  0.076 
_reflns.pdbx_Rpim_I_all                  0.033 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         222412 
_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 
1.400 1.480  ? 2.800  30921 ? ? ? 6421 99.000 ? ? ? ? 0.262 ? ? ? ? ? ? ? ? 4.800 0.262 ? ? 4.700  0.321 0.143 ? 1  1 ? ? ? 
1.480 1.570  ? 3.900  29612 ? ? ? 6075 98.800 ? ? ? ? 0.186 ? ? ? ? ? ? ? ? 4.900 0.186 ? ? 6.000  0.229 0.101 ? 2  1 ? ? ? 
1.570 1.670  ? 5.300  28850 ? ? ? 5735 99.100 ? ? ? ? 0.139 ? ? ? ? ? ? ? ? 5.000 0.139 ? ? 7.600  0.170 0.075 ? 3  1 ? ? ? 
1.670 1.810  ? 6.900  27531 ? ? ? 5351 99.300 ? ? ? ? 0.104 ? ? ? ? ? ? ? ? 5.100 0.104 ? ? 9.600  0.126 0.055 ? 4  1 ? ? ? 
1.810 1.980  ? 8.700  25262 ? ? ? 4935 99.200 ? ? ? ? 0.079 ? ? ? ? ? ? ? ? 5.100 0.079 ? ? 12.400 0.096 0.042 ? 5  1 ? ? ? 
1.980 2.210  ? 9.300  22605 ? ? ? 4478 99.700 ? ? ? ? 0.072 ? ? ? ? ? ? ? ? 5.000 0.072 ? ? 15.000 0.085 0.038 ? 6  1 ? ? ? 
2.210 2.560  ? 10.200 20387 ? ? ? 3987 99.600 ? ? ? ? 0.065 ? ? ? ? ? ? ? ? 5.100 0.065 ? ? 16.700 0.077 0.034 ? 7  1 ? ? ? 
2.560 3.130  ? 11.000 17188 ? ? ? 3353 99.600 ? ? ? ? 0.058 ? ? ? ? ? ? ? ? 5.100 0.058 ? ? 19.200 0.068 0.030 ? 8  1 ? ? ? 
3.130 4.430  ? 11.500 12438 ? ? ? 2626 99.500 ? ? ? ? 0.052 ? ? ? ? ? ? ? ? 4.700 0.052 ? ? 21.400 0.061 0.027 ? 9  1 ? ? ? 
4.430 40.746 ? 13.200 7618  ? ? ? 1491 99.700 ? ? ? ? 0.046 ? ? ? ? ? ? ? ? 5.100 0.046 ? ? 22.600 0.054 0.024 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.3400 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            1.1800 
_refine.aniso_B[2][2]                            -2.8200 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            2.2600 
_refine.B_iso_max                                64.760 
_refine.B_iso_mean                               17.8780 
_refine.B_iso_min                                8.690 
_refine.correlation_coeff_Fo_to_Fc               0.9740 
_refine.correlation_coeff_Fo_to_Fc_free          0.9530 
_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                                 6YH6 
_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                            1.4000 
_refine.ls_d_res_low                             40.4700 
_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                     39952 
_refine.ls_number_reflns_R_free                  4475 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.1300 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1447 
_refine.ls_R_factor_R_free                       0.1971 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1388 
_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                       0.0700 
_refine.pdbx_overall_ESU_R_Free                  0.0690 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.4000 
_refine_hist.d_res_low                        40.4700 
_refine_hist.number_atoms_solvent             207 
_refine_hist.number_atoms_total               2249 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       257 
_refine_hist.pdbx_B_iso_mean_ligand           22.52 
_refine_hist.pdbx_B_iso_mean_solvent          28.34 
_refine_hist.pdbx_number_atoms_protein        2015 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_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' ? 0.013  0.012  2173 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.964  1.650  2963 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.948  5.000  271  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.400 23.429 105  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.664 15.000 348  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 15.377 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.123  0.200  266  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  1700 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 5.429  3.000  2173 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 23.862 5.000  123  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 15.117 5.000  2190 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.4000 
_refine_ls_shell.d_res_low                        1.4360 
_refine_ls_shell.number_reflns_all                3243 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             318 
_refine_ls_shell.number_reflns_R_work             2925 
_refine_ls_shell.percent_reflns_obs               98.8100 
_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                  0.2540 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1870 
_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                     6YH6 
_struct.title                        
'Crystal structure of chimeric carbonic anhydrase XII with 2-(Cyclooctylamino)-3,5,6-trifluorobenzenesulfonamide' 
_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        6YH6 
_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 ? 
# 
_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              6YH6 
_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 6YH6 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YH6 LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YH6 THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YH6 ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YH6 SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YH6 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)' 230   ? 
1 MORE         2     ? 
1 'SSA (A^2)'  11040 ? 
# 
_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 
# 
_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 ? ? ? ? ? ? ? 1.868 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D OQW . S2  ? ? A ZN  301 A OQW 303 1_555 ? ? ? ? ? ? ? 2.952 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D OQW . N21 ? ? A ZN  301 A OQW 303 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
# 
_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_555 100.6 ? 
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_555 109.7 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.8  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S2  ? D OQW .   ? A OQW 303 ? 1_555 101.2 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S2  ? D OQW .   ? A OQW 303 ? 1_555 145.5 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S2  ? D OQW .   ? A OQW 303 ? 1_555 97.5  ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N21 ? D OQW .   ? A OQW 303 ? 1_555 116.8 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N21 ? D OQW .   ? A OQW 303 ? 1_555 112.8 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N21 ? D OQW .   ? A OQW 303 ? 1_555 114.9 ? 
10 S2  ? D OQW .   ? A OQW 303 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N21 ? D OQW .   ? A OQW 303 ? 1_555 32.8  ? 
# 
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 1.30 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 3.44 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LYS A 45  ? SER A 50  ? LYS A 45  SER A 50  
AA3 2  VAL A 78  ? GLY A 82  ? VAL A 78  GLY A 82  
AA3 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O 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 THR A 91  ? N THR A 91  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 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 THR A 91  ? N THR A 91  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 LYS A 148 ? N LYS A 149 O VAL A 217 ? O VAL A 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 3  'binding site for residue DMS A 302' 
AC3 Software A OQW 303 ? 15 'binding site for residue OQW A 303' 
# 
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  OQW D .   ? OQW A 303 . ? 1_555 ? 
5  AC2 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC3 15 ASN A 62  ? ASN A 62  . ? 1_555 ? 
9  AC3 15 HIS A 64  ? HIS A 64  . ? 1_555 ? 
10 AC3 15 SER A 65  ? SER A 65  . ? 1_555 ? 
11 AC3 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
12 AC3 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
13 AC3 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
14 AC3 15 VAL A 121 ? VAL A 121 . ? 1_555 ? 
15 AC3 15 LEU A 140 ? LEU A 141 . ? 1_555 ? 
16 AC3 15 VAL A 142 ? VAL A 143 . ? 1_555 ? 
17 AC3 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
18 AC3 15 THR A 198 ? THR A 199 . ? 1_555 ? 
19 AC3 15 THR A 199 ? THR A 200 . ? 1_555 ? 
20 AC3 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
21 AC3 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
22 AC3 15 HOH E .   ? HOH A 441 . ? 1_555 ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    214 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_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             2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            THR 
_pdbx_validate_rmsd_bond.auth_seq_id_1             125 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             127 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.494 
_pdbx_validate_rmsd_bond.bond_target_value         1.336 
_pdbx_validate_rmsd_bond.bond_deviation            0.158 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.023 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? B -143.85 38.99   
2 1 LEU A 57  ? ? -122.47 -53.73  
3 1 ALA A 77  ? ? 56.60   76.52   
4 1 LYS A 111 ? ? 76.49   -14.23  
5 1 ASN A 244 ? ? -97.90  51.58   
6 1 LYS A 252 ? ? 60.93   -129.01 
# 
_pdbx_entry_details.entry_id                 6YH6 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
OQW C6   C  Y N 260 
OQW C4   C  Y N 261 
OQW C3   C  Y N 262 
OQW O1   O  N N 263 
OQW C8   C  Y N 264 
OQW C11  C  Y N 265 
OQW C13  C  N N 266 
OQW C14  C  N N 267 
OQW C9   C  Y N 268 
OQW C15  C  N N 269 
OQW C16  C  N N 270 
OQW C17  C  N N 271 
OQW C20  C  N N 272 
OQW C19  C  N N 273 
OQW C18  C  N N 274 
OQW O22  O  N N 275 
OQW S2   S  N N 276 
OQW N21  N  N N 277 
OQW F10  F  N N 278 
OQW F7   F  N N 279 
OQW F5   F  N N 280 
OQW N12  N  N N 281 
OQW H1   H  N N 282 
OQW H2   H  N N 283 
OQW H3   H  N N 284 
OQW H4   H  N N 285 
OQW H5   H  N N 286 
OQW H6   H  N N 287 
OQW H7   H  N N 288 
OQW H8   H  N N 289 
OQW H9   H  N N 290 
OQW H10  H  N N 291 
OQW H11  H  N N 292 
OQW H12  H  N N 293 
OQW H13  H  N N 294 
OQW H14  H  N N 295 
OQW H15  H  N N 296 
OQW H16  H  N N 297 
OQW H17  H  N N 298 
OQW H18  H  N N 299 
OQW H19  H  N N 300 
PHE N    N  N N 301 
PHE CA   C  N S 302 
PHE C    C  N N 303 
PHE O    O  N N 304 
PHE CB   C  N N 305 
PHE CG   C  Y N 306 
PHE CD1  C  Y N 307 
PHE CD2  C  Y N 308 
PHE CE1  C  Y N 309 
PHE CE2  C  Y N 310 
PHE CZ   C  Y N 311 
PHE OXT  O  N N 312 
PHE H    H  N N 313 
PHE H2   H  N N 314 
PHE HA   H  N N 315 
PHE HB2  H  N N 316 
PHE HB3  H  N N 317 
PHE HD1  H  N N 318 
PHE HD2  H  N N 319 
PHE HE1  H  N N 320 
PHE HE2  H  N N 321 
PHE HZ   H  N N 322 
PHE HXT  H  N N 323 
PRO N    N  N N 324 
PRO CA   C  N S 325 
PRO C    C  N N 326 
PRO O    O  N N 327 
PRO CB   C  N N 328 
PRO CG   C  N N 329 
PRO CD   C  N N 330 
PRO OXT  O  N N 331 
PRO H    H  N N 332 
PRO HA   H  N N 333 
PRO HB2  H  N N 334 
PRO HB3  H  N N 335 
PRO HG2  H  N N 336 
PRO HG3  H  N N 337 
PRO HD2  H  N N 338 
PRO HD3  H  N N 339 
PRO HXT  H  N N 340 
SER N    N  N N 341 
SER CA   C  N S 342 
SER C    C  N N 343 
SER O    O  N N 344 
SER CB   C  N N 345 
SER OG   O  N N 346 
SER OXT  O  N N 347 
SER H    H  N N 348 
SER H2   H  N N 349 
SER HA   H  N N 350 
SER HB2  H  N N 351 
SER HB3  H  N N 352 
SER HG   H  N N 353 
SER HXT  H  N N 354 
THR N    N  N N 355 
THR CA   C  N S 356 
THR C    C  N N 357 
THR O    O  N N 358 
THR CB   C  N R 359 
THR OG1  O  N N 360 
THR CG2  C  N N 361 
THR OXT  O  N N 362 
THR H    H  N N 363 
THR H2   H  N N 364 
THR HA   H  N N 365 
THR HB   H  N N 366 
THR HG1  H  N N 367 
THR HG21 H  N N 368 
THR HG22 H  N N 369 
THR HG23 H  N N 370 
THR HXT  H  N N 371 
TRP N    N  N N 372 
TRP CA   C  N S 373 
TRP C    C  N N 374 
TRP O    O  N N 375 
TRP CB   C  N N 376 
TRP CG   C  Y N 377 
TRP CD1  C  Y N 378 
TRP CD2  C  Y N 379 
TRP NE1  N  Y N 380 
TRP CE2  C  Y N 381 
TRP CE3  C  Y N 382 
TRP CZ2  C  Y N 383 
TRP CZ3  C  Y N 384 
TRP CH2  C  Y N 385 
TRP OXT  O  N N 386 
TRP H    H  N N 387 
TRP H2   H  N N 388 
TRP HA   H  N N 389 
TRP HB2  H  N N 390 
TRP HB3  H  N N 391 
TRP HD1  H  N N 392 
TRP HE1  H  N N 393 
TRP HE3  H  N N 394 
TRP HZ2  H  N N 395 
TRP HZ3  H  N N 396 
TRP HH2  H  N N 397 
TRP HXT  H  N N 398 
TYR N    N  N N 399 
TYR CA   C  N S 400 
TYR C    C  N N 401 
TYR O    O  N N 402 
TYR CB   C  N N 403 
TYR CG   C  Y N 404 
TYR CD1  C  Y N 405 
TYR CD2  C  Y N 406 
TYR CE1  C  Y N 407 
TYR CE2  C  Y N 408 
TYR CZ   C  Y N 409 
TYR OH   O  N N 410 
TYR OXT  O  N N 411 
TYR H    H  N N 412 
TYR H2   H  N N 413 
TYR HA   H  N N 414 
TYR HB2  H  N N 415 
TYR HB3  H  N N 416 
TYR HD1  H  N N 417 
TYR HD2  H  N N 418 
TYR HE1  H  N N 419 
TYR HE2  H  N N 420 
TYR HH   H  N N 421 
TYR HXT  H  N N 422 
VAL N    N  N N 423 
VAL CA   C  N S 424 
VAL C    C  N N 425 
VAL O    O  N N 426 
VAL CB   C  N N 427 
VAL CG1  C  N N 428 
VAL CG2  C  N N 429 
VAL OXT  O  N N 430 
VAL H    H  N N 431 
VAL H2   H  N N 432 
VAL HA   H  N N 433 
VAL HB   H  N N 434 
VAL HG11 H  N N 435 
VAL HG12 H  N N 436 
VAL HG13 H  N N 437 
VAL HG21 H  N N 438 
VAL HG22 H  N N 439 
VAL HG23 H  N N 440 
VAL HXT  H  N N 441 
ZN  ZN   ZN N N 442 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
OQW C18 C17  sing N N 246 
OQW C18 C19  sing N N 247 
OQW C17 C16  sing N N 248 
OQW C16 C15  sing N N 249 
OQW C19 C20  sing N N 250 
OQW C15 C14  sing N N 251 
OQW C20 C13  sing N N 252 
OQW C14 C13  sing N N 253 
OQW C13 N12  sing N N 254 
OQW F10 C9   sing N N 255 
OQW C9  C8   doub Y N 256 
OQW C9  C11  sing Y N 257 
OQW N12 C11  sing N N 258 
OQW C8  C6   sing Y N 259 
OQW C11 C3   doub Y N 260 
OQW C6  F7   sing N N 261 
OQW C6  C4   doub Y N 262 
OQW C3  C4   sing Y N 263 
OQW C3  S2   sing N N 264 
OQW N21 S2   sing N N 265 
OQW C4  F5   sing N N 266 
OQW O22 S2   doub N N 267 
OQW S2  O1   doub N N 268 
OQW C8  H1   sing N N 269 
OQW C13 H2   sing N N 270 
OQW C14 H3   sing N N 271 
OQW C14 H4   sing N N 272 
OQW C15 H5   sing N N 273 
OQW C15 H6   sing N N 274 
OQW C16 H7   sing N N 275 
OQW C16 H8   sing N N 276 
OQW C17 H9   sing N N 277 
OQW C17 H10  sing N N 278 
OQW C20 H11  sing N N 279 
OQW C20 H12  sing N N 280 
OQW C19 H13  sing N N 281 
OQW C19 H14  sing N N 282 
OQW C18 H15  sing N N 283 
OQW C18 H16  sing N N 284 
OQW N21 H17  sing N N 285 
OQW N21 H18  sing N N 286 
OQW N12 H19  sing N N 287 
PHE N   CA   sing N N 288 
PHE N   H    sing N N 289 
PHE N   H2   sing N N 290 
PHE CA  C    sing N N 291 
PHE CA  CB   sing N N 292 
PHE CA  HA   sing N N 293 
PHE C   O    doub N N 294 
PHE C   OXT  sing N N 295 
PHE CB  CG   sing N N 296 
PHE CB  HB2  sing N N 297 
PHE CB  HB3  sing N N 298 
PHE CG  CD1  doub Y N 299 
PHE CG  CD2  sing Y N 300 
PHE CD1 CE1  sing Y N 301 
PHE CD1 HD1  sing N N 302 
PHE CD2 CE2  doub Y N 303 
PHE CD2 HD2  sing N N 304 
PHE CE1 CZ   doub Y N 305 
PHE CE1 HE1  sing N N 306 
PHE CE2 CZ   sing Y N 307 
PHE CE2 HE2  sing N N 308 
PHE CZ  HZ   sing N N 309 
PHE OXT HXT  sing N N 310 
PRO N   CA   sing N N 311 
PRO N   CD   sing N N 312 
PRO N   H    sing N N 313 
PRO CA  C    sing N N 314 
PRO CA  CB   sing N N 315 
PRO CA  HA   sing N N 316 
PRO C   O    doub N N 317 
PRO C   OXT  sing N N 318 
PRO CB  CG   sing N N 319 
PRO CB  HB2  sing N N 320 
PRO CB  HB3  sing N N 321 
PRO CG  CD   sing N N 322 
PRO CG  HG2  sing N N 323 
PRO CG  HG3  sing N N 324 
PRO CD  HD2  sing N N 325 
PRO CD  HD3  sing N N 326 
PRO OXT HXT  sing N N 327 
SER N   CA   sing N N 328 
SER N   H    sing N N 329 
SER N   H2   sing N N 330 
SER CA  C    sing N N 331 
SER CA  CB   sing N N 332 
SER CA  HA   sing N N 333 
SER C   O    doub N N 334 
SER C   OXT  sing N N 335 
SER CB  OG   sing N N 336 
SER CB  HB2  sing N N 337 
SER CB  HB3  sing N N 338 
SER OG  HG   sing N N 339 
SER OXT HXT  sing N N 340 
THR N   CA   sing N N 341 
THR N   H    sing N N 342 
THR N   H2   sing N N 343 
THR CA  C    sing N N 344 
THR CA  CB   sing N N 345 
THR CA  HA   sing N N 346 
THR C   O    doub N N 347 
THR C   OXT  sing N N 348 
THR CB  OG1  sing N N 349 
THR CB  CG2  sing N N 350 
THR CB  HB   sing N N 351 
THR OG1 HG1  sing N N 352 
THR CG2 HG21 sing N N 353 
THR CG2 HG22 sing N N 354 
THR CG2 HG23 sing N N 355 
THR OXT HXT  sing N N 356 
TRP N   CA   sing N N 357 
TRP N   H    sing N N 358 
TRP N   H2   sing N N 359 
TRP CA  C    sing N N 360 
TRP CA  CB   sing N N 361 
TRP CA  HA   sing N N 362 
TRP C   O    doub N N 363 
TRP C   OXT  sing N N 364 
TRP CB  CG   sing N N 365 
TRP CB  HB2  sing N N 366 
TRP CB  HB3  sing N N 367 
TRP CG  CD1  doub Y N 368 
TRP CG  CD2  sing Y N 369 
TRP CD1 NE1  sing Y N 370 
TRP CD1 HD1  sing N N 371 
TRP CD2 CE2  doub Y N 372 
TRP CD2 CE3  sing Y N 373 
TRP NE1 CE2  sing Y N 374 
TRP NE1 HE1  sing N N 375 
TRP CE2 CZ2  sing Y N 376 
TRP CE3 CZ3  doub Y N 377 
TRP CE3 HE3  sing N N 378 
TRP CZ2 CH2  doub Y N 379 
TRP CZ2 HZ2  sing N N 380 
TRP CZ3 CH2  sing Y N 381 
TRP CZ3 HZ3  sing N N 382 
TRP CH2 HH2  sing N N 383 
TRP OXT HXT  sing N N 384 
TYR N   CA   sing N N 385 
TYR N   H    sing N N 386 
TYR N   H2   sing N N 387 
TYR CA  C    sing N N 388 
TYR CA  CB   sing N N 389 
TYR CA  HA   sing N N 390 
TYR C   O    doub N N 391 
TYR C   OXT  sing N N 392 
TYR CB  CG   sing N N 393 
TYR CB  HB2  sing N N 394 
TYR CB  HB3  sing N N 395 
TYR CG  CD1  doub Y N 396 
TYR CG  CD2  sing Y N 397 
TYR CD1 CE1  sing Y N 398 
TYR CD1 HD1  sing N N 399 
TYR CD2 CE2  doub Y N 400 
TYR CD2 HD2  sing N N 401 
TYR CE1 CZ   doub Y N 402 
TYR CE1 HE1  sing N N 403 
TYR CE2 CZ   sing Y N 404 
TYR CE2 HE2  sing N N 405 
TYR CZ  OH   sing N N 406 
TYR OH  HH   sing N N 407 
TYR OXT HXT  sing N N 408 
VAL N   CA   sing N N 409 
VAL N   H    sing N N 410 
VAL N   H2   sing N N 411 
VAL CA  C    sing N N 412 
VAL CA  CB   sing N N 413 
VAL CA  HA   sing N N 414 
VAL C   O    doub N N 415 
VAL C   OXT  sing N N 416 
VAL CB  CG1  sing N N 417 
VAL CB  CG2  sing N N 418 
VAL CB  HB   sing N N 419 
VAL CG1 HG11 sing N N 420 
VAL CG1 HG12 sing N N 421 
VAL CG1 HG13 sing N N 422 
VAL CG2 HG21 sing N N 423 
VAL CG2 HG22 sing N N 424 
VAL CG2 HG23 sing N N 425 
VAL OXT HXT  sing N N 426 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        OQW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   OQW 
_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                    6YH6 
_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]   0.023939 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006134 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024542 
_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]   0.014870 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 32.509 1.213   6.747   1.00 59.55 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.762 1.951   7.779   1.00 39.08 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 31.058 0.957   8.698   1.00 32.05 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 31.296 -0.252  8.576   1.00 29.70 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 30.784 2.920   7.109   1.00 35.62 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 30.472 4.098   7.993   1.00 28.99 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 31.274 4.412   9.093   1.00 47.47 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 29.579 5.115   7.855   1.00 54.32 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 30.844 5.531   9.644   1.00 54.21 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 29.793 5.985   8.910   1.00 59.49 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 30.205 1.448   9.617   1.00 31.40 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 29.511 0.514   10.486  1.00 22.11 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 28.540 -0.341  9.679   1.00 19.01 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 28.047 0.053   8.610   1.00 24.04 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.843 1.187   11.701  1.00 20.02 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 27.645 2.014   11.336  1.00 16.89 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 27.593 3.330   10.983  1.00 25.09 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 26.306 1.526   11.237  1.00 17.75 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 26.306 3.701   10.677  1.00 24.07 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 25.495 2.617   10.838  1.00 18.84 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.728 0.269   11.466  1.00 16.25 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 24.107 2.474   10.704  1.00 22.54 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 24.356 0.125   11.339  1.00 18.03 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 23.572 1.220   10.959  1.00 19.20 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 28.285 -1.540  10.178  1.00 17.18 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 27.243 -2.392  9.646   1.00 17.88 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.874 -3.517  10.589  1.00 16.19 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.850 -3.331  11.814  1.00 17.83 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 26.546 -4.689  10.051  1.00 19.57 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 26.076 -5.793  10.873  1.00 20.18 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.926 -7.046  10.691  1.00 24.32 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.579 -8.106  11.220  1.00 32.03 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 24.614 -6.079  10.558  1.00 20.35 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.661 -5.039  11.062  1.00 17.51 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 23.307 -4.981  12.421  1.00 14.58 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 23.146 -4.091  10.212  1.00 18.74 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 22.414 -4.037  12.901  1.00 16.09 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 22.296 -3.115  10.677  1.00 16.13 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.918 -3.094  12.012  1.00 15.90 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 21.014 -2.166  12.404  1.00 18.85 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 28.093 -6.866  10.053  1.00 24.53 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 29.004 -7.954  9.750   1.00 26.04 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.970 -8.237  10.902  1.00 23.64 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.992 -7.518  11.919  1.00 22.27 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.727 -9.327  10.706  1.00 22.78 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.737 -9.800  11.627  1.00 22.65 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.727 -8.693  11.979  1.00 20.86 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 33.194 -8.649  13.113  1.00 21.53 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 32.509 -10.985 11.021  1.00 29.24 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 33.608 -11.580 11.881  1.00 28.27 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 33.959 -13.050 11.671  1.00 37.97 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 33.854 -13.540 10.246  1.00 40.87 ? 9   LYS A CE  1 
ATOM   53   N  N   . HIS A 1 10  ? 33.093 -7.816  11.046  1.00 21.99 ? 10  HIS A N   1 
ATOM   54   C  CA  . HIS A 1 10  ? 34.195 -6.901  11.313  1.00 21.71 ? 10  HIS A CA  1 
ATOM   55   C  C   . HIS A 1 10  ? 33.719 -5.464  11.534  1.00 19.14 ? 10  HIS A C   1 
ATOM   56   O  O   . HIS A 1 10  ? 34.534 -4.589  11.879  1.00 22.62 ? 10  HIS A O   1 
ATOM   57   C  CB  . HIS A 1 10  ? 35.222 -6.966  10.168  1.00 26.26 ? 10  HIS A CB  1 
ATOM   58   C  CG  . HIS A 1 10  ? 35.749 -8.348  9.996   1.00 24.68 ? 10  HIS A CG  1 
ATOM   59   N  ND1 . HIS A 1 10  ? 36.778 -8.823  10.773  1.00 26.54 ? 10  HIS A ND1 1 
ATOM   60   C  CD2 . HIS A 1 10  ? 35.373 -9.356  9.181   1.00 27.26 ? 10  HIS A CD2 1 
ATOM   61   C  CE1 . HIS A 1 10  ? 37.027 -10.071 10.456  1.00 27.59 ? 10  HIS A CE1 1 
ATOM   62   N  NE2 . HIS A 1 10  ? 36.180 -10.419 9.465   1.00 35.21 ? 10  HIS A NE2 1 
ATOM   63   N  N   . ASN A 1 11  ? 32.411 -5.223  11.402  1.00 20.25 ? 11  ASN A N   1 
ATOM   64   C  CA  . ASN A 1 11  ? 31.910 -3.863  11.472  1.00 19.14 ? 11  ASN A CA  1 
ATOM   65   C  C   . ASN A 1 11  ? 30.600 -3.803  12.254  1.00 15.99 ? 11  ASN A C   1 
ATOM   66   O  O   . ASN A 1 11  ? 29.976 -2.727  12.327  1.00 16.62 ? 11  ASN A O   1 
ATOM   67   C  CB  . ASN A 1 11  ? 31.795 -3.219  10.079  1.00 21.63 ? 11  ASN A CB  1 
ATOM   68   C  CG  . ASN A 1 11  ? 30.674 -3.827  9.265   1.00 22.82 ? 11  ASN A CG  1 
ATOM   69   O  OD1 . ASN A 1 11  ? 30.074 -4.798  9.697   1.00 22.04 ? 11  ASN A OD1 1 
ATOM   70   N  ND2 . ASN A 1 11  ? 30.412 -3.325  8.063   1.00 23.22 ? 11  ASN A ND2 1 
ATOM   71   N  N   . GLY A 1 12  ? 30.202 -4.942  12.836  1.00 16.18 ? 12  GLY A N   1 
ATOM   72   C  CA  . GLY A 1 12  ? 28.896 -5.073  13.483  1.00 17.92 ? 12  GLY A CA  1 
ATOM   73   C  C   . GLY A 1 12  ? 28.881 -4.569  14.931  1.00 14.58 ? 12  GLY A C   1 
ATOM   74   O  O   . GLY A 1 12  ? 29.799 -3.884  15.397  1.00 16.25 ? 12  GLY A O   1 
ATOM   75   N  N   . PRO A 1 13  ? 27.788 -4.906  15.655  1.00 13.86 ? 13  PRO A N   1 
ATOM   76   C  CA  . PRO A 1 13  ? 27.502 -4.411  16.998  1.00 14.71 ? 13  PRO A CA  1 
ATOM   77   C  C   . PRO A 1 13  ? 28.647 -4.458  17.992  1.00 15.15 ? 13  PRO A C   1 
ATOM   78   O  O   . PRO A 1 13  ? 28.770 -3.509  18.769  1.00 16.11 ? 13  PRO A O   1 
ATOM   79   C  CB  . PRO A 1 13  ? 26.303 -5.261  17.446  1.00 15.71 ? 13  PRO A CB  1 
ATOM   80   C  CG  . PRO A 1 13  ? 25.570 -5.470  16.166  1.00 15.00 ? 13  PRO A CG  1 
ATOM   81   C  CD  . PRO A 1 13  ? 26.643 -5.618  15.101  1.00 15.22 ? 13  PRO A CD  1 
ATOM   82   N  N   . GLU A 1 14  ? 29.483 -5.495  17.928  1.00 15.97 ? 14  GLU A N   1 
ATOM   83   C  CA  . GLU A 1 14  ? 30.609 -5.598  18.873  1.00 15.60 ? 14  GLU A CA  1 
ATOM   84   C  C   . GLU A 1 14  ? 31.700 -4.549  18.640  1.00 15.40 ? 14  GLU A C   1 
ATOM   85   O  O   . GLU A 1 14  ? 32.587 -4.339  19.485  1.00 19.88 ? 14  GLU A O   1 
ATOM   86   C  CB  . GLU A 1 14  ? 31.197 -7.009  18.795  1.00 22.54 ? 14  GLU A CB  1 
ATOM   87   C  CG  . GLU A 1 14  ? 30.149 -8.044  19.118  1.00 30.54 ? 14  GLU A CG  1 
ATOM   88   C  CD  . GLU A 1 14  ? 29.358 -7.826  20.419  1.00 43.73 ? 14  GLU A CD  1 
ATOM   89   O  OE1 . GLU A 1 14  ? 30.001 -7.640  21.497  1.00 38.58 ? 14  GLU A OE1 1 
ATOM   90   O  OE2 . GLU A 1 14  ? 28.070 -7.800  20.348  1.00 53.27 ? 14  GLU A OE2 1 
ATOM   91   N  N   . HIS A 1 15  ? 31.695 -3.952  17.449  1.00 16.44 ? 15  HIS A N   1 
ATOM   92   C  CA  . HIS A 1 15  ? 32.700 -2.974  17.041  1.00 13.68 ? 15  HIS A CA  1 
ATOM   93   C  C   . HIS A 1 15  ? 32.240 -1.517  17.223  1.00 13.61 ? 15  HIS A C   1 
ATOM   94   O  O   . HIS A 1 15  ? 33.050 -0.595  17.186  1.00 13.81 ? 15  HIS A O   1 
ATOM   95   C  CB  . HIS A 1 15  ? 33.008 -3.175  15.544  1.00 15.00 ? 15  HIS A CB  1 
ATOM   96   C  CG  . HIS A 1 15  ? 33.744 -4.441  15.257  1.00 14.83 ? 15  HIS A CG  1 
ATOM   97   N  ND1 . HIS A 1 15  ? 35.141 -4.529  15.390  1.00 14.90 ? 15  HIS A ND1 1 
ATOM   98   C  CD2 . HIS A 1 15  ? 33.322 -5.682  14.919  1.00 18.85 ? 15  HIS A CD2 1 
ATOM   99   C  CE1 . HIS A 1 15  ? 35.550 -5.778  15.125  1.00 17.42 ? 15  HIS A CE1 1 
ATOM   100  N  NE2 . HIS A 1 15  ? 34.449 -6.503  14.798  1.00 19.46 ? 15  HIS A NE2 1 
ATOM   101  N  N   . TRP A 1 16  ? 30.934 -1.300  17.433  1.00 14.38 ? 16  TRP A N   1 
ATOM   102  C  CA  . TRP A 1 16  ? 30.385 0.047   17.355  1.00 13.97 ? 16  TRP A CA  1 
ATOM   103  C  C   . TRP A 1 16  ? 30.980 1.001   18.393  1.00 12.83 ? 16  TRP A C   1 
ATOM   104  O  O   . TRP A 1 16  ? 31.055 2.194   18.156  1.00 13.73 ? 16  TRP A O   1 
ATOM   105  C  CB  . TRP A 1 16  ? 28.849 -0.002  17.424  1.00 13.83 ? 16  TRP A CB  1 
ATOM   106  C  CG  . TRP A 1 16  ? 28.223 -0.643  16.220  1.00 13.53 ? 16  TRP A CG  1 
ATOM   107  C  CD1 . TRP A 1 16  ? 28.798 -0.988  15.023  1.00 12.33 ? 16  TRP A CD1 1 
ATOM   108  C  CD2 . TRP A 1 16  ? 26.839 -0.998  16.116  1.00 13.69 ? 16  TRP A CD2 1 
ATOM   109  N  NE1 . TRP A 1 16  ? 27.831 -1.519  14.190  1.00 14.94 ? 16  TRP A NE1 1 
ATOM   110  C  CE2 . TRP A 1 16  ? 26.636 -1.587  14.860  1.00 13.69 ? 16  TRP A CE2 1 
ATOM   111  C  CE3 . TRP A 1 16  ? 25.759 -0.925  17.003  1.00 12.46 ? 16  TRP A CE3 1 
ATOM   112  C  CZ2 . TRP A 1 16  ? 25.376 -2.006  14.419  1.00 14.87 ? 16  TRP A CZ2 1 
ATOM   113  C  CZ3 . TRP A 1 16  ? 24.518 -1.373  16.573  1.00 13.14 ? 16  TRP A CZ3 1 
ATOM   114  C  CH2 . TRP A 1 16  ? 24.314 -1.914  15.293  1.00 13.65 ? 16  TRP A CH2 1 
ATOM   115  N  N   . HIS A 1 17  ? 31.338 0.470   19.573  1.00 14.26 ? 17  HIS A N   1 
ATOM   116  C  CA  . HIS A 1 17  ? 31.783 1.316   20.661  1.00 13.83 ? 17  HIS A CA  1 
ATOM   117  C  C   . HIS A 1 17  ? 33.045 2.082   20.291  1.00 14.62 ? 17  HIS A C   1 
ATOM   118  O  O   . HIS A 1 17  ? 33.345 3.125   20.869  1.00 15.16 ? 17  HIS A O   1 
ATOM   119  C  CB  . HIS A 1 17  ? 32.009 0.430   21.885  1.00 16.22 ? 17  HIS A CB  1 
ATOM   120  C  CG  . HIS A 1 17  ? 33.228 -0.407  21.750  1.00 14.01 ? 17  HIS A CG  1 
ATOM   121  N  ND1 . HIS A 1 17  ? 34.434 -0.056  22.358  1.00 17.85 ? 17  HIS A ND1 1 
ATOM   122  C  CD2 . HIS A 1 17  ? 33.428 -1.589  21.130  1.00 15.52 ? 17  HIS A CD2 1 
ATOM   123  C  CE1 . HIS A 1 17  ? 35.307 -1.002  22.129  1.00 19.86 ? 17  HIS A CE1 1 
ATOM   124  N  NE2 . HIS A 1 17  ? 34.728 -1.929  21.339  1.00 17.50 ? 17  HIS A NE2 1 
ATOM   125  N  N   . LYS A 1 18  ? 33.808 1.610   19.285  1.00 14.20 ? 18  LYS A N   1 
ATOM   126  C  CA  . LYS A 1 18  ? 35.036 2.312   18.979  1.00 14.41 ? 18  LYS A CA  1 
ATOM   127  C  C   . LYS A 1 18  ? 34.742 3.693   18.397  1.00 15.80 ? 18  LYS A C   1 
ATOM   128  O  O   . LYS A 1 18  ? 35.459 4.661   18.660  1.00 21.56 ? 18  LYS A O   1 
ATOM   129  C  CB  . LYS A 1 18  ? 35.929 1.459   18.087  1.00 14.76 ? 18  LYS A CB  1 
ATOM   130  C  CG  . LYS A 1 18  ? 36.542 0.276   18.821  1.00 15.80 ? 18  LYS A CG  1 
ATOM   131  C  CD  . LYS A 1 18  ? 37.211 -0.727  17.869  1.00 17.83 ? 18  LYS A CD  1 
ATOM   132  C  CE  . LYS A 1 18  ? 36.232 -1.687  17.192  1.00 18.27 ? 18  LYS A CE  1 
ATOM   133  N  NZ  . LYS A 1 18  ? 36.890 -2.471  16.097  1.00 15.90 ? 18  LYS A NZ  1 
ATOM   134  N  N   . ASP A 1 19  ? 33.741 3.736   17.515  1.00 16.47 ? 19  ASP A N   1 
ATOM   135  C  CA  . ASP A 1 19  ? 33.392 5.023   16.940  1.00 16.04 ? 19  ASP A CA  1 
ATOM   136  C  C   . ASP A 1 19  ? 32.372 5.734   17.818  1.00 15.37 ? 19  ASP A C   1 
ATOM   137  O  O   . ASP A 1 19  ? 32.333 6.961   17.778  1.00 17.52 ? 19  ASP A O   1 
ATOM   138  C  CB  . ASP A 1 19  ? 32.739 4.920   15.561  1.00 20.49 ? 19  ASP A CB  1 
ATOM   139  C  CG  . ASP A 1 19  ? 33.676 5.133   14.380  1.00 32.04 ? 19  ASP A CG  1 
ATOM   140  O  OD1 . ASP A 1 19  ? 34.807 5.654   14.560  1.00 31.18 ? 19  ASP A OD1 1 
ATOM   141  O  OD2 . ASP A 1 19  ? 33.257 4.805   13.290  1.00 39.70 ? 19  ASP A OD2 1 
ATOM   142  N  N   . PHE A 1 20  ? 31.570 4.963   18.581  1.00 14.21 ? 20  PHE A N   1 
ATOM   143  C  CA  . PHE A 1 20  ? 30.512 5.559   19.386  1.00 15.41 ? 20  PHE A CA  1 
ATOM   144  C  C   . PHE A 1 20  ? 30.604 5.009   20.799  1.00 16.81 ? 20  PHE A C   1 
ATOM   145  O  O   . PHE A 1 20  ? 29.950 4.027   21.130  1.00 15.32 ? 20  PHE A O   1 
ATOM   146  C  CB  . PHE A 1 20  ? 29.125 5.270   18.790  1.00 16.40 ? 20  PHE A CB  1 
ATOM   147  C  CG  . PHE A 1 20  ? 29.042 5.759   17.359  1.00 19.42 ? 20  PHE A CG  1 
ATOM   148  C  CD1 . PHE A 1 20  ? 28.790 7.089   17.113  1.00 23.07 ? 20  PHE A CD1 1 
ATOM   149  C  CD2 . PHE A 1 20  ? 29.337 4.905   16.293  1.00 20.51 ? 20  PHE A CD2 1 
ATOM   150  C  CE1 . PHE A 1 20  ? 28.813 7.560   15.803  1.00 26.32 ? 20  PHE A CE1 1 
ATOM   151  C  CE2 . PHE A 1 20  ? 29.315 5.365   14.984  1.00 22.72 ? 20  PHE A CE2 1 
ATOM   152  C  CZ  . PHE A 1 20  ? 29.045 6.692   14.750  1.00 23.63 ? 20  PHE A CZ  1 
ATOM   153  N  N   . PRO A 1 21  ? 31.460 5.598   21.659  1.00 16.89 ? 21  PRO A N   1 
ATOM   154  C  CA  . PRO A 1 21  ? 31.675 5.037   22.980  1.00 16.42 ? 21  PRO A CA  1 
ATOM   155  C  C   . PRO A 1 21  ? 30.447 4.883   23.879  1.00 15.36 ? 21  PRO A C   1 
ATOM   156  O  O   . PRO A 1 21  ? 30.504 4.069   24.799  1.00 16.59 ? 21  PRO A O   1 
ATOM   157  C  CB  . PRO A 1 21  ? 32.722 5.931   23.660  1.00 18.68 ? 21  PRO A CB  1 
ATOM   158  C  CG  . PRO A 1 21  ? 32.831 7.125   22.763  1.00 25.29 ? 21  PRO A CG  1 
ATOM   159  C  CD  . PRO A 1 21  ? 32.361 6.722   21.382  1.00 20.38 ? 21  PRO A CD  1 
ATOM   160  N  N   . ILE A 1 22  ? 29.368 5.632   23.554  1.00 13.11 ? 22  ILE A N   1 
ATOM   161  C  CA  . ILE A 1 22  ? 28.105 5.526   24.267  1.00 13.26 ? 22  ILE A CA  1 
ATOM   162  C  C   . ILE A 1 22  ? 27.525 4.115   24.090  1.00 11.38 ? 22  ILE A C   1 
ATOM   163  O  O   . ILE A 1 22  ? 26.659 3.704   24.841  1.00 14.27 ? 22  ILE A O   1 
ATOM   164  C  CB  . ILE A 1 22  ? 27.101 6.646   23.866  1.00 13.64 ? 22  ILE A CB  1 
ATOM   165  C  CG1 . ILE A 1 22  ? 25.994 6.869   24.903  1.00 15.85 ? 22  ILE A CG1 1 
ATOM   166  C  CG2 . ILE A 1 22  ? 26.535 6.393   22.478  1.00 14.06 ? 22  ILE A CG2 1 
ATOM   167  C  CD1 . ILE A 1 22  ? 26.475 7.472   26.241  1.00 22.25 ? 22  ILE A CD1 1 
ATOM   168  N  N   . ALA A 1 23  ? 28.053 3.330   23.138  1.00 14.38 ? 23  ALA A N   1 
ATOM   169  C  CA  . ALA A 1 23  ? 27.670 1.924   23.012  1.00 13.60 ? 23  ALA A CA  1 
ATOM   170  C  C   . ALA A 1 23  ? 27.765 1.163   24.337  1.00 15.37 ? 23  ALA A C   1 
ATOM   171  O  O   . ALA A 1 23  ? 27.089 0.135   24.509  1.00 17.00 ? 23  ALA A O   1 
ATOM   172  C  CB  . ALA A 1 23  ? 28.457 1.226   21.940  1.00 14.24 ? 23  ALA A CB  1 
ATOM   173  N  N   . LYS A 1 24  ? 28.707 1.592   25.198  1.00 16.32 ? 24  LYS A N   1 
ATOM   174  C  CA  . LYS A 1 24  ? 28.885 0.961   26.502  1.00 18.31 ? 24  LYS A CA  1 
ATOM   175  C  C   . LYS A 1 24  ? 28.288 1.807   27.629  1.00 16.31 ? 24  LYS A C   1 
ATOM   176  O  O   . LYS A 1 24  ? 28.706 1.701   28.827  1.00 20.56 ? 24  LYS A O   1 
ATOM   177  C  CB  . LYS A 1 24  ? 30.370 0.654   26.741  1.00 22.09 ? 24  LYS A CB  1 
ATOM   178  C  CG  . LYS A 1 24  ? 30.989 -0.321  25.734  1.00 23.06 ? 24  LYS A CG  1 
ATOM   179  C  CD  . LYS A 1 24  ? 32.462 -0.537  26.047  1.00 30.37 ? 24  LYS A CD  1 
ATOM   180  C  CE  . LYS A 1 24  ? 33.066 -1.576  25.135  1.00 34.06 ? 24  LYS A CE  1 
ATOM   181  N  NZ  . LYS A 1 24  ? 32.496 -2.907  25.464  1.00 41.18 ? 24  LYS A NZ  1 
ATOM   182  N  N   . GLY A 1 25  ? 27.263 2.600   27.269  1.00 17.57 ? 25  GLY A N   1 
ATOM   183  C  CA  . GLY A 1 25  ? 26.678 3.543   28.205  1.00 16.25 ? 25  GLY A CA  1 
ATOM   184  C  C   . GLY A 1 25  ? 25.723 2.838   29.174  1.00 15.86 ? 25  GLY A C   1 
ATOM   185  O  O   . GLY A 1 25  ? 25.568 1.606   29.168  1.00 16.29 ? 25  GLY A O   1 
ATOM   186  N  N   . GLU A 1 26  ? 25.014 3.673   29.932  1.00 15.56 ? 26  GLU A N   1 
ATOM   187  C  CA  . GLU A 1 26  ? 24.101 3.216   30.961  1.00 16.64 ? 26  GLU A CA  1 
ATOM   188  C  C   . GLU A 1 26  ? 22.652 3.007   30.505  1.00 15.86 ? 26  GLU A C   1 
ATOM   189  O  O   . GLU A 1 26  ? 21.875 2.424   31.275  1.00 16.83 ? 26  GLU A O   1 
ATOM   190  C  CB  . GLU A 1 26  ? 24.100 4.204   32.121  1.00 19.26 ? 26  GLU A CB  1 
ATOM   191  C  CG  . GLU A 1 26  ? 25.474 4.428   32.720  1.00 25.80 ? 26  GLU A CG  1 
ATOM   192  C  CD  . GLU A 1 26  ? 26.051 3.116   33.250  1.00 31.79 ? 26  GLU A CD  1 
ATOM   193  O  OE1 . GLU A 1 26  ? 25.295 2.351   33.926  1.00 35.95 ? 26  GLU A OE1 1 
ATOM   194  O  OE2 . GLU A 1 26  ? 27.247 2.833   32.965  1.00 37.89 ? 26  GLU A OE2 1 
ATOM   195  N  N   A ARG A 1 27  ? 22.284 3.541   29.318  0.50 13.21 ? 27  ARG A N   1 
ATOM   196  N  N   B ARG A 1 27  ? 22.354 3.293   29.228  0.50 12.12 ? 27  ARG A N   1 
ATOM   197  C  CA  A ARG A 1 27  ? 20.932 3.400   28.795  0.50 13.94 ? 27  ARG A CA  1 
ATOM   198  C  CA  B ARG A 1 27  ? 20.961 3.275   28.834  0.50 13.86 ? 27  ARG A CA  1 
ATOM   199  C  C   A ARG A 1 27  ? 20.961 2.887   27.352  0.50 13.78 ? 27  ARG A C   1 
ATOM   200  C  C   B ARG A 1 27  ? 20.814 2.739   27.416  0.50 12.78 ? 27  ARG A C   1 
ATOM   201  O  O   A ARG A 1 27  ? 20.391 3.561   26.503  0.50 10.50 ? 27  ARG A O   1 
ATOM   202  O  O   B ARG A 1 27  ? 20.032 3.257   26.636  0.50 12.21 ? 27  ARG A O   1 
ATOM   203  C  CB  A ARG A 1 27  ? 19.985 4.614   28.979  0.50 16.27 ? 27  ARG A CB  1 
ATOM   204  C  CB  B ARG A 1 27  ? 20.352 4.672   28.910  0.50 14.59 ? 27  ARG A CB  1 
ATOM   205  C  CG  A ARG A 1 27  ? 20.516 6.031   28.727  0.50 19.09 ? 27  ARG A CG  1 
ATOM   206  C  CG  B ARG A 1 27  ? 20.316 5.241   30.326  0.50 20.71 ? 27  ARG A CG  1 
ATOM   207  C  CD  A ARG A 1 27  ? 19.635 7.314   28.760  0.50 21.83 ? 27  ARG A CD  1 
ATOM   208  C  CD  B ARG A 1 27  ? 19.442 6.462   30.153  0.50 23.87 ? 27  ARG A CD  1 
ATOM   209  N  NE  A ARG A 1 27  ? 18.340 7.177   28.061  0.50 19.69 ? 27  ARG A NE  1 
ATOM   210  N  NE  B ARG A 1 27  ? 20.160 7.640   30.556  0.50 23.98 ? 27  ARG A NE  1 
ATOM   211  C  CZ  A ARG A 1 27  ? 17.537 8.191   27.759  0.50 15.48 ? 27  ARG A CZ  1 
ATOM   212  C  CZ  B ARG A 1 27  ? 20.412 7.973   31.817  0.50 22.91 ? 27  ARG A CZ  1 
ATOM   213  N  NH1 A ARG A 1 27  ? 17.878 9.425   28.086  0.50 9.34  ? 27  ARG A NH1 1 
ATOM   214  N  NH1 B ARG A 1 27  ? 19.992 7.199   32.802  0.50 30.57 ? 27  ARG A NH1 1 
ATOM   215  N  NH2 A ARG A 1 27  ? 16.397 7.967   27.130  0.50 12.43 ? 27  ARG A NH2 1 
ATOM   216  N  NH2 B ARG A 1 27  ? 21.081 9.079   32.087  0.50 27.17 ? 27  ARG A NH2 1 
ATOM   217  N  N   . GLN A 1 28  ? 21.604 1.723   27.070  1.00 11.02 ? 28  GLN A N   1 
ATOM   218  C  CA  . GLN A 1 28  ? 21.639 1.218   25.688  1.00 11.08 ? 28  GLN A CA  1 
ATOM   219  C  C   . GLN A 1 28  ? 20.499 0.242   25.449  1.00 11.30 ? 28  GLN A C   1 
ATOM   220  O  O   . GLN A 1 28  ? 20.029 -0.463  26.311  1.00 12.79 ? 28  GLN A O   1 
ATOM   221  C  CB  . GLN A 1 28  ? 23.003 0.556   25.394  1.00 12.89 ? 28  GLN A CB  1 
ATOM   222  C  CG  . GLN A 1 28  ? 24.127 1.606   25.416  1.00 12.65 ? 28  GLN A CG  1 
ATOM   223  C  CD  . GLN A 1 28  ? 23.953 2.410   24.138  1.00 12.76 ? 28  GLN A CD  1 
ATOM   224  O  OE1 . GLN A 1 28  ? 24.193 1.906   23.027  1.00 12.72 ? 28  GLN A OE1 1 
ATOM   225  N  NE2 . GLN A 1 28  ? 23.639 3.696   24.271  1.00 12.30 ? 28  GLN A NE2 1 
ATOM   226  N  N   . SER A 1 29  ? 20.065 0.221   24.180  1.00 10.30 ? 29  SER A N   1 
ATOM   227  C  CA  . SER A 1 29  ? 18.980 -0.626  23.680  1.00 11.90 ? 29  SER A CA  1 
ATOM   228  C  C   . SER A 1 29  ? 19.511 -1.512  22.584  1.00 11.16 ? 29  SER A C   1 
ATOM   229  O  O   . SER A 1 29  ? 20.458 -1.125  21.881  1.00 11.44 ? 29  SER A O   1 
ATOM   230  C  CB  . SER A 1 29  ? 17.877 0.211   23.102  1.00 12.63 ? 29  SER A CB  1 
ATOM   231  O  OG  . SER A 1 29  ? 17.289 0.971   24.186  1.00 11.95 ? 29  SER A OG  1 
ATOM   232  N  N   . PRO A 1 30  ? 18.873 -2.666  22.303  1.00 10.69 ? 30  PRO A N   1 
ATOM   233  C  CA  . PRO A 1 30  ? 17.668 -3.133  22.965  1.00 10.60 ? 30  PRO A CA  1 
ATOM   234  C  C   . PRO A 1 30  ? 18.095 -3.845  24.247  1.00 9.65  ? 30  PRO A C   1 
ATOM   235  O  O   . PRO A 1 30  ? 19.288 -3.904  24.598  1.00 11.91 ? 30  PRO A O   1 
ATOM   236  C  CB  . PRO A 1 30  ? 17.132 -4.131  21.912  1.00 11.88 ? 30  PRO A CB  1 
ATOM   237  C  CG  . PRO A 1 30  ? 18.395 -4.744  21.316  1.00 12.57 ? 30  PRO A CG  1 
ATOM   238  C  CD  . PRO A 1 30  ? 19.316 -3.549  21.208  1.00 11.44 ? 30  PRO A CD  1 
ATOM   239  N  N   . VAL A 1 31  ? 17.093 -4.391  24.954  1.00 11.56 ? 31  VAL A N   1 
ATOM   240  C  CA  . VAL A 1 31  ? 17.362 -5.173  26.155  1.00 11.72 ? 31  VAL A CA  1 
ATOM   241  C  C   . VAL A 1 31  ? 16.439 -6.395  26.112  1.00 11.41 ? 31  VAL A C   1 
ATOM   242  O  O   . VAL A 1 31  ? 15.452 -6.447  25.334  1.00 11.93 ? 31  VAL A O   1 
ATOM   243  C  CB  . VAL A 1 31  ? 17.032 -4.322  27.395  1.00 12.40 ? 31  VAL A CB  1 
ATOM   244  C  CG1 . VAL A 1 31  ? 17.940 -3.110  27.519  1.00 13.16 ? 31  VAL A CG1 1 
ATOM   245  C  CG2 . VAL A 1 31  ? 15.552 -3.934  27.470  1.00 13.17 ? 31  VAL A CG2 1 
ATOM   246  N  N   . ASP A 1 32  ? 16.752 -7.375  26.936  1.00 12.90 ? 32  ASP A N   1 
ATOM   247  C  CA  . ASP A 1 32  ? 15.841 -8.464  27.211  1.00 13.46 ? 32  ASP A CA  1 
ATOM   248  C  C   . ASP A 1 32  ? 14.791 -7.945  28.195  1.00 13.07 ? 32  ASP A C   1 
ATOM   249  O  O   . ASP A 1 32  ? 15.094 -7.434  29.274  1.00 15.82 ? 32  ASP A O   1 
ATOM   250  C  CB  . ASP A 1 32  ? 16.574 -9.682  27.782  1.00 13.69 ? 32  ASP A CB  1 
ATOM   251  C  CG  . ASP A 1 32  ? 15.614 -10.831 28.063  1.00 17.82 ? 32  ASP A CG  1 
ATOM   252  O  OD1 . ASP A 1 32  ? 14.904 -11.241 27.134  1.00 15.15 ? 32  ASP A OD1 1 
ATOM   253  O  OD2 . ASP A 1 32  ? 15.589 -11.360 29.171  1.00 20.47 ? 32  ASP A OD2 1 
ATOM   254  N  N   . ILE A 1 33  ? 13.518 -8.112  27.854  1.00 12.89 ? 33  ILE A N   1 
ATOM   255  C  CA  . ILE A 1 33  ? 12.415 -7.776  28.737  1.00 12.65 ? 33  ILE A CA  1 
ATOM   256  C  C   . ILE A 1 33  ? 12.002 -9.004  29.512  1.00 15.61 ? 33  ILE A C   1 
ATOM   257  O  O   . ILE A 1 33  ? 11.486 -9.984  28.969  1.00 16.74 ? 33  ILE A O   1 
ATOM   258  C  CB  . ILE A 1 33  ? 11.218 -7.271  27.901  1.00 12.68 ? 33  ILE A CB  1 
ATOM   259  C  CG1 . ILE A 1 33  ? 11.618 -6.028  27.097  1.00 14.65 ? 33  ILE A CG1 1 
ATOM   260  C  CG2 . ILE A 1 33  ? 10.005 -6.989  28.770  1.00 15.46 ? 33  ILE A CG2 1 
ATOM   261  C  CD1 . ILE A 1 33  ? 10.587 -5.716  26.003  1.00 15.06 ? 33  ILE A CD1 1 
ATOM   262  N  N   . ASP A 1 34  ? 12.227 -8.893  30.822  1.00 15.12 ? 34  ASP A N   1 
ATOM   263  C  CA  . ASP A 1 34  ? 11.798 -9.933  31.734  1.00 15.97 ? 34  ASP A CA  1 
ATOM   264  C  C   . ASP A 1 34  ? 10.339 -9.629  32.117  1.00 18.20 ? 34  ASP A C   1 
ATOM   265  O  O   . ASP A 1 34  ? 10.087 -8.651  32.810  1.00 17.39 ? 34  ASP A O   1 
ATOM   266  C  CB  . ASP A 1 34  ? 12.741 -9.974  32.954  1.00 16.79 ? 34  ASP A CB  1 
ATOM   267  C  CG  . ASP A 1 34  ? 12.382 -11.111 33.901  1.00 23.52 ? 34  ASP A CG  1 
ATOM   268  O  OD1 . ASP A 1 34  ? 11.142 -11.356 34.123  1.00 26.02 ? 34  ASP A OD1 1 
ATOM   269  O  OD2 . ASP A 1 34  ? 13.350 -11.746 34.410  1.00 29.99 ? 34  ASP A OD2 1 
ATOM   270  N  N   . THR A 1 35  ? 9.369  -10.402 31.600  1.00 16.32 ? 35  THR A N   1 
ATOM   271  C  CA  . THR A 1 35  ? 7.973  -9.991  31.729  1.00 17.50 ? 35  THR A CA  1 
ATOM   272  C  C   . THR A 1 35  ? 7.507  -10.092 33.182  1.00 17.34 ? 35  THR A C   1 
ATOM   273  O  O   . THR A 1 35  ? 6.549  -9.446  33.576  1.00 19.00 ? 35  THR A O   1 
ATOM   274  C  CB  . THR A 1 35  ? 7.069  -10.757 30.768  1.00 17.63 ? 35  THR A CB  1 
ATOM   275  O  OG1 . THR A 1 35  ? 7.104  -12.128 31.172  1.00 21.60 ? 35  THR A OG1 1 
ATOM   276  C  CG2 . THR A 1 35  ? 7.557  -10.606 29.348  1.00 24.42 ? 35  THR A CG2 1 
ATOM   277  N  N   . HIS A 1 36  ? 8.284  -10.799 34.012  1.00 18.62 ? 36  HIS A N   1 
ATOM   278  C  CA  . HIS A 1 36  ? 7.818  -11.039 35.369  1.00 20.93 ? 36  HIS A CA  1 
ATOM   279  C  C   . HIS A 1 36  ? 8.414  -10.033 36.337  1.00 25.59 ? 36  HIS A C   1 
ATOM   280  O  O   . HIS A 1 36  ? 7.944  -9.929  37.466  1.00 35.07 ? 36  HIS A O   1 
ATOM   281  C  CB  . HIS A 1 36  ? 8.194  -12.490 35.782  1.00 27.02 ? 36  HIS A CB  1 
ATOM   282  C  CG  . HIS A 1 36  ? 7.867  -13.463 34.690  1.00 27.95 ? 36  HIS A CG  1 
ATOM   283  N  ND1 . HIS A 1 36  ? 6.628  -14.108 34.606  1.00 31.49 ? 36  HIS A ND1 1 
ATOM   284  C  CD2 . HIS A 1 36  ? 8.583  -13.871 33.600  1.00 33.89 ? 36  HIS A CD2 1 
ATOM   285  C  CE1 . HIS A 1 36  ? 6.603  -14.881 33.519  1.00 31.96 ? 36  HIS A CE1 1 
ATOM   286  N  NE2 . HIS A 1 36  ? 7.791  -14.765 32.900  1.00 34.06 ? 36  HIS A NE2 1 
ATOM   287  N  N   . THR A 1 37  ? 9.495  -9.357  35.956  1.00 21.35 ? 37  THR A N   1 
ATOM   288  C  CA  . THR A 1 37  ? 10.050 -8.356  36.845  1.00 23.93 ? 37  THR A CA  1 
ATOM   289  C  C   . THR A 1 37  ? 9.688  -6.961  36.362  1.00 19.90 ? 37  THR A C   1 
ATOM   290  O  O   . THR A 1 37  ? 9.947  -6.009  37.107  1.00 25.40 ? 37  THR A O   1 
ATOM   291  C  CB  . THR A 1 37  ? 11.562 -8.494  37.076  1.00 22.72 ? 37  THR A CB  1 
ATOM   292  O  OG1 . THR A 1 37  ? 12.143 -8.438  35.780  1.00 26.59 ? 37  THR A OG1 1 
ATOM   293  C  CG2 . THR A 1 37  ? 11.975 -9.767  37.781  1.00 27.24 ? 37  THR A CG2 1 
ATOM   294  N  N   . ALA A 1 38  ? 9.115  -6.855  35.135  1.00 16.38 ? 38  ALA A N   1 
ATOM   295  C  CA  . ALA A 1 38  ? 8.548  -5.614  34.698  1.00 17.99 ? 38  ALA A CA  1 
ATOM   296  C  C   . ALA A 1 38  ? 7.554  -5.146  35.751  1.00 18.12 ? 38  ALA A C   1 
ATOM   297  O  O   . ALA A 1 38  ? 6.684  -5.876  36.204  1.00 21.45 ? 38  ALA A O   1 
ATOM   298  C  CB  . ALA A 1 38  ? 7.921  -5.724  33.328  1.00 18.97 ? 38  ALA A CB  1 
ATOM   299  N  N   . LYS A 1 39  ? 7.681  -3.870  36.073  1.00 17.55 ? 39  LYS A N   1 
ATOM   300  C  CA  . LYS A 1 39  ? 6.900  -3.303  37.162  1.00 20.65 ? 39  LYS A CA  1 
ATOM   301  C  C   . LYS A 1 39  ? 5.669  -2.597  36.590  1.00 18.62 ? 39  LYS A C   1 
ATOM   302  O  O   . LYS A 1 39  ? 5.788  -1.540  35.951  1.00 17.17 ? 39  LYS A O   1 
ATOM   303  C  CB  . LYS A 1 39  ? 7.774  -2.286  37.914  1.00 24.75 ? 39  LYS A CB  1 
ATOM   304  C  CG  . LYS A 1 39  ? 7.092  -1.452  39.005  1.00 36.26 ? 39  LYS A CG  1 
ATOM   305  N  N   . TYR A 1 40  ? 4.477  -3.067  36.954  1.00 22.45 ? 40  TYR A N   1 
ATOM   306  C  CA  . TYR A 1 40  ? 3.280  -2.298  36.643  1.00 20.00 ? 40  TYR A CA  1 
ATOM   307  C  C   . TYR A 1 40  ? 3.401  -0.921  37.291  1.00 18.54 ? 40  TYR A C   1 
ATOM   308  O  O   . TYR A 1 40  ? 3.714  -0.788  38.480  1.00 20.19 ? 40  TYR A O   1 
ATOM   309  C  CB  . TYR A 1 40  ? 1.996  -3.004  37.093  1.00 23.38 ? 40  TYR A CB  1 
ATOM   310  C  CG  . TYR A 1 40  ? 0.779  -2.133  36.981  1.00 22.80 ? 40  TYR A CG  1 
ATOM   311  C  CD1 . TYR A 1 40  ? 0.291  -1.726  35.740  1.00 24.97 ? 40  TYR A CD1 1 
ATOM   312  C  CD2 . TYR A 1 40  ? 0.095  -1.711  38.119  1.00 27.12 ? 40  TYR A CD2 1 
ATOM   313  C  CE1 . TYR A 1 40  ? -0.812 -0.883  35.641  1.00 28.79 ? 40  TYR A CE1 1 
ATOM   314  C  CE2 . TYR A 1 40  ? -0.999 -0.856  38.043  1.00 30.69 ? 40  TYR A CE2 1 
ATOM   315  C  CZ  . TYR A 1 40  ? -1.482 -0.479  36.796  1.00 22.38 ? 40  TYR A CZ  1 
ATOM   316  O  OH  . TYR A 1 40  ? -2.588 0.332   36.739  1.00 31.90 ? 40  TYR A OH  1 
ATOM   317  N  N   . ASP A 1 41  ? 3.108  0.120   36.525  1.00 17.57 ? 41  ASP A N   1 
ATOM   318  C  CA  . ASP A 1 41  ? 3.183  1.488   37.007  1.00 21.54 ? 41  ASP A CA  1 
ATOM   319  C  C   . ASP A 1 41  ? 1.824  2.159   36.854  1.00 20.90 ? 41  ASP A C   1 
ATOM   320  O  O   . ASP A 1 41  ? 1.424  2.541   35.766  1.00 19.19 ? 41  ASP A O   1 
ATOM   321  C  CB  . ASP A 1 41  ? 4.287  2.310   36.330  1.00 19.50 ? 41  ASP A CB  1 
ATOM   322  C  CG  . ASP A 1 41  ? 4.396  3.765   36.804  1.00 22.47 ? 41  ASP A CG  1 
ATOM   323  O  OD1 . ASP A 1 41  ? 3.625  4.142   37.681  1.00 21.03 ? 41  ASP A OD1 1 
ATOM   324  O  OD2 . ASP A 1 41  ? 5.247  4.517   36.284  1.00 24.46 ? 41  ASP A OD2 1 
ATOM   325  N  N   . PRO A 1 42  ? 1.105  2.355   37.968  1.00 19.70 ? 42  PRO A N   1 
ATOM   326  C  CA  . PRO A 1 42  ? -0.229 2.950   37.902  1.00 22.21 ? 42  PRO A CA  1 
ATOM   327  C  C   . PRO A 1 42  ? -0.260 4.413   37.455  1.00 22.92 ? 42  PRO A C   1 
ATOM   328  O  O   . PRO A 1 42  ? -1.321 4.919   37.084  1.00 25.22 ? 42  PRO A O   1 
ATOM   329  C  CB  . PRO A 1 42  ? -0.816 2.749   39.313  1.00 27.53 ? 42  PRO A CB  1 
ATOM   330  C  CG  . PRO A 1 42  ? 0.345  2.286   40.206  1.00 26.35 ? 42  PRO A CG  1 
ATOM   331  C  CD  . PRO A 1 42  ? 1.573  2.088   39.353  1.00 22.64 ? 42  PRO A CD  1 
ATOM   332  N  N   A SER A 1 43  ? 0.897  5.084   37.481  0.50 22.22 ? 43  SER A N   1 
ATOM   333  N  N   B SER A 1 43  ? 0.914  5.057   37.457  0.50 19.22 ? 43  SER A N   1 
ATOM   334  C  CA  A SER A 1 43  ? 0.967  6.485   37.091  0.50 23.34 ? 43  SER A CA  1 
ATOM   335  C  CA  B SER A 1 43  ? 1.087  6.452   37.070  0.50 20.76 ? 43  SER A CA  1 
ATOM   336  C  C   A SER A 1 43  ? 1.109  6.649   35.578  0.50 23.60 ? 43  SER A C   1 
ATOM   337  C  C   B SER A 1 43  ? 1.032  6.629   35.564  0.50 21.62 ? 43  SER A C   1 
ATOM   338  O  O   A SER A 1 43  ? 1.065  7.788   35.099  0.50 27.56 ? 43  SER A O   1 
ATOM   339  O  O   B SER A 1 43  ? 0.847  7.755   35.089  0.50 26.37 ? 43  SER A O   1 
ATOM   340  C  CB  A SER A 1 43  ? 2.070  7.228   37.815  0.50 31.54 ? 43  SER A CB  1 
ATOM   341  C  CB  B SER A 1 43  ? 2.408  6.983   37.530  0.50 18.44 ? 43  SER A CB  1 
ATOM   342  O  OG  A SER A 1 43  ? 3.309  7.097   37.129  0.50 30.59 ? 43  SER A OG  1 
ATOM   343  O  OG  B SER A 1 43  ? 2.405  7.060   38.945  0.50 19.32 ? 43  SER A OG  1 
ATOM   344  N  N   . LEU A 1 44  ? 1.300  5.544   34.826  1.00 23.53 ? 44  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 44  ? 1.310  5.662   33.369  1.00 20.12 ? 44  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 44  ? -0.074 6.122   32.918  1.00 21.41 ? 44  LEU A C   1 
ATOM   347  O  O   . LEU A 1 44  ? -1.096 5.599   33.395  1.00 26.60 ? 44  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 44  ? 1.691  4.313   32.735  1.00 20.39 ? 44  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 44  ? 3.131  3.855   33.017  1.00 17.88 ? 44  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 44  ? 3.321  2.392   32.621  1.00 23.14 ? 44  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 44  ? 4.129  4.767   32.318  1.00 18.71 ? 44  LEU A CD2 1 
ATOM   352  N  N   . LYS A 1 45  ? -0.112 7.094   31.982  1.00 22.06 ? 45  LYS A N   1 
ATOM   353  C  CA  . LYS A 1 45  ? -1.402 7.579   31.503  1.00 24.17 ? 45  LYS A CA  1 
ATOM   354  C  C   . LYS A 1 45  ? -1.829 6.662   30.356  1.00 26.25 ? 45  LYS A C   1 
ATOM   355  O  O   . LYS A 1 45  ? -1.006 5.936   29.797  1.00 22.12 ? 45  LYS A O   1 
ATOM   356  C  CB  . LYS A 1 45  ? -1.339 9.036   31.006  1.00 27.14 ? 45  LYS A CB  1 
ATOM   357  C  CG  . LYS A 1 45  ? -0.816 10.092  31.977  1.00 32.25 ? 45  LYS A CG  1 
ATOM   358  N  N   . PRO A 1 46  ? -3.106 6.685   29.912  1.00 24.07 ? 46  PRO A N   1 
ATOM   359  C  CA  . PRO A 1 46  ? -3.486 5.903   28.731  1.00 25.88 ? 46  PRO A CA  1 
ATOM   360  C  C   . PRO A 1 46  ? -2.594 6.272   27.528  1.00 21.93 ? 46  PRO A C   1 
ATOM   361  O  O   . PRO A 1 46  ? -2.312 7.452   27.298  1.00 21.72 ? 46  PRO A O   1 
ATOM   362  C  CB  . PRO A 1 46  ? -4.973 6.280   28.542  1.00 25.85 ? 46  PRO A CB  1 
ATOM   363  C  CG  . PRO A 1 46  ? -5.414 6.659   29.981  1.00 27.34 ? 46  PRO A CG  1 
ATOM   364  C  CD  . PRO A 1 46  ? -4.217 7.409   30.544  1.00 24.66 ? 46  PRO A CD  1 
ATOM   365  N  N   . LEU A 1 47  ? -2.114 5.260   26.798  1.00 18.34 ? 47  LEU A N   1 
ATOM   366  C  CA  . LEU A 1 47  ? -1.365 5.440   25.545  1.00 19.96 ? 47  LEU A CA  1 
ATOM   367  C  C   . LEU A 1 47  ? -2.280 5.731   24.362  1.00 20.35 ? 47  LEU A C   1 
ATOM   368  O  O   . LEU A 1 47  ? -3.231 4.994   24.081  1.00 23.28 ? 47  LEU A O   1 
ATOM   369  C  CB  . LEU A 1 47  ? -0.582 4.186   25.188  1.00 25.00 ? 47  LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 47  ? 0.430  4.378   24.061  1.00 24.70 ? 47  LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 47  ? 1.595  5.232   24.546  1.00 23.51 ? 47  LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 47  ? 0.939  3.038   23.562  1.00 26.83 ? 47  LEU A CD2 1 
ATOM   373  N  N   . SER A 1 48  ? -1.926 6.809   23.667  1.00 14.73 ? 48  SER A N   1 
ATOM   374  C  CA  . SER A 1 48  ? -2.750 7.280   22.552  1.00 13.21 ? 48  SER A CA  1 
ATOM   375  C  C   . SER A 1 48  ? -1.937 7.259   21.253  1.00 14.50 ? 48  SER A C   1 
ATOM   376  O  O   . SER A 1 48  ? -0.938 7.966   21.139  1.00 15.00 ? 48  SER A O   1 
ATOM   377  C  CB  . SER A 1 48  ? -3.129 8.713   22.906  1.00 20.35 ? 48  SER A CB  1 
ATOM   378  O  OG  . SER A 1 48  ? -3.763 9.353   21.836  1.00 26.56 ? 48  SER A OG  1 
ATOM   379  N  N   . VAL A 1 49  ? -2.355 6.405   20.309  1.00 16.81 ? 49  VAL A N   1 
ATOM   380  C  CA  . VAL A 1 49  ? -1.738 6.323   18.987  1.00 17.64 ? 49  VAL A CA  1 
ATOM   381  C  C   . VAL A 1 49  ? -2.765 6.847   17.999  1.00 15.86 ? 49  VAL A C   1 
ATOM   382  O  O   . VAL A 1 49  ? -3.807 6.220   17.815  1.00 25.09 ? 49  VAL A O   1 
ATOM   383  C  CB  . VAL A 1 49  ? -1.404 4.848   18.679  1.00 18.53 ? 49  VAL A CB  1 
ATOM   384  C  CG1 . VAL A 1 49  ? -0.725 4.692   17.329  1.00 24.71 ? 49  VAL A CG1 1 
ATOM   385  C  CG2 . VAL A 1 49  ? -0.662 4.153   19.819  1.00 21.96 ? 49  VAL A CG2 1 
ATOM   386  N  N   . SER A 1 50  ? -2.507 8.057   17.482  1.00 16.56 ? 50  SER A N   1 
ATOM   387  C  CA  . SER A 1 50  ? -3.457 8.717   16.605  1.00 16.79 ? 50  SER A CA  1 
ATOM   388  C  C   . SER A 1 50  ? -2.856 8.868   15.212  1.00 16.03 ? 50  SER A C   1 
ATOM   389  O  O   . SER A 1 50  ? -2.159 9.862   14.945  1.00 16.27 ? 50  SER A O   1 
ATOM   390  C  CB  . SER A 1 50  ? -3.829 10.102  17.096  1.00 20.48 ? 50  SER A CB  1 
ATOM   391  O  OG  . SER A 1 50  ? -4.394 9.998   18.383  1.00 28.03 ? 50  SER A OG  1 
ATOM   392  N  N   . TYR A 1 51  ? -3.092 7.844   14.396  1.00 16.85 ? 51  TYR A N   1 
ATOM   393  C  CA  . TYR A 1 51  ? -2.480 7.711   13.072  1.00 16.95 ? 51  TYR A CA  1 
ATOM   394  C  C   . TYR A 1 51  ? -3.450 8.004   11.928  1.00 17.68 ? 51  TYR A C   1 
ATOM   395  O  O   . TYR A 1 51  ? -3.027 7.866   10.779  1.00 18.46 ? 51  TYR A O   1 
ATOM   396  C  CB  . TYR A 1 51  ? -1.877 6.314   12.909  1.00 16.04 ? 51  TYR A CB  1 
ATOM   397  C  CG  . TYR A 1 51  ? -0.602 6.050   13.687  1.00 14.83 ? 51  TYR A CG  1 
ATOM   398  C  CD1 . TYR A 1 51  ? 0.045  7.069   14.366  1.00 14.33 ? 51  TYR A CD1 1 
ATOM   399  C  CD2 . TYR A 1 51  ? -0.047 4.782   13.742  1.00 15.19 ? 51  TYR A CD2 1 
ATOM   400  C  CE1 . TYR A 1 51  ? 1.210  6.837   15.079  1.00 14.66 ? 51  TYR A CE1 1 
ATOM   401  C  CE2 . TYR A 1 51  ? 1.117  4.533   14.450  1.00 16.19 ? 51  TYR A CE2 1 
ATOM   402  C  CZ  . TYR A 1 51  ? 1.748  5.564   15.121  1.00 13.95 ? 51  TYR A CZ  1 
ATOM   403  O  OH  . TYR A 1 51  ? 2.896  5.327   15.821  1.00 14.74 ? 51  TYR A OH  1 
ATOM   404  N  N   . ASP A 1 52  ? -4.667 8.486   12.196  1.00 17.24 ? 52  ASP A N   1 
ATOM   405  C  CA  . ASP A 1 52  ? -5.645 8.641   11.130  1.00 17.71 ? 52  ASP A CA  1 
ATOM   406  C  C   . ASP A 1 52  ? -5.236 9.638   10.041  1.00 21.54 ? 52  ASP A C   1 
ATOM   407  O  O   . ASP A 1 52  ? -5.709 9.515   8.882   1.00 23.48 ? 52  ASP A O   1 
ATOM   408  C  CB  . ASP A 1 52  ? -7.004 8.996   11.740  1.00 22.36 ? 52  ASP A CB  1 
ATOM   409  C  CG  . ASP A 1 52  ? -6.982 10.135  12.753  1.00 37.79 ? 52  ASP A CG  1 
ATOM   410  O  OD1 . ASP A 1 52  ? -6.257 10.003  13.808  1.00 48.22 ? 52  ASP A OD1 1 
ATOM   411  O  OD2 . ASP A 1 52  ? -7.710 11.150  12.499  1.00 45.31 ? 52  ASP A OD2 1 
ATOM   412  N  N   . GLN A 1 53  ? -4.413 10.647  10.389  1.00 20.39 ? 53  GLN A N   1 
ATOM   413  C  CA  . GLN A 1 53  ? -4.041 11.610  9.341   1.00 16.40 ? 53  GLN A CA  1 
ATOM   414  C  C   . GLN A 1 53  ? -2.582 11.375  8.863   1.00 14.33 ? 53  GLN A C   1 
ATOM   415  O  O   . GLN A 1 53  ? -1.996 12.214  8.169   1.00 17.70 ? 53  GLN A O   1 
ATOM   416  C  CB  . GLN A 1 53  ? -4.285 13.069  9.758   1.00 22.59 ? 53  GLN A CB  1 
ATOM   417  C  CG  . GLN A 1 53  ? -5.750 13.462  10.033  1.00 21.85 ? 53  GLN A CG  1 
ATOM   418  C  CD  . GLN A 1 53  ? -6.628 13.396  8.813   1.00 23.73 ? 53  GLN A CD  1 
ATOM   419  O  OE1 . GLN A 1 53  ? -7.745 12.881  8.825   1.00 44.98 ? 53  GLN A OE1 1 
ATOM   420  N  NE2 . GLN A 1 53  ? -6.077 13.839  7.683   1.00 31.31 ? 53  GLN A NE2 1 
ATOM   421  N  N   . ALA A 1 54  ? -2.031 10.177  9.105   1.00 14.49 ? 54  ALA A N   1 
ATOM   422  C  CA  . ALA A 1 54  ? -0.653 9.930   8.695   1.00 13.53 ? 54  ALA A CA  1 
ATOM   423  C  C   . ALA A 1 54  ? -0.482 10.037  7.177   1.00 13.59 ? 54  ALA A C   1 
ATOM   424  O  O   . ALA A 1 54  ? -1.381 9.620   6.432   1.00 16.35 ? 54  ALA A O   1 
ATOM   425  C  CB  . ALA A 1 54  ? -0.183 8.584   9.129   1.00 14.19 ? 54  ALA A CB  1 
ATOM   426  N  N   . THR A 1 55  ? 0.628  10.649  6.754   1.00 11.36 ? 55  THR A N   1 
ATOM   427  C  CA  . THR A 1 55  ? 0.934  10.845  5.348   1.00 11.96 ? 55  THR A CA  1 
ATOM   428  C  C   . THR A 1 55  ? 2.297  10.234  5.042   1.00 11.75 ? 55  THR A C   1 
ATOM   429  O  O   . THR A 1 55  ? 3.334  10.854  5.285   1.00 12.97 ? 55  THR A O   1 
ATOM   430  C  CB  . THR A 1 55  ? 1.019  12.337  5.007   1.00 13.92 ? 55  THR A CB  1 
ATOM   431  O  OG1 . THR A 1 55  ? -0.277 12.904  5.160   1.00 18.33 ? 55  THR A OG1 1 
ATOM   432  C  CG2 . THR A 1 55  ? 1.435  12.573  3.564   1.00 16.60 ? 55  THR A CG2 1 
ATOM   433  N  N   . SER A 1 56  ? 2.299  8.998   4.531   1.00 10.92 ? 56  SER A N   1 
ATOM   434  C  CA  . SER A 1 56  ? 3.561  8.403   4.096   1.00 10.79 ? 56  SER A CA  1 
ATOM   435  C  C   . SER A 1 56  ? 3.999  9.088   2.808   1.00 11.41 ? 56  SER A C   1 
ATOM   436  O  O   . SER A 1 56  ? 3.139  9.568   2.009   1.00 12.99 ? 56  SER A O   1 
ATOM   437  C  CB  . SER A 1 56  ? 3.434  6.896   3.931   1.00 11.05 ? 56  SER A CB  1 
ATOM   438  O  OG  . SER A 1 56  ? 2.569  6.582   2.838   1.00 11.87 ? 56  SER A OG  1 
ATOM   439  N  N   . LEU A 1 57  ? 5.315  9.110   2.571   1.00 12.26 ? 57  LEU A N   1 
ATOM   440  C  CA  . LEU A 1 57  ? 5.855  9.782   1.406   1.00 13.54 ? 57  LEU A CA  1 
ATOM   441  C  C   . LEU A 1 57  ? 6.666  8.847   0.539   1.00 12.13 ? 57  LEU A C   1 
ATOM   442  O  O   . LEU A 1 57  ? 6.465  8.807   -0.669  1.00 16.15 ? 57  LEU A O   1 
ATOM   443  C  CB  . LEU A 1 57  ? 6.654  11.016  1.790   1.00 14.94 ? 57  LEU A CB  1 
ATOM   444  C  CG  . LEU A 1 57  ? 5.826  12.174  2.370   1.00 16.77 ? 57  LEU A CG  1 
ATOM   445  C  CD1 . LEU A 1 57  ? 6.751  13.256  2.933   1.00 20.81 ? 57  LEU A CD1 1 
ATOM   446  C  CD2 . LEU A 1 57  ? 4.783  12.694  1.367   1.00 18.38 ? 57  LEU A CD2 1 
ATOM   447  N  N   . ARG A 1 58  ? 7.644  8.161   1.084   1.00 12.74 ? 58  ARG A N   1 
ATOM   448  C  CA  . ARG A 1 58  ? 8.639  7.452   0.296   1.00 13.18 ? 58  ARG A CA  1 
ATOM   449  C  C   . ARG A 1 58  ? 9.128  6.218   1.050   1.00 10.77 ? 58  ARG A C   1 
ATOM   450  O  O   . ARG A 1 58  ? 9.018  6.184   2.280   1.00 12.28 ? 58  ARG A O   1 
ATOM   451  C  CB  . ARG A 1 58  ? 9.898  8.309   0.163   1.00 20.58 ? 58  ARG A CB  1 
ATOM   452  C  CG  . ARG A 1 58  ? 9.685  9.590   -0.628  1.00 27.56 ? 58  ARG A CG  1 
ATOM   453  C  CD  . ARG A 1 58  ? 11.017 10.160  -1.086  1.00 30.22 ? 58  ARG A CD  1 
ATOM   454  N  NE  . ARG A 1 58  ? 11.677 9.328   -2.093  1.00 34.50 ? 58  ARG A NE  1 
ATOM   455  C  CZ  . ARG A 1 58  ? 11.298 9.227   -3.373  1.00 40.09 ? 58  ARG A CZ  1 
ATOM   456  N  NH1 . ARG A 1 58  ? 10.260 9.926   -3.816  1.00 43.84 ? 58  ARG A NH1 1 
ATOM   457  N  NH2 . ARG A 1 58  ? 11.974 8.448   -4.207  1.00 32.17 ? 58  ARG A NH2 1 
ATOM   458  N  N   . ILE A 1 59  ? 9.676  5.271   0.360   1.00 11.72 ? 59  ILE A N   1 
ATOM   459  C  CA  . ILE A 1 59  ? 10.282 4.110   0.953   1.00 11.18 ? 59  ILE A CA  1 
ATOM   460  C  C   . ILE A 1 59  ? 11.670 4.011   0.390   1.00 11.13 ? 59  ILE A C   1 
ATOM   461  O  O   . ILE A 1 59  ? 11.873 4.209   -0.800  1.00 11.42 ? 59  ILE A O   1 
ATOM   462  C  CB  . ILE A 1 59  ? 9.457  2.834   0.702   1.00 10.78 ? 59  ILE A CB  1 
ATOM   463  C  CG1 . ILE A 1 59  ? 9.964  1.667   1.534   1.00 13.45 ? 59  ILE A CG1 1 
ATOM   464  C  CG2 . ILE A 1 59  ? 9.340  2.479   -0.770  1.00 11.28 ? 59  ILE A CG2 1 
ATOM   465  C  CD1 . ILE A 1 59  ? 9.012  0.518   1.567   1.00 13.32 ? 59  ILE A CD1 1 
ATOM   466  N  N   . LEU A 1 60  ? 12.667 3.706   1.189   1.00 11.19 ? 60  LEU A N   1 
ATOM   467  C  CA  . LEU A 1 60  ? 14.028 3.689   0.689   1.00 11.99 ? 60  LEU A CA  1 
ATOM   468  C  C   . LEU A 1 60  ? 14.848 2.597   1.353   1.00 11.65 ? 60  LEU A C   1 
ATOM   469  O  O   . LEU A 1 60  ? 14.619 2.218   2.519   1.00 12.62 ? 60  LEU A O   1 
ATOM   470  C  CB  . LEU A 1 60  ? 14.690 5.038   0.864   1.00 13.45 ? 60  LEU A CB  1 
ATOM   471  C  CG  . LEU A 1 60  ? 14.802 5.454   2.338   1.00 15.39 ? 60  LEU A CG  1 
ATOM   472  C  CD1 . LEU A 1 60  ? 16.228 5.662   2.767   1.00 26.65 ? 60  LEU A CD1 1 
ATOM   473  C  CD2 . LEU A 1 60  ? 13.974 6.705   2.523   1.00 23.71 ? 60  LEU A CD2 1 
ATOM   474  N  N   . ASN A 1 61  ? 15.830 2.111   0.630   1.00 10.93 ? 61  ASN A N   1 
ATOM   475  C  CA  . ASN A 1 61  ? 16.833 1.181   1.163   1.00 11.75 ? 61  ASN A CA  1 
ATOM   476  C  C   . ASN A 1 61  ? 18.101 1.988   1.447   1.00 11.28 ? 61  ASN A C   1 
ATOM   477  O  O   . ASN A 1 61  ? 18.695 2.557   0.537   1.00 13.69 ? 61  ASN A O   1 
ATOM   478  C  CB  . ASN A 1 61  ? 17.189 0.142   0.078   1.00 11.15 ? 61  ASN A CB  1 
ATOM   479  C  CG  . ASN A 1 61  ? 18.236 -0.850  0.497   1.00 12.20 ? 61  ASN A CG  1 
ATOM   480  O  OD1 . ASN A 1 61  ? 19.125 -0.496  1.277   1.00 13.59 ? 61  ASN A OD1 1 
ATOM   481  N  ND2 . ASN A 1 61  ? 18.190 -2.066  -0.044  1.00 12.31 ? 61  ASN A ND2 1 
ATOM   482  N  N   . ASN A 1 62  ? 18.465 2.135   2.728   1.00 12.59 ? 62  ASN A N   1 
ATOM   483  C  CA  . ASN A 1 62  ? 19.608 2.968   3.120   1.00 14.28 ? 62  ASN A CA  1 
ATOM   484  C  C   . ASN A 1 62  ? 20.897 2.167   3.315   1.00 12.33 ? 62  ASN A C   1 
ATOM   485  O  O   . ASN A 1 62  ? 21.876 2.715   3.821   1.00 17.24 ? 62  ASN A O   1 
ATOM   486  C  CB  . ASN A 1 62  ? 19.303 3.831   4.339   1.00 16.61 ? 62  ASN A CB  1 
ATOM   487  C  CG  . ASN A 1 62  ? 19.420 3.083   5.633   1.00 19.16 ? 62  ASN A CG  1 
ATOM   488  O  OD1 . ASN A 1 62  ? 19.306 1.858   5.683   1.00 18.25 ? 62  ASN A OD1 1 
ATOM   489  N  ND2 . ASN A 1 62  ? 19.715 3.836   6.674   1.00 26.84 ? 62  ASN A ND2 1 
ATOM   490  N  N   . GLY A 1 63  ? 20.895 0.862   2.948   1.00 12.97 ? 63  GLY A N   1 
ATOM   491  C  CA  . GLY A 1 63  ? 22.089 0.057   3.075   1.00 13.25 ? 63  GLY A CA  1 
ATOM   492  C  C   . GLY A 1 63  ? 22.177 -0.675  4.412   1.00 14.36 ? 63  GLY A C   1 
ATOM   493  O  O   . GLY A 1 63  ? 23.055 -1.528  4.559   1.00 18.05 ? 63  GLY A O   1 
ATOM   494  N  N   . HIS A 1 64  ? 21.232 -0.393  5.316   1.00 13.50 ? 64  HIS A N   1 
ATOM   495  C  CA  . HIS A 1 64  ? 21.191 -1.007  6.642   1.00 14.75 ? 64  HIS A CA  1 
ATOM   496  C  C   . HIS A 1 64  ? 19.817 -1.667  6.858   1.00 15.31 ? 64  HIS A C   1 
ATOM   497  O  O   . HIS A 1 64  ? 19.729 -2.741  7.450   1.00 17.49 ? 64  HIS A O   1 
ATOM   498  C  CB  . HIS A 1 64  ? 21.568 -0.040  7.784   1.00 16.99 ? 64  HIS A CB  1 
ATOM   499  C  CG  . HIS A 1 64  ? 22.905 0.617   7.626   1.00 20.18 ? 64  HIS A CG  1 
ATOM   500  N  ND1 . HIS A 1 64  ? 24.103 -0.075  7.838   1.00 25.02 ? 64  HIS A ND1 1 
ATOM   501  C  CD2 . HIS A 1 64  ? 23.254 1.901   7.350   1.00 24.59 ? 64  HIS A CD2 1 
ATOM   502  C  CE1 . HIS A 1 64  ? 25.120 0.737   7.682   1.00 23.77 ? 64  HIS A CE1 1 
ATOM   503  N  NE2 . HIS A 1 64  ? 24.633 1.965   7.351   1.00 29.95 ? 64  HIS A NE2 1 
ATOM   504  N  N   . SER A 1 65  ? 18.760 -0.997  6.377   1.00 12.25 ? 65  SER A N   1 
ATOM   505  C  CA  . SER A 1 65  ? 17.412 -1.516  6.422   1.00 12.48 ? 65  SER A CA  1 
ATOM   506  C  C   . SER A 1 65  ? 16.641 -0.803  5.341   1.00 13.25 ? 65  SER A C   1 
ATOM   507  O  O   . SER A 1 65  ? 17.251 -0.108  4.523   1.00 14.13 ? 65  SER A O   1 
ATOM   508  C  CB  . SER A 1 65  ? 16.760 -1.271  7.779   1.00 14.21 ? 65  SER A CB  1 
ATOM   509  O  OG  . SER A 1 65  ? 15.620 -2.106  7.877   1.00 20.27 ? 65  SER A OG  1 
ATOM   510  N  N   . PHE A 1 66  ? 15.319 -0.979  5.360   1.00 12.33 ? 66  PHE A N   1 
ATOM   511  C  CA  . PHE A 1 66  ? 14.502 -0.044  4.602   1.00 11.47 ? 66  PHE A CA  1 
ATOM   512  C  C   . PHE A 1 66  ? 13.636 0.757   5.553   1.00 12.01 ? 66  PHE A C   1 
ATOM   513  O  O   . PHE A 1 66  ? 13.290 0.294   6.657   1.00 13.08 ? 66  PHE A O   1 
ATOM   514  C  CB  . PHE A 1 66  ? 13.680 -0.762  3.541   1.00 13.83 ? 66  PHE A CB  1 
ATOM   515  C  CG  . PHE A 1 66  ? 12.562 -1.595  4.083   1.00 11.49 ? 66  PHE A CG  1 
ATOM   516  C  CD1 . PHE A 1 66  ? 11.306 -1.025  4.302   1.00 12.31 ? 66  PHE A CD1 1 
ATOM   517  C  CD2 . PHE A 1 66  ? 12.714 -2.951  4.388   1.00 12.49 ? 66  PHE A CD2 1 
ATOM   518  C  CE1 . PHE A 1 66  ? 10.244 -1.793  4.767   1.00 12.18 ? 66  PHE A CE1 1 
ATOM   519  C  CE2 . PHE A 1 66  ? 11.664 -3.708  4.889   1.00 13.31 ? 66  PHE A CE2 1 
ATOM   520  C  CZ  . PHE A 1 66  ? 10.403 -3.137  5.054   1.00 12.99 ? 66  PHE A CZ  1 
ATOM   521  N  N   . LYS A 1 67  ? 13.304 1.960   5.108   1.00 11.93 ? 67  LYS A N   1 
ATOM   522  C  CA  . LYS A 1 67  ? 12.450 2.766   5.936   1.00 11.98 ? 67  LYS A CA  1 
ATOM   523  C  C   . LYS A 1 67  ? 11.374 3.433   5.112   1.00 9.75  ? 67  LYS A C   1 
ATOM   524  O  O   . LYS A 1 67  ? 11.567 3.730   3.911   1.00 11.21 ? 67  LYS A O   1 
ATOM   525  C  CB  . LYS A 1 67  ? 13.162 3.741   6.853   1.00 19.43 ? 67  LYS A CB  1 
ATOM   526  C  CG  . LYS A 1 67  ? 13.701 4.959   6.180   1.00 21.05 ? 67  LYS A CG  1 
ATOM   527  C  CD  . LYS A 1 67  ? 14.283 5.970   7.134   1.00 21.51 ? 67  LYS A CD  1 
ATOM   528  C  CE  . LYS A 1 67  ? 15.296 6.797   6.355   1.00 25.13 ? 67  LYS A CE  1 
ATOM   529  N  NZ  . LYS A 1 67  ? 15.568 8.087   6.997   1.00 24.60 ? 67  LYS A NZ  1 
ATOM   530  N  N   . VAL A 1 68  ? 10.221 3.630   5.716   1.00 10.75 ? 68  VAL A N   1 
ATOM   531  C  CA  . VAL A 1 68  ? 9.128  4.425   5.128   1.00 11.20 ? 68  VAL A CA  1 
ATOM   532  C  C   . VAL A 1 68  ? 9.179  5.775   5.835   1.00 10.08 ? 68  VAL A C   1 
ATOM   533  O  O   . VAL A 1 68  ? 9.025  5.816   7.073   1.00 11.15 ? 68  VAL A O   1 
ATOM   534  C  CB  . VAL A 1 68  ? 7.784  3.726   5.333   1.00 11.30 ? 68  VAL A CB  1 
ATOM   535  C  CG1 . VAL A 1 68  ? 6.601  4.627   4.860   1.00 12.26 ? 68  VAL A CG1 1 
ATOM   536  C  CG2 . VAL A 1 68  ? 7.747  2.399   4.520   1.00 12.18 ? 68  VAL A CG2 1 
ATOM   537  N  N   . GLU A 1 69  ? 9.281  6.879   5.104   1.00 10.67 ? 69  GLU A N   1 
ATOM   538  C  CA  . GLU A 1 69  ? 9.336  8.236   5.579   1.00 11.78 ? 69  GLU A CA  1 
ATOM   539  C  C   . GLU A 1 69  ? 7.945  8.833   5.540   1.00 10.69 ? 69  GLU A C   1 
ATOM   540  O  O   . GLU A 1 69  ? 7.247  8.639   4.532   1.00 11.71 ? 69  GLU A O   1 
ATOM   541  C  CB  . GLU A 1 69  ? 10.203 9.108   4.661   1.00 15.09 ? 69  GLU A CB  1 
ATOM   542  C  CG  . GLU A 1 69  ? 11.687 8.791   4.765   1.00 17.14 ? 69  GLU A CG  1 
ATOM   543  C  CD  . GLU A 1 69  ? 12.309 9.483   5.982   1.00 19.30 ? 69  GLU A CD  1 
ATOM   544  O  OE1 . GLU A 1 69  ? 13.502 9.778   5.958   1.00 23.25 ? 69  GLU A OE1 1 
ATOM   545  O  OE2 . GLU A 1 69  ? 11.607 9.676   6.988   1.00 29.45 ? 69  GLU A OE2 1 
ATOM   546  N  N   . PHE A 1 70  ? 7.532  9.539   6.577   1.00 11.86 ? 70  PHE A N   1 
ATOM   547  C  CA  . PHE A 1 70  ? 6.279  10.247  6.623   1.00 10.19 ? 70  PHE A CA  1 
ATOM   548  C  C   . PHE A 1 70  ? 6.504  11.757  6.576   1.00 11.30 ? 70  PHE A C   1 
ATOM   549  O  O   . PHE A 1 70  ? 7.561  12.294  6.929   1.00 13.52 ? 70  PHE A O   1 
ATOM   550  C  CB  . PHE A 1 70  ? 5.607  9.921   7.960   1.00 11.24 ? 70  PHE A CB  1 
ATOM   551  C  CG  . PHE A 1 70  ? 4.978  8.563   7.950   1.00 10.69 ? 70  PHE A CG  1 
ATOM   552  C  CD1 . PHE A 1 70  ? 5.751  7.427   8.161   1.00 13.79 ? 70  PHE A CD1 1 
ATOM   553  C  CD2 . PHE A 1 70  ? 3.618  8.399   7.700   1.00 11.34 ? 70  PHE A CD2 1 
ATOM   554  C  CE1 . PHE A 1 70  ? 5.230  6.155   8.040   1.00 14.13 ? 70  PHE A CE1 1 
ATOM   555  C  CE2 . PHE A 1 70  ? 3.091  7.125   7.591   1.00 12.25 ? 70  PHE A CE2 1 
ATOM   556  C  CZ  . PHE A 1 70  ? 3.882  6.003   7.759   1.00 13.85 ? 70  PHE A CZ  1 
ATOM   557  N  N   . ASP A 1 71  ? 5.473  12.473  6.149   1.00 12.89 ? 71  ASP A N   1 
ATOM   558  C  CA  . ASP A 1 71  ? 5.456  13.920  6.249   1.00 12.75 ? 71  ASP A CA  1 
ATOM   559  C  C   . ASP A 1 71  ? 5.141  14.297  7.679   1.00 15.01 ? 71  ASP A C   1 
ATOM   560  O  O   . ASP A 1 71  ? 4.009  14.162  8.126   1.00 20.69 ? 71  ASP A O   1 
ATOM   561  C  CB  . ASP A 1 71  ? 4.405  14.473  5.315   1.00 16.33 ? 71  ASP A CB  1 
ATOM   562  C  CG  . ASP A 1 71  ? 4.326  15.991  5.315   1.00 20.46 ? 71  ASP A CG  1 
ATOM   563  O  OD1 . ASP A 1 71  ? 4.985  16.649  6.101   1.00 18.85 ? 71  ASP A OD1 1 
ATOM   564  O  OD2 . ASP A 1 71  ? 3.499  16.489  4.570   1.00 27.24 ? 71  ASP A OD2 1 
ATOM   565  N  N   . ASP A 1 72  ? 6.192  14.717  8.379   1.00 14.02 ? 72  ASP A N   1 
ATOM   566  C  CA  . ASP A 1 72  ? 6.033  15.069  9.792   1.00 12.64 ? 72  ASP A CA  1 
ATOM   567  C  C   . ASP A 1 72  ? 6.055  16.588  9.964   1.00 13.85 ? 72  ASP A C   1 
ATOM   568  O  O   . ASP A 1 72  ? 6.465  17.132  11.028  1.00 15.30 ? 72  ASP A O   1 
ATOM   569  C  CB  . ASP A 1 72  ? 7.111  14.407  10.656  1.00 14.44 ? 72  ASP A CB  1 
ATOM   570  C  CG  . ASP A 1 72  ? 8.525  14.708  10.197  1.00 14.83 ? 72  ASP A CG  1 
ATOM   571  O  OD1 . ASP A 1 72  ? 8.689  15.471  9.212   1.00 19.40 ? 72  ASP A OD1 1 
ATOM   572  O  OD2 . ASP A 1 72  ? 9.491  14.244  10.859  1.00 15.33 ? 72  ASP A OD2 1 
ATOM   573  N  N   . SER A 1 73  ? 5.689  17.320  8.928   1.00 16.35 ? 73  SER A N   1 
ATOM   574  C  CA  . SER A 1 73  ? 5.751  18.784  9.007   1.00 15.52 ? 73  SER A CA  1 
ATOM   575  C  C   . SER A 1 73  ? 4.466  19.383  9.583   1.00 16.70 ? 73  SER A C   1 
ATOM   576  O  O   . SER A 1 73  ? 4.326  20.605  9.668   1.00 18.36 ? 73  SER A O   1 
ATOM   577  C  CB  . SER A 1 73  ? 6.051  19.362  7.654   1.00 18.23 ? 73  SER A CB  1 
ATOM   578  O  OG  . SER A 1 73  ? 4.925  19.249  6.789   1.00 20.63 ? 73  SER A OG  1 
ATOM   579  N  N   . GLN A 1 74  ? 3.504  18.506  9.906   1.00 21.00 ? 74  GLN A N   1 
ATOM   580  C  CA  . GLN A 1 74  ? 2.274  18.947  10.531  1.00 22.32 ? 74  GLN A CA  1 
ATOM   581  C  C   . GLN A 1 74  ? 1.910  17.994  11.641  1.00 18.04 ? 74  GLN A C   1 
ATOM   582  O  O   . GLN A 1 74  ? 2.433  16.871  11.706  1.00 17.91 ? 74  GLN A O   1 
ATOM   583  C  CB  . GLN A 1 74  ? 1.107  18.861  9.552   1.00 27.94 ? 74  GLN A CB  1 
ATOM   584  C  CG  . GLN A 1 74  ? 1.021  20.081  8.664   1.00 36.97 ? 74  GLN A CG  1 
ATOM   585  C  CD  . GLN A 1 74  ? 0.569  19.685  7.284   1.00 30.91 ? 74  GLN A CD  1 
ATOM   586  O  OE1 . GLN A 1 74  ? -0.601 19.449  7.060   1.00 33.74 ? 74  GLN A OE1 1 
ATOM   587  N  NE2 . GLN A 1 74  ? 1.498  19.615  6.342   1.00 30.35 ? 74  GLN A NE2 1 
ATOM   588  N  N   . ASP A 1 75  ? 0.879  18.449  12.373  1.00 22.47 ? 75  ASP A N   1 
ATOM   589  C  CA  . ASP A 1 75  ? 0.326  17.759  13.507  1.00 25.39 ? 75  ASP A CA  1 
ATOM   590  C  C   . ASP A 1 75  ? -0.532 16.601  12.989  1.00 25.46 ? 75  ASP A C   1 
ATOM   591  O  O   . ASP A 1 75  ? -1.739 16.733  12.893  1.00 32.38 ? 75  ASP A O   1 
ATOM   592  C  CB  . ASP A 1 75  ? -0.345 18.784  14.427  1.00 28.92 ? 75  ASP A CB  1 
ATOM   593  C  CG  . ASP A 1 75  ? -0.433 18.233  15.825  1.00 42.81 ? 75  ASP A CG  1 
ATOM   594  O  OD1 . ASP A 1 75  ? -0.858 17.068  15.924  1.00 33.34 ? 75  ASP A OD1 1 
ATOM   595  O  OD2 . ASP A 1 75  ? 0.013  18.934  16.781  1.00 45.85 ? 75  ASP A OD2 1 
ATOM   596  N  N   . LYS A 1 76  ? 0.136  15.523  12.561  1.00 20.63 ? 76  LYS A N   1 
ATOM   597  C  CA  . LYS A 1 76  ? -0.470 14.291  12.094  1.00 21.09 ? 76  LYS A CA  1 
ATOM   598  C  C   . LYS A 1 76  ? 0.388  13.185  12.711  1.00 24.81 ? 76  LYS A C   1 
ATOM   599  O  O   . LYS A 1 76  ? 1.596  13.345  12.901  1.00 27.16 ? 76  LYS A O   1 
ATOM   600  C  CB  . LYS A 1 76  ? -0.481 14.101  10.563  1.00 25.15 ? 76  LYS A CB  1 
ATOM   601  C  CG  . LYS A 1 76  ? -0.686 15.276  9.628   1.00 33.11 ? 76  LYS A CG  1 
ATOM   602  C  CD  . LYS A 1 76  ? -0.017 14.983  8.290   1.00 30.05 ? 76  LYS A CD  1 
ATOM   603  C  CE  . LYS A 1 76  ? -0.255 16.088  7.274   1.00 37.60 ? 76  LYS A CE  1 
ATOM   604  N  NZ  . LYS A 1 76  ? -1.030 15.668  6.094   1.00 31.72 ? 76  LYS A NZ  1 
ATOM   605  N  N   . ALA A 1 77  ? -0.246 12.053  12.938  1.00 22.57 ? 77  ALA A N   1 
ATOM   606  C  CA  . ALA A 1 77  ? 0.335  10.791  13.327  1.00 15.70 ? 77  ALA A CA  1 
ATOM   607  C  C   . ALA A 1 77  ? 1.120  11.032  14.606  1.00 14.99 ? 77  ALA A C   1 
ATOM   608  O  O   . ALA A 1 77  ? 2.320  11.201  14.571  1.00 21.14 ? 77  ALA A O   1 
ATOM   609  C  CB  . ALA A 1 77  ? 1.143  10.172  12.191  1.00 18.72 ? 77  ALA A CB  1 
ATOM   610  N  N   . VAL A 1 78  ? 0.386  11.147  15.701  1.00 14.76 ? 78  VAL A N   1 
ATOM   611  C  CA  . VAL A 1 78  ? 1.089  11.433  16.953  1.00 16.04 ? 78  VAL A CA  1 
ATOM   612  C  C   . VAL A 1 78  ? 0.879  10.323  17.958  1.00 13.86 ? 78  VAL A C   1 
ATOM   613  O  O   . VAL A 1 78  ? -0.153 9.662   17.996  1.00 14.95 ? 78  VAL A O   1 
ATOM   614  C  CB  . VAL A 1 78  ? 0.613  12.782  17.476  1.00 21.85 ? 78  VAL A CB  1 
ATOM   615  C  CG1 . VAL A 1 78  ? 0.846  13.848  16.422  1.00 23.36 ? 78  VAL A CG1 1 
ATOM   616  C  CG2 . VAL A 1 78  ? -0.864 12.698  17.770  1.00 26.11 ? 78  VAL A CG2 1 
ATOM   617  N  N   . LEU A 1 79  ? 1.873  10.272  18.851  1.00 13.77 ? 79  LEU A N   1 
ATOM   618  C  CA  . LEU A 1 79  ? 1.835  9.358   19.966  1.00 15.14 ? 79  LEU A CA  1 
ATOM   619  C  C   . LEU A 1 79  ? 1.885  10.236  21.203  1.00 15.57 ? 79  LEU A C   1 
ATOM   620  O  O   . LEU A 1 79  ? 2.718  11.141  21.269  1.00 17.14 ? 79  LEU A O   1 
ATOM   621  C  CB  . LEU A 1 79  ? 3.090  8.491   19.802  1.00 17.48 ? 79  LEU A CB  1 
ATOM   622  C  CG  . LEU A 1 79  ? 3.305  7.390   20.815  1.00 18.40 ? 79  LEU A CG  1 
ATOM   623  C  CD1 . LEU A 1 79  ? 2.271  6.283   20.694  1.00 21.86 ? 79  LEU A CD1 1 
ATOM   624  C  CD2 . LEU A 1 79  ? 4.707  6.872   20.642  1.00 20.35 ? 79  LEU A CD2 1 
ATOM   625  N  N   . LYS A 1 80  ? 0.958  9.964   22.141  1.00 14.67 ? 80  LYS A N   1 
ATOM   626  C  CA  . LYS A 1 80  ? 1.016  10.689  23.395  1.00 17.56 ? 80  LYS A CA  1 
ATOM   627  C  C   . LYS A 1 80  ? 0.511  9.781   24.520  1.00 13.74 ? 80  LYS A C   1 
ATOM   628  O  O   . LYS A 1 80  ? 0.129  8.644   24.274  1.00 16.22 ? 80  LYS A O   1 
ATOM   629  C  CB  . LYS A 1 80  ? 0.333  12.048  23.314  1.00 21.13 ? 80  LYS A CB  1 
ATOM   630  C  CG  . LYS A 1 80  ? -1.177 12.006  23.220  1.00 24.01 ? 80  LYS A CG  1 
ATOM   631  C  CD  . LYS A 1 80  ? -1.825 13.331  22.762  1.00 31.40 ? 80  LYS A CD  1 
ATOM   632  N  N   . GLY A 1 81  ? 0.633  10.254  25.782  1.00 16.25 ? 81  GLY A N   1 
ATOM   633  C  CA  . GLY A 1 81  ? 0.218  9.457   26.921  1.00 16.91 ? 81  GLY A CA  1 
ATOM   634  C  C   . GLY A 1 81  ? 1.264  8.399   27.259  1.00 15.28 ? 81  GLY A C   1 
ATOM   635  O  O   . GLY A 1 81  ? 2.417  8.540   26.893  1.00 14.57 ? 81  GLY A O   1 
ATOM   636  N  N   . GLY A 1 82  ? 0.826  7.321   27.928  1.00 18.08 ? 82  GLY A N   1 
ATOM   637  C  CA  . GLY A 1 82  ? 1.764  6.336   28.406  1.00 17.22 ? 82  GLY A CA  1 
ATOM   638  C  C   . GLY A 1 82  ? 2.760  6.983   29.362  1.00 17.03 ? 82  GLY A C   1 
ATOM   639  O  O   . GLY A 1 82  ? 2.361  7.757   30.238  1.00 18.77 ? 82  GLY A O   1 
ATOM   640  N  N   . PRO A 1 83  ? 4.074  6.787   29.119  1.00 15.56 ? 83  PRO A N   1 
ATOM   641  C  CA  . PRO A 1 83  ? 5.119  7.380   29.970  1.00 17.13 ? 83  PRO A CA  1 
ATOM   642  C  C   . PRO A 1 83  ? 5.472  8.779   29.472  1.00 17.06 ? 83  PRO A C   1 
ATOM   643  O  O   . PRO A 1 83  ? 6.320  9.467   30.047  1.00 18.80 ? 83  PRO A O   1 
ATOM   644  C  CB  . PRO A 1 83  ? 6.324  6.487   29.667  1.00 17.01 ? 83  PRO A CB  1 
ATOM   645  C  CG  . PRO A 1 83  ? 6.129  6.037   28.221  1.00 17.17 ? 83  PRO A CG  1 
ATOM   646  C  CD  . PRO A 1 83  ? 4.621  5.913   28.063  1.00 16.10 ? 83  PRO A CD  1 
ATOM   647  N  N   . LEU A 1 84  ? 4.883  9.163   28.332  1.00 16.44 ? 84  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 84  ? 5.380  10.344  27.635  1.00 14.91 ? 84  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 84  ? 4.836  11.650  28.197  1.00 16.78 ? 84  LEU A C   1 
ATOM   650  O  O   . LEU A 1 84  ? 3.631  11.783  28.503  1.00 18.60 ? 84  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 84  ? 4.945  10.287  26.154  1.00 13.06 ? 84  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 84  ? 5.471  9.030   25.447  1.00 13.20 ? 84  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 84  ? 4.852  8.991   24.046  1.00 15.17 ? 84  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 84  ? 6.996  9.052   25.302  1.00 15.11 ? 84  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 85  ? 5.731  12.648  28.223  1.00 16.45 ? 85  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 85  ? 5.310  14.021  28.471  1.00 18.78 ? 85  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 85  ? 5.185  14.714  27.133  1.00 17.70 ? 85  ASP A C   1 
ATOM   658  O  O   . ASP A 1 85  ? 6.166  14.732  26.378  1.00 21.67 ? 85  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 85  ? 6.340  14.731  29.365  1.00 21.88 ? 85  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 85  ? 6.480  14.129  30.752  1.00 23.65 ? 85  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 85  ? 5.440  13.874  31.377  1.00 27.64 ? 85  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 85  ? 7.635  13.867  31.181  1.00 27.13 ? 85  ASP A OD2 1 
ATOM   663  N  N   . GLY A 1 86  ? 4.013  15.299  26.884  1.00 20.30 ? 86  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 86  ? 3.815  16.067  25.667  1.00 20.37 ? 86  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 86  ? 3.468  15.160  24.482  1.00 18.23 ? 86  GLY A C   1 
ATOM   666  O  O   . GLY A 1 86  ? 2.937  14.067  24.665  1.00 21.65 ? 86  GLY A O   1 
ATOM   667  N  N   . THR A 1 87  ? 3.813  15.613  23.281  1.00 15.63 ? 87  THR A N   1 
ATOM   668  C  CA  . THR A 1 87  ? 3.356  15.000  22.030  1.00 14.38 ? 87  THR A CA  1 
ATOM   669  C  C   . THR A 1 87  ? 4.567  14.612  21.169  1.00 14.09 ? 87  THR A C   1 
ATOM   670  O  O   . THR A 1 87  ? 5.485  15.397  21.074  1.00 14.15 ? 87  THR A O   1 
ATOM   671  C  CB  . THR A 1 87  ? 2.516  16.029  21.256  1.00 18.79 ? 87  THR A CB  1 
ATOM   672  O  OG1 . THR A 1 87  ? 1.343  16.223  22.083  1.00 26.85 ? 87  THR A OG1 1 
ATOM   673  C  CG2 . THR A 1 87  ? 2.082  15.516  19.899  1.00 26.26 ? 87  THR A CG2 1 
ATOM   674  N  N   . TYR A 1 88  ? 4.535  13.382  20.614  1.00 11.98 ? 88  TYR A N   1 
ATOM   675  C  CA  . TYR A 1 88  ? 5.592  12.886  19.767  1.00 12.70 ? 88  TYR A CA  1 
ATOM   676  C  C   . TYR A 1 88  ? 5.021  12.577  18.379  1.00 13.07 ? 88  TYR A C   1 
ATOM   677  O  O   . TYR A 1 88  ? 3.992  11.909  18.229  1.00 15.84 ? 88  TYR A O   1 
ATOM   678  C  CB  . TYR A 1 88  ? 6.208  11.616  20.357  1.00 12.44 ? 88  TYR A CB  1 
ATOM   679  C  CG  . TYR A 1 88  ? 7.034  11.861  21.608  1.00 12.21 ? 88  TYR A CG  1 
ATOM   680  C  CD1 . TYR A 1 88  ? 6.492  12.307  22.831  1.00 11.62 ? 88  TYR A CD1 1 
ATOM   681  C  CD2 . TYR A 1 88  ? 8.394  11.673  21.576  1.00 11.44 ? 88  TYR A CD2 1 
ATOM   682  C  CE1 . TYR A 1 88  ? 7.324  12.493  23.931  1.00 14.05 ? 88  TYR A CE1 1 
ATOM   683  C  CE2 . TYR A 1 88  ? 9.224  11.861  22.667  1.00 12.44 ? 88  TYR A CE2 1 
ATOM   684  C  CZ  . TYR A 1 88  ? 8.662  12.223  23.868  1.00 12.22 ? 88  TYR A CZ  1 
ATOM   685  O  OH  . TYR A 1 88  ? 9.453  12.426  24.999  1.00 16.38 ? 88  TYR A OH  1 
ATOM   686  N  N   . ARG A 1 89  ? 5.694  13.068  17.344  1.00 12.76 ? 89  ARG A N   1 
ATOM   687  C  CA  . ARG A 1 89  ? 5.179  12.965  15.981  1.00 12.40 ? 89  ARG A CA  1 
ATOM   688  C  C   . ARG A 1 89  ? 5.899  11.852  15.208  1.00 11.05 ? 89  ARG A C   1 
ATOM   689  O  O   . ARG A 1 89  ? 7.135  11.798  15.177  1.00 11.17 ? 89  ARG A O   1 
ATOM   690  C  CB  . ARG A 1 89  ? 5.440  14.299  15.283  1.00 17.67 ? 89  ARG A CB  1 
ATOM   691  C  CG  . ARG A 1 89  ? 4.604  14.425  14.029  1.00 16.43 ? 89  ARG A CG  1 
ATOM   692  C  CD  . ARG A 1 89  ? 4.742  15.805  13.368  1.00 17.79 ? 89  ARG A CD  1 
ATOM   693  N  NE  . ARG A 1 89  ? 4.217  16.852  14.267  1.00 20.54 ? 89  ARG A NE  1 
ATOM   694  C  CZ  . ARG A 1 89  ? 4.378  18.179  14.091  1.00 18.20 ? 89  ARG A CZ  1 
ATOM   695  N  NH1 . ARG A 1 89  ? 5.150  18.680  13.116  1.00 18.84 ? 89  ARG A NH1 1 
ATOM   696  N  NH2 . ARG A 1 89  ? 3.785  19.018  14.897  1.00 20.25 ? 89  ARG A NH2 1 
ATOM   697  N  N   . LEU A 1 90  ? 5.135  11.023  14.488  1.00 12.30 ? 90  LEU A N   1 
ATOM   698  C  CA  . LEU A 1 90  ? 5.739  9.956   13.669  1.00 12.43 ? 90  LEU A CA  1 
ATOM   699  C  C   . LEU A 1 90  ? 6.528  10.520  12.500  1.00 12.70 ? 90  LEU A C   1 
ATOM   700  O  O   . LEU A 1 90  ? 6.033  11.361  11.740  1.00 13.56 ? 90  LEU A O   1 
ATOM   701  C  CB  . LEU A 1 90  ? 4.624  9.071   13.106  1.00 11.78 ? 90  LEU A CB  1 
ATOM   702  C  CG  . LEU A 1 90  ? 5.045  7.930   12.174  1.00 12.36 ? 90  LEU A CG  1 
ATOM   703  C  CD1 . LEU A 1 90  ? 5.800  6.837   12.917  1.00 13.01 ? 90  LEU A CD1 1 
ATOM   704  C  CD2 . LEU A 1 90  ? 3.816  7.330   11.458  1.00 14.74 ? 90  LEU A CD2 1 
ATOM   705  N  N   . THR A 1 91  ? 7.763  10.037  12.377  1.00 10.64 ? 91  THR A N   1 
ATOM   706  C  CA  . THR A 1 91  ? 8.593  10.471  11.257  1.00 10.52 ? 91  THR A CA  1 
ATOM   707  C  C   . THR A 1 91  ? 8.971  9.340   10.302  1.00 10.47 ? 91  THR A C   1 
ATOM   708  O  O   . THR A 1 91  ? 9.066  9.566   9.071   1.00 10.64 ? 91  THR A O   1 
ATOM   709  C  CB  . THR A 1 91  ? 9.861  11.187  11.758  1.00 12.99 ? 91  THR A CB  1 
ATOM   710  O  OG1 . THR A 1 91  ? 10.580 11.728  10.654  1.00 15.21 ? 91  THR A OG1 1 
ATOM   711  C  CG2 . THR A 1 91  ? 10.832 10.297  12.516  1.00 14.36 ? 91  THR A CG2 1 
ATOM   712  N  N   . GLN A 1 92  ? 9.077  8.099   10.767  1.00 9.63  ? 92  GLN A N   1 
ATOM   713  C  CA  . GLN A 1 92  ? 9.429  7.010   9.858   1.00 10.30 ? 92  GLN A CA  1 
ATOM   714  C  C   . GLN A 1 92  ? 9.108  5.707   10.551  1.00 9.44  ? 92  GLN A C   1 
ATOM   715  O  O   . GLN A 1 92  ? 9.009  5.698   11.796  1.00 11.57 ? 92  GLN A O   1 
ATOM   716  C  CB  . GLN A 1 92  ? 10.902 7.005   9.432   1.00 9.98  ? 92  GLN A CB  1 
ATOM   717  C  CG  . GLN A 1 92  ? 11.869 7.047   10.612  1.00 13.18 ? 92  GLN A CG  1 
ATOM   718  C  CD  . GLN A 1 92  ? 12.667 5.791   10.740  1.00 13.13 ? 92  GLN A CD  1 
ATOM   719  O  OE1 . GLN A 1 92  ? 12.146 4.699   10.734  1.00 15.19 ? 92  GLN A OE1 1 
ATOM   720  N  NE2 . GLN A 1 92  ? 13.954 5.944   10.953  1.00 17.44 ? 92  GLN A NE2 1 
ATOM   721  N  N   . PHE A 1 93  ? 8.970  4.608   9.859   1.00 9.57  ? 93  PHE A N   1 
ATOM   722  C  CA  . PHE A 1 93  ? 9.129  3.294   10.447  1.00 10.49 ? 93  PHE A CA  1 
ATOM   723  C  C   . PHE A 1 93  ? 10.100 2.474   9.615   1.00 8.95  ? 93  PHE A C   1 
ATOM   724  O  O   . PHE A 1 93  ? 10.356 2.721   8.438   1.00 9.90  ? 93  PHE A O   1 
ATOM   725  C  CB  . PHE A 1 93  ? 7.800  2.557   10.670  1.00 9.93  ? 93  PHE A CB  1 
ATOM   726  C  CG  . PHE A 1 93  ? 7.101  2.138   9.394   1.00 9.92  ? 93  PHE A CG  1 
ATOM   727  C  CD1 . PHE A 1 93  ? 7.531  1.043   8.638   1.00 9.84  ? 93  PHE A CD1 1 
ATOM   728  C  CD2 . PHE A 1 93  ? 5.914  2.768   9.073   1.00 10.00 ? 93  PHE A CD2 1 
ATOM   729  C  CE1 . PHE A 1 93  ? 6.781  0.678   7.509   1.00 10.40 ? 93  PHE A CE1 1 
ATOM   730  C  CE2 . PHE A 1 93  ? 5.204  2.443   7.910   1.00 11.13 ? 93  PHE A CE2 1 
ATOM   731  C  CZ  . PHE A 1 93  ? 5.637  1.368   7.180   1.00 11.04 ? 93  PHE A CZ  1 
ATOM   732  N  N   . HIS A 1 94  ? 10.642 1.446   10.238  1.00 10.16 ? 94  HIS A N   1 
ATOM   733  C  CA  . HIS A 1 94  ? 11.582 0.524   9.622   1.00 9.05  ? 94  HIS A CA  1 
ATOM   734  C  C   . HIS A 1 94  ? 11.521 -0.800  10.385  1.00 9.25  ? 94  HIS A C   1 
ATOM   735  O  O   . HIS A 1 94  ? 10.849 -0.880  11.416  1.00 10.58 ? 94  HIS A O   1 
ATOM   736  C  CB  . HIS A 1 94  ? 13.017 1.106   9.594   1.00 10.40 ? 94  HIS A CB  1 
ATOM   737  C  CG  . HIS A 1 94  ? 13.546 1.309   10.994  1.00 11.31 ? 94  HIS A CG  1 
ATOM   738  N  ND1 . HIS A 1 94  ? 13.350 2.434   11.734  1.00 9.83  ? 94  HIS A ND1 1 
ATOM   739  C  CD2 . HIS A 1 94  ? 14.151 0.375   11.743  1.00 14.00 ? 94  HIS A CD2 1 
ATOM   740  C  CE1 . HIS A 1 94  ? 13.940 2.214   12.991  1.00 14.08 ? 94  HIS A CE1 1 
ATOM   741  N  NE2 . HIS A 1 94  ? 14.375 0.870   13.084  1.00 18.51 ? 94  HIS A NE2 1 
ATOM   742  N  N   . PHE A 1 95  ? 12.241 -1.773  9.883   1.00 10.26 ? 95  PHE A N   1 
ATOM   743  C  CA  . PHE A 1 95  ? 12.229 -3.095  10.484  1.00 9.19  ? 95  PHE A CA  1 
ATOM   744  C  C   . PHE A 1 95  ? 13.662 -3.587  10.686  1.00 9.79  ? 95  PHE A C   1 
ATOM   745  O  O   . PHE A 1 95  ? 14.625 -3.110  10.079  1.00 11.03 ? 95  PHE A O   1 
ATOM   746  C  CB  . PHE A 1 95  ? 11.520 -4.113  9.583   1.00 10.88 ? 95  PHE A CB  1 
ATOM   747  C  CG  . PHE A 1 95  ? 10.062 -3.829  9.302   1.00 9.71  ? 95  PHE A CG  1 
ATOM   748  C  CD1 . PHE A 1 95  ? 9.687  -2.897  8.327   1.00 11.35 ? 95  PHE A CD1 1 
ATOM   749  C  CD2 . PHE A 1 95  ? 9.075  -4.495  10.030  1.00 10.36 ? 95  PHE A CD2 1 
ATOM   750  C  CE1 . PHE A 1 95  ? 8.337  -2.741  8.047   1.00 12.53 ? 95  PHE A CE1 1 
ATOM   751  C  CE2 . PHE A 1 95  ? 7.713  -4.321  9.756   1.00 11.12 ? 95  PHE A CE2 1 
ATOM   752  C  CZ  . PHE A 1 95  ? 7.361  -3.442  8.734   1.00 12.91 ? 95  PHE A CZ  1 
ATOM   753  N  N   . HIS A 1 96  ? 13.765 -4.595  11.558  1.00 11.26 ? 96  HIS A N   1 
ATOM   754  C  CA  . HIS A 1 96  ? 14.991 -5.384  11.679  1.00 10.39 ? 96  HIS A CA  1 
ATOM   755  C  C   . HIS A 1 96  ? 14.576 -6.839  11.601  1.00 9.20  ? 96  HIS A C   1 
ATOM   756  O  O   . HIS A 1 96  ? 13.477 -7.150  12.079  1.00 10.44 ? 96  HIS A O   1 
ATOM   757  C  CB  . HIS A 1 96  ? 15.628 -5.199  13.061  1.00 10.25 ? 96  HIS A CB  1 
ATOM   758  C  CG  . HIS A 1 96  ? 15.900 -3.760  13.375  1.00 10.10 ? 96  HIS A CG  1 
ATOM   759  N  ND1 . HIS A 1 96  ? 17.135 -3.192  13.229  1.00 10.03 ? 96  HIS A ND1 1 
ATOM   760  C  CD2 . HIS A 1 96  ? 15.084 -2.773  13.837  1.00 12.13 ? 96  HIS A CD2 1 
ATOM   761  C  CE1 . HIS A 1 96  ? 17.089 -1.903  13.636  1.00 10.85 ? 96  HIS A CE1 1 
ATOM   762  N  NE2 . HIS A 1 96  ? 15.813 -1.644  13.943  1.00 11.76 ? 96  HIS A NE2 1 
ATOM   763  N  N   . TRP A 1 97  ? 15.377 -7.681  10.931  1.00 9.45  ? 97  TRP A N   1 
ATOM   764  C  CA  . TRP A 1 97  ? 14.937 -9.062  10.741  1.00 9.24  ? 97  TRP A CA  1 
ATOM   765  C  C   . TRP A 1 97  ? 16.146 -9.990  10.624  1.00 9.02  ? 97  TRP A C   1 
ATOM   766  O  O   . TRP A 1 97  ? 17.308 -9.530  10.518  1.00 10.34 ? 97  TRP A O   1 
ATOM   767  C  CB  . TRP A 1 97  ? 14.005 -9.219  9.505   1.00 10.38 ? 97  TRP A CB  1 
ATOM   768  C  CG  . TRP A 1 97  ? 14.669 -8.840  8.193   1.00 9.91  ? 97  TRP A CG  1 
ATOM   769  C  CD1 . TRP A 1 97  ? 15.415 -9.638  7.353   1.00 10.11 ? 97  TRP A CD1 1 
ATOM   770  C  CD2 . TRP A 1 97  ? 14.746 -7.519  7.649   1.00 9.91  ? 97  TRP A CD2 1 
ATOM   771  N  NE1 . TRP A 1 97  ? 15.856 -8.910  6.275   1.00 12.28 ? 97  TRP A NE1 1 
ATOM   772  C  CE2 . TRP A 1 97  ? 15.458 -7.605  6.427   1.00 10.13 ? 97  TRP A CE2 1 
ATOM   773  C  CE3 . TRP A 1 97  ? 14.214 -6.283  8.032   1.00 11.07 ? 97  TRP A CE3 1 
ATOM   774  C  CZ2 . TRP A 1 97  ? 15.694 -6.471  5.631   1.00 13.09 ? 97  TRP A CZ2 1 
ATOM   775  C  CZ3 . TRP A 1 97  ? 14.474 -5.165  7.253   1.00 12.17 ? 97  TRP A CZ3 1 
ATOM   776  C  CH2 . TRP A 1 97  ? 15.147 -5.268  6.006   1.00 11.93 ? 97  TRP A CH2 1 
ATOM   777  N  N   . GLY A 1 98  ? 15.826 -11.280 10.606  1.00 10.29 ? 98  GLY A N   1 
ATOM   778  C  CA  . GLY A 1 98  ? 16.829 -12.326 10.609  1.00 10.70 ? 98  GLY A CA  1 
ATOM   779  C  C   . GLY A 1 98  ? 17.046 -13.072 9.295   1.00 11.58 ? 98  GLY A C   1 
ATOM   780  O  O   . GLY A 1 98  ? 16.295 -12.878 8.335   1.00 12.30 ? 98  GLY A O   1 
ATOM   781  N  N   . SER A 1 99  ? 18.098 -13.907 9.267   1.00 11.25 ? 99  SER A N   1 
ATOM   782  C  CA  . SER A 1 99  ? 18.342 -14.758 8.093   1.00 13.09 ? 99  SER A CA  1 
ATOM   783  C  C   . SER A 1 99  ? 17.549 -16.064 8.207   1.00 13.38 ? 99  SER A C   1 
ATOM   784  O  O   . SER A 1 99  ? 17.496 -16.841 7.263   1.00 14.80 ? 99  SER A O   1 
ATOM   785  C  CB  . SER A 1 99  ? 19.816 -15.021 7.962   1.00 15.52 ? 99  SER A CB  1 
ATOM   786  O  OG  . SER A 1 99  ? 20.206 -15.676 9.150   1.00 14.50 ? 99  SER A OG  1 
ATOM   787  N  N   . LEU A 1 100 ? 16.834 -16.266 9.336   1.00 11.56 ? 100 LEU A N   1 
ATOM   788  C  CA  . LEU A 1 100 ? 15.937 -17.380 9.609   1.00 14.41 ? 100 LEU A CA  1 
ATOM   789  C  C   . LEU A 1 100 ? 14.868 -16.940 10.618  1.00 15.49 ? 100 LEU A C   1 
ATOM   790  O  O   . LEU A 1 100 ? 15.058 -15.941 11.276  1.00 15.92 ? 100 LEU A O   1 
ATOM   791  C  CB  . LEU A 1 100 ? 16.758 -18.559 10.119  1.00 16.59 ? 100 LEU A CB  1 
ATOM   792  C  CG  . LEU A 1 100 ? 17.631 -18.216 11.338  1.00 19.30 ? 100 LEU A CG  1 
ATOM   793  C  CD1 . LEU A 1 100 ? 17.014 -18.724 12.630  1.00 26.70 ? 100 LEU A CD1 1 
ATOM   794  C  CD2 . LEU A 1 100 ? 19.046 -18.752 11.189  1.00 25.82 ? 100 LEU A CD2 1 
ATOM   795  N  N   . ASP A 1 101 ? 13.746 -17.670 10.726  1.00 17.09 ? 101 ASP A N   1 
ATOM   796  C  CA  . ASP A 1 101 ? 12.591 -17.171 11.485  1.00 15.76 ? 101 ASP A CA  1 
ATOM   797  C  C   . ASP A 1 101 ? 12.899 -17.098 12.988  1.00 16.92 ? 101 ASP A C   1 
ATOM   798  O  O   . ASP A 1 101 ? 12.262 -16.334 13.732  1.00 19.34 ? 101 ASP A O   1 
ATOM   799  C  CB  . ASP A 1 101 ? 11.393 -18.085 11.273  1.00 17.69 ? 101 ASP A CB  1 
ATOM   800  C  CG  . ASP A 1 101 ? 10.773 -18.007 9.861   1.00 20.21 ? 101 ASP A CG  1 
ATOM   801  O  OD1 . ASP A 1 101 ? 11.158 -17.124 9.066   1.00 23.39 ? 101 ASP A OD1 1 
ATOM   802  O  OD2 . ASP A 1 101 ? 9.883  -18.826 9.552   1.00 28.45 ? 101 ASP A OD2 1 
ATOM   803  N  N   . GLY A 1 102 ? 13.886 -17.888 13.436  1.00 17.80 ? 102 GLY A N   1 
ATOM   804  C  CA  . GLY A 1 102 ? 14.206 -17.977 14.858  1.00 18.48 ? 102 GLY A CA  1 
ATOM   805  C  C   . GLY A 1 102 ? 15.012 -16.794 15.433  1.00 17.82 ? 102 GLY A C   1 
ATOM   806  O  O   . GLY A 1 102 ? 15.418 -16.813 16.609  1.00 18.48 ? 102 GLY A O   1 
ATOM   807  N  N   . GLN A 1 103 ? 15.316 -15.771 14.625  1.00 14.52 ? 103 GLN A N   1 
ATOM   808  C  CA  . GLN A 1 103 ? 16.009 -14.583 15.124  1.00 13.24 ? 103 GLN A CA  1 
ATOM   809  C  C   . GLN A 1 103 ? 15.627 -13.399 14.271  1.00 13.11 ? 103 GLN A C   1 
ATOM   810  O  O   . GLN A 1 103 ? 15.077 -13.597 13.179  1.00 13.56 ? 103 GLN A O   1 
ATOM   811  C  CB  . GLN A 1 103 ? 17.521 -14.807 15.172  1.00 12.65 ? 103 GLN A CB  1 
ATOM   812  C  CG  . GLN A 1 103 ? 18.133 -14.969 13.785  1.00 12.78 ? 103 GLN A CG  1 
ATOM   813  C  CD  . GLN A 1 103 ? 19.572 -15.455 13.856  1.00 13.69 ? 103 GLN A CD  1 
ATOM   814  O  OE1 . GLN A 1 103 ? 20.416 -15.128 13.022  1.00 18.08 ? 103 GLN A OE1 1 
ATOM   815  N  NE2 . GLN A 1 103 ? 19.867 -16.375 14.730  1.00 16.42 ? 103 GLN A NE2 1 
ATOM   816  N  N   . GLY A 1 104 ? 15.935 -12.181 14.692  1.00 11.28 ? 104 GLY A N   1 
ATOM   817  C  CA  . GLY A 1 104 ? 15.695 -10.993 13.889  1.00 11.81 ? 104 GLY A CA  1 
ATOM   818  C  C   . GLY A 1 104 ? 15.250 -9.804  14.752  1.00 10.57 ? 104 GLY A C   1 
ATOM   819  O  O   . GLY A 1 104 ? 15.484 -8.641  14.409  1.00 11.56 ? 104 GLY A O   1 
ATOM   820  N  N   . SER A 1 105 ? 14.519 -10.103 15.875  1.00 10.58 ? 105 SER A N   1 
ATOM   821  C  CA  . SER A 1 105 ? 14.134 -8.998  16.761  1.00 11.27 ? 105 SER A CA  1 
ATOM   822  C  C   . SER A 1 105 ? 15.341 -8.447  17.531  1.00 9.75  ? 105 SER A C   1 
ATOM   823  O  O   . SER A 1 105 ? 16.347 -9.146  17.686  1.00 11.85 ? 105 SER A O   1 
ATOM   824  C  CB  . SER A 1 105 ? 12.968 -9.332  17.707  1.00 11.22 ? 105 SER A CB  1 
ATOM   825  O  OG  . SER A 1 105 ? 13.343 -10.304 18.660  1.00 11.53 ? 105 SER A OG  1 
ATOM   826  N  N   . GLU A 1 106 ? 15.240 -7.167  17.910  1.00 9.72  ? 106 GLU A N   1 
ATOM   827  C  CA  . GLU A 1 106 ? 16.239 -6.523  18.752  1.00 10.22 ? 106 GLU A CA  1 
ATOM   828  C  C   . GLU A 1 106 ? 15.895 -6.769  20.224  1.00 10.45 ? 106 GLU A C   1 
ATOM   829  O  O   . GLU A 1 106 ? 16.715 -7.348  20.975  1.00 12.01 ? 106 GLU A O   1 
ATOM   830  C  CB  . GLU A 1 106 ? 16.291 -5.035  18.404  1.00 10.49 ? 106 GLU A CB  1 
ATOM   831  C  CG  . GLU A 1 106 ? 16.692 -4.885  16.936  1.00 10.57 ? 106 GLU A CG  1 
ATOM   832  C  CD  . GLU A 1 106 ? 17.414 -3.583  16.662  1.00 10.70 ? 106 GLU A CD  1 
ATOM   833  O  OE1 . GLU A 1 106 ? 16.809 -2.515  16.922  1.00 11.40 ? 106 GLU A OE1 1 
ATOM   834  O  OE2 . GLU A 1 106 ? 18.601 -3.623  16.152  1.00 13.46 ? 106 GLU A OE2 1 
ATOM   835  N  N   . HIS A 1 107 ? 14.694 -6.311  20.626  1.00 11.54 ? 107 HIS A N   1 
ATOM   836  C  CA  . HIS A 1 107 ? 14.249 -6.653  21.972  1.00 10.36 ? 107 HIS A CA  1 
ATOM   837  C  C   . HIS A 1 107 ? 13.983 -8.145  22.003  1.00 11.39 ? 107 HIS A C   1 
ATOM   838  O  O   . HIS A 1 107 ? 13.675 -8.753  20.977  1.00 12.19 ? 107 HIS A O   1 
ATOM   839  C  CB  . HIS A 1 107 ? 13.005 -5.887  22.397  1.00 11.91 ? 107 HIS A CB  1 
ATOM   840  C  CG  . HIS A 1 107 ? 13.336 -4.452  22.579  1.00 10.73 ? 107 HIS A CG  1 
ATOM   841  N  ND1 . HIS A 1 107 ? 13.362 -3.551  21.537  1.00 11.52 ? 107 HIS A ND1 1 
ATOM   842  C  CD2 . HIS A 1 107 ? 13.833 -3.801  23.656  1.00 11.71 ? 107 HIS A CD2 1 
ATOM   843  C  CE1 . HIS A 1 107 ? 13.776 -2.354  21.966  1.00 10.38 ? 107 HIS A CE1 1 
ATOM   844  N  NE2 . HIS A 1 107 ? 14.087 -2.484  23.302  1.00 10.33 ? 107 HIS A NE2 1 
ATOM   845  N  N   . THR A 1 108 ? 14.132 -8.734  23.198  1.00 12.72 ? 108 THR A N   1 
ATOM   846  C  CA  . THR A 1 108 ? 13.727 -10.096 23.409  1.00 12.02 ? 108 THR A CA  1 
ATOM   847  C  C   . THR A 1 108 ? 12.775 -10.158 24.587  1.00 11.43 ? 108 THR A C   1 
ATOM   848  O  O   . THR A 1 108 ? 12.742 -9.224  25.376  1.00 13.09 ? 108 THR A O   1 
ATOM   849  C  CB  . THR A 1 108 ? 14.898 -11.045 23.599  1.00 11.39 ? 108 THR A CB  1 
ATOM   850  O  OG1 . THR A 1 108 ? 15.730 -10.608 24.682  1.00 13.60 ? 108 THR A OG1 1 
ATOM   851  C  CG2 . THR A 1 108 ? 15.722 -11.113 22.348  1.00 11.97 ? 108 THR A CG2 1 
ATOM   852  N  N   . VAL A 1 109 ? 11.973 -11.206 24.642  1.00 12.65 ? 109 VAL A N   1 
ATOM   853  C  CA  . VAL A 1 109 ? 10.952 -11.282 25.702  1.00 12.65 ? 109 VAL A CA  1 
ATOM   854  C  C   . VAL A 1 109 ? 11.182 -12.580 26.465  1.00 13.63 ? 109 VAL A C   1 
ATOM   855  O  O   . VAL A 1 109 ? 11.004 -13.660 25.930  1.00 14.97 ? 109 VAL A O   1 
ATOM   856  C  CB  . VAL A 1 109 ? 9.522  -11.251 25.115  1.00 14.43 ? 109 VAL A CB  1 
ATOM   857  C  CG1 . VAL A 1 109 ? 8.467  -11.339 26.207  1.00 16.45 ? 109 VAL A CG1 1 
ATOM   858  C  CG2 . VAL A 1 109 ? 9.299  -9.982  24.346  1.00 16.17 ? 109 VAL A CG2 1 
ATOM   859  N  N   . ASP A 1 110 ? 11.674 -12.465 27.712  1.00 15.11 ? 110 ASP A N   1 
ATOM   860  C  CA  . ASP A 1 110 ? 12.054 -13.682 28.432  1.00 15.41 ? 110 ASP A CA  1 
ATOM   861  C  C   . ASP A 1 110 ? 13.016 -14.538 27.587  1.00 15.24 ? 110 ASP A C   1 
ATOM   862  O  O   . ASP A 1 110 ? 12.879 -15.772 27.517  1.00 15.58 ? 110 ASP A O   1 
ATOM   863  C  CB  . ASP A 1 110 ? 10.810 -14.447 28.946  1.00 16.46 ? 110 ASP A CB  1 
ATOM   864  C  CG  . ASP A 1 110 ? 9.898  -13.612 29.845  1.00 19.01 ? 110 ASP A CG  1 
ATOM   865  O  OD1 . ASP A 1 110 ? 10.463 -12.815 30.625  1.00 19.48 ? 110 ASP A OD1 1 
ATOM   866  O  OD2 . ASP A 1 110 ? 8.634  -13.762 29.776  1.00 19.89 ? 110 ASP A OD2 1 
ATOM   867  N  N   . LYS A 1 111 ? 13.975 -13.849 26.955  1.00 13.75 ? 111 LYS A N   1 
ATOM   868  C  CA  . LYS A 1 111 ? 14.960 -14.432 26.045  1.00 14.12 ? 111 LYS A CA  1 
ATOM   869  C  C   . LYS A 1 111 ? 14.405 -14.768 24.645  1.00 12.91 ? 111 LYS A C   1 
ATOM   870  O  O   . LYS A 1 111 ? 15.238 -15.127 23.805  1.00 15.76 ? 111 LYS A O   1 
ATOM   871  C  CB  . LYS A 1 111 ? 15.648 -15.663 26.643  1.00 18.22 ? 111 LYS A CB  1 
ATOM   872  C  CG  . LYS A 1 111 ? 16.334 -15.424 27.982  1.00 18.26 ? 111 LYS A CG  1 
ATOM   873  C  CD  . LYS A 1 111 ? 17.519 -14.470 27.963  1.00 22.46 ? 111 LYS A CD  1 
ATOM   874  N  N   . LYS A 1 112 ? 13.086 -14.795 24.431  1.00 12.94 ? 112 LYS A N   1 
ATOM   875  C  CA  . LYS A 1 112 ? 12.558 -15.164 23.100  1.00 14.37 ? 112 LYS A CA  1 
ATOM   876  C  C   . LYS A 1 112 ? 12.955 -14.122 22.068  1.00 11.83 ? 112 LYS A C   1 
ATOM   877  O  O   . LYS A 1 112 ? 12.730 -12.920 22.276  1.00 13.81 ? 112 LYS A O   1 
ATOM   878  C  CB  . LYS A 1 112 ? 11.028 -15.343 23.081  1.00 16.05 ? 112 LYS A CB  1 
ATOM   879  C  CG  . LYS A 1 112 ? 10.389 -15.622 21.728  1.00 23.34 ? 112 LYS A CG  1 
ATOM   880  C  CD  . LYS A 1 112 ? 8.896  -15.983 21.776  1.00 24.76 ? 112 LYS A CD  1 
ATOM   881  C  CE  . LYS A 1 112 ? 8.332  -16.197 20.376  1.00 28.75 ? 112 LYS A CE  1 
ATOM   882  N  NZ  . LYS A 1 112 ? 9.357  -16.561 19.373  1.00 40.22 ? 112 LYS A NZ  1 
ATOM   883  N  N   A LYS A 1 113 ? 13.508 -14.610 20.941  0.50 13.86 ? 113 LYS A N   1 
ATOM   884  N  N   B LYS A 1 113 ? 13.475 -14.620 20.931  0.50 14.29 ? 113 LYS A N   1 
ATOM   885  C  CA  A LYS A 1 113 ? 13.696 -13.785 19.756  0.50 14.54 ? 113 LYS A CA  1 
ATOM   886  C  CA  B LYS A 1 113 ? 13.674 -13.797 19.748  0.50 14.54 ? 113 LYS A CA  1 
ATOM   887  C  C   A LYS A 1 113 ? 12.549 -13.998 18.771  0.50 11.73 ? 113 LYS A C   1 
ATOM   888  C  C   B LYS A 1 113 ? 12.551 -14.006 18.742  0.50 11.41 ? 113 LYS A C   1 
ATOM   889  O  O   A LYS A 1 113 ? 12.124 -15.129 18.553  0.50 17.18 ? 113 LYS A O   1 
ATOM   890  O  O   B LYS A 1 113 ? 12.156 -15.138 18.475  0.50 16.67 ? 113 LYS A O   1 
ATOM   891  C  CB  A LYS A 1 113 ? 15.029 -14.072 19.052  0.50 13.70 ? 113 LYS A CB  1 
ATOM   892  C  CB  B LYS A 1 113 ? 15.013 -14.087 19.063  0.50 14.05 ? 113 LYS A CB  1 
ATOM   893  C  CG  A LYS A 1 113 ? 16.272 -13.878 19.917  0.50 14.30 ? 113 LYS A CG  1 
ATOM   894  C  CG  B LYS A 1 113 ? 16.204 -13.888 19.986  0.50 14.75 ? 113 LYS A CG  1 
ATOM   895  C  CD  A LYS A 1 113 ? 17.452 -14.647 19.355  0.50 13.73 ? 113 LYS A CD  1 
ATOM   896  C  CD  B LYS A 1 113 ? 17.508 -14.339 19.361  0.50 13.83 ? 113 LYS A CD  1 
ATOM   897  C  CE  A LYS A 1 113 ? 18.825 -14.195 19.805  0.50 15.09 ? 113 LYS A CE  1 
ATOM   898  C  CE  B LYS A 1 113 ? 18.717 -13.924 20.173  0.50 16.80 ? 113 LYS A CE  1 
ATOM   899  N  NZ  A LYS A 1 113 ? 19.199 -14.688 21.160  0.50 17.01 ? 113 LYS A NZ  1 
ATOM   900  N  NZ  B LYS A 1 113 ? 19.922 -14.741 19.881  0.50 17.85 ? 113 LYS A NZ  1 
ATOM   901  N  N   . TYR A 1 114 ? 12.042 -12.880 18.234  1.00 11.92 ? 114 TYR A N   1 
ATOM   902  C  CA  . TYR A 1 114 ? 11.008 -12.919 17.212  1.00 10.57 ? 114 TYR A CA  1 
ATOM   903  C  C   . TYR A 1 114 ? 11.707 -12.864 15.840  1.00 12.21 ? 114 TYR A C   1 
ATOM   904  O  O   . TYR A 1 114 ? 12.900 -12.624 15.731  1.00 13.41 ? 114 TYR A O   1 
ATOM   905  C  CB  . TYR A 1 114 ? 9.995  -11.793 17.419  1.00 10.96 ? 114 TYR A CB  1 
ATOM   906  C  CG  . TYR A 1 114 ? 9.031  -12.072 18.542  1.00 10.56 ? 114 TYR A CG  1 
ATOM   907  C  CD1 . TYR A 1 114 ? 9.324  -11.714 19.845  1.00 15.28 ? 114 TYR A CD1 1 
ATOM   908  C  CD2 . TYR A 1 114 ? 7.853  -12.738 18.314  1.00 14.52 ? 114 TYR A CD2 1 
ATOM   909  C  CE1 . TYR A 1 114 ? 8.416  -11.961 20.842  1.00 16.04 ? 114 TYR A CE1 1 
ATOM   910  C  CE2 . TYR A 1 114 ? 6.931  -13.004 19.317  1.00 18.29 ? 114 TYR A CE2 1 
ATOM   911  C  CZ  . TYR A 1 114 ? 7.260  -12.665 20.609  1.00 18.37 ? 114 TYR A CZ  1 
ATOM   912  O  OH  . TYR A 1 114 ? 6.466  -12.827 21.710  1.00 27.28 ? 114 TYR A OH  1 
ATOM   913  N  N   . ALA A 1 115 ? 10.942 -13.116 14.772  1.00 11.29 ? 115 ALA A N   1 
ATOM   914  C  CA  . ALA A 1 115 ? 11.542 -13.133 13.437  1.00 12.04 ? 115 ALA A CA  1 
ATOM   915  C  C   . ALA A 1 115 ? 11.902 -11.726 12.938  1.00 11.54 ? 115 ALA A C   1 
ATOM   916  O  O   . ALA A 1 115 ? 12.750 -11.576 12.053  1.00 12.62 ? 115 ALA A O   1 
ATOM   917  C  CB  . ALA A 1 115 ? 10.581 -13.777 12.458  1.00 14.16 ? 115 ALA A CB  1 
ATOM   918  N  N   . ALA A 1 116 ? 11.258 -10.694 13.483  1.00 10.81 ? 116 ALA A N   1 
ATOM   919  C  CA  . ALA A 1 116 ? 11.510 -9.329  13.048  1.00 10.49 ? 116 ALA A CA  1 
ATOM   920  C  C   . ALA A 1 116 ? 10.984 -8.404  14.135  1.00 10.75 ? 116 ALA A C   1 
ATOM   921  O  O   . ALA A 1 116 ? 10.222 -8.837  15.022  1.00 11.55 ? 116 ALA A O   1 
ATOM   922  C  CB  . ALA A 1 116 ? 10.935 -9.054  11.632  1.00 10.43 ? 116 ALA A CB  1 
ATOM   923  N  N   . GLU A 1 117 ? 11.320 -7.129  13.973  1.00 9.83  ? 117 GLU A N   1 
ATOM   924  C  CA  . GLU A 1 117 ? 10.802 -6.095  14.867  1.00 9.57  ? 117 GLU A CA  1 
ATOM   925  C  C   . GLU A 1 117 ? 10.586 -4.810  14.081  1.00 9.63  ? 117 GLU A C   1 
ATOM   926  O  O   . GLU A 1 117 ? 11.447 -4.449  13.284  1.00 10.46 ? 117 GLU A O   1 
ATOM   927  C  CB  . GLU A 1 117 ? 11.778 -5.874  16.019  1.00 11.53 ? 117 GLU A CB  1 
ATOM   928  C  CG  . GLU A 1 117 ? 11.255 -5.012  17.202  1.00 11.48 ? 117 GLU A CG  1 
ATOM   929  C  CD  . GLU A 1 117 ? 12.177 -4.973  18.413  1.00 11.62 ? 117 GLU A CD  1 
ATOM   930  O  OE1 . GLU A 1 117 ? 12.788 -6.004  18.674  1.00 14.14 ? 117 GLU A OE1 1 
ATOM   931  O  OE2 . GLU A 1 117 ? 12.264 -3.842  19.032  1.00 13.94 ? 117 GLU A OE2 1 
ATOM   932  N  N   . LEU A 1 118 ? 9.398  -4.229  14.260  1.00 9.69  ? 118 LEU A N   1 
ATOM   933  C  CA  . LEU A 1 118 ? 8.992  -2.992  13.599  1.00 10.03 ? 118 LEU A CA  1 
ATOM   934  C  C   . LEU A 1 118 ? 9.240  -1.851  14.578  1.00 8.69  ? 118 LEU A C   1 
ATOM   935  O  O   . LEU A 1 118 ? 8.842  -1.937  15.781  1.00 9.24  ? 118 LEU A O   1 
ATOM   936  C  CB  . LEU A 1 118 ? 7.501  -3.086  13.231  1.00 10.71 ? 118 LEU A CB  1 
ATOM   937  C  CG  . LEU A 1 118 ? 6.789  -1.769  12.938  1.00 10.71 ? 118 LEU A CG  1 
ATOM   938  C  CD1 . LEU A 1 118 ? 7.326  -1.098  11.660  1.00 10.75 ? 118 LEU A CD1 1 
ATOM   939  C  CD2 . LEU A 1 118 ? 5.298  -2.069  12.727  1.00 12.94 ? 118 LEU A CD2 1 
ATOM   940  N  N   . HIS A 1 119 ? 9.858  -0.761  14.114  1.00 9.01  ? 119 HIS A N   1 
ATOM   941  C  CA  . HIS A 1 119 ? 10.124 0.424   14.931  1.00 10.34 ? 119 HIS A CA  1 
ATOM   942  C  C   . HIS A 1 119 ? 9.406  1.602   14.279  1.00 10.62 ? 119 HIS A C   1 
ATOM   943  O  O   . HIS A 1 119 ? 9.759  1.991   13.155  1.00 10.48 ? 119 HIS A O   1 
ATOM   944  C  CB  . HIS A 1 119 ? 11.620 0.743   15.021  1.00 10.72 ? 119 HIS A CB  1 
ATOM   945  C  CG  . HIS A 1 119 ? 12.291 -0.278  15.876  1.00 13.31 ? 119 HIS A CG  1 
ATOM   946  N  ND1 . HIS A 1 119 ? 13.644 -0.499  15.840  1.00 11.76 ? 119 HIS A ND1 1 
ATOM   947  C  CD2 . HIS A 1 119 ? 11.760 -1.156  16.775  1.00 10.89 ? 119 HIS A CD2 1 
ATOM   948  C  CE1 . HIS A 1 119 ? 13.946 -1.476  16.705  1.00 9.56  ? 119 HIS A CE1 1 
ATOM   949  N  NE2 . HIS A 1 119 ? 12.819 -1.881  17.307  1.00 10.37 ? 119 HIS A NE2 1 
ATOM   950  N  N   . LEU A 1 120 ? 8.415  2.152   14.969  1.00 10.96 ? 120 LEU A N   1 
ATOM   951  C  CA  . LEU A 1 120 ? 7.770  3.381   14.516  1.00 9.82  ? 120 LEU A CA  1 
ATOM   952  C  C   . LEU A 1 120 ? 8.387  4.530   15.319  1.00 9.41  ? 120 LEU A C   1 
ATOM   953  O  O   . LEU A 1 120 ? 8.296  4.552   16.590  1.00 9.73  ? 120 LEU A O   1 
ATOM   954  C  CB  . LEU A 1 120 ? 6.259  3.302   14.734  1.00 10.06 ? 120 LEU A CB  1 
ATOM   955  C  CG  . LEU A 1 120 ? 5.576  2.242   13.866  1.00 10.62 ? 120 LEU A CG  1 
ATOM   956  C  CD1 . LEU A 1 120 ? 4.789  1.307   14.751  1.00 15.66 ? 120 LEU A CD1 1 
ATOM   957  C  CD2 . LEU A 1 120 ? 4.625  2.914   12.882  1.00 13.82 ? 120 LEU A CD2 1 
ATOM   958  N  N   . VAL A 1 121 ? 9.125  5.398   14.664  1.00 10.61 ? 121 VAL A N   1 
ATOM   959  C  CA  . VAL A 1 121 ? 9.973  6.399   15.313  1.00 9.38  ? 121 VAL A CA  1 
ATOM   960  C  C   . VAL A 1 121 ? 9.274  7.741   15.383  1.00 9.77  ? 121 VAL A C   1 
ATOM   961  O  O   . VAL A 1 121 ? 8.775  8.195   14.350  1.00 10.83 ? 121 VAL A O   1 
ATOM   962  C  CB  . VAL A 1 121 ? 11.301 6.531   14.538  1.00 11.39 ? 121 VAL A CB  1 
ATOM   963  C  CG1 . VAL A 1 121 ? 12.196 7.610   15.160  1.00 13.48 ? 121 VAL A CG1 1 
ATOM   964  C  CG2 . VAL A 1 121 ? 12.025 5.188   14.473  1.00 11.54 ? 121 VAL A CG2 1 
ATOM   965  N  N   . HIS A 1 122 ? 9.122  8.309   16.575  1.00 11.14 ? 122 HIS A N   1 
ATOM   966  C  CA  . HIS A 1 122 ? 8.446  9.586   16.767  1.00 10.99 ? 122 HIS A CA  1 
ATOM   967  C  C   . HIS A 1 122 ? 9.354  10.561  17.460  1.00 9.13  ? 122 HIS A C   1 
ATOM   968  O  O   . HIS A 1 122 ? 10.152 10.124  18.314  1.00 11.15 ? 122 HIS A O   1 
ATOM   969  C  CB  . HIS A 1 122 ? 7.222  9.431   17.682  1.00 11.07 ? 122 HIS A CB  1 
ATOM   970  C  CG  . HIS A 1 122 ? 6.342  8.289   17.296  1.00 9.87  ? 122 HIS A CG  1 
ATOM   971  N  ND1 . HIS A 1 122 ? 6.698  6.979   17.472  1.00 12.17 ? 122 HIS A ND1 1 
ATOM   972  C  CD2 . HIS A 1 122 ? 5.105  8.243   16.732  1.00 11.02 ? 122 HIS A CD2 1 
ATOM   973  C  CE1 . HIS A 1 122 ? 5.734  6.146   17.064  1.00 12.22 ? 122 HIS A CE1 1 
ATOM   974  N  NE2 . HIS A 1 122 ? 4.741  6.908   16.615  1.00 11.85 ? 122 HIS A NE2 1 
ATOM   975  N  N   . TRP A 1 123 ? 9.208  11.869  17.217  1.00 10.39 ? 123 TRP A N   1 
ATOM   976  C  CA  . TRP A 1 123 ? 10.053 12.850  17.898  1.00 10.81 ? 123 TRP A CA  1 
ATOM   977  C  C   . TRP A 1 123 ? 9.201  13.842  18.674  1.00 11.87 ? 123 TRP A C   1 
ATOM   978  O  O   . TRP A 1 123 ? 8.061  14.166  18.347  1.00 11.57 ? 123 TRP A O   1 
ATOM   979  C  CB  . TRP A 1 123 ? 10.959 13.598  16.932  1.00 12.31 ? 123 TRP A CB  1 
ATOM   980  C  CG  . TRP A 1 123 ? 10.224 14.132  15.721  1.00 11.57 ? 123 TRP A CG  1 
ATOM   981  C  CD1 . TRP A 1 123 ? 10.053 13.531  14.496  1.00 12.55 ? 123 TRP A CD1 1 
ATOM   982  C  CD2 . TRP A 1 123 ? 9.691  15.475  15.553  1.00 11.81 ? 123 TRP A CD2 1 
ATOM   983  N  NE1 . TRP A 1 123 ? 9.398  14.350  13.630  1.00 14.91 ? 123 TRP A NE1 1 
ATOM   984  C  CE2 . TRP A 1 123 ? 9.212  15.579  14.204  1.00 12.10 ? 123 TRP A CE2 1 
ATOM   985  C  CE3 . TRP A 1 123 ? 9.611  16.608  16.374  1.00 12.89 ? 123 TRP A CE3 1 
ATOM   986  C  CZ2 . TRP A 1 123 ? 8.610  16.747  13.719  1.00 15.23 ? 123 TRP A CZ2 1 
ATOM   987  C  CZ3 . TRP A 1 123 ? 9.020  17.759  15.899  1.00 13.06 ? 123 TRP A CZ3 1 
ATOM   988  C  CH2 . TRP A 1 123 ? 8.537  17.829  14.562  1.00 13.18 ? 123 TRP A CH2 1 
ATOM   989  N  N   . ASN A 1 124 ? 9.775  14.225  19.827  1.00 11.75 ? 124 ASN A N   1 
ATOM   990  C  CA  . ASN A 1 124 ? 9.104  15.137  20.741  1.00 12.53 ? 124 ASN A CA  1 
ATOM   991  C  C   . ASN A 1 124 ? 8.943  16.513  20.080  1.00 11.94 ? 124 ASN A C   1 
ATOM   992  O  O   . ASN A 1 124 ? 9.924  17.128  19.685  1.00 12.58 ? 124 ASN A O   1 
ATOM   993  C  CB  . ASN A 1 124 ? 9.978  15.264  21.999  1.00 13.07 ? 124 ASN A CB  1 
ATOM   994  C  CG  . ASN A 1 124 ? 9.265  15.941  23.143  1.00 12.74 ? 124 ASN A CG  1 
ATOM   995  O  OD1 . ASN A 1 124 ? 8.498  16.905  22.947  1.00 15.96 ? 124 ASN A OD1 1 
ATOM   996  N  ND2 . ASN A 1 124 ? 9.698  15.531  24.339  1.00 16.75 ? 124 ASN A ND2 1 
ATOM   997  N  N   . THR A 1 125 ? 7.697  16.989  19.943  1.00 13.56 ? 125 THR A N   1 
ATOM   998  C  CA  . THR A 1 125 ? 7.393  18.204  19.174  1.00 17.51 ? 125 THR A CA  1 
ATOM   999  C  C   . THR A 1 125 ? 8.023  19.446  19.816  1.00 17.13 ? 125 THR A C   1 
ATOM   1000 O  O   . THR A 1 125 ? 8.154  20.472  19.123  1.00 22.04 ? 125 THR A O   1 
ATOM   1001 C  CB  . THR A 1 125 ? 5.874  18.378  18.953  1.00 20.57 ? 125 THR A CB  1 
ATOM   1002 O  OG1 . THR A 1 125 ? 5.222  18.470  20.223  1.00 21.59 ? 125 THR A OG1 1 
ATOM   1003 C  CG2 . THR A 1 125 ? 5.289  17.215  18.184  1.00 21.79 ? 125 THR A CG2 1 
ATOM   1004 N  N   . LYS A 1 126 ? 8.552  19.226  21.196  1.00 17.84 ? 127 LYS A N   1 
ATOM   1005 C  CA  . LYS A 1 126 ? 9.239  20.425  21.707  1.00 18.79 ? 127 LYS A CA  1 
ATOM   1006 C  C   . LYS A 1 126 ? 10.488 20.774  20.885  1.00 20.75 ? 127 LYS A C   1 
ATOM   1007 O  O   . LYS A 1 126 ? 10.971 21.898  21.009  1.00 27.55 ? 127 LYS A O   1 
ATOM   1008 C  CB  . LYS A 1 126 ? 9.532  20.288  23.214  1.00 24.97 ? 127 LYS A CB  1 
ATOM   1009 C  CG  . LYS A 1 126 ? 10.470 19.178  23.619  1.00 27.64 ? 127 LYS A CG  1 
ATOM   1010 C  CD  . LYS A 1 126 ? 11.258 19.447  24.858  1.00 40.47 ? 127 LYS A CD  1 
ATOM   1011 C  CE  . LYS A 1 126 ? 10.650 18.872  26.112  1.00 37.08 ? 127 LYS A CE  1 
ATOM   1012 N  NZ  . LYS A 1 126 ? 11.683 18.817  27.178  1.00 32.22 ? 127 LYS A NZ  1 
ATOM   1013 N  N   . TYR A 1 127 ? 11.009 19.849  20.066  1.00 17.21 ? 128 TYR A N   1 
ATOM   1014 C  CA  . TYR A 1 127 ? 12.334 20.010  19.483  1.00 17.70 ? 128 TYR A CA  1 
ATOM   1015 C  C   . TYR A 1 127 ? 12.239 20.346  18.006  1.00 16.08 ? 128 TYR A C   1 
ATOM   1016 O  O   . TYR A 1 127 ? 13.252 20.599  17.376  1.00 18.06 ? 128 TYR A O   1 
ATOM   1017 C  CB  . TYR A 1 127 ? 13.222 18.791  19.728  1.00 17.63 ? 128 TYR A CB  1 
ATOM   1018 C  CG  . TYR A 1 127 ? 13.495 18.605  21.199  1.00 17.38 ? 128 TYR A CG  1 
ATOM   1019 C  CD1 . TYR A 1 127 ? 14.124 19.607  21.943  1.00 18.94 ? 128 TYR A CD1 1 
ATOM   1020 C  CD2 . TYR A 1 127 ? 13.193 17.407  21.839  1.00 16.04 ? 128 TYR A CD2 1 
ATOM   1021 C  CE1 . TYR A 1 127 ? 14.386 19.472  23.304  1.00 19.42 ? 128 TYR A CE1 1 
ATOM   1022 C  CE2 . TYR A 1 127 ? 13.495 17.249  23.190  1.00 17.68 ? 128 TYR A CE2 1 
ATOM   1023 C  CZ  . TYR A 1 127 ? 14.067 18.282  23.917  1.00 18.42 ? 128 TYR A CZ  1 
ATOM   1024 O  OH  . TYR A 1 127 ? 14.299 18.096  25.246  1.00 23.30 ? 128 TYR A OH  1 
ATOM   1025 N  N   . GLY A 1 128 ? 11.033 20.311  17.454  1.00 17.51 ? 129 GLY A N   1 
ATOM   1026 C  CA  . GLY A 1 128 ? 10.848 20.878  16.126  1.00 18.57 ? 129 GLY A CA  1 
ATOM   1027 C  C   . GLY A 1 128 ? 11.267 20.020  14.937  1.00 16.36 ? 129 GLY A C   1 
ATOM   1028 O  O   . GLY A 1 128 ? 10.751 20.243  13.858  1.00 21.86 ? 129 GLY A O   1 
ATOM   1029 N  N   A ASP A 1 129 ? 12.219 19.119  15.087  0.50 16.16 ? 130 ASP A N   1 
ATOM   1030 N  N   B ASP A 1 129 ? 12.141 19.025  15.182  0.50 16.85 ? 130 ASP A N   1 
ATOM   1031 C  CA  A ASP A 1 129 ? 12.435 18.129  14.042  0.50 16.17 ? 130 ASP A CA  1 
ATOM   1032 C  CA  B ASP A 1 129 ? 12.965 18.305  14.203  0.50 16.74 ? 130 ASP A CA  1 
ATOM   1033 C  C   A ASP A 1 129 ? 13.120 16.933  14.690  0.50 14.96 ? 130 ASP A C   1 
ATOM   1034 C  C   B ASP A 1 129 ? 13.407 16.927  14.716  0.50 15.03 ? 130 ASP A C   1 
ATOM   1035 O  O   A ASP A 1 129 ? 13.525 16.981  15.856  0.50 17.80 ? 130 ASP A O   1 
ATOM   1036 O  O   B ASP A 1 129 ? 13.979 16.816  15.812  0.50 14.08 ? 130 ASP A O   1 
ATOM   1037 C  CB  A ASP A 1 129 ? 13.126 18.758  12.820  0.50 14.04 ? 130 ASP A CB  1 
ATOM   1038 C  CB  B ASP A 1 129 ? 14.201 19.159  13.878  0.50 15.91 ? 130 ASP A CB  1 
ATOM   1039 C  CG  A ASP A 1 129 ? 14.600 19.049  13.061  0.50 17.95 ? 130 ASP A CG  1 
ATOM   1040 C  CG  B ASP A 1 129 ? 15.261 18.466  13.039  0.50 16.07 ? 130 ASP A CG  1 
ATOM   1041 O  OD1 A ASP A 1 129 ? 15.378 18.084  13.246  0.50 16.35 ? 130 ASP A OD1 1 
ATOM   1042 O  OD1 B ASP A 1 129 ? 14.974 18.241  11.867  0.50 16.76 ? 130 ASP A OD1 1 
ATOM   1043 O  OD2 A ASP A 1 129 ? 14.958 20.220  13.090  0.50 19.74 ? 130 ASP A OD2 1 
ATOM   1044 O  OD2 B ASP A 1 129 ? 16.348 18.129  13.572  0.50 18.89 ? 130 ASP A OD2 1 
ATOM   1045 N  N   . ALA A 1 130 ? 13.222 15.849  13.929  1.00 16.89 ? 131 ALA A N   1 
ATOM   1046 C  CA  . ALA A 1 130 ? 13.731 14.552  14.390  1.00 15.33 ? 131 ALA A CA  1 
ATOM   1047 C  C   . ALA A 1 130 ? 15.244 14.567  14.684  1.00 16.64 ? 131 ALA A C   1 
ATOM   1048 O  O   . ALA A 1 130 ? 15.695 14.060  15.730  1.00 17.97 ? 131 ALA A O   1 
ATOM   1049 C  CB  . ALA A 1 130 ? 13.393 13.479  13.375  1.00 17.84 ? 131 ALA A CB  1 
ATOM   1050 N  N   . GLY A 1 131 ? 16.034 15.268  13.872  1.00 20.13 ? 132 GLY A N   1 
ATOM   1051 C  CA  . GLY A 1 131 ? 17.476 15.364  14.107  1.00 22.97 ? 132 GLY A CA  1 
ATOM   1052 C  C   . GLY A 1 131 ? 17.782 16.038  15.437  1.00 21.32 ? 132 GLY A C   1 
ATOM   1053 O  O   . GLY A 1 131 ? 18.521 15.480  16.253  1.00 22.17 ? 132 GLY A O   1 
ATOM   1054 N  N   A LYS A 1 132 ? 17.205 17.230  15.658  0.50 22.04 ? 133 LYS A N   1 
ATOM   1055 N  N   B LYS A 1 132 ? 17.186 17.212  15.674  0.50 19.73 ? 133 LYS A N   1 
ATOM   1056 C  CA  A LYS A 1 132 ? 17.395 17.950  16.914  0.50 21.01 ? 133 LYS A CA  1 
ATOM   1057 C  CA  B LYS A 1 132 ? 17.420 17.934  16.919  0.50 19.07 ? 133 LYS A CA  1 
ATOM   1058 C  C   A LYS A 1 132 ? 16.927 17.085  18.080  0.50 14.74 ? 133 LYS A C   1 
ATOM   1059 C  C   B LYS A 1 132 ? 16.886 17.141  18.109  0.50 14.90 ? 133 LYS A C   1 
ATOM   1060 O  O   A LYS A 1 132 ? 17.588 17.010  19.128  0.50 16.49 ? 133 LYS A O   1 
ATOM   1061 O  O   B LYS A 1 132 ? 17.466 17.176  19.207  0.50 19.65 ? 133 LYS A O   1 
ATOM   1062 C  CB  A LYS A 1 132 ? 16.639 19.286  16.925  0.50 26.43 ? 133 LYS A CB  1 
ATOM   1063 C  CB  B LYS A 1 132 ? 16.780 19.324  16.856  0.50 19.27 ? 133 LYS A CB  1 
ATOM   1064 C  CG  A LYS A 1 132 ? 17.343 20.450  16.242  0.50 29.59 ? 133 LYS A CG  1 
ATOM   1065 C  CG  B LYS A 1 132 ? 17.491 20.306  15.943  0.50 19.83 ? 133 LYS A CG  1 
ATOM   1066 C  CD  A LYS A 1 132 ? 18.679 20.867  16.879  0.50 28.52 ? 133 LYS A CD  1 
ATOM   1067 C  CD  B LYS A 1 132 ? 19.002 20.215  16.043  0.50 20.30 ? 133 LYS A CD  1 
ATOM   1068 C  CE  A LYS A 1 132 ? 18.538 21.974  17.901  0.50 29.85 ? 133 LYS A CE  1 
ATOM   1069 C  CE  B LYS A 1 132 ? 19.692 21.097  15.019  0.50 22.86 ? 133 LYS A CE  1 
ATOM   1070 N  NZ  A LYS A 1 132 ? 19.846 22.545  18.303  0.50 32.55 ? 133 LYS A NZ  1 
ATOM   1071 N  NZ  B LYS A 1 132 ? 20.926 21.707  15.560  0.50 25.36 ? 133 LYS A NZ  1 
ATOM   1072 N  N   . ALA A 1 133 ? 15.780 16.423  17.893  1.00 14.78 ? 134 ALA A N   1 
ATOM   1073 C  CA  . ALA A 1 133 ? 15.211 15.604  18.957  1.00 15.69 ? 134 ALA A CA  1 
ATOM   1074 C  C   . ALA A 1 133 ? 16.155 14.489  19.380  1.00 14.88 ? 134 ALA A C   1 
ATOM   1075 O  O   . ALA A 1 133 ? 16.330 14.208  20.588  1.00 17.72 ? 134 ALA A O   1 
ATOM   1076 C  CB  . ALA A 1 133 ? 13.849 15.110  18.597  1.00 13.27 ? 134 ALA A CB  1 
ATOM   1077 N  N   . SER A 1 134 ? 16.858 13.931  18.415  1.00 19.29 ? 135 SER A N   1 
ATOM   1078 C  CA  . SER A 1 134 ? 17.737 12.810  18.691  1.00 18.63 ? 135 SER A CA  1 
ATOM   1079 C  C   . SER A 1 134 ? 18.961 13.194  19.533  1.00 20.36 ? 135 SER A C   1 
ATOM   1080 O  O   . SER A 1 134 ? 19.646 12.276  20.026  1.00 22.43 ? 135 SER A O   1 
ATOM   1081 C  CB  . SER A 1 134 ? 18.096 12.136  17.389  1.00 20.97 ? 135 SER A CB  1 
ATOM   1082 O  OG  . SER A 1 134 ? 19.148 12.821  16.698  1.00 23.24 ? 135 SER A OG  1 
ATOM   1083 N  N   . GLN A 1 135 ? 19.183 14.508  19.780  1.00 19.18 ? 136 GLN A N   1 
ATOM   1084 C  CA  . GLN A 1 135 ? 20.304 15.003  20.591  1.00 23.04 ? 136 GLN A CA  1 
ATOM   1085 C  C   . GLN A 1 135 ? 19.886 15.161  22.035  1.00 22.71 ? 136 GLN A C   1 
ATOM   1086 O  O   . GLN A 1 135 ? 20.687 15.605  22.869  1.00 22.82 ? 136 GLN A O   1 
ATOM   1087 C  CB  . GLN A 1 135 ? 20.731 16.428  20.227  1.00 23.81 ? 136 GLN A CB  1 
ATOM   1088 C  CG  . GLN A 1 135 ? 20.638 16.754  18.746  1.00 36.67 ? 136 GLN A CG  1 
ATOM   1089 C  CD  . GLN A 1 135 ? 21.693 16.049  17.948  1.00 39.50 ? 136 GLN A CD  1 
ATOM   1090 O  OE1 . GLN A 1 135 ? 22.044 14.909  18.241  1.00 55.50 ? 136 GLN A OE1 1 
ATOM   1091 N  NE2 . GLN A 1 135 ? 22.215 16.737  16.940  1.00 49.78 ? 136 GLN A NE2 1 
ATOM   1092 N  N   . GLN A 1 136 ? 18.622 14.902  22.305  1.00 17.12 ? 137 GLN A N   1 
ATOM   1093 C  CA  . GLN A 1 136 ? 18.090 15.182  23.634  1.00 19.13 ? 137 GLN A CA  1 
ATOM   1094 C  C   . GLN A 1 136 ? 17.666 13.898  24.311  1.00 19.34 ? 137 GLN A C   1 
ATOM   1095 O  O   . GLN A 1 136 ? 17.111 13.027  23.666  1.00 17.15 ? 137 GLN A O   1 
ATOM   1096 C  CB  . GLN A 1 136 ? 16.902 16.134  23.527  1.00 17.77 ? 137 GLN A CB  1 
ATOM   1097 C  CG  . GLN A 1 136 ? 17.306 17.472  22.914  1.00 27.25 ? 137 GLN A CG  1 
ATOM   1098 C  CD  . GLN A 1 136 ? 18.259 18.251  23.801  1.00 38.05 ? 137 GLN A CD  1 
ATOM   1099 O  OE1 . GLN A 1 136 ? 18.246 18.212  25.038  1.00 46.99 ? 137 GLN A OE1 1 
ATOM   1100 N  NE2 . GLN A 1 136 ? 19.126 18.967  23.139  1.00 29.62 ? 137 GLN A NE2 1 
ATOM   1101 N  N   . PRO A 1 137 ? 17.789 13.821  25.658  1.00 18.68 ? 138 PRO A N   1 
ATOM   1102 C  CA  . PRO A 1 137 ? 17.442 12.609  26.405  1.00 18.06 ? 138 PRO A CA  1 
ATOM   1103 C  C   . PRO A 1 137 ? 15.979 12.192  26.308  1.00 17.00 ? 138 PRO A C   1 
ATOM   1104 O  O   . PRO A 1 137 ? 15.679 11.001  26.447  1.00 21.24 ? 138 PRO A O   1 
ATOM   1105 C  CB  . PRO A 1 137 ? 17.895 12.892  27.858  1.00 21.82 ? 138 PRO A CB  1 
ATOM   1106 C  CG  . PRO A 1 137 ? 17.839 14.397  27.898  1.00 31.45 ? 138 PRO A CG  1 
ATOM   1107 C  CD  . PRO A 1 137 ? 18.382 14.838  26.551  1.00 21.99 ? 138 PRO A CD  1 
ATOM   1108 N  N   . ASP A 1 138 ? 15.099 13.185  26.052  1.00 16.18 ? 139 ASP A N   1 
ATOM   1109 C  CA  . ASP A 1 138 ? 13.685 12.946  25.957  1.00 15.92 ? 139 ASP A CA  1 
ATOM   1110 C  C   . ASP A 1 138 ? 13.222 13.162  24.517  1.00 14.95 ? 139 ASP A C   1 
ATOM   1111 O  O   . ASP A 1 138 ? 12.068 13.497  24.301  1.00 15.98 ? 139 ASP A O   1 
ATOM   1112 C  CB  . ASP A 1 138 ? 12.943 13.831  26.964  1.00 17.04 ? 139 ASP A CB  1 
ATOM   1113 C  CG  . ASP A 1 138 ? 13.074 15.313  26.697  1.00 19.44 ? 139 ASP A CG  1 
ATOM   1114 O  OD1 . ASP A 1 138 ? 14.008 15.699  25.950  1.00 20.52 ? 139 ASP A OD1 1 
ATOM   1115 O  OD2 . ASP A 1 138 ? 12.276 16.082  27.303  1.00 26.03 ? 139 ASP A OD2 1 
ATOM   1116 N  N   . GLY A 1 139 ? 14.145 12.974  23.573  1.00 13.40 ? 140 GLY A N   1 
ATOM   1117 C  CA  . GLY A 1 139 ? 13.875 13.443  22.213  1.00 13.11 ? 140 GLY A CA  1 
ATOM   1118 C  C   . GLY A 1 139 ? 12.970 12.523  21.386  1.00 12.37 ? 140 GLY A C   1 
ATOM   1119 O  O   . GLY A 1 139 ? 12.148 13.011  20.568  1.00 13.27 ? 140 GLY A O   1 
ATOM   1120 N  N   . LEU A 1 140 ? 13.063 11.215  21.582  1.00 11.13 ? 141 LEU A N   1 
ATOM   1121 C  CA  . LEU A 1 140 ? 12.346 10.323  20.661  1.00 10.35 ? 141 LEU A CA  1 
ATOM   1122 C  C   . LEU A 1 140 ? 11.527 9.341   21.487  1.00 10.73 ? 141 LEU A C   1 
ATOM   1123 O  O   . LEU A 1 140 ? 11.862 9.007   22.641  1.00 12.04 ? 141 LEU A O   1 
ATOM   1124 C  CB  . LEU A 1 140 ? 13.352 9.503   19.838  1.00 12.50 ? 141 LEU A CB  1 
ATOM   1125 C  CG  . LEU A 1 140 ? 14.311 10.273  18.910  1.00 14.62 ? 141 LEU A CG  1 
ATOM   1126 C  CD1 . LEU A 1 140 ? 15.108 9.291   18.038  1.00 13.82 ? 141 LEU A CD1 1 
ATOM   1127 C  CD2 . LEU A 1 140 ? 13.561 11.236  17.963  1.00 13.95 ? 141 LEU A CD2 1 
ATOM   1128 N  N   . ALA A 1 141 ? 10.472 8.806   20.891  1.00 11.58 ? 142 ALA A N   1 
ATOM   1129 C  CA  . ALA A 1 141 ? 9.725  7.684   21.431  1.00 11.49 ? 142 ALA A CA  1 
ATOM   1130 C  C   . ALA A 1 141 ? 9.613  6.677   20.300  1.00 10.58 ? 142 ALA A C   1 
ATOM   1131 O  O   . ALA A 1 141 ? 9.171  7.030   19.171  1.00 11.46 ? 142 ALA A O   1 
ATOM   1132 C  CB  . ALA A 1 141 ? 8.368  8.101   21.958  1.00 12.80 ? 142 ALA A CB  1 
ATOM   1133 N  N   . VAL A 1 142 ? 10.013 5.420   20.537  1.00 10.91 ? 143 VAL A N   1 
ATOM   1134 C  CA  . VAL A 1 142 ? 9.936  4.401   19.498  1.00 10.80 ? 143 VAL A CA  1 
ATOM   1135 C  C   . VAL A 1 142 ? 8.923  3.386   19.973  1.00 10.21 ? 143 VAL A C   1 
ATOM   1136 O  O   . VAL A 1 142 ? 9.043  2.866   21.080  1.00 11.49 ? 143 VAL A O   1 
ATOM   1137 C  CB  . VAL A 1 142 ? 11.285 3.753   19.134  1.00 11.64 ? 143 VAL A CB  1 
ATOM   1138 C  CG1 . VAL A 1 142 ? 11.092 2.729   18.006  1.00 12.91 ? 143 VAL A CG1 1 
ATOM   1139 C  CG2 . VAL A 1 142 ? 12.283 4.828   18.729  1.00 14.46 ? 143 VAL A CG2 1 
ATOM   1140 N  N   . LEU A 1 143 ? 7.882  3.166   19.174  1.00 10.50 ? 144 LEU A N   1 
ATOM   1141 C  CA  . LEU A 1 143 ? 6.918  2.111   19.395  1.00 10.41 ? 144 LEU A CA  1 
ATOM   1142 C  C   . LEU A 1 143 ? 7.432  0.860   18.697  1.00 11.65 ? 144 LEU A C   1 
ATOM   1143 O  O   . LEU A 1 143 ? 7.605  0.841   17.459  1.00 11.55 ? 144 LEU A O   1 
ATOM   1144 C  CB  . LEU A 1 143 ? 5.589  2.543   18.781  1.00 12.14 ? 144 LEU A CB  1 
ATOM   1145 C  CG  . LEU A 1 143 ? 4.445  1.573   18.978  1.00 13.07 ? 144 LEU A CG  1 
ATOM   1146 C  CD1 . LEU A 1 143 ? 4.133  1.453   20.469  1.00 17.18 ? 144 LEU A CD1 1 
ATOM   1147 C  CD2 . LEU A 1 143 ? 3.260  2.181   18.250  1.00 18.08 ? 144 LEU A CD2 1 
ATOM   1148 N  N   . GLY A 1 144 ? 7.786  -0.167  19.471  1.00 11.93 ? 145 GLY A N   1 
ATOM   1149 C  CA  . GLY A 1 144 ? 8.334  -1.396  18.936  1.00 10.14 ? 145 GLY A CA  1 
ATOM   1150 C  C   . GLY A 1 144 ? 7.307  -2.501  18.947  1.00 11.42 ? 145 GLY A C   1 
ATOM   1151 O  O   . GLY A 1 144 ? 6.591  -2.675  19.926  1.00 11.88 ? 145 GLY A O   1 
ATOM   1152 N  N   . ILE A 1 145 ? 7.209  -3.205  17.817  1.00 9.57  ? 146 ILE A N   1 
ATOM   1153 C  CA  . ILE A 1 145 ? 6.241  -4.266  17.647  1.00 10.86 ? 146 ILE A CA  1 
ATOM   1154 C  C   . ILE A 1 145 ? 6.965  -5.509  17.160  1.00 9.71  ? 146 ILE A C   1 
ATOM   1155 O  O   . ILE A 1 145 ? 7.671  -5.463  16.142  1.00 11.39 ? 146 ILE A O   1 
ATOM   1156 C  CB  . ILE A 1 145 ? 5.144  -3.803  16.693  1.00 9.68  ? 146 ILE A CB  1 
ATOM   1157 C  CG1 . ILE A 1 145 ? 4.474  -2.535  17.233  1.00 11.83 ? 146 ILE A CG1 1 
ATOM   1158 C  CG2 . ILE A 1 145 ? 4.167  -4.924  16.410  1.00 13.76 ? 146 ILE A CG2 1 
ATOM   1159 C  CD1 . ILE A 1 145 ? 3.430  -1.957  16.380  1.00 12.28 ? 146 ILE A CD1 1 
ATOM   1160 N  N   . PHE A 1 146 ? 6.732  -6.643  17.818  1.00 11.02 ? 147 PHE A N   1 
ATOM   1161 C  CA  . PHE A 1 146 ? 7.358  -7.878  17.360  1.00 11.29 ? 147 PHE A CA  1 
ATOM   1162 C  C   . PHE A 1 146 ? 6.602  -8.482  16.180  1.00 9.86  ? 147 PHE A C   1 
ATOM   1163 O  O   . PHE A 1 146 ? 5.386  -8.363  16.143  1.00 11.27 ? 147 PHE A O   1 
ATOM   1164 C  CB  . PHE A 1 146 ? 7.369  -8.854  18.542  1.00 10.13 ? 147 PHE A CB  1 
ATOM   1165 C  CG  . PHE A 1 146 ? 8.241  -8.388  19.672  1.00 9.73  ? 147 PHE A CG  1 
ATOM   1166 C  CD1 . PHE A 1 146 ? 9.608  -8.248  19.508  1.00 10.04 ? 147 PHE A CD1 1 
ATOM   1167 C  CD2 . PHE A 1 146 ? 7.652  -8.067  20.905  1.00 10.33 ? 147 PHE A CD2 1 
ATOM   1168 C  CE1 . PHE A 1 146 ? 10.401 -7.873  20.593  1.00 10.60 ? 147 PHE A CE1 1 
ATOM   1169 C  CE2 . PHE A 1 146 ? 8.445  -7.676  21.958  1.00 13.08 ? 147 PHE A CE2 1 
ATOM   1170 C  CZ  . PHE A 1 146 ? 9.795  -7.595  21.789  1.00 10.33 ? 147 PHE A CZ  1 
ATOM   1171 N  N   . LEU A 1 147 ? 7.330  -9.215  15.294  1.00 10.11 ? 148 LEU A N   1 
ATOM   1172 C  CA  . LEU A 1 147 ? 6.685  -9.944  14.216  1.00 10.26 ? 148 LEU A CA  1 
ATOM   1173 C  C   . LEU A 1 147 ? 6.984  -11.431 14.399  1.00 10.95 ? 148 LEU A C   1 
ATOM   1174 O  O   . LEU A 1 147 ? 8.154  -11.799 14.505  1.00 12.58 ? 148 LEU A O   1 
ATOM   1175 C  CB  . LEU A 1 147 ? 7.256  -9.536  12.849  1.00 11.69 ? 148 LEU A CB  1 
ATOM   1176 C  CG  . LEU A 1 147 ? 6.689  -8.259  12.226  1.00 10.19 ? 148 LEU A CG  1 
ATOM   1177 C  CD1 . LEU A 1 147 ? 6.922  -7.002  13.107  1.00 12.82 ? 148 LEU A CD1 1 
ATOM   1178 C  CD2 . LEU A 1 147 ? 7.316  -8.058  10.867  1.00 10.88 ? 148 LEU A CD2 1 
ATOM   1179 N  N   . LYS A 1 148 ? 5.896  -12.226 14.511  1.00 13.44 ? 149 LYS A N   1 
ATOM   1180 C  CA  . LYS A 1 148 ? 6.067  -13.659 14.543  1.00 13.44 ? 149 LYS A CA  1 
ATOM   1181 C  C   . LYS A 1 148 ? 5.586  -14.205 13.197  1.00 13.43 ? 149 LYS A C   1 
ATOM   1182 O  O   . LYS A 1 148 ? 4.699  -13.620 12.606  1.00 16.84 ? 149 LYS A O   1 
ATOM   1183 C  CB  . LYS A 1 148 ? 5.298  -14.275 15.710  1.00 16.32 ? 149 LYS A CB  1 
ATOM   1184 C  CG  . LYS A 1 148 ? 3.807  -14.360 15.621  1.00 20.85 ? 149 LYS A CG  1 
ATOM   1185 C  CD  . LYS A 1 148 ? 3.214  -15.099 16.850  1.00 29.37 ? 149 LYS A CD  1 
ATOM   1186 C  CE  . LYS A 1 148 ? 1.707  -15.000 16.945  1.00 35.19 ? 149 LYS A CE  1 
ATOM   1187 N  NZ  . LYS A 1 148 ? 1.146  -15.767 18.091  1.00 47.70 ? 149 LYS A NZ  1 
ATOM   1188 N  N   . VAL A 1 149 ? 6.087  -15.373 12.821  1.00 13.24 ? 150 VAL A N   1 
ATOM   1189 C  CA  . VAL A 1 149 ? 5.704  -15.912 11.539  1.00 12.98 ? 150 VAL A CA  1 
ATOM   1190 C  C   . VAL A 1 149 ? 4.531  -16.873 11.777  1.00 14.63 ? 150 VAL A C   1 
ATOM   1191 O  O   . VAL A 1 149 ? 4.597  -17.836 12.547  1.00 15.54 ? 150 VAL A O   1 
ATOM   1192 C  CB  . VAL A 1 149 ? 6.905  -16.637 10.898  1.00 13.00 ? 150 VAL A CB  1 
ATOM   1193 C  CG1 . VAL A 1 149 ? 6.523  -17.469 9.695   1.00 16.19 ? 150 VAL A CG1 1 
ATOM   1194 C  CG2 . VAL A 1 149 ? 7.971  -15.628 10.486  1.00 14.80 ? 150 VAL A CG2 1 
ATOM   1195 N  N   . GLY A 1 150 ? 3.478  -16.674 10.983  1.00 15.82 ? 151 GLY A N   1 
ATOM   1196 C  CA  . GLY A 1 150 ? 2.264  -17.478 11.082  1.00 17.50 ? 151 GLY A CA  1 
ATOM   1197 C  C   . GLY A 1 150 ? 1.300  -17.031 9.986   1.00 13.89 ? 151 GLY A C   1 
ATOM   1198 O  O   . GLY A 1 150 ? 1.681  -17.024 8.790   1.00 16.56 ? 151 GLY A O   1 
ATOM   1199 N  N   . SER A 1 151 ? 0.132  -16.520 10.369  1.00 16.36 ? 152 SER A N   1 
ATOM   1200 C  CA  . SER A 1 151 ? -0.781 -15.967 9.358   1.00 14.73 ? 152 SER A CA  1 
ATOM   1201 C  C   . SER A 1 151 ? -0.230 -14.633 8.860   1.00 13.03 ? 152 SER A C   1 
ATOM   1202 O  O   . SER A 1 151 ? 0.581  -13.996 9.533   1.00 13.97 ? 152 SER A O   1 
ATOM   1203 C  CB  . SER A 1 151 ? -2.171 -15.792 9.908   1.00 25.18 ? 152 SER A CB  1 
ATOM   1204 O  OG  . SER A 1 151 ? -2.212 -14.754 10.846  1.00 31.95 ? 152 SER A OG  1 
ATOM   1205 N  N   . ALA A 1 152 ? -0.609 -14.239 7.633   1.00 16.57 ? 153 ALA A N   1 
ATOM   1206 C  CA  . ALA A 1 152 ? -0.149 -12.995 7.045   1.00 13.58 ? 153 ALA A CA  1 
ATOM   1207 C  C   . ALA A 1 152 ? -0.749 -11.782 7.772   1.00 14.00 ? 153 ALA A C   1 
ATOM   1208 O  O   . ALA A 1 152 ? -1.832 -11.879 8.392   1.00 16.30 ? 153 ALA A O   1 
ATOM   1209 C  CB  . ALA A 1 152 ? -0.499 -12.962 5.583   1.00 17.92 ? 153 ALA A CB  1 
ATOM   1210 N  N   . LYS A 1 153 ? -0.040 -10.633 7.652   1.00 12.69 ? 154 LYS A N   1 
ATOM   1211 C  CA  . LYS A 1 153 ? -0.574 -9.363  8.131   1.00 13.70 ? 154 LYS A CA  1 
ATOM   1212 C  C   . LYS A 1 153 ? -1.034 -8.618  6.887   1.00 12.72 ? 154 LYS A C   1 
ATOM   1213 O  O   . LYS A 1 153 ? -0.182 -8.117  6.148   1.00 12.70 ? 154 LYS A O   1 
ATOM   1214 C  CB  . LYS A 1 153 ? 0.463  -8.583  8.962   1.00 14.29 ? 154 LYS A CB  1 
ATOM   1215 C  CG  . LYS A 1 153 ? -0.103 -7.329  9.608   1.00 12.84 ? 154 LYS A CG  1 
ATOM   1216 C  CD  . LYS A 1 153 ? -0.986 -7.705  10.781  1.00 16.61 ? 154 LYS A CD  1 
ATOM   1217 C  CE  . LYS A 1 153 ? -1.320 -6.493  11.609  1.00 17.08 ? 154 LYS A CE  1 
ATOM   1218 N  NZ  . LYS A 1 153 ? -2.094 -6.883  12.802  1.00 22.74 ? 154 LYS A NZ  1 
ATOM   1219 N  N   . PRO A 1 154 ? -2.336 -8.504  6.573   1.00 12.87 ? 155 PRO A N   1 
ATOM   1220 C  CA  . PRO A 1 154 ? -2.697 -7.912  5.275   1.00 12.31 ? 155 PRO A CA  1 
ATOM   1221 C  C   . PRO A 1 154 ? -2.179 -6.483  5.132   1.00 12.10 ? 155 PRO A C   1 
ATOM   1222 O  O   . PRO A 1 154 ? -1.847 -6.033  4.032   1.00 14.17 ? 155 PRO A O   1 
ATOM   1223 C  CB  . PRO A 1 154 ? -4.217 -7.977  5.323   1.00 17.38 ? 155 PRO A CB  1 
ATOM   1224 C  CG  . PRO A 1 154 ? -4.484 -9.213  6.156   1.00 17.54 ? 155 PRO A CG  1 
ATOM   1225 C  CD  . PRO A 1 154 ? -3.507 -9.059  7.282   1.00 14.42 ? 155 PRO A CD  1 
ATOM   1226 N  N   . GLY A 1 155 ? -2.104 -5.755  6.261   1.00 12.00 ? 156 GLY A N   1 
ATOM   1227 C  CA  . GLY A 1 155 ? -1.710 -4.356  6.238   1.00 11.29 ? 156 GLY A CA  1 
ATOM   1228 C  C   . GLY A 1 155 ? -0.228 -4.160  5.921   1.00 12.43 ? 156 GLY A C   1 
ATOM   1229 O  O   . GLY A 1 155 ? 0.203  -3.004  5.704   1.00 14.76 ? 156 GLY A O   1 
ATOM   1230 N  N   . LEU A 1 156 ? 0.539  -5.260  6.017   1.00 12.09 ? 157 LEU A N   1 
ATOM   1231 C  CA  . LEU A 1 156 ? 1.947  -5.210  5.650   1.00 12.71 ? 157 LEU A CA  1 
ATOM   1232 C  C   . LEU A 1 156 ? 2.176  -5.406  4.143   1.00 12.71 ? 157 LEU A C   1 
ATOM   1233 O  O   . LEU A 1 156 ? 3.260  -5.155  3.630   1.00 11.48 ? 157 LEU A O   1 
ATOM   1234 C  CB  . LEU A 1 156 ? 2.693  -6.260  6.480   1.00 11.98 ? 157 LEU A CB  1 
ATOM   1235 C  CG  . LEU A 1 156 ? 4.206  -6.442  6.221   1.00 12.75 ? 157 LEU A CG  1 
ATOM   1236 C  CD1 . LEU A 1 156 ? 4.990  -5.178  6.589   1.00 14.80 ? 157 LEU A CD1 1 
ATOM   1237 C  CD2 . LEU A 1 156 ? 4.779  -7.631  6.946   1.00 15.58 ? 157 LEU A CD2 1 
ATOM   1238 N  N   . GLN A 1 157 ? 1.152  -5.885  3.435   1.00 11.94 ? 158 GLN A N   1 
ATOM   1239 C  CA  . GLN A 1 157 ? 1.408  -6.385  2.098   1.00 13.85 ? 158 GLN A CA  1 
ATOM   1240 C  C   . GLN A 1 157 ? 1.854  -5.260  1.167   1.00 13.08 ? 158 GLN A C   1 
ATOM   1241 O  O   . GLN A 1 157 ? 2.701  -5.505  0.308   1.00 12.94 ? 158 GLN A O   1 
ATOM   1242 C  CB  . GLN A 1 157 ? 0.167  -7.114  1.573   1.00 13.31 ? 158 GLN A CB  1 
ATOM   1243 C  CG  . GLN A 1 157 ? 0.482  -7.929  0.306   1.00 14.48 ? 158 GLN A CG  1 
ATOM   1244 C  CD  . GLN A 1 157 ? 1.522  -9.009  0.563   1.00 15.25 ? 158 GLN A CD  1 
ATOM   1245 O  OE1 . GLN A 1 157 ? 1.677  -9.562  1.655   1.00 16.19 ? 158 GLN A OE1 1 
ATOM   1246 N  NE2 . GLN A 1 157 ? 2.290  -9.341  -0.442  1.00 15.13 ? 158 GLN A NE2 1 
ATOM   1247 N  N   . LYS A 1 158 ? 1.326  -4.028  1.299   1.00 10.77 ? 159 LYS A N   1 
ATOM   1248 C  CA  . LYS A 1 158 ? 1.715  -2.910  0.436   1.00 12.56 ? 159 LYS A CA  1 
ATOM   1249 C  C   . LYS A 1 158 ? 3.220  -2.724  0.504   1.00 12.89 ? 159 LYS A C   1 
ATOM   1250 O  O   . LYS A 1 158 ? 3.868  -2.364  -0.465  1.00 13.38 ? 159 LYS A O   1 
ATOM   1251 C  CB  . LYS A 1 158 ? 0.942  -1.641  0.809   1.00 16.08 ? 159 LYS A CB  1 
ATOM   1252 C  CG  . LYS A 1 158 ? 1.108  -0.425  -0.103  1.00 25.25 ? 159 LYS A CG  1 
ATOM   1253 C  CD  . LYS A 1 158 ? 0.233  0.794   0.296   1.00 23.86 ? 159 LYS A CD  1 
ATOM   1254 C  CE  . LYS A 1 158 ? 0.620  2.082   -0.422  1.00 32.08 ? 159 LYS A CE  1 
ATOM   1255 N  NZ  . LYS A 1 158 ? 0.062  2.074   -1.800  1.00 26.24 ? 159 LYS A NZ  1 
ATOM   1256 N  N   . VAL A 1 159 ? 3.769  -2.865  1.737   1.00 12.12 ? 160 VAL A N   1 
ATOM   1257 C  CA  . VAL A 1 159 ? 5.211  -2.710  1.935   1.00 12.05 ? 160 VAL A CA  1 
ATOM   1258 C  C   . VAL A 1 159 ? 5.955  -3.837  1.213   1.00 10.71 ? 160 VAL A C   1 
ATOM   1259 O  O   . VAL A 1 159 ? 6.881  -3.607  0.423   1.00 14.97 ? 160 VAL A O   1 
ATOM   1260 C  CB  . VAL A 1 159 ? 5.578  -2.708  3.425   1.00 12.12 ? 160 VAL A CB  1 
ATOM   1261 C  CG1 . VAL A 1 159 ? 7.082  -2.795  3.616   1.00 15.57 ? 160 VAL A CG1 1 
ATOM   1262 C  CG2 . VAL A 1 159 ? 5.037  -1.446  4.039   1.00 16.35 ? 160 VAL A CG2 1 
ATOM   1263 N  N   . VAL A 1 160 ? 5.573  -5.076  1.489   1.00 12.64 ? 161 VAL A N   1 
ATOM   1264 C  CA  . VAL A 1 160 ? 6.247  -6.251  0.935   1.00 14.57 ? 161 VAL A CA  1 
ATOM   1265 C  C   . VAL A 1 160 ? 6.298  -6.163  -0.587  1.00 14.84 ? 161 VAL A C   1 
ATOM   1266 O  O   . VAL A 1 160 ? 7.318  -6.501  -1.190  1.00 14.20 ? 161 VAL A O   1 
ATOM   1267 C  CB  . VAL A 1 160 ? 5.524  -7.539  1.416   1.00 19.42 ? 161 VAL A CB  1 
ATOM   1268 C  CG1 . VAL A 1 160 ? 5.767  -8.764  0.572   1.00 20.62 ? 161 VAL A CG1 1 
ATOM   1269 C  CG2 . VAL A 1 160 ? 5.940  -7.728  2.871   1.00 23.04 ? 161 VAL A CG2 1 
ATOM   1270 N  N   . ASP A 1 161 ? 5.195  -5.691  -1.178  1.00 12.28 ? 162 ASP A N   1 
ATOM   1271 C  CA  . ASP A 1 161 ? 5.061  -5.799  -2.622  1.00 15.50 ? 162 ASP A CA  1 
ATOM   1272 C  C   . ASP A 1 161 ? 5.918  -4.789  -3.380  1.00 15.14 ? 162 ASP A C   1 
ATOM   1273 O  O   . ASP A 1 161 ? 6.148  -4.986  -4.561  1.00 18.79 ? 162 ASP A O   1 
ATOM   1274 C  CB  . ASP A 1 161 ? 3.602  -5.674  -3.032  1.00 17.04 ? 162 ASP A CB  1 
ATOM   1275 C  CG  . ASP A 1 161 ? 2.834  -6.989  -2.914  1.00 19.18 ? 162 ASP A CG  1 
ATOM   1276 O  OD1 . ASP A 1 161 ? 3.452  -8.082  -3.012  1.00 24.15 ? 162 ASP A OD1 1 
ATOM   1277 O  OD2 . ASP A 1 161 ? 1.602  -6.916  -2.729  1.00 23.56 ? 162 ASP A OD2 1 
ATOM   1278 N  N   . VAL A 1 162 ? 6.432  -3.750  -2.710  1.00 13.33 ? 163 VAL A N   1 
ATOM   1279 C  CA  . VAL A 1 162 ? 7.286  -2.777  -3.354  1.00 13.75 ? 163 VAL A CA  1 
ATOM   1280 C  C   . VAL A 1 162 ? 8.763  -3.043  -3.109  1.00 12.84 ? 163 VAL A C   1 
ATOM   1281 O  O   . VAL A 1 162 ? 9.587  -2.358  -3.694  1.00 13.70 ? 163 VAL A O   1 
ATOM   1282 C  CB  . VAL A 1 162 ? 6.945  -1.307  -3.043  1.00 18.13 ? 163 VAL A CB  1 
ATOM   1283 C  CG1 . VAL A 1 162 ? 5.501  -1.051  -3.446  1.00 20.97 ? 163 VAL A CG1 1 
ATOM   1284 C  CG2 . VAL A 1 162 ? 7.287  -0.953  -1.577  1.00 16.47 ? 163 VAL A CG2 1 
ATOM   1285 N  N   . LEU A 1 163 ? 9.100  -4.044  -2.301  1.00 11.88 ? 164 LEU A N   1 
ATOM   1286 C  CA  . LEU A 1 163 ? 10.479 -4.191  -1.896  1.00 12.75 ? 164 LEU A CA  1 
ATOM   1287 C  C   . LEU A 1 163 ? 11.346 -4.592  -3.089  1.00 14.90 ? 164 LEU A C   1 
ATOM   1288 O  O   . LEU A 1 163 ? 12.506 -4.241  -3.169  1.00 13.35 ? 164 LEU A O   1 
ATOM   1289 C  CB  . LEU A 1 163 ? 10.594 -5.194  -0.756  1.00 13.49 ? 164 LEU A CB  1 
ATOM   1290 C  CG  . LEU A 1 163 ? 10.055 -4.730  0.608   1.00 13.03 ? 164 LEU A CG  1 
ATOM   1291 C  CD1 . LEU A 1 163 ? 10.322 -5.809  1.605   1.00 15.87 ? 164 LEU A CD1 1 
ATOM   1292 C  CD2 . LEU A 1 163 ? 10.636 -3.411  1.021   1.00 14.04 ? 164 LEU A CD2 1 
ATOM   1293 N  N   . ASP A 1 164 ? 10.745 -5.210  -4.112  1.00 14.95 ? 165 ASP A N   1 
ATOM   1294 C  CA  . ASP A 1 164 ? 11.543 -5.598  -5.285  1.00 15.45 ? 165 ASP A CA  1 
ATOM   1295 C  C   . ASP A 1 164 ? 12.062 -4.351  -6.000  1.00 16.33 ? 165 ASP A C   1 
ATOM   1296 O  O   . ASP A 1 164 ? 13.033 -4.442  -6.785  1.00 19.52 ? 165 ASP A O   1 
ATOM   1297 C  CB  . ASP A 1 164 ? 10.708 -6.450  -6.244  1.00 22.52 ? 165 ASP A CB  1 
ATOM   1298 C  CG  . ASP A 1 164 ? 9.692  -5.591  -6.997  1.00 33.09 ? 165 ASP A CG  1 
ATOM   1299 O  OD1 . ASP A 1 164 ? 8.749  -5.050  -6.328  1.00 35.43 ? 165 ASP A OD1 1 
ATOM   1300 O  OD2 . ASP A 1 164 ? 9.856  -5.431  -8.249  1.00 38.49 ? 165 ASP A OD2 1 
ATOM   1301 N  N   . SER A 1 165 ? 11.401 -3.201  -5.805  1.00 14.71 ? 166 SER A N   1 
ATOM   1302 C  CA  . SER A 1 165 ? 11.765 -1.947  -6.449  1.00 15.04 ? 166 SER A CA  1 
ATOM   1303 C  C   . SER A 1 165 ? 12.889 -1.208  -5.703  1.00 14.59 ? 166 SER A C   1 
ATOM   1304 O  O   . SER A 1 165 ? 13.399 -0.196  -6.163  1.00 15.82 ? 166 SER A O   1 
ATOM   1305 C  CB  . SER A 1 165 ? 10.544 -1.046  -6.656  1.00 18.06 ? 166 SER A CB  1 
ATOM   1306 O  OG  . SER A 1 165 ? 10.204 -0.422  -5.431  1.00 18.09 ? 166 SER A OG  1 
ATOM   1307 N  N   . ILE A 1 166 ? 13.226 -1.661  -4.474  1.00 12.41 ? 167 ILE A N   1 
ATOM   1308 C  CA  . ILE A 1 166 ? 14.276 -0.979  -3.720  1.00 13.28 ? 167 ILE A CA  1 
ATOM   1309 C  C   . ILE A 1 166 ? 15.276 -2.011  -3.216  1.00 10.55 ? 167 ILE A C   1 
ATOM   1310 O  O   . ILE A 1 166 ? 15.733 -1.989  -2.068  1.00 11.32 ? 167 ILE A O   1 
ATOM   1311 C  CB  . ILE A 1 166 ? 13.675 -0.109  -2.603  1.00 12.47 ? 167 ILE A CB  1 
ATOM   1312 C  CG1 . ILE A 1 166 ? 12.890 -0.942  -1.607  1.00 11.80 ? 167 ILE A CG1 1 
ATOM   1313 C  CG2 . ILE A 1 166 ? 12.812 1.020   -3.160  1.00 15.24 ? 167 ILE A CG2 1 
ATOM   1314 C  CD1 . ILE A 1 166 ? 12.841 -0.315  -0.173  1.00 13.36 ? 167 ILE A CD1 1 
ATOM   1315 N  N   . LYS A 1 167 ? 15.714 -2.910  -4.083  1.00 13.07 ? 168 LYS A N   1 
ATOM   1316 C  CA  . LYS A 1 167 ? 16.554 -4.026  -3.661  1.00 12.76 ? 168 LYS A CA  1 
ATOM   1317 C  C   . LYS A 1 167 ? 17.878 -3.585  -3.061  1.00 13.50 ? 168 LYS A C   1 
ATOM   1318 O  O   . LYS A 1 167 ? 18.344 -4.243  -2.116  1.00 12.31 ? 168 LYS A O   1 
ATOM   1319 C  CB  . LYS A 1 167 ? 16.782 -4.960  -4.859  1.00 15.28 ? 168 LYS A CB  1 
ATOM   1320 C  CG  . LYS A 1 167 ? 17.467 -6.278  -4.499  1.00 17.84 ? 168 LYS A CG  1 
ATOM   1321 C  CD  . LYS A 1 167 ? 17.758 -7.102  -5.731  1.00 22.15 ? 168 LYS A CD  1 
ATOM   1322 C  CE  . LYS A 1 167 ? 18.776 -8.206  -5.527  1.00 31.77 ? 168 LYS A CE  1 
ATOM   1323 N  NZ  . LYS A 1 167 ? 19.731 -8.191  -6.666  1.00 39.00 ? 168 LYS A NZ  1 
ATOM   1324 N  N   . THR A 1 168 ? 18.496 -2.562  -3.651  1.00 11.97 ? 169 THR A N   1 
ATOM   1325 C  CA  . THR A 1 168 ? 19.865 -2.246  -3.290  1.00 12.59 ? 169 THR A CA  1 
ATOM   1326 C  C   . THR A 1 168 ? 19.947 -0.863  -2.635  1.00 12.51 ? 169 THR A C   1 
ATOM   1327 O  O   . THR A 1 168 ? 19.085 -0.013  -2.781  1.00 12.58 ? 169 THR A O   1 
ATOM   1328 C  CB  . THR A 1 168 ? 20.783 -2.319  -4.532  1.00 13.75 ? 169 THR A CB  1 
ATOM   1329 O  OG1 . THR A 1 168 ? 20.152 -1.579  -5.586  1.00 15.06 ? 169 THR A OG1 1 
ATOM   1330 C  CG2 . THR A 1 168 ? 21.117 -3.743  -4.920  1.00 16.64 ? 169 THR A CG2 1 
ATOM   1331 N  N   . LYS A 1 169 ? 21.073 -0.646  -1.948  1.00 13.88 ? 170 LYS A N   1 
ATOM   1332 C  CA  . LYS A 1 169 ? 21.326 0.612   -1.267  1.00 14.47 ? 170 LYS A CA  1 
ATOM   1333 C  C   . LYS A 1 169 ? 21.148 1.800   -2.207  1.00 14.74 ? 170 LYS A C   1 
ATOM   1334 O  O   . LYS A 1 169 ? 21.721 1.791   -3.288  1.00 15.05 ? 170 LYS A O   1 
ATOM   1335 C  CB  . LYS A 1 169 ? 22.725 0.545   -0.659  1.00 14.50 ? 170 LYS A CB  1 
ATOM   1336 C  CG  . LYS A 1 169 ? 23.149 1.861   -0.010  1.00 16.74 ? 170 LYS A CG  1 
ATOM   1337 C  CD  . LYS A 1 169 ? 24.487 1.760   0.687   1.00 20.56 ? 170 LYS A CD  1 
ATOM   1338 C  CE  . LYS A 1 169 ? 24.966 3.005   1.407   1.00 34.38 ? 170 LYS A CE  1 
ATOM   1339 N  NZ  . LYS A 1 169 ? 26.255 2.756   2.107   1.00 36.97 ? 170 LYS A NZ  1 
ATOM   1340 N  N   . GLY A 1 170 ? 20.397 2.823   -1.790  1.00 15.25 ? 171 GLY A N   1 
ATOM   1341 C  CA  . GLY A 1 170 ? 20.244 4.055   -2.530  1.00 14.84 ? 171 GLY A CA  1 
ATOM   1342 C  C   . GLY A 1 170 ? 19.044 4.021   -3.473  1.00 15.43 ? 171 GLY A C   1 
ATOM   1343 O  O   . GLY A 1 170 ? 18.751 5.044   -4.072  1.00 19.02 ? 171 GLY A O   1 
ATOM   1344 N  N   . LYS A 1 171 ? 18.345 2.889   -3.535  1.00 13.41 ? 172 LYS A N   1 
ATOM   1345 C  CA  . LYS A 1 171 ? 17.070 2.898   -4.265  1.00 13.65 ? 172 LYS A CA  1 
ATOM   1346 C  C   . LYS A 1 171 ? 15.944 3.371   -3.368  1.00 13.85 ? 172 LYS A C   1 
ATOM   1347 O  O   . LYS A 1 171 ? 15.924 3.108   -2.192  1.00 13.37 ? 172 LYS A O   1 
ATOM   1348 C  CB  . LYS A 1 171 ? 16.775 1.501   -4.795  1.00 14.26 ? 172 LYS A CB  1 
ATOM   1349 C  CG  . LYS A 1 171 ? 17.723 1.179   -5.958  1.00 14.02 ? 172 LYS A CG  1 
ATOM   1350 C  CD  . LYS A 1 171 ? 17.297 -0.009  -6.769  1.00 16.31 ? 172 LYS A CD  1 
ATOM   1351 C  CE  . LYS A 1 171 ? 16.364 0.435   -7.889  1.00 23.84 ? 172 LYS A CE  1 
ATOM   1352 N  NZ  . LYS A 1 171 ? 15.629 -0.676  -8.577  1.00 29.97 ? 172 LYS A NZ  1 
ATOM   1353 N  N   . SER A 1 172 ? 14.977 4.073   -3.935  1.00 13.24 ? 173 SER A N   1 
ATOM   1354 C  CA  . SER A 1 172 ? 13.821 4.552   -3.231  1.00 13.63 ? 173 SER A CA  1 
ATOM   1355 C  C   . SER A 1 172 ? 12.661 4.596   -4.197  1.00 13.37 ? 173 SER A C   1 
ATOM   1356 O  O   . SER A 1 172 ? 12.856 4.506   -5.430  1.00 16.17 ? 173 SER A O   1 
ATOM   1357 C  CB  . SER A 1 172 ? 14.071 5.939   -2.649  1.00 16.88 ? 173 SER A CB  1 
ATOM   1358 O  OG  . SER A 1 172 ? 14.299 6.918   -3.653  1.00 17.46 ? 173 SER A OG  1 
ATOM   1359 N  N   . ALA A 1 173 ? 11.474 4.786   -3.652  1.00 13.26 ? 174 ALA A N   1 
ATOM   1360 C  CA  . ALA A 1 173 ? 10.299 4.913   -4.508  1.00 16.53 ? 174 ALA A CA  1 
ATOM   1361 C  C   . ALA A 1 173 ? 9.281  5.771   -3.754  1.00 16.20 ? 174 ALA A C   1 
ATOM   1362 O  O   . ALA A 1 173 ? 9.278  5.824   -2.517  1.00 15.62 ? 174 ALA A O   1 
ATOM   1363 C  CB  . ALA A 1 173 ? 9.742  3.538   -4.812  1.00 19.19 ? 174 ALA A CB  1 
ATOM   1364 N  N   . ASP A 1 174 ? 8.388  6.448   -4.475  1.00 18.64 ? 175 ASP A N   1 
ATOM   1365 C  CA  . ASP A 1 174 ? 7.269  7.124   -3.837  1.00 18.18 ? 175 ASP A CA  1 
ATOM   1366 C  C   . ASP A 1 174 ? 6.434  6.050   -3.144  1.00 17.14 ? 175 ASP A C   1 
ATOM   1367 O  O   . ASP A 1 174 ? 6.351  4.910   -3.581  1.00 19.91 ? 175 ASP A O   1 
ATOM   1368 C  CB  . ASP A 1 174 ? 6.505  7.996   -4.858  1.00 26.21 ? 175 ASP A CB  1 
ATOM   1369 C  CG  . ASP A 1 174 ? 7.377  9.126   -5.408  1.00 29.33 ? 175 ASP A CG  1 
ATOM   1370 O  OD1 . ASP A 1 174 ? 7.800  9.992   -4.574  1.00 38.91 ? 175 ASP A OD1 1 
ATOM   1371 O  OD2 . ASP A 1 174 ? 7.670  9.134   -6.650  1.00 48.70 ? 175 ASP A OD2 1 
ATOM   1372 N  N   . PHE A 1 175 ? 5.896  6.389   -1.966  1.00 15.33 ? 176 PHE A N   1 
ATOM   1373 C  CA  . PHE A 1 175 ? 5.138  5.420   -1.208  1.00 14.51 ? 176 PHE A CA  1 
ATOM   1374 C  C   . PHE A 1 175 ? 4.080  6.158   -0.403  1.00 13.89 ? 176 PHE A C   1 
ATOM   1375 O  O   . PHE A 1 175 ? 4.238  6.344   0.816   1.00 15.07 ? 176 PHE A O   1 
ATOM   1376 C  CB  . PHE A 1 175 ? 6.094  4.637   -0.314  1.00 13.39 ? 176 PHE A CB  1 
ATOM   1377 C  CG  . PHE A 1 175 ? 5.487  3.361   0.215   1.00 12.65 ? 176 PHE A CG  1 
ATOM   1378 C  CD1 . PHE A 1 175 ? 5.146  2.302   -0.629  1.00 14.96 ? 176 PHE A CD1 1 
ATOM   1379 C  CD2 . PHE A 1 175 ? 5.259  3.211   1.594   1.00 13.66 ? 176 PHE A CD2 1 
ATOM   1380 C  CE1 . PHE A 1 175 ? 4.623  1.116   -0.131  1.00 16.29 ? 176 PHE A CE1 1 
ATOM   1381 C  CE2 . PHE A 1 175 ? 4.748  2.012   2.098   1.00 13.93 ? 176 PHE A CE2 1 
ATOM   1382 C  CZ  . PHE A 1 175 ? 4.363  1.001   1.234   1.00 13.39 ? 176 PHE A CZ  1 
ATOM   1383 N  N   . THR A 1 176 ? 2.981  6.544   -1.076  1.00 14.81 ? 177 THR A N   1 
ATOM   1384 C  CA  . THR A 1 176 ? 1.906  7.353   -0.484  1.00 14.77 ? 177 THR A CA  1 
ATOM   1385 C  C   . THR A 1 176 ? 0.742  6.477   -0.045  1.00 12.47 ? 177 THR A C   1 
ATOM   1386 O  O   . THR A 1 176 ? 0.666  5.307   -0.451  1.00 15.64 ? 177 THR A O   1 
ATOM   1387 C  CB  . THR A 1 176 ? 1.434  8.485   -1.401  1.00 18.16 ? 177 THR A CB  1 
ATOM   1388 O  OG1 . THR A 1 176 ? 0.936  7.815   -2.546  1.00 19.42 ? 177 THR A OG1 1 
ATOM   1389 C  CG2 . THR A 1 176 ? 2.574  9.384   -1.836  1.00 22.11 ? 177 THR A CG2 1 
ATOM   1390 N  N   . ASN A 1 177 ? -0.062 7.032   0.903   1.00 12.37 ? 178 ASN A N   1 
ATOM   1391 C  CA  . ASN A 1 177 ? -1.275 6.439   1.385   1.00 14.60 ? 178 ASN A CA  1 
ATOM   1392 C  C   . ASN A 1 177 ? -1.024 5.114   2.067   1.00 13.80 ? 178 ASN A C   1 
ATOM   1393 O  O   . ASN A 1 177 ? -1.953 4.304   2.092   1.00 20.05 ? 178 ASN A O   1 
ATOM   1394 C  CB  . ASN A 1 177 ? -2.281 6.250   0.245   1.00 16.88 ? 178 ASN A CB  1 
ATOM   1395 C  CG  . ASN A 1 177 ? -2.656 7.593   -0.334  1.00 17.95 ? 178 ASN A CG  1 
ATOM   1396 O  OD1 . ASN A 1 177 ? -3.399 8.363   0.306   1.00 22.13 ? 178 ASN A OD1 1 
ATOM   1397 N  ND2 . ASN A 1 177 ? -2.037 7.907   -1.463  1.00 20.78 ? 178 ASN A ND2 1 
ATOM   1398 N  N   . PHE A 1 178 ? 0.176  4.936   2.686   1.00 13.36 ? 179 PHE A N   1 
ATOM   1399 C  CA  . PHE A 1 178 ? 0.323  3.722   3.467   1.00 13.24 ? 179 PHE A CA  1 
ATOM   1400 C  C   . PHE A 1 178 ? -0.138 3.991   4.899   1.00 13.44 ? 179 PHE A C   1 
ATOM   1401 O  O   . PHE A 1 178 ? 0.268  4.995   5.513   1.00 15.59 ? 179 PHE A O   1 
ATOM   1402 C  CB  . PHE A 1 178 ? 1.776  3.215   3.484   1.00 15.53 ? 179 PHE A CB  1 
ATOM   1403 C  CG  . PHE A 1 178 ? 1.904  2.000   4.374   1.00 14.01 ? 179 PHE A CG  1 
ATOM   1404 C  CD1 . PHE A 1 178 ? 1.530  0.756   3.891   1.00 14.88 ? 179 PHE A CD1 1 
ATOM   1405 C  CD2 . PHE A 1 178 ? 2.228  2.098   5.734   1.00 12.34 ? 179 PHE A CD2 1 
ATOM   1406 C  CE1 . PHE A 1 178 ? 1.516  -0.377  4.691   1.00 13.78 ? 179 PHE A CE1 1 
ATOM   1407 C  CE2 . PHE A 1 178 ? 2.222  0.962   6.511   1.00 14.60 ? 179 PHE A CE2 1 
ATOM   1408 C  CZ  . PHE A 1 178 ? 1.838  -0.256  6.018   1.00 12.58 ? 179 PHE A CZ  1 
ATOM   1409 N  N   . ASP A 1 179 ? -1.060 3.144   5.357   1.00 12.85 ? 180 ASP A N   1 
ATOM   1410 C  CA  . ASP A 1 179 ? -1.714 3.369   6.654   1.00 12.93 ? 180 ASP A CA  1 
ATOM   1411 C  C   . ASP A 1 179 ? -1.012 2.563   7.743   1.00 12.13 ? 180 ASP A C   1 
ATOM   1412 O  O   . ASP A 1 179 ? -1.159 1.339   7.795   1.00 14.15 ? 180 ASP A O   1 
ATOM   1413 C  CB  . ASP A 1 179 ? -3.175 2.953   6.580   1.00 14.86 ? 180 ASP A CB  1 
ATOM   1414 C  CG  . ASP A 1 179 ? -3.984 3.371   7.791   1.00 17.08 ? 180 ASP A CG  1 
ATOM   1415 O  OD1 . ASP A 1 179 ? -3.371 3.664   8.816   1.00 15.82 ? 180 ASP A OD1 1 
ATOM   1416 O  OD2 . ASP A 1 179 ? -5.175 3.494   7.662   1.00 23.80 ? 180 ASP A OD2 1 
ATOM   1417 N  N   . PRO A 1 180 ? -0.218 3.178   8.642   1.00 11.96 ? 181 PRO A N   1 
ATOM   1418 C  CA  . PRO A 1 180 ? 0.488  2.387   9.648   1.00 12.88 ? 181 PRO A CA  1 
ATOM   1419 C  C   . PRO A 1 180 ? -0.450 1.754   10.672  1.00 12.56 ? 181 PRO A C   1 
ATOM   1420 O  O   . PRO A 1 180 ? 0.033  0.895   11.440  1.00 14.11 ? 181 PRO A O   1 
ATOM   1421 C  CB  . PRO A 1 180 ? 1.455  3.405   10.292  1.00 13.91 ? 181 PRO A CB  1 
ATOM   1422 C  CG  . PRO A 1 180 ? 0.828  4.778   10.064  1.00 13.53 ? 181 PRO A CG  1 
ATOM   1423 C  CD  . PRO A 1 180 ? 0.088  4.611   8.741   1.00 11.96 ? 181 PRO A CD  1 
ATOM   1424 N  N   . ARG A 1 181 ? -1.713 2.146   10.692  1.00 12.08 ? 182 ARG A N   1 
ATOM   1425 C  CA  . ARG A 1 181 ? -2.650 1.486   11.602  1.00 12.05 ? 182 ARG A CA  1 
ATOM   1426 C  C   . ARG A 1 181 ? -2.711 -0.005  11.244  1.00 12.99 ? 182 ARG A C   1 
ATOM   1427 O  O   . ARG A 1 181 ? -3.082 -0.836  12.045  1.00 14.54 ? 182 ARG A O   1 
ATOM   1428 C  CB  . ARG A 1 181 ? -4.049 2.121   11.570  1.00 16.19 ? 182 ARG A CB  1 
ATOM   1429 C  CG  . ARG A 1 181 ? -4.024 3.553   12.085  1.00 16.17 ? 182 ARG A CG  1 
ATOM   1430 C  CD  . ARG A 1 181 ? -5.370 4.216   12.016  1.00 19.91 ? 182 ARG A CD  1 
ATOM   1431 N  NE  . ARG A 1 181 ? -5.649 4.444   10.596  1.00 20.49 ? 182 ARG A NE  1 
ATOM   1432 C  CZ  . ARG A 1 181 ? -6.713 5.132   10.156  1.00 21.86 ? 182 ARG A CZ  1 
ATOM   1433 N  NH1 . ARG A 1 181 ? -7.567 5.680   11.012  1.00 29.64 ? 182 ARG A NH1 1 
ATOM   1434 N  NH2 . ARG A 1 181 ? -6.904 5.300   8.867   1.00 28.16 ? 182 ARG A NH2 1 
ATOM   1435 N  N   . GLY A 1 182 ? -2.473 -0.347  9.949   1.00 12.61 ? 183 GLY A N   1 
ATOM   1436 C  CA  . GLY A 1 182 ? -2.534 -1.745  9.554   1.00 12.97 ? 183 GLY A CA  1 
ATOM   1437 C  C   . GLY A 1 182 ? -1.368 -2.618  10.024  1.00 11.22 ? 183 GLY A C   1 
ATOM   1438 O  O   . GLY A 1 182 ? -1.385 -3.831  9.745   1.00 14.18 ? 183 GLY A O   1 
ATOM   1439 N  N   . LEU A 1 183 ? -0.418 -2.054  10.798  1.00 13.13 ? 184 LEU A N   1 
ATOM   1440 C  CA  . LEU A 1 183 ? 0.693  -2.831  11.330  1.00 11.97 ? 184 LEU A CA  1 
ATOM   1441 C  C   . LEU A 1 183 ? 0.545  -3.013  12.843  1.00 10.94 ? 184 LEU A C   1 
ATOM   1442 O  O   . LEU A 1 183 ? 1.466  -3.571  13.428  1.00 14.80 ? 184 LEU A O   1 
ATOM   1443 C  CB  . LEU A 1 183 ? 2.008  -2.088  11.009  1.00 12.64 ? 184 LEU A CB  1 
ATOM   1444 C  CG  . LEU A 1 183 ? 2.296  -1.853  9.523   1.00 13.70 ? 184 LEU A CG  1 
ATOM   1445 C  CD1 . LEU A 1 183 ? 3.554  -1.002  9.389   1.00 15.81 ? 184 LEU A CD1 1 
ATOM   1446 C  CD2 . LEU A 1 183 ? 2.478  -3.186  8.841   1.00 16.08 ? 184 LEU A CD2 1 
ATOM   1447 N  N   . LEU A 1 184 ? -0.580 -2.622  13.428  1.00 11.73 ? 185 LEU A N   1 
ATOM   1448 C  CA  . LEU A 1 184 ? -0.714 -2.661  14.869  1.00 12.18 ? 185 LEU A CA  1 
ATOM   1449 C  C   . LEU A 1 184 ? -1.449 -3.920  15.276  1.00 14.32 ? 185 LEU A C   1 
ATOM   1450 O  O   . LEU A 1 184 ? -2.462 -4.299  14.697  1.00 16.52 ? 185 LEU A O   1 
ATOM   1451 C  CB  . LEU A 1 184 ? -1.472 -1.420  15.360  1.00 14.14 ? 185 LEU A CB  1 
ATOM   1452 C  CG  . LEU A 1 184 ? -0.819 -0.078  14.995  1.00 15.46 ? 185 LEU A CG  1 
ATOM   1453 C  CD1 . LEU A 1 184 ? -1.623 1.106   15.564  1.00 17.78 ? 185 LEU A CD1 1 
ATOM   1454 C  CD2 . LEU A 1 184 ? 0.614  -0.010  15.485  1.00 17.53 ? 185 LEU A CD2 1 
ATOM   1455 N  N   . PRO A 1 185 ? -1.041 -4.537  16.410  1.00 12.68 ? 186 PRO A N   1 
ATOM   1456 C  CA  . PRO A 1 185 ? -1.802 -5.657  16.982  1.00 13.01 ? 186 PRO A CA  1 
ATOM   1457 C  C   . PRO A 1 185 ? -3.073 -5.141  17.698  1.00 11.59 ? 186 PRO A C   1 
ATOM   1458 O  O   . PRO A 1 185 ? -3.281 -3.928  17.794  1.00 14.17 ? 186 PRO A O   1 
ATOM   1459 C  CB  . PRO A 1 185 ? -0.818 -6.248  18.005  1.00 14.21 ? 186 PRO A CB  1 
ATOM   1460 C  CG  . PRO A 1 185 ? -0.110 -5.015  18.448  1.00 15.41 ? 186 PRO A CG  1 
ATOM   1461 C  CD  . PRO A 1 185 ? 0.073  -4.101  17.250  1.00 12.50 ? 186 PRO A CD  1 
ATOM   1462 N  N   . GLU A 1 186 ? -3.905 -6.076  18.208  1.00 14.86 ? 187 GLU A N   1 
ATOM   1463 C  CA  . GLU A 1 186 ? -5.164 -5.668  18.823  1.00 15.64 ? 187 GLU A CA  1 
ATOM   1464 C  C   . GLU A 1 186 ? -4.905 -4.896  20.103  1.00 12.95 ? 187 GLU A C   1 
ATOM   1465 O  O   . GLU A 1 186 ? -5.505 -3.842  20.294  1.00 17.13 ? 187 GLU A O   1 
ATOM   1466 C  CB  . GLU A 1 186 ? -6.074 -6.851  19.201  1.00 16.69 ? 187 GLU A CB  1 
ATOM   1467 C  CG  . GLU A 1 186 ? -6.702 -7.567  18.010  1.00 19.82 ? 187 GLU A CG  1 
ATOM   1468 C  CD  . GLU A 1 186 ? -7.456 -8.850  18.403  1.00 24.86 ? 187 GLU A CD  1 
ATOM   1469 O  OE1 . GLU A 1 186 ? -7.378 -9.282  19.573  1.00 25.77 ? 187 GLU A OE1 1 
ATOM   1470 O  OE2 . GLU A 1 186 ? -8.110 -9.445  17.541  1.00 30.63 ? 187 GLU A OE2 1 
ATOM   1471 N  N   . SER A 1 187 ? -3.990 -5.401  20.928  1.00 16.27 ? 188 SER A N   1 
ATOM   1472 C  CA  . SER A 1 187 ? -3.753 -4.820  22.246  1.00 17.31 ? 188 SER A CA  1 
ATOM   1473 C  C   . SER A 1 187 ? -2.678 -3.725  22.202  1.00 15.37 ? 188 SER A C   1 
ATOM   1474 O  O   . SER A 1 187 ? -1.685 -3.878  21.470  1.00 15.11 ? 188 SER A O   1 
ATOM   1475 C  CB  . SER A 1 187 ? -3.352 -5.909  23.243  1.00 17.20 ? 188 SER A CB  1 
ATOM   1476 O  OG  . SER A 1 187 ? -3.140 -5.321  24.529  1.00 17.63 ? 188 SER A OG  1 
ATOM   1477 N  N   . LEU A 1 188 ? -2.916 -2.606  22.928  1.00 15.32 ? 189 LEU A N   1 
ATOM   1478 C  CA  . LEU A 1 188 ? -1.848 -1.632  23.176  1.00 14.49 ? 189 LEU A CA  1 
ATOM   1479 C  C   . LEU A 1 188 ? -1.179 -1.850  24.538  1.00 14.55 ? 189 LEU A C   1 
ATOM   1480 O  O   . LEU A 1 188 ? -0.477 -0.948  24.990  1.00 17.88 ? 189 LEU A O   1 
ATOM   1481 C  CB  . LEU A 1 188 ? -2.327 -0.172  23.017  1.00 16.62 ? 189 LEU A CB  1 
ATOM   1482 C  CG  . LEU A 1 188 ? -2.767 0.199   21.590  1.00 16.58 ? 189 LEU A CG  1 
ATOM   1483 C  CD1 . LEU A 1 188 ? -3.229 1.637   21.573  1.00 20.20 ? 189 LEU A CD1 1 
ATOM   1484 C  CD2 . LEU A 1 188 ? -1.627 0.008   20.616  1.00 19.38 ? 189 LEU A CD2 1 
ATOM   1485 N  N   . ASP A 1 189 ? -1.316 -3.046  25.157  1.00 14.14 ? 190 ASP A N   1 
ATOM   1486 C  CA  . ASP A 1 189 ? -0.540 -3.244  26.394  1.00 13.27 ? 190 ASP A CA  1 
ATOM   1487 C  C   . ASP A 1 189 ? 0.951  -3.201  26.036  1.00 12.71 ? 190 ASP A C   1 
ATOM   1488 O  O   . ASP A 1 189 ? 1.400  -3.692  25.000  1.00 13.79 ? 190 ASP A O   1 
ATOM   1489 C  CB  . ASP A 1 189 ? -0.793 -4.618  27.002  1.00 17.28 ? 190 ASP A CB  1 
ATOM   1490 C  CG  . ASP A 1 189 ? -2.131 -4.790  27.697  1.00 16.69 ? 190 ASP A CG  1 
ATOM   1491 O  OD1 . ASP A 1 189 ? -2.768 -3.778  27.992  1.00 23.91 ? 190 ASP A OD1 1 
ATOM   1492 O  OD2 . ASP A 1 189 ? -2.571 -5.965  27.823  1.00 25.76 ? 190 ASP A OD2 1 
ATOM   1493 N  N   . TYR A 1 190 ? 1.773  -2.593  26.903  1.00 12.99 ? 191 TYR A N   1 
ATOM   1494 C  CA  . TYR A 1 190 ? 3.165  -2.364  26.539  1.00 11.84 ? 191 TYR A CA  1 
ATOM   1495 C  C   . TYR A 1 190 ? 4.074  -2.415  27.743  1.00 11.32 ? 191 TYR A C   1 
ATOM   1496 O  O   . TYR A 1 190 ? 3.633  -2.267  28.876  1.00 12.36 ? 191 TYR A O   1 
ATOM   1497 C  CB  . TYR A 1 190 ? 3.300  -1.009  25.823  1.00 12.66 ? 191 TYR A CB  1 
ATOM   1498 C  CG  . TYR A 1 190 ? 2.980  0.203   26.697  1.00 12.62 ? 191 TYR A CG  1 
ATOM   1499 C  CD1 . TYR A 1 190 ? 3.929  0.761   27.572  1.00 14.19 ? 191 TYR A CD1 1 
ATOM   1500 C  CD2 . TYR A 1 190 ? 1.708  0.749   26.693  1.00 14.37 ? 191 TYR A CD2 1 
ATOM   1501 C  CE1 . TYR A 1 190 ? 3.608  1.838   28.384  1.00 15.65 ? 191 TYR A CE1 1 
ATOM   1502 C  CE2 . TYR A 1 190 ? 1.355  1.823   27.528  1.00 13.05 ? 191 TYR A CE2 1 
ATOM   1503 C  CZ  . TYR A 1 190 ? 2.307  2.339   28.406  1.00 13.33 ? 191 TYR A CZ  1 
ATOM   1504 O  OH  . TYR A 1 190 ? 2.019  3.413   29.208  1.00 15.39 ? 191 TYR A OH  1 
ATOM   1505 N  N   . TRP A 1 191 ? 5.348  -2.522  27.451  1.00 10.45 ? 192 TRP A N   1 
ATOM   1506 C  CA  . TRP A 1 191 ? 6.421  -2.305  28.403  1.00 12.34 ? 192 TRP A CA  1 
ATOM   1507 C  C   . TRP A 1 191 ? 7.076  -1.012  27.994  1.00 12.66 ? 192 TRP A C   1 
ATOM   1508 O  O   . TRP A 1 191 ? 7.194  -0.732  26.811  1.00 13.54 ? 192 TRP A O   1 
ATOM   1509 C  CB  . TRP A 1 191 ? 7.398  -3.463  28.363  1.00 12.55 ? 192 TRP A CB  1 
ATOM   1510 C  CG  . TRP A 1 191 ? 6.806  -4.769  28.741  1.00 12.70 ? 192 TRP A CG  1 
ATOM   1511 C  CD1 . TRP A 1 191 ? 6.384  -5.161  29.989  1.00 12.81 ? 192 TRP A CD1 1 
ATOM   1512 C  CD2 . TRP A 1 191 ? 6.551  -5.883  27.869  1.00 12.08 ? 192 TRP A CD2 1 
ATOM   1513 N  NE1 . TRP A 1 191 ? 5.893  -6.431  29.924  1.00 14.13 ? 192 TRP A NE1 1 
ATOM   1514 C  CE2 . TRP A 1 191 ? 5.986  -6.915  28.640  1.00 12.38 ? 192 TRP A CE2 1 
ATOM   1515 C  CE3 . TRP A 1 191 ? 6.733  -6.108  26.485  1.00 13.45 ? 192 TRP A CE3 1 
ATOM   1516 C  CZ2 . TRP A 1 191 ? 5.617  -8.147  28.110  1.00 13.59 ? 192 TRP A CZ2 1 
ATOM   1517 C  CZ3 . TRP A 1 191 ? 6.424  -7.350  25.966  1.00 14.45 ? 192 TRP A CZ3 1 
ATOM   1518 C  CH2 . TRP A 1 191 ? 5.845  -8.350  26.760  1.00 15.00 ? 192 TRP A CH2 1 
ATOM   1519 N  N   . THR A 1 192 ? 7.724  -0.326  28.927  1.00 12.01 ? 193 THR A N   1 
ATOM   1520 C  CA  . THR A 1 192 ? 8.425  0.914   28.602  1.00 10.78 ? 193 THR A CA  1 
ATOM   1521 C  C   . THR A 1 192 ? 9.685  1.025   29.447  1.00 11.32 ? 193 THR A C   1 
ATOM   1522 O  O   . THR A 1 192 ? 9.714  0.624   30.635  1.00 14.36 ? 193 THR A O   1 
ATOM   1523 C  CB  . THR A 1 192 ? 7.527  2.155   28.694  1.00 11.44 ? 193 THR A CB  1 
ATOM   1524 O  OG1 . THR A 1 192 ? 8.266  3.315   28.350  1.00 13.63 ? 193 THR A OG1 1 
ATOM   1525 C  CG2 . THR A 1 192 ? 7.008  2.381   30.100  1.00 12.76 ? 193 THR A CG2 1 
ATOM   1526 N  N   . TYR A 1 193 ? 10.747 1.542   28.837  1.00 12.49 ? 194 TYR A N   1 
ATOM   1527 C  CA  . TYR A 1 193 ? 11.987 1.738   29.587  1.00 10.94 ? 194 TYR A CA  1 
ATOM   1528 C  C   . TYR A 1 193 ? 12.752 2.816   28.834  1.00 13.09 ? 194 TYR A C   1 
ATOM   1529 O  O   . TYR A 1 193 ? 12.554 3.015   27.609  1.00 12.09 ? 194 TYR A O   1 
ATOM   1530 C  CB  . TYR A 1 193 ? 12.756 0.412   29.732  1.00 12.50 ? 194 TYR A CB  1 
ATOM   1531 C  CG  . TYR A 1 193 ? 13.465 -0.007  28.467  1.00 11.03 ? 194 TYR A CG  1 
ATOM   1532 C  CD1 . TYR A 1 193 ? 12.773 -0.627  27.433  1.00 11.55 ? 194 TYR A CD1 1 
ATOM   1533 C  CD2 . TYR A 1 193 ? 14.815 0.292   28.278  1.00 11.23 ? 194 TYR A CD2 1 
ATOM   1534 C  CE1 . TYR A 1 193 ? 13.435 -0.950  26.238  1.00 11.81 ? 194 TYR A CE1 1 
ATOM   1535 C  CE2 . TYR A 1 193 ? 15.478 -0.002  27.100  1.00 12.04 ? 194 TYR A CE2 1 
ATOM   1536 C  CZ  . TYR A 1 193 ? 14.770 -0.615  26.075  1.00 10.63 ? 194 TYR A CZ  1 
ATOM   1537 O  OH  . TYR A 1 193 ? 15.461 -0.896  24.922  1.00 11.78 ? 194 TYR A OH  1 
ATOM   1538 N  N   . PRO A 1 194 ? 13.711 3.490   29.505  1.00 12.56 ? 195 PRO A N   1 
ATOM   1539 C  CA  . PRO A 1 194 ? 14.548 4.463   28.817  1.00 13.43 ? 195 PRO A CA  1 
ATOM   1540 C  C   . PRO A 1 194 ? 15.734 3.810   28.124  1.00 12.29 ? 195 PRO A C   1 
ATOM   1541 O  O   . PRO A 1 194 ? 16.453 2.985   28.741  1.00 13.10 ? 195 PRO A O   1 
ATOM   1542 C  CB  . PRO A 1 194 ? 15.086 5.293   30.004  1.00 14.42 ? 195 PRO A CB  1 
ATOM   1543 C  CG  . PRO A 1 194 ? 15.148 4.297   31.180  1.00 17.78 ? 195 PRO A CG  1 
ATOM   1544 C  CD  . PRO A 1 194 ? 13.939 3.390   30.958  1.00 13.74 ? 195 PRO A CD  1 
ATOM   1545 N  N   . GLY A 1 195 ? 15.978 4.223   26.880  1.00 11.50 ? 196 GLY A N   1 
ATOM   1546 C  CA  . GLY A 1 195 ? 17.103 3.662   26.176  1.00 12.57 ? 196 GLY A CA  1 
ATOM   1547 C  C   . GLY A 1 195 ? 17.655 4.550   25.073  1.00 10.26 ? 196 GLY A C   1 
ATOM   1548 O  O   . GLY A 1 195 ? 17.676 5.775   25.193  1.00 11.04 ? 196 GLY A O   1 
ATOM   1549 N  N   . SER A 1 196 ? 17.994 3.868   23.963  1.00 11.04 ? 197 SER A N   1 
ATOM   1550 C  CA  . SER A 1 196 ? 18.878 4.473   22.972  1.00 11.21 ? 197 SER A CA  1 
ATOM   1551 C  C   . SER A 1 196 ? 18.393 4.095   21.564  1.00 12.46 ? 197 SER A C   1 
ATOM   1552 O  O   . SER A 1 196 ? 17.648 3.129   21.350  1.00 11.70 ? 197 SER A O   1 
ATOM   1553 C  CB  . SER A 1 196 ? 20.339 4.016   23.143  1.00 12.23 ? 197 SER A CB  1 
ATOM   1554 O  OG  . SER A 1 196 ? 20.518 2.661   22.744  1.00 11.78 ? 197 SER A OG  1 
ATOM   1555 N  N   . LEU A 1 197 ? 19.007 4.792   20.629  1.00 11.68 ? 198 LEU A N   1 
ATOM   1556 C  CA  . LEU A 1 197 ? 18.994 4.287   19.238  1.00 11.16 ? 198 LEU A CA  1 
ATOM   1557 C  C   . LEU A 1 197 ? 19.657 2.901   19.248  1.00 10.28 ? 198 LEU A C   1 
ATOM   1558 O  O   . LEU A 1 197 ? 20.653 2.701   20.027  1.00 11.48 ? 198 LEU A O   1 
ATOM   1559 C  CB  . LEU A 1 197 ? 19.812 5.175   18.320  1.00 13.18 ? 198 LEU A CB  1 
ATOM   1560 C  CG  . LEU A 1 197 ? 19.396 6.637   18.285  1.00 17.15 ? 198 LEU A CG  1 
ATOM   1561 C  CD1 . LEU A 1 197 ? 20.267 7.408   17.311  1.00 19.09 ? 198 LEU A CD1 1 
ATOM   1562 C  CD2 . LEU A 1 197 ? 17.948 6.792   17.876  1.00 18.81 ? 198 LEU A CD2 1 
ATOM   1563 N  N   . THR A 1 198 ? 19.208 2.013   18.323  1.00 11.96 ? 199 THR A N   1 
ATOM   1564 C  CA  . THR A 1 198 ? 19.865 0.720   18.251  1.00 13.03 ? 199 THR A CA  1 
ATOM   1565 C  C   . THR A 1 198 ? 20.892 0.651   17.130  1.00 11.55 ? 199 THR A C   1 
ATOM   1566 O  O   . THR A 1 198 ? 21.435 -0.430  16.881  1.00 12.19 ? 199 THR A O   1 
ATOM   1567 C  CB  . THR A 1 198 ? 18.885 -0.446  18.176  1.00 10.91 ? 199 THR A CB  1 
ATOM   1568 O  OG1 . THR A 1 198 ? 18.190 -0.338  16.922  1.00 10.36 ? 199 THR A OG1 1 
ATOM   1569 C  CG2 . THR A 1 198 ? 17.943 -0.392  19.367  1.00 12.17 ? 199 THR A CG2 1 
ATOM   1570 N  N   . THR A 1 199 ? 21.084 1.771   16.439  1.00 12.06 ? 200 THR A N   1 
ATOM   1571 C  CA  . THR A 1 199 ? 22.150 1.865   15.446  1.00 11.70 ? 200 THR A CA  1 
ATOM   1572 C  C   . THR A 1 199 ? 22.983 3.086   15.798  1.00 13.09 ? 200 THR A C   1 
ATOM   1573 O  O   . THR A 1 199 ? 22.501 3.998   16.445  1.00 13.36 ? 200 THR A O   1 
ATOM   1574 C  CB  . THR A 1 199 ? 21.557 2.028   14.035  1.00 13.66 ? 200 THR A CB  1 
ATOM   1575 O  OG1 . THR A 1 199 ? 20.637 3.136   14.038  1.00 16.27 ? 200 THR A OG1 1 
ATOM   1576 C  CG2 . THR A 1 199 ? 20.926 0.738   13.583  1.00 16.64 ? 200 THR A CG2 1 
ATOM   1577 N  N   . PRO A 1 200 ? 24.238 3.142   15.314  1.00 14.49 ? 201 PRO A N   1 
ATOM   1578 C  CA  . PRO A 1 200 ? 25.053 4.343   15.382  1.00 14.45 ? 201 PRO A CA  1 
ATOM   1579 C  C   . PRO A 1 200 ? 24.234 5.554   14.996  1.00 15.29 ? 201 PRO A C   1 
ATOM   1580 O  O   . PRO A 1 200 ? 23.584 5.553   13.932  1.00 17.81 ? 201 PRO A O   1 
ATOM   1581 C  CB  . PRO A 1 200 ? 26.233 4.031   14.429  1.00 16.75 ? 201 PRO A CB  1 
ATOM   1582 C  CG  . PRO A 1 200 ? 26.398 2.542   14.641  1.00 16.73 ? 201 PRO A CG  1 
ATOM   1583 C  CD  . PRO A 1 200 ? 24.952 2.046   14.651  1.00 16.70 ? 201 PRO A CD  1 
ATOM   1584 N  N   . PRO A 1 201 ? 24.329 6.699   15.684  1.00 14.13 ? 202 PRO A N   1 
ATOM   1585 C  CA  . PRO A 1 201 ? 25.249 6.953   16.807  1.00 13.53 ? 202 PRO A CA  1 
ATOM   1586 C  C   . PRO A 1 201 ? 24.835 6.514   18.217  1.00 15.38 ? 202 PRO A C   1 
ATOM   1587 O  O   . PRO A 1 201 ? 25.532 6.889   19.175  1.00 16.20 ? 202 PRO A O   1 
ATOM   1588 C  CB  . PRO A 1 201 ? 25.357 8.491   16.780  1.00 20.56 ? 202 PRO A CB  1 
ATOM   1589 C  CG  . PRO A 1 201 ? 23.997 8.977   16.231  1.00 23.34 ? 202 PRO A CG  1 
ATOM   1590 C  CD  . PRO A 1 201 ? 23.584 7.902   15.258  1.00 19.95 ? 202 PRO A CD  1 
ATOM   1591 N  N   . LEU A 1 202 ? 23.771 5.693   18.334  1.00 13.74 ? 203 LEU A N   1 
ATOM   1592 C  CA  . LEU A 1 202 ? 23.481 5.017   19.603  1.00 11.93 ? 203 LEU A CA  1 
ATOM   1593 C  C   . LEU A 1 202 ? 23.093 6.023   20.677  1.00 12.78 ? 203 LEU A C   1 
ATOM   1594 O  O   . LEU A 1 202 ? 23.180 5.658   21.867  1.00 14.61 ? 203 LEU A O   1 
ATOM   1595 C  CB  . LEU A 1 202 ? 24.666 4.122   20.032  1.00 14.47 ? 203 LEU A CB  1 
ATOM   1596 C  CG  . LEU A 1 202 ? 24.978 2.973   19.050  1.00 13.62 ? 203 LEU A CG  1 
ATOM   1597 C  CD1 . LEU A 1 202 ? 26.233 2.273   19.486  1.00 16.61 ? 203 LEU A CD1 1 
ATOM   1598 C  CD2 . LEU A 1 202 ? 23.830 1.982   18.940  1.00 13.12 ? 203 LEU A CD2 1 
ATOM   1599 N  N   A ASN A 1 203 ? 22.608 7.214   20.305  0.50 14.29 ? 204 ASN A N   1 
ATOM   1600 N  N   B ASN A 1 203 ? 22.690 7.233   20.307  0.50 14.22 ? 204 ASN A N   1 
ATOM   1601 C  CA  A ASN A 1 203 ? 22.208 8.243   21.254  0.50 15.37 ? 204 ASN A CA  1 
ATOM   1602 C  CA  B ASN A 1 203 ? 22.289 8.250   21.268  0.50 15.71 ? 204 ASN A CA  1 
ATOM   1603 C  C   A ASN A 1 203 ? 21.198 7.722   22.258  0.50 13.89 ? 204 ASN A C   1 
ATOM   1604 C  C   B ASN A 1 203 ? 21.268 7.716   22.257  0.50 13.91 ? 204 ASN A C   1 
ATOM   1605 O  O   A ASN A 1 203 ? 20.214 7.061   21.887  0.50 13.34 ? 204 ASN A O   1 
ATOM   1606 O  O   B ASN A 1 203 ? 20.302 7.049   21.871  0.50 13.48 ? 204 ASN A O   1 
ATOM   1607 C  CB  A ASN A 1 203 ? 21.600 9.452   20.554  0.50 16.78 ? 204 ASN A CB  1 
ATOM   1608 C  CB  B ASN A 1 203 ? 21.663 9.461   20.586  0.50 17.53 ? 204 ASN A CB  1 
ATOM   1609 C  CG  A ASN A 1 203 ? 22.578 10.171  19.645  0.50 20.88 ? 204 ASN A CG  1 
ATOM   1610 C  CG  B ASN A 1 203 ? 22.660 10.256  19.771  0.50 24.64 ? 204 ASN A CG  1 
ATOM   1611 O  OD1 A ASN A 1 203 ? 23.735 9.792   19.508  0.50 23.74 ? 204 ASN A OD1 1 
ATOM   1612 O  OD1 B ASN A 1 203 ? 22.644 10.212  18.552  0.50 31.99 ? 204 ASN A OD1 1 
ATOM   1613 N  ND2 A ASN A 1 203 ? 22.133 11.269  19.078  0.50 19.63 ? 204 ASN A ND2 1 
ATOM   1614 N  ND2 B ASN A 1 203 ? 23.532 10.978  20.448  0.50 29.86 ? 204 ASN A ND2 1 
ATOM   1615 N  N   . GLU A 1 204 ? 21.400 8.119   23.524  1.00 14.58 ? 205 GLU A N   1 
ATOM   1616 C  CA  . GLU A 1 204 ? 20.489 7.697   24.580  1.00 12.50 ? 205 GLU A CA  1 
ATOM   1617 C  C   . GLU A 1 204 ? 19.337 8.691   24.696  1.00 14.52 ? 205 GLU A C   1 
ATOM   1618 O  O   . GLU A 1 204 ? 19.191 9.472   25.620  1.00 17.13 ? 205 GLU A O   1 
ATOM   1619 C  CB  . GLU A 1 204 ? 21.278 7.583   25.874  1.00 14.59 ? 205 GLU A CB  1 
ATOM   1620 C  CG  . GLU A 1 204 ? 22.260 6.416   25.785  1.00 15.00 ? 205 GLU A CG  1 
ATOM   1621 C  CD  . GLU A 1 204 ? 23.122 6.126   27.007  1.00 15.56 ? 205 GLU A CD  1 
ATOM   1622 O  OE1 . GLU A 1 204 ? 23.291 7.007   27.879  1.00 20.58 ? 205 GLU A OE1 1 
ATOM   1623 O  OE2 . GLU A 1 204 ? 23.559 4.969   27.094  1.00 14.61 ? 205 GLU A OE2 1 
ATOM   1624 N  N   . CYS A 1 205 ? 18.488 8.676   23.670  1.00 12.45 ? 206 CYS A N   1 
ATOM   1625 C  CA  . CYS A 1 205 ? 17.459 9.689   23.453  1.00 15.52 ? 206 CYS A CA  1 
ATOM   1626 C  C   . CYS A 1 205 ? 16.060 9.072   23.348  1.00 13.61 ? 206 CYS A C   1 
ATOM   1627 O  O   . CYS A 1 205 ? 15.118 9.784   22.942  1.00 15.83 ? 206 CYS A O   1 
ATOM   1628 C  CB  . CYS A 1 205 ? 17.725 10.469  22.169  1.00 15.11 ? 206 CYS A CB  1 
ATOM   1629 S  SG  . CYS A 1 205 ? 17.801 9.493   20.647  1.00 16.75 ? 206 CYS A SG  1 
ATOM   1630 N  N   . VAL A 1 206 ? 15.927 7.759   23.611  1.00 11.82 ? 207 VAL A N   1 
ATOM   1631 C  CA  . VAL A 1 206 ? 14.672 7.067   23.231  1.00 12.74 ? 207 VAL A CA  1 
ATOM   1632 C  C   . VAL A 1 206 ? 13.913 6.607   24.487  1.00 14.20 ? 207 VAL A C   1 
ATOM   1633 O  O   . VAL A 1 206 ? 14.464 5.969   25.384  1.00 14.62 ? 207 VAL A O   1 
ATOM   1634 C  CB  . VAL A 1 206 ? 14.914 5.843   22.345  1.00 12.68 ? 207 VAL A CB  1 
ATOM   1635 C  CG1 . VAL A 1 206 ? 13.644 5.128   22.011  1.00 13.48 ? 207 VAL A CG1 1 
ATOM   1636 C  CG2 . VAL A 1 206 ? 15.643 6.163   21.050  1.00 12.84 ? 207 VAL A CG2 1 
ATOM   1637 N  N   . THR A 1 207 ? 12.622 6.944   24.540  1.00 10.76 ? 208 THR A N   1 
ATOM   1638 C  CA  . THR A 1 207 ? 11.681 6.299   25.422  1.00 10.33 ? 208 THR A CA  1 
ATOM   1639 C  C   . THR A 1 207 ? 11.102 5.123   24.626  1.00 10.79 ? 208 THR A C   1 
ATOM   1640 O  O   . THR A 1 207 ? 10.399 5.318   23.591  1.00 12.20 ? 208 THR A O   1 
ATOM   1641 C  CB  . THR A 1 207 ? 10.557 7.235   25.889  1.00 14.83 ? 208 THR A CB  1 
ATOM   1642 O  OG1 . THR A 1 207 ? 11.142 8.299   26.657  1.00 13.47 ? 208 THR A OG1 1 
ATOM   1643 C  CG2 . THR A 1 207 ? 9.544  6.452   26.689  1.00 13.80 ? 208 THR A CG2 1 
ATOM   1644 N  N   . TRP A 1 208 ? 11.487 3.901   24.996  1.00 11.46 ? 209 TRP A N   1 
ATOM   1645 C  CA  . TRP A 1 208 ? 10.985 2.725   24.288  1.00 10.42 ? 209 TRP A CA  1 
ATOM   1646 C  C   . TRP A 1 208 ? 9.613  2.365   24.810  1.00 9.88  ? 209 TRP A C   1 
ATOM   1647 O  O   . TRP A 1 208 ? 9.382  2.311   26.019  1.00 11.62 ? 209 TRP A O   1 
ATOM   1648 C  CB  . TRP A 1 208 ? 11.969 1.557   24.494  1.00 10.97 ? 209 TRP A CB  1 
ATOM   1649 C  CG  . TRP A 1 208 ? 13.114 1.680   23.527  1.00 10.56 ? 209 TRP A CG  1 
ATOM   1650 C  CD1 . TRP A 1 208 ? 14.354 2.243   23.719  1.00 10.90 ? 209 TRP A CD1 1 
ATOM   1651 C  CD2 . TRP A 1 208 ? 13.076 1.324   22.135  1.00 11.56 ? 209 TRP A CD2 1 
ATOM   1652 N  NE1 . TRP A 1 208 ? 15.098 2.238   22.562  1.00 11.50 ? 209 TRP A NE1 1 
ATOM   1653 C  CE2 . TRP A 1 208 ? 14.309 1.678   21.577  1.00 11.62 ? 209 TRP A CE2 1 
ATOM   1654 C  CE3 . TRP A 1 208 ? 12.100 0.701   21.335  1.00 10.90 ? 209 TRP A CE3 1 
ATOM   1655 C  CZ2 . TRP A 1 208 ? 14.598 1.418   20.220  1.00 12.72 ? 209 TRP A CZ2 1 
ATOM   1656 C  CZ3 . TRP A 1 208 ? 12.394 0.458   20.021  1.00 12.18 ? 209 TRP A CZ3 1 
ATOM   1657 C  CH2 . TRP A 1 208 ? 13.613 0.831   19.466  1.00 12.56 ? 209 TRP A CH2 1 
ATOM   1658 N  N   . ILE A 1 209 ? 8.722  2.079   23.852  1.00 10.51 ? 210 ILE A N   1 
ATOM   1659 C  CA  . ILE A 1 209 ? 7.388  1.563   24.133  1.00 10.21 ? 210 ILE A CA  1 
ATOM   1660 C  C   . ILE A 1 209 ? 7.192  0.267   23.371  1.00 9.03  ? 210 ILE A C   1 
ATOM   1661 O  O   . ILE A 1 209 ? 7.074  0.394   22.151  1.00 11.08 ? 210 ILE A O   1 
ATOM   1662 C  CB  . ILE A 1 209 ? 6.285  2.605   23.885  1.00 11.59 ? 210 ILE A CB  1 
ATOM   1663 C  CG1 . ILE A 1 209 ? 6.516  3.825   24.778  1.00 13.11 ? 210 ILE A CG1 1 
ATOM   1664 C  CG2 . ILE A 1 209 ? 4.894  2.035   24.114  1.00 14.39 ? 210 ILE A CG2 1 
ATOM   1665 C  CD1 . ILE A 1 209 ? 5.697  5.011   24.328  1.00 14.59 ? 210 ILE A CD1 1 
ATOM   1666 N  N   . VAL A 1 210 ? 7.301  -0.904  23.978  1.00 10.85 ? 211 VAL A N   1 
ATOM   1667 C  CA  . VAL A 1 210 ? 7.341  -2.190  23.283  1.00 9.85  ? 211 VAL A CA  1 
ATOM   1668 C  C   . VAL A 1 210 ? 6.030  -2.869  23.546  1.00 11.86 ? 211 VAL A C   1 
ATOM   1669 O  O   . VAL A 1 210 ? 5.638  -3.143  24.668  1.00 11.90 ? 211 VAL A O   1 
ATOM   1670 C  CB  . VAL A 1 210 ? 8.541  -3.042  23.736  1.00 10.56 ? 211 VAL A CB  1 
ATOM   1671 C  CG1 . VAL A 1 210 ? 8.530  -4.425  23.058  1.00 11.64 ? 211 VAL A CG1 1 
ATOM   1672 C  CG2 . VAL A 1 210 ? 9.811  -2.259  23.396  1.00 11.38 ? 211 VAL A CG2 1 
ATOM   1673 N  N   . LEU A 1 211 ? 5.274  -3.131  22.478  1.00 10.34 ? 212 LEU A N   1 
ATOM   1674 C  CA  . LEU A 1 211 ? 3.985  -3.769  22.695  1.00 11.13 ? 212 LEU A CA  1 
ATOM   1675 C  C   . LEU A 1 211 ? 4.122  -5.249  23.016  1.00 11.45 ? 212 LEU A C   1 
ATOM   1676 O  O   . LEU A 1 211 ? 4.975  -5.952  22.484  1.00 12.14 ? 212 LEU A O   1 
ATOM   1677 C  CB  . LEU A 1 211 ? 3.135  -3.634  21.423  1.00 10.35 ? 212 LEU A CB  1 
ATOM   1678 C  CG  . LEU A 1 211 ? 2.741  -2.210  21.036  1.00 11.54 ? 212 LEU A CG  1 
ATOM   1679 C  CD1 . LEU A 1 211 ? 1.727  -2.183  19.871  1.00 12.68 ? 212 LEU A CD1 1 
ATOM   1680 C  CD2 . LEU A 1 211 ? 2.197  -1.435  22.208  1.00 14.17 ? 212 LEU A CD2 1 
ATOM   1681 N  N   . LYS A 1 212 ? 3.281  -5.684  23.971  1.00 12.05 ? 213 LYS A N   1 
ATOM   1682 C  CA  . LYS A 1 212 ? 3.279  -7.082  24.411  1.00 12.94 ? 213 LYS A CA  1 
ATOM   1683 C  C   . LYS A 1 212 ? 2.875  -8.068  23.297  1.00 11.88 ? 213 LYS A C   1 
ATOM   1684 O  O   . LYS A 1 212 ? 3.392  -9.189  23.181  1.00 15.76 ? 213 LYS A O   1 
ATOM   1685 C  CB  . LYS A 1 212 ? 2.482  -7.265  25.720  1.00 16.71 ? 213 LYS A CB  1 
ATOM   1686 C  CG  . LYS A 1 212 ? 2.262  -8.714  26.106  1.00 21.37 ? 213 LYS A CG  1 
ATOM   1687 C  CD  . LYS A 1 212 ? 1.299  -8.896  27.279  1.00 29.40 ? 213 LYS A CD  1 
ATOM   1688 C  CE  . LYS A 1 212 ? 0.043  -8.042  27.191  1.00 30.37 ? 213 LYS A CE  1 
ATOM   1689 N  NZ  . LYS A 1 212 ? -0.908 -8.500  26.144  1.00 43.57 ? 213 LYS A NZ  1 
ATOM   1690 N  N   . GLU A 1 213 ? 1.837  -7.695  22.530  1.00 12.82 ? 214 GLU A N   1 
ATOM   1691 C  CA  . GLU A 1 213 ? 1.280  -8.598  21.526  1.00 14.12 ? 214 GLU A CA  1 
ATOM   1692 C  C   . GLU A 1 213 ? 2.022  -8.474  20.215  1.00 12.05 ? 214 GLU A C   1 
ATOM   1693 O  O   . GLU A 1 213 ? 2.099  -7.390  19.664  1.00 12.24 ? 214 GLU A O   1 
ATOM   1694 C  CB  . GLU A 1 213 ? -0.175 -8.238  21.317  1.00 13.60 ? 214 GLU A CB  1 
ATOM   1695 C  CG  . GLU A 1 213 ? -0.864 -9.142  20.319  1.00 18.53 ? 214 GLU A CG  1 
ATOM   1696 C  CD  . GLU A 1 213 ? -2.362 -8.876  20.163  1.00 22.95 ? 214 GLU A CD  1 
ATOM   1697 O  OE1 . GLU A 1 213 ? -2.932 -8.169  20.996  1.00 22.86 ? 214 GLU A OE1 1 
ATOM   1698 O  OE2 . GLU A 1 213 ? -2.940 -9.320  19.145  1.00 35.45 ? 214 GLU A OE2 1 
ATOM   1699 N  N   A PRO A 1 214 ? 2.540  -9.592  19.676  0.50 12.85 ? 215 PRO A N   1 
ATOM   1700 N  N   B PRO A 1 214 ? 2.670  -9.552  19.737  0.50 11.69 ? 215 PRO A N   1 
ATOM   1701 C  CA  A PRO A 1 214 ? 3.199  -9.508  18.379  0.50 12.35 ? 215 PRO A CA  1 
ATOM   1702 C  CA  B PRO A 1 214 ? 3.271  -9.528  18.397  0.50 11.76 ? 215 PRO A CA  1 
ATOM   1703 C  C   A PRO A 1 214 ? 2.114  -9.331  17.327  0.50 11.36 ? 215 PRO A C   1 
ATOM   1704 C  C   B PRO A 1 214 ? 2.216  -9.546  17.295  0.50 11.76 ? 215 PRO A C   1 
ATOM   1705 O  O   A PRO A 1 214 ? 0.932  -9.465  17.594  0.50 12.72 ? 215 PRO A O   1 
ATOM   1706 O  O   B PRO A 1 214 ? 1.144  -10.098 17.487  0.50 10.50 ? 215 PRO A O   1 
ATOM   1707 C  CB  A PRO A 1 214 ? 3.892  -10.879 18.246  0.50 13.18 ? 215 PRO A CB  1 
ATOM   1708 C  CB  B PRO A 1 214 ? 4.022  -10.879 18.323  0.50 12.05 ? 215 PRO A CB  1 
ATOM   1709 C  CG  A PRO A 1 214 ? 3.049  -11.820 19.075  0.50 13.18 ? 215 PRO A CG  1 
ATOM   1710 C  CG  B PRO A 1 214 ? 4.150  -11.331 19.752  0.50 12.79 ? 215 PRO A CG  1 
ATOM   1711 C  CD  A PRO A 1 214 ? 2.475  -10.979 20.213  0.50 13.30 ? 215 PRO A CD  1 
ATOM   1712 C  CD  B PRO A 1 214 ? 2.898  -10.830 20.455  0.50 12.28 ? 215 PRO A CD  1 
ATOM   1713 N  N   . ILE A 1 215 ? 2.566  -8.955  16.150  1.00 11.60 ? 216 ILE A N   1 
ATOM   1714 C  CA  . ILE A 1 215 ? 1.734  -9.155  14.963  1.00 11.79 ? 216 ILE A CA  1 
ATOM   1715 C  C   . ILE A 1 215 ? 2.237  -10.445 14.305  1.00 12.01 ? 216 ILE A C   1 
ATOM   1716 O  O   . ILE A 1 215 ? 3.417  -10.799 14.400  1.00 14.40 ? 216 ILE A O   1 
ATOM   1717 C  CB  . ILE A 1 215 ? 1.724  -7.951  13.977  1.00 13.62 ? 216 ILE A CB  1 
ATOM   1718 C  CG1 . ILE A 1 215 ? 3.141  -7.593  13.505  1.00 12.90 ? 216 ILE A CG1 1 
ATOM   1719 C  CG2 . ILE A 1 215 ? 1.053  -6.747  14.665  1.00 13.80 ? 216 ILE A CG2 1 
ATOM   1720 C  CD1 . ILE A 1 215 ? 3.154  -6.640  12.291  1.00 15.63 ? 216 ILE A CD1 1 
ATOM   1721 N  N   A SER A 1 216 ? 1.308  -11.123 13.627  0.50 13.96 ? 217 SER A N   1 
ATOM   1722 N  N   B SER A 1 216 ? 1.314  -11.193 13.682  0.50 13.64 ? 217 SER A N   1 
ATOM   1723 C  CA  A SER A 1 216 ? 1.598  -12.291 12.806  0.50 15.34 ? 217 SER A CA  1 
ATOM   1724 C  CA  B SER A 1 216 ? 1.667  -12.337 12.841  0.50 14.45 ? 217 SER A CA  1 
ATOM   1725 C  C   A SER A 1 216 ? 1.857  -11.853 11.369  0.50 13.15 ? 217 SER A C   1 
ATOM   1726 C  C   B SER A 1 216 ? 1.879  -11.853 11.409  0.50 13.14 ? 217 SER A C   1 
ATOM   1727 O  O   A SER A 1 216 ? 1.042  -11.135 10.805  0.50 15.10 ? 217 SER A O   1 
ATOM   1728 O  O   B SER A 1 216 ? 1.077  -11.078 10.901  0.50 14.71 ? 217 SER A O   1 
ATOM   1729 C  CB  A SER A 1 216 ? 0.439  -13.262 12.849  0.50 17.89 ? 217 SER A CB  1 
ATOM   1730 C  CB  B SER A 1 216 ? 0.615  -13.454 12.885  0.50 16.39 ? 217 SER A CB  1 
ATOM   1731 O  OG  A SER A 1 216 ? 0.837  -14.489 12.291  0.50 20.51 ? 217 SER A OG  1 
ATOM   1732 O  OG  B SER A 1 216 ? 0.482  -14.025 14.186  0.50 17.80 ? 217 SER A OG  1 
ATOM   1733 N  N   . VAL A 1 217 ? 3.023  -12.227 10.825  1.00 13.67 ? 218 VAL A N   1 
ATOM   1734 C  CA  . VAL A 1 217 ? 3.230  -12.075 9.389   1.00 12.69 ? 218 VAL A CA  1 
ATOM   1735 C  C   . VAL A 1 217 ? 3.501  -13.431 8.782   1.00 14.03 ? 218 VAL A C   1 
ATOM   1736 O  O   . VAL A 1 217 ? 3.855  -14.389 9.472   1.00 13.13 ? 218 VAL A O   1 
ATOM   1737 C  CB  . VAL A 1 217 ? 4.439  -11.153 9.184   1.00 14.05 ? 218 VAL A CB  1 
ATOM   1738 C  CG1 . VAL A 1 217 ? 4.188  -9.803  9.837   1.00 15.35 ? 218 VAL A CG1 1 
ATOM   1739 C  CG2 . VAL A 1 217 ? 5.729  -11.780 9.746   1.00 14.79 ? 218 VAL A CG2 1 
ATOM   1740 N  N   . SER A 1 218 ? 3.335  -13.542 7.442   1.00 13.84 ? 219 SER A N   1 
ATOM   1741 C  CA  . SER A 1 218 ? 3.539  -14.851 6.868   1.00 12.81 ? 219 SER A CA  1 
ATOM   1742 C  C   . SER A 1 218 ? 5.014  -15.060 6.514   1.00 13.01 ? 219 SER A C   1 
ATOM   1743 O  O   . SER A 1 218 ? 5.778  -14.101 6.366   1.00 13.47 ? 219 SER A O   1 
ATOM   1744 C  CB  . SER A 1 218 ? 2.675  -15.063 5.686   1.00 12.70 ? 219 SER A CB  1 
ATOM   1745 O  OG  . SER A 1 218 ? 3.036  -14.190 4.624   1.00 15.85 ? 219 SER A OG  1 
ATOM   1746 N  N   . SER A 1 219 ? 5.379  -16.344 6.342   1.00 14.71 ? 220 SER A N   1 
ATOM   1747 C  CA  . SER A 1 219 ? 6.721  -16.681 5.891   1.00 15.49 ? 220 SER A CA  1 
ATOM   1748 C  C   . SER A 1 219 ? 6.986  -15.973 4.550   1.00 13.08 ? 220 SER A C   1 
ATOM   1749 O  O   . SER A 1 219 ? 8.079  -15.503 4.319   1.00 17.94 ? 220 SER A O   1 
ATOM   1750 C  CB  . SER A 1 219 ? 6.854  -18.181 5.800   1.00 20.29 ? 220 SER A CB  1 
ATOM   1751 O  OG  . SER A 1 219 ? 5.887  -18.749 4.895   1.00 23.79 ? 220 SER A OG  1 
ATOM   1752 N  N   . GLU A 1 220 ? 5.978  -15.924 3.643   1.00 13.91 ? 221 GLU A N   1 
ATOM   1753 C  CA  . GLU A 1 220 ? 6.188  -15.243 2.374   1.00 16.39 ? 221 GLU A CA  1 
ATOM   1754 C  C   . GLU A 1 220 ? 6.509  -13.761 2.556   1.00 13.67 ? 221 GLU A C   1 
ATOM   1755 O  O   . GLU A 1 220 ? 7.315  -13.187 1.820   1.00 14.98 ? 221 GLU A O   1 
ATOM   1756 C  CB  . GLU A 1 220 ? 4.965  -15.310 1.443   1.00 16.24 ? 221 GLU A CB  1 
ATOM   1757 C  CG  . GLU A 1 220 ? 4.647  -16.714 0.969   1.00 20.19 ? 221 GLU A CG  1 
ATOM   1758 C  CD  . GLU A 1 220 ? 3.661  -17.512 1.800   1.00 24.36 ? 221 GLU A CD  1 
ATOM   1759 O  OE1 . GLU A 1 220 ? 3.420  -17.128 2.974   1.00 23.06 ? 221 GLU A OE1 1 
ATOM   1760 O  OE2 . GLU A 1 220 ? 3.046  -18.451 1.233   1.00 30.72 ? 221 GLU A OE2 1 
ATOM   1761 N  N   . GLN A 1 221 ? 5.881  -13.108 3.528   1.00 13.11 ? 222 GLN A N   1 
ATOM   1762 C  CA  . GLN A 1 221 ? 6.138  -11.715 3.769   1.00 12.33 ? 222 GLN A CA  1 
ATOM   1763 C  C   . GLN A 1 221 ? 7.582  -11.528 4.228   1.00 13.95 ? 222 GLN A C   1 
ATOM   1764 O  O   . GLN A 1 221 ? 8.261  -10.653 3.730   1.00 13.91 ? 222 GLN A O   1 
ATOM   1765 C  CB  . GLN A 1 221 ? 5.107  -11.183 4.772   1.00 13.09 ? 222 GLN A CB  1 
ATOM   1766 C  CG  . GLN A 1 221 ? 3.707  -11.100 4.118   1.00 12.80 ? 222 GLN A CG  1 
ATOM   1767 C  CD  . GLN A 1 221 ? 2.617  -10.574 5.026   1.00 11.75 ? 222 GLN A CD  1 
ATOM   1768 O  OE1 . GLN A 1 221 ? 2.618  -10.882 6.250   1.00 13.18 ? 222 GLN A OE1 1 
ATOM   1769 N  NE2 . GLN A 1 221 ? 1.819  -9.650  4.516   1.00 13.21 ? 222 GLN A NE2 1 
ATOM   1770 N  N   . VAL A 1 222 ? 8.000  -12.297 5.250   1.00 13.95 ? 223 VAL A N   1 
ATOM   1771 C  CA  . VAL A 1 222 ? 9.353  -12.138 5.774   1.00 14.42 ? 223 VAL A CA  1 
ATOM   1772 C  C   . VAL A 1 222 ? 10.407 -12.536 4.721   1.00 14.87 ? 223 VAL A C   1 
ATOM   1773 O  O   . VAL A 1 222 ? 11.471 -11.925 4.645   1.00 14.03 ? 223 VAL A O   1 
ATOM   1774 C  CB  . VAL A 1 222 ? 9.528  -12.787 7.172   1.00 17.17 ? 223 VAL A CB  1 
ATOM   1775 C  CG1 . VAL A 1 222 ? 9.316  -14.282 7.176   1.00 26.50 ? 223 VAL A CG1 1 
ATOM   1776 C  CG2 . VAL A 1 222 ? 10.853 -12.438 7.850   1.00 20.67 ? 223 VAL A CG2 1 
ATOM   1777 N  N   . LEU A 1 223 ? 10.122 -13.552 3.891   1.00 13.95 ? 224 LEU A N   1 
ATOM   1778 C  CA  . LEU A 1 223 ? 11.055 -13.938 2.834   1.00 15.52 ? 224 LEU A CA  1 
ATOM   1779 C  C   . LEU A 1 223 ? 11.353 -12.747 1.914   1.00 15.70 ? 224 LEU A C   1 
ATOM   1780 O  O   . LEU A 1 223 ? 12.461 -12.627 1.414   1.00 15.86 ? 224 LEU A O   1 
ATOM   1781 C  CB  . LEU A 1 223 ? 10.512 -15.184 2.124   1.00 20.64 ? 224 LEU A CB  1 
ATOM   1782 C  CG  . LEU A 1 223 ? 11.142 -15.588 0.799   1.00 29.77 ? 224 LEU A CG  1 
ATOM   1783 N  N   . LYS A 1 224 ? 10.365 -11.877 1.683   1.00 12.97 ? 225 LYS A N   1 
ATOM   1784 C  CA  . LYS A 1 224 ? 10.568 -10.705 0.851   1.00 15.03 ? 225 LYS A CA  1 
ATOM   1785 C  C   . LYS A 1 224 ? 11.544 -9.722  1.479   1.00 13.48 ? 225 LYS A C   1 
ATOM   1786 O  O   . LYS A 1 224 ? 12.323 -9.118  0.780   1.00 14.20 ? 225 LYS A O   1 
ATOM   1787 C  CB  . LYS A 1 224 ? 9.244  -10.069 0.411   1.00 19.39 ? 225 LYS A CB  1 
ATOM   1788 C  CG  . LYS A 1 224 ? 8.551  -10.926 -0.630  1.00 23.03 ? 225 LYS A CG  1 
ATOM   1789 C  CD  . LYS A 1 224 ? 7.113  -10.594 -0.990  1.00 31.18 ? 225 LYS A CD  1 
ATOM   1790 C  CE  . LYS A 1 224 ? 6.691  -11.171 -2.330  1.00 42.26 ? 225 LYS A CE  1 
ATOM   1791 N  NZ  . LYS A 1 224 ? 5.488  -12.037 -2.239  1.00 44.30 ? 225 LYS A NZ  1 
ATOM   1792 N  N   . PHE A 1 225 ? 11.521 -9.590  2.813   1.00 12.33 ? 226 PHE A N   1 
ATOM   1793 C  CA  . PHE A 1 225 ? 12.509 -8.758  3.459   1.00 11.84 ? 226 PHE A CA  1 
ATOM   1794 C  C   . PHE A 1 225 ? 13.913 -9.279  3.167   1.00 11.73 ? 226 PHE A C   1 
ATOM   1795 O  O   . PHE A 1 225 ? 14.836 -8.499  2.993   1.00 13.77 ? 226 PHE A O   1 
ATOM   1796 C  CB  . PHE A 1 225 ? 12.355 -8.803  4.998   1.00 11.53 ? 226 PHE A CB  1 
ATOM   1797 C  CG  . PHE A 1 225 ? 11.182 -8.077  5.627   1.00 13.49 ? 226 PHE A CG  1 
ATOM   1798 C  CD1 . PHE A 1 225 ? 10.150 -7.507  4.899   1.00 15.78 ? 226 PHE A CD1 1 
ATOM   1799 C  CD2 . PHE A 1 225 ? 11.068 -8.031  6.999   1.00 14.94 ? 226 PHE A CD2 1 
ATOM   1800 C  CE1 . PHE A 1 225 ? 9.073  -6.863  5.490   1.00 16.54 ? 226 PHE A CE1 1 
ATOM   1801 C  CE2 . PHE A 1 225 ? 10.015 -7.376  7.605   1.00 17.45 ? 226 PHE A CE2 1 
ATOM   1802 C  CZ  . PHE A 1 225 ? 9.014  -6.791  6.869   1.00 15.33 ? 226 PHE A CZ  1 
ATOM   1803 N  N   . ARG A 1 226 ? 14.056 -10.619 3.188   1.00 12.37 ? 227 ARG A N   1 
ATOM   1804 C  CA  . ARG A 1 226 ? 15.357 -11.247 3.079   1.00 12.34 ? 227 ARG A CA  1 
ATOM   1805 C  C   . ARG A 1 226 ? 15.884 -11.207 1.647   1.00 13.64 ? 227 ARG A C   1 
ATOM   1806 O  O   . ARG A 1 226 ? 16.995 -11.668 1.419   1.00 18.23 ? 227 ARG A O   1 
ATOM   1807 C  CB  . ARG A 1 226 ? 15.285 -12.696 3.506   1.00 12.39 ? 227 ARG A CB  1 
ATOM   1808 C  CG  . ARG A 1 226 ? 14.960 -12.856 4.992   1.00 11.59 ? 227 ARG A CG  1 
ATOM   1809 C  CD  . ARG A 1 226 ? 15.086 -14.312 5.442   1.00 13.12 ? 227 ARG A CD  1 
ATOM   1810 N  NE  . ARG A 1 226 ? 14.593 -14.448 6.810   1.00 12.94 ? 227 ARG A NE  1 
ATOM   1811 C  CZ  . ARG A 1 226 ? 13.591 -15.250 7.143   1.00 14.74 ? 227 ARG A CZ  1 
ATOM   1812 N  NH1 . ARG A 1 226 ? 13.040 -16.041 6.234   1.00 20.62 ? 227 ARG A NH1 1 
ATOM   1813 N  NH2 . ARG A 1 226 ? 13.130 -15.303 8.377   1.00 17.14 ? 227 ARG A NH2 1 
ATOM   1814 N  N   . LYS A 1 227 ? 15.110 -10.696 0.678   1.00 12.82 ? 228 LYS A N   1 
ATOM   1815 C  CA  . LYS A 1 227 ? 15.670 -10.591 -0.672  1.00 12.56 ? 228 LYS A CA  1 
ATOM   1816 C  C   . LYS A 1 227 ? 16.376 -9.245  -0.892  1.00 13.58 ? 228 LYS A C   1 
ATOM   1817 O  O   . LYS A 1 227 ? 17.033 -9.026  -1.930  1.00 15.78 ? 228 LYS A O   1 
ATOM   1818 C  CB  . LYS A 1 227 ? 14.526 -10.713 -1.687  1.00 15.49 ? 228 LYS A CB  1 
ATOM   1819 C  CG  . LYS A 1 227 ? 13.880 -12.099 -1.713  1.00 18.94 ? 228 LYS A CG  1 
ATOM   1820 C  CD  . LYS A 1 227 ? 12.757 -12.303 -2.768  1.00 23.02 ? 228 LYS A CD  1 
ATOM   1821 N  N   . LEU A 1 228 ? 16.246 -8.307  0.057   1.00 13.57 ? 229 LEU A N   1 
ATOM   1822 C  CA  . LEU A 1 228 ? 16.949 -7.038  -0.030  1.00 12.76 ? 229 LEU A CA  1 
ATOM   1823 C  C   . LEU A 1 228 ? 18.456 -7.223  0.130   1.00 10.97 ? 229 LEU A C   1 
ATOM   1824 O  O   . LEU A 1 228 ? 18.919 -8.277  0.547   1.00 12.52 ? 229 LEU A O   1 
ATOM   1825 C  CB  . LEU A 1 228 ? 16.454 -6.051  1.034   1.00 13.32 ? 229 LEU A CB  1 
ATOM   1826 C  CG  . LEU A 1 228 ? 14.961 -5.671  0.938   1.00 12.79 ? 229 LEU A CG  1 
ATOM   1827 C  CD1 . LEU A 1 228 ? 14.530 -4.923  2.189   1.00 14.56 ? 229 LEU A CD1 1 
ATOM   1828 C  CD2 . LEU A 1 228 ? 14.738 -4.832  -0.322  1.00 16.56 ? 229 LEU A CD2 1 
ATOM   1829 N  N   . ASN A 1 229 ? 19.206 -6.218  -0.334  1.00 12.42 ? 230 ASN A N   1 
ATOM   1830 C  CA  . ASN A 1 229 ? 20.655 -6.263  -0.287  1.00 12.64 ? 230 ASN A CA  1 
ATOM   1831 C  C   . ASN A 1 229 ? 21.193 -5.073  0.518   1.00 13.85 ? 230 ASN A C   1 
ATOM   1832 O  O   . ASN A 1 229 ? 20.702 -3.957  0.409   1.00 13.06 ? 230 ASN A O   1 
ATOM   1833 C  CB  . ASN A 1 229 ? 21.279 -6.110  -1.676  1.00 14.66 ? 230 ASN A CB  1 
ATOM   1834 C  CG  . ASN A 1 229 ? 21.166 -7.299  -2.612  1.00 17.91 ? 230 ASN A CG  1 
ATOM   1835 O  OD1 . ASN A 1 229 ? 21.629 -7.186  -3.747  1.00 22.82 ? 230 ASN A OD1 1 
ATOM   1836 N  ND2 . ASN A 1 229 ? 20.509 -8.377  -2.222  1.00 19.05 ? 230 ASN A ND2 1 
ATOM   1837 N  N   . PHE A 1 230 ? 22.242 -5.330  1.322   1.00 11.69 ? 231 PHE A N   1 
ATOM   1838 C  CA  . PHE A 1 230 ? 22.923 -4.224  1.957   1.00 12.83 ? 231 PHE A CA  1 
ATOM   1839 C  C   . PHE A 1 230 ? 23.718 -3.374  0.937   1.00 15.28 ? 231 PHE A C   1 
ATOM   1840 O  O   . PHE A 1 230 ? 23.864 -2.154  1.079   1.00 15.17 ? 231 PHE A O   1 
ATOM   1841 C  CB  . PHE A 1 230 ? 23.941 -4.771  2.947   1.00 15.43 ? 231 PHE A CB  1 
ATOM   1842 C  CG  . PHE A 1 230 ? 23.466 -5.375  4.240   1.00 12.29 ? 231 PHE A CG  1 
ATOM   1843 C  CD1 . PHE A 1 230 ? 22.659 -4.632  5.091   1.00 14.09 ? 231 PHE A CD1 1 
ATOM   1844 C  CD2 . PHE A 1 230 ? 23.833 -6.677  4.584   1.00 14.51 ? 231 PHE A CD2 1 
ATOM   1845 C  CE1 . PHE A 1 230 ? 22.273 -5.171  6.312   1.00 14.50 ? 231 PHE A CE1 1 
ATOM   1846 C  CE2 . PHE A 1 230 ? 23.447 -7.215  5.806   1.00 14.88 ? 231 PHE A CE2 1 
ATOM   1847 C  CZ  . PHE A 1 230 ? 22.682 -6.454  6.674   1.00 14.57 ? 231 PHE A CZ  1 
ATOM   1848 N  N   . ASN A 1 231 ? 24.211 -4.008  -0.126  1.00 15.44 ? 232 ASN A N   1 
ATOM   1849 C  CA  . ASN A 1 231 ? 25.086 -3.330  -1.071  1.00 16.49 ? 232 ASN A CA  1 
ATOM   1850 C  C   . ASN A 1 231 ? 24.304 -2.464  -2.038  1.00 17.05 ? 232 ASN A C   1 
ATOM   1851 O  O   . ASN A 1 231 ? 23.098 -2.685  -2.260  1.00 15.22 ? 232 ASN A O   1 
ATOM   1852 C  CB  . ASN A 1 231 ? 25.868 -4.348  -1.906  1.00 17.55 ? 232 ASN A CB  1 
ATOM   1853 C  CG  . ASN A 1 231 ? 24.955 -5.370  -2.558  1.00 17.17 ? 232 ASN A CG  1 
ATOM   1854 O  OD1 . ASN A 1 231 ? 24.435 -6.269  -1.877  1.00 16.60 ? 232 ASN A OD1 1 
ATOM   1855 N  ND2 . ASN A 1 231 ? 24.721 -5.234  -3.870  1.00 17.63 ? 232 ASN A ND2 1 
ATOM   1856 N  N   . GLY A 1 232 ? 25.069 -1.627  -2.748  1.00 16.05 ? 233 GLY A N   1 
ATOM   1857 C  CA  . GLY A 1 232 ? 24.522 -0.847  -3.854  1.00 18.07 ? 233 GLY A CA  1 
ATOM   1858 C  C   . GLY A 1 232 ? 24.583 -1.693  -5.113  1.00 17.98 ? 233 GLY A C   1 
ATOM   1859 O  O   . GLY A 1 232 ? 25.316 -2.681  -5.141  1.00 20.43 ? 233 GLY A O   1 
ATOM   1860 N  N   . GLU A 1 233 ? 23.809 -1.275  -6.133  1.00 19.01 ? 234 GLU A N   1 
ATOM   1861 C  CA  . GLU A 1 233 ? 23.839 -1.996  -7.396  1.00 19.19 ? 234 GLU A CA  1 
ATOM   1862 C  C   . GLU A 1 233 ? 25.263 -1.882  -7.946  1.00 20.55 ? 234 GLU A C   1 
ATOM   1863 O  O   . GLU A 1 233 ? 25.867 -0.803  -7.860  1.00 19.75 ? 234 GLU A O   1 
ATOM   1864 C  CB  . GLU A 1 233 ? 22.771 -1.468  -8.369  1.00 25.87 ? 234 GLU A CB  1 
ATOM   1865 C  CG  . GLU A 1 233 ? 22.741 -2.197  -9.725  1.00 24.80 ? 234 GLU A CG  1 
ATOM   1866 N  N   . GLY A 1 234 ? 25.802 -3.009  -8.444  1.00 25.17 ? 235 GLY A N   1 
ATOM   1867 C  CA  . GLY A 1 234 ? 27.124 -3.070  -9.054  1.00 29.78 ? 235 GLY A CA  1 
ATOM   1868 C  C   . GLY A 1 234 ? 28.215 -3.317  -8.015  1.00 29.88 ? 235 GLY A C   1 
ATOM   1869 O  O   . GLY A 1 234 ? 29.398 -3.360  -8.319  1.00 36.35 ? 235 GLY A O   1 
ATOM   1870 N  N   . GLU A 1 235 ? 27.819 -3.471  -6.760  1.00 25.30 ? 236 GLU A N   1 
ATOM   1871 C  CA  . GLU A 1 235 ? 28.822 -3.792  -5.758  1.00 21.04 ? 236 GLU A CA  1 
ATOM   1872 C  C   . GLU A 1 235 ? 28.658 -5.266  -5.420  1.00 20.66 ? 236 GLU A C   1 
ATOM   1873 O  O   . GLU A 1 235 ? 27.608 -5.856  -5.679  1.00 20.00 ? 236 GLU A O   1 
ATOM   1874 C  CB  . GLU A 1 235 ? 28.635 -2.973  -4.472  1.00 25.68 ? 236 GLU A CB  1 
ATOM   1875 C  CG  . GLU A 1 235 ? 28.824 -1.475  -4.666  1.00 30.17 ? 236 GLU A CG  1 
ATOM   1876 C  CD  . GLU A 1 235 ? 28.451 -0.582  -3.483  1.00 35.22 ? 236 GLU A CD  1 
ATOM   1877 O  OE1 . GLU A 1 235 ? 27.842 -1.079  -2.478  1.00 32.44 ? 236 GLU A OE1 1 
ATOM   1878 O  OE2 . GLU A 1 235 ? 28.770 0.626   -3.562  1.00 43.92 ? 236 GLU A OE2 1 
ATOM   1879 N  N   . PRO A 1 236 ? 29.622 -5.883  -4.699  1.00 19.05 ? 237 PRO A N   1 
ATOM   1880 C  CA  . PRO A 1 236 ? 29.470 -7.288  -4.292  1.00 19.49 ? 237 PRO A CA  1 
ATOM   1881 C  C   . PRO A 1 236 ? 28.192 -7.508  -3.477  1.00 21.26 ? 237 PRO A C   1 
ATOM   1882 O  O   . PRO A 1 236 ? 27.887 -6.740  -2.558  1.00 21.54 ? 237 PRO A O   1 
ATOM   1883 C  CB  . PRO A 1 236 ? 30.707 -7.553  -3.435  1.00 26.80 ? 237 PRO A CB  1 
ATOM   1884 C  CG  . PRO A 1 236 ? 31.702 -6.539  -3.954  1.00 31.06 ? 237 PRO A CG  1 
ATOM   1885 C  CD  . PRO A 1 236 ? 30.906 -5.293  -4.301  1.00 31.11 ? 237 PRO A CD  1 
ATOM   1886 N  N   . GLU A 1 237 ? 27.488 -8.593  -3.806  1.00 17.62 ? 238 GLU A N   1 
ATOM   1887 C  CA  . GLU A 1 237 ? 26.214 -8.956  -3.210  1.00 18.00 ? 238 GLU A CA  1 
ATOM   1888 C  C   . GLU A 1 237 ? 26.439 -9.347  -1.755  1.00 18.70 ? 238 GLU A C   1 
ATOM   1889 O  O   . GLU A 1 237 ? 27.301 -10.181 -1.419  1.00 21.28 ? 238 GLU A O   1 
ATOM   1890 C  CB  . GLU A 1 237 ? 25.526 -10.099 -3.966  1.00 19.15 ? 238 GLU A CB  1 
ATOM   1891 C  CG  . GLU A 1 237 ? 24.104 -10.363 -3.565  1.00 24.20 ? 238 GLU A CG  1 
ATOM   1892 C  CD  . GLU A 1 237 ? 23.500 -11.561 -4.278  1.00 23.28 ? 238 GLU A CD  1 
ATOM   1893 O  OE1 . GLU A 1 237 ? 23.992 -11.914 -5.368  1.00 33.00 ? 238 GLU A OE1 1 
ATOM   1894 O  OE2 . GLU A 1 237 ? 22.465 -12.033 -3.806  1.00 33.57 ? 238 GLU A OE2 1 
ATOM   1895 N  N   . GLU A 1 238 ? 25.658 -8.684  -0.894  1.00 17.47 ? 239 GLU A N   1 
ATOM   1896 C  CA  . GLU A 1 238 ? 25.490 -9.090  0.488   1.00 17.85 ? 239 GLU A CA  1 
ATOM   1897 C  C   . GLU A 1 238 ? 24.003 -8.980  0.849   1.00 14.20 ? 239 GLU A C   1 
ATOM   1898 O  O   . GLU A 1 238 ? 23.466 -7.881  0.885   1.00 15.97 ? 239 GLU A O   1 
ATOM   1899 C  CB  . GLU A 1 238 ? 26.280 -8.127  1.372   1.00 22.46 ? 239 GLU A CB  1 
ATOM   1900 C  CG  . GLU A 1 238 ? 27.738 -7.991  1.087   1.00 29.70 ? 239 GLU A CG  1 
ATOM   1901 C  CD  . GLU A 1 238 ? 28.340 -7.223  2.252   1.00 47.66 ? 239 GLU A CD  1 
ATOM   1902 O  OE1 . GLU A 1 238 ? 28.248 -7.722  3.427   1.00 53.69 ? 239 GLU A OE1 1 
ATOM   1903 O  OE2 . GLU A 1 238 ? 28.839 -6.097  2.004   1.00 55.38 ? 239 GLU A OE2 1 
ATOM   1904 N  N   . LEU A 1 239 ? 23.354 -10.108 1.131   1.00 16.95 ? 240 LEU A N   1 
ATOM   1905 C  CA  . LEU A 1 239 ? 21.923 -10.088 1.451   1.00 14.40 ? 240 LEU A CA  1 
ATOM   1906 C  C   . LEU A 1 239 ? 21.682 -9.301  2.740   1.00 13.63 ? 240 LEU A C   1 
ATOM   1907 O  O   . LEU A 1 239 ? 22.429 -9.439  3.738   1.00 14.24 ? 240 LEU A O   1 
ATOM   1908 C  CB  . LEU A 1 239 ? 21.409 -11.506 1.691   1.00 19.43 ? 240 LEU A CB  1 
ATOM   1909 C  CG  . LEU A 1 239 ? 20.725 -12.313 0.623   1.00 27.93 ? 240 LEU A CG  1 
ATOM   1910 C  CD1 . LEU A 1 239 ? 19.984 -13.432 1.344   1.00 27.35 ? 240 LEU A CD1 1 
ATOM   1911 C  CD2 . LEU A 1 239 ? 19.833 -11.476 -0.255  1.00 19.19 ? 240 LEU A CD2 1 
ATOM   1912 N  N   . MET A 1 240 ? 20.611 -8.529  2.742   1.00 12.90 ? 241 MET A N   1 
ATOM   1913 C  CA  . MET A 1 240 ? 20.231 -7.752  3.914   1.00 11.79 ? 241 MET A CA  1 
ATOM   1914 C  C   . MET A 1 240 ? 19.443 -8.667  4.829   1.00 13.27 ? 241 MET A C   1 
ATOM   1915 O  O   . MET A 1 240 ? 18.245 -8.805  4.701   1.00 12.63 ? 241 MET A O   1 
ATOM   1916 C  CB  . MET A 1 240 ? 19.370 -6.536  3.519   1.00 12.05 ? 241 MET A CB  1 
ATOM   1917 C  CG  . MET A 1 240 ? 19.063 -5.620  4.735   1.00 13.83 ? 241 MET A CG  1 
ATOM   1918 S  SD  . MET A 1 240 ? 18.030 -4.228  4.204   1.00 13.90 ? 241 MET A SD  1 
ATOM   1919 C  CE  . MET A 1 240 ? 19.299 -3.183  3.424   1.00 15.13 ? 241 MET A CE  1 
ATOM   1920 N  N   . VAL A 1 241 ? 20.161 -9.288  5.769   1.00 12.39 ? 242 VAL A N   1 
ATOM   1921 C  CA  . VAL A 1 241 ? 19.602 -10.188 6.760   1.00 11.81 ? 242 VAL A CA  1 
ATOM   1922 C  C   . VAL A 1 241 ? 20.422 -9.970  8.018   1.00 10.66 ? 242 VAL A C   1 
ATOM   1923 O  O   . VAL A 1 241 ? 21.576 -9.536  7.952   1.00 13.83 ? 242 VAL A O   1 
ATOM   1924 C  CB  . VAL A 1 241 ? 19.662 -11.675 6.337   1.00 11.69 ? 242 VAL A CB  1 
ATOM   1925 C  CG1 . VAL A 1 241 ? 18.663 -11.989 5.226   1.00 14.81 ? 242 VAL A CG1 1 
ATOM   1926 C  CG2 . VAL A 1 241 ? 21.046 -12.118 5.923   1.00 14.94 ? 242 VAL A CG2 1 
ATOM   1927 N  N   . ASP A 1 242 ? 19.745 -10.229 9.149   1.00 9.70  ? 243 ASP A N   1 
ATOM   1928 C  CA  . ASP A 1 242 ? 20.395 -10.148 10.474  1.00 11.03 ? 243 ASP A CA  1 
ATOM   1929 C  C   . ASP A 1 242 ? 20.858 -8.721  10.770  1.00 10.92 ? 243 ASP A C   1 
ATOM   1930 O  O   . ASP A 1 242 ? 21.992 -8.497  11.271  1.00 13.66 ? 243 ASP A O   1 
ATOM   1931 C  CB  . ASP A 1 242 ? 21.487 -11.204 10.669  1.00 12.28 ? 243 ASP A CB  1 
ATOM   1932 C  CG  . ASP A 1 242 ? 20.916 -12.598 10.770  1.00 11.99 ? 243 ASP A CG  1 
ATOM   1933 O  OD1 . ASP A 1 242 ? 19.855 -12.757 11.455  1.00 12.90 ? 243 ASP A OD1 1 
ATOM   1934 O  OD2 . ASP A 1 242 ? 21.522 -13.516 10.223  1.00 15.33 ? 243 ASP A OD2 1 
ATOM   1935 N  N   . ASN A 1 243 ? 19.987 -7.745  10.530  1.00 9.82  ? 244 ASN A N   1 
ATOM   1936 C  CA  . ASN A 1 243 ? 20.316 -6.329  10.759  1.00 8.77  ? 244 ASN A CA  1 
ATOM   1937 C  C   . ASN A 1 243 ? 19.754 -5.908  12.124  1.00 10.76 ? 244 ASN A C   1 
ATOM   1938 O  O   . ASN A 1 243 ? 19.039 -4.930  12.233  1.00 12.86 ? 244 ASN A O   1 
ATOM   1939 C  CB  . ASN A 1 243 ? 19.815 -5.440  9.607   1.00 10.34 ? 244 ASN A CB  1 
ATOM   1940 C  CG  . ASN A 1 243 ? 18.344 -5.618  9.289   1.00 10.37 ? 244 ASN A CG  1 
ATOM   1941 O  OD1 . ASN A 1 243 ? 17.671 -6.477  9.863   1.00 12.57 ? 244 ASN A OD1 1 
ATOM   1942 N  ND2 . ASN A 1 243 ? 17.797 -4.793  8.404   1.00 13.15 ? 244 ASN A ND2 1 
ATOM   1943 N  N   . TRP A 1 244 ? 20.087 -6.702  13.155  1.00 11.04 ? 245 TRP A N   1 
ATOM   1944 C  CA  . TRP A 1 244 ? 19.626 -6.464  14.510  1.00 9.30  ? 245 TRP A CA  1 
ATOM   1945 C  C   . TRP A 1 244 ? 20.819 -6.389  15.454  1.00 10.34 ? 245 TRP A C   1 
ATOM   1946 O  O   . TRP A 1 244 ? 21.764 -7.113  15.312  1.00 12.59 ? 245 TRP A O   1 
ATOM   1947 C  CB  . TRP A 1 244 ? 18.648 -7.526  14.987  1.00 10.63 ? 245 TRP A CB  1 
ATOM   1948 C  CG  . TRP A 1 244 ? 19.070 -8.946  14.755  1.00 10.75 ? 245 TRP A CG  1 
ATOM   1949 C  CD1 . TRP A 1 244 ? 19.041 -9.654  13.587  1.00 11.07 ? 245 TRP A CD1 1 
ATOM   1950 C  CD2 . TRP A 1 244 ? 19.668 -9.837  15.722  1.00 12.80 ? 245 TRP A CD2 1 
ATOM   1951 N  NE1 . TRP A 1 244 ? 19.471 -10.938 13.749  1.00 11.20 ? 245 TRP A NE1 1 
ATOM   1952 C  CE2 . TRP A 1 244 ? 19.868 -11.087 15.087  1.00 13.58 ? 245 TRP A CE2 1 
ATOM   1953 C  CE3 . TRP A 1 244 ? 19.904 -9.719  17.114  1.00 12.33 ? 245 TRP A CE3 1 
ATOM   1954 C  CZ2 . TRP A 1 244 ? 20.417 -12.157 15.806  1.00 13.53 ? 245 TRP A CZ2 1 
ATOM   1955 C  CZ3 . TRP A 1 244 ? 20.488 -10.767 17.802  1.00 13.08 ? 245 TRP A CZ3 1 
ATOM   1956 C  CH2 . TRP A 1 244 ? 20.737 -11.984 17.157  1.00 13.54 ? 245 TRP A CH2 1 
ATOM   1957 N  N   . ARG A 1 245 ? 20.691 -5.484  16.423  1.00 11.58 ? 246 ARG A N   1 
ATOM   1958 C  CA  . ARG A 1 245 ? 21.636 -5.371  17.537  1.00 11.00 ? 246 ARG A CA  1 
ATOM   1959 C  C   . ARG A 1 245 ? 21.134 -6.316  18.622  1.00 10.70 ? 246 ARG A C   1 
ATOM   1960 O  O   . ARG A 1 245 ? 19.956 -6.336  18.941  1.00 12.84 ? 246 ARG A O   1 
ATOM   1961 C  CB  . ARG A 1 245 ? 21.656 -3.946  18.106  1.00 10.70 ? 246 ARG A CB  1 
ATOM   1962 C  CG  . ARG A 1 245 ? 22.798 -3.745  19.110  1.00 11.57 ? 246 ARG A CG  1 
ATOM   1963 C  CD  . ARG A 1 245 ? 22.735 -2.357  19.727  1.00 11.24 ? 246 ARG A CD  1 
ATOM   1964 N  NE  . ARG A 1 245 ? 23.948 -2.092  20.487  1.00 12.30 ? 246 ARG A NE  1 
ATOM   1965 C  CZ  . ARG A 1 245 ? 24.141 -1.072  21.312  1.00 12.99 ? 246 ARG A CZ  1 
ATOM   1966 N  NH1 . ARG A 1 245 ? 23.179 -0.237  21.593  1.00 14.43 ? 246 ARG A NH1 1 
ATOM   1967 N  NH2 . ARG A 1 245 ? 25.351 -0.878  21.848  1.00 15.04 ? 246 ARG A NH2 1 
ATOM   1968 N  N   . PRO A 1 246 ? 22.022 -7.120  19.238  1.00 12.21 ? 247 PRO A N   1 
ATOM   1969 C  CA  . PRO A 1 246 ? 21.632 -7.972  20.344  1.00 14.53 ? 247 PRO A CA  1 
ATOM   1970 C  C   . PRO A 1 246 ? 21.344 -7.173  21.626  1.00 12.20 ? 247 PRO A C   1 
ATOM   1971 O  O   . PRO A 1 246 ? 21.687 -6.009  21.726  1.00 13.40 ? 247 PRO A O   1 
ATOM   1972 C  CB  . PRO A 1 246 ? 22.848 -8.844  20.643  1.00 15.47 ? 247 PRO A CB  1 
ATOM   1973 C  CG  . PRO A 1 246 ? 23.864 -8.569  19.575  1.00 19.63 ? 247 PRO A CG  1 
ATOM   1974 C  CD  . PRO A 1 246 ? 23.427 -7.296  18.869  1.00 14.02 ? 247 PRO A CD  1 
ATOM   1975 N  N   . ALA A 1 247 ? 20.672 -7.849  22.578  1.00 13.30 ? 248 ALA A N   1 
ATOM   1976 C  CA  . ALA A 1 247 ? 20.349 -7.268  23.877  1.00 13.44 ? 248 ALA A CA  1 
ATOM   1977 C  C   . ALA A 1 247 ? 21.608 -6.778  24.598  1.00 13.83 ? 248 ALA A C   1 
ATOM   1978 O  O   . ALA A 1 247 ? 22.662 -7.444  24.617  1.00 16.32 ? 248 ALA A O   1 
ATOM   1979 C  CB  . ALA A 1 247 ? 19.577 -8.272  24.730  1.00 14.47 ? 248 ALA A CB  1 
ATOM   1980 N  N   . GLN A 1 248 ? 21.433 -5.600  25.192  1.00 13.35 ? 249 GLN A N   1 
ATOM   1981 C  CA  . GLN A 1 248 ? 22.478 -4.882  25.904  1.00 14.33 ? 249 GLN A CA  1 
ATOM   1982 C  C   . GLN A 1 248 ? 22.173 -4.925  27.395  1.00 14.68 ? 249 GLN A C   1 
ATOM   1983 O  O   . GLN A 1 248 ? 21.036 -5.129  27.763  1.00 15.13 ? 249 GLN A O   1 
ATOM   1984 C  CB  . GLN A 1 248 ? 22.536 -3.436  25.409  1.00 13.06 ? 249 GLN A CB  1 
ATOM   1985 C  CG  . GLN A 1 248 ? 22.770 -3.348  23.906  1.00 13.11 ? 249 GLN A CG  1 
ATOM   1986 C  CD  . GLN A 1 248 ? 24.080 -4.045  23.575  1.00 13.73 ? 249 GLN A CD  1 
ATOM   1987 O  OE1 . GLN A 1 248 ? 25.136 -3.699  24.132  1.00 17.38 ? 249 GLN A OE1 1 
ATOM   1988 N  NE2 . GLN A 1 248 ? 24.085 -4.952  22.591  1.00 15.14 ? 249 GLN A NE2 1 
ATOM   1989 N  N   . PRO A 1 249 ? 23.169 -4.701  28.294  1.00 15.39 ? 250 PRO A N   1 
ATOM   1990 C  CA  . PRO A 1 249 ? 22.904 -4.816  29.730  1.00 15.37 ? 250 PRO A CA  1 
ATOM   1991 C  C   . PRO A 1 249 ? 21.863 -3.801  30.203  1.00 16.00 ? 250 PRO A C   1 
ATOM   1992 O  O   . PRO A 1 249 ? 21.947 -2.628  29.865  1.00 14.95 ? 250 PRO A O   1 
ATOM   1993 C  CB  . PRO A 1 249 ? 24.277 -4.460  30.344  1.00 17.18 ? 250 PRO A CB  1 
ATOM   1994 C  CG  . PRO A 1 249 ? 25.295 -4.607  29.242  1.00 19.44 ? 250 PRO A CG  1 
ATOM   1995 C  CD  . PRO A 1 249 ? 24.557 -4.384  27.946  1.00 16.29 ? 250 PRO A CD  1 
ATOM   1996 N  N   . LEU A 1 250 ? 20.940 -4.219  31.078  1.00 15.41 ? 251 LEU A N   1 
ATOM   1997 C  CA  . LEU A 1 250 ? 19.935 -3.291  31.623  1.00 15.78 ? 251 LEU A CA  1 
ATOM   1998 C  C   . LEU A 1 250 ? 20.551 -2.253  32.568  1.00 13.16 ? 251 LEU A C   1 
ATOM   1999 O  O   . LEU A 1 250 ? 20.028 -1.137  32.673  1.00 14.69 ? 251 LEU A O   1 
ATOM   2000 C  CB  . LEU A 1 250 ? 18.807 -4.111  32.258  1.00 15.61 ? 251 LEU A CB  1 
ATOM   2001 C  CG  . LEU A 1 250 ? 17.575 -3.326  32.670  1.00 16.04 ? 251 LEU A CG  1 
ATOM   2002 C  CD1 . LEU A 1 250 ? 16.943 -2.704  31.446  1.00 20.44 ? 251 LEU A CD1 1 
ATOM   2003 C  CD2 . LEU A 1 250 ? 16.569 -4.258  33.368  1.00 20.34 ? 251 LEU A CD2 1 
ATOM   2004 N  N   . LYS A 1 251 ? 21.615 -2.626  33.296  1.00 16.58 ? 252 LYS A N   1 
ATOM   2005 C  CA  . LYS A 1 251 ? 22.307 -1.704  34.198  1.00 19.00 ? 252 LYS A CA  1 
ATOM   2006 C  C   . LYS A 1 251 ? 21.326 -1.225  35.273  1.00 20.04 ? 252 LYS A C   1 
ATOM   2007 O  O   . LYS A 1 251 ? 20.663 -2.083  35.860  1.00 23.55 ? 252 LYS A O   1 
ATOM   2008 C  CB  . LYS A 1 251 ? 23.097 -0.671  33.385  1.00 20.69 ? 252 LYS A CB  1 
ATOM   2009 C  CG  . LYS A 1 251 ? 24.128 -1.344  32.489  1.00 25.63 ? 252 LYS A CG  1 
ATOM   2010 C  CD  . LYS A 1 251 ? 25.142 -0.409  31.956  1.00 24.50 ? 252 LYS A CD  1 
ATOM   2011 C  CE  . LYS A 1 251 ? 26.439 -1.083  31.584  1.00 33.86 ? 252 LYS A CE  1 
ATOM   2012 N  NZ  . LYS A 1 251 ? 27.237 -0.215  30.689  1.00 32.80 ? 252 LYS A NZ  1 
ATOM   2013 N  N   . ASN A 1 252 ? 21.190 0.081   35.512  1.00 19.37 ? 253 ASN A N   1 
ATOM   2014 C  CA  . ASN A 1 252 ? 20.397 0.440   36.705  1.00 24.25 ? 253 ASN A CA  1 
ATOM   2015 C  C   . ASN A 1 252 ? 18.903 0.579   36.408  1.00 31.27 ? 253 ASN A C   1 
ATOM   2016 O  O   . ASN A 1 252 ? 18.138 0.933   37.286  1.00 33.91 ? 253 ASN A O   1 
ATOM   2017 C  CB  . ASN A 1 252 ? 20.953 1.622   37.502  1.00 26.51 ? 253 ASN A CB  1 
ATOM   2018 N  N   . ARG A 1 253 ? 18.465 0.253   35.181  1.00 19.64 ? 254 ARG A N   1 
ATOM   2019 C  CA  . ARG A 1 253 ? 17.166 0.704   34.714  1.00 16.27 ? 254 ARG A CA  1 
ATOM   2020 C  C   . ARG A 1 253 ? 16.077 -0.271  35.130  1.00 19.24 ? 254 ARG A C   1 
ATOM   2021 O  O   . ARG A 1 253 ? 16.341 -1.445  35.410  1.00 23.98 ? 254 ARG A O   1 
ATOM   2022 C  CB  . ARG A 1 253 ? 17.160 0.773   33.182  1.00 16.56 ? 254 ARG A CB  1 
ATOM   2023 C  CG  . ARG A 1 253 ? 18.075 1.854   32.643  1.00 16.04 ? 254 ARG A CG  1 
ATOM   2024 C  CD  . ARG A 1 253 ? 18.149 1.756   31.134  1.00 14.56 ? 254 ARG A CD  1 
ATOM   2025 N  NE  . ARG A 1 253 ? 18.925 0.629   30.675  1.00 15.44 ? 254 ARG A NE  1 
ATOM   2026 C  CZ  . ARG A 1 253 ? 19.121 0.321   29.398  1.00 12.80 ? 254 ARG A CZ  1 
ATOM   2027 N  NH1 . ARG A 1 253 ? 18.590 1.069   28.447  1.00 11.55 ? 254 ARG A NH1 1 
ATOM   2028 N  NH2 . ARG A 1 253 ? 19.849 -0.734  29.077  1.00 12.76 ? 254 ARG A NH2 1 
ATOM   2029 N  N   . GLN A 1 254 ? 14.850 0.251   35.129  1.00 20.95 ? 255 GLN A N   1 
ATOM   2030 C  CA  . GLN A 1 254 ? 13.647 -0.517  35.424  1.00 20.02 ? 255 GLN A CA  1 
ATOM   2031 C  C   . GLN A 1 254 ? 12.777 -0.503  34.191  1.00 19.24 ? 255 GLN A C   1 
ATOM   2032 O  O   . GLN A 1 254 ? 12.675 0.507   33.482  1.00 22.38 ? 255 GLN A O   1 
ATOM   2033 C  CB  . GLN A 1 254 ? 12.873 0.143   36.569  1.00 23.91 ? 255 GLN A CB  1 
ATOM   2034 C  CG  . GLN A 1 254 ? 13.578 0.073   37.917  1.00 33.73 ? 255 GLN A CG  1 
ATOM   2035 N  N   . ILE A 1 255 ? 12.199 -1.670  33.912  1.00 16.05 ? 256 ILE A N   1 
ATOM   2036 C  CA  . ILE A 1 255 ? 11.222 -1.713  32.823  1.00 12.60 ? 256 ILE A CA  1 
ATOM   2037 C  C   . ILE A 1 255 ? 9.840  -1.704  33.450  1.00 14.45 ? 256 ILE A C   1 
ATOM   2038 O  O   . ILE A 1 255 ? 9.569  -2.439  34.399  1.00 17.37 ? 256 ILE A O   1 
ATOM   2039 C  CB  . ILE A 1 255 ? 11.401 -2.992  31.988  1.00 14.35 ? 256 ILE A CB  1 
ATOM   2040 C  CG1 . ILE A 1 255 ? 12.794 -3.086  31.346  1.00 15.07 ? 256 ILE A CG1 1 
ATOM   2041 C  CG2 . ILE A 1 255 ? 10.281 -3.104  30.927  1.00 16.22 ? 256 ILE A CG2 1 
ATOM   2042 C  CD1 . ILE A 1 255 ? 13.036 -4.410  30.656  1.00 18.19 ? 256 ILE A CD1 1 
ATOM   2043 N  N   . LYS A 1 256 ? 8.979  -0.815  32.998  1.00 15.36 ? 257 LYS A N   1 
ATOM   2044 C  CA  . LYS A 1 256 ? 7.622  -0.714  33.522  1.00 15.58 ? 257 LYS A CA  1 
ATOM   2045 C  C   . LYS A 1 256 ? 6.649  -1.398  32.588  1.00 13.47 ? 257 LYS A C   1 
ATOM   2046 O  O   . LYS A 1 256 ? 6.915  -1.589  31.385  1.00 15.88 ? 257 LYS A O   1 
ATOM   2047 C  CB  . LYS A 1 256 ? 7.188  0.755   33.607  1.00 16.68 ? 257 LYS A CB  1 
ATOM   2048 C  CG  . LYS A 1 256 ? 8.028  1.590   34.559  1.00 17.26 ? 257 LYS A CG  1 
ATOM   2049 C  CD  . LYS A 1 256 ? 7.648  3.048   34.513  1.00 21.30 ? 257 LYS A CD  1 
ATOM   2050 C  CE  . LYS A 1 256 ? 8.513  3.967   35.336  1.00 30.76 ? 257 LYS A CE  1 
ATOM   2051 N  NZ  . LYS A 1 256 ? 7.794  5.257   35.457  1.00 30.04 ? 257 LYS A NZ  1 
ATOM   2052 N  N   . ALA A 1 257 ? 5.538  -1.872  33.179  1.00 15.46 ? 258 ALA A N   1 
ATOM   2053 C  CA  . ALA A 1 257 ? 4.458  -2.438  32.366  1.00 12.58 ? 258 ALA A CA  1 
ATOM   2054 C  C   . ALA A 1 257 ? 3.224  -1.559  32.490  1.00 13.38 ? 258 ALA A C   1 
ATOM   2055 O  O   . ALA A 1 257 ? 2.943  -1.002  33.544  1.00 14.96 ? 258 ALA A O   1 
ATOM   2056 C  CB  . ALA A 1 257 ? 4.150  -3.840  32.835  1.00 18.25 ? 258 ALA A CB  1 
ATOM   2057 N  N   . SER A 1 258 ? 2.427  -1.463  31.420  1.00 14.21 ? 259 SER A N   1 
ATOM   2058 C  CA  . SER A 1 258 ? 1.181  -0.690  31.426  1.00 15.80 ? 259 SER A CA  1 
ATOM   2059 C  C   . SER A 1 258 ? 0.017  -1.495  31.994  1.00 14.94 ? 259 SER A C   1 
ATOM   2060 O  O   . SER A 1 258 ? -1.083 -0.975  32.115  1.00 20.16 ? 259 SER A O   1 
ATOM   2061 C  CB  . SER A 1 258 ? 0.791  -0.277  29.992  1.00 15.38 ? 259 SER A CB  1 
ATOM   2062 O  OG  . SER A 1 258 ? 0.398  -1.407  29.243  1.00 15.08 ? 259 SER A OG  1 
ATOM   2063 N  N   . PHE A 1 259 ? 0.249  -2.777  32.298  1.00 15.24 ? 260 PHE A N   1 
ATOM   2064 C  CA  . PHE A 1 259 ? -0.817 -3.725  32.572  1.00 17.76 ? 260 PHE A CA  1 
ATOM   2065 C  C   . PHE A 1 259 ? -0.357 -4.611  33.725  1.00 24.53 ? 260 PHE A C   1 
ATOM   2066 O  O   . PHE A 1 259 ? 0.872  -4.788  33.929  1.00 20.19 ? 260 PHE A O   1 
ATOM   2067 C  CB  . PHE A 1 259 ? -1.155 -4.536  31.316  1.00 18.06 ? 260 PHE A CB  1 
ATOM   2068 C  CG  . PHE A 1 259 ? 0.015  -5.336  30.801  1.00 18.24 ? 260 PHE A CG  1 
ATOM   2069 C  CD1 . PHE A 1 259 ? 1.021  -4.742  30.047  1.00 16.37 ? 260 PHE A CD1 1 
ATOM   2070 C  CD2 . PHE A 1 259 ? 0.219  -6.643  31.225  1.00 21.14 ? 260 PHE A CD2 1 
ATOM   2071 C  CE1 . PHE A 1 259 ? 2.145  -5.461  29.648  1.00 16.86 ? 260 PHE A CE1 1 
ATOM   2072 C  CE2 . PHE A 1 259 ? 1.339  -7.367  30.827  1.00 21.72 ? 260 PHE A CE2 1 
ATOM   2073 C  CZ  . PHE A 1 259 ? 2.304  -6.782  30.035  1.00 16.45 ? 260 PHE A CZ  1 
ATOM   2074 N  N   . LYS A 1 260 ? -1.395 -5.082  34.459  1.00 33.40 ? 261 LYS A N   1 
ATOM   2075 C  CA  . LYS A 1 260 ? -1.481 -6.163  35.440  1.00 48.22 ? 261 LYS A CA  1 
ATOM   2076 C  C   . LYS A 1 260 ? -1.408 -5.645  36.891  1.00 51.49 ? 261 LYS A C   1 
ATOM   2077 O  O   . LYS A 1 260 ? -2.221 -4.758  37.225  1.00 64.76 ? 261 LYS A O   1 
ATOM   2078 C  CB  . LYS A 1 260 ? -0.557 -7.343  35.128  1.00 48.64 ? 261 LYS A CB  1 
ATOM   2079 C  CG  . LYS A 1 260 ? -1.262 -8.564  34.541  1.00 58.38 ? 261 LYS A CG  1 
HETATM 2080 ZN ZN  . ZN  B 2 .   ? 15.108 0.153   14.646  1.00 11.07 ? 301 ZN  A ZN  1 
HETATM 2081 S  S   . DMS C 3 .   ? 23.098 -9.770  14.093  1.00 26.60 ? 302 DMS A S   1 
HETATM 2082 O  O   . DMS C 3 .   ? 23.662 -11.102 13.621  1.00 35.03 ? 302 DMS A O   1 
HETATM 2083 C  C1  . DMS C 3 .   ? 23.424 -9.749  15.823  1.00 23.74 ? 302 DMS A C1  1 
HETATM 2084 C  C2  . DMS C 3 .   ? 24.311 -8.566  13.570  1.00 31.31 ? 302 DMS A C2  1 
HETATM 2085 C  C6  . OQW D 4 .   ? 16.022 6.404   14.882  1.00 23.66 ? 303 OQW A C6  1 
HETATM 2086 C  C4  . OQW D 4 .   ? 15.716 5.294   15.641  1.00 17.02 ? 303 OQW A C4  1 
HETATM 2087 C  C3  . OQW D 4 .   ? 16.211 4.014   15.195  1.00 18.06 ? 303 OQW A C3  1 
HETATM 2088 O  O1  . OQW D 4 .   ? 16.311 2.737   17.510  1.00 20.39 ? 303 OQW A O1  1 
HETATM 2089 C  C8  . OQW D 4 .   ? 16.863 6.318   13.811  1.00 24.40 ? 303 OQW A C8  1 
HETATM 2090 C  C11 . OQW D 4 .   ? 17.110 3.872   14.120  1.00 22.36 ? 303 OQW A C11 1 
HETATM 2091 C  C13 . OQW D 4 .   ? 17.782 2.385   12.132  1.00 18.17 ? 303 OQW A C13 1 
HETATM 2092 C  C14 . OQW D 4 .   ? 17.783 0.884   12.117  1.00 21.81 ? 303 OQW A C14 1 
HETATM 2093 C  C9  . OQW D 4 .   ? 17.417 5.093   13.463  1.00 22.17 ? 303 OQW A C9  1 
HETATM 2094 C  C15 . OQW D 4 .   ? 17.886 0.286   10.782  1.00 19.66 ? 303 OQW A C15 1 
HETATM 2095 C  C16 . OQW D 4 .   ? 18.847 0.731   9.697   1.00 23.59 ? 303 OQW A C16 1 
HETATM 2096 C  C17 . OQW D 4 .   ? 18.514 2.078   9.026   1.00 26.40 ? 303 OQW A C17 1 
HETATM 2097 C  C20 . OQW D 4 .   ? 16.596 3.038   11.404  1.00 22.61 ? 303 OQW A C20 1 
HETATM 2098 C  C19 . OQW D 4 .   ? 16.760 3.580   10.008  1.00 24.93 ? 303 OQW A C19 1 
HETATM 2099 C  C18 . OQW D 4 .   ? 16.992 2.495   8.921   1.00 21.60 ? 303 OQW A C18 1 
HETATM 2100 O  O22 . OQW D 4 .   ? 14.281 2.585   16.062  1.00 20.25 ? 303 OQW A O22 1 
HETATM 2101 S  S2  . OQW D 4 .   ? 15.770 2.606   16.149  1.00 19.34 ? 303 OQW A S2  1 
HETATM 2102 N  N21 . OQW D 4 .   ? 16.516 1.232   15.555  1.00 26.28 ? 303 OQW A N21 1 
HETATM 2103 F  F10 . OQW D 4 .   ? 18.299 5.069   12.398  1.00 23.50 ? 303 OQW A F10 1 
HETATM 2104 F  F7  . OQW D 4 .   ? 15.553 7.588   15.274  1.00 26.69 ? 303 OQW A F7  1 
HETATM 2105 F  F5  . OQW D 4 .   ? 14.858 5.504   16.694  1.00 20.61 ? 303 OQW A F5  1 
HETATM 2106 N  N12 . OQW D 4 .   ? 17.698 2.638   13.588  1.00 16.71 ? 303 OQW A N12 1 
HETATM 2107 O  O   . HOH E 5 .   ? -3.624 -8.988  17.096  1.00 36.16 ? 401 HOH A O   1 
HETATM 2108 O  O   . HOH E 5 .   ? 3.764  20.852  5.649   1.00 15.11 ? 402 HOH A O   1 
HETATM 2109 O  O   . HOH E 5 .   ? -4.727 15.673  6.793   1.00 26.99 ? 403 HOH A O   1 
HETATM 2110 O  O   . HOH E 5 .   ? 7.091  -7.003  -5.676  1.00 19.46 ? 404 HOH A O   1 
HETATM 2111 O  O   . HOH E 5 .   ? 18.447 -2.269  36.989  1.00 46.35 ? 405 HOH A O   1 
HETATM 2112 O  O   . HOH E 5 .   ? 3.269  -19.075 14.267  1.00 32.50 ? 406 HOH A O   1 
HETATM 2113 O  O   . HOH E 5 .   ? -0.414 -16.437 13.260  1.00 27.90 ? 407 HOH A O   1 
HETATM 2114 O  O   . HOH E 5 .   ? 23.667 9.458   27.454  1.00 30.47 ? 408 HOH A O   1 
HETATM 2115 O  O   . HOH E 5 .   ? 1.334  19.751  3.824   1.00 29.63 ? 409 HOH A O   1 
HETATM 2116 O  O   . HOH E 5 .   ? 23.243 -7.174  -5.708  1.00 36.68 ? 410 HOH A O   1 
HETATM 2117 O  O   . HOH E 5 .   ? 20.373 -2.254  14.934  1.00 14.27 ? 411 HOH A O   1 
HETATM 2118 O  O   . HOH E 5 .   ? 4.547  -14.502 21.506  1.00 41.26 ? 412 HOH A O   1 
HETATM 2119 O  O   . HOH E 5 .   ? 32.722 -5.089  21.929  1.00 28.32 ? 413 HOH A O   1 
HETATM 2120 O  O   . HOH E 5 .   ? 5.383  6.895   35.317  1.00 33.54 ? 414 HOH A O   1 
HETATM 2121 O  O   . HOH E 5 .   ? 29.401 -5.457  -0.915  1.00 35.35 ? 415 HOH A O   1 
HETATM 2122 O  O   . HOH E 5 .   ? -0.508 3.347   29.778  1.00 25.13 ? 416 HOH A O   1 
HETATM 2123 O  O   . HOH E 5 .   ? 11.250 -16.336 16.133  1.00 20.99 ? 417 HOH A O   1 
HETATM 2124 O  O   . HOH E 5 .   ? 6.461  -19.631 12.867  1.00 33.01 ? 418 HOH A O   1 
HETATM 2125 O  O   . HOH E 5 .   ? -1.476 -9.533  16.586  1.00 35.21 ? 419 HOH A O   1 
HETATM 2126 O  O   . HOH E 5 .   ? 8.084  16.482  26.687  1.00 25.88 ? 420 HOH A O   1 
HETATM 2127 O  O   . HOH E 5 .   ? 15.175 -18.548 18.550  1.00 18.55 ? 421 HOH A O   1 
HETATM 2128 O  O   . HOH E 5 .   ? 20.337 -10.559 -4.191  1.00 25.21 ? 422 HOH A O   1 
HETATM 2129 O  O   . HOH E 5 .   ? 37.280 5.171   15.279  1.00 32.46 ? 423 HOH A O   1 
HETATM 2130 O  O   . HOH E 5 .   ? 26.296 -0.983  28.365  1.00 33.98 ? 424 HOH A O   1 
HETATM 2131 O  O   . HOH E 5 .   ? 1.933  10.481  30.034  1.00 27.56 ? 425 HOH A O   1 
HETATM 2132 O  O   . HOH E 5 .   ? 7.034  -3.189  -7.058  1.00 29.75 ? 426 HOH A O   1 
HETATM 2133 O  O   . HOH E 5 .   ? 2.014  -10.250 -3.451  1.00 22.82 ? 427 HOH A O   1 
HETATM 2134 O  O   . HOH E 5 .   ? 17.699 -11.086 -3.442  1.00 20.50 ? 428 HOH A O   1 
HETATM 2135 O  O   . HOH E 5 .   ? 1.794  12.709  26.621  1.00 19.57 ? 429 HOH A O   1 
HETATM 2136 O  O   . HOH E 5 .   ? 25.966 -1.879  25.857  1.00 25.06 ? 430 HOH A O   1 
HETATM 2137 O  O   . HOH E 5 .   ? 0.348  -4.603  -2.481  1.00 28.50 ? 431 HOH A O   1 
HETATM 2138 O  O   . HOH E 5 .   ? 21.669 2.472   33.917  1.00 27.78 ? 432 HOH A O   1 
HETATM 2139 O  O   . HOH E 5 .   ? 3.390  15.559  31.351  1.00 25.76 ? 433 HOH A O   1 
HETATM 2140 O  O   . HOH E 5 .   ? 13.778 -13.505 10.545  1.00 13.53 ? 434 HOH A O   1 
HETATM 2141 O  O   . HOH E 5 .   ? 21.558 0.665   -5.793  1.00 20.00 ? 435 HOH A O   1 
HETATM 2142 O  O   . HOH E 5 .   ? 20.517 24.924  17.310  1.00 30.72 ? 436 HOH A O   1 
HETATM 2143 O  O   . HOH E 5 .   ? 16.472 -10.349 31.472  1.00 31.31 ? 437 HOH A O   1 
HETATM 2144 O  O   . HOH E 5 .   ? 16.233 -18.925 6.179   1.00 17.77 ? 438 HOH A O   1 
HETATM 2145 O  O   . HOH E 5 .   ? 23.655 -13.498 8.621   1.00 22.04 ? 439 HOH A O   1 
HETATM 2146 O  O   . HOH E 5 .   ? 5.433  -8.231  36.114  1.00 25.83 ? 440 HOH A O   1 
HETATM 2147 O  O   . HOH E 5 .   ? 21.043 5.079   12.254  1.00 48.52 ? 441 HOH A O   1 
HETATM 2148 O  O   . HOH E 5 .   ? 15.219 -2.926  -7.049  1.00 19.74 ? 442 HOH A O   1 
HETATM 2149 O  O   . HOH E 5 .   ? -2.260 -1.262  28.753  1.00 26.09 ? 443 HOH A O   1 
HETATM 2150 O  O   . HOH E 5 .   ? 3.957  -2.591  40.445  1.00 28.73 ? 444 HOH A O   1 
HETATM 2151 O  O   . HOH E 5 .   ? 2.089  -18.852 4.537   1.00 23.25 ? 445 HOH A O   1 
HETATM 2152 O  O   . HOH E 5 .   ? 19.574 -2.926  -7.831  1.00 25.48 ? 446 HOH A O   1 
HETATM 2153 O  O   . HOH E 5 .   ? 12.821 2.189   -7.252  1.00 28.61 ? 447 HOH A O   1 
HETATM 2154 O  O   . HOH E 5 .   ? 8.498  -20.412 11.218  1.00 38.71 ? 448 HOH A O   1 
HETATM 2155 O  O   . HOH E 5 .   ? -0.172 7.488   4.613   1.00 15.47 ? 449 HOH A O   1 
HETATM 2156 O  O   . HOH E 5 .   ? 17.007 7.088   -3.972  1.00 20.22 ? 450 HOH A O   1 
HETATM 2157 O  O   . HOH E 5 .   ? 10.116 11.860  7.655   1.00 19.91 ? 451 HOH A O   1 
HETATM 2158 O  O   . HOH E 5 .   ? 30.132 -2.019  20.551  1.00 18.71 ? 452 HOH A O   1 
HETATM 2159 O  O   . HOH E 5 .   ? 26.982 8.841   20.335  1.00 23.39 ? 453 HOH A O   1 
HETATM 2160 O  O   . HOH E 5 .   ? 25.265 6.411   29.613  1.00 22.84 ? 454 HOH A O   1 
HETATM 2161 O  O   . HOH E 5 .   ? -2.193 10.594  20.030  1.00 22.65 ? 455 HOH A O   1 
HETATM 2162 O  O   . HOH E 5 .   ? 8.516  12.129  27.512  1.00 20.39 ? 456 HOH A O   1 
HETATM 2163 O  O   . HOH E 5 .   ? 24.659 -2.544  6.897   1.00 28.53 ? 457 HOH A O   1 
HETATM 2164 O  O   . HOH E 5 .   ? 12.575 -13.757 32.024  1.00 26.11 ? 458 HOH A O   1 
HETATM 2165 O  O   . HOH E 5 .   ? 14.814 -13.598 30.483  1.00 24.86 ? 459 HOH A O   1 
HETATM 2166 O  O   . HOH E 5 .   ? 24.432 -10.879 4.860   1.00 19.22 ? 460 HOH A O   1 
HETATM 2167 O  O   . HOH E 5 .   ? 35.016 1.854   24.194  1.00 24.30 ? 461 HOH A O   1 
HETATM 2168 O  O   . HOH E 5 .   ? 29.004 -2.510  -0.488  1.00 34.30 ? 462 HOH A O   1 
HETATM 2169 O  O   . HOH E 5 .   ? 17.187 -11.695 17.257  1.00 13.28 ? 463 HOH A O   1 
HETATM 2170 O  O   . HOH E 5 .   ? 36.889 -0.531  14.192  1.00 20.25 ? 464 HOH A O   1 
HETATM 2171 O  O   . HOH E 5 .   ? -4.101 9.580   6.346   1.00 38.37 ? 465 HOH A O   1 
HETATM 2172 O  O   . HOH E 5 .   ? 5.606  -10.675 23.739  1.00 23.12 ? 466 HOH A O   1 
HETATM 2173 O  O   . HOH E 5 .   ? 4.786  -7.986  32.095  1.00 19.86 ? 467 HOH A O   1 
HETATM 2174 O  O   . HOH E 5 .   ? 7.732  -14.064 -0.730  1.00 30.84 ? 468 HOH A O   1 
HETATM 2175 O  O   . HOH E 5 .   ? 11.757 10.443  25.081  1.00 20.27 ? 469 HOH A O   1 
HETATM 2176 O  O   . HOH E 5 .   ? 18.723 19.360  20.264  1.00 25.84 ? 470 HOH A O   1 
HETATM 2177 O  O   . HOH E 5 .   ? -2.238 0.544   26.454  1.00 28.56 ? 471 HOH A O   1 
HETATM 2178 O  O   . HOH E 5 .   ? 18.292 -9.397  20.081  1.00 14.39 ? 472 HOH A O   1 
HETATM 2179 O  O   . HOH E 5 .   ? 5.896  17.705  23.250  1.00 24.75 ? 473 HOH A O   1 
HETATM 2180 O  O   . HOH E 5 .   ? 17.917 -14.276 23.551  1.00 17.52 ? 474 HOH A O   1 
HETATM 2181 O  O   . HOH E 5 .   ? 3.624  12.523  11.119  1.00 17.50 ? 475 HOH A O   1 
HETATM 2182 O  O   . HOH E 5 .   ? 4.768  -6.526  19.806  1.00 12.98 ? 476 HOH A O   1 
HETATM 2183 O  O   . HOH E 5 .   ? 8.420  -7.140  -3.626  1.00 22.81 ? 477 HOH A O   1 
HETATM 2184 O  O   . HOH E 5 .   ? -3.237 6.423   8.437   1.00 27.84 ? 478 HOH A O   1 
HETATM 2185 O  O   . HOH E 5 .   ? 18.280 -11.652 24.454  1.00 17.76 ? 479 HOH A O   1 
HETATM 2186 O  O   . HOH E 5 .   ? -1.020 2.730   34.487  1.00 28.67 ? 480 HOH A O   1 
HETATM 2187 O  O   . HOH E 5 .   ? -1.306 -3.814  2.471   1.00 20.89 ? 481 HOH A O   1 
HETATM 2188 O  O   . HOH E 5 .   ? -4.115 -4.157  12.479  1.00 30.22 ? 482 HOH A O   1 
HETATM 2189 O  O   . HOH E 5 .   ? 2.466  11.900  8.554   1.00 13.66 ? 483 HOH A O   1 
HETATM 2190 O  O   . HOH E 5 .   ? 19.223 -7.128  28.423  1.00 15.77 ? 484 HOH A O   1 
HETATM 2191 O  O   . HOH E 5 .   ? 26.583 -3.152  20.449  1.00 17.71 ? 485 HOH A O   1 
HETATM 2192 O  O   . HOH E 5 .   ? 4.568  21.140  20.668  1.00 46.71 ? 486 HOH A O   1 
HETATM 2193 O  O   . HOH E 5 .   ? 33.259 1.656   15.559  1.00 25.90 ? 487 HOH A O   1 
HETATM 2194 O  O   . HOH E 5 .   ? 17.526 -7.138  30.606  1.00 22.80 ? 488 HOH A O   1 
HETATM 2195 O  O   . HOH E 5 .   ? 9.191  9.633   28.142  1.00 23.18 ? 489 HOH A O   1 
HETATM 2196 O  O   . HOH E 5 .   ? -2.533 2.741   27.931  1.00 26.00 ? 490 HOH A O   1 
HETATM 2197 O  O   . HOH E 5 .   ? 3.659  22.328  7.571   1.00 14.55 ? 491 HOH A O   1 
HETATM 2198 O  O   . HOH E 5 .   ? 16.815 -14.266 0.403   1.00 28.03 ? 492 HOH A O   1 
HETATM 2199 O  O   . HOH E 5 .   ? 0.209  -5.284  22.971  1.00 15.99 ? 493 HOH A O   1 
HETATM 2200 O  O   . HOH E 5 .   ? -3.275 -5.681  8.838   1.00 18.39 ? 494 HOH A O   1 
HETATM 2201 O  O   . HOH E 5 .   ? -1.671 -0.992  6.253   1.00 19.50 ? 495 HOH A O   1 
HETATM 2202 O  O   . HOH E 5 .   ? -1.857 -11.364 11.153  1.00 25.94 ? 496 HOH A O   1 
HETATM 2203 O  O   . HOH E 5 .   ? 8.024  1.092   -6.358  1.00 30.68 ? 497 HOH A O   1 
HETATM 2204 O  O   . HOH E 5 .   ? 31.960 -9.108  15.602  1.00 25.16 ? 498 HOH A O   1 
HETATM 2205 O  O   . HOH E 5 .   ? 16.031 -11.903 33.563  1.00 34.78 ? 499 HOH A O   1 
HETATM 2206 O  O   . HOH E 5 .   ? 21.194 -6.906  31.891  1.00 27.17 ? 500 HOH A O   1 
HETATM 2207 O  O   . HOH E 5 .   ? 10.264 -17.124 6.388   1.00 37.39 ? 501 HOH A O   1 
HETATM 2208 O  O   . HOH E 5 .   ? 14.412 -6.665  -7.851  1.00 27.85 ? 502 HOH A O   1 
HETATM 2209 O  O   . HOH E 5 .   ? 8.495  -14.941 25.680  1.00 30.01 ? 503 HOH A O   1 
HETATM 2210 O  O   . HOH E 5 .   ? 26.154 -4.995  7.265   1.00 27.33 ? 504 HOH A O   1 
HETATM 2211 O  O   . HOH E 5 .   ? 23.146 -10.178 24.065  1.00 30.41 ? 505 HOH A O   1 
HETATM 2212 O  O   . HOH E 5 .   ? 15.433 -17.863 23.087  1.00 27.21 ? 506 HOH A O   1 
HETATM 2213 O  O   . HOH E 5 .   ? -3.350 13.741  6.197   1.00 21.54 ? 507 HOH A O   1 
HETATM 2214 O  O   . HOH E 5 .   ? 2.528  -2.034  -2.945  1.00 25.74 ? 508 HOH A O   1 
HETATM 2215 O  O   . HOH E 5 .   ? 27.830 -1.128  6.033   1.00 41.93 ? 509 HOH A O   1 
HETATM 2216 O  O   . HOH E 5 .   ? 13.120 7.383   28.483  1.00 28.77 ? 510 HOH A O   1 
HETATM 2217 O  O   . HOH E 5 .   ? -4.047 -4.263  33.781  1.00 34.37 ? 511 HOH A O   1 
HETATM 2218 O  O   . HOH E 5 .   ? 2.145  17.066  16.387  1.00 26.24 ? 512 HOH A O   1 
HETATM 2219 O  O   . HOH E 5 .   ? 32.092 -7.104  8.458   1.00 32.07 ? 513 HOH A O   1 
HETATM 2220 O  O   . HOH E 5 .   ? 5.769  10.958  -2.449  1.00 28.51 ? 514 HOH A O   1 
HETATM 2221 O  O   . HOH E 5 .   ? 32.968 2.920   25.742  1.00 23.79 ? 515 HOH A O   1 
HETATM 2222 O  O   . HOH E 5 .   ? -5.106 -2.324  24.775  1.00 23.91 ? 516 HOH A O   1 
HETATM 2223 O  O   . HOH E 5 .   ? -3.325 11.620  12.872  1.00 28.50 ? 517 HOH A O   1 
HETATM 2224 O  O   . HOH E 5 .   ? 14.150 -14.813 0.566   1.00 37.19 ? 518 HOH A O   1 
HETATM 2225 O  O   . HOH E 5 .   ? 14.362 -7.266  32.065  1.00 25.72 ? 519 HOH A O   1 
HETATM 2226 O  O   . HOH E 5 .   ? 4.586  5.517   40.052  1.00 41.66 ? 520 HOH A O   1 
HETATM 2227 O  O   . HOH E 5 .   ? 13.806 -17.488 20.735  1.00 19.08 ? 521 HOH A O   1 
HETATM 2228 O  O   . HOH E 5 .   ? 28.315 0.489   -8.705  1.00 30.61 ? 522 HOH A O   1 
HETATM 2229 O  O   . HOH E 5 .   ? 21.180 -18.161 8.019   1.00 25.91 ? 523 HOH A O   1 
HETATM 2230 O  O   . HOH E 5 .   ? 18.543 -16.279 4.616   1.00 19.58 ? 524 HOH A O   1 
HETATM 2231 O  O   . HOH E 5 .   ? 2.828  5.756   -3.868  1.00 29.51 ? 525 HOH A O   1 
HETATM 2232 O  O   . HOH E 5 .   ? 23.606 9.888   24.200  1.00 29.00 ? 526 HOH A O   1 
HETATM 2233 O  O   . HOH E 5 .   ? 21.636 -12.734 21.101  1.00 33.53 ? 527 HOH A O   1 
HETATM 2234 O  O   . HOH E 5 .   ? 8.170  6.057   32.687  1.00 33.00 ? 528 HOH A O   1 
HETATM 2235 O  O   . HOH E 5 .   ? -2.992 -15.577 6.623   1.00 42.94 ? 529 HOH A O   1 
HETATM 2236 O  O   . HOH E 5 .   ? -4.973 5.236   20.834  1.00 29.85 ? 530 HOH A O   1 
HETATM 2237 O  O   . HOH E 5 .   ? 10.842 2.683   32.835  1.00 25.58 ? 531 HOH A O   1 
HETATM 2238 O  O   . HOH E 5 .   ? 13.432 16.515  29.951  1.00 38.29 ? 532 HOH A O   1 
HETATM 2239 O  O   . HOH E 5 .   ? 2.017  15.535  29.014  1.00 24.45 ? 533 HOH A O   1 
HETATM 2240 O  O   . HOH E 5 .   ? 29.697 -7.407  15.719  1.00 24.59 ? 534 HOH A O   1 
HETATM 2241 O  O   . HOH E 5 .   ? 12.820 -4.164  35.351  1.00 24.08 ? 535 HOH A O   1 
HETATM 2242 O  O   . HOH E 5 .   ? -2.091 0.952   3.678   1.00 23.77 ? 536 HOH A O   1 
HETATM 2243 O  O   . HOH E 5 .   ? 11.101 -17.582 26.015  1.00 32.50 ? 537 HOH A O   1 
HETATM 2244 O  O   . HOH E 5 .   ? 34.746 -4.308  24.170  1.00 40.62 ? 538 HOH A O   1 
HETATM 2245 O  O   . HOH E 5 .   ? 23.141 -0.051  28.909  1.00 18.44 ? 539 HOH A O   1 
HETATM 2246 O  O   . HOH E 5 .   ? -1.277 1.968   31.926  1.00 24.56 ? 540 HOH A O   1 
HETATM 2247 O  O   . HOH E 5 .   ? 31.867 -0.567  13.080  1.00 31.03 ? 541 HOH A O   1 
HETATM 2248 O  O   . HOH E 5 .   ? 24.892 -12.646 1.175   1.00 19.63 ? 542 HOH A O   1 
HETATM 2249 O  O   . HOH E 5 .   ? -6.469 7.886   18.594  1.00 41.10 ? 543 HOH A O   1 
HETATM 2250 O  O   . HOH E 5 .   ? 8.369  -16.495 14.353  1.00 29.40 ? 544 HOH A O   1 
HETATM 2251 O  O   . HOH E 5 .   ? 35.489 3.928   22.759  1.00 33.84 ? 545 HOH A O   1 
HETATM 2252 O  O   . HOH E 5 .   ? 12.055 -8.071  -1.990  1.00 29.98 ? 546 HOH A O   1 
HETATM 2253 O  O   . HOH E 5 .   ? 7.920  16.410  5.674   1.00 45.59 ? 547 HOH A O   1 
HETATM 2254 O  O   . HOH E 5 .   ? -3.454 -7.198  1.808   1.00 27.22 ? 548 HOH A O   1 
HETATM 2255 O  O   . HOH E 5 .   ? 12.463 -6.287  33.727  1.00 33.69 ? 549 HOH A O   1 
HETATM 2256 O  O   . HOH E 5 .   ? 30.661 -6.044  -7.863  1.00 24.03 ? 550 HOH A O   1 
HETATM 2257 O  O   . HOH E 5 .   ? 19.670 -10.628 22.037  1.00 15.48 ? 551 HOH A O   1 
HETATM 2258 O  O   . HOH E 5 .   ? 8.186  -16.671 30.381  1.00 32.35 ? 552 HOH A O   1 
HETATM 2259 O  O   . HOH E 5 .   ? 23.336 -15.790 12.743  1.00 38.08 ? 553 HOH A O   1 
HETATM 2260 O  O   . HOH E 5 .   ? 23.658 12.786  16.850  1.00 44.46 ? 554 HOH A O   1 
HETATM 2261 O  O   . HOH E 5 .   ? -1.372 -9.731  13.753  1.00 23.17 ? 555 HOH A O   1 
HETATM 2262 O  O   . HOH E 5 .   ? 14.636 -17.742 4.310   1.00 25.88 ? 556 HOH A O   1 
HETATM 2263 O  O   . HOH E 5 .   ? -0.176 6.799   40.522  1.00 42.20 ? 557 HOH A O   1 
HETATM 2264 O  O   . HOH E 5 .   ? 2.920  -7.033  33.968  1.00 21.51 ? 558 HOH A O   1 
HETATM 2265 O  O   . HOH E 5 .   ? 19.573 6.837   6.212   1.00 33.12 ? 559 HOH A O   1 
HETATM 2266 O  O   . HOH E 5 .   ? 18.300 5.478   -0.216  1.00 25.10 ? 560 HOH A O   1 
HETATM 2267 O  O   . HOH E 5 .   ? 9.893  4.521   30.622  1.00 26.40 ? 561 HOH A O   1 
HETATM 2268 O  O   . HOH E 5 .   ? 14.271 8.455   -0.737  1.00 22.18 ? 562 HOH A O   1 
HETATM 2269 O  O   . HOH E 5 .   ? 29.245 7.976   21.573  1.00 21.13 ? 563 HOH A O   1 
HETATM 2270 O  O   . HOH E 5 .   ? 34.582 -1.635  12.730  1.00 27.50 ? 564 HOH A O   1 
HETATM 2271 O  O   . HOH E 5 .   ? 18.451 4.691   -7.117  1.00 23.66 ? 565 HOH A O   1 
HETATM 2272 O  O   . HOH E 5 .   ? 24.347 -9.396  9.326   1.00 30.62 ? 566 HOH A O   1 
HETATM 2273 O  O   . HOH E 5 .   ? 14.728 3.301   34.595  1.00 27.28 ? 567 HOH A O   1 
HETATM 2274 O  O   . HOH E 5 .   ? 15.705 4.507   -6.946  1.00 22.78 ? 568 HOH A O   1 
HETATM 2275 O  O   . HOH E 5 .   ? 25.797 10.162  22.475  1.00 32.99 ? 569 HOH A O   1 
HETATM 2276 O  O   . HOH E 5 .   ? 29.703 5.281   27.616  1.00 35.24 ? 570 HOH A O   1 
HETATM 2277 O  O   . HOH E 5 .   ? 4.099  19.553  3.738   1.00 29.06 ? 571 HOH A O   1 
HETATM 2278 O  O   . HOH E 5 .   ? 23.117 0.566   37.994  1.00 49.05 ? 572 HOH A O   1 
HETATM 2279 O  O   . HOH E 5 .   ? 30.118 -4.474  -11.255 1.00 20.06 ? 573 HOH A O   1 
HETATM 2280 O  O   . HOH E 5 .   ? 26.524 -7.770  7.388   1.00 37.20 ? 574 HOH A O   1 
HETATM 2281 O  O   . HOH E 5 .   ? 4.773  8.644   40.457  1.00 27.62 ? 575 HOH A O   1 
HETATM 2282 O  O   . HOH E 5 .   ? 27.946 -8.815  14.104  1.00 40.03 ? 576 HOH A O   1 
HETATM 2283 O  O   . HOH E 5 .   ? -3.664 13.044  19.343  1.00 33.44 ? 577 HOH A O   1 
HETATM 2284 O  O   . HOH E 5 .   ? -0.407 -10.697 -1.740  1.00 13.67 ? 578 HOH A O   1 
HETATM 2285 O  O   . HOH E 5 .   ? 4.228  21.497  17.034  1.00 38.06 ? 579 HOH A O   1 
HETATM 2286 O  O   . HOH E 5 .   ? 14.112 -7.135  -3.191  1.00 29.06 ? 580 HOH A O   1 
HETATM 2287 O  O   . HOH E 5 .   ? 30.150 -3.073  23.093  1.00 31.51 ? 581 HOH A O   1 
HETATM 2288 O  O   . HOH E 5 .   ? 0.047  -19.346 12.235  1.00 39.32 ? 582 HOH A O   1 
HETATM 2289 O  O   . HOH E 5 .   ? 37.510 -13.214 8.071   1.00 40.58 ? 583 HOH A O   1 
HETATM 2290 O  O   . HOH E 5 .   ? 20.872 4.656   9.857   1.00 37.19 ? 584 HOH A O   1 
HETATM 2291 O  O   . HOH E 5 .   ? 4.713  18.577  27.873  1.00 50.40 ? 585 HOH A O   1 
HETATM 2292 O  O   . HOH E 5 .   ? -5.048 11.862  4.923   1.00 30.77 ? 586 HOH A O   1 
HETATM 2293 O  O   . HOH E 5 .   ? 0.296  23.090  6.265   1.00 28.15 ? 587 HOH A O   1 
HETATM 2294 O  O   . HOH E 5 .   ? 18.798 6.363   9.219   1.00 40.86 ? 588 HOH A O   1 
HETATM 2295 O  O   . HOH E 5 .   ? -4.382 -0.865  30.368  1.00 38.73 ? 589 HOH A O   1 
HETATM 2296 O  O   . HOH E 5 .   ? -5.482 -4.641  7.552   1.00 39.71 ? 590 HOH A O   1 
HETATM 2297 O  O   . HOH E 5 .   ? -5.758 -9.410  14.568  1.00 46.19 ? 591 HOH A O   1 
HETATM 2298 O  O   . HOH E 5 .   ? 12.233 4.039   34.977  1.00 30.51 ? 592 HOH A O   1 
HETATM 2299 O  O   . HOH E 5 .   ? 16.999 -4.337  -8.564  1.00 31.03 ? 593 HOH A O   1 
HETATM 2300 O  O   . HOH E 5 .   ? 25.678 -10.277 22.438  1.00 40.93 ? 594 HOH A O   1 
HETATM 2301 O  O   . HOH E 5 .   ? 3.501  -10.183 30.887  1.00 26.25 ? 595 HOH A O   1 
HETATM 2302 O  O   . HOH E 5 .   ? -0.111 14.142  27.489  1.00 46.73 ? 596 HOH A O   1 
HETATM 2303 O  O   . HOH E 5 .   ? 16.919 10.544  13.863  1.00 36.49 ? 597 HOH A O   1 
HETATM 2304 O  O   . HOH E 5 .   ? 11.661 6.798   30.999  1.00 32.18 ? 598 HOH A O   1 
HETATM 2305 O  O   . HOH E 5 .   ? 4.726  -12.274 25.752  1.00 37.79 ? 599 HOH A O   1 
HETATM 2306 O  O   . HOH E 5 .   ? 17.467 -13.748 -2.289  1.00 31.42 ? 600 HOH A O   1 
HETATM 2307 O  O   . HOH E 5 .   ? 20.665 -9.568  28.190  1.00 26.01 ? 601 HOH A O   1 
HETATM 2308 O  O   . HOH E 5 .   ? 16.868 -16.109 2.540   1.00 33.26 ? 602 HOH A O   1 
HETATM 2309 O  O   . HOH E 5 .   ? -5.827 2.069   14.542  1.00 26.81 ? 603 HOH A O   1 
HETATM 2310 O  O   . HOH E 5 .   ? 1.598  15.221  33.550  1.00 23.82 ? 604 HOH A O   1 
HETATM 2311 O  O   . HOH E 5 .   ? 18.174 -9.089  32.332  1.00 24.93 ? 605 HOH A O   1 
HETATM 2312 O  O   . HOH E 5 .   ? 11.131 2.669   37.508  1.00 34.25 ? 606 HOH A O   1 
HETATM 2313 O  O   . HOH E 5 .   ? 16.428 -8.146  33.833  1.00 46.56 ? 607 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 4   ? 0.8973 0.4714 0.8941 0.0353  0.4833  0.0063  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.5287 0.3424 0.6138 0.1181  0.2943  0.2131  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.3902 0.4439 0.3837 0.0427  0.1483  0.1580  4   HIS A C   
4    O  O   . HIS A 4   ? 0.3091 0.4276 0.3919 -0.0204 0.0381  0.1184  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.5050 0.3449 0.5035 0.1407  0.3137  0.1663  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.3938 0.3983 0.3093 0.1544  0.2249  0.1521  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.5329 0.6704 0.6003 0.0502  0.0600  -0.0251 4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.7174 0.5804 0.7663 0.3737  0.2056  0.1846  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.4972 0.7251 0.8376 0.3987  0.0633  0.1351  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.7736 0.6616 0.8251 0.2284  -0.0849 0.2620  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.3103 0.4731 0.4096 -0.0029 0.1178  0.0979  5   TRP A N   
12   C  CA  . TRP A 5   ? 0.2074 0.3630 0.2695 -0.0116 -0.0289 0.0483  5   TRP A CA  
13   C  C   . TRP A 5   ? 0.1364 0.4084 0.1773 -0.0050 -0.0445 0.0932  5   TRP A C   
14   O  O   . TRP A 5   ? 0.1707 0.5333 0.2095 0.0299  -0.0398 0.1577  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.1806 0.3208 0.2594 0.0035  -0.0520 0.0589  5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.1878 0.3243 0.1296 -0.0111 -0.0573 0.0834  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2786 0.3422 0.3326 -0.0064 -0.0055 0.1411  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.1769 0.3850 0.1126 -0.0175 -0.0607 0.0581  5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2685 0.4427 0.2035 -0.0500 -0.0558 0.0863  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.2480 0.3907 0.0770 -0.0131 -0.0207 0.0291  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1348 0.3692 0.1136 -0.0396 -0.0429 0.0365  5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.2276 0.4467 0.1820 0.0203  -0.0201 0.0330  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1256 0.4075 0.1518 0.0190  -0.0445 -0.0307 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.2206 0.4239 0.0849 0.0390  -0.0127 0.0137  5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.1612 0.3394 0.1518 -0.0057 -0.0201 0.0017  6   GLY A N   
26   C  CA  . GLY A 6   ? 0.2194 0.3437 0.1163 -0.0408 0.0020  -0.0251 6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1648 0.3629 0.0876 -0.0062 0.0052  -0.0140 6   GLY A C   
28   O  O   . GLY A 6   ? 0.2006 0.3804 0.0962 -0.0006 0.0008  -0.0675 6   GLY A O   
29   N  N   . TYR A 7   ? 0.1908 0.4139 0.1389 -0.0377 -0.0064 -0.0499 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1553 0.4093 0.2020 -0.0671 -0.0324 -0.0510 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.1873 0.4311 0.3055 -0.0701 -0.0974 -0.0569 7   TYR A C   
32   O  O   . TYR A 7   ? 0.2546 0.3774 0.5850 -0.0681 0.0333  -0.0857 7   TYR A O   
33   C  CB  . TYR A 7   ? 0.1518 0.4295 0.1917 -0.0167 -0.0574 -0.0903 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1896 0.3733 0.1023 -0.0398 -0.0109 -0.0586 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1610 0.3075 0.0855 -0.0330 -0.0341 -0.0507 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.1966 0.3327 0.1827 -0.0615 -0.0462 -0.0260 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1989 0.2333 0.1791 -0.0272 -0.0604 -0.0103 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.2118 0.3102 0.0907 -0.0879 -0.0184 -0.0185 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.2390 0.2727 0.0925 -0.0186 -0.0084 0.0161  7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.2940 0.2592 0.1632 -0.0059 -0.0715 -0.0238 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.2212 0.4953 0.2157 -0.0152 -0.0536 -0.1184 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.2465 0.4582 0.2848 -0.0362 -0.0422 -0.0531 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.1844 0.3712 0.3427 0.0068  -0.0267 -0.0723 8   GLY A C   
44   O  O   . GLY A 8   ? 0.2631 0.3255 0.2576 0.0012  0.0162  -0.0208 8   GLY A O   
45   N  N   . LYS A 9   ? 0.2100 0.3276 0.3280 0.0127  0.0286  -0.0405 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.2147 0.3526 0.2934 -0.0193 -0.0035 -0.0417 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.2727 0.2886 0.2311 -0.0067 -0.0150 -0.0316 9   LYS A C   
48   O  O   . LYS A 9   ? 0.2409 0.4166 0.1604 -0.0395 0.0460  -0.0392 9   LYS A O   
49   C  CB  . LYS A 9   ? 0.2568 0.4058 0.4483 0.0138  0.0304  -0.0944 9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.3092 0.3295 0.4355 -0.0542 0.0023  -0.0281 9   LYS A CG  
51   C  CD  . LYS A 9   ? 0.4763 0.4097 0.5567 0.0026  0.0697  -0.2052 9   LYS A CD  
52   C  CE  . LYS A 9   ? 0.6696 0.4155 0.4678 0.0137  0.2736  -0.0922 9   LYS A CE  
53   N  N   . HIS A 10  ? 0.2249 0.3521 0.2585 -0.0241 0.0432  -0.0118 10  HIS A N   
54   C  CA  . HIS A 10  ? 0.2514 0.3292 0.2443 -0.0376 0.0921  -0.0253 10  HIS A CA  
55   C  C   . HIS A 10  ? 0.1877 0.3575 0.1819 -0.0172 0.0695  -0.0409 10  HIS A C   
56   O  O   . HIS A 10  ? 0.2221 0.3452 0.2921 -0.0146 -0.0133 0.0077  10  HIS A O   
57   C  CB  . HIS A 10  ? 0.2782 0.3847 0.3349 0.0748  0.1461  0.0434  10  HIS A CB  
58   C  CG  . HIS A 10  ? 0.3416 0.3473 0.2487 0.0560  0.1427  0.0553  10  HIS A CG  
59   N  ND1 . HIS A 10  ? 0.3934 0.3732 0.2418 0.0557  0.1165  0.0854  10  HIS A ND1 
60   C  CD2 . HIS A 10  ? 0.2818 0.4081 0.3459 -0.0004 0.0203  0.0571  10  HIS A CD2 
61   C  CE1 . HIS A 10  ? 0.4101 0.3738 0.2645 0.1101  0.0477  0.0960  10  HIS A CE1 
62   N  NE2 . HIS A 10  ? 0.3441 0.4923 0.5013 0.0611  0.0109  0.0391  10  HIS A NE2 
63   N  N   . ASN A 11  ? 0.1812 0.3434 0.2449 -0.0249 0.0586  -0.0419 11  ASN A N   
64   C  CA  . ASN A 11  ? 0.1934 0.3325 0.2014 -0.0187 0.0297  -0.0054 11  ASN A CA  
65   C  C   . ASN A 11  ? 0.1964 0.2764 0.1345 -0.0398 0.0111  -0.0343 11  ASN A C   
66   O  O   . ASN A 11  ? 0.1698 0.3258 0.1356 -0.0142 0.0034  -0.0353 11  ASN A O   
67   C  CB  . ASN A 11  ? 0.2117 0.3908 0.2192 0.0160  0.0002  0.0277  11  ASN A CB  
68   C  CG  . ASN A 11  ? 0.2687 0.4841 0.1142 -0.0038 0.0040  0.0052  11  ASN A CG  
69   O  OD1 . ASN A 11  ? 0.2682 0.4644 0.1048 0.0290  -0.0141 0.0026  11  ASN A OD1 
70   N  ND2 . ASN A 11  ? 0.3046 0.4575 0.1201 0.0142  0.0093  0.0166  11  ASN A ND2 
71   N  N   . GLY A 12  ? 0.1619 0.3047 0.1482 -0.0294 -0.0210 0.0161  12  GLY A N   
72   C  CA  . GLY A 12  ? 0.2228 0.3093 0.1489 -0.0405 0.0319  -0.0067 12  GLY A CA  
73   C  C   . GLY A 12  ? 0.1238 0.2730 0.1571 -0.0413 -0.0091 -0.0075 12  GLY A C   
74   O  O   . GLY A 12  ? 0.1428 0.2890 0.1856 -0.0381 -0.0281 -0.0030 12  GLY A O   
75   N  N   . PRO A 13  ? 0.1429 0.2468 0.1368 -0.0465 -0.0104 -0.0111 13  PRO A N   
76   C  CA  . PRO A 13  ? 0.1669 0.2861 0.1059 -0.0195 -0.0269 -0.0082 13  PRO A CA  
77   C  C   . PRO A 13  ? 0.1470 0.2395 0.1892 -0.0312 -0.0425 0.0242  13  PRO A C   
78   O  O   . PRO A 13  ? 0.1912 0.2764 0.1445 -0.0074 -0.0181 -0.0133 13  PRO A O   
79   C  CB  . PRO A 13  ? 0.2073 0.2801 0.1093 -0.0357 -0.0328 -0.0389 13  PRO A CB  
80   C  CG  . PRO A 13  ? 0.1720 0.2916 0.1062 0.0019  -0.0403 -0.0125 13  PRO A CG  
81   C  CD  . PRO A 13  ? 0.1231 0.2777 0.1773 -0.0502 -0.0297 -0.0108 13  PRO A CD  
82   N  N   . GLU A 14  ? 0.1694 0.2596 0.1777 -0.0052 -0.0674 0.0205  14  GLU A N   
83   C  CA  . GLU A 14  ? 0.1424 0.2830 0.1673 -0.0137 -0.0557 0.0201  14  GLU A CA  
84   C  C   . GLU A 14  ? 0.1482 0.2694 0.1673 -0.0244 -0.0374 -0.0108 14  GLU A C   
85   O  O   . GLU A 14  ? 0.1687 0.3429 0.2438 -0.0150 -0.0976 0.0181  14  GLU A O   
86   C  CB  . GLU A 14  ? 0.2832 0.2573 0.3158 0.0000  -0.1241 0.0233  14  GLU A CB  
87   C  CG  . GLU A 14  ? 0.4611 0.2664 0.4328 -0.0161 -0.0163 0.1039  14  GLU A CG  
88   C  CD  . GLU A 14  ? 0.7570 0.6240 0.2805 -0.0094 -0.1039 -0.0170 14  GLU A CD  
89   O  OE1 . GLU A 14  ? 0.6130 0.4577 0.3953 -0.0017 -0.1477 -0.0319 14  GLU A OE1 
90   O  OE2 . GLU A 14  ? 0.7764 0.5721 0.6754 0.0722  -0.0863 0.1392  14  GLU A OE2 
91   N  N   . HIS A 15  ? 0.2145 0.2269 0.1831 -0.0073 -0.0099 -0.0116 15  HIS A N   
92   C  CA  . HIS A 15  ? 0.1605 0.2732 0.0861 -0.0001 -0.0107 -0.0215 15  HIS A CA  
93   C  C   . HIS A 15  ? 0.1529 0.2582 0.1061 -0.0013 -0.0176 0.0104  15  HIS A C   
94   O  O   . HIS A 15  ? 0.1335 0.2777 0.1134 -0.0179 -0.0228 -0.0308 15  HIS A O   
95   C  CB  . HIS A 15  ? 0.2301 0.2503 0.0894 -0.0073 0.0058  -0.0289 15  HIS A CB  
96   C  CG  . HIS A 15  ? 0.1630 0.2744 0.1262 0.0154  -0.0328 -0.0193 15  HIS A CG  
97   N  ND1 . HIS A 15  ? 0.1709 0.3091 0.0860 0.0220  -0.0432 0.0032  15  HIS A ND1 
98   C  CD2 . HIS A 15  ? 0.2617 0.2665 0.1881 0.0068  -0.0079 -0.0425 15  HIS A CD2 
99   C  CE1 . HIS A 15  ? 0.2286 0.3327 0.1005 0.0441  -0.0658 -0.0236 15  HIS A CE1 
100  N  NE2 . HIS A 15  ? 0.2501 0.3420 0.1472 0.0168  -0.0397 -0.0518 15  HIS A NE2 
101  N  N   . TRP A 16  ? 0.1375 0.2526 0.1562 -0.0049 -0.0266 -0.0321 16  TRP A N   
102  C  CA  . TRP A 16  ? 0.1296 0.2646 0.1366 -0.0167 -0.0461 -0.0222 16  TRP A CA  
103  C  C   . TRP A 16  ? 0.1203 0.2102 0.1571 -0.0095 -0.0340 -0.0157 16  TRP A C   
104  O  O   . TRP A 16  ? 0.1504 0.2624 0.1086 -0.0242 -0.0217 0.0062  16  TRP A O   
105  C  CB  . TRP A 16  ? 0.1165 0.2689 0.1398 -0.0138 -0.0690 0.0245  16  TRP A CB  
106  C  CG  . TRP A 16  ? 0.1429 0.2666 0.1045 0.0033  -0.0122 -0.0011 16  TRP A CG  
107  C  CD1 . TRP A 16  ? 0.1270 0.2663 0.0752 -0.0234 -0.0367 0.0013  16  TRP A CD1 
108  C  CD2 . TRP A 16  ? 0.1364 0.2778 0.1058 0.0001  -0.0157 0.0026  16  TRP A CD2 
109  N  NE1 . TRP A 16  ? 0.1277 0.3254 0.1147 -0.0172 -0.0666 -0.0046 16  TRP A NE1 
110  C  CE2 . TRP A 16  ? 0.1370 0.2821 0.1009 -0.0081 -0.0490 0.0049  16  TRP A CE2 
111  C  CE3 . TRP A 16  ? 0.1312 0.2176 0.1244 -0.0286 0.0026  0.0411  16  TRP A CE3 
112  C  CZ2 . TRP A 16  ? 0.1567 0.2633 0.1449 -0.0444 -0.0336 0.0289  16  TRP A CZ2 
113  C  CZ3 . TRP A 16  ? 0.1472 0.2517 0.1004 -0.0295 -0.0228 0.0145  16  TRP A CZ3 
114  C  CH2 . TRP A 16  ? 0.1538 0.2748 0.0901 -0.0183 -0.0550 0.0323  16  TRP A CH2 
115  N  N   . HIS A 17  ? 0.1363 0.2548 0.1506 -0.0051 -0.0341 -0.0220 17  HIS A N   
116  C  CA  . HIS A 17  ? 0.1465 0.2594 0.1195 -0.0163 -0.0029 -0.0135 17  HIS A CA  
117  C  C   . HIS A 17  ? 0.1367 0.2588 0.1597 -0.0089 0.0005  -0.0232 17  HIS A C   
118  O  O   . HIS A 17  ? 0.1779 0.2731 0.1252 -0.0110 -0.0265 -0.0317 17  HIS A O   
119  C  CB  . HIS A 17  ? 0.1586 0.2603 0.1975 -0.0015 -0.0573 0.0363  17  HIS A CB  
120  C  CG  . HIS A 17  ? 0.1403 0.3079 0.0840 -0.0122 -0.0568 0.0167  17  HIS A CG  
121  N  ND1 . HIS A 17  ? 0.1403 0.3764 0.1617 -0.0285 -0.0606 -0.0190 17  HIS A ND1 
122  C  CD2 . HIS A 17  ? 0.1662 0.3120 0.1115 0.0130  0.0330  0.0155  17  HIS A CD2 
123  C  CE1 . HIS A 17  ? 0.2488 0.3597 0.1460 0.0168  0.0059  0.0197  17  HIS A CE1 
124  N  NE2 . HIS A 17  ? 0.2043 0.3511 0.1097 0.0422  0.0142  0.0179  17  HIS A NE2 
125  N  N   . LYS A 18  ? 0.1050 0.3223 0.1120 0.0107  -0.0252 -0.0017 18  LYS A N   
126  C  CA  . LYS A 18  ? 0.1260 0.3019 0.1195 -0.0154 -0.0545 -0.0276 18  LYS A CA  
127  C  C   . LYS A 18  ? 0.1734 0.3127 0.1140 -0.0120 -0.0232 -0.0353 18  LYS A C   
128  O  O   . LYS A 18  ? 0.2052 0.3492 0.2646 -0.0664 -0.0326 -0.0003 18  LYS A O   
129  C  CB  . LYS A 18  ? 0.1399 0.3134 0.1076 0.0054  -0.0268 -0.0026 18  LYS A CB  
130  C  CG  . LYS A 18  ? 0.1359 0.3300 0.1344 0.0198  -0.0067 0.0047  18  LYS A CG  
131  C  CD  . LYS A 18  ? 0.1817 0.3051 0.1906 0.0313  -0.0407 -0.0447 18  LYS A CD  
132  C  CE  . LYS A 18  ? 0.2063 0.3988 0.0892 -0.0272 -0.0272 -0.0451 18  LYS A CE  
133  N  NZ  . LYS A 18  ? 0.1669 0.3480 0.0890 -0.0044 -0.0554 -0.0126 18  LYS A NZ  
134  N  N   . ASP A 19  ? 0.2400 0.3198 0.0660 -0.0240 -0.0561 0.0148  19  ASP A N   
135  C  CA  . ASP A 19  ? 0.2172 0.3199 0.0725 -0.0369 -0.0425 0.0321  19  ASP A CA  
136  C  C   . ASP A 19  ? 0.1453 0.2595 0.1791 -0.0486 -0.0615 0.0015  19  ASP A C   
137  O  O   . ASP A 19  ? 0.2100 0.2670 0.1885 -0.0482 -0.0266 0.0262  19  ASP A O   
138  C  CB  . ASP A 19  ? 0.3319 0.3537 0.0930 -0.0231 -0.0895 -0.0037 19  ASP A CB  
139  C  CG  . ASP A 19  ? 0.4156 0.5048 0.2969 0.0233  0.0770  -0.0814 19  ASP A CG  
140  O  OD1 . ASP A 19  ? 0.4913 0.4892 0.2042 -0.0031 -0.0232 -0.0277 19  ASP A OD1 
141  O  OD2 . ASP A 19  ? 0.4299 0.7796 0.2991 0.0741  0.0308  -0.0632 19  ASP A OD2 
142  N  N   . PHE A 20  ? 0.1345 0.2922 0.1131 -0.0383 -0.0557 -0.0094 20  PHE A N   
143  C  CA  . PHE A 20  ? 0.1216 0.2547 0.2093 -0.0091 -0.0275 0.0152  20  PHE A CA  
144  C  C   . PHE A 20  ? 0.2226 0.2479 0.1683 -0.0337 -0.0186 -0.0379 20  PHE A C   
145  O  O   . PHE A 20  ? 0.2063 0.2642 0.1115 -0.0170 -0.0445 -0.0272 20  PHE A O   
146  C  CB  . PHE A 20  ? 0.1586 0.2829 0.1817 -0.0364 -0.0572 0.0088  20  PHE A CB  
147  C  CG  . PHE A 20  ? 0.1371 0.3633 0.2376 0.0030  -0.0422 0.1011  20  PHE A CG  
148  C  CD1 . PHE A 20  ? 0.1330 0.4151 0.3286 -0.0008 -0.0116 0.1740  20  PHE A CD1 
149  C  CD2 . PHE A 20  ? 0.1543 0.4140 0.2111 -0.0604 -0.0807 0.0675  20  PHE A CD2 
150  C  CE1 . PHE A 20  ? 0.2117 0.4956 0.2928 0.0149  0.0365  0.1515  20  PHE A CE1 
151  C  CE2 . PHE A 20  ? 0.1485 0.4446 0.2702 -0.0418 -0.1108 0.1206  20  PHE A CE2 
152  C  CZ  . PHE A 20  ? 0.1213 0.4268 0.3498 -0.0374 0.0052  0.1198  20  PHE A CZ  
153  N  N   . PRO A 21  ? 0.2038 0.2503 0.1876 -0.0540 -0.0095 -0.0188 21  PRO A N   
154  C  CA  . PRO A 21  ? 0.1367 0.3253 0.1619 -0.0323 -0.0203 -0.0228 21  PRO A CA  
155  C  C   . PRO A 21  ? 0.1576 0.2449 0.1809 -0.0063 0.0061  -0.0182 21  PRO A C   
156  O  O   . PRO A 21  ? 0.1647 0.2876 0.1781 -0.0377 -0.0220 -0.0106 21  PRO A O   
157  C  CB  . PRO A 21  ? 0.1546 0.3621 0.1928 -0.0805 0.0041  -0.0439 21  PRO A CB  
158  C  CG  . PRO A 21  ? 0.3313 0.3356 0.2940 -0.1251 -0.0544 -0.0178 21  PRO A CG  
159  C  CD  . PRO A 21  ? 0.2118 0.2798 0.2825 -0.0738 0.0136  -0.0508 21  PRO A CD  
160  N  N   . ILE A 22  ? 0.1558 0.2572 0.0853 -0.0047 -0.0256 -0.0301 22  ILE A N   
161  C  CA  . ILE A 22  ? 0.1781 0.2284 0.0974 -0.0095 -0.0142 -0.0458 22  ILE A CA  
162  C  C   . ILE A 22  ? 0.1265 0.2222 0.0837 -0.0186 -0.0446 -0.0010 22  ILE A C   
163  O  O   . ILE A 22  ? 0.1395 0.2782 0.1244 -0.0354 -0.0236 -0.0221 22  ILE A O   
164  C  CB  . ILE A 22  ? 0.2046 0.2794 0.0341 0.0094  -0.0352 -0.0392 22  ILE A CB  
165  C  CG1 . ILE A 22  ? 0.2027 0.3288 0.0709 -0.0506 0.0065  -0.0363 22  ILE A CG1 
166  C  CG2 . ILE A 22  ? 0.1866 0.2864 0.0612 -0.0355 -0.0726 -0.0030 22  ILE A CG2 
167  C  CD1 . ILE A 22  ? 0.3316 0.4167 0.0971 0.0088  -0.0320 -0.0884 22  ILE A CD1 
168  N  N   . ALA A 23  ? 0.2028 0.2366 0.1068 -0.0151 -0.0427 -0.0401 23  ALA A N   
169  C  CA  . ALA A 23  ? 0.1777 0.2111 0.1278 0.0188  -0.0011 -0.0036 23  ALA A CA  
170  C  C   . ALA A 23  ? 0.1831 0.2593 0.1417 -0.0135 -0.0186 0.0236  23  ALA A C   
171  O  O   . ALA A 23  ? 0.1953 0.2579 0.1927 -0.0003 -0.0081 0.0258  23  ALA A O   
172  C  CB  . ALA A 23  ? 0.1723 0.2359 0.1328 -0.0175 0.0189  -0.0225 23  ALA A CB  
173  N  N   . LYS A 24  ? 0.1623 0.2811 0.1766 0.0242  -0.0286 -0.0082 24  LYS A N   
174  C  CA  . LYS A 24  ? 0.1985 0.3169 0.1802 0.0316  0.0499  0.0279  24  LYS A CA  
175  C  C   . LYS A 24  ? 0.2046 0.3465 0.0687 -0.0337 -0.0535 -0.0257 24  LYS A C   
176  O  O   . LYS A 24  ? 0.2125 0.4744 0.0944 -0.0518 -0.0864 0.0098  24  LYS A O   
177  C  CB  . LYS A 24  ? 0.1941 0.4143 0.2309 -0.0164 -0.0234 0.0054  24  LYS A CB  
178  C  CG  . LYS A 24  ? 0.1856 0.4373 0.2532 0.0825  0.0037  0.0463  24  LYS A CG  
179  C  CD  . LYS A 24  ? 0.2192 0.4957 0.4391 0.0759  -0.0790 0.0337  24  LYS A CD  
180  C  CE  . LYS A 24  ? 0.4037 0.4964 0.3939 0.0937  0.0772  0.1412  24  LYS A CE  
181  N  NZ  . LYS A 24  ? 0.3124 0.5691 0.6830 -0.1073 0.1018  0.0513  24  LYS A NZ  
182  N  N   . GLY A 25  ? 0.1716 0.3640 0.1319 -0.0139 -0.0033 -0.0293 25  GLY A N   
183  C  CA  . GLY A 25  ? 0.1844 0.3160 0.1169 -0.0228 -0.0247 -0.0185 25  GLY A CA  
184  C  C   . GLY A 25  ? 0.2115 0.3011 0.0899 -0.0055 -0.0790 0.0489  25  GLY A C   
185  O  O   . GLY A 25  ? 0.2134 0.3264 0.0791 -0.0057 -0.0617 0.0179  25  GLY A O   
186  N  N   . GLU A 26  ? 0.2027 0.3286 0.0599 -0.0293 -0.0719 0.0061  26  GLU A N   
187  C  CA  . GLU A 26  ? 0.2275 0.3485 0.0560 -0.0517 -0.0609 -0.0153 26  GLU A CA  
188  C  C   . GLU A 26  ? 0.2341 0.3371 0.0312 -0.0365 -0.0753 0.0077  26  GLU A C   
189  O  O   . GLU A 26  ? 0.2305 0.3415 0.0675 -0.0480 -0.0632 -0.0023 26  GLU A O   
190  C  CB  . GLU A 26  ? 0.2042 0.4445 0.0829 -0.0937 0.0108  -0.0730 26  GLU A CB  
191  C  CG  . GLU A 26  ? 0.1842 0.5177 0.2782 -0.0102 -0.0386 -0.0740 26  GLU A CG  
192  C  CD  . GLU A 26  ? 0.3033 0.5179 0.3867 -0.1097 -0.0866 0.0055  26  GLU A CD  
193  O  OE1 . GLU A 26  ? 0.4147 0.6053 0.3461 -0.1523 -0.0837 0.0447  26  GLU A OE1 
194  O  OE2 . GLU A 26  ? 0.3808 0.5820 0.4770 -0.0790 -0.0692 -0.1751 26  GLU A OE2 
195  N  N   A ARG A 27  ? 0.2138 0.2641 0.0240 -0.0227 -0.0552 0.0000  27  ARG A N   
196  N  N   B ARG A 27  ? 0.1702 0.2722 0.0179 -0.0094 -0.0376 -0.0256 27  ARG A N   
197  C  CA  A ARG A 27  ? 0.1905 0.2319 0.1073 -0.0447 -0.0291 -0.0250 27  ARG A CA  
198  C  CA  B ARG A 27  ? 0.1571 0.2883 0.0810 -0.0447 -0.0342 -0.0559 27  ARG A CA  
199  C  C   A ARG A 27  ? 0.2050 0.2357 0.0829 0.0087  -0.0551 0.0122  27  ARG A C   
200  C  C   B ARG A 27  ? 0.1549 0.2642 0.0664 -0.0037 -0.0682 -0.0252 27  ARG A C   
201  O  O   A ARG A 27  ? 0.1165 0.2182 0.0641 0.0040  -0.0283 -0.0006 27  ARG A O   
202  O  O   B ARG A 27  ? 0.1298 0.2829 0.0513 -0.0299 -0.0402 0.0251  27  ARG A O   
203  C  CB  A ARG A 27  ? 0.2507 0.2823 0.0849 -0.0075 -0.0517 -0.0400 27  ARG A CB  
204  C  CB  B ARG A 27  ? 0.1305 0.3436 0.0802 -0.0184 -0.0714 -0.0941 27  ARG A CB  
205  C  CG  A ARG A 27  ? 0.2315 0.3236 0.1704 -0.0280 -0.0685 0.0225  27  ARG A CG  
206  C  CG  B ARG A 27  ? 0.2387 0.4485 0.0994 0.0245  -0.1403 -0.0757 27  ARG A CG  
207  C  CD  A ARG A 27  ? 0.2803 0.2796 0.2697 -0.0580 -0.0719 -0.0211 27  ARG A CD  
208  C  CD  B ARG A 27  ? 0.2503 0.4146 0.2420 0.0383  -0.0266 -0.0606 27  ARG A CD  
209  N  NE  A ARG A 27  ? 0.2284 0.3114 0.2082 0.0042  -0.0143 0.0089  27  ARG A NE  
210  N  NE  B ARG A 27  ? 0.2491 0.3958 0.2663 0.0236  0.0070  -0.0164 27  ARG A NE  
211  C  CZ  A ARG A 27  ? 0.1909 0.2125 0.1847 -0.0456 0.0215  -0.0307 27  ARG A CZ  
212  C  CZ  B ARG A 27  ? 0.2893 0.2784 0.3027 0.0668  -0.0957 -0.0447 27  ARG A CZ  
213  N  NH1 A ARG A 27  ? 0.1065 0.2179 0.0306 -0.0823 0.0071  -0.0642 27  ARG A NH1 
214  N  NH1 B ARG A 27  ? 0.2544 0.3359 0.5712 0.0133  -0.0267 0.0614  27  ARG A NH1 
215  N  NH2 A ARG A 27  ? 0.1946 0.2057 0.0718 -0.0561 0.0610  -0.0913 27  ARG A NH2 
216  N  NH2 B ARG A 27  ? 0.2136 0.3660 0.4528 -0.0446 -0.0138 0.0571  27  ARG A NH2 
217  N  N   . GLN A 28  ? 0.1606 0.2264 0.0317 -0.0167 -0.0609 -0.0100 28  GLN A N   
218  C  CA  . GLN A 28  ? 0.1678 0.2176 0.0354 -0.0248 -0.0220 -0.0165 28  GLN A CA  
219  C  C   . GLN A 28  ? 0.1885 0.1982 0.0425 -0.0189 -0.0659 -0.0082 28  GLN A C   
220  O  O   . GLN A 28  ? 0.1712 0.2293 0.0853 -0.0330 -0.0668 0.0136  28  GLN A O   
221  C  CB  . GLN A 28  ? 0.1513 0.2491 0.0892 -0.0085 -0.0328 0.0047  28  GLN A CB  
222  C  CG  . GLN A 28  ? 0.1923 0.1985 0.0895 -0.0144 -0.0287 0.0055  28  GLN A CG  
223  C  CD  . GLN A 28  ? 0.2174 0.2046 0.0628 -0.0177 -0.0486 -0.0142 28  GLN A CD  
224  O  OE1 . GLN A 28  ? 0.1540 0.2311 0.0980 -0.0364 -0.0414 -0.0456 28  GLN A OE1 
225  N  NE2 . GLN A 28  ? 0.1551 0.2316 0.0806 -0.0222 -0.0817 -0.0236 28  GLN A NE2 
226  N  N   . SER A 29  ? 0.1522 0.2035 0.0357 -0.0041 -0.0501 -0.0193 29  SER A N   
227  C  CA  . SER A 29  ? 0.1167 0.2380 0.0973 -0.0068 -0.0317 -0.0347 29  SER A CA  
228  C  C   . SER A 29  ? 0.1335 0.2102 0.0802 -0.0167 -0.0250 -0.0041 29  SER A C   
229  O  O   . SER A 29  ? 0.1477 0.2328 0.0540 -0.0346 -0.0255 0.0167  29  SER A O   
230  C  CB  . SER A 29  ? 0.1880 0.2317 0.0600 0.0216  -0.0215 -0.0047 29  SER A CB  
231  O  OG  . SER A 29  ? 0.1736 0.2099 0.0704 -0.0091 -0.0414 -0.0170 29  SER A OG  
232  N  N   . PRO A 30  ? 0.1459 0.2254 0.0346 -0.0223 -0.0524 -0.0122 30  PRO A N   
233  C  CA  . PRO A 30  ? 0.1376 0.2276 0.0374 -0.0138 -0.0636 0.0001  30  PRO A CA  
234  C  C   . PRO A 30  ? 0.1258 0.1984 0.0425 -0.0124 -0.0451 0.0184  30  PRO A C   
235  O  O   . PRO A 30  ? 0.1357 0.2371 0.0797 -0.0139 -0.0656 -0.0022 30  PRO A O   
236  C  CB  . PRO A 30  ? 0.1819 0.2075 0.0619 -0.0095 -0.0291 -0.0399 30  PRO A CB  
237  C  CG  . PRO A 30  ? 0.1623 0.2408 0.0743 -0.0137 -0.0422 -0.0223 30  PRO A CG  
238  C  CD  . PRO A 30  ? 0.1659 0.2471 0.0216 -0.0042 -0.0479 -0.0131 30  PRO A CD  
239  N  N   . VAL A 31  ? 0.1508 0.2021 0.0862 -0.0153 -0.0286 0.0442  31  VAL A N   
240  C  CA  . VAL A 31  ? 0.1883 0.2384 0.0187 -0.0350 -0.0474 0.0083  31  VAL A CA  
241  C  C   . VAL A 31  ? 0.1949 0.2016 0.0371 -0.0135 -0.0544 -0.0046 31  VAL A C   
242  O  O   . VAL A 31  ? 0.1682 0.2310 0.0540 -0.0229 -0.0508 0.0124  31  VAL A O   
243  C  CB  . VAL A 31  ? 0.1623 0.2133 0.0955 -0.0168 -0.0171 -0.0199 31  VAL A CB  
244  C  CG1 . VAL A 31  ? 0.1917 0.2264 0.0819 -0.0198 -0.0474 -0.0231 31  VAL A CG1 
245  C  CG2 . VAL A 31  ? 0.1707 0.2311 0.0986 -0.0159 -0.0347 0.0093  31  VAL A CG2 
246  N  N   . ASP A 32  ? 0.1931 0.2086 0.0883 -0.0036 -0.0323 0.0316  32  ASP A N   
247  C  CA  . ASP A 32  ? 0.1872 0.2333 0.0908 0.0000  -0.0209 0.0609  32  ASP A CA  
248  C  C   . ASP A 32  ? 0.1675 0.2474 0.0817 -0.0245 -0.0296 0.0171  32  ASP A C   
249  O  O   . ASP A 32  ? 0.1914 0.3066 0.1030 -0.0381 -0.0244 -0.0220 32  ASP A O   
250  C  CB  . ASP A 32  ? 0.2337 0.2133 0.0730 -0.0339 -0.0796 0.0480  32  ASP A CB  
251  C  CG  . ASP A 32  ? 0.3495 0.1752 0.1524 -0.0673 -0.1386 0.0688  32  ASP A CG  
252  O  OD1 . ASP A 32  ? 0.2497 0.2208 0.1048 -0.0495 -0.0630 0.0021  32  ASP A OD1 
253  O  OD2 . ASP A 32  ? 0.3457 0.2644 0.1676 -0.0637 -0.0994 0.1046  32  ASP A OD2 
254  N  N   . ILE A 33  ? 0.1529 0.2601 0.0766 0.0275  -0.0278 0.0295  33  ILE A N   
255  C  CA  . ILE A 33  ? 0.1540 0.2619 0.0646 0.0183  -0.0365 0.0212  33  ILE A CA  
256  C  C   . ILE A 33  ? 0.2474 0.2737 0.0719 0.0185  -0.0551 0.0298  33  ILE A C   
257  O  O   . ILE A 33  ? 0.2271 0.2945 0.1145 -0.0115 0.0052  0.0074  33  ILE A O   
258  C  CB  . ILE A 33  ? 0.1366 0.2684 0.0767 -0.0013 -0.0348 0.0436  33  ILE A CB  
259  C  CG1 . ILE A 33  ? 0.1769 0.2806 0.0991 -0.0002 -0.0420 0.0622  33  ILE A CG1 
260  C  CG2 . ILE A 33  ? 0.1590 0.3080 0.1203 0.0389  -0.0201 0.0055  33  ILE A CG2 
261  C  CD1 . ILE A 33  ? 0.1795 0.2938 0.0989 -0.0162 -0.0636 0.0257  33  ILE A CD1 
262  N  N   . ASP A 34  ? 0.2176 0.2992 0.0577 0.0505  -0.0201 0.0189  34  ASP A N   
263  C  CA  . ASP A 34  ? 0.1959 0.3205 0.0905 0.0369  -0.0275 0.0462  34  ASP A CA  
264  C  C   . ASP A 34  ? 0.2197 0.2803 0.1914 0.0324  0.0082  0.0498  34  ASP A C   
265  O  O   . ASP A 34  ? 0.2833 0.2922 0.0851 -0.0051 0.0130  0.0603  34  ASP A O   
266  C  CB  . ASP A 34  ? 0.2890 0.3243 0.0247 -0.0103 -0.0271 0.0079  34  ASP A CB  
267  C  CG  . ASP A 34  ? 0.2835 0.4538 0.1562 0.0001  -0.0070 0.1162  34  ASP A CG  
268  O  OD1 . ASP A 34  ? 0.2840 0.5013 0.2032 0.0453  0.0004  0.1319  34  ASP A OD1 
269  O  OD2 . ASP A 34  ? 0.3735 0.5545 0.2113 0.0623  -0.0653 0.1326  34  ASP A OD2 
270  N  N   . THR A 35  ? 0.2071 0.3093 0.1037 0.0110  0.0111  0.0567  35  THR A N   
271  C  CA  . THR A 35  ? 0.2492 0.3137 0.1021 0.0555  -0.0163 0.0285  35  THR A CA  
272  C  C   . THR A 35  ? 0.2466 0.2963 0.1161 0.0517  0.0062  0.0613  35  THR A C   
273  O  O   . THR A 35  ? 0.2657 0.3225 0.1338 0.0704  0.0181  0.0623  35  THR A O   
274  C  CB  . THR A 35  ? 0.2317 0.3432 0.0950 0.0212  -0.0376 0.0691  35  THR A CB  
275  O  OG1 . THR A 35  ? 0.2722 0.3345 0.2141 -0.0189 0.0027  0.0366  35  THR A OG1 
276  C  CG2 . THR A 35  ? 0.2756 0.5299 0.1223 0.1104  0.0133  0.0807  35  THR A CG2 
277  N  N   . HIS A 36  ? 0.2801 0.2869 0.1404 0.0642  0.0504  0.1131  36  HIS A N   
278  C  CA  . HIS A 36  ? 0.3788 0.2703 0.1461 0.1037  0.1146  0.0727  36  HIS A CA  
279  C  C   . HIS A 36  ? 0.3773 0.3148 0.2801 0.1340  0.1471  0.0019  36  HIS A C   
280  O  O   . HIS A 36  ? 0.4932 0.5037 0.3353 0.0562  0.2561  -0.0206 36  HIS A O   
281  C  CB  . HIS A 36  ? 0.5949 0.2415 0.1903 0.0925  0.0607  0.0609  36  HIS A CB  
282  C  CG  . HIS A 36  ? 0.6297 0.2200 0.2122 0.0461  0.0457  0.0480  36  HIS A CG  
283  N  ND1 . HIS A 36  ? 0.6290 0.3976 0.1698 0.0200  0.0220  0.0586  36  HIS A ND1 
284  C  CD2 . HIS A 36  ? 0.8016 0.3595 0.1267 0.1889  -0.0476 -0.0287 36  HIS A CD2 
285  C  CE1 . HIS A 36  ? 0.7602 0.2945 0.1597 -0.0015 -0.0399 0.0889  36  HIS A CE1 
286  N  NE2 . HIS A 36  ? 0.7391 0.3761 0.1788 0.1745  -0.0673 -0.0093 36  HIS A NE2 
287  N  N   . THR A 37  ? 0.3644 0.3733 0.0734 0.0735  -0.0386 0.0893  37  THR A N   
288  C  CA  . THR A 37  ? 0.2786 0.4416 0.1892 0.0740  -0.0072 0.0013  37  THR A CA  
289  C  C   . THR A 37  ? 0.2188 0.4570 0.0803 0.0555  -0.0564 0.0022  37  THR A C   
290  O  O   . THR A 37  ? 0.3624 0.4978 0.1050 0.0449  -0.0813 0.0203  37  THR A O   
291  C  CB  . THR A 37  ? 0.2800 0.4751 0.1082 0.0939  -0.0484 0.0324  37  THR A CB  
292  O  OG1 . THR A 37  ? 0.3039 0.4980 0.2082 0.1054  0.0487  0.0031  37  THR A OG1 
293  C  CG2 . THR A 37  ? 0.3660 0.4588 0.2100 0.0087  -0.1351 0.0420  37  THR A CG2 
294  N  N   . ALA A 38  ? 0.2725 0.3035 0.0463 0.0552  -0.0247 0.0365  38  ALA A N   
295  C  CA  . ALA A 38  ? 0.2824 0.3097 0.0915 0.0474  -0.0083 0.0579  38  ALA A CA  
296  C  C   . ALA A 38  ? 0.2993 0.2301 0.1589 0.0302  0.0190  0.0462  38  ALA A C   
297  O  O   . ALA A 38  ? 0.3401 0.2397 0.2353 -0.0116 0.0243  0.0552  38  ALA A O   
298  C  CB  . ALA A 38  ? 0.2564 0.2945 0.1700 0.0516  -0.0913 0.0088  38  ALA A CB  
299  N  N   . LYS A 39  ? 0.3235 0.2653 0.0779 0.0219  -0.0392 0.0172  39  LYS A N   
300  C  CA  . LYS A 39  ? 0.3995 0.2541 0.1309 0.0653  0.0249  0.0075  39  LYS A CA  
301  C  C   . LYS A 39  ? 0.3175 0.2975 0.0926 0.0085  0.0392  0.0206  39  LYS A C   
302  O  O   . LYS A 39  ? 0.2989 0.3008 0.0528 0.0096  0.0164  0.0078  39  LYS A O   
303  C  CB  . LYS A 39  ? 0.3708 0.3945 0.1751 0.0840  -0.0523 -0.0165 39  LYS A CB  
304  C  CG  . LYS A 39  ? 0.6456 0.5863 0.1460 0.0703  0.1866  0.0564  39  LYS A CG  
305  N  N   . TYR A 40  ? 0.3432 0.3735 0.1362 -0.0297 0.0093  0.0033  40  TYR A N   
306  C  CA  . TYR A 40  ? 0.3409 0.3662 0.0525 -0.0555 0.0359  0.0193  40  TYR A CA  
307  C  C   . TYR A 40  ? 0.3138 0.3488 0.0419 -0.0227 -0.0566 0.0082  40  TYR A C   
308  O  O   . TYR A 40  ? 0.3312 0.3995 0.0366 0.0206  -0.0508 -0.0100 40  TYR A O   
309  C  CB  . TYR A 40  ? 0.3380 0.4796 0.0706 -0.0576 0.0747  -0.0110 40  TYR A CB  
310  C  CG  . TYR A 40  ? 0.3033 0.4979 0.0650 -0.0694 -0.0042 -0.0041 40  TYR A CG  
311  C  CD1 . TYR A 40  ? 0.3573 0.5404 0.0511 -0.0762 -0.0377 -0.0249 40  TYR A CD1 
312  C  CD2 . TYR A 40  ? 0.4178 0.5502 0.0626 -0.0576 0.0186  -0.0215 40  TYR A CD2 
313  C  CE1 . TYR A 40  ? 0.3018 0.6072 0.1849 -0.0699 0.0727  -0.0723 40  TYR A CE1 
314  C  CE2 . TYR A 40  ? 0.3260 0.7659 0.0741 -0.0665 -0.0744 -0.0677 40  TYR A CE2 
315  C  CZ  . TYR A 40  ? 0.1939 0.5472 0.1091 -0.0525 -0.0098 -0.0218 40  TYR A CZ  
316  O  OH  . TYR A 40  ? 0.2551 0.6732 0.2836 0.0418  -0.0107 -0.0203 40  TYR A OH  
317  N  N   . ASP A 41  ? 0.2629 0.3240 0.0806 -0.0006 0.0062  0.0174  41  ASP A N   
318  C  CA  . ASP A 41  ? 0.3043 0.3330 0.1812 -0.0093 -0.0111 -0.0009 41  ASP A CA  
319  C  C   . ASP A 41  ? 0.2332 0.4364 0.1244 -0.0579 -0.0216 -0.0475 41  ASP A C   
320  O  O   . ASP A 41  ? 0.2188 0.3894 0.1210 -0.0355 -0.0205 -0.0276 41  ASP A O   
321  C  CB  . ASP A 41  ? 0.2667 0.3662 0.1080 -0.0157 -0.0070 -0.0119 41  ASP A CB  
322  C  CG  . ASP A 41  ? 0.3355 0.3475 0.1707 -0.0398 -0.0022 0.0000  41  ASP A CG  
323  O  OD1 . ASP A 41  ? 0.2381 0.3944 0.1666 -0.0013 -0.1028 -0.0383 41  ASP A OD1 
324  O  OD2 . ASP A 41  ? 0.3039 0.3816 0.2438 -0.0734 0.0350  -0.0696 41  ASP A OD2 
325  N  N   . PRO A 42  ? 0.2706 0.3897 0.0882 0.0255  -0.0220 0.0077  42  PRO A N   
326  C  CA  . PRO A 42  ? 0.2724 0.4220 0.1495 0.0460  0.0515  -0.0290 42  PRO A CA  
327  C  C   . PRO A 42  ? 0.2635 0.4312 0.1761 -0.0022 0.0625  0.0133  42  PRO A C   
328  O  O   . PRO A 42  ? 0.2675 0.5075 0.1833 0.0108  0.0244  -0.0262 42  PRO A O   
329  C  CB  . PRO A 42  ? 0.3443 0.6397 0.0621 0.0629  -0.0195 -0.0598 42  PRO A CB  
330  C  CG  . PRO A 42  ? 0.3129 0.5575 0.1307 0.0949  0.0054  -0.0408 42  PRO A CG  
331  C  CD  . PRO A 42  ? 0.3660 0.4438 0.0505 0.0200  0.0367  0.0472  42  PRO A CD  
332  N  N   A SER A 43  ? 0.3244 0.4145 0.1054 -0.0340 -0.0229 -0.0334 43  SER A N   
333  N  N   B SER A 43  ? 0.2934 0.4174 0.0192 -0.0093 -0.0537 -0.0329 43  SER A N   
334  C  CA  A SER A 43  ? 0.3138 0.4194 0.1535 -0.0791 -0.0326 0.0356  43  SER A CA  
335  C  CA  B SER A 43  ? 0.2951 0.4044 0.0894 -0.0367 -0.0217 0.0109  43  SER A CA  
336  C  C   A SER A 43  ? 0.3322 0.4382 0.1263 -0.0636 -0.0856 -0.0573 43  SER A C   
337  C  C   B SER A 43  ? 0.3000 0.4404 0.0812 -0.0444 -0.0734 -0.0443 43  SER A C   
338  O  O   A SER A 43  ? 0.4061 0.4434 0.1975 -0.0060 -0.0693 -0.0332 43  SER A O   
339  O  O   B SER A 43  ? 0.3716 0.4356 0.1949 0.0075  -0.0576 -0.0293 43  SER A O   
340  C  CB  A SER A 43  ? 0.4087 0.4811 0.3087 -0.1479 -0.0509 -0.0389 43  SER A CB  
341  C  CB  B SER A 43  ? 0.2427 0.4241 0.0336 -0.0238 0.0530  -0.0036 43  SER A CB  
342  O  OG  A SER A 43  ? 0.4915 0.5049 0.1657 -0.1776 -0.0012 -0.0883 43  SER A OG  
343  O  OG  B SER A 43  ? 0.3086 0.3823 0.0431 -0.0306 -0.1050 0.0007  43  SER A OG  
344  N  N   . LEU A 44  ? 0.3431 0.4236 0.1274 -0.0358 0.0048  -0.0231 44  LEU A N   
345  C  CA  . LEU A 44  ? 0.2598 0.3881 0.1165 0.0074  -0.0282 -0.0137 44  LEU A CA  
346  C  C   . LEU A 44  ? 0.2707 0.4584 0.0842 0.0197  -0.0055 0.0207  44  LEU A C   
347  O  O   . LEU A 44  ? 0.2366 0.6171 0.1567 -0.0337 -0.0322 -0.0141 44  LEU A O   
348  C  CB  . LEU A 44  ? 0.2569 0.3690 0.1490 0.0029  -0.0552 0.0267  44  LEU A CB  
349  C  CG  . LEU A 44  ? 0.2497 0.3195 0.1100 -0.0115 -0.0282 -0.0027 44  LEU A CG  
350  C  CD1 . LEU A 44  ? 0.3816 0.2928 0.2049 -0.0561 -0.0110 0.0274  44  LEU A CD1 
351  C  CD2 . LEU A 44  ? 0.2329 0.3486 0.1292 -0.0295 -0.0234 0.0068  44  LEU A CD2 
352  N  N   . LYS A 45  ? 0.2764 0.4433 0.1183 0.0064  -0.0201 0.0283  45  LYS A N   
353  C  CA  . LYS A 45  ? 0.2415 0.4698 0.2070 0.0192  -0.0160 -0.0155 45  LYS A CA  
354  C  C   . LYS A 45  ? 0.2340 0.4384 0.3251 -0.0286 0.0133  -0.0775 45  LYS A C   
355  O  O   . LYS A 45  ? 0.2636 0.4150 0.1619 0.0064  -0.0281 0.0374  45  LYS A O   
356  C  CB  . LYS A 45  ? 0.3111 0.4036 0.3166 0.0252  -0.0398 -0.0557 45  LYS A CB  
357  C  CG  . LYS A 45  ? 0.4106 0.5544 0.2602 -0.0337 -0.0006 -0.0881 45  LYS A CG  
358  N  N   . PRO A 46  ? 0.2779 0.3715 0.2652 0.0040  0.0037  -0.0077 46  PRO A N   
359  C  CA  . PRO A 46  ? 0.2275 0.4663 0.2897 -0.0930 0.0482  -0.0452 46  PRO A CA  
360  C  C   . PRO A 46  ? 0.2300 0.3966 0.2068 -0.0256 -0.0264 0.0357  46  PRO A C   
361  O  O   . PRO A 46  ? 0.2622 0.4354 0.1278 -0.0691 -0.0253 0.0176  46  PRO A O   
362  C  CB  . PRO A 46  ? 0.2864 0.4786 0.2171 0.0351  0.0485  0.0468  46  PRO A CB  
363  C  CG  . PRO A 46  ? 0.3353 0.4932 0.2100 -0.0085 -0.0613 -0.0811 46  PRO A CG  
364  C  CD  . PRO A 46  ? 0.2434 0.4490 0.2443 0.0201  -0.0227 0.0094  46  PRO A CD  
365  N  N   . LEU A 47  ? 0.1772 0.3971 0.1226 -0.0513 -0.0208 0.0173  47  LEU A N   
366  C  CA  . LEU A 47  ? 0.1888 0.4480 0.1215 -0.0372 -0.0302 0.0600  47  LEU A CA  
367  C  C   . LEU A 47  ? 0.2064 0.3486 0.2179 -0.0678 -0.0974 0.0725  47  LEU A C   
368  O  O   . LEU A 47  ? 0.2819 0.3709 0.2318 -0.1077 -0.0942 0.0253  47  LEU A O   
369  C  CB  . LEU A 47  ? 0.2933 0.3371 0.3193 -0.0665 -0.0729 0.0287  47  LEU A CB  
370  C  CG  . LEU A 47  ? 0.1903 0.4091 0.3389 -0.0222 -0.1054 0.0652  47  LEU A CG  
371  C  CD1 . LEU A 47  ? 0.1672 0.5442 0.1820 -0.0809 -0.0165 0.0301  47  LEU A CD1 
372  C  CD2 . LEU A 47  ? 0.3467 0.3981 0.2746 -0.0326 -0.0541 0.0381  47  LEU A CD2 
373  N  N   . SER A 48  ? 0.1763 0.3510 0.0325 -0.0425 -0.0533 0.0223  48  SER A N   
374  C  CA  . SER A 48  ? 0.1665 0.3233 0.0119 -0.0095 -0.0301 0.0002  48  SER A CA  
375  C  C   . SER A 48  ? 0.2183 0.2673 0.0651 -0.0427 0.0252  0.0079  48  SER A C   
376  O  O   . SER A 48  ? 0.1866 0.3230 0.0601 -0.0374 -0.0035 -0.0115 48  SER A O   
377  C  CB  . SER A 48  ? 0.1988 0.3620 0.2124 0.0595  0.0628  0.0230  48  SER A CB  
378  O  OG  . SER A 48  ? 0.3257 0.3968 0.2868 0.0775  0.0466  0.0566  48  SER A OG  
379  N  N   . VAL A 49  ? 0.2499 0.3234 0.0653 -0.0696 -0.0207 -0.0074 49  VAL A N   
380  C  CA  . VAL A 49  ? 0.2922 0.3513 0.0267 -0.0556 -0.0572 0.0496  49  VAL A CA  
381  C  C   . VAL A 49  ? 0.2246 0.3263 0.0515 -0.0568 -0.0515 0.0097  49  VAL A C   
382  O  O   . VAL A 49  ? 0.3042 0.4556 0.1934 -0.1559 -0.0544 0.0000  49  VAL A O   
383  C  CB  . VAL A 49  ? 0.2243 0.4176 0.0621 -0.0010 -0.0137 -0.0427 49  VAL A CB  
384  C  CG1 . VAL A 49  ? 0.3847 0.4703 0.0838 -0.1349 0.0754  -0.0029 49  VAL A CG1 
385  C  CG2 . VAL A 49  ? 0.2890 0.3881 0.1574 -0.0623 -0.0833 -0.0126 49  VAL A CG2 
386  N  N   . SER A 50  ? 0.2039 0.2933 0.1319 -0.0252 -0.0196 -0.0027 50  SER A N   
387  C  CA  . SER A 50  ? 0.1812 0.3491 0.1077 -0.0222 -0.0017 0.0339  50  SER A CA  
388  C  C   . SER A 50  ? 0.1526 0.3326 0.1238 -0.0177 0.0164  -0.0178 50  SER A C   
389  O  O   . SER A 50  ? 0.1640 0.3215 0.1327 -0.0113 -0.0083 0.0110  50  SER A O   
390  C  CB  . SER A 50  ? 0.2232 0.3633 0.1917 -0.0378 0.0168  -0.0110 50  SER A CB  
391  O  OG  . SER A 50  ? 0.3171 0.4868 0.2613 -0.0307 0.1102  -0.0691 50  SER A OG  
392  N  N   . TYR A 51  ? 0.1671 0.3497 0.1234 -0.0299 -0.0167 -0.0351 51  TYR A N   
393  C  CA  . TYR A 51  ? 0.1788 0.3160 0.1490 -0.0043 0.0148  0.0348  51  TYR A CA  
394  C  C   . TYR A 51  ? 0.1946 0.3013 0.1759 -0.0064 -0.0079 0.0501  51  TYR A C   
395  O  O   . TYR A 51  ? 0.2229 0.3349 0.1436 -0.0024 -0.0697 0.0375  51  TYR A O   
396  C  CB  . TYR A 51  ? 0.1903 0.3069 0.1122 -0.0023 -0.0570 0.0193  51  TYR A CB  
397  C  CG  . TYR A 51  ? 0.1795 0.3075 0.0763 -0.0062 -0.0344 0.0137  51  TYR A CG  
398  C  CD1 . TYR A 51  ? 0.1654 0.2655 0.1134 -0.0183 -0.0220 0.0452  51  TYR A CD1 
399  C  CD2 . TYR A 51  ? 0.1626 0.3040 0.1102 -0.0032 -0.0043 0.0377  51  TYR A CD2 
400  C  CE1 . TYR A 51  ? 0.1662 0.2713 0.1194 0.0020  -0.0185 0.0362  51  TYR A CE1 
401  C  CE2 . TYR A 51  ? 0.1691 0.3317 0.1141 -0.0530 -0.0414 0.0099  51  TYR A CE2 
402  C  CZ  . TYR A 51  ? 0.1932 0.2630 0.0740 -0.0130 -0.0467 0.0166  51  TYR A CZ  
403  O  OH  . TYR A 51  ? 0.1905 0.2856 0.0838 -0.0105 -0.0475 0.0053  51  TYR A OH  
404  N  N   . ASP A 52  ? 0.1743 0.3045 0.1763 -0.0160 -0.0948 0.0189  52  ASP A N   
405  C  CA  . ASP A 52  ? 0.1535 0.3911 0.1283 0.0072  -0.0530 0.0449  52  ASP A CA  
406  C  C   . ASP A 52  ? 0.3167 0.3615 0.1403 -0.0238 -0.0561 0.0217  52  ASP A C   
407  O  O   . ASP A 52  ? 0.2770 0.4506 0.1644 -0.0165 -0.1060 0.0310  52  ASP A O   
408  C  CB  . ASP A 52  ? 0.1535 0.4673 0.2287 0.0027  -0.0520 -0.0122 52  ASP A CB  
409  C  CG  . ASP A 52  ? 0.3737 0.5177 0.5443 0.0145  0.0807  -0.1687 52  ASP A CG  
410  O  OD1 . ASP A 52  ? 0.3666 0.8005 0.6652 -0.1203 0.0359  -0.1310 52  ASP A OD1 
411  O  OD2 . ASP A 52  ? 0.4195 0.5401 0.7621 -0.0042 0.1055  0.0231  52  ASP A OD2 
412  N  N   . GLN A 53  ? 0.1996 0.3514 0.2237 -0.0264 0.0662  0.0551  53  GLN A N   
413  C  CA  . GLN A 53  ? 0.1802 0.3586 0.0842 0.0543  -0.0050 0.0457  53  GLN A CA  
414  C  C   . GLN A 53  ? 0.1744 0.3157 0.0544 0.0423  -0.0053 0.0116  53  GLN A C   
415  O  O   . GLN A 53  ? 0.2314 0.3105 0.1306 0.0515  -0.0168 0.0534  53  GLN A O   
416  C  CB  . GLN A 53  ? 0.2570 0.4092 0.1920 0.0897  0.0152  0.0120  53  GLN A CB  
417  C  CG  . GLN A 53  ? 0.1910 0.5177 0.1215 0.0161  -0.0102 0.0577  53  GLN A CG  
418  C  CD  . GLN A 53  ? 0.1560 0.5875 0.1580 0.0084  -0.0245 0.0652  53  GLN A CD  
419  O  OE1 . GLN A 53  ? 0.2575 0.8998 0.5519 -0.1332 0.0709  -0.0104 53  GLN A OE1 
420  N  NE2 . GLN A 53  ? 0.2290 0.6573 0.3032 0.0036  0.0190  0.2251  53  GLN A NE2 
421  N  N   . ALA A 54  ? 0.1538 0.3213 0.0752 0.0380  -0.0316 -0.0276 54  ALA A N   
422  C  CA  . ALA A 54  ? 0.1676 0.2803 0.0662 0.0368  0.0144  0.0107  54  ALA A CA  
423  C  C   . ALA A 54  ? 0.1653 0.2919 0.0591 0.0074  0.0003  -0.0236 54  ALA A C   
424  O  O   . ALA A 54  ? 0.1777 0.3156 0.1280 -0.0002 -0.0451 -0.0144 54  ALA A O   
425  C  CB  . ALA A 54  ? 0.1844 0.2781 0.0766 0.0134  -0.0702 0.0164  54  ALA A CB  
426  N  N   . THR A 55  ? 0.1594 0.2396 0.0328 0.0330  -0.0258 0.0184  55  THR A N   
427  C  CA  . THR A 55  ? 0.1799 0.2381 0.0364 0.0389  -0.0151 0.0179  55  THR A CA  
428  C  C   . THR A 55  ? 0.1707 0.1845 0.0910 0.0234  -0.0284 0.0304  55  THR A C   
429  O  O   . THR A 55  ? 0.1896 0.2143 0.0885 0.0075  -0.0310 -0.0173 55  THR A O   
430  C  CB  . THR A 55  ? 0.2041 0.2438 0.0811 0.0194  -0.0196 0.0302  55  THR A CB  
431  O  OG1 . THR A 55  ? 0.2276 0.3062 0.1626 0.0284  -0.0061 -0.0296 55  THR A OG1 
432  C  CG2 . THR A 55  ? 0.2384 0.3037 0.0885 0.0610  0.0055  0.0221  55  THR A CG2 
433  N  N   . SER A 56  ? 0.1583 0.2196 0.0372 0.0234  -0.0675 -0.0122 56  SER A N   
434  C  CA  . SER A 56  ? 0.1672 0.2190 0.0235 0.0258  -0.0433 -0.0072 56  SER A CA  
435  C  C   . SER A 56  ? 0.1572 0.1974 0.0790 0.0472  -0.0396 0.0373  56  SER A C   
436  O  O   . SER A 56  ? 0.1910 0.2409 0.0616 0.0443  -0.0717 0.0139  56  SER A O   
437  C  CB  . SER A 56  ? 0.1659 0.2122 0.0418 0.0231  -0.0538 -0.0218 56  SER A CB  
438  O  OG  . SER A 56  ? 0.1802 0.2278 0.0428 0.0099  -0.0659 0.0095  56  SER A OG  
439  N  N   . LEU A 57  ? 0.1622 0.2256 0.0779 0.0221  -0.0212 0.0210  57  LEU A N   
440  C  CA  . LEU A 57  ? 0.2075 0.2391 0.0678 0.0363  -0.0223 0.0408  57  LEU A CA  
441  C  C   . LEU A 57  ? 0.1654 0.2029 0.0926 0.0357  -0.0422 0.0351  57  LEU A C   
442  O  O   . LEU A 57  ? 0.2757 0.2666 0.0713 0.0582  -0.0026 0.0484  57  LEU A O   
443  C  CB  . LEU A 57  ? 0.1896 0.2587 0.1192 0.0074  0.0409  0.0228  57  LEU A CB  
444  C  CG  . LEU A 57  ? 0.2512 0.2370 0.1488 0.0326  -0.0571 0.0189  57  LEU A CG  
445  C  CD1 . LEU A 57  ? 0.3440 0.3198 0.1269 -0.0834 -0.0311 0.0068  57  LEU A CD1 
446  C  CD2 . LEU A 57  ? 0.2419 0.3253 0.1310 0.0904  -0.0229 0.0262  57  LEU A CD2 
447  N  N   . ARG A 58  ? 0.1744 0.2107 0.0989 0.0614  -0.0207 0.0329  58  ARG A N   
448  C  CA  . ARG A 58  ? 0.2020 0.2071 0.0915 0.0504  0.0130  0.0444  58  ARG A CA  
449  C  C   . ARG A 58  ? 0.1712 0.2190 0.0187 0.0546  0.0035  0.0285  58  ARG A C   
450  O  O   . ARG A 58  ? 0.2096 0.2397 0.0171 0.0188  -0.0008 0.0286  58  ARG A O   
451  C  CB  . ARG A 58  ? 0.2474 0.2329 0.3015 0.0157  0.1161  0.0937  58  ARG A CB  
452  C  CG  . ARG A 58  ? 0.3467 0.2800 0.4205 0.0761  0.1729  0.1454  58  ARG A CG  
453  C  CD  . ARG A 58  ? 0.3748 0.3231 0.4503 0.0469  0.2425  0.1498  58  ARG A CD  
454  N  NE  . ARG A 58  ? 0.4085 0.3771 0.5253 0.0699  0.2484  0.1182  58  ARG A NE  
455  C  CZ  . ARG A 58  ? 0.5554 0.3956 0.5723 0.1458  0.1847  0.1887  58  ARG A CZ  
456  N  NH1 . ARG A 58  ? 0.4494 0.6339 0.5826 0.1699  0.2813  0.2739  58  ARG A NH1 
457  N  NH2 . ARG A 58  ? 0.4169 0.4384 0.3670 0.1515  0.0996  0.2482  58  ARG A NH2 
458  N  N   . ILE A 59  ? 0.1641 0.1872 0.0939 0.0318  -0.0053 0.0107  59  ILE A N   
459  C  CA  . ILE A 59  ? 0.1751 0.1812 0.0682 0.0250  0.0192  0.0155  59  ILE A CA  
460  C  C   . ILE A 59  ? 0.1632 0.2280 0.0314 0.0000  0.0107  0.0087  59  ILE A C   
461  O  O   . ILE A 59  ? 0.1610 0.2455 0.0273 -0.0016 0.0006  0.0151  59  ILE A O   
462  C  CB  . ILE A 59  ? 0.2076 0.1929 0.0092 0.0032  -0.0154 0.0176  59  ILE A CB  
463  C  CG1 . ILE A 59  ? 0.2291 0.2041 0.0777 -0.0054 -0.0524 0.0456  59  ILE A CG1 
464  C  CG2 . ILE A 59  ? 0.1662 0.2397 0.0224 0.0084  -0.0063 -0.0289 59  ILE A CG2 
465  C  CD1 . ILE A 59  ? 0.2265 0.2088 0.0707 -0.0015 -0.0040 0.0339  59  ILE A CD1 
466  N  N   . LEU A 60  ? 0.1569 0.2025 0.0655 0.0163  -0.0072 0.0061  60  LEU A N   
467  C  CA  . LEU A 60  ? 0.1733 0.2005 0.0817 0.0261  0.0031  -0.0070 60  LEU A CA  
468  C  C   . LEU A 60  ? 0.1303 0.2133 0.0991 0.0141  0.0121  0.0260  60  LEU A C   
469  O  O   . LEU A 60  ? 0.1783 0.2192 0.0820 0.0312  -0.0003 0.0259  60  LEU A O   
470  C  CB  . LEU A 60  ? 0.1702 0.2312 0.1095 -0.0167 0.0055  -0.0128 60  LEU A CB  
471  C  CG  . LEU A 60  ? 0.2127 0.2440 0.1281 -0.0124 -0.0118 -0.0514 60  LEU A CG  
472  C  CD1 . LEU A 60  ? 0.2304 0.4969 0.2851 0.0009  -0.0172 -0.1249 60  LEU A CD1 
473  C  CD2 . LEU A 60  ? 0.3957 0.3221 0.1829 0.0954  -0.0133 -0.0084 60  LEU A CD2 
474  N  N   . ASN A 61  ? 0.1362 0.1808 0.0980 0.0222  -0.0050 -0.0051 61  ASN A N   
475  C  CA  . ASN A 61  ? 0.1109 0.2063 0.1292 0.0292  -0.0064 -0.0316 61  ASN A CA  
476  C  C   . ASN A 61  ? 0.1502 0.2197 0.0585 -0.0055 -0.0171 -0.0151 61  ASN A C   
477  O  O   . ASN A 61  ? 0.1750 0.2294 0.1156 -0.0234 0.0116  0.0027  61  ASN A O   
478  C  CB  . ASN A 61  ? 0.1547 0.1884 0.0804 0.0330  -0.0036 -0.0074 61  ASN A CB  
479  C  CG  . ASN A 61  ? 0.1295 0.1845 0.1496 0.0054  -0.0037 0.0171  61  ASN A CG  
480  O  OD1 . ASN A 61  ? 0.1400 0.2450 0.1310 0.0065  -0.0053 -0.0146 61  ASN A OD1 
481  N  ND2 . ASN A 61  ? 0.1860 0.1910 0.0907 0.0011  -0.0034 0.0348  61  ASN A ND2 
482  N  N   . ASN A 62  ? 0.1590 0.2253 0.0937 0.0084  -0.0881 -0.0139 62  ASN A N   
483  C  CA  . ASN A 62  ? 0.1683 0.2242 0.1502 0.0050  -0.0554 -0.0092 62  ASN A CA  
484  C  C   . ASN A 62  ? 0.1589 0.2280 0.0813 -0.0072 -0.0518 -0.0103 62  ASN A C   
485  O  O   . ASN A 62  ? 0.1664 0.2774 0.2114 -0.0359 -0.0562 -0.0457 62  ASN A O   
486  C  CB  . ASN A 62  ? 0.2687 0.2326 0.1296 0.0061  -0.0108 0.0172  62  ASN A CB  
487  C  CG  . ASN A 62  ? 0.3521 0.2617 0.1142 0.0152  -0.0498 0.0019  62  ASN A CG  
488  O  OD1 . ASN A 62  ? 0.3643 0.2634 0.0659 0.0161  -0.0370 -0.0232 62  ASN A OD1 
489  N  ND2 . ASN A 62  ? 0.5116 0.3303 0.1777 -0.0472 0.0013  -0.0697 62  ASN A ND2 
490  N  N   . GLY A 63  ? 0.1755 0.2071 0.1102 0.0076  -0.0267 0.0168  63  GLY A N   
491  C  CA  . GLY A 63  ? 0.1892 0.2039 0.1100 0.0143  -0.0592 0.0111  63  GLY A CA  
492  C  C   . GLY A 63  ? 0.2025 0.2310 0.1119 -0.0006 -0.0132 0.0245  63  GLY A C   
493  O  O   . GLY A 63  ? 0.2025 0.2851 0.1981 0.0381  -0.0185 -0.0008 63  GLY A O   
494  N  N   . HIS A 64  ? 0.1687 0.2201 0.1242 -0.0038 -0.0359 -0.0004 64  HIS A N   
495  C  CA  . HIS A 64  ? 0.1909 0.2353 0.1341 -0.0055 -0.0618 0.0216  64  HIS A CA  
496  C  C   . HIS A 64  ? 0.1822 0.2432 0.1562 0.0118  -0.0478 0.0074  64  HIS A C   
497  O  O   . HIS A 64  ? 0.1666 0.2694 0.2283 -0.0124 -0.0756 0.0414  64  HIS A O   
498  C  CB  . HIS A 64  ? 0.1841 0.3601 0.1014 0.0070  -0.0736 -0.0207 64  HIS A CB  
499  C  CG  . HIS A 64  ? 0.2569 0.4271 0.0827 -0.0419 -0.0730 0.0043  64  HIS A CG  
500  N  ND1 . HIS A 64  ? 0.1830 0.5258 0.2420 -0.0542 -0.0644 0.0223  64  HIS A ND1 
501  C  CD2 . HIS A 64  ? 0.2909 0.4346 0.2088 -0.0030 -0.0465 0.0210  64  HIS A CD2 
502  C  CE1 . HIS A 64  ? 0.2164 0.5042 0.1826 -0.0595 -0.0989 0.0531  64  HIS A CE1 
503  N  NE2 . HIS A 64  ? 0.3019 0.4442 0.3917 -0.1088 -0.0749 0.0659  64  HIS A NE2 
504  N  N   . SER A 65  ? 0.1571 0.2400 0.0682 -0.0025 -0.0578 -0.0058 65  SER A N   
505  C  CA  . SER A 65  ? 0.1799 0.2472 0.0469 -0.0024 -0.0262 0.0238  65  SER A CA  
506  C  C   . SER A 65  ? 0.1569 0.2136 0.1328 0.0215  -0.0341 0.0386  65  SER A C   
507  O  O   . SER A 65  ? 0.1676 0.2379 0.1314 0.0096  -0.0237 0.0301  65  SER A O   
508  C  CB  . SER A 65  ? 0.1716 0.3195 0.0487 -0.0398 -0.0218 0.0211  65  SER A CB  
509  O  OG  . SER A 65  ? 0.1712 0.4344 0.1644 -0.0653 -0.0825 0.0936  65  SER A OG  
510  N  N   . PHE A 66  ? 0.1500 0.1959 0.1223 0.0530  0.0070  -0.0067 66  PHE A N   
511  C  CA  . PHE A 66  ? 0.1323 0.2163 0.0873 0.0177  -0.0276 -0.0107 66  PHE A CA  
512  C  C   . PHE A 66  ? 0.1580 0.2059 0.0926 0.0260  -0.0088 0.0111  66  PHE A C   
513  O  O   . PHE A 66  ? 0.2147 0.2143 0.0680 0.0289  0.0032  0.0055  66  PHE A O   
514  C  CB  . PHE A 66  ? 0.1914 0.2266 0.1073 -0.0067 -0.0366 -0.0308 66  PHE A CB  
515  C  CG  . PHE A 66  ? 0.1578 0.2179 0.0607 0.0041  -0.0618 -0.0427 66  PHE A CG  
516  C  CD1 . PHE A 66  ? 0.1733 0.2534 0.0411 0.0308  -0.0465 0.0203  66  PHE A CD1 
517  C  CD2 . PHE A 66  ? 0.1781 0.2264 0.0702 0.0099  -0.0608 -0.0317 66  PHE A CD2 
518  C  CE1 . PHE A 66  ? 0.1596 0.2541 0.0491 0.0234  -0.0473 -0.0133 66  PHE A CE1 
519  C  CE2 . PHE A 66  ? 0.2031 0.2249 0.0777 0.0130  -0.0577 -0.0075 66  PHE A CE2 
520  C  CZ  . PHE A 66  ? 0.1788 0.2309 0.0838 -0.0017 -0.0552 -0.0319 66  PHE A CZ  
521  N  N   . LYS A 67  ? 0.1618 0.2134 0.0782 0.0367  -0.0488 -0.0079 67  LYS A N   
522  C  CA  . LYS A 67  ? 0.0998 0.2542 0.1012 0.0316  -0.0483 -0.0049 67  LYS A CA  
523  C  C   . LYS A 67  ? 0.1493 0.1989 0.0221 0.0352  -0.0139 0.0313  67  LYS A C   
524  O  O   . LYS A 67  ? 0.1723 0.2450 0.0086 0.0209  -0.0072 0.0074  67  LYS A O   
525  C  CB  . LYS A 67  ? 0.1932 0.2574 0.2875 -0.0100 -0.0882 -0.0507 67  LYS A CB  
526  C  CG  . LYS A 67  ? 0.2818 0.2897 0.2282 -0.0414 -0.1890 0.0121  67  LYS A CG  
527  C  CD  . LYS A 67  ? 0.2873 0.2834 0.2463 -0.1089 -0.1655 0.0167  67  LYS A CD  
528  C  CE  . LYS A 67  ? 0.3539 0.3143 0.2865 -0.1078 -0.1073 -0.0347 67  LYS A CE  
529  N  NZ  . LYS A 67  ? 0.3358 0.2670 0.3319 -0.0917 -0.0119 -0.0281 67  LYS A NZ  
530  N  N   . VAL A 68  ? 0.1265 0.1993 0.0824 0.0245  -0.0276 -0.0032 68  VAL A N   
531  C  CA  . VAL A 68  ? 0.1404 0.1784 0.1066 0.0242  -0.0472 -0.0083 68  VAL A CA  
532  C  C   . VAL A 68  ? 0.1582 0.1673 0.0574 0.0255  0.0103  0.0042  68  VAL A C   
533  O  O   . VAL A 68  ? 0.1441 0.2305 0.0489 0.0185  -0.0216 -0.0061 68  VAL A O   
534  C  CB  . VAL A 68  ? 0.1587 0.2132 0.0572 0.0155  -0.0467 -0.0070 68  VAL A CB  
535  C  CG1 . VAL A 68  ? 0.1402 0.2611 0.0644 0.0137  -0.0616 0.0066  68  VAL A CG1 
536  C  CG2 . VAL A 68  ? 0.1712 0.2443 0.0472 0.0017  -0.0428 -0.0362 68  VAL A CG2 
537  N  N   . GLU A 69  ? 0.1599 0.1733 0.0722 0.0282  -0.0425 0.0109  69  GLU A N   
538  C  CA  . GLU A 69  ? 0.1737 0.1780 0.0957 0.0496  0.0039  0.0175  69  GLU A CA  
539  C  C   . GLU A 69  ? 0.1203 0.2106 0.0750 0.0073  -0.0329 -0.0050 69  GLU A C   
540  O  O   . GLU A 69  ? 0.1705 0.2129 0.0616 0.0267  -0.0463 -0.0086 69  GLU A O   
541  C  CB  . GLU A 69  ? 0.2032 0.2006 0.1694 0.0002  0.0147  0.0332  69  GLU A CB  
542  C  CG  . GLU A 69  ? 0.2242 0.2833 0.1438 0.0209  -0.0262 -0.0290 69  GLU A CG  
543  C  CD  . GLU A 69  ? 0.2375 0.3797 0.1161 -0.0283 -0.0135 -0.0258 69  GLU A CD  
544  O  OE1 . GLU A 69  ? 0.2456 0.3966 0.2411 -0.0248 0.0183  0.0265  69  GLU A OE1 
545  O  OE2 . GLU A 69  ? 0.4257 0.4340 0.2592 -0.0629 0.1446  -0.0643 69  GLU A OE2 
546  N  N   . PHE A 70  ? 0.1587 0.1949 0.0970 0.0284  -0.0049 0.0138  70  PHE A N   
547  C  CA  . PHE A 70  ? 0.1456 0.1927 0.0488 0.0206  -0.0096 0.0039  70  PHE A CA  
548  C  C   . PHE A 70  ? 0.1508 0.1945 0.0840 0.0238  -0.0303 0.0185  70  PHE A C   
549  O  O   . PHE A 70  ? 0.1991 0.2134 0.1012 -0.0141 -0.0607 0.0075  70  PHE A O   
550  C  CB  . PHE A 70  ? 0.1543 0.2090 0.0636 0.0114  0.0033  0.0062  70  PHE A CB  
551  C  CG  . PHE A 70  ? 0.1478 0.2165 0.0417 0.0120  -0.0137 0.0198  70  PHE A CG  
552  C  CD1 . PHE A 70  ? 0.1830 0.2325 0.1086 0.0286  0.0085  0.0389  70  PHE A CD1 
553  C  CD2 . PHE A 70  ? 0.1535 0.2611 0.0161 -0.0033 -0.0192 0.0434  70  PHE A CD2 
554  C  CE1 . PHE A 70  ? 0.1998 0.2389 0.0980 0.0119  -0.0124 0.0416  70  PHE A CE1 
555  C  CE2 . PHE A 70  ? 0.1932 0.2523 0.0199 0.0013  -0.0052 0.0509  70  PHE A CE2 
556  C  CZ  . PHE A 70  ? 0.1928 0.2287 0.1045 -0.0016 0.0099  0.0153  70  PHE A CZ  
557  N  N   . ASP A 71  ? 0.2023 0.1888 0.0985 0.0496  -0.0399 0.0250  71  ASP A N   
558  C  CA  . ASP A 71  ? 0.1824 0.1969 0.1048 0.0409  -0.0641 0.0337  71  ASP A CA  
559  C  C   . ASP A 71  ? 0.2182 0.1995 0.1525 -0.0201 0.0098  0.0063  71  ASP A C   
560  O  O   . ASP A 71  ? 0.2067 0.2883 0.2910 0.0061  0.0280  -0.0356 71  ASP A O   
561  C  CB  . ASP A 71  ? 0.2134 0.2444 0.1625 0.0353  -0.1236 0.0244  71  ASP A CB  
562  C  CG  . ASP A 71  ? 0.2519 0.2323 0.2933 0.0015  -0.1156 0.0282  71  ASP A CG  
563  O  OD1 . ASP A 71  ? 0.2558 0.2337 0.2266 0.0292  -0.0989 0.0268  71  ASP A OD1 
564  O  OD2 . ASP A 71  ? 0.3876 0.2973 0.3501 0.0888  -0.1573 0.0556  71  ASP A OD2 
565  N  N   . ASP A 72  ? 0.2472 0.1813 0.1040 -0.0256 -0.0165 -0.0055 72  ASP A N   
566  C  CA  . ASP A 72  ? 0.1946 0.1784 0.1072 0.0032  -0.0004 -0.0018 72  ASP A CA  
567  C  C   . ASP A 72  ? 0.2425 0.1580 0.1258 -0.0002 0.0053  0.0006  72  ASP A C   
568  O  O   . ASP A 72  ? 0.2861 0.1817 0.1133 0.0125  -0.0288 -0.0048 72  ASP A O   
569  C  CB  . ASP A 72  ? 0.2231 0.1759 0.1497 0.0464  0.0128  0.0455  72  ASP A CB  
570  C  CG  . ASP A 72  ? 0.2244 0.2050 0.1339 0.0122  -0.0168 0.0290  72  ASP A CG  
571  O  OD1 . ASP A 72  ? 0.2563 0.3165 0.1644 0.0220  0.0324  0.0832  72  ASP A OD1 
572  O  OD2 . ASP A 72  ? 0.2622 0.2646 0.0557 0.0272  -0.0158 0.0146  72  ASP A OD2 
573  N  N   . SER A 73  ? 0.2591 0.1745 0.1874 0.0456  0.0200  0.0441  73  SER A N   
574  C  CA  . SER A 73  ? 0.2575 0.1957 0.1364 -0.0106 0.0271  0.0150  73  SER A CA  
575  C  C   . SER A 73  ? 0.2957 0.1932 0.1454 0.0264  -0.0070 -0.0254 73  SER A C   
576  O  O   . SER A 73  ? 0.3068 0.2048 0.1860 0.0505  -0.0030 -0.0097 73  SER A O   
577  C  CB  . SER A 73  ? 0.2824 0.2823 0.1280 -0.0135 0.0049  0.0394  73  SER A CB  
578  O  OG  . SER A 73  ? 0.3367 0.2514 0.1959 0.0278  -0.0738 0.0497  73  SER A OG  
579  N  N   . GLN A 74  ? 0.3025 0.2427 0.2527 0.0172  0.0741  -0.0266 74  GLN A N   
580  C  CA  . GLN A 74  ? 0.2716 0.2530 0.3236 -0.0002 0.0806  0.0263  74  GLN A CA  
581  C  C   . GLN A 74  ? 0.2280 0.2873 0.1698 0.0059  0.0451  -0.0471 74  GLN A C   
582  O  O   . GLN A 74  ? 0.2210 0.2694 0.1902 -0.0135 0.0100  -0.0196 74  GLN A O   
583  C  CB  . GLN A 74  ? 0.2804 0.4210 0.3601 -0.0564 0.0823  0.0174  74  GLN A CB  
584  C  CG  . GLN A 74  ? 0.6167 0.4720 0.3161 -0.0716 0.0460  0.0282  74  GLN A CG  
585  C  CD  . GLN A 74  ? 0.3559 0.4275 0.3910 -0.1367 0.0282  0.0211  74  GLN A CD  
586  O  OE1 . GLN A 74  ? 0.2912 0.4647 0.5259 0.0471  -0.1193 0.0960  74  GLN A OE1 
587  N  NE2 . GLN A 74  ? 0.3788 0.4123 0.3620 -0.1192 0.0281  0.1134  74  GLN A NE2 
588  N  N   . ASP A 75  ? 0.2352 0.3647 0.2540 -0.0319 0.0651  -0.1323 75  ASP A N   
589  C  CA  . ASP A 75  ? 0.4128 0.3810 0.1709 -0.0511 -0.0164 -0.1062 75  ASP A CA  
590  C  C   . ASP A 75  ? 0.2759 0.4426 0.2488 -0.0154 -0.0258 -0.1204 75  ASP A C   
591  O  O   . ASP A 75  ? 0.2811 0.4894 0.4597 -0.0032 -0.0370 -0.1087 75  ASP A O   
592  C  CB  . ASP A 75  ? 0.4796 0.4014 0.2179 -0.0958 0.0894  -0.0864 75  ASP A CB  
593  C  CG  . ASP A 75  ? 0.8196 0.4892 0.3176 -0.1454 0.0446  0.0669  75  ASP A CG  
594  O  OD1 . ASP A 75  ? 0.3789 0.4509 0.4368 -0.0553 -0.1560 0.0098  75  ASP A OD1 
595  O  OD2 . ASP A 75  ? 0.6856 0.6419 0.4146 -0.1859 0.1847  -0.1180 75  ASP A OD2 
596  N  N   . LYS A 76  ? 0.2851 0.2970 0.2018 -0.0118 -0.1242 0.0516  76  LYS A N   
597  C  CA  . LYS A 76  ? 0.3066 0.3028 0.1921 -0.0013 -0.0061 -0.0067 76  LYS A CA  
598  C  C   . LYS A 76  ? 0.4458 0.3473 0.1493 0.0126  -0.1150 -0.0193 76  LYS A C   
599  O  O   . LYS A 76  ? 0.4863 0.4361 0.1093 0.0746  -0.0675 0.0514  76  LYS A O   
600  C  CB  . LYS A 76  ? 0.4729 0.2879 0.1949 -0.0196 -0.1726 -0.0042 76  LYS A CB  
601  C  CG  . LYS A 76  ? 0.7005 0.3512 0.2064 -0.0674 -0.1373 0.0318  76  LYS A CG  
602  C  CD  . LYS A 76  ? 0.5665 0.4008 0.1745 -0.0376 -0.1610 0.0219  76  LYS A CD  
603  C  CE  . LYS A 76  ? 0.5626 0.4720 0.3940 0.2127  -0.2699 0.0744  76  LYS A CE  
604  N  NZ  . LYS A 76  ? 0.6922 0.3479 0.1653 -0.0726 0.0055  0.0317  76  LYS A NZ  
605  N  N   . ALA A 77  ? 0.2634 0.3652 0.2291 0.0032  -0.0734 -0.0484 77  ALA A N   
606  C  CA  . ALA A 77  ? 0.2284 0.2893 0.0788 -0.0361 -0.0675 -0.0359 77  ALA A CA  
607  C  C   . ALA A 77  ? 0.1991 0.3065 0.0637 -0.0201 -0.0453 -0.0447 77  ALA A C   
608  O  O   . ALA A 77  ? 0.1867 0.4391 0.1776 0.0012  -0.0291 -0.0627 77  ALA A O   
609  C  CB  . ALA A 77  ? 0.2634 0.2938 0.1540 0.0119  -0.0257 -0.0094 77  ALA A CB  
610  N  N   . VAL A 78  ? 0.2121 0.3160 0.0326 -0.0408 -0.0403 -0.0122 78  VAL A N   
611  C  CA  . VAL A 78  ? 0.2727 0.2893 0.0475 -0.0519 -0.0697 -0.0058 78  VAL A CA  
612  C  C   . VAL A 78  ? 0.1890 0.2357 0.1019 -0.0431 -0.0344 -0.0274 78  VAL A C   
613  O  O   . VAL A 78  ? 0.1722 0.2962 0.0994 -0.0340 -0.0568 0.0340  78  VAL A O   
614  C  CB  . VAL A 78  ? 0.3677 0.2889 0.1734 -0.0222 -0.0179 0.0130  78  VAL A CB  
615  C  CG1 . VAL A 78  ? 0.4531 0.2249 0.2096 -0.0646 0.0219  -0.0121 78  VAL A CG1 
616  C  CG2 . VAL A 78  ? 0.3318 0.4494 0.2109 -0.0184 -0.0186 -0.0424 78  VAL A CG2 
617  N  N   . LEU A 79  ? 0.1811 0.2720 0.0700 -0.0035 -0.0087 0.0005  79  LEU A N   
618  C  CA  . LEU A 79  ? 0.2125 0.2452 0.1176 -0.0248 -0.0177 0.0001  79  LEU A CA  
619  C  C   . LEU A 79  ? 0.1959 0.2693 0.1265 -0.0248 -0.0135 -0.0100 79  LEU A C   
620  O  O   . LEU A 79  ? 0.2590 0.2977 0.0944 -0.0607 -0.0089 0.0289  79  LEU A O   
621  C  CB  . LEU A 79  ? 0.1714 0.2886 0.2042 -0.0168 -0.0241 0.0282  79  LEU A CB  
622  C  CG  . LEU A 79  ? 0.2373 0.2684 0.1932 0.0197  -0.0482 -0.0034 79  LEU A CG  
623  C  CD1 . LEU A 79  ? 0.2722 0.2750 0.2832 -0.0098 0.0505  0.0053  79  LEU A CD1 
624  C  CD2 . LEU A 79  ? 0.3030 0.3015 0.1686 0.0741  0.0662  0.0196  79  LEU A CD2 
625  N  N   . LYS A 80  ? 0.2132 0.3132 0.0311 -0.0494 -0.0713 0.0097  80  LYS A N   
626  C  CA  . LYS A 80  ? 0.3230 0.3154 0.0287 -0.0706 -0.0697 0.0047  80  LYS A CA  
627  C  C   . LYS A 80  ? 0.2070 0.2818 0.0331 -0.0359 -0.0598 -0.0043 80  LYS A C   
628  O  O   . LYS A 80  ? 0.2564 0.2751 0.0847 -0.0501 -0.0501 0.0280  80  LYS A O   
629  C  CB  . LYS A 80  ? 0.3048 0.3340 0.1641 -0.0380 -0.0418 -0.0753 80  LYS A CB  
630  C  CG  . LYS A 80  ? 0.2904 0.3565 0.2652 -0.0383 -0.0966 -0.0723 80  LYS A CG  
631  C  CD  . LYS A 80  ? 0.4746 0.3373 0.3810 0.0434  -0.1065 -0.0886 80  LYS A CD  
632  N  N   . GLY A 81  ? 0.2606 0.3353 0.0212 -0.0177 -0.0420 -0.0076 81  GLY A N   
633  C  CA  . GLY A 81  ? 0.2598 0.2618 0.1210 0.0053  -0.0175 0.0290  81  GLY A CA  
634  C  C   . GLY A 81  ? 0.2046 0.2447 0.1312 -0.0064 0.0222  -0.0067 81  GLY A C   
635  O  O   . GLY A 81  ? 0.2079 0.3006 0.0452 0.0000  -0.0020 -0.0200 81  GLY A O   
636  N  N   . GLY A 82  ? 0.2408 0.2431 0.2030 -0.0092 0.0074  0.0262  82  GLY A N   
637  C  CA  . GLY A 82  ? 0.2493 0.2433 0.1615 -0.0227 -0.0032 0.0157  82  GLY A CA  
638  C  C   . GLY A 82  ? 0.2171 0.2149 0.2151 0.0041  -0.0216 0.0087  82  GLY A C   
639  O  O   . GLY A 82  ? 0.2381 0.2832 0.1920 0.0166  -0.0343 0.0049  82  GLY A O   
640  N  N   . PRO A 83  ? 0.2246 0.2794 0.0872 -0.0082 0.0013  0.0051  83  PRO A N   
641  C  CA  . PRO A 83  ? 0.1946 0.2732 0.1827 -0.0144 -0.0284 0.0309  83  PRO A CA  
642  C  C   . PRO A 83  ? 0.2842 0.2685 0.0955 -0.0567 -0.0440 -0.0004 83  PRO A C   
643  O  O   . PRO A 83  ? 0.3265 0.3148 0.0731 -0.0467 -0.0903 -0.0046 83  PRO A O   
644  C  CB  . PRO A 83  ? 0.2511 0.2952 0.1000 0.0401  -0.0716 0.0333  83  PRO A CB  
645  C  CG  . PRO A 83  ? 0.2254 0.3573 0.0698 0.0458  -0.0138 0.0465  83  PRO A CG  
646  C  CD  . PRO A 83  ? 0.2038 0.2171 0.1910 0.0055  0.0460  0.0018  83  PRO A CD  
647  N  N   . LEU A 84  ? 0.3098 0.2705 0.0441 0.0316  0.0061  -0.0242 84  LEU A N   
648  C  CA  . LEU A 84  ? 0.2680 0.2581 0.0405 0.0023  -0.0239 -0.0359 84  LEU A CA  
649  C  C   . LEU A 84  ? 0.2657 0.2671 0.1048 0.0111  -0.0197 -0.0471 84  LEU A C   
650  O  O   . LEU A 84  ? 0.2658 0.2810 0.1601 0.0320  0.0208  -0.0339 84  LEU A O   
651  C  CB  . LEU A 84  ? 0.2035 0.2485 0.0443 0.0139  -0.0298 0.0004  84  LEU A CB  
652  C  CG  . LEU A 84  ? 0.2063 0.2595 0.0355 0.0185  -0.0505 -0.0009 84  LEU A CG  
653  C  CD1 . LEU A 84  ? 0.1960 0.3204 0.0598 0.0159  -0.0760 0.0021  84  LEU A CD1 
654  C  CD2 . LEU A 84  ? 0.1874 0.3051 0.0815 0.0384  -0.0647 -0.0153 84  LEU A CD2 
655  N  N   . ASP A 85  ? 0.3047 0.2544 0.0660 -0.0041 -0.0023 -0.0170 85  ASP A N   
656  C  CA  . ASP A 85  ? 0.3912 0.2347 0.0876 -0.0399 -0.0317 -0.0355 85  ASP A CA  
657  C  C   . ASP A 85  ? 0.3043 0.2273 0.1407 -0.0093 0.0299  0.0159  85  ASP A C   
658  O  O   . ASP A 85  ? 0.3053 0.4112 0.1066 0.0419  -0.0144 -0.0050 85  ASP A O   
659  C  CB  . ASP A 85  ? 0.4121 0.3150 0.1043 -0.0868 -0.0049 -0.0883 85  ASP A CB  
660  C  CG  . ASP A 85  ? 0.3218 0.3819 0.1948 -0.0190 -0.0758 -0.0241 85  ASP A CG  
661  O  OD1 . ASP A 85  ? 0.3922 0.4640 0.1941 -0.0309 0.0110  -0.1054 85  ASP A OD1 
662  O  OD2 . ASP A 85  ? 0.3574 0.5295 0.1439 0.0744  -0.0990 -0.0593 85  ASP A OD2 
663  N  N   . GLY A 86  ? 0.2938 0.3173 0.1601 -0.0245 -0.0506 0.0234  86  GLY A N   
664  C  CA  . GLY A 86  ? 0.3686 0.3021 0.1030 0.0199  -0.0345 -0.0238 86  GLY A CA  
665  C  C   . GLY A 86  ? 0.2540 0.3191 0.1195 -0.0468 0.0031  -0.0244 86  GLY A C   
666  O  O   . GLY A 86  ? 0.3666 0.3464 0.1097 -0.0680 -0.0352 -0.0060 86  GLY A O   
667  N  N   . THR A 87  ? 0.2193 0.2821 0.0926 -0.0321 0.0111  -0.0414 87  THR A N   
668  C  CA  . THR A 87  ? 0.1899 0.2663 0.0900 0.0313  -0.0231 -0.0275 87  THR A CA  
669  C  C   . THR A 87  ? 0.1910 0.2064 0.1377 -0.0035 0.0129  -0.0175 87  THR A C   
670  O  O   . THR A 87  ? 0.2025 0.2117 0.1235 -0.0067 -0.0063 -0.0342 87  THR A O   
671  C  CB  . THR A 87  ? 0.1939 0.4383 0.0818 0.1363  -0.0576 -0.0451 87  THR A CB  
672  O  OG1 . THR A 87  ? 0.2781 0.5219 0.2200 0.1161  -0.0100 -0.0789 87  THR A OG1 
673  C  CG2 . THR A 87  ? 0.3929 0.4789 0.1260 0.0535  -0.1116 -0.0510 87  THR A CG2 
674  N  N   . TYR A 88  ? 0.1579 0.2377 0.0593 0.0070  -0.0323 -0.0274 88  TYR A N   
675  C  CA  . TYR A 88  ? 0.1637 0.2363 0.0826 0.0179  -0.0278 -0.0441 88  TYR A CA  
676  C  C   . TYR A 88  ? 0.1802 0.2325 0.0838 -0.0152 -0.0413 -0.0129 88  TYR A C   
677  O  O   . TYR A 88  ? 0.2247 0.2936 0.0835 -0.0499 -0.0074 0.0086  88  TYR A O   
678  C  CB  . TYR A 88  ? 0.1869 0.2172 0.0682 0.0071  -0.0081 -0.0275 88  TYR A CB  
679  C  CG  . TYR A 88  ? 0.1985 0.2095 0.0560 0.0206  -0.0072 -0.0115 88  TYR A CG  
680  C  CD1 . TYR A 88  ? 0.1964 0.2009 0.0442 0.0117  -0.0266 -0.0203 88  TYR A CD1 
681  C  CD2 . TYR A 88  ? 0.1675 0.2201 0.0468 -0.0015 -0.0336 -0.0172 88  TYR A CD2 
682  C  CE1 . TYR A 88  ? 0.2030 0.2312 0.0994 -0.0150 -0.0669 0.0063  88  TYR A CE1 
683  C  CE2 . TYR A 88  ? 0.1723 0.2300 0.0700 0.0080  -0.0513 -0.0170 88  TYR A CE2 
684  C  CZ  . TYR A 88  ? 0.2036 0.2020 0.0586 0.0038  -0.0300 0.0005  88  TYR A CZ  
685  O  OH  . TYR A 88  ? 0.2469 0.3355 0.0399 -0.0072 -0.0286 -0.0044 88  TYR A OH  
686  N  N   . ARG A 89  ? 0.1716 0.2528 0.0603 0.0144  -0.0443 -0.0206 89  ARG A N   
687  C  CA  . ARG A 89  ? 0.1671 0.2452 0.0586 0.0212  -0.0374 -0.0436 89  ARG A CA  
688  C  C   . ARG A 89  ? 0.1513 0.1719 0.0967 0.0010  -0.0175 -0.0046 89  ARG A C   
689  O  O   . ARG A 89  ? 0.1436 0.2084 0.0724 0.0110  -0.0214 -0.0114 89  ARG A O   
690  C  CB  . ARG A 89  ? 0.3047 0.2358 0.1307 -0.0018 -0.0986 -0.0516 89  ARG A CB  
691  C  CG  . ARG A 89  ? 0.2886 0.2664 0.0694 -0.0653 -0.0417 0.0012  89  ARG A CG  
692  C  CD  . ARG A 89  ? 0.2942 0.2395 0.1421 -0.0381 0.0336  0.0055  89  ARG A CD  
693  N  NE  . ARG A 89  ? 0.3302 0.3169 0.1334 0.0046  0.0150  -0.0303 89  ARG A NE  
694  C  CZ  . ARG A 89  ? 0.2064 0.3112 0.1738 0.0079  0.0002  0.0175  89  ARG A CZ  
695  N  NH1 . ARG A 89  ? 0.3071 0.3156 0.0933 -0.0040 -0.0368 0.0591  89  ARG A NH1 
696  N  NH2 . ARG A 89  ? 0.2766 0.3499 0.1429 0.0008  -0.0049 -0.0094 89  ARG A NH2 
697  N  N   . LEU A 90  ? 0.2043 0.2178 0.0452 0.0040  -0.0558 -0.0137 90  LEU A N   
698  C  CA  . LEU A 90  ? 0.1862 0.1908 0.0951 -0.0103 -0.0031 0.0032  90  LEU A CA  
699  C  C   . LEU A 90  ? 0.1944 0.1841 0.1041 0.0148  0.0004  0.0064  90  LEU A C   
700  O  O   . LEU A 90  ? 0.1870 0.2365 0.0917 0.0118  0.0096  0.0387  90  LEU A O   
701  C  CB  . LEU A 90  ? 0.1928 0.1824 0.0723 0.0085  -0.0271 0.0098  90  LEU A CB  
702  C  CG  . LEU A 90  ? 0.1878 0.2082 0.0736 0.0027  -0.0195 -0.0099 90  LEU A CG  
703  C  CD1 . LEU A 90  ? 0.1899 0.1996 0.1047 0.0283  -0.0226 -0.0249 90  LEU A CD1 
704  C  CD2 . LEU A 90  ? 0.2504 0.2315 0.0782 -0.0381 -0.0370 -0.0185 90  LEU A CD2 
705  N  N   . THR A 91  ? 0.1867 0.1903 0.0270 0.0138  0.0053  -0.0049 91  THR A N   
706  C  CA  . THR A 91  ? 0.1608 0.1856 0.0531 0.0197  0.0046  0.0139  91  THR A CA  
707  C  C   . THR A 91  ? 0.1967 0.1779 0.0233 0.0018  -0.0289 0.0099  91  THR A C   
708  O  O   . THR A 91  ? 0.1783 0.2034 0.0224 -0.0023 -0.0490 0.0207  91  THR A O   
709  C  CB  . THR A 91  ? 0.1849 0.2024 0.1059 -0.0315 0.0111  0.0139  91  THR A CB  
710  O  OG1 . THR A 91  ? 0.2226 0.2705 0.0847 -0.0515 -0.0086 0.0243  91  THR A OG1 
711  C  CG2 . THR A 91  ? 0.2366 0.2054 0.1037 -0.0050 -0.0233 -0.0115 91  THR A CG2 
712  N  N   . GLN A 92  ? 0.1596 0.1835 0.0227 0.0173  -0.0356 -0.0048 92  GLN A N   
713  C  CA  . GLN A 92  ? 0.1600 0.1636 0.0679 0.0062  -0.0223 -0.0148 92  GLN A CA  
714  C  C   . GLN A 92  ? 0.1648 0.1567 0.0372 0.0190  -0.0061 -0.0050 92  GLN A C   
715  O  O   . GLN A 92  ? 0.1982 0.2104 0.0310 0.0209  -0.0336 -0.0122 92  GLN A O   
716  C  CB  . GLN A 92  ? 0.1508 0.2080 0.0204 0.0277  -0.0442 0.0018  92  GLN A CB  
717  C  CG  . GLN A 92  ? 0.1905 0.2424 0.0680 0.0063  -0.0952 -0.0167 92  GLN A CG  
718  C  CD  . GLN A 92  ? 0.2011 0.2520 0.0459 -0.0073 -0.0549 0.0042  92  GLN A CD  
719  O  OE1 . GLN A 92  ? 0.2326 0.2168 0.1278 0.0252  -0.0773 0.0055  92  GLN A OE1 
720  N  NE2 . GLN A 92  ? 0.1715 0.3430 0.1483 0.0089  -0.0088 0.0086  92  GLN A NE2 
721  N  N   . PHE A 93  ? 0.1493 0.1641 0.0501 0.0100  -0.0190 -0.0068 93  PHE A N   
722  C  CA  . PHE A 93  ? 0.1411 0.1565 0.1007 0.0183  -0.0182 -0.0105 93  PHE A CA  
723  C  C   . PHE A 93  ? 0.1359 0.1565 0.0475 0.0027  0.0050  0.0227  93  PHE A C   
724  O  O   . PHE A 93  ? 0.1587 0.1910 0.0261 0.0143  -0.0102 0.0046  93  PHE A O   
725  C  CB  . PHE A 93  ? 0.1366 0.1956 0.0450 0.0005  -0.0653 -0.0111 93  PHE A CB  
726  C  CG  . PHE A 93  ? 0.1667 0.1794 0.0306 0.0153  -0.0611 0.0069  93  PHE A CG  
727  C  CD1 . PHE A 93  ? 0.1503 0.2023 0.0212 -0.0134 -0.0255 -0.0006 93  PHE A CD1 
728  C  CD2 . PHE A 93  ? 0.1353 0.2011 0.0434 0.0176  -0.0489 -0.0001 93  PHE A CD2 
729  C  CE1 . PHE A 93  ? 0.1579 0.2002 0.0371 0.0013  -0.0494 0.0087  93  PHE A CE1 
730  C  CE2 . PHE A 93  ? 0.1655 0.2074 0.0497 -0.0001 -0.0646 0.0125  93  PHE A CE2 
731  C  CZ  . PHE A 93  ? 0.1449 0.2049 0.0698 -0.0008 -0.0257 0.0165  93  PHE A CZ  
732  N  N   . HIS A 94  ? 0.1637 0.1715 0.0507 0.0145  -0.0378 0.0151  94  HIS A N   
733  C  CA  . HIS A 94  ? 0.1369 0.1770 0.0299 0.0068  -0.0554 -0.0032 94  HIS A CA  
734  C  C   . HIS A 94  ? 0.1091 0.1960 0.0463 0.0067  -0.0282 0.0098  94  HIS A C   
735  O  O   . HIS A 94  ? 0.1819 0.1758 0.0442 0.0160  0.0107  0.0032  94  HIS A O   
736  C  CB  . HIS A 94  ? 0.1486 0.1867 0.0597 -0.0348 -0.0403 -0.0282 94  HIS A CB  
737  C  CG  . HIS A 94  ? 0.1770 0.2115 0.0414 0.0046  -0.0233 -0.0316 94  HIS A CG  
738  N  ND1 . HIS A 94  ? 0.1429 0.1787 0.0519 0.0237  -0.0787 -0.0073 94  HIS A ND1 
739  C  CD2 . HIS A 94  ? 0.2123 0.2838 0.0359 -0.0374 -0.0733 -0.0171 94  HIS A CD2 
740  C  CE1 . HIS A 94  ? 0.1732 0.3308 0.0311 -0.0237 -0.0621 -0.0141 94  HIS A CE1 
741  N  NE2 . HIS A 94  ? 0.2135 0.3843 0.1054 -0.0068 -0.1280 -0.0823 94  HIS A NE2 
742  N  N   . PHE A 95  ? 0.1463 0.1835 0.0602 0.0307  -0.0864 -0.0104 95  PHE A N   
743  C  CA  . PHE A 95  ? 0.1267 0.1766 0.0459 0.0094  -0.0195 -0.0162 95  PHE A CA  
744  C  C   . PHE A 95  ? 0.1525 0.1551 0.0643 0.0307  -0.0304 -0.0177 95  PHE A C   
745  O  O   . PHE A 95  ? 0.1465 0.2199 0.0524 0.0126  -0.0511 -0.0001 95  PHE A O   
746  C  CB  . PHE A 95  ? 0.1319 0.2045 0.0770 0.0250  -0.0412 -0.0496 95  PHE A CB  
747  C  CG  . PHE A 95  ? 0.1233 0.1830 0.0625 0.0046  -0.0386 -0.0013 95  PHE A CG  
748  C  CD1 . PHE A 95  ? 0.1680 0.1648 0.0985 0.0154  -0.0793 -0.0193 95  PHE A CD1 
749  C  CD2 . PHE A 95  ? 0.1210 0.2122 0.0603 -0.0055 -0.0274 -0.0249 95  PHE A CD2 
750  C  CE1 . PHE A 95  ? 0.1535 0.2106 0.1120 0.0011  -0.0714 -0.0348 95  PHE A CE1 
751  C  CE2 . PHE A 95  ? 0.1226 0.2025 0.0973 -0.0031 -0.0347 -0.0168 95  PHE A CE2 
752  C  CZ  . PHE A 95  ? 0.1691 0.2179 0.1034 0.0147  -0.0563 -0.0220 95  PHE A CZ  
753  N  N   . HIS A 96  ? 0.1637 0.1599 0.1043 0.0066  -0.0401 0.0165  96  HIS A N   
754  C  CA  . HIS A 96  ? 0.1696 0.1847 0.0403 0.0164  -0.0738 -0.0171 96  HIS A CA  
755  C  C   . HIS A 96  ? 0.1338 0.1830 0.0329 0.0189  -0.0442 0.0146  96  HIS A C   
756  O  O   . HIS A 96  ? 0.1341 0.1902 0.0724 -0.0002 -0.0131 0.0156  96  HIS A O   
757  C  CB  . HIS A 96  ? 0.1697 0.1892 0.0303 0.0124  -0.0529 -0.0395 96  HIS A CB  
758  C  CG  . HIS A 96  ? 0.1404 0.1849 0.0585 -0.0129 -0.0528 0.0076  96  HIS A CG  
759  N  ND1 . HIS A 96  ? 0.1321 0.1773 0.0716 -0.0017 -0.0452 0.0095  96  HIS A ND1 
760  C  CD2 . HIS A 96  ? 0.2185 0.2020 0.0400 0.0086  -0.0361 -0.0099 96  HIS A CD2 
761  C  CE1 . HIS A 96  ? 0.1445 0.1859 0.0819 0.0040  -0.0710 0.0050  96  HIS A CE1 
762  N  NE2 . HIS A 96  ? 0.1788 0.2011 0.0666 0.0232  -0.0268 0.0034  96  HIS A NE2 
763  N  N   . TRP A 97  ? 0.1321 0.1518 0.0752 0.0250  -0.0439 0.0043  97  TRP A N   
764  C  CA  . TRP A 97  ? 0.1571 0.1637 0.0302 0.0253  -0.0532 -0.0030 97  TRP A CA  
765  C  C   . TRP A 97  ? 0.1353 0.1619 0.0454 0.0097  -0.0335 0.0129  97  TRP A C   
766  O  O   . TRP A 97  ? 0.1283 0.1833 0.0811 0.0070  -0.0438 0.0172  97  TRP A O   
767  C  CB  . TRP A 97  ? 0.1728 0.1990 0.0223 -0.0009 -0.0512 0.0059  97  TRP A CB  
768  C  CG  . TRP A 97  ? 0.1465 0.1781 0.0516 -0.0027 -0.0364 -0.0183 97  TRP A CG  
769  C  CD1 . TRP A 97  ? 0.1543 0.2054 0.0244 0.0165  -0.0511 -0.0078 97  TRP A CD1 
770  C  CD2 . TRP A 97  ? 0.1453 0.1928 0.0382 0.0031  -0.0665 -0.0025 97  TRP A CD2 
771  N  NE1 . TRP A 97  ? 0.2239 0.1860 0.0567 0.0146  -0.0613 0.0316  97  TRP A NE1 
772  C  CE2 . TRP A 97  ? 0.1600 0.1852 0.0397 0.0033  -0.0525 -0.0061 97  TRP A CE2 
773  C  CE3 . TRP A 97  ? 0.1508 0.1964 0.0734 0.0103  -0.0717 -0.0077 97  TRP A CE3 
774  C  CZ2 . TRP A 97  ? 0.2430 0.2082 0.0461 0.0038  -0.0971 -0.0032 97  TRP A CZ2 
775  C  CZ3 . TRP A 97  ? 0.1921 0.2011 0.0689 0.0268  -0.0424 0.0030  97  TRP A CZ3 
776  C  CH2 . TRP A 97  ? 0.1866 0.2188 0.0478 0.0163  -0.0632 -0.0082 97  TRP A CH2 
777  N  N   . GLY A 98  ? 0.1691 0.1615 0.0603 0.0054  -0.0427 -0.0055 98  GLY A N   
778  C  CA  . GLY A 98  ? 0.1819 0.1683 0.0562 0.0290  0.0168  -0.0038 98  GLY A CA  
779  C  C   . GLY A 98  ? 0.1758 0.2016 0.0627 0.0486  -0.0189 -0.0251 98  GLY A C   
780  O  O   . GLY A 98  ? 0.1786 0.2124 0.0763 0.0226  -0.0304 -0.0033 98  GLY A O   
781  N  N   . SER A 99  ? 0.1425 0.1806 0.1043 0.0066  -0.0037 -0.0361 99  SER A N   
782  C  CA  . SER A 99  ? 0.1714 0.1862 0.1395 0.0204  0.0236  -0.0526 99  SER A CA  
783  C  C   . SER A 99  ? 0.1737 0.2220 0.1127 -0.0166 -0.0055 -0.0373 99  SER A C   
784  O  O   . SER A 99  ? 0.2322 0.1895 0.1406 -0.0096 0.0238  -0.0414 99  SER A O   
785  C  CB  . SER A 99  ? 0.1612 0.2821 0.1464 0.0335  -0.0525 0.0309  99  SER A CB  
786  O  OG  . SER A 99  ? 0.1985 0.2371 0.1151 0.0135  -0.0292 0.0181  99  SER A OG  
787  N  N   . LEU A 100 ? 0.1610 0.1802 0.0980 -0.0017 -0.0210 0.0186  100 LEU A N   
788  C  CA  . LEU A 100 ? 0.2205 0.2107 0.1163 -0.0279 0.0409  0.0018  100 LEU A CA  
789  C  C   . LEU A 100 ? 0.2550 0.1975 0.1360 -0.0119 0.0427  -0.0185 100 LEU A C   
790  O  O   . LEU A 100 ? 0.2132 0.1963 0.1952 -0.0256 0.0273  -0.0296 100 LEU A O   
791  C  CB  . LEU A 100 ? 0.3471 0.1912 0.0919 -0.0130 0.0065  0.0049  100 LEU A CB  
792  C  CG  . LEU A 100 ? 0.4499 0.2586 0.0247 0.0949  -0.0151 0.0012  100 LEU A CG  
793  C  CD1 . LEU A 100 ? 0.3215 0.4550 0.2377 -0.0238 0.1046  0.0675  100 LEU A CD1 
794  C  CD2 . LEU A 100 ? 0.4069 0.4481 0.1262 0.0066  0.0934  -0.0207 100 LEU A CD2 
795  N  N   . ASP A 101 ? 0.2508 0.2175 0.1809 -0.0372 0.0728  -0.0577 101 ASP A N   
796  C  CA  . ASP A 101 ? 0.2029 0.2188 0.1772 -0.0398 0.0242  -0.0582 101 ASP A CA  
797  C  C   . ASP A 101 ? 0.2028 0.2370 0.2032 -0.0350 -0.0321 -0.0092 101 ASP A C   
798  O  O   . ASP A 101 ? 0.2794 0.2706 0.1849 0.0221  -0.0305 -0.0012 101 ASP A O   
799  C  CB  . ASP A 101 ? 0.1786 0.3154 0.1783 -0.0666 -0.0187 -0.0229 101 ASP A CB  
800  C  CG  . ASP A 101 ? 0.2828 0.2866 0.1985 -0.0684 -0.0467 -0.0668 101 ASP A CG  
801  O  OD1 . ASP A 101 ? 0.3016 0.2868 0.3003 -0.0403 0.0532  -0.0502 101 ASP A OD1 
802  O  OD2 . ASP A 101 ? 0.3309 0.4220 0.3281 -0.1722 -0.0027 -0.1037 101 ASP A OD2 
803  N  N   . GLY A 102 ? 0.2086 0.2304 0.2373 -0.0126 0.0388  0.0206  102 GLY A N   
804  C  CA  . GLY A 102 ? 0.2771 0.2027 0.2222 -0.0330 0.0110  0.0450  102 GLY A CA  
805  C  C   . GLY A 102 ? 0.2863 0.1805 0.2104 -0.0208 -0.0095 0.0234  102 GLY A C   
806  O  O   . GLY A 102 ? 0.2472 0.2404 0.2146 -0.0011 -0.0194 0.0284  102 GLY A O   
807  N  N   . GLN A 103 ? 0.2038 0.1773 0.1704 -0.0093 -0.0069 0.0044  103 GLN A N   
808  C  CA  . GLN A 103 ? 0.1883 0.1694 0.1452 0.0038  -0.0012 0.0175  103 GLN A CA  
809  C  C   . GLN A 103 ? 0.2244 0.1743 0.0993 0.0170  -0.0226 -0.0003 103 GLN A C   
810  O  O   . GLN A 103 ? 0.1971 0.1975 0.1206 -0.0128 -0.0326 -0.0229 103 GLN A O   
811  C  CB  . GLN A 103 ? 0.1747 0.2032 0.1025 0.0083  0.0000  -0.0054 103 GLN A CB  
812  C  CG  . GLN A 103 ? 0.1700 0.2279 0.0874 0.0247  -0.0165 -0.0230 103 GLN A CG  
813  C  CD  . GLN A 103 ? 0.1858 0.2153 0.1188 0.0509  0.0006  -0.0133 103 GLN A CD  
814  O  OE1 . GLN A 103 ? 0.1916 0.2929 0.2024 0.0381  0.0370  0.0232  103 GLN A OE1 
815  N  NE2 . GLN A 103 ? 0.1928 0.2531 0.1779 0.0568  -0.0182 0.0435  103 GLN A NE2 
816  N  N   . GLY A 104 ? 0.1619 0.1895 0.0768 -0.0121 0.0272  0.0134  104 GLY A N   
817  C  CA  . GLY A 104 ? 0.1894 0.1817 0.0777 -0.0031 -0.0324 -0.0032 104 GLY A CA  
818  C  C   . GLY A 104 ? 0.1404 0.1766 0.0845 -0.0220 -0.0422 -0.0107 104 GLY A C   
819  O  O   . GLY A 104 ? 0.1730 0.1908 0.0754 0.0034  -0.0508 0.0131  104 GLY A O   
820  N  N   . SER A 105 ? 0.1454 0.1969 0.0598 0.0260  -0.0288 -0.0060 105 SER A N   
821  C  CA  . SER A 105 ? 0.1698 0.2057 0.0527 -0.0103 -0.0299 -0.0307 105 SER A CA  
822  C  C   . SER A 105 ? 0.1603 0.1617 0.0486 0.0003  -0.0292 0.0069  105 SER A C   
823  O  O   . SER A 105 ? 0.2182 0.1786 0.0533 0.0359  -0.0290 -0.0096 105 SER A O   
824  C  CB  . SER A 105 ? 0.1671 0.2369 0.0222 0.0351  -0.0212 0.0168  105 SER A CB  
825  O  OG  . SER A 105 ? 0.1745 0.1948 0.0688 -0.0053 -0.0385 0.0192  105 SER A OG  
826  N  N   . GLU A 106 ? 0.1382 0.1666 0.0646 -0.0154 -0.0318 -0.0122 106 GLU A N   
827  C  CA  . GLU A 106 ? 0.1873 0.1868 0.0141 -0.0318 -0.0332 -0.0110 106 GLU A CA  
828  C  C   . GLU A 106 ? 0.1661 0.2056 0.0250 0.0038  -0.0544 0.0043  106 GLU A C   
829  O  O   . GLU A 106 ? 0.1393 0.2452 0.0716 0.0060  -0.0750 0.0238  106 GLU A O   
830  C  CB  . GLU A 106 ? 0.1894 0.1903 0.0188 -0.0270 -0.0378 -0.0018 106 GLU A CB  
831  C  CG  . GLU A 106 ? 0.1729 0.1865 0.0423 0.0002  -0.0044 0.0251  106 GLU A CG  
832  C  CD  . GLU A 106 ? 0.1792 0.2102 0.0170 -0.0146 -0.0403 -0.0126 106 GLU A CD  
833  O  OE1 . GLU A 106 ? 0.1639 0.2228 0.0464 0.0170  -0.0641 0.0094  106 GLU A OE1 
834  O  OE2 . GLU A 106 ? 0.1529 0.2778 0.0809 -0.0115 -0.0364 0.0118  106 GLU A OE2 
835  N  N   . HIS A 107 ? 0.1923 0.1862 0.0600 -0.0225 -0.0003 0.0240  107 HIS A N   
836  C  CA  . HIS A 107 ? 0.1732 0.1842 0.0362 -0.0141 -0.0374 0.0243  107 HIS A CA  
837  C  C   . HIS A 107 ? 0.2054 0.1691 0.0584 -0.0106 -0.0287 0.0149  107 HIS A C   
838  O  O   . HIS A 107 ? 0.1718 0.2030 0.0883 -0.0135 -0.0444 -0.0059 107 HIS A O   
839  C  CB  . HIS A 107 ? 0.2318 0.1691 0.0516 -0.0124 -0.0106 -0.0181 107 HIS A CB  
840  C  CG  . HIS A 107 ? 0.1698 0.1669 0.0709 -0.0281 -0.0535 0.0035  107 HIS A CG  
841  N  ND1 . HIS A 107 ? 0.1838 0.1769 0.0770 0.0010  -0.0230 0.0171  107 HIS A ND1 
842  C  CD2 . HIS A 107 ? 0.1594 0.1901 0.0953 -0.0212 -0.0469 -0.0386 107 HIS A CD2 
843  C  CE1 . HIS A 107 ? 0.1628 0.1748 0.0566 -0.0023 -0.0811 0.0384  107 HIS A CE1 
844  N  NE2 . HIS A 107 ? 0.1483 0.2086 0.0355 0.0026  -0.0642 -0.0078 107 HIS A NE2 
845  N  N   . THR A 108 ? 0.2085 0.1928 0.0820 -0.0095 -0.0341 0.0478  108 THR A N   
846  C  CA  . THR A 108 ? 0.1898 0.2116 0.0553 -0.0170 -0.0094 0.0183  108 THR A CA  
847  C  C   . THR A 108 ? 0.1756 0.1892 0.0695 0.0019  -0.0100 0.0328  108 THR A C   
848  O  O   . THR A 108 ? 0.1898 0.1984 0.1091 0.0040  -0.0300 -0.0086 108 THR A O   
849  C  CB  . THR A 108 ? 0.1939 0.2250 0.0137 0.0001  -0.0374 -0.0001 108 THR A CB  
850  O  OG1 . THR A 108 ? 0.2236 0.2359 0.0571 -0.0172 -0.0794 0.0070  108 THR A OG1 
851  C  CG2 . THR A 108 ? 0.1824 0.2416 0.0309 -0.0127 -0.0189 0.0154  108 THR A CG2 
852  N  N   . VAL A 109 ? 0.2111 0.2063 0.0632 -0.0225 -0.0027 0.0447  109 VAL A N   
853  C  CA  . VAL A 109 ? 0.1775 0.2221 0.0812 0.0008  -0.0043 0.0220  109 VAL A CA  
854  C  C   . VAL A 109 ? 0.1975 0.2056 0.1147 0.0301  -0.0142 0.0096  109 VAL A C   
855  O  O   . VAL A 109 ? 0.2085 0.2231 0.1373 -0.0008 -0.0166 0.0321  109 VAL A O   
856  C  CB  . VAL A 109 ? 0.1546 0.2442 0.1493 -0.0012 0.0019  0.0391  109 VAL A CB  
857  C  CG1 . VAL A 109 ? 0.2233 0.2727 0.1288 0.0343  0.0259  0.0494  109 VAL A CG1 
858  C  CG2 . VAL A 109 ? 0.2732 0.2569 0.0840 -0.0297 -0.0583 0.0341  109 VAL A CG2 
859  N  N   . ASP A 110 ? 0.2275 0.2671 0.0795 0.0285  0.0126  0.0486  110 ASP A N   
860  C  CA  . ASP A 110 ? 0.2147 0.2502 0.1205 0.0075  0.0107  0.0477  110 ASP A CA  
861  C  C   . ASP A 110 ? 0.2794 0.2165 0.0833 0.0040  -0.0217 0.0305  110 ASP A C   
862  O  O   . ASP A 110 ? 0.2696 0.2201 0.1023 0.0037  -0.0017 0.0465  110 ASP A O   
863  C  CB  . ASP A 110 ? 0.2271 0.3323 0.0661 -0.0245 -0.0013 0.0509  110 ASP A CB  
864  C  CG  . ASP A 110 ? 0.2692 0.2964 0.1565 -0.0334 0.0408  0.0491  110 ASP A CG  
865  O  OD1 . ASP A 110 ? 0.2919 0.2701 0.1780 -0.0195 -0.0024 0.0420  110 ASP A OD1 
866  O  OD2 . ASP A 110 ? 0.2611 0.3588 0.1357 -0.0165 0.0192  0.0249  110 ASP A OD2 
867  N  N   . LYS A 111 ? 0.2134 0.2390 0.0698 -0.0091 -0.0555 0.0207  111 LYS A N   
868  C  CA  . LYS A 111 ? 0.2176 0.2390 0.0798 0.0172  -0.0532 0.0460  111 LYS A CA  
869  C  C   . LYS A 111 ? 0.1833 0.2215 0.0855 0.0129  -0.0418 0.0281  111 LYS A C   
870  O  O   . LYS A 111 ? 0.2002 0.2584 0.1400 0.0232  0.0027  0.0109  111 LYS A O   
871  C  CB  . LYS A 111 ? 0.2542 0.3245 0.1137 0.1002  -0.0499 0.0518  111 LYS A CB  
872  C  CG  . LYS A 111 ? 0.2540 0.3429 0.0969 0.0183  -0.0289 0.0641  111 LYS A CG  
873  C  CD  . LYS A 111 ? 0.2476 0.4265 0.1793 -0.0275 -0.0890 0.0302  111 LYS A CD  
874  N  N   . LYS A 112 ? 0.1829 0.2131 0.0957 0.0015  -0.0095 0.0137  112 LYS A N   
875  C  CA  . LYS A 112 ? 0.2311 0.2145 0.1003 0.0157  -0.0322 0.0109  112 LYS A CA  
876  C  C   . LYS A 112 ? 0.1597 0.1930 0.0968 0.0178  -0.0576 0.0024  112 LYS A C   
877  O  O   . LYS A 112 ? 0.2031 0.2062 0.1156 0.0127  -0.0469 -0.0071 112 LYS A O   
878  C  CB  . LYS A 112 ? 0.2495 0.2586 0.1014 -0.0176 -0.0210 -0.0001 112 LYS A CB  
879  C  CG  . LYS A 112 ? 0.3271 0.3964 0.1632 -0.0111 -0.0574 -0.1097 112 LYS A CG  
880  C  CD  . LYS A 112 ? 0.3373 0.4034 0.1999 -0.0141 0.0076  -0.0703 112 LYS A CD  
881  C  CE  . LYS A 112 ? 0.5657 0.3906 0.1362 0.0631  0.0111  -0.0886 112 LYS A CE  
882  N  NZ  . LYS A 112 ? 0.5771 0.5622 0.3887 0.0348  0.1656  -0.0468 112 LYS A NZ  
883  N  N   A LYS A 113 ? 0.2082 0.2384 0.0801 0.0125  -0.0445 0.0092  113 LYS A N   
884  N  N   B LYS A 113 ? 0.2154 0.2422 0.0851 0.0110  -0.0368 0.0082  113 LYS A N   
885  C  CA  A LYS A 113 ? 0.1917 0.2459 0.1147 -0.0027 -0.0517 0.0344  113 LYS A CA  
886  C  CA  B LYS A 113 ? 0.1806 0.2516 0.1199 -0.0022 -0.0442 0.0346  113 LYS A CA  
887  C  C   A LYS A 113 ? 0.1852 0.1885 0.0716 -0.0066 -0.0188 0.0006  113 LYS A C   
888  C  C   B LYS A 113 ? 0.1865 0.1945 0.0524 -0.0064 -0.0081 0.0066  113 LYS A C   
889  O  O   A LYS A 113 ? 0.3173 0.1675 0.1678 0.0173  -0.0842 0.0211  113 LYS A O   
890  O  O   B LYS A 113 ? 0.3186 0.1806 0.1342 0.0157  -0.0754 0.0256  113 LYS A O   
891  C  CB  A LYS A 113 ? 0.1905 0.2601 0.0700 0.0011  -0.0551 0.0053  113 LYS A CB  
892  C  CB  B LYS A 113 ? 0.1808 0.2682 0.0847 0.0017  -0.0434 0.0058  113 LYS A CB  
893  C  CG  A LYS A 113 ? 0.2007 0.2722 0.0706 -0.0155 -0.0607 0.0159  113 LYS A CG  
894  C  CG  B LYS A 113 ? 0.1399 0.2897 0.1307 -0.0168 -0.0307 0.0047  113 LYS A CG  
895  C  CD  A LYS A 113 ? 0.1641 0.2692 0.0883 -0.0106 -0.0664 0.0194  113 LYS A CD  
896  C  CD  B LYS A 113 ? 0.1186 0.2611 0.1456 0.0102  -0.0423 0.0366  113 LYS A CD  
897  C  CE  A LYS A 113 ? 0.1802 0.2515 0.1414 -0.0172 -0.0853 0.0269  113 LYS A CE  
898  C  CE  B LYS A 113 ? 0.1000 0.3202 0.2179 0.0060  -0.0450 0.0217  113 LYS A CE  
899  N  NZ  A LYS A 113 ? 0.2442 0.2372 0.1648 0.0568  -0.0609 0.0601  113 LYS A NZ  
900  N  NZ  B LYS A 113 ? 0.1084 0.3150 0.2547 -0.0006 -0.0159 -0.0042 113 LYS A NZ  
901  N  N   . TYR A 114 ? 0.1795 0.1759 0.0973 -0.0159 -0.0351 0.0044  114 TYR A N   
902  C  CA  . TYR A 114 ? 0.1314 0.1671 0.1029 -0.0104 -0.0186 0.0063  114 TYR A CA  
903  C  C   . TYR A 114 ? 0.1709 0.1913 0.1016 -0.0127 -0.0150 -0.0136 114 TYR A C   
904  O  O   . TYR A 114 ? 0.1750 0.2163 0.1181 0.0009  -0.0495 0.0096  114 TYR A O   
905  C  CB  . TYR A 114 ? 0.1418 0.1935 0.0809 -0.0095 -0.0136 0.0082  114 TYR A CB  
906  C  CG  . TYR A 114 ? 0.1655 0.1705 0.0651 -0.0138 -0.0145 0.0099  114 TYR A CG  
907  C  CD1 . TYR A 114 ? 0.2462 0.2642 0.0702 0.0029  -0.0471 0.0087  114 TYR A CD1 
908  C  CD2 . TYR A 114 ? 0.1763 0.2187 0.1567 -0.0519 -0.0093 0.0506  114 TYR A CD2 
909  C  CE1 . TYR A 114 ? 0.2305 0.2637 0.1150 0.0603  -0.0044 0.0322  114 TYR A CE1 
910  C  CE2 . TYR A 114 ? 0.2468 0.2569 0.1912 -0.0466 0.0161  0.0824  114 TYR A CE2 
911  C  CZ  . TYR A 114 ? 0.2929 0.2556 0.1493 0.0384  0.0678  0.0548  114 TYR A CZ  
912  O  OH  . TYR A 114 ? 0.4149 0.4226 0.1992 0.0466  0.1436  0.0673  114 TYR A OH  
913  N  N   . ALA A 115 ? 0.1888 0.1621 0.0779 0.0149  -0.0272 0.0098  115 ALA A N   
914  C  CA  . ALA A 115 ? 0.1583 0.1913 0.1077 -0.0192 -0.0013 -0.0175 115 ALA A CA  
915  C  C   . ALA A 115 ? 0.1432 0.1824 0.1127 -0.0030 -0.0391 -0.0063 115 ALA A C   
916  O  O   . ALA A 115 ? 0.1673 0.2095 0.1027 -0.0044 -0.0249 -0.0363 115 ALA A O   
917  C  CB  . ALA A 115 ? 0.1518 0.2493 0.1368 0.0038  -0.0461 -0.0241 115 ALA A CB  
918  N  N   . ALA A 116 ? 0.1712 0.1696 0.0700 -0.0012 -0.0411 0.0030  116 ALA A N   
919  C  CA  . ALA A 116 ? 0.2055 0.1662 0.0267 0.0170  -0.0634 -0.0006 116 ALA A CA  
920  C  C   . ALA A 116 ? 0.1309 0.1809 0.0966 -0.0044 -0.0384 -0.0257 116 ALA A C   
921  O  O   . ALA A 116 ? 0.1533 0.1923 0.0933 -0.0005 -0.0164 -0.0026 116 ALA A O   
922  C  CB  . ALA A 116 ? 0.1508 0.2092 0.0363 0.0054  -0.0649 0.0096  116 ALA A CB  
923  N  N   . GLU A 117 ? 0.1224 0.1708 0.0802 -0.0128 -0.0331 -0.0086 117 GLU A N   
924  C  CA  . GLU A 117 ? 0.1330 0.1630 0.0675 0.0087  -0.0708 -0.0100 117 GLU A CA  
925  C  C   . GLU A 117 ? 0.1493 0.1614 0.0551 0.0172  -0.0096 -0.0116 117 GLU A C   
926  O  O   . GLU A 117 ? 0.1342 0.2050 0.0580 0.0166  -0.0158 0.0217  117 GLU A O   
927  C  CB  . GLU A 117 ? 0.1586 0.2422 0.0371 0.0231  -0.0674 0.0044  117 GLU A CB  
928  C  CG  . GLU A 117 ? 0.1571 0.2570 0.0220 0.0022  -0.0444 0.0167  117 GLU A CG  
929  C  CD  . GLU A 117 ? 0.1860 0.2297 0.0259 -0.0304 -0.0548 0.0341  117 GLU A CD  
930  O  OE1 . GLU A 117 ? 0.2038 0.2240 0.1091 -0.0118 -0.0363 -0.0184 117 GLU A OE1 
931  O  OE2 . GLU A 117 ? 0.2357 0.2091 0.0847 0.0055  -0.0525 0.0057  117 GLU A OE2 
932  N  N   . LEU A 118 ? 0.1431 0.1823 0.0427 0.0218  -0.0361 -0.0352 118 LEU A N   
933  C  CA  . LEU A 118 ? 0.1281 0.1546 0.0983 0.0027  -0.0231 -0.0222 118 LEU A CA  
934  C  C   . LEU A 118 ? 0.1472 0.1511 0.0317 0.0016  -0.0377 0.0046  118 LEU A C   
935  O  O   . LEU A 118 ? 0.1269 0.1729 0.0512 -0.0043 -0.0154 0.0307  118 LEU A O   
936  C  CB  . LEU A 118 ? 0.1385 0.1849 0.0835 0.0070  -0.0326 0.0065  118 LEU A CB  
937  C  CG  . LEU A 118 ? 0.1172 0.2161 0.0732 0.0244  -0.0377 0.0046  118 LEU A CG  
938  C  CD1 . LEU A 118 ? 0.1334 0.2276 0.0472 0.0039  -0.0446 -0.0003 118 LEU A CD1 
939  C  CD2 . LEU A 118 ? 0.1346 0.2832 0.0740 -0.0376 -0.0610 0.0220  118 LEU A CD2 
940  N  N   . HIS A 119 ? 0.1533 0.1543 0.0348 -0.0165 -0.0644 0.0022  119 HIS A N   
941  C  CA  . HIS A 119 ? 0.1360 0.1496 0.1072 -0.0190 -0.0256 -0.0209 119 HIS A CA  
942  C  C   . HIS A 119 ? 0.1536 0.1863 0.0635 -0.0044 -0.0403 0.0019  119 HIS A C   
943  O  O   . HIS A 119 ? 0.1407 0.2000 0.0575 0.0117  -0.0220 -0.0027 119 HIS A O   
944  C  CB  . HIS A 119 ? 0.1363 0.1806 0.0903 -0.0144 -0.0358 0.0031  119 HIS A CB  
945  C  CG  . HIS A 119 ? 0.1935 0.2020 0.1100 0.0175  -0.0446 0.0051  119 HIS A CG  
946  N  ND1 . HIS A 119 ? 0.2000 0.2269 0.0198 0.0253  -0.0422 -0.0126 119 HIS A ND1 
947  C  CD2 . HIS A 119 ? 0.1364 0.2068 0.0704 0.0017  -0.0778 -0.0040 119 HIS A CD2 
948  C  CE1 . HIS A 119 ? 0.1231 0.1691 0.0709 -0.0308 -0.0598 -0.0043 119 HIS A CE1 
949  N  NE2 . HIS A 119 ? 0.1373 0.2217 0.0348 0.0025  -0.0610 0.0044  119 HIS A NE2 
950  N  N   . LEU A 120 ? 0.1414 0.1770 0.0982 0.0071  -0.0341 0.0091  120 LEU A N   
951  C  CA  . LEU A 120 ? 0.1306 0.1849 0.0576 0.0033  -0.0449 0.0049  120 LEU A CA  
952  C  C   . LEU A 120 ? 0.1438 0.1816 0.0321 -0.0027 -0.0262 0.0000  120 LEU A C   
953  O  O   . LEU A 120 ? 0.1485 0.1935 0.0276 0.0020  -0.0337 0.0074  120 LEU A O   
954  C  CB  . LEU A 120 ? 0.1335 0.1659 0.0828 -0.0062 -0.0458 -0.0032 120 LEU A CB  
955  C  CG  . LEU A 120 ? 0.1028 0.2445 0.0560 -0.0311 -0.0602 -0.0095 120 LEU A CG  
956  C  CD1 . LEU A 120 ? 0.2305 0.2368 0.1278 -0.0732 -0.0334 0.0052  120 LEU A CD1 
957  C  CD2 . LEU A 120 ? 0.1719 0.2794 0.0738 -0.0048 -0.0741 0.0166  120 LEU A CD2 
958  N  N   . VAL A 121 ? 0.1734 0.1682 0.0613 -0.0218 -0.0170 -0.0113 121 VAL A N   
959  C  CA  . VAL A 121 ? 0.1306 0.1617 0.0642 -0.0297 -0.0097 0.0203  121 VAL A CA  
960  C  C   . VAL A 121 ? 0.1513 0.1747 0.0451 -0.0052 -0.0412 0.0118  121 VAL A C   
961  O  O   . VAL A 121 ? 0.1531 0.1969 0.0613 0.0131  -0.0489 0.0239  121 VAL A O   
962  C  CB  . VAL A 121 ? 0.1436 0.1928 0.0964 -0.0222 0.0132  -0.0005 121 VAL A CB  
963  C  CG1 . VAL A 121 ? 0.1502 0.2416 0.1201 -0.0484 -0.0076 -0.0010 121 VAL A CG1 
964  C  CG2 . VAL A 121 ? 0.1479 0.1885 0.1018 -0.0061 -0.0136 0.0111  121 VAL A CG2 
965  N  N   . HIS A 122 ? 0.1820 0.1712 0.0698 -0.0096 -0.0287 -0.0042 122 HIS A N   
966  C  CA  . HIS A 122 ? 0.1572 0.1896 0.0707 -0.0060 -0.0149 -0.0160 122 HIS A CA  
967  C  C   . HIS A 122 ? 0.1256 0.1773 0.0436 0.0107  -0.0292 0.0139  122 HIS A C   
968  O  O   . HIS A 122 ? 0.1769 0.2121 0.0346 0.0024  -0.0660 0.0083  122 HIS A O   
969  C  CB  . HIS A 122 ? 0.1335 0.1989 0.0882 -0.0146 -0.0296 -0.0134 122 HIS A CB  
970  C  CG  . HIS A 122 ? 0.1134 0.1952 0.0662 -0.0267 0.0184  -0.0062 122 HIS A CG  
971  N  ND1 . HIS A 122 ? 0.1801 0.2169 0.0653 0.0051  -0.0333 -0.0071 122 HIS A ND1 
972  C  CD2 . HIS A 122 ? 0.1474 0.2146 0.0565 0.0154  -0.0236 0.0044  122 HIS A CD2 
973  C  CE1 . HIS A 122 ? 0.1664 0.2154 0.0824 0.0204  0.0021  -0.0189 122 HIS A CE1 
974  N  NE2 . HIS A 122 ? 0.1628 0.2240 0.0634 0.0036  -0.0392 -0.0134 122 HIS A NE2 
975  N  N   . TRP A 123 ? 0.1486 0.1788 0.0673 -0.0044 -0.0122 -0.0172 123 TRP A N   
976  C  CA  . TRP A 123 ? 0.1576 0.1870 0.0662 -0.0084 -0.0516 -0.0049 123 TRP A CA  
977  C  C   . TRP A 123 ? 0.1966 0.2170 0.0373 0.0220  -0.0768 -0.0082 123 TRP A C   
978  O  O   . TRP A 123 ? 0.1574 0.1975 0.0847 0.0358  -0.0103 -0.0143 123 TRP A O   
979  C  CB  . TRP A 123 ? 0.1761 0.2138 0.0777 -0.0268 -0.0549 0.0061  123 TRP A CB  
980  C  CG  . TRP A 123 ? 0.1964 0.2013 0.0418 -0.0285 -0.0480 -0.0116 123 TRP A CG  
981  C  CD1 . TRP A 123 ? 0.2549 0.1862 0.0358 0.0100  -0.0165 -0.0130 123 TRP A CD1 
982  C  CD2 . TRP A 123 ? 0.2050 0.1985 0.0450 -0.0261 -0.0423 -0.0060 123 TRP A CD2 
983  N  NE1 . TRP A 123 ? 0.2866 0.1849 0.0950 0.0136  -0.0089 0.0381  123 TRP A NE1 
984  C  CE2 . TRP A 123 ? 0.2376 0.1982 0.0239 0.0082  -0.0052 0.0389  123 TRP A CE2 
985  C  CE3 . TRP A 123 ? 0.1902 0.1708 0.1285 -0.0098 -0.0204 0.0024  123 TRP A CE3 
986  C  CZ2 . TRP A 123 ? 0.2593 0.1912 0.1280 0.0122  0.0168  0.0218  123 TRP A CZ2 
987  C  CZ3 . TRP A 123 ? 0.2142 0.2020 0.0801 0.0150  -0.0281 0.0201  123 TRP A CZ3 
988  C  CH2 . TRP A 123 ? 0.2098 0.2043 0.0865 0.0400  -0.0395 0.0053  123 TRP A CH2 
989  N  N   . ASN A 124 ? 0.1996 0.2121 0.0346 -0.0198 -0.0595 -0.0200 124 ASN A N   
990  C  CA  . ASN A 124 ? 0.2248 0.1751 0.0759 -0.0085 -0.0650 -0.0273 124 ASN A CA  
991  C  C   . ASN A 124 ? 0.2089 0.1888 0.0560 -0.0281 -0.0469 -0.0248 124 ASN A C   
992  O  O   . ASN A 124 ? 0.2075 0.1993 0.0709 -0.0216 -0.0166 -0.0046 124 ASN A O   
993  C  CB  . ASN A 124 ? 0.2139 0.2147 0.0678 -0.0114 -0.0577 -0.0160 124 ASN A CB  
994  C  CG  . ASN A 124 ? 0.2311 0.2024 0.0505 -0.0263 -0.0666 -0.0023 124 ASN A CG  
995  O  OD1 . ASN A 124 ? 0.2748 0.2350 0.0967 0.0040  -0.0031 -0.0325 124 ASN A OD1 
996  N  ND2 . ASN A 124 ? 0.2635 0.3171 0.0558 0.0055  -0.0871 0.0022  124 ASN A ND2 
997  N  N   . THR A 125 ? 0.1964 0.2121 0.1066 -0.0078 -0.0166 -0.0022 125 THR A N   
998  C  CA  . THR A 125 ? 0.2409 0.1949 0.2292 -0.0094 -0.0177 0.0175  125 THR A CA  
999  C  C   . THR A 125 ? 0.2432 0.1892 0.2185 -0.0063 -0.0173 0.0075  125 THR A C   
1000 O  O   . THR A 125 ? 0.3574 0.2124 0.2677 -0.0389 -0.0001 0.0116  125 THR A O   
1001 C  CB  . THR A 125 ? 0.2409 0.2924 0.2484 0.0111  0.0399  0.0293  125 THR A CB  
1002 O  OG1 . THR A 125 ? 0.2525 0.2617 0.3063 0.0499  0.0886  -0.0021 125 THR A OG1 
1003 C  CG2 . THR A 125 ? 0.1927 0.3896 0.2456 -0.0162 -0.0130 0.0157  125 THR A CG2 
1004 N  N   . LYS A 126 ? 0.3119 0.1964 0.1694 -0.0114 0.0416  -0.0521 127 LYS A N   
1005 C  CA  . LYS A 126 ? 0.3012 0.2644 0.1482 -0.0361 0.0413  -0.0895 127 LYS A CA  
1006 C  C   . LYS A 126 ? 0.3598 0.2072 0.2214 -0.0161 0.1028  -0.0502 127 LYS A C   
1007 O  O   . LYS A 126 ? 0.4398 0.2269 0.3799 -0.0226 0.1351  -0.1034 127 LYS A O   
1008 C  CB  . LYS A 126 ? 0.4616 0.3654 0.1217 -0.0347 0.0522  -0.1165 127 LYS A CB  
1009 C  CG  . LYS A 126 ? 0.4323 0.2933 0.3246 -0.1029 0.0212  -0.1126 127 LYS A CG  
1010 C  CD  . LYS A 126 ? 0.5681 0.5690 0.4007 0.0644  -0.1306 -0.0385 127 LYS A CD  
1011 C  CE  . LYS A 126 ? 0.4326 0.5696 0.4066 0.1086  -0.1788 0.0283  127 LYS A CE  
1012 N  NZ  . LYS A 126 ? 0.2932 0.5407 0.3905 -0.0424 -0.1263 -0.0163 127 LYS A NZ  
1013 N  N   . TYR A 127 ? 0.2572 0.2172 0.1795 -0.0187 0.0223  -0.0613 128 TYR A N   
1014 C  CA  . TYR A 127 ? 0.2764 0.2122 0.1838 -0.0355 0.0058  0.0081  128 TYR A CA  
1015 C  C   . TYR A 127 ? 0.2336 0.2153 0.1622 -0.0425 -0.0177 -0.0273 128 TYR A C   
1016 O  O   . TYR A 127 ? 0.2272 0.2562 0.2027 -0.0370 -0.0010 -0.0145 128 TYR A O   
1017 C  CB  . TYR A 127 ? 0.2926 0.1937 0.1835 -0.0336 -0.0550 -0.0356 128 TYR A CB  
1018 C  CG  . TYR A 127 ? 0.2526 0.2280 0.1795 -0.0297 -0.0397 -0.0336 128 TYR A CG  
1019 C  CD1 . TYR A 127 ? 0.3460 0.2127 0.1611 -0.0086 -0.0476 -0.0502 128 TYR A CD1 
1020 C  CD2 . TYR A 127 ? 0.2384 0.2463 0.1248 -0.0367 0.0243  -0.0387 128 TYR A CD2 
1021 C  CE1 . TYR A 127 ? 0.2640 0.2974 0.1766 0.0061  -0.0485 -0.0188 128 TYR A CE1 
1022 C  CE2 . TYR A 127 ? 0.2518 0.2745 0.1454 -0.0215 -0.0089 -0.0409 128 TYR A CE2 
1023 C  CZ  . TYR A 127 ? 0.2925 0.2796 0.1277 -0.0067 -0.0268 -0.0362 128 TYR A CZ  
1024 O  OH  . TYR A 127 ? 0.4519 0.2720 0.1615 -0.0134 -0.1173 -0.0336 128 TYR A OH  
1025 N  N   . GLY A 128 ? 0.2499 0.2122 0.2031 -0.0055 -0.0688 -0.0048 129 GLY A N   
1026 C  CA  . GLY A 128 ? 0.3446 0.1928 0.1679 -0.0034 0.0022  -0.0118 129 GLY A CA  
1027 C  C   . GLY A 128 ? 0.2359 0.2088 0.1769 -0.0076 -0.0290 -0.0114 129 GLY A C   
1028 O  O   . GLY A 128 ? 0.4024 0.2850 0.1432 -0.0223 -0.0172 0.0394  129 GLY A O   
1029 N  N   A ASP A 129 ? 0.2441 0.2218 0.1479 0.0052  0.0308  -0.0002 130 ASP A N   
1030 N  N   B ASP A 129 ? 0.2658 0.2079 0.1665 0.0199  -0.0020 -0.0523 130 ASP A N   
1031 C  CA  A ASP A 129 ? 0.2680 0.2108 0.1357 -0.0269 0.0737  0.0189  130 ASP A CA  
1032 C  CA  B ASP A 129 ? 0.2499 0.2207 0.1653 0.0225  0.0165  -0.0245 130 ASP A CA  
1033 C  C   A ASP A 129 ? 0.2170 0.2298 0.1217 -0.0093 0.0412  -0.0081 130 ASP A C   
1034 C  C   B ASP A 129 ? 0.2667 0.2388 0.0653 -0.0027 -0.0290 0.0002  130 ASP A C   
1035 O  O   A ASP A 129 ? 0.2444 0.3172 0.1147 -0.0318 0.0511  -0.0114 130 ASP A O   
1036 O  O   B ASP A 129 ? 0.2416 0.2368 0.0564 -0.0275 -0.0240 -0.0281 130 ASP A O   
1037 C  CB  A ASP A 129 ? 0.2722 0.2391 0.0220 -0.0038 -0.0308 0.0479  130 ASP A CB  
1038 C  CB  B ASP A 129 ? 0.2470 0.2512 0.1062 0.0198  0.0153  -0.0150 130 ASP A CB  
1039 C  CG  A ASP A 129 ? 0.2953 0.2140 0.1729 -0.0262 -0.0142 0.0402  130 ASP A CG  
1040 C  CG  B ASP A 129 ? 0.2781 0.2833 0.0490 0.0236  0.0086  -0.0222 130 ASP A CG  
1041 O  OD1 A ASP A 129 ? 0.3008 0.2393 0.0813 -0.0363 -0.0435 0.1121  130 ASP A OD1 
1042 O  OD1 B ASP A 129 ? 0.3348 0.2758 0.0262 0.0825  -0.0260 0.0551  130 ASP A OD1 
1043 O  OD2 A ASP A 129 ? 0.2794 0.1916 0.2789 0.0128  -0.0162 0.0179  130 ASP A OD2 
1044 O  OD2 B ASP A 129 ? 0.1842 0.3189 0.2147 -0.0397 0.0430  0.0059  130 ASP A OD2 
1045 N  N   . ALA A 130 ? 0.2745 0.2211 0.1461 -0.0447 0.0474  -0.0146 131 ALA A N   
1046 C  CA  . ALA A 130 ? 0.2593 0.2114 0.1116 -0.0553 0.0499  -0.0354 131 ALA A CA  
1047 C  C   . ALA A 130 ? 0.2576 0.2895 0.0851 -0.0239 0.0000  -0.0129 131 ALA A C   
1048 O  O   . ALA A 130 ? 0.2473 0.2939 0.1414 -0.0061 -0.0050 0.0237  131 ALA A O   
1049 C  CB  . ALA A 130 ? 0.3519 0.2265 0.0994 -0.0869 -0.0168 -0.0175 131 ALA A CB  
1050 N  N   . GLY A 131 ? 0.2433 0.3367 0.1849 -0.0439 0.0768  -0.0568 132 GLY A N   
1051 C  CA  . GLY A 131 ? 0.2395 0.4462 0.1872 0.0048  0.1072  -0.0576 132 GLY A CA  
1052 C  C   . GLY A 131 ? 0.2472 0.3712 0.1916 -0.0563 0.0175  0.0016  132 GLY A C   
1053 O  O   . GLY A 131 ? 0.2599 0.3844 0.1982 -0.0304 0.0289  -0.0542 132 GLY A O   
1054 N  N   A LYS A 132 ? 0.2837 0.3639 0.1899 -0.0915 0.0520  -0.0196 133 LYS A N   
1055 N  N   B LYS A 132 ? 0.2845 0.3522 0.1127 -0.1083 0.0493  -0.0330 133 LYS A N   
1056 C  CA  A LYS A 132 ? 0.3177 0.3165 0.1640 -0.0745 0.0441  0.0125  133 LYS A CA  
1057 C  CA  B LYS A 132 ? 0.3280 0.2906 0.1058 -0.0836 0.0337  -0.0127 133 LYS A CA  
1058 C  C   A LYS A 132 ? 0.2340 0.2218 0.1043 -0.0712 -0.0345 -0.0170 133 LYS A C   
1059 C  C   B LYS A 132 ? 0.2552 0.2212 0.0894 -0.0838 -0.0447 -0.0004 133 LYS A C   
1060 O  O   A LYS A 132 ? 0.2159 0.3108 0.0998 -0.0610 -0.0181 -0.0156 133 LYS A O   
1061 O  O   B LYS A 132 ? 0.2823 0.3625 0.1018 -0.0849 -0.0569 -0.0355 133 LYS A O   
1062 C  CB  A LYS A 132 ? 0.3116 0.3826 0.3100 -0.0271 0.0419  0.0681  133 LYS A CB  
1063 C  CB  B LYS A 132 ? 0.3837 0.2764 0.0719 -0.0947 0.0237  0.0140  133 LYS A CB  
1064 C  CG  A LYS A 132 ? 0.3006 0.4170 0.4066 -0.0579 0.0251  0.0942  133 LYS A CG  
1065 C  CG  B LYS A 132 ? 0.3577 0.3820 0.0137 -0.0696 -0.0151 0.0526  133 LYS A CG  
1066 C  CD  A LYS A 132 ? 0.2566 0.4515 0.3757 0.0320  0.0115  0.0948  133 LYS A CD  
1067 C  CD  B LYS A 132 ? 0.3315 0.3725 0.0673 -0.1155 0.0658  -0.0265 133 LYS A CD  
1068 C  CE  A LYS A 132 ? 0.2840 0.3963 0.4540 -0.0622 -0.0856 0.0693  133 LYS A CE  
1069 C  CE  B LYS A 132 ? 0.3319 0.3797 0.1571 -0.0718 -0.0570 0.1498  133 LYS A CE  
1070 N  NZ  A LYS A 132 ? 0.2436 0.5753 0.4179 -0.0455 -0.1177 0.1467  133 LYS A NZ  
1071 N  NZ  B LYS A 132 ? 0.2497 0.2339 0.4799 0.0525  -0.0789 -0.0161 133 LYS A NZ  
1072 N  N   . ALA A 133 ? 0.2114 0.2089 0.1413 -0.0666 0.0403  -0.0284 134 ALA A N   
1073 C  CA  . ALA A 133 ? 0.2201 0.2153 0.1608 -0.0559 0.0176  0.0024  134 ALA A CA  
1074 C  C   . ALA A 133 ? 0.2663 0.1985 0.1005 -0.0198 -0.0288 -0.0148 134 ALA A C   
1075 O  O   . ALA A 133 ? 0.2477 0.3063 0.1190 -0.0183 -0.0080 0.0222  134 ALA A O   
1076 C  CB  . ALA A 133 ? 0.1762 0.2443 0.0837 -0.0289 0.0107  -0.0085 134 ALA A CB  
1077 N  N   . SER A 134 ? 0.2556 0.2628 0.2147 -0.0141 0.0452  -0.0302 135 SER A N   
1078 C  CA  . SER A 134 ? 0.2939 0.2551 0.1587 -0.0400 0.0375  -0.0620 135 SER A CA  
1079 C  C   . SER A 134 ? 0.3004 0.3129 0.1601 -0.0621 0.0359  0.0227  135 SER A C   
1080 O  O   . SER A 134 ? 0.3514 0.3388 0.1619 -0.0399 0.0524  0.0187  135 SER A O   
1081 C  CB  . SER A 134 ? 0.3296 0.3492 0.1177 -0.0348 0.0390  -0.0480 135 SER A CB  
1082 O  OG  . SER A 134 ? 0.3523 0.3961 0.1345 -0.0204 0.0680  0.0039  135 SER A OG  
1083 N  N   . GLN A 135 ? 0.2339 0.3134 0.1812 -0.0294 -0.0107 -0.0244 136 GLN A N   
1084 C  CA  . GLN A 135 ? 0.2922 0.3340 0.2494 -0.0825 -0.0359 -0.0493 136 GLN A CA  
1085 C  C   . GLN A 135 ? 0.2481 0.3763 0.2383 -0.0635 -0.0684 -0.0201 136 GLN A C   
1086 O  O   . GLN A 135 ? 0.2559 0.4278 0.1833 -0.0873 -0.0487 -0.0452 136 GLN A O   
1087 C  CB  . GLN A 135 ? 0.2039 0.3365 0.3641 -0.0420 -0.0035 -0.0201 136 GLN A CB  
1088 C  CG  . GLN A 135 ? 0.4670 0.5572 0.3690 -0.0247 -0.0253 -0.0519 136 GLN A CG  
1089 C  CD  . GLN A 135 ? 0.4550 0.5527 0.4933 -0.0878 0.1397  0.0346  136 GLN A CD  
1090 O  OE1 . GLN A 135 ? 0.8431 0.5848 0.6808 -0.0336 0.3124  0.1309  136 GLN A OE1 
1091 N  NE2 . GLN A 135 ? 0.6174 0.6781 0.5959 -0.3844 -0.0128 0.1738  136 GLN A NE2 
1092 N  N   . GLN A 136 ? 0.2458 0.2808 0.1238 -0.0293 -0.0105 -0.0096 137 GLN A N   
1093 C  CA  . GLN A 136 ? 0.3126 0.3108 0.1034 -0.0168 -0.0091 -0.0269 137 GLN A CA  
1094 C  C   . GLN A 136 ? 0.3048 0.2825 0.1474 -0.0279 -0.0278 -0.0589 137 GLN A C   
1095 O  O   . GLN A 136 ? 0.2559 0.2695 0.1260 -0.0440 0.0107  -0.0347 137 GLN A O   
1096 C  CB  . GLN A 136 ? 0.2847 0.2983 0.0923 -0.0234 -0.0156 -0.0155 137 GLN A CB  
1097 C  CG  . GLN A 136 ? 0.4030 0.3948 0.2377 -0.0194 0.1375  0.0942  137 GLN A CG  
1098 C  CD  . GLN A 136 ? 0.4698 0.2970 0.6790 -0.0990 0.0159  -0.0185 137 GLN A CD  
1099 O  OE1 . GLN A 136 ? 0.7133 0.3707 0.7014 -0.0059 -0.1901 0.0660  137 GLN A OE1 
1100 N  NE2 . GLN A 136 ? 0.3895 0.4445 0.2914 -0.0184 -0.0954 -0.0234 137 GLN A NE2 
1101 N  N   . PRO A 137 ? 0.2593 0.3092 0.1411 -0.0561 -0.0537 -0.0097 138 PRO A N   
1102 C  CA  . PRO A 137 ? 0.2977 0.3182 0.0703 -0.0487 -0.0455 -0.0108 138 PRO A CA  
1103 C  C   . PRO A 137 ? 0.2828 0.2458 0.1174 -0.0078 -0.0143 -0.0176 138 PRO A C   
1104 O  O   . PRO A 137 ? 0.3542 0.2445 0.2085 0.0052  0.0358  -0.0064 138 PRO A O   
1105 C  CB  . PRO A 137 ? 0.3071 0.4647 0.0574 -0.0100 -0.0956 0.0637  138 PRO A CB  
1106 C  CG  . PRO A 137 ? 0.5447 0.4562 0.1939 -0.1481 0.0060  0.0144  138 PRO A CG  
1107 C  CD  . PRO A 137 ? 0.3735 0.2733 0.1887 -0.1289 -0.0504 0.0179  138 PRO A CD  
1108 N  N   . ASP A 138 ? 0.2661 0.2434 0.1050 -0.0036 -0.0216 -0.0080 139 ASP A N   
1109 C  CA  . ASP A 138 ? 0.2816 0.2442 0.0790 -0.0348 -0.0121 -0.0081 139 ASP A CA  
1110 C  C   . ASP A 138 ? 0.2573 0.2179 0.0926 0.0072  -0.0168 -0.0197 139 ASP A C   
1111 O  O   . ASP A 138 ? 0.2303 0.2816 0.0953 -0.0109 -0.0023 -0.0058 139 ASP A O   
1112 C  CB  . ASP A 138 ? 0.3122 0.2557 0.0795 -0.0125 -0.0431 -0.0305 139 ASP A CB  
1113 C  CG  . ASP A 138 ? 0.3518 0.2678 0.1192 0.0442  -0.0510 -0.0463 139 ASP A CG  
1114 O  OD1 . ASP A 138 ? 0.3753 0.2699 0.1342 0.0054  -0.0186 -0.0511 139 ASP A OD1 
1115 O  OD2 . ASP A 138 ? 0.4325 0.3373 0.2194 0.0915  0.0210  -0.0572 139 ASP A OD2 
1116 N  N   . GLY A 139 ? 0.1939 0.1978 0.1172 0.0163  -0.0225 0.0272  140 GLY A N   
1117 C  CA  . GLY A 139 ? 0.2381 0.1511 0.1086 0.0029  -0.0440 0.0178  140 GLY A CA  
1118 C  C   . GLY A 139 ? 0.1824 0.1849 0.1025 0.0044  0.0000  -0.0023 140 GLY A C   
1119 O  O   . GLY A 139 ? 0.2220 0.1856 0.0966 0.0262  -0.0210 -0.0085 140 GLY A O   
1120 N  N   . LEU A 140 ? 0.1869 0.2018 0.0343 -0.0256 -0.0520 -0.0166 141 LEU A N   
1121 C  CA  . LEU A 140 ? 0.1436 0.1939 0.0555 -0.0158 -0.0400 -0.0276 141 LEU A CA  
1122 C  C   . LEU A 140 ? 0.1759 0.1622 0.0696 0.0054  -0.0484 0.0226  141 LEU A C   
1123 O  O   . LEU A 140 ? 0.2063 0.1899 0.0610 -0.0212 -0.0536 0.0245  141 LEU A O   
1124 C  CB  . LEU A 140 ? 0.1761 0.2238 0.0749 0.0305  -0.0333 -0.0171 141 LEU A CB  
1125 C  CG  . LEU A 140 ? 0.2323 0.2192 0.1037 0.0336  -0.0122 0.0094  141 LEU A CG  
1126 C  CD1 . LEU A 140 ? 0.2265 0.2660 0.0327 0.0337  -0.0429 -0.0305 141 LEU A CD1 
1127 C  CD2 . LEU A 140 ? 0.2070 0.2481 0.0749 -0.0016 -0.0646 0.0086  141 LEU A CD2 
1128 N  N   . ALA A 141 ? 0.1597 0.1901 0.0901 -0.0215 -0.0201 0.0096  142 ALA A N   
1129 C  CA  . ALA A 141 ? 0.1734 0.1822 0.0806 -0.0303 -0.0374 -0.0234 142 ALA A CA  
1130 C  C   . ALA A 141 ? 0.1890 0.1720 0.0408 -0.0178 -0.0519 -0.0011 142 ALA A C   
1131 O  O   . ALA A 141 ? 0.1890 0.1756 0.0707 0.0107  -0.0589 0.0281  142 ALA A O   
1132 C  CB  . ALA A 141 ? 0.1709 0.2354 0.0801 -0.0315 -0.0367 -0.0156 142 ALA A CB  
1133 N  N   . VAL A 142 ? 0.1665 0.1567 0.0914 -0.0098 -0.0247 -0.0293 143 VAL A N   
1134 C  CA  . VAL A 142 ? 0.1837 0.1632 0.0633 0.0118  -0.0315 -0.0120 143 VAL A CA  
1135 C  C   . VAL A 142 ? 0.1702 0.1574 0.0601 -0.0013 -0.0649 0.0173  143 VAL A C   
1136 O  O   . VAL A 142 ? 0.1756 0.2156 0.0452 -0.0081 -0.0564 0.0176  143 VAL A O   
1137 C  CB  . VAL A 142 ? 0.1752 0.2028 0.0641 0.0201  -0.0421 -0.0044 143 VAL A CB  
1138 C  CG1 . VAL A 142 ? 0.1891 0.2509 0.0504 0.0271  -0.0520 -0.0254 143 VAL A CG1 
1139 C  CG2 . VAL A 142 ? 0.1939 0.2713 0.0842 -0.0109 -0.0265 0.0243  143 VAL A CG2 
1140 N  N   . LEU A 143 ? 0.1666 0.1860 0.0461 -0.0146 -0.0478 -0.0161 144 LEU A N   
1141 C  CA  . LEU A 143 ? 0.1667 0.1972 0.0316 -0.0016 -0.0636 0.0027  144 LEU A CA  
1142 C  C   . LEU A 143 ? 0.1988 0.2017 0.0419 0.0031  0.0035  -0.0036 144 LEU A C   
1143 O  O   . LEU A 143 ? 0.1842 0.2225 0.0321 -0.0283 -0.0226 0.0267  144 LEU A O   
1144 C  CB  . LEU A 143 ? 0.1468 0.2551 0.0592 -0.0075 -0.0820 -0.0104 144 LEU A CB  
1145 C  CG  . LEU A 143 ? 0.1872 0.2692 0.0401 -0.0086 -0.0618 0.0003  144 LEU A CG  
1146 C  CD1 . LEU A 143 ? 0.2255 0.3614 0.0657 0.0000  0.0020  0.0128  144 LEU A CD1 
1147 C  CD2 . LEU A 143 ? 0.1960 0.3899 0.1009 0.0269  -0.0838 0.0103  144 LEU A CD2 
1148 N  N   . GLY A 144 ? 0.1597 0.1659 0.1274 -0.0212 -0.0583 -0.0078 145 GLY A N   
1149 C  CA  . GLY A 144 ? 0.1759 0.1777 0.0314 -0.0201 -0.0277 0.0010  145 GLY A CA  
1150 C  C   . GLY A 144 ? 0.1565 0.1878 0.0892 -0.0089 0.0005  -0.0383 145 GLY A C   
1151 O  O   . GLY A 144 ? 0.1751 0.2085 0.0679 0.0018  -0.0117 0.0080  145 GLY A O   
1152 N  N   . ILE A 145 ? 0.1558 0.1576 0.0501 -0.0048 -0.0339 -0.0006 146 ILE A N   
1153 C  CA  . ILE A 145 ? 0.1457 0.1745 0.0924 0.0143  -0.0671 0.0142  146 ILE A CA  
1154 C  C   . ILE A 145 ? 0.1220 0.1840 0.0628 -0.0067 -0.0348 -0.0177 146 ILE A C   
1155 O  O   . ILE A 145 ? 0.1531 0.1987 0.0807 0.0100  -0.0148 0.0222  146 ILE A O   
1156 C  CB  . ILE A 145 ? 0.1457 0.2047 0.0175 0.0207  -0.0345 0.0175  146 ILE A CB  
1157 C  CG1 . ILE A 145 ? 0.1655 0.2296 0.0542 0.0424  -0.0478 0.0076  146 ILE A CG1 
1158 C  CG2 . ILE A 145 ? 0.1921 0.2298 0.1007 -0.0080 -0.0364 0.0066  146 ILE A CG2 
1159 C  CD1 . ILE A 145 ? 0.1730 0.2359 0.0574 0.0609  -0.0522 -0.0137 146 ILE A CD1 
1160 N  N   . PHE A 146 ? 0.1317 0.1941 0.0928 0.0048  -0.0422 0.0023  147 PHE A N   
1161 C  CA  . PHE A 146 ? 0.2152 0.1799 0.0339 0.0016  -0.0484 0.0063  147 PHE A CA  
1162 C  C   . PHE A 146 ? 0.1199 0.1887 0.0659 -0.0006 -0.0252 -0.0130 147 PHE A C   
1163 O  O   . PHE A 146 ? 0.1276 0.2472 0.0533 0.0158  -0.0013 -0.0079 147 PHE A O   
1164 C  CB  . PHE A 146 ? 0.1436 0.1935 0.0478 0.0011  -0.0522 0.0225  147 PHE A CB  
1165 C  CG  . PHE A 146 ? 0.1355 0.1668 0.0675 0.0190  -0.0346 -0.0289 147 PHE A CG  
1166 C  CD1 . PHE A 146 ? 0.1301 0.2176 0.0339 0.0269  -0.0482 -0.0058 147 PHE A CD1 
1167 C  CD2 . PHE A 146 ? 0.1506 0.1716 0.0700 0.0166  -0.0204 -0.0166 147 PHE A CD2 
1168 C  CE1 . PHE A 146 ? 0.1605 0.2243 0.0180 0.0311  -0.0419 -0.0013 147 PHE A CE1 
1169 C  CE2 . PHE A 146 ? 0.1628 0.2276 0.1062 0.0203  -0.0523 -0.0166 147 PHE A CE2 
1170 C  CZ  . PHE A 146 ? 0.1580 0.2067 0.0277 0.0115  -0.0302 -0.0230 147 PHE A CZ  
1171 N  N   . LEU A 147 ? 0.1454 0.1833 0.0555 0.0097  -0.0304 -0.0190 148 LEU A N   
1172 C  CA  . LEU A 147 ? 0.1508 0.2006 0.0384 0.0006  -0.0307 -0.0117 148 LEU A CA  
1173 C  C   . LEU A 147 ? 0.1579 0.1941 0.0639 0.0031  -0.0209 -0.0181 148 LEU A C   
1174 O  O   . LEU A 147 ? 0.1632 0.2102 0.1045 0.0196  -0.0292 0.0030  148 LEU A O   
1175 C  CB  . LEU A 147 ? 0.1788 0.2039 0.0612 -0.0023 -0.0095 0.0126  148 LEU A CB  
1176 C  CG  . LEU A 147 ? 0.1497 0.1982 0.0390 -0.0127 -0.0228 -0.0080 148 LEU A CG  
1177 C  CD1 . LEU A 147 ? 0.2021 0.2233 0.0615 -0.0203 -0.0305 -0.0351 148 LEU A CD1 
1178 C  CD2 . LEU A 147 ? 0.1539 0.2273 0.0321 0.0075  -0.0208 -0.0129 148 LEU A CD2 
1179 N  N   . LYS A 148 ? 0.1795 0.2211 0.1098 -0.0269 -0.0254 -0.0153 149 LYS A N   
1180 C  CA  . LYS A 148 ? 0.1978 0.2291 0.0838 -0.0278 -0.0387 -0.0064 149 LYS A CA  
1181 C  C   . LYS A 148 ? 0.2057 0.2175 0.0869 0.0054  -0.0458 -0.0125 149 LYS A C   
1182 O  O   . LYS A 148 ? 0.2665 0.2474 0.1260 0.0761  -0.0774 -0.0660 149 LYS A O   
1183 C  CB  . LYS A 148 ? 0.2121 0.3431 0.0648 -0.0486 -0.0363 -0.0126 149 LYS A CB  
1184 C  CG  . LYS A 148 ? 0.2171 0.3651 0.2099 0.0001  0.0332  0.0004  149 LYS A CG  
1185 C  CD  . LYS A 148 ? 0.3448 0.5238 0.2472 -0.0703 0.1537  -0.0160 149 LYS A CD  
1186 C  CE  . LYS A 148 ? 0.3388 0.5153 0.4828 -0.1675 0.1083  -0.0642 149 LYS A CE  
1187 N  NZ  . LYS A 148 ? 0.4520 0.7878 0.5725 -0.2276 0.0408  0.1092  149 LYS A NZ  
1188 N  N   . VAL A 149 ? 0.2276 0.2006 0.0745 -0.0199 -0.0480 -0.0140 150 VAL A N   
1189 C  CA  . VAL A 149 ? 0.1759 0.1978 0.1194 -0.0077 -0.0892 -0.0391 150 VAL A CA  
1190 C  C   . VAL A 149 ? 0.1687 0.2150 0.1719 0.0186  -0.0632 0.0003  150 VAL A C   
1191 O  O   . VAL A 149 ? 0.2235 0.2205 0.1463 -0.0054 -0.0762 0.0025  150 VAL A O   
1192 C  CB  . VAL A 149 ? 0.2203 0.2240 0.0496 0.0031  -0.0526 0.0043  150 VAL A CB  
1193 C  CG1 . VAL A 149 ? 0.2163 0.2881 0.1107 -0.0083 -0.1023 -0.0364 150 VAL A CG1 
1194 C  CG2 . VAL A 149 ? 0.2068 0.2231 0.1323 -0.0052 -0.0557 0.0139  150 VAL A CG2 
1195 N  N   . GLY A 150 ? 0.1905 0.2219 0.1885 -0.0055 -0.1057 -0.0176 151 GLY A N   
1196 C  CA  . GLY A 150 ? 0.1795 0.2613 0.2240 -0.0207 -0.0800 0.0038  151 GLY A CA  
1197 C  C   . GLY A 150 ? 0.1888 0.1888 0.1500 -0.0187 -0.0353 0.0078  151 GLY A C   
1198 O  O   . GLY A 150 ? 0.1973 0.2481 0.1838 0.0054  -0.0017 0.0153  151 GLY A O   
1199 N  N   . SER A 151 ? 0.1726 0.2214 0.2275 -0.0143 -0.0602 0.0199  152 SER A N   
1200 C  CA  . SER A 151 ? 0.1790 0.2079 0.1727 -0.0071 -0.0461 -0.0051 152 SER A CA  
1201 C  C   . SER A 151 ? 0.1820 0.1921 0.1206 -0.0223 -0.0397 -0.0317 152 SER A C   
1202 O  O   . SER A 151 ? 0.2027 0.2072 0.1208 -0.0236 -0.0551 -0.0261 152 SER A O   
1203 C  CB  . SER A 151 ? 0.1866 0.3359 0.4343 0.0478  -0.0175 -0.0458 152 SER A CB  
1204 O  OG  . SER A 151 ? 0.2663 0.4871 0.4606 -0.0447 -0.0265 -0.0652 152 SER A OG  
1205 N  N   . ALA A 152 ? 0.2289 0.2427 0.1581 0.0277  -0.0461 0.0122  153 ALA A N   
1206 C  CA  . ALA A 152 ? 0.2016 0.2413 0.0730 -0.0136 -0.1008 -0.0118 153 ALA A CA  
1207 C  C   . ALA A 152 ? 0.2043 0.2355 0.0921 -0.0198 -0.0674 0.0000  153 ALA A C   
1208 O  O   . ALA A 152 ? 0.1799 0.2436 0.1956 -0.0174 -0.0357 0.0093  153 ALA A O   
1209 C  CB  . ALA A 152 ? 0.2474 0.3289 0.1045 -0.0422 -0.1531 0.0098  153 ALA A CB  
1210 N  N   . LYS A 153 ? 0.2256 0.2140 0.0425 0.0044  -0.0787 0.0055  154 LYS A N   
1211 C  CA  . LYS A 153 ? 0.1939 0.2016 0.1248 -0.0132 -0.0853 0.0055  154 LYS A CA  
1212 C  C   . LYS A 153 ? 0.1597 0.2397 0.0838 0.0170  -0.0473 -0.0165 154 LYS A C   
1213 O  O   . LYS A 153 ? 0.1806 0.2538 0.0482 0.0031  -0.0615 -0.0111 154 LYS A O   
1214 C  CB  . LYS A 153 ? 0.1770 0.2043 0.1614 -0.0223 -0.0776 -0.0021 154 LYS A CB  
1215 C  CG  . LYS A 153 ? 0.1870 0.2315 0.0693 -0.0317 -0.0606 -0.0063 154 LYS A CG  
1216 C  CD  . LYS A 153 ? 0.2551 0.2759 0.1000 -0.0242 -0.0310 0.0000  154 LYS A CD  
1217 C  CE  . LYS A 153 ? 0.2559 0.3053 0.0879 -0.0134 -0.0473 -0.0055 154 LYS A CE  
1218 N  NZ  . LYS A 153 ? 0.3292 0.3956 0.1392 -0.0315 0.0142  0.0308  154 LYS A NZ  
1219 N  N   . PRO A 154 ? 0.1619 0.2674 0.0595 -0.0181 -0.0574 0.0061  155 PRO A N   
1220 C  CA  . PRO A 154 ? 0.1791 0.2470 0.0413 -0.0276 -0.0476 -0.0039 155 PRO A CA  
1221 C  C   . PRO A 154 ? 0.1763 0.2211 0.0622 -0.0160 -0.0696 -0.0159 155 PRO A C   
1222 O  O   . PRO A 154 ? 0.1662 0.2793 0.0926 -0.0188 -0.0617 0.0096  155 PRO A O   
1223 C  CB  . PRO A 154 ? 0.1700 0.2851 0.2050 -0.0583 -0.0530 0.0137  155 PRO A CB  
1224 C  CG  . PRO A 154 ? 0.1317 0.3296 0.2049 -0.0574 -0.1245 0.0523  155 PRO A CG  
1225 C  CD  . PRO A 154 ? 0.1320 0.2913 0.1246 -0.0405 -0.0730 0.0039  155 PRO A CD  
1226 N  N   . GLY A 155 ? 0.1453 0.2164 0.0943 -0.0098 -0.0463 -0.0436 156 GLY A N   
1227 C  CA  . GLY A 155 ? 0.1599 0.2214 0.0475 -0.0049 -0.0230 -0.0089 156 GLY A CA  
1228 C  C   . GLY A 155 ? 0.1733 0.2285 0.0704 0.0141  0.0057  0.0018  156 GLY A C   
1229 O  O   . GLY A 155 ? 0.1847 0.2396 0.1364 0.0070  -0.0452 0.0150  156 GLY A O   
1230 N  N   . LEU A 156 ? 0.1363 0.2214 0.1016 0.0133  -0.0544 -0.0259 157 LEU A N   
1231 C  CA  . LEU A 156 ? 0.1461 0.2470 0.0897 0.0372  -0.0568 0.0160  157 LEU A CA  
1232 C  C   . LEU A 156 ? 0.1283 0.2509 0.1036 -0.0379 -0.0300 -0.0095 157 LEU A C   
1233 O  O   . LEU A 156 ? 0.1431 0.2608 0.0321 -0.0238 -0.0461 0.0089  157 LEU A O   
1234 C  CB  . LEU A 156 ? 0.1463 0.2572 0.0515 -0.0068 -0.0737 0.0435  157 LEU A CB  
1235 C  CG  . LEU A 156 ? 0.1664 0.2659 0.0521 0.0011  -0.0776 0.0355  157 LEU A CG  
1236 C  CD1 . LEU A 156 ? 0.1459 0.2947 0.1217 -0.0343 -0.0615 0.0264  157 LEU A CD1 
1237 C  CD2 . LEU A 156 ? 0.1790 0.2828 0.1301 0.0245  -0.0611 0.0611  157 LEU A CD2 
1238 N  N   . GLN A 157 ? 0.1452 0.2298 0.0785 0.0085  -0.0600 -0.0068 158 GLN A N   
1239 C  CA  . GLN A 157 ? 0.1754 0.2723 0.0786 -0.0199 -0.0665 -0.0337 158 GLN A CA  
1240 C  C   . GLN A 157 ? 0.1222 0.2395 0.1353 -0.0078 -0.0535 -0.0438 158 GLN A C   
1241 O  O   . GLN A 157 ? 0.1526 0.2760 0.0628 0.0220  -0.0508 -0.0279 158 GLN A O   
1242 C  CB  . GLN A 157 ? 0.1554 0.2775 0.0727 -0.0124 -0.0462 -0.0370 158 GLN A CB  
1243 C  CG  . GLN A 157 ? 0.2067 0.2872 0.0562 0.0210  -0.0027 -0.0122 158 GLN A CG  
1244 C  CD  . GLN A 157 ? 0.2136 0.2519 0.1138 -0.0057 -0.0210 -0.0029 158 GLN A CD  
1245 O  OE1 . GLN A 157 ? 0.2705 0.2836 0.0610 -0.0018 -0.0469 -0.0200 158 GLN A OE1 
1246 N  NE2 . GLN A 157 ? 0.1985 0.2773 0.0991 -0.0149 -0.0362 -0.0476 158 GLN A NE2 
1247 N  N   . LYS A 158 ? 0.1459 0.2372 0.0259 -0.0075 -0.0508 -0.0126 159 LYS A N   
1248 C  CA  . LYS A 158 ? 0.1661 0.2465 0.0646 -0.0179 -0.0510 0.0173  159 LYS A CA  
1249 C  C   . LYS A 158 ? 0.1756 0.2634 0.0508 -0.0359 -0.0584 0.0234  159 LYS A C   
1250 O  O   . LYS A 158 ? 0.1741 0.2771 0.0569 -0.0318 -0.0476 0.0096  159 LYS A O   
1251 C  CB  . LYS A 158 ? 0.2612 0.2444 0.1055 0.0075  -0.0727 0.0154  159 LYS A CB  
1252 C  CG  . LYS A 158 ? 0.4060 0.2730 0.2804 0.0687  -0.0787 0.0987  159 LYS A CG  
1253 C  CD  . LYS A 158 ? 0.4243 0.3698 0.1125 0.1223  -0.1368 0.0706  159 LYS A CD  
1254 C  CE  . LYS A 158 ? 0.5113 0.4268 0.2807 0.0848  -0.1357 0.1708  159 LYS A CE  
1255 N  NZ  . LYS A 158 ? 0.2690 0.4323 0.2956 -0.0200 -0.1239 0.1584  159 LYS A NZ  
1256 N  N   . VAL A 159 ? 0.1589 0.2289 0.0727 -0.0005 -0.0825 -0.0025 160 VAL A N   
1257 C  CA  . VAL A 159 ? 0.1599 0.2452 0.0527 -0.0044 -0.0619 -0.0117 160 VAL A CA  
1258 C  C   . VAL A 159 ? 0.1410 0.2072 0.0589 -0.0076 -0.0836 -0.0016 160 VAL A C   
1259 O  O   . VAL A 159 ? 0.1931 0.2563 0.1192 -0.0427 -0.0383 0.0073  160 VAL A O   
1260 C  CB  . VAL A 159 ? 0.1684 0.2414 0.0506 0.0110  -0.0604 0.0023  160 VAL A CB  
1261 C  CG1 . VAL A 159 ? 0.1743 0.2744 0.1429 0.0060  -0.0610 0.0011  160 VAL A CG1 
1262 C  CG2 . VAL A 159 ? 0.2283 0.2778 0.1151 0.0353  -0.0443 -0.0231 160 VAL A CG2 
1263 N  N   . VAL A 160 ? 0.1838 0.2045 0.0919 -0.0261 -0.0442 -0.0076 161 VAL A N   
1264 C  CA  . VAL A 160 ? 0.2388 0.2092 0.1055 -0.0161 -0.0137 -0.0230 161 VAL A CA  
1265 C  C   . VAL A 160 ? 0.1891 0.2601 0.1145 -0.0157 -0.0105 -0.0027 161 VAL A C   
1266 O  O   . VAL A 160 ? 0.2084 0.2379 0.0932 -0.0058 -0.0221 -0.0151 161 VAL A O   
1267 C  CB  . VAL A 160 ? 0.4052 0.2257 0.1068 0.0214  0.0251  0.0188  161 VAL A CB  
1268 C  CG1 . VAL A 160 ? 0.3108 0.2996 0.1730 -0.0351 -0.0099 -0.0431 161 VAL A CG1 
1269 C  CG2 . VAL A 160 ? 0.4833 0.2799 0.1120 0.1099  0.0192  0.0589  161 VAL A CG2 
1270 N  N   . ASP A 161 ? 0.1526 0.2315 0.0822 -0.0168 0.0052  -0.0392 162 ASP A N   
1271 C  CA  . ASP A 161 ? 0.2068 0.2888 0.0932 -0.0499 -0.0305 -0.0651 162 ASP A CA  
1272 C  C   . ASP A 161 ? 0.2312 0.2605 0.0833 -0.0163 -0.0379 -0.0414 162 ASP A C   
1273 O  O   . ASP A 161 ? 0.2920 0.3292 0.0925 -0.0330 0.0041  -0.0449 162 ASP A O   
1274 C  CB  . ASP A 161 ? 0.1953 0.3043 0.1477 -0.0381 -0.0097 -0.0598 162 ASP A CB  
1275 C  CG  . ASP A 161 ? 0.2875 0.3189 0.1223 -0.0725 -0.0364 -0.0225 162 ASP A CG  
1276 O  OD1 . ASP A 161 ? 0.3168 0.3565 0.2443 -0.0434 -0.0008 -0.0143 162 ASP A OD1 
1277 O  OD2 . ASP A 161 ? 0.3177 0.3529 0.2244 -0.0665 -0.0091 -0.0279 162 ASP A OD2 
1278 N  N   . VAL A 162 ? 0.1899 0.2504 0.0662 -0.0425 -0.0517 0.0006  163 VAL A N   
1279 C  CA  . VAL A 162 ? 0.1729 0.2605 0.0890 -0.0155 -0.0292 0.0147  163 VAL A CA  
1280 C  C   . VAL A 162 ? 0.1755 0.1971 0.1151 -0.0298 -0.0583 0.0061  163 VAL A C   
1281 O  O   . VAL A 162 ? 0.2064 0.2600 0.0540 -0.0190 -0.0365 0.0199  163 VAL A O   
1282 C  CB  . VAL A 162 ? 0.2098 0.2908 0.1884 0.0504  -0.0817 0.0132  163 VAL A CB  
1283 C  CG1 . VAL A 162 ? 0.1720 0.3318 0.2927 0.0148  -0.0342 0.0568  163 VAL A CG1 
1284 C  CG2 . VAL A 162 ? 0.2100 0.2348 0.1808 -0.0238 0.0253  -0.0164 163 VAL A CG2 
1285 N  N   . LEU A 163 ? 0.1586 0.2269 0.0657 -0.0096 -0.0095 0.0088  164 LEU A N   
1286 C  CA  . LEU A 163 ? 0.1363 0.2463 0.1018 -0.0558 -0.0047 0.0250  164 LEU A CA  
1287 C  C   . LEU A 163 ? 0.1985 0.2849 0.0826 0.0117  -0.0206 0.0150  164 LEU A C   
1288 O  O   . LEU A 163 ? 0.2188 0.2314 0.0572 -0.0067 -0.0336 0.0114  164 LEU A O   
1289 C  CB  . LEU A 163 ? 0.2002 0.2711 0.0411 -0.0166 -0.0079 0.0100  164 LEU A CB  
1290 C  CG  . LEU A 163 ? 0.2136 0.2400 0.0413 -0.0013 -0.0179 0.0078  164 LEU A CG  
1291 C  CD1 . LEU A 163 ? 0.2035 0.2624 0.1368 -0.0025 -0.0324 0.0597  164 LEU A CD1 
1292 C  CD2 . LEU A 163 ? 0.1773 0.2547 0.1012 0.0000  -0.0083 0.0157  164 LEU A CD2 
1293 N  N   . ASP A 164 ? 0.2684 0.2603 0.0394 -0.0098 0.0228  0.0032  165 ASP A N   
1294 C  CA  . ASP A 164 ? 0.2427 0.3039 0.0405 -0.0044 0.0070  -0.0221 165 ASP A CA  
1295 C  C   . ASP A 164 ? 0.2688 0.3029 0.0486 -0.0146 -0.0055 -0.0348 165 ASP A C   
1296 O  O   . ASP A 164 ? 0.2891 0.3769 0.0754 0.0083  0.0130  -0.0252 165 ASP A O   
1297 C  CB  . ASP A 164 ? 0.3092 0.4654 0.0810 -0.0564 0.0452  -0.1250 165 ASP A CB  
1298 C  CG  . ASP A 164 ? 0.3713 0.6538 0.2322 -0.0150 -0.0293 -0.1059 165 ASP A CG  
1299 O  OD1 . ASP A 164 ? 0.2807 0.8362 0.2294 -0.1922 0.0381  -0.1722 165 ASP A OD1 
1300 O  OD2 . ASP A 164 ? 0.4820 0.7648 0.2157 -0.0757 0.0599  -0.1882 165 ASP A OD2 
1301 N  N   . SER A 165 ? 0.2276 0.2967 0.0345 -0.0205 -0.0289 0.0003  166 SER A N   
1302 C  CA  . SER A 165 ? 0.2190 0.3070 0.0454 -0.0010 -0.0109 0.0307  166 SER A CA  
1303 C  C   . SER A 165 ? 0.2352 0.2629 0.0563 -0.0094 -0.0196 0.0440  166 SER A C   
1304 O  O   . SER A 165 ? 0.2441 0.3031 0.0540 -0.0218 -0.0318 0.0510  166 SER A O   
1305 C  CB  . SER A 165 ? 0.2459 0.3829 0.0575 0.0380  0.0446  0.0491  166 SER A CB  
1306 O  OG  . SER A 165 ? 0.2531 0.3248 0.1095 0.0119  0.0188  0.0120  166 SER A OG  
1307 N  N   . ILE A 166 ? 0.1949 0.2301 0.0463 -0.0237 -0.0283 0.0221  167 ILE A N   
1308 C  CA  . ILE A 166 ? 0.1761 0.1949 0.1332 0.0027  -0.0125 -0.0282 167 ILE A CA  
1309 C  C   . ILE A 166 ? 0.1615 0.2052 0.0339 -0.0020 -0.0206 -0.0242 167 ILE A C   
1310 O  O   . ILE A 166 ? 0.1594 0.2264 0.0443 -0.0141 -0.0361 -0.0030 167 ILE A O   
1311 C  CB  . ILE A 166 ? 0.1425 0.2042 0.1270 0.0019  -0.0022 -0.0089 167 ILE A CB  
1312 C  CG1 . ILE A 166 ? 0.1930 0.1913 0.0639 -0.0157 -0.0377 -0.0001 167 ILE A CG1 
1313 C  CG2 . ILE A 166 ? 0.2154 0.1960 0.1676 0.0301  0.0041  0.0155  167 ILE A CG2 
1314 C  CD1 . ILE A 166 ? 0.2055 0.2111 0.0910 -0.0136 -0.0017 -0.0397 167 ILE A CD1 
1315 N  N   . LYS A 167 ? 0.2017 0.1906 0.1041 0.0225  0.0336  -0.0107 168 LYS A N   
1316 C  CA  . LYS A 167 ? 0.1831 0.1903 0.1113 0.0168  0.0036  -0.0392 168 LYS A CA  
1317 C  C   . LYS A 167 ? 0.2036 0.1896 0.1195 -0.0085 -0.0157 0.0247  168 LYS A C   
1318 O  O   . LYS A 167 ? 0.1902 0.2055 0.0719 -0.0036 0.0104  0.0081  168 LYS A O   
1319 C  CB  . LYS A 167 ? 0.2125 0.2643 0.1037 0.0292  -0.0219 -0.0717 168 LYS A CB  
1320 C  CG  . LYS A 167 ? 0.2768 0.2524 0.1485 0.0504  -0.0080 -0.0811 168 LYS A CG  
1321 C  CD  . LYS A 167 ? 0.3806 0.3615 0.0994 0.0685  -0.0366 -0.0922 168 LYS A CD  
1322 C  CE  . LYS A 167 ? 0.4674 0.4289 0.3110 0.1044  0.0522  -0.0267 168 LYS A CE  
1323 N  NZ  . LYS A 167 ? 0.4785 0.5346 0.4689 0.0897  0.1597  0.0256  168 LYS A NZ  
1324 N  N   . THR A 168 ? 0.1536 0.2050 0.0961 -0.0003 -0.0166 0.0209  169 THR A N   
1325 C  CA  . THR A 168 ? 0.1457 0.2151 0.1174 -0.0215 0.0212  -0.0088 169 THR A CA  
1326 C  C   . THR A 168 ? 0.1761 0.2240 0.0752 0.0017  0.0253  0.0005  169 THR A C   
1327 O  O   . THR A 168 ? 0.1734 0.2251 0.0792 0.0013  0.0089  -0.0011 169 THR A O   
1328 C  CB  . THR A 168 ? 0.2007 0.2287 0.0928 0.0145  0.0197  0.0175  169 THR A CB  
1329 O  OG1 . THR A 168 ? 0.1884 0.2760 0.1077 0.0286  0.0210  0.0330  169 THR A OG1 
1330 C  CG2 . THR A 168 ? 0.2698 0.2460 0.1165 0.0302  0.0185  -0.0030 169 THR A CG2 
1331 N  N   . LYS A 169 ? 0.1697 0.2390 0.1186 -0.0368 0.0192  -0.0207 170 LYS A N   
1332 C  CA  . LYS A 169 ? 0.1682 0.2355 0.1460 -0.0008 -0.0025 -0.0302 170 LYS A CA  
1333 C  C   . LYS A 169 ? 0.1783 0.2418 0.1400 -0.0233 0.0054  -0.0370 170 LYS A C   
1334 O  O   . LYS A 169 ? 0.1752 0.2606 0.1360 0.0081  0.0049  0.0072  170 LYS A O   
1335 C  CB  . LYS A 169 ? 0.2046 0.2591 0.0874 -0.0256 -0.0434 -0.0053 170 LYS A CB  
1336 C  CG  . LYS A 169 ? 0.1951 0.2868 0.1540 -0.0370 -0.0414 -0.0414 170 LYS A CG  
1337 C  CD  . LYS A 169 ? 0.2017 0.3537 0.2258 -0.0282 -0.0703 -0.0358 170 LYS A CD  
1338 C  CE  . LYS A 169 ? 0.4289 0.4432 0.4342 -0.0935 -0.1948 -0.0754 170 LYS A CE  
1339 N  NZ  . LYS A 169 ? 0.2773 0.5219 0.6054 -0.0942 -0.0672 0.0925  170 LYS A NZ  
1340 N  N   . GLY A 170 ? 0.2031 0.2415 0.1350 -0.0048 0.0329  -0.0003 171 GLY A N   
1341 C  CA  . GLY A 170 ? 0.1946 0.2189 0.1500 -0.0414 -0.0175 -0.0262 171 GLY A CA  
1342 C  C   . GLY A 170 ? 0.1914 0.2165 0.1783 -0.0184 -0.0258 -0.0291 171 GLY A C   
1343 O  O   . GLY A 170 ? 0.2261 0.2279 0.2685 0.0059  0.0376  -0.0042 171 GLY A O   
1344 N  N   . LYS A 171 ? 0.1374 0.2441 0.1281 -0.0234 0.0369  -0.0245 172 LYS A N   
1345 C  CA  . LYS A 171 ? 0.1630 0.2397 0.1158 -0.0211 0.0229  0.0012  172 LYS A CA  
1346 C  C   . LYS A 171 ? 0.1960 0.2533 0.0770 0.0182  0.0233  0.0241  172 LYS A C   
1347 O  O   . LYS A 171 ? 0.1842 0.2595 0.0643 -0.0071 -0.0055 0.0115  172 LYS A O   
1348 C  CB  . LYS A 171 ? 0.2283 0.2420 0.0714 -0.0309 0.0606  -0.0126 172 LYS A CB  
1349 C  CG  . LYS A 171 ? 0.2149 0.2799 0.0380 0.0508  0.0125  -0.0229 172 LYS A CG  
1350 C  CD  . LYS A 171 ? 0.2625 0.2579 0.0994 0.0019  0.0377  0.0092  172 LYS A CD  
1351 C  CE  . LYS A 171 ? 0.3529 0.2866 0.2663 0.0127  -0.0684 0.0583  172 LYS A CE  
1352 N  NZ  . LYS A 171 ? 0.5493 0.4133 0.1759 -0.1617 0.1152  0.0002  172 LYS A NZ  
1353 N  N   . SER A 172 ? 0.1991 0.2372 0.0666 0.0186  0.0015  -0.0019 173 SER A N   
1354 C  CA  . SER A 172 ? 0.1576 0.2240 0.1363 0.0037  0.0136  0.0272  173 SER A CA  
1355 C  C   . SER A 172 ? 0.2284 0.2408 0.0387 0.0111  0.0223  0.0417  173 SER A C   
1356 O  O   . SER A 172 ? 0.2827 0.2910 0.0405 0.0095  0.0389  0.0304  173 SER A O   
1357 C  CB  . SER A 172 ? 0.2370 0.2315 0.1729 0.0055  0.0299  0.0054  173 SER A CB  
1358 O  OG  . SER A 172 ? 0.2365 0.2389 0.1878 0.0013  -0.0017 0.0253  173 SER A OG  
1359 N  N   . ALA A 173 ? 0.1895 0.2795 0.0348 0.0441  -0.0226 0.0337  174 ALA A N   
1360 C  CA  . ALA A 173 ? 0.2014 0.3501 0.0766 0.0757  -0.0439 0.0214  174 ALA A CA  
1361 C  C   . ALA A 173 ? 0.2035 0.3607 0.0513 0.0697  -0.0116 0.0309  174 ALA A C   
1362 O  O   . ALA A 173 ? 0.2462 0.2973 0.0497 0.0245  0.0019  0.0298  174 ALA A O   
1363 C  CB  . ALA A 173 ? 0.2147 0.4127 0.1016 0.0402  -0.0683 -0.0186 174 ALA A CB  
1364 N  N   . ASP A 174 ? 0.2350 0.3654 0.1077 0.0938  -0.0284 0.0531  175 ASP A N   
1365 C  CA  . ASP A 174 ? 0.2187 0.3860 0.0860 0.0835  -0.0363 0.0475  175 ASP A CA  
1366 C  C   . ASP A 174 ? 0.1999 0.3700 0.0815 0.0789  -0.0267 0.0111  175 ASP A C   
1367 O  O   . ASP A 174 ? 0.2414 0.3928 0.1224 0.0797  0.0054  -0.0226 175 ASP A O   
1368 C  CB  . ASP A 174 ? 0.3227 0.4396 0.2336 0.1583  -0.0841 0.0859  175 ASP A CB  
1369 C  CG  . ASP A 174 ? 0.4564 0.4188 0.2393 0.1474  -0.0682 0.0104  175 ASP A CG  
1370 O  OD1 . ASP A 174 ? 0.6053 0.6790 0.1939 0.0732  -0.0944 -0.0397 175 ASP A OD1 
1371 O  OD2 . ASP A 174 ? 0.7227 0.8444 0.2834 0.2691  0.0200  0.1167  175 ASP A OD2 
1372 N  N   . PHE A 175 ? 0.2142 0.2865 0.0817 0.0496  -0.0206 0.0083  176 PHE A N   
1373 C  CA  . PHE A 175 ? 0.2013 0.2445 0.1057 0.0575  -0.0491 -0.0011 176 PHE A CA  
1374 C  C   . PHE A 175 ? 0.1931 0.2655 0.0693 0.0525  -0.0469 0.0024  176 PHE A C   
1375 O  O   . PHE A 175 ? 0.2018 0.3033 0.0675 0.0344  -0.0212 -0.0080 176 PHE A O   
1376 C  CB  . PHE A 175 ? 0.1944 0.2462 0.0682 0.0501  -0.0116 0.0229  176 PHE A CB  
1377 C  CG  . PHE A 175 ? 0.1565 0.2431 0.0811 0.0293  -0.0074 0.0150  176 PHE A CG  
1378 C  CD1 . PHE A 175 ? 0.1980 0.2835 0.0867 0.0146  -0.0258 0.0151  176 PHE A CD1 
1379 C  CD2 . PHE A 175 ? 0.1583 0.2797 0.0809 0.0143  -0.0223 0.0344  176 PHE A CD2 
1380 C  CE1 . PHE A 175 ? 0.2401 0.2532 0.1258 0.0341  -0.0236 0.0006  176 PHE A CE1 
1381 C  CE2 . PHE A 175 ? 0.1666 0.2273 0.1352 0.0103  -0.0370 -0.0066 176 PHE A CE2 
1382 C  CZ  . PHE A 175 ? 0.1787 0.2057 0.1244 0.0273  -0.0193 -0.0009 176 PHE A CZ  
1383 N  N   . THR A 176 ? 0.1748 0.2641 0.1238 0.0443  -0.0544 0.0088  177 THR A N   
1384 C  CA  . THR A 176 ? 0.1686 0.2664 0.1263 0.0323  -0.0237 0.0276  177 THR A CA  
1385 C  C   . THR A 176 ? 0.1748 0.2244 0.0743 0.0370  -0.0763 0.0343  177 THR A C   
1386 O  O   . THR A 176 ? 0.1942 0.2495 0.1504 0.0388  -0.0460 0.0085  177 THR A O   
1387 C  CB  . THR A 176 ? 0.2604 0.2758 0.1538 0.0011  -0.0273 0.0405  177 THR A CB  
1388 O  OG1 . THR A 176 ? 0.3462 0.2681 0.1235 0.0501  -0.0467 0.0163  177 THR A OG1 
1389 C  CG2 . THR A 176 ? 0.2379 0.3415 0.2605 0.0049  -0.0299 0.1456  177 THR A CG2 
1390 N  N   . ASN A 177 ? 0.1582 0.2283 0.0836 0.0171  -0.0625 0.0392  178 ASN A N   
1391 C  CA  . ASN A 177 ? 0.1737 0.2601 0.1210 -0.0102 -0.0939 0.0319  178 ASN A CA  
1392 C  C   . ASN A 177 ? 0.1644 0.2358 0.1242 -0.0018 -0.0515 0.0206  178 ASN A C   
1393 O  O   . ASN A 177 ? 0.2167 0.2879 0.2572 -0.0367 -0.1164 0.0796  178 ASN A O   
1394 C  CB  . ASN A 177 ? 0.2461 0.2289 0.1662 -0.0265 -0.1476 0.0427  178 ASN A CB  
1395 C  CG  . ASN A 177 ? 0.2344 0.2559 0.1919 0.0150  -0.1294 0.0496  178 ASN A CG  
1396 O  OD1 . ASN A 177 ? 0.2792 0.2986 0.2632 0.0306  -0.0539 0.0586  178 ASN A OD1 
1397 N  ND2 . ASN A 177 ? 0.2603 0.3435 0.1856 -0.0333 -0.1637 0.0862  178 ASN A ND2 
1398 N  N   . PHE A 178 ? 0.1830 0.2309 0.0939 0.0225  -0.0606 0.0275  179 PHE A N   
1399 C  CA  . PHE A 178 ? 0.1905 0.2539 0.0585 0.0110  -0.0288 0.0374  179 PHE A CA  
1400 C  C   . PHE A 178 ? 0.1964 0.2576 0.0567 -0.0013 -0.0451 0.0111  179 PHE A C   
1401 O  O   . PHE A 178 ? 0.2366 0.2505 0.1052 -0.0110 -0.0346 0.0029  179 PHE A O   
1402 C  CB  . PHE A 178 ? 0.1876 0.2416 0.1607 0.0274  -0.0042 0.0425  179 PHE A CB  
1403 C  CG  . PHE A 178 ? 0.2081 0.2559 0.0685 0.0280  -0.0462 0.0239  179 PHE A CG  
1404 C  CD1 . PHE A 178 ? 0.1829 0.2445 0.1378 0.0047  -0.0168 0.0303  179 PHE A CD1 
1405 C  CD2 . PHE A 178 ? 0.1490 0.2376 0.0820 0.0165  -0.0556 -0.0069 179 PHE A CD2 
1406 C  CE1 . PHE A 178 ? 0.2194 0.2612 0.0428 -0.0325 -0.0499 0.0134  179 PHE A CE1 
1407 C  CE2 . PHE A 178 ? 0.1734 0.2287 0.1528 0.0092  -0.0569 0.0008  179 PHE A CE2 
1408 C  CZ  . PHE A 178 ? 0.1529 0.2667 0.0584 0.0098  -0.0644 -0.0182 179 PHE A CZ  
1409 N  N   . ASP A 179 ? 0.1630 0.2551 0.0700 0.0024  -0.0370 -0.0099 180 ASP A N   
1410 C  CA  . ASP A 179 ? 0.1518 0.2477 0.0917 0.0292  -0.0345 -0.0337 180 ASP A CA  
1411 C  C   . ASP A 179 ? 0.1618 0.2168 0.0822 0.0167  -0.0020 -0.0146 180 ASP A C   
1412 O  O   . ASP A 179 ? 0.1992 0.2353 0.1032 0.0000  0.0060  -0.0097 180 ASP A O   
1413 C  CB  . ASP A 179 ? 0.1478 0.2958 0.1210 0.0206  -0.0266 -0.0146 180 ASP A CB  
1414 C  CG  . ASP A 179 ? 0.1801 0.3243 0.1445 0.0003  -0.0196 -0.0488 180 ASP A CG  
1415 O  OD1 . ASP A 179 ? 0.2212 0.2778 0.1018 0.0222  -0.0301 -0.0061 180 ASP A OD1 
1416 O  OD2 . ASP A 179 ? 0.1951 0.4860 0.2232 0.0166  -0.0156 -0.0092 180 ASP A OD2 
1417 N  N   . PRO A 180 ? 0.1790 0.2231 0.0524 0.0066  -0.0142 0.0276  181 PRO A N   
1418 C  CA  . PRO A 180 ? 0.1956 0.2444 0.0495 0.0054  -0.0286 0.0311  181 PRO A CA  
1419 C  C   . PRO A 180 ? 0.1745 0.2769 0.0259 0.0179  -0.0299 0.0126  181 PRO A C   
1420 O  O   . PRO A 180 ? 0.1885 0.2391 0.1084 0.0401  -0.0544 0.0054  181 PRO A O   
1421 C  CB  . PRO A 180 ? 0.1910 0.2474 0.0899 -0.0030 -0.0159 0.0059  181 PRO A CB  
1422 C  CG  . PRO A 180 ? 0.2030 0.2865 0.0247 0.0319  -0.0399 0.0119  181 PRO A CG  
1423 C  CD  . PRO A 180 ? 0.1982 0.2269 0.0292 0.0039  -0.0401 0.0266  181 PRO A CD  
1424 N  N   . ARG A 181 ? 0.1722 0.2404 0.0463 0.0119  -0.0001 0.0022  182 ARG A N   
1425 C  CA  . ARG A 181 ? 0.1350 0.2396 0.0831 0.0168  -0.0236 0.0188  182 ARG A CA  
1426 C  C   . ARG A 181 ? 0.1539 0.2329 0.1068 0.0103  -0.0196 -0.0054 182 ARG A C   
1427 O  O   . ARG A 181 ? 0.1687 0.2490 0.1349 0.0026  -0.0331 0.0187  182 ARG A O   
1428 C  CB  . ARG A 181 ? 0.1758 0.2445 0.1949 0.0600  0.0288  0.0103  182 ARG A CB  
1429 C  CG  . ARG A 181 ? 0.2165 0.2665 0.1312 0.0322  0.0403  0.0025  182 ARG A CG  
1430 C  CD  . ARG A 181 ? 0.2318 0.2409 0.2836 0.0368  0.0229  0.0039  182 ARG A CD  
1431 N  NE  . ARG A 181 ? 0.2169 0.2841 0.2777 0.0222  0.0302  0.0278  182 ARG A NE  
1432 C  CZ  . ARG A 181 ? 0.1935 0.3063 0.3308 0.0455  0.0354  -0.0378 182 ARG A CZ  
1433 N  NH1 . ARG A 181 ? 0.2677 0.3962 0.4623 0.1218  0.1251  0.0190  182 ARG A NH1 
1434 N  NH2 . ARG A 181 ? 0.3010 0.4095 0.3594 0.1013  0.0157  0.0296  182 ARG A NH2 
1435 N  N   . GLY A 182 ? 0.1604 0.2365 0.0822 0.0114  -0.0521 0.0006  183 GLY A N   
1436 C  CA  . GLY A 182 ? 0.1860 0.2364 0.0704 0.0314  -0.0590 0.0296  183 GLY A CA  
1437 C  C   . GLY A 182 ? 0.1359 0.2228 0.0675 0.0027  -0.0456 0.0270  183 GLY A C   
1438 O  O   . GLY A 182 ? 0.1793 0.2376 0.1220 0.0195  -0.0413 0.0166  183 GLY A O   
1439 N  N   . LEU A 183 ? 0.1515 0.2455 0.1016 0.0011  -0.0496 -0.0210 184 LEU A N   
1440 C  CA  . LEU A 183 ? 0.1542 0.2328 0.0677 0.0099  -0.0137 -0.0174 184 LEU A CA  
1441 C  C   . LEU A 183 ? 0.1427 0.2082 0.0648 0.0133  -0.0331 -0.0225 184 LEU A C   
1442 O  O   . LEU A 183 ? 0.1353 0.2856 0.1416 0.0283  -0.0374 0.0211  184 LEU A O   
1443 C  CB  . LEU A 183 ? 0.1467 0.2738 0.0597 -0.0004 -0.0290 0.0095  184 LEU A CB  
1444 C  CG  . LEU A 183 ? 0.1993 0.2494 0.0718 0.0074  -0.0141 0.0232  184 LEU A CG  
1445 C  CD1 . LEU A 183 ? 0.1711 0.2937 0.1360 -0.0102 -0.0509 0.0398  184 LEU A CD1 
1446 C  CD2 . LEU A 183 ? 0.1928 0.2909 0.1270 0.0409  -0.0295 -0.0282 184 LEU A CD2 
1447 N  N   . LEU A 184 ? 0.1562 0.2522 0.0372 0.0104  -0.0253 -0.0048 185 LEU A N   
1448 C  CA  . LEU A 184 ? 0.2080 0.2176 0.0370 0.0032  -0.0312 -0.0004 185 LEU A CA  
1449 C  C   . LEU A 184 ? 0.2082 0.2073 0.1284 0.0040  -0.0179 0.0176  185 LEU A C   
1450 O  O   . LEU A 184 ? 0.2319 0.2960 0.0996 -0.0298 -0.0279 0.0061  185 LEU A O   
1451 C  CB  . LEU A 184 ? 0.2217 0.2398 0.0759 -0.0114 -0.0275 -0.0603 185 LEU A CB  
1452 C  CG  . LEU A 184 ? 0.1852 0.2501 0.1522 -0.0116 -0.0558 0.0079  185 LEU A CG  
1453 C  CD1 . LEU A 184 ? 0.2152 0.3018 0.1585 0.0273  -0.0210 0.0306  185 LEU A CD1 
1454 C  CD2 . LEU A 184 ? 0.1823 0.3321 0.1515 0.0230  -0.0696 0.0273  185 LEU A CD2 
1455 N  N   . PRO A 185 ? 0.1855 0.2233 0.0731 0.0058  -0.0240 -0.0254 186 PRO A N   
1456 C  CA  . PRO A 185 ? 0.1615 0.2505 0.0822 0.0008  -0.0496 0.0054  186 PRO A CA  
1457 C  C   . PRO A 185 ? 0.1367 0.2388 0.0646 0.0035  -0.0751 0.0138  186 PRO A C   
1458 O  O   . PRO A 185 ? 0.1718 0.2411 0.1253 -0.0154 -0.0365 0.0236  186 PRO A O   
1459 C  CB  . PRO A 185 ? 0.1723 0.2512 0.1165 0.0044  -0.0326 0.0604  186 PRO A CB  
1460 C  CG  . PRO A 185 ? 0.1937 0.2594 0.1324 -0.0270 0.0140  0.0292  186 PRO A CG  
1461 C  CD  . PRO A 185 ? 0.1682 0.2023 0.1043 -0.0111 -0.0189 -0.0029 186 PRO A CD  
1462 N  N   . GLU A 186 ? 0.1928 0.2773 0.0944 -0.0417 -0.0469 0.0144  187 GLU A N   
1463 C  CA  . GLU A 186 ? 0.1745 0.2929 0.1270 -0.0736 -0.0564 -0.0467 187 GLU A CA  
1464 C  C   . GLU A 186 ? 0.1712 0.2606 0.0603 0.0001  -0.0253 -0.0044 187 GLU A C   
1465 O  O   . GLU A 186 ? 0.2136 0.3257 0.1113 0.0407  -0.0553 -0.0247 187 GLU A O   
1466 C  CB  . GLU A 186 ? 0.1971 0.2849 0.1520 -0.0643 -0.0687 0.0085  187 GLU A CB  
1467 C  CG  . GLU A 186 ? 0.2503 0.3563 0.1465 -0.0961 -0.0842 0.0263  187 GLU A CG  
1468 C  CD  . GLU A 186 ? 0.3565 0.3296 0.2582 -0.0765 -0.0254 0.0499  187 GLU A CD  
1469 O  OE1 . GLU A 186 ? 0.3524 0.3739 0.2527 -0.1200 -0.0231 0.1043  187 GLU A OE1 
1470 O  OE2 . GLU A 186 ? 0.4467 0.3818 0.3353 -0.0895 -0.0559 -0.0102 187 GLU A OE2 
1471 N  N   . SER A 187 ? 0.1716 0.2885 0.1581 -0.0100 -0.0643 0.0219  188 SER A N   
1472 C  CA  . SER A 187 ? 0.2146 0.2975 0.1454 -0.0179 -0.0160 -0.0061 188 SER A CA  
1473 C  C   . SER A 187 ? 0.1738 0.3021 0.1080 -0.0024 -0.0370 -0.0040 188 SER A C   
1474 O  O   . SER A 187 ? 0.1716 0.2916 0.1109 -0.0164 -0.0256 -0.0132 188 SER A O   
1475 C  CB  . SER A 187 ? 0.2174 0.3199 0.1161 -0.0421 -0.0510 -0.0067 188 SER A CB  
1476 O  OG  . SER A 187 ? 0.1928 0.3497 0.1274 -0.0798 -0.0637 -0.0096 188 SER A OG  
1477 N  N   . LEU A 188 ? 0.1493 0.2888 0.1438 -0.0043 -0.0402 -0.0122 189 LEU A N   
1478 C  CA  . LEU A 188 ? 0.2082 0.2745 0.0679 -0.0138 -0.0609 0.0355  189 LEU A CA  
1479 C  C   . LEU A 188 ? 0.2258 0.3165 0.0104 0.0047  -0.0128 -0.0324 189 LEU A C   
1480 O  O   . LEU A 188 ? 0.2156 0.3373 0.1265 -0.0135 -0.0234 -0.0037 189 LEU A O   
1481 C  CB  . LEU A 188 ? 0.2111 0.2931 0.1270 0.0044  -0.0473 0.0006  189 LEU A CB  
1482 C  CG  . LEU A 188 ? 0.2096 0.2865 0.1339 0.0127  -0.0504 0.0069  189 LEU A CG  
1483 C  CD1 . LEU A 188 ? 0.2442 0.2988 0.2244 0.0263  -0.0695 0.0450  189 LEU A CD1 
1484 C  CD2 . LEU A 188 ? 0.1939 0.3946 0.1478 0.0312  -0.0608 0.0670  189 LEU A CD2 
1485 N  N   . ASP A 189 ? 0.1508 0.3077 0.0785 0.0121  -0.0570 -0.0075 190 ASP A N   
1486 C  CA  . ASP A 189 ? 0.1443 0.3129 0.0469 -0.0198 -0.0446 -0.0347 190 ASP A CA  
1487 C  C   . ASP A 189 ? 0.1319 0.2832 0.0678 0.0099  -0.0370 -0.0168 190 ASP A C   
1488 O  O   . ASP A 189 ? 0.1506 0.3128 0.0604 0.0080  -0.0217 0.0024  190 ASP A O   
1489 C  CB  . ASP A 189 ? 0.1935 0.3422 0.1208 -0.0592 -0.0411 -0.0187 190 ASP A CB  
1490 C  CG  . ASP A 189 ? 0.2310 0.3782 0.0251 -0.0446 -0.0385 -0.0300 190 ASP A CG  
1491 O  OD1 . ASP A 189 ? 0.2466 0.4921 0.1696 -0.0062 0.0543  -0.0805 190 ASP A OD1 
1492 O  OD2 . ASP A 189 ? 0.3370 0.4510 0.1908 -0.1226 -0.0513 0.0998  190 ASP A OD2 
1493 N  N   . TYR A 190 ? 0.1628 0.2764 0.0544 -0.0201 -0.0431 0.0212  191 TYR A N   
1494 C  CA  . TYR A 190 ? 0.1454 0.2400 0.0643 0.0000  -0.0436 0.0189  191 TYR A CA  
1495 C  C   . TYR A 190 ? 0.1457 0.2523 0.0319 0.0119  -0.0207 -0.0081 191 TYR A C   
1496 O  O   . TYR A 190 ? 0.1662 0.2612 0.0423 -0.0040 0.0011  -0.0080 191 TYR A O   
1497 C  CB  . TYR A 190 ? 0.1697 0.2253 0.0861 -0.0217 0.0061  -0.0108 191 TYR A CB  
1498 C  CG  . TYR A 190 ? 0.1999 0.2671 0.0124 -0.0019 -0.0317 -0.0150 191 TYR A CG  
1499 C  CD1 . TYR A 190 ? 0.2390 0.2708 0.0294 -0.0033 -0.0729 0.0080  191 TYR A CD1 
1500 C  CD2 . TYR A 190 ? 0.2171 0.2743 0.0545 0.0303  0.0355  0.0140  191 TYR A CD2 
1501 C  CE1 . TYR A 190 ? 0.2275 0.2898 0.0773 0.0286  0.0025  0.0204  191 TYR A CE1 
1502 C  CE2 . TYR A 190 ? 0.2096 0.2690 0.0173 -0.0206 -0.0354 -0.0027 191 TYR A CE2 
1503 C  CZ  . TYR A 190 ? 0.1896 0.2614 0.0553 -0.0271 -0.0197 -0.0240 191 TYR A CZ  
1504 O  OH  . TYR A 190 ? 0.2573 0.2854 0.0418 0.0179  -0.0146 -0.0253 191 TYR A OH  
1505 N  N   . TRP A 191 ? 0.1389 0.2271 0.0312 -0.0179 -0.0266 -0.0096 192 TRP A N   
1506 C  CA  . TRP A 191 ? 0.1651 0.2474 0.0560 -0.0295 -0.0457 -0.0262 192 TRP A CA  
1507 C  C   . TRP A 191 ? 0.1590 0.2715 0.0505 -0.0479 0.0039  -0.0154 192 TRP A C   
1508 O  O   . TRP A 191 ? 0.2036 0.2476 0.0630 -0.0359 0.0083  0.0006  192 TRP A O   
1509 C  CB  . TRP A 191 ? 0.2279 0.2386 0.0103 -0.0201 -0.0296 -0.0024 192 TRP A CB  
1510 C  CG  . TRP A 191 ? 0.1665 0.2300 0.0862 0.0039  -0.0348 0.0063  192 TRP A CG  
1511 C  CD1 . TRP A 191 ? 0.1313 0.2516 0.1039 -0.0207 -0.0239 0.0247  192 TRP A CD1 
1512 C  CD2 . TRP A 191 ? 0.1964 0.2384 0.0242 -0.0175 -0.0377 0.0143  192 TRP A CD2 
1513 N  NE1 . TRP A 191 ? 0.1982 0.2441 0.0944 -0.0100 0.0010  -0.0011 192 TRP A NE1 
1514 C  CE2 . TRP A 191 ? 0.1608 0.2244 0.0849 0.0040  -0.0413 0.0181  192 TRP A CE2 
1515 C  CE3 . TRP A 191 ? 0.2127 0.2617 0.0364 0.0158  -0.0344 -0.0172 192 TRP A CE3 
1516 C  CZ2 . TRP A 191 ? 0.2056 0.2132 0.0976 -0.0139 -0.0514 0.0332  192 TRP A CZ2 
1517 C  CZ3 . TRP A 191 ? 0.1996 0.2635 0.0858 -0.0146 -0.0321 -0.0044 192 TRP A CZ3 
1518 C  CH2 . TRP A 191 ? 0.2091 0.2752 0.0858 -0.0276 -0.0943 0.0282  192 TRP A CH2 
1519 N  N   . THR A 192 ? 0.1960 0.1923 0.0680 -0.0089 -0.0395 0.0050  193 THR A N   
1520 C  CA  . THR A 192 ? 0.1738 0.2097 0.0259 -0.0148 -0.0344 -0.0119 193 THR A CA  
1521 C  C   . THR A 192 ? 0.1502 0.2141 0.0657 -0.0177 -0.0378 0.0294  193 THR A C   
1522 O  O   . THR A 192 ? 0.2242 0.2777 0.0436 -0.0320 -0.0147 0.0124  193 THR A O   
1523 C  CB  . THR A 192 ? 0.1935 0.2088 0.0321 -0.0061 -0.0118 -0.0168 193 THR A CB  
1524 O  OG1 . THR A 192 ? 0.1938 0.2261 0.0979 -0.0152 -0.0074 0.0048  193 THR A OG1 
1525 C  CG2 . THR A 192 ? 0.2310 0.2272 0.0265 -0.0087 -0.0146 -0.0226 193 THR A CG2 
1526 N  N   . TYR A 193 ? 0.1594 0.2772 0.0380 -0.0458 -0.0508 0.0225  194 TYR A N   
1527 C  CA  . TYR A 193 ? 0.1636 0.2301 0.0220 -0.0218 -0.0489 -0.0027 194 TYR A CA  
1528 C  C   . TYR A 193 ? 0.1873 0.2549 0.0551 -0.0398 -0.0099 -0.0003 194 TYR A C   
1529 O  O   . TYR A 193 ? 0.1747 0.2163 0.0682 -0.0170 -0.0444 0.0006  194 TYR A O   
1530 C  CB  . TYR A 193 ? 0.1999 0.2398 0.0349 0.0107  -0.0205 -0.0100 194 TYR A CB  
1531 C  CG  . TYR A 193 ? 0.1626 0.2118 0.0445 -0.0171 -0.0269 -0.0085 194 TYR A CG  
1532 C  CD1 . TYR A 193 ? 0.1885 0.2248 0.0252 -0.0124 -0.0494 0.0135  194 TYR A CD1 
1533 C  CD2 . TYR A 193 ? 0.1502 0.2187 0.0576 0.0055  -0.0201 0.0133  194 TYR A CD2 
1534 C  CE1 . TYR A 193 ? 0.1357 0.2404 0.0725 0.0017  -0.0182 0.0276  194 TYR A CE1 
1535 C  CE2 . TYR A 193 ? 0.1612 0.2351 0.0612 -0.0263 -0.0266 -0.0212 194 TYR A CE2 
1536 C  CZ  . TYR A 193 ? 0.1353 0.2373 0.0311 -0.0181 -0.0231 -0.0042 194 TYR A CZ  
1537 O  OH  . TYR A 193 ? 0.1745 0.2363 0.0369 -0.0084 -0.0199 -0.0066 194 TYR A OH  
1538 N  N   . PRO A 194 ? 0.2113 0.2369 0.0292 -0.0249 -0.0200 0.0127  195 PRO A N   
1539 C  CA  . PRO A 194 ? 0.2230 0.2075 0.0797 -0.0378 -0.0364 -0.0286 195 PRO A CA  
1540 C  C   . PRO A 194 ? 0.1921 0.1939 0.0810 -0.0177 -0.0226 0.0343  195 PRO A C   
1541 O  O   . PRO A 194 ? 0.2061 0.2431 0.0486 0.0008  -0.0440 -0.0049 195 PRO A O   
1542 C  CB  . PRO A 194 ? 0.2156 0.2379 0.0944 -0.0661 -0.0174 -0.0560 195 PRO A CB  
1543 C  CG  . PRO A 194 ? 0.2531 0.3332 0.0892 -0.0983 -0.0168 -0.0134 195 PRO A CG  
1544 C  CD  . PRO A 194 ? 0.1906 0.3083 0.0231 -0.0514 -0.0105 -0.0065 195 PRO A CD  
1545 N  N   . GLY A 195 ? 0.1439 0.2174 0.0754 -0.0237 -0.0325 0.0251  196 GLY A N   
1546 C  CA  . GLY A 195 ? 0.1819 0.2305 0.0653 0.0065  -0.0548 0.0266  196 GLY A CA  
1547 C  C   . GLY A 195 ? 0.1342 0.1939 0.0615 0.0193  -0.0474 0.0067  196 GLY A C   
1548 O  O   . GLY A 195 ? 0.1579 0.2054 0.0560 -0.0055 -0.0480 -0.0040 196 GLY A O   
1549 N  N   . SER A 196 ? 0.1409 0.2154 0.0630 -0.0119 -0.0499 -0.0207 197 SER A N   
1550 C  CA  . SER A 196 ? 0.1420 0.1905 0.0934 -0.0272 -0.0637 0.0044  197 SER A CA  
1551 C  C   . SER A 196 ? 0.1848 0.1934 0.0953 -0.0155 -0.0545 -0.0107 197 SER A C   
1552 O  O   . SER A 196 ? 0.1502 0.2187 0.0756 -0.0313 -0.0507 0.0179  197 SER A O   
1553 C  CB  . SER A 196 ? 0.1651 0.2406 0.0589 -0.0027 -0.0587 -0.0144 197 SER A CB  
1554 O  OG  . SER A 196 ? 0.1490 0.2156 0.0829 -0.0150 -0.0479 -0.0049 197 SER A OG  
1555 N  N   . LEU A 197 ? 0.1621 0.2165 0.0653 -0.0133 -0.0452 -0.0182 198 LEU A N   
1556 C  CA  . LEU A 197 ? 0.1518 0.2307 0.0416 -0.0137 -0.0072 0.0024  198 LEU A CA  
1557 C  C   . LEU A 197 ? 0.1124 0.2140 0.0641 -0.0085 -0.0445 -0.0222 198 LEU A C   
1558 O  O   . LEU A 197 ? 0.1465 0.2376 0.0521 0.0015  -0.0490 0.0134  198 LEU A O   
1559 C  CB  . LEU A 197 ? 0.2030 0.2298 0.0680 -0.0526 -0.0071 -0.0010 198 LEU A CB  
1560 C  CG  . LEU A 197 ? 0.2486 0.2603 0.1425 -0.0319 0.0025  0.0326  198 LEU A CG  
1561 C  CD1 . LEU A 197 ? 0.2670 0.2709 0.1874 -0.0785 -0.0350 0.0912  198 LEU A CD1 
1562 C  CD2 . LEU A 197 ? 0.2377 0.2673 0.2095 -0.0363 -0.0458 0.0438  198 LEU A CD2 
1563 N  N   . THR A 198 ? 0.1833 0.2179 0.0531 -0.0408 -0.0158 -0.0210 199 THR A N   
1564 C  CA  . THR A 198 ? 0.2102 0.2576 0.0273 -0.0274 -0.0478 -0.0080 199 THR A CA  
1565 C  C   . THR A 198 ? 0.1328 0.2193 0.0865 -0.0447 -0.0500 -0.0105 199 THR A C   
1566 O  O   . THR A 198 ? 0.1622 0.2408 0.0601 -0.0265 -0.0486 -0.0065 199 THR A O   
1567 C  CB  . THR A 198 ? 0.1594 0.2264 0.0287 -0.0085 -0.0428 0.0220  199 THR A CB  
1568 O  OG1 . THR A 198 ? 0.1442 0.2014 0.0478 -0.0018 -0.0547 0.0271  199 THR A OG1 
1569 C  CG2 . THR A 198 ? 0.1461 0.2629 0.0534 -0.0150 -0.0260 0.0234  199 THR A CG2 
1570 N  N   . THR A 199 ? 0.1727 0.2334 0.0522 -0.0535 -0.0185 -0.0034 200 THR A N   
1571 C  CA  . THR A 199 ? 0.1776 0.2537 0.0130 -0.0444 -0.0293 0.0080  200 THR A CA  
1572 C  C   . THR A 199 ? 0.1680 0.2474 0.0819 -0.0126 -0.0445 -0.0023 200 THR A C   
1573 O  O   . THR A 199 ? 0.1655 0.2519 0.0903 -0.0419 -0.0192 -0.0143 200 THR A O   
1574 C  CB  . THR A 199 ? 0.1932 0.2751 0.0506 0.0016  -0.0780 -0.0144 200 THR A CB  
1575 O  OG1 . THR A 199 ? 0.2285 0.2892 0.1003 -0.0183 -0.0659 -0.0053 200 THR A OG1 
1576 C  CG2 . THR A 199 ? 0.2485 0.2839 0.1000 -0.0355 -0.0353 -0.0400 200 THR A CG2 
1577 N  N   . PRO A 200 ? 0.1655 0.3294 0.0554 -0.0352 -0.0478 -0.0114 201 PRO A N   
1578 C  CA  . PRO A 200 ? 0.1744 0.3055 0.0691 -0.0264 -0.0621 -0.0186 201 PRO A CA  
1579 C  C   . PRO A 200 ? 0.2055 0.2851 0.0903 -0.0400 -0.0208 0.0465  201 PRO A C   
1580 O  O   . PRO A 200 ? 0.2468 0.3239 0.1061 -0.0460 -0.0535 0.0253  201 PRO A O   
1581 C  CB  . PRO A 200 ? 0.1923 0.3348 0.1093 -0.0480 -0.0204 -0.0105 201 PRO A CB  
1582 C  CG  . PRO A 200 ? 0.1363 0.3529 0.1463 -0.0266 0.0009  -0.0269 201 PRO A CG  
1583 C  CD  . PRO A 200 ? 0.1212 0.3686 0.1449 -0.0055 -0.0453 -0.0543 201 PRO A CD  
1584 N  N   . PRO A 201 ? 0.1838 0.3148 0.0382 -0.0298 -0.0652 0.0384  202 PRO A N   
1585 C  CA  . PRO A 201 ? 0.1860 0.2613 0.0666 -0.0520 -0.0730 0.0247  202 PRO A CA  
1586 C  C   . PRO A 201 ? 0.2431 0.2657 0.0756 -0.0625 -0.0538 0.0238  202 PRO A C   
1587 O  O   . PRO A 201 ? 0.1812 0.2893 0.1449 -0.0182 -0.0851 0.0039  202 PRO A O   
1588 C  CB  . PRO A 201 ? 0.2351 0.2835 0.2627 -0.0100 -0.0467 0.0677  202 PRO A CB  
1589 C  CG  . PRO A 201 ? 0.2469 0.3080 0.3318 0.0025  -0.0514 0.0181  202 PRO A CG  
1590 C  CD  . PRO A 201 ? 0.2705 0.3137 0.1738 -0.0196 -0.0248 0.0910  202 PRO A CD  
1591 N  N   . LEU A 202 ? 0.1788 0.2616 0.0815 -0.0277 0.0019  0.0243  203 LEU A N   
1592 C  CA  . LEU A 202 ? 0.1576 0.2326 0.0628 -0.0129 -0.0395 0.0131  203 LEU A CA  
1593 C  C   . LEU A 202 ? 0.2041 0.1953 0.0861 -0.0555 -0.0277 0.0072  203 LEU A C   
1594 O  O   . LEU A 202 ? 0.2081 0.2630 0.0840 -0.0237 -0.0494 0.0270  203 LEU A O   
1595 C  CB  . LEU A 202 ? 0.1726 0.2550 0.1223 0.0240  -0.0300 -0.0155 203 LEU A CB  
1596 C  CG  . LEU A 202 ? 0.1701 0.2487 0.0987 -0.0003 -0.0222 -0.0107 203 LEU A CG  
1597 C  CD1 . LEU A 202 ? 0.2117 0.2871 0.1321 0.0092  -0.0529 0.0258  203 LEU A CD1 
1598 C  CD2 . LEU A 202 ? 0.1727 0.2450 0.0806 0.0042  -0.0283 -0.0146 203 LEU A CD2 
1599 N  N   A ASN A 203 ? 0.1752 0.2169 0.1507 -0.0282 -0.0263 -0.0145 204 ASN A N   
1600 N  N   B ASN A 203 ? 0.1734 0.2154 0.1514 -0.0287 -0.0279 -0.0150 204 ASN A N   
1601 C  CA  A ASN A 203 ? 0.2296 0.1984 0.1558 -0.0357 -0.0084 0.0030  204 ASN A CA  
1602 C  CA  B ASN A 203 ? 0.2355 0.2017 0.1594 -0.0354 -0.0062 -0.0006 204 ASN A CA  
1603 C  C   A ASN A 203 ? 0.1763 0.2100 0.1414 -0.0256 -0.0119 -0.0411 204 ASN A C   
1604 C  C   B ASN A 203 ? 0.1720 0.2134 0.1432 -0.0199 -0.0126 -0.0427 204 ASN A C   
1605 O  O   A ASN A 203 ? 0.1644 0.2412 0.1012 -0.0243 -0.0427 0.0205  204 ASN A O   
1606 O  O   B ASN A 203 ? 0.1690 0.2404 0.1025 -0.0243 -0.0400 0.0201  204 ASN A O   
1607 C  CB  A ASN A 203 ? 0.2534 0.2330 0.1511 -0.0254 -0.0098 0.0405  204 ASN A CB  
1608 C  CB  B ASN A 203 ? 0.2514 0.2436 0.1709 -0.0211 -0.0317 0.0279  204 ASN A CB  
1609 C  CG  A ASN A 203 ? 0.2921 0.2861 0.2153 0.0381  0.0719  0.0948  204 ASN A CG  
1610 C  CG  B ASN A 203 ? 0.2805 0.3481 0.3076 0.0012  0.0774  0.0560  204 ASN A CG  
1611 O  OD1 A ASN A 203 ? 0.3179 0.2494 0.3347 0.0524  0.0781  0.0607  204 ASN A OD1 
1612 O  OD1 B ASN A 203 ? 0.3935 0.4599 0.3619 0.0444  0.0708  0.0259  204 ASN A OD1 
1613 N  ND2 A ASN A 203 ? 0.3833 0.2599 0.1027 0.0466  0.1228  0.0831  204 ASN A ND2 
1614 N  ND2 B ASN A 203 ? 0.3445 0.3732 0.4168 -0.0215 0.0488  0.0357  204 ASN A ND2 
1615 N  N   . GLU A 204 ? 0.1960 0.2201 0.1378 -0.0255 -0.0252 -0.0280 205 GLU A N   
1616 C  CA  . GLU A 204 ? 0.1780 0.2530 0.0441 -0.0002 -0.0657 -0.0143 205 GLU A CA  
1617 C  C   . GLU A 204 ? 0.1788 0.2656 0.1073 0.0012  -0.1002 -0.0221 205 GLU A C   
1618 O  O   . GLU A 204 ? 0.2340 0.2468 0.1698 0.0319  -0.0758 -0.0489 205 GLU A O   
1619 C  CB  . GLU A 204 ? 0.1783 0.3111 0.0651 0.0009  -0.0818 -0.0039 205 GLU A CB  
1620 C  CG  . GLU A 204 ? 0.1896 0.3069 0.0732 0.0152  -0.0660 0.0060  205 GLU A CG  
1621 C  CD  . GLU A 204 ? 0.2020 0.2921 0.0971 0.0164  -0.0905 -0.0122 205 GLU A CD  
1622 O  OE1 . GLU A 204 ? 0.3161 0.3295 0.1364 -0.0071 -0.0635 -0.0543 205 GLU A OE1 
1623 O  OE2 . GLU A 204 ? 0.2244 0.2820 0.0488 -0.0072 -0.0937 0.0050  205 GLU A OE2 
1624 N  N   . CYS A 205 ? 0.1781 0.2158 0.0792 -0.0049 -0.0864 0.0261  206 CYS A N   
1625 C  CA  . CYS A 205 ? 0.1924 0.2322 0.1650 -0.0066 -0.0359 0.0792  206 CYS A CA  
1626 C  C   . CYS A 205 ? 0.2046 0.1975 0.1151 -0.0100 -0.0625 -0.0352 206 CYS A C   
1627 O  O   . CYS A 205 ? 0.2563 0.1802 0.1648 -0.0087 -0.0851 0.0392  206 CYS A O   
1628 C  CB  . CYS A 205 ? 0.2764 0.2315 0.0662 -0.0033 -0.0525 0.0160  206 CYS A CB  
1629 S  SG  . CYS A 205 ? 0.2521 0.2888 0.0953 0.0071  -0.0714 -0.0071 206 CYS A SG  
1630 N  N   . VAL A 206 ? 0.1589 0.1963 0.0937 -0.0087 -0.0496 -0.0221 207 VAL A N   
1631 C  CA  . VAL A 206 ? 0.1472 0.2231 0.1134 -0.0182 -0.0320 -0.0445 207 VAL A CA  
1632 C  C   . VAL A 206 ? 0.1834 0.2354 0.1208 0.0003  -0.0452 0.0044  207 VAL A C   
1633 O  O   . VAL A 206 ? 0.1727 0.2724 0.1104 0.0012  -0.0524 0.0103  207 VAL A O   
1634 C  CB  . VAL A 206 ? 0.1723 0.1959 0.1134 -0.0262 -0.0248 -0.0184 207 VAL A CB  
1635 C  CG1 . VAL A 206 ? 0.2010 0.2175 0.0937 -0.0389 -0.0496 -0.0269 207 VAL A CG1 
1636 C  CG2 . VAL A 206 ? 0.1691 0.2067 0.1122 -0.0230 -0.0290 0.0083  207 VAL A CG2 
1637 N  N   . THR A 207 ? 0.1583 0.2041 0.0464 -0.0344 -0.0483 0.0005  208 THR A N   
1638 C  CA  . THR A 207 ? 0.1967 0.1639 0.0318 -0.0287 -0.0402 0.0061  208 THR A CA  
1639 C  C   . THR A 207 ? 0.1738 0.1822 0.0540 -0.0495 -0.0609 0.0162  208 THR A C   
1640 O  O   . THR A 207 ? 0.1921 0.2256 0.0457 -0.0124 -0.0644 0.0002  208 THR A O   
1641 C  CB  . THR A 207 ? 0.2189 0.2271 0.1176 -0.0212 -0.0102 -0.0358 208 THR A CB  
1642 O  OG1 . THR A 207 ? 0.1964 0.2248 0.0905 0.0022  -0.0325 -0.0390 208 THR A OG1 
1643 C  CG2 . THR A 207 ? 0.2380 0.2440 0.0423 -0.0006 -0.0362 0.0195  208 THR A CG2 
1644 N  N   . TRP A 208 ? 0.1949 0.1761 0.0642 -0.0297 -0.0071 -0.0049 209 TRP A N   
1645 C  CA  . TRP A 208 ? 0.1575 0.2038 0.0346 -0.0326 -0.0506 0.0051  209 TRP A CA  
1646 C  C   . TRP A 208 ? 0.1734 0.1849 0.0172 -0.0348 -0.0412 -0.0022 209 TRP A C   
1647 O  O   . TRP A 208 ? 0.1953 0.2258 0.0203 -0.0100 -0.0254 0.0082  209 TRP A O   
1648 C  CB  . TRP A 208 ? 0.1752 0.2154 0.0261 -0.0148 -0.0257 0.0141  209 TRP A CB  
1649 C  CG  . TRP A 208 ? 0.1474 0.1980 0.0558 -0.0298 -0.0178 -0.0042 209 TRP A CG  
1650 C  CD1 . TRP A 208 ? 0.1327 0.1892 0.0919 -0.0064 -0.0023 -0.0121 209 TRP A CD1 
1651 C  CD2 . TRP A 208 ? 0.1799 0.1966 0.0625 -0.0154 -0.0502 -0.0108 209 TRP A CD2 
1652 N  NE1 . TRP A 208 ? 0.1364 0.2177 0.0828 -0.0151 -0.0134 -0.0027 209 TRP A NE1 
1653 C  CE2 . TRP A 208 ? 0.1826 0.1978 0.0608 -0.0082 -0.0345 -0.0003 209 TRP A CE2 
1654 C  CE3 . TRP A 208 ? 0.1757 0.2117 0.0267 0.0015  -0.0541 -0.0013 209 TRP A CE3 
1655 C  CZ2 . TRP A 208 ? 0.2054 0.2000 0.0777 0.0053  -0.0077 -0.0134 209 TRP A CZ2 
1656 C  CZ3 . TRP A 208 ? 0.1838 0.2305 0.0486 0.0027  -0.0165 -0.0145 209 TRP A CZ3 
1657 C  CH2 . TRP A 208 ? 0.1601 0.2495 0.0675 0.0198  -0.0120 -0.0012 209 TRP A CH2 
1658 N  N   . ILE A 209 ? 0.1536 0.2067 0.0388 -0.0026 -0.0506 -0.0284 210 ILE A N   
1659 C  CA  . ILE A 209 ? 0.1819 0.1720 0.0340 -0.0069 -0.0458 0.0063  210 ILE A CA  
1660 C  C   . ILE A 209 ? 0.1628 0.1662 0.0138 0.0008  -0.0142 0.0093  210 ILE A C   
1661 O  O   . ILE A 209 ? 0.1923 0.2104 0.0181 0.0002  -0.0212 0.0297  210 ILE A O   
1662 C  CB  . ILE A 209 ? 0.1661 0.2017 0.0724 0.0118  -0.0041 -0.0188 210 ILE A CB  
1663 C  CG1 . ILE A 209 ? 0.1592 0.2011 0.1378 0.0076  0.0044  -0.0381 210 ILE A CG1 
1664 C  CG2 . ILE A 209 ? 0.1783 0.2418 0.1267 -0.0094 -0.0106 -0.0241 210 ILE A CG2 
1665 C  CD1 . ILE A 209 ? 0.1758 0.2499 0.1285 0.0040  -0.0015 0.0093  210 ILE A CD1 
1666 N  N   . VAL A 210 ? 0.1587 0.1472 0.1064 0.0181  -0.0195 0.0022  211 VAL A N   
1667 C  CA  . VAL A 210 ? 0.1709 0.1560 0.0475 0.0043  -0.0472 0.0178  211 VAL A CA  
1668 C  C   . VAL A 210 ? 0.1499 0.2406 0.0603 -0.0030 -0.0420 0.0046  211 VAL A C   
1669 O  O   . VAL A 210 ? 0.1564 0.2280 0.0677 -0.0059 -0.0296 0.0150  211 VAL A O   
1670 C  CB  . VAL A 210 ? 0.1465 0.1835 0.0709 0.0155  -0.0234 -0.0003 211 VAL A CB  
1671 C  CG1 . VAL A 210 ? 0.1824 0.1967 0.0630 0.0012  -0.0419 -0.0027 211 VAL A CG1 
1672 C  CG2 . VAL A 210 ? 0.1700 0.1838 0.0784 -0.0016 -0.0315 -0.0018 211 VAL A CG2 
1673 N  N   . LEU A 211 ? 0.1296 0.1909 0.0721 0.0019  -0.0409 -0.0134 212 LEU A N   
1674 C  CA  . LEU A 211 ? 0.1586 0.2229 0.0415 -0.0181 -0.0430 0.0179  212 LEU A CA  
1675 C  C   . LEU A 211 ? 0.1314 0.2287 0.0747 -0.0118 -0.0526 0.0203  212 LEU A C   
1676 O  O   . LEU A 211 ? 0.1515 0.2072 0.1027 -0.0097 -0.0568 0.0098  212 LEU A O   
1677 C  CB  . LEU A 211 ? 0.1727 0.2003 0.0200 -0.0066 -0.0364 -0.0131 212 LEU A CB  
1678 C  CG  . LEU A 211 ? 0.1558 0.2225 0.0601 0.0196  -0.0603 -0.0051 212 LEU A CG  
1679 C  CD1 . LEU A 211 ? 0.1410 0.2940 0.0467 0.0089  -0.0473 -0.0085 212 LEU A CD1 
1680 C  CD2 . LEU A 211 ? 0.2067 0.2450 0.0867 0.0061  0.0228  0.0063  212 LEU A CD2 
1681 N  N   . LYS A 212 ? 0.1819 0.2566 0.0195 -0.0124 -0.0414 0.0117  213 LYS A N   
1682 C  CA  . LYS A 212 ? 0.2167 0.2368 0.0380 0.0019  -0.0449 0.0100  213 LYS A CA  
1683 C  C   . LYS A 212 ? 0.1468 0.2551 0.0494 -0.0008 -0.0129 0.0004  213 LYS A C   
1684 O  O   . LYS A 212 ? 0.1975 0.2705 0.1307 0.0130  -0.0660 0.0283  213 LYS A O   
1685 C  CB  . LYS A 212 ? 0.2529 0.3262 0.0558 -0.0315 -0.0092 -0.0414 213 LYS A CB  
1686 C  CG  . LYS A 212 ? 0.2853 0.3615 0.1651 0.0220  0.0318  0.0048  213 LYS A CG  
1687 C  CD  . LYS A 212 ? 0.4176 0.5104 0.1892 -0.0326 0.1073  -0.0597 213 LYS A CD  
1688 C  CE  . LYS A 212 ? 0.4251 0.5855 0.1435 -0.0275 0.0318  -0.0672 213 LYS A CE  
1689 N  NZ  . LYS A 212 ? 0.4653 0.5977 0.5923 -0.2111 -0.1021 -0.1778 213 LYS A NZ  
1690 N  N   . GLU A 213 ? 0.1714 0.2469 0.0689 -0.0034 -0.0416 0.0254  214 GLU A N   
1691 C  CA  . GLU A 213 ? 0.2100 0.2341 0.0921 -0.0059 -0.0201 0.0096  214 GLU A CA  
1692 C  C   . GLU A 213 ? 0.1593 0.1932 0.1052 -0.0141 -0.0416 0.0189  214 GLU A C   
1693 O  O   . GLU A 213 ? 0.1698 0.1829 0.1122 0.0060  -0.0242 0.0179  214 GLU A O   
1694 C  CB  . GLU A 213 ? 0.1934 0.2309 0.0923 0.0051  -0.0365 -0.0037 214 GLU A CB  
1695 C  CG  . GLU A 213 ? 0.2419 0.3455 0.1167 -0.0187 -0.0219 -0.0699 214 GLU A CG  
1696 C  CD  . GLU A 213 ? 0.2689 0.4120 0.1910 0.0182  -0.0588 -0.0423 214 GLU A CD  
1697 O  OE1 . GLU A 213 ? 0.2643 0.3545 0.2498 -0.0316 0.0064  -0.0540 214 GLU A OE1 
1698 O  OE2 . GLU A 213 ? 0.3684 0.7526 0.2260 -0.0534 -0.0800 -0.1412 214 GLU A OE2 
1699 N  N   A PRO A 214 ? 0.1809 0.2098 0.0973 -0.0001 -0.0217 0.0183  215 PRO A N   
1700 N  N   B PRO A 214 ? 0.1711 0.2075 0.0655 -0.0003 -0.0251 0.0294  215 PRO A N   
1701 C  CA  A PRO A 214 ? 0.1831 0.2249 0.0612 -0.0091 -0.0484 0.0034  215 PRO A CA  
1702 C  CA  B PRO A 214 ? 0.1661 0.2318 0.0489 0.0005  -0.0400 0.0201  215 PRO A CA  
1703 C  C   A PRO A 214 ? 0.1450 0.2169 0.0697 -0.0214 -0.0351 -0.0084 215 PRO A C   
1704 C  C   B PRO A 214 ? 0.1540 0.2364 0.0566 -0.0192 -0.0368 -0.0148 215 PRO A C   
1705 O  O   A PRO A 214 ? 0.1439 0.1798 0.1596 0.0092  -0.0212 -0.0251 215 PRO A O   
1706 O  O   B PRO A 214 ? 0.1510 0.1834 0.0646 0.0055  -0.0290 -0.0061 215 PRO A O   
1707 C  CB  A PRO A 214 ? 0.2007 0.2262 0.0736 -0.0288 -0.0519 -0.0340 215 PRO A CB  
1708 C  CB  B PRO A 214 ? 0.1725 0.2474 0.0378 0.0024  -0.0597 0.0144  215 PRO A CB  
1709 C  CG  A PRO A 214 ? 0.2351 0.2054 0.0603 -0.0403 -0.0693 -0.0269 215 PRO A CG  
1710 C  CG  B PRO A 214 ? 0.1855 0.2458 0.0547 0.0092  0.0043  0.0591  215 PRO A CG  
1711 C  CD  A PRO A 214 ? 0.2168 0.1975 0.0908 0.0000  -0.0463 -0.0044 215 PRO A CD  
1712 C  CD  B PRO A 214 ? 0.1621 0.2129 0.0916 0.0163  -0.0290 0.0346  215 PRO A CD  
1713 N  N   . ILE A 215 ? 0.1278 0.2542 0.0586 -0.0137 -0.0436 -0.0046 216 ILE A N   
1714 C  CA  . ILE A 215 ? 0.1463 0.2218 0.0797 -0.0031 -0.0631 -0.0264 216 ILE A CA  
1715 C  C   . ILE A 215 ? 0.1597 0.2186 0.0779 -0.0105 -0.0268 -0.0162 216 ILE A C   
1716 O  O   . ILE A 215 ? 0.1626 0.2497 0.1346 0.0089  -0.0232 -0.0407 216 ILE A O   
1717 C  CB  . ILE A 215 ? 0.1651 0.2373 0.1149 0.0099  -0.0329 -0.0281 216 ILE A CB  
1718 C  CG1 . ILE A 215 ? 0.1804 0.2376 0.0722 -0.0279 -0.0423 -0.0146 216 ILE A CG1 
1719 C  CG2 . ILE A 215 ? 0.1813 0.2722 0.0709 0.0243  -0.0273 -0.0479 216 ILE A CG2 
1720 C  CD1 . ILE A 215 ? 0.1727 0.2958 0.1253 -0.0192 -0.0679 0.0422  216 ILE A CD1 
1721 N  N   A SER A 216 ? 0.2052 0.2418 0.0835 -0.0220 -0.0553 -0.0243 217 SER A N   
1722 N  N   B SER A 216 ? 0.2009 0.2330 0.0845 -0.0272 -0.0464 -0.0204 217 SER A N   
1723 C  CA  A SER A 216 ? 0.2746 0.2508 0.0574 -0.0265 -0.0543 -0.0252 217 SER A CA  
1724 C  CA  B SER A 216 ? 0.2465 0.2183 0.0842 -0.0372 -0.0434 -0.0142 217 SER A CA  
1725 C  C   A SER A 216 ? 0.2098 0.2215 0.0682 -0.0111 -0.0559 -0.0100 217 SER A C   
1726 C  C   B SER A 216 ? 0.2041 0.2135 0.0815 -0.0113 -0.0567 -0.0083 217 SER A C   
1727 O  O   A SER A 216 ? 0.2110 0.2752 0.0876 0.0200  -0.0312 -0.0041 217 SER A O   
1728 O  O   B SER A 216 ? 0.2170 0.2732 0.0688 0.0274  -0.0418 -0.0215 217 SER A O   
1729 C  CB  A SER A 216 ? 0.3633 0.2014 0.1152 -0.0573 -0.0598 -0.0068 217 SER A CB  
1730 C  CB  B SER A 216 ? 0.3296 0.1320 0.1610 -0.0344 -0.0359 0.0137  217 SER A CB  
1731 O  OG  A SER A 216 ? 0.3542 0.1955 0.2294 -0.0511 -0.0968 -0.0276 217 SER A OG  
1732 O  OG  B SER A 216 ? 0.2430 0.2189 0.2145 -0.0680 -0.0096 0.0785  217 SER A OG  
1733 N  N   . VAL A 217 ? 0.2205 0.2518 0.0470 0.0055  -0.0682 -0.0298 218 VAL A N   
1734 C  CA  . VAL A 217 ? 0.2127 0.2143 0.0551 -0.0122 -0.0627 -0.0088 218 VAL A CA  
1735 C  C   . VAL A 217 ? 0.1959 0.2158 0.1212 0.0062  -0.0322 0.0010  218 VAL A C   
1736 O  O   . VAL A 217 ? 0.1831 0.2156 0.1000 0.0086  -0.0688 -0.0276 218 VAL A O   
1737 C  CB  . VAL A 217 ? 0.1553 0.2341 0.1443 0.0072  -0.0610 -0.0118 218 VAL A CB  
1738 C  CG1 . VAL A 217 ? 0.1615 0.2064 0.2154 0.0345  -0.0703 0.0065  218 VAL A CG1 
1739 C  CG2 . VAL A 217 ? 0.1474 0.2207 0.1939 0.0410  -0.0275 -0.0251 218 VAL A CG2 
1740 N  N   . SER A 218 ? 0.1515 0.2466 0.1277 -0.0016 -0.0740 -0.0057 219 SER A N   
1741 C  CA  . SER A 218 ? 0.1271 0.2643 0.0952 -0.0043 -0.0723 -0.0070 219 SER A CA  
1742 C  C   . SER A 218 ? 0.1583 0.2093 0.1263 -0.0031 -0.0286 -0.0530 219 SER A C   
1743 O  O   . SER A 218 ? 0.1655 0.2118 0.1345 0.0000  -0.0307 0.0016  219 SER A O   
1744 C  CB  . SER A 218 ? 0.1543 0.2396 0.0885 -0.0194 -0.0781 0.0029  219 SER A CB  
1745 O  OG  . SER A 218 ? 0.2064 0.2546 0.1413 -0.0012 -0.0098 0.0030  219 SER A OG  
1746 N  N   . SER A 219 ? 0.1942 0.2074 0.1574 0.0195  -0.0374 -0.0358 220 SER A N   
1747 C  CA  . SER A 219 ? 0.1991 0.1971 0.1921 0.0116  -0.0042 0.0114  220 SER A CA  
1748 C  C   . SER A 219 ? 0.1323 0.2011 0.1632 0.0204  -0.0547 -0.0030 220 SER A C   
1749 O  O   . SER A 219 ? 0.1869 0.2641 0.2307 -0.0160 -0.0199 0.0167  220 SER A O   
1750 C  CB  . SER A 219 ? 0.3145 0.2041 0.2524 0.0230  -0.0179 0.0042  220 SER A CB  
1751 O  OG  . SER A 219 ? 0.3544 0.2315 0.3181 0.0147  0.0126  -0.0330 220 SER A OG  
1752 N  N   . GLU A 220 ? 0.1716 0.2183 0.1384 -0.0066 -0.0688 -0.0061 221 GLU A N   
1753 C  CA  . GLU A 220 ? 0.1824 0.2443 0.1960 -0.0342 -0.0087 0.0218  221 GLU A CA  
1754 C  C   . GLU A 220 ? 0.1623 0.2195 0.1375 0.0054  -0.0282 0.0073  221 GLU A C   
1755 O  O   . GLU A 220 ? 0.2100 0.2294 0.1296 -0.0075 -0.0010 -0.0143 221 GLU A O   
1756 C  CB  . GLU A 220 ? 0.1885 0.2702 0.1582 -0.0660 -0.0067 -0.0347 221 GLU A CB  
1757 C  CG  . GLU A 220 ? 0.2554 0.2904 0.2212 -0.0411 0.0291  -0.0819 221 GLU A CG  
1758 C  CD  . GLU A 220 ? 0.4316 0.2437 0.2501 -0.0787 0.0960  -0.1005 221 GLU A CD  
1759 O  OE1 . GLU A 220 ? 0.2576 0.3993 0.2193 -0.0846 -0.0067 -0.1363 221 GLU A OE1 
1760 O  OE2 . GLU A 220 ? 0.4824 0.2968 0.3881 -0.1001 -0.0219 -0.0894 221 GLU A OE2 
1761 N  N   . GLN A 221 ? 0.1917 0.2122 0.0939 0.0019  -0.0353 0.0068  222 GLN A N   
1762 C  CA  . GLN A 221 ? 0.1345 0.2125 0.1215 -0.0017 -0.0260 0.0089  222 GLN A CA  
1763 C  C   . GLN A 221 ? 0.1644 0.2095 0.1562 -0.0207 -0.0685 0.0089  222 GLN A C   
1764 O  O   . GLN A 221 ? 0.2014 0.2194 0.1076 -0.0074 -0.0471 0.0168  222 GLN A O   
1765 C  CB  . GLN A 221 ? 0.1219 0.2518 0.1237 0.0135  -0.0429 -0.0253 222 GLN A CB  
1766 C  CG  . GLN A 221 ? 0.1486 0.2477 0.0899 -0.0018 -0.0609 0.0085  222 GLN A CG  
1767 C  CD  . GLN A 221 ? 0.1750 0.2124 0.0591 -0.0008 -0.0622 -0.0104 222 GLN A CD  
1768 O  OE1 . GLN A 221 ? 0.1960 0.2572 0.0472 0.0095  -0.0653 -0.0265 222 GLN A OE1 
1769 N  NE2 . GLN A 221 ? 0.1797 0.2291 0.0932 -0.0030 -0.0641 -0.0311 222 GLN A NE2 
1770 N  N   . VAL A 222 ? 0.1659 0.2513 0.1127 -0.0046 -0.0294 0.0149  223 VAL A N   
1771 C  CA  . VAL A 222 ? 0.1689 0.2692 0.1098 -0.0352 -0.0271 0.0284  223 VAL A CA  
1772 C  C   . VAL A 222 ? 0.1684 0.2551 0.1413 -0.0233 -0.0277 0.0068  223 VAL A C   
1773 O  O   . VAL A 222 ? 0.1676 0.2460 0.1192 -0.0098 -0.0414 0.0091  223 VAL A O   
1774 C  CB  . VAL A 222 ? 0.2382 0.3253 0.0889 -0.0609 -0.0796 0.0152  223 VAL A CB  
1775 C  CG1 . VAL A 222 ? 0.3952 0.3680 0.2434 -0.0625 -0.1117 0.0479  223 VAL A CG1 
1776 C  CG2 . VAL A 222 ? 0.2335 0.3994 0.1525 -0.1002 -0.0737 0.0319  223 VAL A CG2 
1777 N  N   . LEU A 223 ? 0.1641 0.2917 0.0743 -0.0058 -0.0568 0.0039  224 LEU A N   
1778 C  CA  . LEU A 223 ? 0.1770 0.2319 0.1805 -0.0268 -0.0048 -0.0077 224 LEU A CA  
1779 C  C   . LEU A 223 ? 0.1957 0.2375 0.1630 -0.0026 0.0211  -0.0162 224 LEU A C   
1780 O  O   . LEU A 223 ? 0.1791 0.2734 0.1502 0.0092  0.0002  -0.0040 224 LEU A O   
1781 C  CB  . LEU A 223 ? 0.2386 0.3137 0.2321 -0.0529 -0.0721 -0.0611 224 LEU A CB  
1782 C  CG  . LEU A 223 ? 0.3833 0.4312 0.3168 -0.0097 0.0386  -0.0042 224 LEU A CG  
1783 N  N   . LYS A 224 ? 0.1841 0.2377 0.0709 -0.0159 -0.0744 -0.0281 225 LYS A N   
1784 C  CA  . LYS A 224 ? 0.1722 0.2763 0.1224 -0.0003 -0.0419 0.0084  225 LYS A CA  
1785 C  C   . LYS A 224 ? 0.2000 0.2286 0.0836 -0.0113 0.0027  0.0048  225 LYS A C   
1786 O  O   . LYS A 224 ? 0.1960 0.2721 0.0713 -0.0104 -0.0201 0.0163  225 LYS A O   
1787 C  CB  . LYS A 224 ? 0.1863 0.4051 0.1452 0.0474  -0.0605 -0.0242 225 LYS A CB  
1788 C  CG  . LYS A 224 ? 0.3553 0.3285 0.1910 -0.0673 -0.0262 -0.0029 225 LYS A CG  
1789 C  CD  . LYS A 224 ? 0.3768 0.6546 0.1533 -0.0265 0.0916  0.0440  225 LYS A CD  
1790 C  CE  . LYS A 224 ? 0.6330 0.7293 0.2432 -0.0594 -0.1837 0.0871  225 LYS A CE  
1791 N  NZ  . LYS A 224 ? 0.9077 0.3684 0.4070 -0.0928 0.1265  -0.0291 225 LYS A NZ  
1792 N  N   . PHE A 225 ? 0.2011 0.1951 0.0722 0.0189  -0.0506 0.0023  226 PHE A N   
1793 C  CA  . PHE A 225 ? 0.1899 0.1963 0.0636 0.0104  0.0160  -0.0307 226 PHE A CA  
1794 C  C   . PHE A 225 ? 0.1892 0.2129 0.0434 0.0158  -0.0179 -0.0098 226 PHE A C   
1795 O  O   . PHE A 225 ? 0.2182 0.2531 0.0518 -0.0038 -0.0378 -0.0023 226 PHE A O   
1796 C  CB  . PHE A 225 ? 0.1593 0.2254 0.0531 0.0082  -0.0253 0.0114  226 PHE A CB  
1797 C  CG  . PHE A 225 ? 0.1903 0.2642 0.0581 0.0036  -0.0073 -0.0176 226 PHE A CG  
1798 C  CD1 . PHE A 225 ? 0.1862 0.2540 0.1593 0.0294  -0.0109 -0.0042 226 PHE A CD1 
1799 C  CD2 . PHE A 225 ? 0.2024 0.3088 0.0566 -0.0188 -0.0149 -0.0279 226 PHE A CD2 
1800 C  CE1 . PHE A 225 ? 0.2016 0.2775 0.1492 0.0271  0.0222  0.0089  226 PHE A CE1 
1801 C  CE2 . PHE A 225 ? 0.1615 0.3111 0.1902 -0.0013 0.0027  0.0021  226 PHE A CE2 
1802 C  CZ  . PHE A 225 ? 0.2086 0.2098 0.1639 0.0395  -0.0026 -0.0524 226 PHE A CZ  
1803 N  N   . ARG A 226 ? 0.2020 0.2122 0.0556 0.0244  -0.0048 0.0044  227 ARG A N   
1804 C  CA  . ARG A 226 ? 0.1885 0.2079 0.0724 0.0237  -0.0315 0.0179  227 ARG A CA  
1805 C  C   . ARG A 226 ? 0.1815 0.2409 0.0960 0.0005  -0.0048 0.0193  227 ARG A C   
1806 O  O   . ARG A 226 ? 0.2409 0.2796 0.1720 0.0010  0.0332  -0.0307 227 ARG A O   
1807 C  CB  . ARG A 226 ? 0.2200 0.1949 0.0557 0.0096  -0.0044 0.0006  227 ARG A CB  
1808 C  CG  . ARG A 226 ? 0.1759 0.2242 0.0403 0.0254  -0.0458 0.0098  227 ARG A CG  
1809 C  CD  . ARG A 226 ? 0.2034 0.2240 0.0710 -0.0132 -0.0082 0.0176  227 ARG A CD  
1810 N  NE  . ARG A 226 ? 0.2050 0.2225 0.0642 -0.0165 -0.0289 0.0444  227 ARG A NE  
1811 C  CZ  . ARG A 226 ? 0.1844 0.2732 0.1025 -0.0473 -0.0027 -0.0200 227 ARG A CZ  
1812 N  NH1 . ARG A 226 ? 0.2268 0.3353 0.2214 -0.0991 -0.0205 -0.0961 227 ARG A NH1 
1813 N  NH2 . ARG A 226 ? 0.2442 0.2760 0.1310 -0.0225 0.0601  -0.0047 227 ARG A NH2 
1814 N  N   . LYS A 227 ? 0.2197 0.2115 0.0558 -0.0058 -0.0135 -0.0055 228 LYS A N   
1815 C  CA  . LYS A 227 ? 0.2048 0.2358 0.0366 -0.0376 -0.0278 -0.0489 228 LYS A CA  
1816 C  C   . LYS A 227 ? 0.2143 0.2103 0.0912 -0.0138 -0.0135 -0.0134 228 LYS A C   
1817 O  O   . LYS A 227 ? 0.2141 0.2622 0.1233 -0.0443 0.0012  0.0001  228 LYS A O   
1818 C  CB  . LYS A 227 ? 0.2138 0.2764 0.0983 -0.0295 -0.0634 -0.0424 228 LYS A CB  
1819 C  CG  . LYS A 227 ? 0.3158 0.3414 0.0624 -0.0993 -0.0174 0.0044  228 LYS A CG  
1820 C  CD  . LYS A 227 ? 0.2600 0.4568 0.1579 0.0532  -0.0539 -0.0269 228 LYS A CD  
1821 N  N   . LEU A 228 ? 0.1795 0.2230 0.1129 0.0036  -0.0402 -0.0239 229 LEU A N   
1822 C  CA  . LEU A 228 ? 0.1687 0.2096 0.1065 0.0150  -0.0249 -0.0121 229 LEU A CA  
1823 C  C   . LEU A 228 ? 0.1679 0.1743 0.0745 0.0162  -0.0022 -0.0358 229 LEU A C   
1824 O  O   . LEU A 228 ? 0.1935 0.1985 0.0835 0.0062  -0.0027 -0.0013 229 LEU A O   
1825 C  CB  . LEU A 228 ? 0.1806 0.2336 0.0917 0.0329  -0.0236 -0.0046 229 LEU A CB  
1826 C  CG  . LEU A 228 ? 0.1684 0.2917 0.0256 0.0273  -0.0548 -0.0231 229 LEU A CG  
1827 C  CD1 . LEU A 228 ? 0.2305 0.2777 0.0451 -0.0065 -0.0250 -0.0329 229 LEU A CD1 
1828 C  CD2 . LEU A 228 ? 0.2348 0.2568 0.1374 0.0006  -0.0291 0.0535  229 LEU A CD2 
1829 N  N   . ASN A 229 ? 0.1610 0.2135 0.0973 -0.0025 -0.0285 -0.0183 230 ASN A N   
1830 C  CA  . ASN A 229 ? 0.1540 0.2171 0.1091 -0.0015 0.0190  0.0336  230 ASN A CA  
1831 C  C   . ASN A 229 ? 0.1817 0.2221 0.1226 0.0170  -0.0041 0.0308  230 ASN A C   
1832 O  O   . ASN A 229 ? 0.1802 0.2335 0.0824 0.0116  -0.0161 0.0013  230 ASN A O   
1833 C  CB  . ASN A 229 ? 0.2140 0.2666 0.0763 -0.0050 0.0017  0.0280  230 ASN A CB  
1834 C  CG  . ASN A 229 ? 0.2232 0.2894 0.1679 0.0097  0.0245  -0.0168 230 ASN A CG  
1835 O  OD1 . ASN A 229 ? 0.3250 0.3546 0.1874 0.0412  0.0677  0.0226  230 ASN A OD1 
1836 N  ND2 . ASN A 229 ? 0.3457 0.2547 0.1233 -0.0005 0.0044  -0.0773 230 ASN A ND2 
1837 N  N   . PHE A 230 ? 0.1641 0.2330 0.0469 0.0026  0.0133  -0.0116 231 PHE A N   
1838 C  CA  . PHE A 230 ? 0.1362 0.2542 0.0969 -0.0141 -0.0156 -0.0182 231 PHE A CA  
1839 C  C   . PHE A 230 ? 0.1647 0.2613 0.1546 -0.0081 0.0063  -0.0073 231 PHE A C   
1840 O  O   . PHE A 230 ? 0.2007 0.2643 0.1113 -0.0207 -0.0136 0.0218  231 PHE A O   
1841 C  CB  . PHE A 230 ? 0.1751 0.2830 0.1281 0.0407  -0.0018 0.0195  231 PHE A CB  
1842 C  CG  . PHE A 230 ? 0.1479 0.2139 0.1052 -0.0020 -0.0413 -0.0168 231 PHE A CG  
1843 C  CD1 . PHE A 230 ? 0.1432 0.2512 0.1411 0.0173  -0.0337 -0.0240 231 PHE A CD1 
1844 C  CD2 . PHE A 230 ? 0.1953 0.2108 0.1453 -0.0035 -0.0396 -0.0357 231 PHE A CD2 
1845 C  CE1 . PHE A 230 ? 0.1723 0.2558 0.1226 -0.0008 -0.0406 -0.0270 231 PHE A CE1 
1846 C  CE2 . PHE A 230 ? 0.1892 0.2279 0.1482 0.0291  -0.0320 -0.0216 231 PHE A CE2 
1847 C  CZ  . PHE A 230 ? 0.2028 0.2523 0.0985 0.0221  -0.0730 -0.0663 231 PHE A CZ  
1848 N  N   . ASN A 231 ? 0.1589 0.2754 0.1525 0.0024  0.0200  -0.0154 232 ASN A N   
1849 C  CA  . ASN A 231 ? 0.1539 0.2867 0.1860 0.0055  0.0238  -0.0168 232 ASN A CA  
1850 C  C   . ASN A 231 ? 0.2102 0.2563 0.1815 -0.0036 0.0664  0.0069  232 ASN A C   
1851 O  O   . ASN A 231 ? 0.2159 0.2842 0.0781 -0.0027 0.0284  -0.0113 232 ASN A O   
1852 C  CB  . ASN A 231 ? 0.1980 0.3089 0.1597 -0.0021 0.0150  -0.0451 232 ASN A CB  
1853 C  CG  . ASN A 231 ? 0.2337 0.2624 0.1562 0.0141  -0.0637 0.0209  232 ASN A CG  
1854 O  OD1 . ASN A 231 ? 0.2199 0.2786 0.1324 0.0411  -0.0297 -0.0013 232 ASN A OD1 
1855 N  ND2 . ASN A 231 ? 0.2365 0.2924 0.1409 0.0330  -0.0394 -0.0001 232 ASN A ND2 
1856 N  N   . GLY A 232 ? 0.1543 0.2546 0.2010 -0.0150 0.0143  0.0314  233 GLY A N   
1857 C  CA  . GLY A 232 ? 0.2675 0.2328 0.1863 0.0262  0.0051  0.0021  233 GLY A CA  
1858 C  C   . GLY A 232 ? 0.2503 0.2519 0.1808 0.0044  0.0639  0.0095  233 GLY A C   
1859 O  O   . GLY A 232 ? 0.2744 0.2723 0.2294 0.0136  0.1063  0.0364  233 GLY A O   
1860 N  N   . GLU A 233 ? 0.2431 0.2982 0.1808 0.0190  0.0480  0.0093  234 GLU A N   
1861 C  CA  . GLU A 233 ? 0.2714 0.2741 0.1835 0.0391  0.0730  0.0198  234 GLU A CA  
1862 C  C   . GLU A 233 ? 0.2745 0.3114 0.1948 0.0168  0.0592  0.0815  234 GLU A C   
1863 O  O   . GLU A 233 ? 0.2649 0.3623 0.1230 0.0038  0.0728  0.0372  234 GLU A O   
1864 C  CB  . GLU A 233 ? 0.3707 0.4611 0.1510 0.0332  0.0630  0.1098  234 GLU A CB  
1865 C  CG  . GLU A 233 ? 0.2925 0.5396 0.1102 0.0388  -0.0584 0.1421  234 GLU A CG  
1866 N  N   . GLY A 234 ? 0.3169 0.3479 0.2917 0.0335  0.0759  0.0363  235 GLY A N   
1867 C  CA  . GLY A 234 ? 0.3876 0.3674 0.3764 0.0716  0.1643  0.0337  235 GLY A CA  
1868 C  C   . GLY A 234 ? 0.3560 0.3933 0.3859 0.0582  0.1674  0.0359  235 GLY A C   
1869 O  O   . GLY A 234 ? 0.3696 0.4632 0.5482 0.0974  0.1963  0.1105  235 GLY A O   
1870 N  N   . GLU A 235 ? 0.3145 0.3208 0.3259 0.0330  0.0938  0.0297  236 GLU A N   
1871 C  CA  . GLU A 235 ? 0.1808 0.3044 0.3141 -0.0171 0.0746  -0.0453 236 GLU A CA  
1872 C  C   . GLU A 235 ? 0.2045 0.3297 0.2507 0.0243  0.0312  -0.0178 236 GLU A C   
1873 O  O   . GLU A 235 ? 0.2222 0.3206 0.2170 -0.0089 0.0604  0.0102  236 GLU A O   
1874 C  CB  . GLU A 235 ? 0.3233 0.3039 0.3484 -0.0440 0.1232  -0.0557 236 GLU A CB  
1875 C  CG  . GLU A 235 ? 0.3362 0.3376 0.4724 -0.1280 0.2001  -0.0368 236 GLU A CG  
1876 C  CD  . GLU A 235 ? 0.3580 0.3336 0.6467 -0.0784 0.1209  -0.1351 236 GLU A CD  
1877 O  OE1 . GLU A 235 ? 0.2541 0.4089 0.5696 -0.0836 -0.0036 -0.0271 236 GLU A OE1 
1878 O  OE2 . GLU A 235 ? 0.4354 0.3885 0.8447 -0.1094 0.0817  0.1192  236 GLU A OE2 
1879 N  N   . PRO A 236 ? 0.2181 0.3391 0.1668 0.0289  0.0037  -0.0447 237 PRO A N   
1880 C  CA  . PRO A 236 ? 0.2163 0.3088 0.2154 0.0790  0.0189  -0.0516 237 PRO A CA  
1881 C  C   . PRO A 236 ? 0.2177 0.3340 0.2561 0.0412  0.0201  -0.0528 237 PRO A C   
1882 O  O   . PRO A 236 ? 0.2321 0.3328 0.2535 0.0433  0.0253  -0.0591 237 PRO A O   
1883 C  CB  . PRO A 236 ? 0.2719 0.4648 0.2816 0.0694  -0.0769 -0.1238 237 PRO A CB  
1884 C  CG  . PRO A 236 ? 0.3426 0.4572 0.3805 0.0801  -0.1442 -0.0254 237 PRO A CG  
1885 C  CD  . PRO A 236 ? 0.1969 0.4830 0.5023 0.0562  -0.0759 -0.0455 237 PRO A CD  
1886 N  N   . GLU A 237 ? 0.2551 0.3063 0.1079 0.0416  0.0156  -0.0148 238 GLU A N   
1887 C  CA  . GLU A 237 ? 0.2728 0.3252 0.0860 0.0111  0.0209  0.0085  238 GLU A CA  
1888 C  C   . GLU A 237 ? 0.3005 0.3238 0.0863 0.0958  0.0301  -0.0100 238 GLU A C   
1889 O  O   . GLU A 237 ? 0.3319 0.3098 0.1669 0.1045  0.0767  0.0233  238 GLU A O   
1890 C  CB  . GLU A 237 ? 0.2422 0.2760 0.2093 0.0231  0.0148  0.0085  238 GLU A CB  
1891 C  CG  . GLU A 237 ? 0.2762 0.3708 0.2724 -0.0085 0.0188  -0.0133 238 GLU A CG  
1892 C  CD  . GLU A 237 ? 0.3496 0.3044 0.2305 0.0242  0.0377  0.0159  238 GLU A CD  
1893 O  OE1 . GLU A 237 ? 0.4361 0.4573 0.3604 -0.0447 0.1054  -0.1085 238 GLU A OE1 
1894 O  OE2 . GLU A 237 ? 0.4080 0.5025 0.3649 -0.0716 0.0162  0.0651  238 GLU A OE2 
1895 N  N   . GLU A 238 ? 0.2405 0.2776 0.1457 0.1053  0.0399  0.0222  239 GLU A N   
1896 C  CA  . GLU A 238 ? 0.2423 0.3015 0.1344 0.0627  0.0633  0.0139  239 GLU A CA  
1897 C  C   . GLU A 238 ? 0.2160 0.2329 0.0905 0.0334  -0.0017 -0.0158 239 GLU A C   
1898 O  O   . GLU A 238 ? 0.2262 0.2301 0.1502 0.0436  -0.0013 0.0357  239 GLU A O   
1899 C  CB  . GLU A 238 ? 0.2183 0.4040 0.2308 0.0140  -0.0428 0.0408  239 GLU A CB  
1900 C  CG  . GLU A 238 ? 0.2548 0.4783 0.3955 0.0031  0.0131  -0.0648 239 GLU A CG  
1901 C  CD  . GLU A 238 ? 0.6091 0.6103 0.5916 -0.1314 -0.1233 -0.1357 239 GLU A CD  
1902 O  OE1 . GLU A 238 ? 0.6615 0.6562 0.7223 -0.0245 0.0071  -0.0323 239 GLU A OE1 
1903 O  OE2 . GLU A 238 ? 0.7072 0.8971 0.5000 -0.4831 -0.0378 -0.1856 239 GLU A OE2 
1904 N  N   . LEU A 239 ? 0.2583 0.2531 0.1324 0.0356  0.0122  0.0226  240 LEU A N   
1905 C  CA  . LEU A 239 ? 0.2188 0.2569 0.0713 0.0431  -0.0693 0.0195  240 LEU A CA  
1906 C  C   . LEU A 239 ? 0.1805 0.2388 0.0985 0.0344  -0.0148 0.0108  240 LEU A C   
1907 O  O   . LEU A 239 ? 0.1812 0.2445 0.1152 0.0450  -0.0287 0.0283  240 LEU A O   
1908 C  CB  . LEU A 239 ? 0.3945 0.2534 0.0901 0.0478  -0.0177 0.0125  240 LEU A CB  
1909 C  CG  . LEU A 239 ? 0.3694 0.2993 0.3926 -0.0575 -0.1901 0.0601  240 LEU A CG  
1910 C  CD1 . LEU A 239 ? 0.2864 0.3317 0.4211 0.0313  -0.0465 0.0795  240 LEU A CD1 
1911 C  CD2 . LEU A 239 ? 0.2970 0.2971 0.1352 -0.0289 -0.1023 -0.0196 240 LEU A CD2 
1912 N  N   . MET A 240 ? 0.1887 0.2064 0.0951 0.0364  0.0121  0.0025  241 MET A N   
1913 C  CA  . MET A 240 ? 0.1256 0.2188 0.1032 0.0508  0.0242  0.0175  241 MET A CA  
1914 C  C   . MET A 240 ? 0.1576 0.2492 0.0973 0.0038  -0.0139 0.0234  241 MET A C   
1915 O  O   . MET A 240 ? 0.1518 0.2445 0.0835 0.0018  0.0162  0.0076  241 MET A O   
1916 C  CB  . MET A 240 ? 0.1715 0.1777 0.1086 0.0515  0.0203  0.0037  241 MET A CB  
1917 C  CG  . MET A 240 ? 0.1888 0.2420 0.0946 0.0253  -0.0042 -0.0164 241 MET A CG  
1918 S  SD  . MET A 240 ? 0.1813 0.2354 0.1113 0.0151  -0.0171 -0.0006 241 MET A SD  
1919 C  CE  . MET A 240 ? 0.2146 0.2926 0.0675 0.0124  -0.0013 0.0303  241 MET A CE  
1920 N  N   . VAL A 241 ? 0.1971 0.1909 0.0826 -0.0070 -0.0303 0.0103  242 VAL A N   
1921 C  CA  . VAL A 241 ? 0.1587 0.1977 0.0921 -0.0173 -0.0384 -0.0025 242 VAL A CA  
1922 C  C   . VAL A 241 ? 0.1489 0.1802 0.0759 0.0121  -0.0220 -0.0089 242 VAL A C   
1923 O  O   . VAL A 241 ? 0.1678 0.2468 0.1107 0.0052  -0.0196 0.0186  242 VAL A O   
1924 C  CB  . VAL A 241 ? 0.1468 0.2084 0.0886 -0.0065 -0.0494 -0.0145 242 VAL A CB  
1925 C  CG1 . VAL A 241 ? 0.1917 0.2754 0.0955 -0.0055 -0.0686 -0.0461 242 VAL A CG1 
1926 C  CG2 . VAL A 241 ? 0.1655 0.2120 0.1899 0.0198  -0.0173 -0.0108 242 VAL A CG2 
1927 N  N   . ASP A 242 ? 0.1470 0.1802 0.0410 -0.0035 -0.0460 -0.0108 243 ASP A N   
1928 C  CA  . ASP A 242 ? 0.1619 0.1874 0.0697 0.0111  -0.0798 -0.0089 243 ASP A CA  
1929 C  C   . ASP A 242 ? 0.1445 0.1694 0.1009 0.0030  -0.0179 0.0023  243 ASP A C   
1930 O  O   . ASP A 242 ? 0.1605 0.2246 0.1338 -0.0049 -0.0453 0.0104  243 ASP A O   
1931 C  CB  . ASP A 242 ? 0.1765 0.1694 0.1206 0.0182  -0.0266 -0.0218 243 ASP A CB  
1932 C  CG  . ASP A 242 ? 0.1659 0.1920 0.0976 0.0032  -0.0436 -0.0095 243 ASP A CG  
1933 O  OD1 . ASP A 242 ? 0.1671 0.2168 0.1062 0.0026  -0.0275 0.0016  243 ASP A OD1 
1934 O  OD2 . ASP A 242 ? 0.2027 0.2174 0.1623 0.0395  -0.0313 -0.0135 243 ASP A OD2 
1935 N  N   . ASN A 243 ? 0.1704 0.1773 0.0253 0.0187  -0.0294 0.0032  244 ASN A N   
1936 C  CA  . ASN A 243 ? 0.1208 0.1658 0.0468 0.0245  -0.0423 0.0153  244 ASN A CA  
1937 C  C   . ASN A 243 ? 0.1787 0.1344 0.0957 -0.0165 -0.0136 -0.0276 244 ASN A C   
1938 O  O   . ASN A 243 ? 0.1880 0.2125 0.0880 0.0265  -0.0353 0.0117  244 ASN A O   
1939 C  CB  . ASN A 243 ? 0.1147 0.1982 0.0797 0.0089  -0.0732 0.0370  244 ASN A CB  
1940 C  CG  . ASN A 243 ? 0.1004 0.1892 0.1045 0.0062  -0.0312 0.0155  244 ASN A CG  
1941 O  OD1 . ASN A 243 ? 0.1355 0.2104 0.1317 -0.0146 -0.0383 0.0201  244 ASN A OD1 
1942 N  ND2 . ASN A 243 ? 0.1353 0.2134 0.1508 0.0179  -0.0697 0.0264  244 ASN A ND2 
1943 N  N   . TRP A 244 ? 0.1429 0.1946 0.0819 0.0145  -0.0084 -0.0119 245 TRP A N   
1944 C  CA  . TRP A 244 ? 0.1511 0.1468 0.0555 0.0072  -0.0430 -0.0214 245 TRP A CA  
1945 C  C   . TRP A 244 ? 0.1565 0.1845 0.0516 0.0245  -0.0440 0.0031  245 TRP A C   
1946 O  O   . TRP A 244 ? 0.1824 0.2183 0.0776 0.0329  -0.0258 -0.0113 245 TRP A O   
1947 C  CB  . TRP A 244 ? 0.1605 0.1917 0.0513 -0.0025 -0.0508 -0.0048 245 TRP A CB  
1948 C  CG  . TRP A 244 ? 0.1532 0.1942 0.0612 0.0143  -0.0312 -0.0013 245 TRP A CG  
1949 C  CD1 . TRP A 244 ? 0.1784 0.1698 0.0721 -0.0039 0.0201  -0.0094 245 TRP A CD1 
1950 C  CD2 . TRP A 244 ? 0.2003 0.2064 0.0797 0.0105  -0.0390 0.0201  245 TRP A CD2 
1951 N  NE1 . TRP A 244 ? 0.1589 0.1860 0.0804 0.0033  -0.0362 0.0177  245 TRP A NE1 
1952 C  CE2 . TRP A 244 ? 0.2118 0.2301 0.0740 0.0230  -0.0240 0.0290  245 TRP A CE2 
1953 C  CE3 . TRP A 244 ? 0.1611 0.2371 0.0702 0.0145  -0.0137 0.0284  245 TRP A CE3 
1954 C  CZ2 . TRP A 244 ? 0.1770 0.2093 0.1276 -0.0359 -0.0999 0.0239  245 TRP A CZ2 
1955 C  CZ3 . TRP A 244 ? 0.1581 0.2140 0.1248 -0.0195 -0.0446 0.0265  245 TRP A CZ3 
1956 C  CH2 . TRP A 244 ? 0.1874 0.2054 0.1216 -0.0026 -0.0831 0.0207  245 TRP A CH2 
1957 N  N   . ARG A 245 ? 0.1432 0.2136 0.0831 0.0039  -0.0666 -0.0392 246 ARG A N   
1958 C  CA  . ARG A 245 ? 0.1309 0.2106 0.0765 -0.0230 -0.0622 0.0155  246 ARG A CA  
1959 C  C   . ARG A 245 ? 0.1317 0.2092 0.0655 -0.0177 -0.0517 0.0002  246 ARG A C   
1960 O  O   . ARG A 245 ? 0.1398 0.2741 0.0741 -0.0092 -0.0425 -0.0210 246 ARG A O   
1961 C  CB  . ARG A 245 ? 0.1403 0.2140 0.0522 -0.0355 -0.0677 -0.0138 246 ARG A CB  
1962 C  CG  . ARG A 245 ? 0.1231 0.2519 0.0644 0.0076  -0.0712 -0.0198 246 ARG A CG  
1963 C  CD  . ARG A 245 ? 0.1217 0.2582 0.0470 -0.0018 -0.0476 -0.0273 246 ARG A CD  
1964 N  NE  . ARG A 245 ? 0.1219 0.2789 0.0666 -0.0231 -0.0525 -0.0004 246 ARG A NE  
1965 C  CZ  . ARG A 245 ? 0.1353 0.2447 0.1134 -0.0322 -0.0339 0.0043  246 ARG A CZ  
1966 N  NH1 . ARG A 245 ? 0.1586 0.2734 0.1163 -0.0134 -0.0557 -0.0004 246 ARG A NH1 
1967 N  NH2 . ARG A 245 ? 0.1418 0.3172 0.1122 -0.0422 -0.0383 -0.0156 246 ARG A NH2 
1968 N  N   . PRO A 246 ? 0.1632 0.2181 0.0824 0.0175  -0.0397 0.0095  247 PRO A N   
1969 C  CA  . PRO A 246 ? 0.1964 0.2563 0.0993 0.0113  0.0055  0.0163  247 PRO A CA  
1970 C  C   . PRO A 246 ? 0.1905 0.1974 0.0754 0.0239  -0.0269 0.0395  247 PRO A C   
1971 O  O   . PRO A 246 ? 0.2286 0.2233 0.0571 0.0051  -0.0356 -0.0034 247 PRO A O   
1972 C  CB  . PRO A 246 ? 0.2197 0.2912 0.0768 0.0411  -0.0348 0.0032  247 PRO A CB  
1973 C  CG  . PRO A 246 ? 0.2099 0.3367 0.1993 0.0949  0.0069  0.0973  247 PRO A CG  
1974 C  CD  . PRO A 246 ? 0.1529 0.2655 0.1144 0.0148  -0.0436 0.0445  247 PRO A CD  
1975 N  N   . ALA A 247 ? 0.1971 0.2569 0.0513 -0.0095 -0.0272 0.0166  248 ALA A N   
1976 C  CA  . ALA A 247 ? 0.1881 0.2578 0.0648 -0.0395 -0.0212 -0.0042 248 ALA A CA  
1977 C  C   . ALA A 247 ? 0.1916 0.2329 0.1011 -0.0316 -0.0474 0.0469  248 ALA A C   
1978 O  O   . ALA A 247 ? 0.2657 0.2909 0.0634 0.0221  -0.0614 0.0204  248 ALA A O   
1979 C  CB  . ALA A 247 ? 0.2163 0.2876 0.0459 -0.0308 -0.0157 0.0209  248 ALA A CB  
1980 N  N   . GLN A 248 ? 0.1651 0.2286 0.1134 -0.0168 -0.0665 0.0267  249 GLN A N   
1981 C  CA  . GLN A 248 ? 0.1870 0.2498 0.1075 -0.0354 -0.0678 0.0322  249 GLN A CA  
1982 C  C   . GLN A 248 ? 0.1831 0.2624 0.1120 -0.0107 -0.0543 0.0318  249 GLN A C   
1983 O  O   . GLN A 248 ? 0.2152 0.2904 0.0691 -0.0261 -0.0550 0.0121  249 GLN A O   
1984 C  CB  . GLN A 248 ? 0.2020 0.2308 0.0633 -0.0336 -0.0131 0.0087  249 GLN A CB  
1985 C  CG  . GLN A 248 ? 0.1930 0.2569 0.0481 -0.0086 -0.0484 0.0113  249 GLN A CG  
1986 C  CD  . GLN A 248 ? 0.1996 0.2472 0.0749 -0.0053 -0.0506 -0.0155 249 GLN A CD  
1987 O  OE1 . GLN A 248 ? 0.1996 0.3547 0.1061 -0.0122 -0.0465 -0.0416 249 GLN A OE1 
1988 N  NE2 . GLN A 248 ? 0.2294 0.2929 0.0527 0.0183  -0.0093 -0.0280 249 GLN A NE2 
1989 N  N   . PRO A 249 ? 0.1953 0.3169 0.0725 0.0127  -0.0458 0.0232  250 PRO A N   
1990 C  CA  . PRO A 249 ? 0.1659 0.3546 0.0636 0.0153  -0.0636 -0.0048 250 PRO A CA  
1991 C  C   . PRO A 249 ? 0.2212 0.2840 0.1025 -0.0006 -0.0558 0.0104  250 PRO A C   
1992 O  O   . PRO A 249 ? 0.2141 0.2920 0.0621 -0.0006 -0.0554 0.0110  250 PRO A O   
1993 C  CB  . PRO A 249 ? 0.1812 0.3899 0.0815 0.0354  -0.0938 -0.0417 250 PRO A CB  
1994 C  CG  . PRO A 249 ? 0.2225 0.4583 0.0577 -0.0487 -0.0833 0.0253  250 PRO A CG  
1995 C  CD  . PRO A 249 ? 0.1989 0.3629 0.0572 -0.0398 -0.0776 0.0089  250 PRO A CD  
1996 N  N   . LEU A 250 ? 0.2427 0.3192 0.0234 0.0170  -0.0527 -0.0006 251 LEU A N   
1997 C  CA  . LEU A 250 ? 0.2262 0.3011 0.0721 -0.0105 -0.0453 -0.0021 251 LEU A CA  
1998 C  C   . LEU A 250 ? 0.2139 0.2657 0.0204 0.0071  -0.0438 0.0336  251 LEU A C   
1999 O  O   . LEU A 250 ? 0.2215 0.2932 0.0433 -0.0215 -0.0355 0.0115  251 LEU A O   
2000 C  CB  . LEU A 250 ? 0.2463 0.2820 0.0648 0.0027  -0.0707 0.0477  251 LEU A CB  
2001 C  CG  . LEU A 250 ? 0.3001 0.2735 0.0358 0.0196  -0.0643 0.0456  251 LEU A CG  
2002 C  CD1 . LEU A 250 ? 0.2445 0.4131 0.1188 0.0623  -0.1634 -0.0323 251 LEU A CD1 
2003 C  CD2 . LEU A 250 ? 0.3116 0.4048 0.0564 -0.0222 -0.0343 0.0573  251 LEU A CD2 
2004 N  N   . LYS A 251 ? 0.2644 0.2818 0.0838 -0.0055 -0.1186 0.0178  252 LYS A N   
2005 C  CA  . LYS A 251 ? 0.3267 0.3324 0.0627 -0.0469 -0.0641 -0.0275 252 LYS A CA  
2006 C  C   . LYS A 251 ? 0.3105 0.3863 0.0646 -0.0167 -0.0816 0.0009  252 LYS A C   
2007 O  O   . LYS A 251 ? 0.3698 0.3906 0.1342 0.0004  -0.0248 0.0318  252 LYS A O   
2008 C  CB  . LYS A 251 ? 0.2447 0.3280 0.2136 -0.0422 -0.0499 -0.0113 252 LYS A CB  
2009 C  CG  . LYS A 251 ? 0.3812 0.3768 0.2157 -0.0298 0.0261  -0.0068 252 LYS A CG  
2010 C  CD  . LYS A 251 ? 0.4301 0.3109 0.1899 -0.0544 -0.0203 -0.0089 252 LYS A CD  
2011 C  CE  . LYS A 251 ? 0.3439 0.4873 0.4552 -0.0314 -0.0020 0.0854  252 LYS A CE  
2012 N  NZ  . LYS A 251 ? 0.4075 0.4093 0.4292 0.0579  0.0911  0.0688  252 LYS A NZ  
2013 N  N   . ASN A 252 ? 0.2993 0.3878 0.0488 0.0039  -0.1116 0.0022  253 ASN A N   
2014 C  CA  . ASN A 252 ? 0.3331 0.4434 0.1449 -0.0275 -0.0256 -0.0521 253 ASN A CA  
2015 C  C   . ASN A 252 ? 0.3604 0.6860 0.1418 0.0666  -0.0776 -0.0846 253 ASN A C   
2016 O  O   . ASN A 252 ? 0.3925 0.7345 0.1612 0.0978  -0.0475 -0.0453 253 ASN A O   
2017 C  CB  . ASN A 252 ? 0.4078 0.4757 0.1238 0.0280  -0.1118 -0.0635 253 ASN A CB  
2018 N  N   . ARG A 253 ? 0.2805 0.3723 0.0932 0.0740  -0.0351 0.0143  254 ARG A N   
2019 C  CA  . ARG A 253 ? 0.2427 0.3612 0.0139 0.0148  -0.0358 0.0256  254 ARG A CA  
2020 C  C   . ARG A 253 ? 0.3170 0.3825 0.0316 -0.0370 -0.0355 -0.0446 254 ARG A C   
2021 O  O   . ARG A 253 ? 0.3503 0.3718 0.1892 -0.0175 0.0753  -0.0080 254 ARG A O   
2022 C  CB  . ARG A 253 ? 0.2551 0.3534 0.0207 -0.0154 -0.0586 0.0174  254 ARG A CB  
2023 C  CG  . ARG A 253 ? 0.3028 0.2671 0.0394 -0.0190 -0.0425 0.0058  254 ARG A CG  
2024 C  CD  . ARG A 253 ? 0.2213 0.2938 0.0382 0.0249  -0.0791 0.0027  254 ARG A CD  
2025 N  NE  . ARG A 253 ? 0.2131 0.3001 0.0736 0.0002  -0.0441 -0.0122 254 ARG A NE  
2026 C  CZ  . ARG A 253 ? 0.1702 0.2418 0.0741 -0.0017 -0.0530 0.0212  254 ARG A CZ  
2027 N  NH1 . ARG A 253 ? 0.1317 0.2429 0.0642 0.0065  -0.0715 -0.0074 254 ARG A NH1 
2028 N  NH2 . ARG A 253 ? 0.1633 0.2723 0.0493 -0.0011 -0.0719 0.0060  254 ARG A NH2 
2029 N  N   . GLN A 254 ? 0.3092 0.4232 0.0635 -0.0212 -0.0675 -0.0356 255 GLN A N   
2030 C  CA  . GLN A 254 ? 0.2678 0.3991 0.0937 -0.0100 -0.0915 -0.0797 255 GLN A CA  
2031 C  C   . GLN A 254 ? 0.2851 0.3170 0.1288 -0.0264 -0.1221 0.0335  255 GLN A C   
2032 O  O   . GLN A 254 ? 0.3644 0.3152 0.1708 -0.0538 -0.1042 -0.0212 255 GLN A O   
2033 C  CB  . GLN A 254 ? 0.3993 0.4673 0.0418 -0.0981 -0.0347 -0.1101 255 GLN A CB  
2034 C  CG  . GLN A 254 ? 0.4747 0.6636 0.1431 -0.0564 -0.1476 -0.0370 255 GLN A CG  
2035 N  N   . ILE A 255 ? 0.2750 0.3013 0.0335 -0.0161 -0.0732 0.0504  256 ILE A N   
2036 C  CA  . ILE A 255 ? 0.1849 0.2645 0.0294 0.0108  -0.0514 0.0430  256 ILE A CA  
2037 C  C   . ILE A 255 ? 0.2350 0.2384 0.0758 -0.0100 0.0047  0.0027  256 ILE A C   
2038 O  O   . ILE A 255 ? 0.2606 0.3312 0.0680 -0.0380 -0.0295 0.0477  256 ILE A O   
2039 C  CB  . ILE A 255 ? 0.2157 0.3064 0.0231 -0.0055 -0.0358 0.0093  256 ILE A CB  
2040 C  CG1 . ILE A 255 ? 0.1901 0.2749 0.1077 0.0414  -0.0539 -0.0026 256 ILE A CG1 
2041 C  CG2 . ILE A 255 ? 0.2611 0.2904 0.0648 0.0458  -0.0833 0.0243  256 ILE A CG2 
2042 C  CD1 . ILE A 255 ? 0.2268 0.2859 0.1784 -0.0201 0.0321  -0.0447 256 ILE A CD1 
2043 N  N   . LYS A 256 ? 0.2334 0.3323 0.0178 0.0195  -0.0509 -0.0098 257 LYS A N   
2044 C  CA  . LYS A 256 ? 0.2511 0.3223 0.0185 -0.0332 -0.0418 -0.0339 257 LYS A CA  
2045 C  C   . LYS A 256 ? 0.1739 0.3235 0.0142 -0.0101 -0.0289 -0.0283 257 LYS A C   
2046 O  O   . LYS A 256 ? 0.2390 0.3574 0.0070 -0.0537 0.0092  -0.0130 257 LYS A O   
2047 C  CB  . LYS A 256 ? 0.2558 0.3152 0.0628 -0.0337 -0.0414 -0.0577 257 LYS A CB  
2048 C  CG  . LYS A 256 ? 0.2576 0.3147 0.0835 -0.0399 -0.0097 -0.0969 257 LYS A CG  
2049 C  CD  . LYS A 256 ? 0.2761 0.3410 0.1921 -0.0267 0.0624  -0.1729 257 LYS A CD  
2050 C  CE  . LYS A 256 ? 0.5205 0.4055 0.2427 -0.1086 -0.0285 -0.1947 257 LYS A CE  
2051 N  NZ  . LYS A 256 ? 0.2601 0.4792 0.4020 -0.0831 0.0292  -0.0825 257 LYS A NZ  
2052 N  N   . ALA A 257 ? 0.2031 0.3206 0.0637 -0.0576 -0.0214 -0.0079 258 ALA A N   
2053 C  CA  . ALA A 257 ? 0.2035 0.2637 0.0107 -0.0280 -0.0055 -0.0233 258 ALA A CA  
2054 C  C   . ALA A 257 ? 0.2291 0.2671 0.0119 -0.0020 -0.0183 0.0187  258 ALA A C   
2055 O  O   . ALA A 257 ? 0.2357 0.3058 0.0269 0.0257  -0.0030 -0.0049 258 ALA A O   
2056 C  CB  . ALA A 257 ? 0.2494 0.2815 0.1626 -0.0122 0.0137  0.0339  258 ALA A CB  
2057 N  N   . SER A 258 ? 0.2314 0.2598 0.0486 0.0201  -0.0479 0.0253  259 SER A N   
2058 C  CA  . SER A 258 ? 0.2505 0.2697 0.0803 0.0152  0.0295  0.0588  259 SER A CA  
2059 C  C   . SER A 258 ? 0.2336 0.2838 0.0504 -0.0038 0.0021  0.0091  259 SER A C   
2060 O  O   . SER A 258 ? 0.2193 0.3779 0.1686 0.0006  0.0286  0.0392  259 SER A O   
2061 C  CB  . SER A 258 ? 0.2440 0.2658 0.0745 0.0011  -0.0077 0.0167  259 SER A CB  
2062 O  OG  . SER A 258 ? 0.1960 0.2851 0.0917 0.0190  -0.0322 -0.0086 259 SER A OG  
2063 N  N   . PHE A 259 ? 0.2647 0.3005 0.0136 -0.0318 -0.0041 0.0465  260 PHE A N   
2064 C  CA  . PHE A 259 ? 0.2477 0.2842 0.1429 -0.0234 -0.0048 0.0199  260 PHE A CA  
2065 C  C   . PHE A 259 ? 0.3035 0.4542 0.1743 -0.0222 -0.0443 0.0924  260 PHE A C   
2066 O  O   . PHE A 259 ? 0.3273 0.3294 0.1104 -0.0432 -0.0822 0.0609  260 PHE A O   
2067 C  CB  . PHE A 259 ? 0.2035 0.3120 0.1707 -0.0276 -0.0792 0.0036  260 PHE A CB  
2068 C  CG  . PHE A 259 ? 0.1988 0.3181 0.1759 -0.0091 -0.0707 0.0485  260 PHE A CG  
2069 C  CD1 . PHE A 259 ? 0.2147 0.3272 0.0798 0.0075  -0.0614 -0.0093 260 PHE A CD1 
2070 C  CD2 . PHE A 259 ? 0.2760 0.3258 0.2014 0.0140  -0.0174 0.0413  260 PHE A CD2 
2071 C  CE1 . PHE A 259 ? 0.2314 0.3436 0.0656 0.0344  -0.1154 -0.0208 260 PHE A CE1 
2072 C  CE2 . PHE A 259 ? 0.3323 0.2675 0.2256 0.0222  0.0206  0.0461  260 PHE A CE2 
2073 C  CZ  . PHE A 259 ? 0.2207 0.3160 0.0882 0.0323  -0.0304 -0.0127 260 PHE A CZ  
2074 N  N   . LYS A 260 ? 0.3206 0.6111 0.3375 -0.0306 0.0605  0.1242  261 LYS A N   
2075 C  CA  . LYS A 260 ? 0.6362 0.6646 0.5314 0.0594  0.0861  0.2291  261 LYS A CA  
2076 C  C   . LYS A 260 ? 0.5475 0.9531 0.4558 0.1197  0.2618  0.2800  261 LYS A C   
2077 O  O   . LYS A 260 ? 0.5890 1.0455 0.8262 0.2940  0.1285  0.4358  261 LYS A O   
2078 C  CB  . LYS A 260 ? 0.7658 0.5551 0.5271 -0.0071 0.4449  0.0679  261 LYS A CB  
2079 C  CG  . LYS A 260 ? 0.7109 0.6540 0.8532 -0.1515 0.1331  0.1764  261 LYS A CG  
2080 ZN ZN  . ZN  B .   ? 0.1583 0.2192 0.0428 0.0081  -0.0562 -0.0097 301 ZN  A ZN  
2081 S  S   . DMS C .   ? 0.3361 0.4025 0.2721 -0.0231 -0.0647 -0.0363 302 DMS A S   
2082 O  O   . DMS C .   ? 0.5213 0.3931 0.4165 -0.0367 0.0378  -0.1190 302 DMS A O   
2083 C  C1  . DMS C .   ? 0.3118 0.3758 0.2146 0.0631  -0.0103 -0.0723 302 DMS A C1  
2084 C  C2  . DMS C .   ? 0.3674 0.3446 0.4778 -0.0444 -0.0175 -0.0253 302 DMS A C2  
2085 C  C6  . OQW D .   ? 0.3142 0.3240 0.2606 0.0089  0.0780  -0.0075 303 OQW A C6  
2086 C  C4  . OQW D .   ? 0.2333 0.3285 0.0847 -0.0493 -0.0633 -0.0412 303 OQW A C4  
2087 C  C3  . OQW D .   ? 0.2211 0.3212 0.1439 -0.0668 -0.0891 -0.0157 303 OQW A C3  
2088 O  O1  . OQW D .   ? 0.3195 0.3143 0.1407 -0.0533 -0.0980 -0.0602 303 OQW A O1  
2089 C  C8  . OQW D .   ? 0.3652 0.3698 0.1920 0.0934  0.0693  -0.0428 303 OQW A C8  
2090 C  C11 . OQW D .   ? 0.2377 0.3536 0.2583 -0.0417 -0.0363 -0.1218 303 OQW A C11 
2091 C  C13 . OQW D .   ? 0.2011 0.3136 0.1756 0.0100  -0.0216 -0.1112 303 OQW A C13 
2092 C  C14 . OQW D .   ? 0.3021 0.3137 0.2129 -0.0029 0.0142  -0.0923 303 OQW A C14 
2093 C  C9  . OQW D .   ? 0.3492 0.3333 0.1597 0.0460  0.0256  -0.0367 303 OQW A C9  
2094 C  C15 . OQW D .   ? 0.2232 0.3807 0.1429 0.0565  0.0104  -0.0414 303 OQW A C15 
2095 C  C16 . OQW D .   ? 0.2498 0.3607 0.2857 0.0126  0.0417  0.0122  303 OQW A C16 
2096 C  C17 . OQW D .   ? 0.3759 0.4041 0.2228 0.0433  -0.0779 -0.0052 303 OQW A C17 
2097 C  C20 . OQW D .   ? 0.2608 0.3902 0.2082 0.0219  -0.0165 0.0223  303 OQW A C20 
2098 C  C19 . OQW D .   ? 0.3529 0.4652 0.1289 -0.1258 -0.0245 -0.0500 303 OQW A C19 
2099 C  C18 . OQW D .   ? 0.3648 0.4000 0.0560 0.0186  -0.1307 0.0175  303 OQW A C18 
2100 O  O22 . OQW D .   ? 0.2330 0.2839 0.2525 0.0098  -0.0971 -0.0152 303 OQW A O22 
2101 S  S2  . OQW D .   ? 0.2442 0.3384 0.1522 -0.0073 -0.0732 0.0076  303 OQW A S2  
2102 N  N21 . OQW D .   ? 0.3048 0.5935 0.1003 0.1571  -0.1509 -0.1738 303 OQW A N21 
2103 F  F10 . OQW D .   ? 0.4022 0.3589 0.1317 0.0807  0.0293  -0.0301 303 OQW A F10 
2104 F  F7  . OQW D .   ? 0.3346 0.3347 0.3449 0.0134  0.0783  -0.0241 303 OQW A F7  
2105 F  F5  . OQW D .   ? 0.2664 0.3767 0.1399 -0.0361 -0.0301 -0.0059 303 OQW A F5  
2106 N  N12 . OQW D .   ? 0.1460 0.3292 0.1597 -0.0468 -0.0245 -0.0862 303 OQW A N12 
2107 O  O   . HOH E .   ? 0.4024 0.3236 0.6478 -0.0170 -0.1214 -0.0424 401 HOH A O   
2108 O  O   . HOH E .   ? 0.1987 0.2240 0.1515 -0.0223 -0.1020 -0.0211 402 HOH A O   
2109 O  O   . HOH E .   ? 0.4798 0.3904 0.1553 0.1444  0.0502  0.0798  403 HOH A O   
2110 O  O   . HOH E .   ? 0.2474 0.3746 0.1174 -0.0419 0.0469  -0.0508 404 HOH A O   
2111 O  O   . HOH E .   ? 0.7172 0.5806 0.4631 0.3122  0.1033  -0.0508 405 HOH A O   
2112 O  O   . HOH E .   ? 0.4569 0.4299 0.3481 0.0110  0.0127  0.0455  406 HOH A O   
2113 O  O   . HOH E .   ? 0.4005 0.3913 0.2681 0.0626  0.0588  -0.0086 407 HOH A O   
2114 O  O   . HOH E .   ? 0.4519 0.3440 0.3619 -0.0502 -0.1372 -0.0994 408 HOH A O   
2115 O  O   . HOH E .   ? 0.3433 0.4853 0.2971 -0.1251 0.0687  -0.0828 409 HOH A O   
2116 O  O   . HOH E .   ? 0.5200 0.4207 0.4529 0.0435  0.0600  0.0707  410 HOH A O   
2117 O  O   . HOH E .   ? 0.1784 0.2431 0.1206 -0.0134 -0.0320 -0.0088 411 HOH A O   
2118 O  O   . HOH E .   ? 0.6020 0.5068 0.4590 0.0114  0.1119  0.1986  412 HOH A O   
2119 O  O   . HOH E .   ? 0.3045 0.4777 0.2940 -0.0171 -0.0384 0.0688  413 HOH A O   
2120 O  O   . HOH E .   ? 0.4268 0.4118 0.4357 0.0020  -0.0038 0.0163  414 HOH A O   
2121 O  O   . HOH E .   ? 0.4143 0.5535 0.3752 0.0996  -0.1559 -0.2154 415 HOH A O   
2122 O  O   . HOH E .   ? 0.2739 0.5280 0.1529 0.0115  0.0042  -0.0469 416 HOH A O   
2123 O  O   . HOH E .   ? 0.3090 0.2625 0.2258 -0.0034 0.0176  -0.0245 417 HOH A O   
2124 O  O   . HOH E .   ? 0.4307 0.2617 0.5619 0.0043  0.0549  0.0859  418 HOH A O   
2125 O  O   . HOH E .   ? 0.3238 0.4972 0.5169 -0.0148 -0.1363 0.0345  419 HOH A O   
2126 O  O   . HOH E .   ? 0.3168 0.5202 0.1461 0.0587  -0.0270 -0.0231 420 HOH A O   
2127 O  O   . HOH E .   ? 0.2853 0.3013 0.1181 0.0055  -0.0146 -0.0094 421 HOH A O   
2128 O  O   . HOH E .   ? 0.3371 0.3510 0.2697 -0.0151 0.0031  -0.0744 422 HOH A O   
2129 O  O   . HOH E .   ? 0.2657 0.8105 0.1569 -0.1385 -0.0212 -0.1270 423 HOH A O   
2130 O  O   . HOH E .   ? 0.4816 0.4720 0.3373 -0.0051 -0.0418 0.0096  424 HOH A O   
2131 O  O   . HOH E .   ? 0.4637 0.3552 0.2282 -0.0281 0.0652  -0.0288 425 HOH A O   
2132 O  O   . HOH E .   ? 0.3442 0.5831 0.2032 -0.0259 -0.0343 0.0030  426 HOH A O   
2133 O  O   . HOH E .   ? 0.3121 0.4268 0.1283 -0.0309 -0.0427 -0.0072 427 HOH A O   
2134 O  O   . HOH E .   ? 0.2677 0.3463 0.1650 -0.0037 0.0394  -0.0699 428 HOH A O   
2135 O  O   . HOH E .   ? 0.3195 0.3111 0.1127 -0.0383 -0.0173 -0.0727 429 HOH A O   
2136 O  O   . HOH E .   ? 0.4140 0.3576 0.1806 -0.0504 -0.0595 0.0016  430 HOH A O   
2137 O  O   . HOH E .   ? 0.2127 0.4876 0.3825 0.0188  -0.1364 -0.0954 431 HOH A O   
2138 O  O   . HOH E .   ? 0.5262 0.3948 0.1344 -0.0902 -0.0295 0.0450  432 HOH A O   
2139 O  O   . HOH E .   ? 0.3611 0.3989 0.2187 0.0225  0.0121  -0.0741 433 HOH A O   
2140 O  O   . HOH E .   ? 0.1673 0.2052 0.1413 -0.0067 0.0053  -0.0313 434 HOH A O   
2141 O  O   . HOH E .   ? 0.2812 0.2833 0.1955 -0.0037 0.0842  -0.0065 435 HOH A O   
2142 O  O   . HOH E .   ? 0.4049 0.5274 0.2350 0.1298  -0.1242 0.0408  436 HOH A O   
2143 O  O   . HOH E .   ? 0.5339 0.5001 0.1553 -0.1404 -0.1402 0.0791  437 HOH A O   
2144 O  O   . HOH E .   ? 0.2646 0.2957 0.1147 -0.0361 0.0223  -0.0535 438 HOH A O   
2145 O  O   . HOH E .   ? 0.2345 0.3795 0.2233 0.0147  0.0069  -0.0291 439 HOH A O   
2146 O  O   . HOH E .   ? 0.3550 0.3145 0.3121 -0.0402 -0.0593 -0.0055 440 HOH A O   
2147 O  O   . HOH E .   ? 0.3314 0.5012 1.0110 -0.1151 -0.0886 0.2782  441 HOH A O   
2148 O  O   . HOH E .   ? 0.3450 0.3553 0.0497 0.0023  -0.0488 0.0150  442 HOH A O   
2149 O  O   . HOH E .   ? 0.3616 0.5404 0.0894 -0.0084 -0.0607 -0.0646 443 HOH A O   
2150 O  O   . HOH E .   ? 0.3766 0.5029 0.2122 -0.0195 -0.1525 0.0893  444 HOH A O   
2151 O  O   . HOH E .   ? 0.2700 0.3628 0.2506 -0.0603 0.0017  -0.0407 445 HOH A O   
2152 O  O   . HOH E .   ? 0.3158 0.5194 0.1331 0.1022  -0.0402 -0.0690 446 HOH A O   
2153 O  O   . HOH E .   ? 0.5424 0.3399 0.2049 0.0263  -0.0187 0.0860  447 HOH A O   
2154 O  O   . HOH E .   ? 0.3404 0.3838 0.7464 0.0208  0.1601  0.0567  448 HOH A O   
2155 O  O   . HOH E .   ? 0.2212 0.2586 0.1079 -0.0153 -0.0802 -0.0046 449 HOH A O   
2156 O  O   . HOH E .   ? 0.2066 0.2940 0.2675 -0.0196 0.0282  0.0253  450 HOH A O   
2157 O  O   . HOH E .   ? 0.2789 0.3198 0.1578 0.0447  -0.0283 -0.0033 451 HOH A O   
2158 O  O   . HOH E .   ? 0.2297 0.3670 0.1142 -0.0358 -0.0023 0.0001  452 HOH A O   
2159 O  O   . HOH E .   ? 0.2714 0.3067 0.3107 -0.0365 -0.0915 -0.0199 453 HOH A O   
2160 O  O   . HOH E .   ? 0.2474 0.3746 0.2459 -0.0234 -0.1005 -0.0329 454 HOH A O   
2161 O  O   . HOH E .   ? 0.3398 0.4371 0.0838 -0.0266 -0.0727 0.0250  455 HOH A O   
2162 O  O   . HOH E .   ? 0.2637 0.4075 0.1034 -0.0134 0.0252  -0.0451 456 HOH A O   
2163 O  O   . HOH E .   ? 0.3201 0.3486 0.4153 -0.0040 -0.0870 -0.0412 457 HOH A O   
2164 O  O   . HOH E .   ? 0.5201 0.3424 0.1296 0.0295  0.0004  0.0507  458 HOH A O   
2165 O  O   . HOH E .   ? 0.4384 0.4048 0.1012 -0.0173 -0.0394 0.0809  459 HOH A O   
2166 O  O   . HOH E .   ? 0.2452 0.2477 0.2373 0.0350  -0.0497 0.0067  460 HOH A O   
2167 O  O   . HOH E .   ? 0.2499 0.5588 0.1145 -0.0054 -0.0263 -0.0635 461 HOH A O   
2168 O  O   . HOH E .   ? 0.4208 0.4266 0.4557 0.0105  0.0139  -0.0281 462 HOH A O   
2169 O  O   . HOH E .   ? 0.1669 0.2284 0.1093 -0.0228 -0.0457 0.0068  463 HOH A O   
2170 O  O   . HOH E .   ? 0.2205 0.4381 0.1107 0.0368  0.0055  0.0749  464 HOH A O   
2171 O  O   . HOH E .   ? 0.4530 0.8308 0.1741 0.0545  -0.0480 0.0586  465 HOH A O   
2172 O  O   . HOH E .   ? 0.2565 0.3638 0.2583 0.0464  -0.0259 -0.0411 466 HOH A O   
2173 O  O   . HOH E .   ? 0.2570 0.2956 0.2017 0.0175  0.0046  0.1122  467 HOH A O   
2174 O  O   . HOH E .   ? 0.4014 0.4914 0.2787 -0.0710 0.1080  -0.1018 468 HOH A O   
2175 O  O   . HOH E .   ? 0.3814 0.2980 0.0908 -0.0435 -0.0478 -0.0282 469 HOH A O   
2176 O  O   . HOH E .   ? 0.4068 0.3571 0.2179 -0.0653 -0.1850 0.0295  470 HOH A O   
2177 O  O   . HOH E .   ? 0.3571 0.4863 0.2419 0.0214  -0.0401 -0.1526 471 HOH A O   
2178 O  O   . HOH E .   ? 0.2064 0.2863 0.0540 0.0173  -0.0444 0.0269  472 HOH A O   
2179 O  O   . HOH E .   ? 0.3410 0.2683 0.3310 -0.0993 0.0392  -0.0592 473 HOH A O   
2180 O  O   . HOH E .   ? 0.2408 0.3084 0.1163 -0.0002 -0.0061 0.0201  474 HOH A O   
2181 O  O   . HOH E .   ? 0.2190 0.2915 0.1544 0.0029  -0.0497 -0.0050 475 HOH A O   
2182 O  O   . HOH E .   ? 0.1831 0.2168 0.0933 0.0167  -0.0162 0.0122  476 HOH A O   
2183 O  O   . HOH E .   ? 0.3125 0.3400 0.2143 -0.0117 0.0315  -0.0595 477 HOH A O   
2184 O  O   . HOH E .   ? 0.3520 0.3783 0.3274 -0.0295 0.0128  -0.0922 478 HOH A O   
2185 O  O   . HOH E .   ? 0.2176 0.2764 0.1806 0.0075  -0.0960 0.0292  479 HOH A O   
2186 O  O   . HOH E .   ? 0.2416 0.6338 0.2138 -0.0546 0.0526  -0.0672 480 HOH A O   
2187 O  O   . HOH E .   ? 0.1978 0.3468 0.2491 0.0385  -0.0065 0.0340  481 HOH A O   
2188 O  O   . HOH E .   ? 0.4106 0.5704 0.1673 0.0714  0.0037  0.0611  482 HOH A O   
2189 O  O   . HOH E .   ? 0.1974 0.2716 0.0501 0.0330  -0.0129 -0.0070 483 HOH A O   
2190 O  O   . HOH E .   ? 0.1964 0.3280 0.0745 -0.0225 -0.0961 0.0488  484 HOH A O   
2191 O  O   . HOH E .   ? 0.1612 0.3550 0.1567 0.0189  -0.0633 -0.0188 485 HOH A O   
2192 O  O   . HOH E .   ? 0.6296 0.4349 0.7103 0.2354  0.0444  -0.0528 486 HOH A O   
2193 O  O   . HOH E .   ? 0.1941 0.5740 0.2160 -0.0214 -0.0179 0.0229  487 HOH A O   
2194 O  O   . HOH E .   ? 0.2842 0.4714 0.1106 -0.0266 -0.0741 -0.0622 488 HOH A O   
2195 O  O   . HOH E .   ? 0.2803 0.4073 0.1932 0.0111  -0.0117 -0.0185 489 HOH A O   
2196 O  O   . HOH E .   ? 0.3208 0.4252 0.2419 0.0018  0.0226  -0.0026 490 HOH A O   
2197 O  O   . HOH E .   ? 0.2169 0.2274 0.1084 -0.0226 -0.0369 0.0037  491 HOH A O   
2198 O  O   . HOH E .   ? 0.4171 0.3758 0.2720 0.0073  -0.0154 -0.0773 492 HOH A O   
2199 O  O   . HOH E .   ? 0.1937 0.2744 0.1395 -0.0148 -0.0270 -0.0142 493 HOH A O   
2200 O  O   . HOH E .   ? 0.2372 0.3264 0.1353 0.0467  0.0008  0.0262  494 HOH A O   
2201 O  O   . HOH E .   ? 0.2615 0.2879 0.1914 -0.0052 -0.0425 -0.0552 495 HOH A O   
2202 O  O   . HOH E .   ? 0.3051 0.4406 0.2398 -0.0174 -0.0775 0.0233  496 HOH A O   
2203 O  O   . HOH E .   ? 0.3592 0.3905 0.4160 0.0380  0.0787  0.0100  497 HOH A O   
2204 O  O   . HOH E .   ? 0.2712 0.3653 0.3194 -0.0305 0.0219  0.0010  498 HOH A O   
2205 O  O   . HOH E .   ? 0.5939 0.5711 0.1565 0.1793  -0.1273 -0.0388 499 HOH A O   
2206 O  O   . HOH E .   ? 0.4022 0.3545 0.2757 -0.0339 0.0440  -0.0031 500 HOH A O   
2207 O  O   . HOH E .   ? 0.3191 0.3401 0.7615 -0.0514 -0.0721 -0.0882 501 HOH A O   
2208 O  O   . HOH E .   ? 0.4096 0.3957 0.2527 0.0523  0.0690  -0.0484 502 HOH A O   
2209 O  O   . HOH E .   ? 0.2696 0.3779 0.4929 -0.0458 0.0867  -0.0215 503 HOH A O   
2210 O  O   . HOH E .   ? 0.3290 0.5941 0.1155 -0.0561 -0.0385 -0.0429 504 HOH A O   
2211 O  O   . HOH E .   ? 0.4284 0.3310 0.3961 0.0725  -0.1296 0.0139  505 HOH A O   
2212 O  O   . HOH E .   ? 0.5345 0.2877 0.2115 0.0299  -0.0861 -0.0961 506 HOH A O   
2213 O  O   . HOH E .   ? 0.3004 0.3798 0.1384 0.0314  -0.0161 0.0228  507 HOH A O   
2214 O  O   . HOH E .   ? 0.3430 0.5394 0.0955 0.0417  -0.0935 0.0658  508 HOH A O   
2215 O  O   . HOH E .   ? 0.5881 0.7560 0.2491 0.0207  -0.0483 0.1456  509 HOH A O   
2216 O  O   . HOH E .   ? 0.4923 0.3583 0.2427 0.0425  -0.0978 -0.0831 510 HOH A O   
2217 O  O   . HOH E .   ? 0.3813 0.4503 0.4742 -0.0047 0.0367  0.0216  511 HOH A O   
2218 O  O   . HOH E .   ? 0.3032 0.4452 0.2485 0.0146  -0.0352 0.0684  512 HOH A O   
2219 O  O   . HOH E .   ? 0.3511 0.5260 0.3414 -0.0688 0.0165  -0.0618 513 HOH A O   
2220 O  O   . HOH E .   ? 0.4954 0.3447 0.2432 0.1141  -0.0177 0.0567  514 HOH A O   
2221 O  O   . HOH E .   ? 0.1928 0.4021 0.3091 -0.0181 -0.0019 -0.0009 515 HOH A O   
2222 O  O   . HOH E .   ? 0.2711 0.4207 0.2168 0.0484  0.0505  0.0446  516 HOH A O   
2223 O  O   . HOH E .   ? 0.4290 0.3903 0.2637 -0.0337 -0.2262 0.0757  517 HOH A O   
2224 O  O   . HOH E .   ? 0.5008 0.4464 0.4658 -0.1627 0.1377  -0.1104 518 HOH A O   
2225 O  O   . HOH E .   ? 0.2522 0.3708 0.3541 -0.0397 0.0454  -0.0284 519 HOH A O   
2226 O  O   . HOH E .   ? 0.7720 0.5983 0.2125 -0.2160 -0.0122 -0.0488 520 HOH A O   
2227 O  O   . HOH E .   ? 0.3535 0.2274 0.1442 0.0430  0.0018  0.0166  521 HOH A O   
2228 O  O   . HOH E .   ? 0.3301 0.3101 0.5229 0.0068  0.0741  0.1850  522 HOH A O   
2229 O  O   . HOH E .   ? 0.4971 0.2957 0.1914 0.1246  -0.0368 -0.0373 523 HOH A O   
2230 O  O   . HOH E .   ? 0.2685 0.3179 0.1575 0.0117  0.0068  -0.0095 524 HOH A O   
2231 O  O   . HOH E .   ? 0.3230 0.6265 0.1719 0.1483  -0.1389 -0.1162 525 HOH A O   
2232 O  O   . HOH E .   ? 0.2745 0.3866 0.4408 -0.0826 -0.0058 -0.1870 526 HOH A O   
2233 O  O   . HOH E .   ? 0.2612 0.3750 0.6376 0.0104  -0.0665 0.0315  527 HOH A O   
2234 O  O   . HOH E .   ? 0.4511 0.5750 0.2278 -0.0840 -0.0801 -0.0606 528 HOH A O   
2235 O  O   . HOH E .   ? 0.6195 0.4085 0.6035 -0.1161 -0.3834 0.0770  529 HOH A O   
2236 O  O   . HOH E .   ? 0.4383 0.5140 0.1819 -0.2296 0.0114  -0.0091 530 HOH A O   
2237 O  O   . HOH E .   ? 0.3591 0.3655 0.2474 -0.0621 0.1054  -0.0261 531 HOH A O   
2238 O  O   . HOH E .   ? 0.5396 0.6868 0.2283 0.0431  0.0009  -0.0257 532 HOH A O   
2239 O  O   . HOH E .   ? 0.3047 0.3714 0.2530 0.0037  -0.0350 0.0001  533 HOH A O   
2240 O  O   . HOH E .   ? 0.2821 0.3496 0.3027 0.0289  -0.0991 -0.0911 534 HOH A O   
2241 O  O   . HOH E .   ? 0.4095 0.3992 0.1062 0.0025  -0.0575 0.0697  535 HOH A O   
2242 O  O   . HOH E .   ? 0.3733 0.3517 0.1783 -0.0504 -0.0529 -0.0535 536 HOH A O   
2243 O  O   . HOH E .   ? 0.3863 0.4216 0.4269 -0.0121 -0.0256 0.0242  537 HOH A O   
2244 O  O   . HOH E .   ? 0.4632 0.5403 0.5400 -0.1609 0.1047  0.1472  538 HOH A O   
2245 O  O   . HOH E .   ? 0.2528 0.3461 0.1016 -0.0306 -0.1114 0.0557  539 HOH A O   
2246 O  O   . HOH E .   ? 0.3093 0.3989 0.2251 -0.0119 0.0001  -0.0181 540 HOH A O   
2247 O  O   . HOH E .   ? 0.1953 0.4700 0.5138 -0.0274 -0.0272 -0.0157 541 HOH A O   
2248 O  O   . HOH E .   ? 0.3231 0.2938 0.1289 0.0666  -0.0347 -0.0141 542 HOH A O   
2249 O  O   . HOH E .   ? 0.3605 0.3747 0.8263 -0.1167 0.2247  -0.1262 543 HOH A O   
2250 O  O   . HOH E .   ? 0.3309 0.4879 0.2981 0.0779  -0.0943 0.0986  544 HOH A O   
2251 O  O   . HOH E .   ? 0.4140 0.4335 0.4382 0.0350  0.0343  -0.0079 545 HOH A O   
2252 O  O   . HOH E .   ? 0.5599 0.4497 0.1296 0.2225  -0.0712 0.0108  546 HOH A O   
2253 O  O   . HOH E .   ? 0.3308 0.4650 0.9365 -0.0334 0.2436  -0.1407 547 HOH A O   
2254 O  O   . HOH E .   ? 0.3190 0.5437 0.1716 -0.0787 -0.0853 -0.0791 548 HOH A O   
2255 O  O   . HOH E .   ? 0.4648 0.3850 0.4302 0.0000  0.2094  0.0110  549 HOH A O   
2256 O  O   . HOH E .   ? 0.2710 0.4524 0.1898 -0.0215 0.0480  -0.0741 550 HOH A O   
2257 O  O   . HOH E .   ? 0.2231 0.2269 0.1378 -0.0273 -0.0420 0.0216  551 HOH A O   
2258 O  O   . HOH E .   ? 0.4111 0.4150 0.4030 -0.0284 -0.0362 0.0145  552 HOH A O   
2259 O  O   . HOH E .   ? 0.2676 0.5305 0.6486 0.0372  -0.1012 0.0182  553 HOH A O   
2260 O  O   . HOH E .   ? 0.7537 0.3882 0.5473 -0.1395 0.2198  0.0601  554 HOH A O   
2261 O  O   . HOH E .   ? 0.1737 0.4166 0.2901 -0.0017 -0.0324 0.1029  555 HOH A O   
2262 O  O   . HOH E .   ? 0.4410 0.3371 0.2050 -0.0179 0.0680  -0.0919 556 HOH A O   
2263 O  O   . HOH E .   ? 0.7270 0.6202 0.2561 -0.0981 0.0489  -0.1114 557 HOH A O   
2264 O  O   . HOH E .   ? 0.2598 0.3708 0.1867 -0.0183 0.0223  0.0411  558 HOH A O   
2265 O  O   . HOH E .   ? 0.4986 0.3773 0.3825 0.0368  -0.0434 -0.0265 559 HOH A O   
2266 O  O   . HOH E .   ? 0.4024 0.3185 0.2328 0.0001  0.1143  -0.0168 560 HOH A O   
2267 O  O   . HOH E .   ? 0.3337 0.4059 0.2634 -0.0731 -0.0539 -0.0377 561 HOH A O   
2268 O  O   . HOH E .   ? 0.3131 0.3134 0.2161 -0.0522 0.0482  -0.0562 562 HOH A O   
2269 O  O   . HOH E .   ? 0.2577 0.3750 0.1702 -0.0303 -0.0324 -0.0242 563 HOH A O   
2270 O  O   . HOH E .   ? 0.2613 0.5334 0.2503 -0.0055 0.0012  0.0057  564 HOH A O   
2271 O  O   . HOH E .   ? 0.3049 0.3887 0.2054 -0.0640 0.0020  0.0136  565 HOH A O   
2272 O  O   . HOH E .   ? 0.1932 0.3908 0.5793 -0.0204 -0.0057 -0.0328 566 HOH A O   
2273 O  O   . HOH E .   ? 0.3159 0.4293 0.2915 -0.0491 0.0125  0.1025  567 HOH A O   
2274 O  O   . HOH E .   ? 0.2602 0.4785 0.1267 0.0912  0.0565  0.1008  568 HOH A O   
2275 O  O   . HOH E .   ? 0.3386 0.4526 0.4623 -0.0644 -0.0087 -0.1267 569 HOH A O   
2276 O  O   . HOH E .   ? 0.5626 0.5589 0.2174 -0.0272 0.0256  -0.0320 570 HOH A O   
2277 O  O   . HOH E .   ? 0.3852 0.5111 0.2078 -0.0326 -0.0456 -0.0113 571 HOH A O   
2278 O  O   . HOH E .   ? 0.8210 0.5148 0.5277 0.0824  -0.3823 -0.2024 572 HOH A O   
2279 O  O   . HOH E .   ? 0.3295 0.3208 0.1116 0.0096  -0.0055 -0.0027 573 HOH A O   
2280 O  O   . HOH E .   ? 0.4089 0.6477 0.3569 0.0945  -0.1658 -0.2613 574 HOH A O   
2281 O  O   . HOH E .   ? 0.3941 0.4058 0.2497 -0.0362 -0.1487 0.0552  575 HOH A O   
2282 O  O   . HOH E .   ? 0.3527 0.4044 0.7637 0.0508  0.0130  -0.0617 576 HOH A O   
2283 O  O   . HOH E .   ? 0.4610 0.3744 0.4350 0.0044  -0.0008 -0.0092 577 HOH A O   
2284 O  O   . HOH E .   ? 0.1891 0.2335 0.0969 -0.0212 -0.0297 -0.0126 578 HOH A O   
2285 O  O   . HOH E .   ? 0.4674 0.4951 0.4836 0.0800  -0.0281 -0.0798 579 HOH A O   
2286 O  O   . HOH E .   ? 0.3376 0.4169 0.3498 0.0089  -0.0249 0.0422  580 HOH A O   
2287 O  O   . HOH E .   ? 0.4965 0.5389 0.1619 -0.1597 -0.1179 -0.0121 581 HOH A O   
2288 O  O   . HOH E .   ? 0.3450 0.4250 0.7240 0.0292  0.0374  0.0717  582 HOH A O   
2289 O  O   . HOH E .   ? 0.2563 0.3547 0.9310 -0.0829 -0.2022 0.0628  583 HOH A O   
2290 O  O   . HOH E .   ? 0.3254 0.4669 0.6208 0.0171  0.1074  -0.0538 584 HOH A O   
2291 O  O   . HOH E .   ? 1.0624 0.4448 0.4077 0.0271  -0.1846 -0.2016 585 HOH A O   
2292 O  O   . HOH E .   ? 0.4200 0.4819 0.2674 0.0106  -0.0405 0.1013  586 HOH A O   
2293 O  O   . HOH E .   ? 0.3630 0.4171 0.2895 -0.0016 0.0074  -0.0418 587 HOH A O   
2294 O  O   . HOH E .   ? 0.6451 0.4445 0.4628 -0.0773 0.2174  -0.1139 588 HOH A O   
2295 O  O   . HOH E .   ? 0.4979 0.4306 0.5431 0.0549  0.0936  0.0294  589 HOH A O   
2296 O  O   . HOH E .   ? 0.2562 0.7239 0.5287 0.0512  -0.0854 0.1193  590 HOH A O   
2297 O  O   . HOH E .   ? 0.2594 0.7266 0.7691 0.0294  -0.1854 -0.1622 591 HOH A O   
2298 O  O   . HOH E .   ? 0.4071 0.3656 0.3865 -0.0044 0.0374  -0.0389 592 HOH A O   
2299 O  O   . HOH E .   ? 0.3941 0.5493 0.2355 0.1248  0.0971  0.0827  593 HOH A O   
2300 O  O   . HOH E .   ? 0.3987 0.6894 0.4670 0.1901  -0.0981 0.1040  594 HOH A O   
2301 O  O   . HOH E .   ? 0.2949 0.3409 0.3614 -0.0021 0.0218  0.0070  595 HOH A O   
2302 O  O   . HOH E .   ? 0.3576 0.5906 0.8272 0.1638  0.1693  -0.1543 596 HOH A O   
2303 O  O   . HOH E .   ? 0.2993 0.5233 0.5638 -0.1040 -0.0792 0.0727  597 HOH A O   
2304 O  O   . HOH E .   ? 0.4507 0.4953 0.2766 -0.0055 0.1055  0.0780  598 HOH A O   
2305 O  O   . HOH E .   ? 0.4110 0.3218 0.7032 -0.0179 -0.0147 0.1115  599 HOH A O   
2306 O  O   . HOH E .   ? 0.4194 0.3443 0.4301 0.0084  -0.0071 -0.0469 600 HOH A O   
2307 O  O   . HOH E .   ? 0.4166 0.3318 0.2400 0.0241  -0.1494 0.0264  601 HOH A O   
2308 O  O   . HOH E .   ? 0.5784 0.4164 0.2690 0.0807  -0.1412 -0.1046 602 HOH A O   
2309 O  O   . HOH E .   ? 0.3685 0.4215 0.2285 0.1098  0.0930  0.0082  603 HOH A O   
2310 O  O   . HOH E .   ? 0.3086 0.4857 0.1107 -0.1043 -0.0904 -0.0527 604 HOH A O   
2311 O  O   . HOH E .   ? 0.3246 0.5371 0.0856 -0.0253 -0.0798 0.0294  605 HOH A O   
2312 O  O   . HOH E .   ? 0.5053 0.4623 0.3339 -0.0910 0.1291  -0.2039 606 HOH A O   
2313 O  O   . HOH E .   ? 0.9150 0.6790 0.1751 -0.1591 -0.0111 0.0868  607 HOH A O   
# 
