data_6YH8
# 
_entry.id   6YH8 
# 
_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   6YH8         pdb_00006yh8 10.2210/pdb6yh8/pdb 
WWPDB D_1292106686 ?            ?                   
# 
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                        6YH8 
_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 BICINE                                                                             163.172   1   ?       ? ? ? 
5 non-polymer syn '2-[(1S)-1,2,3,4-Tetrahydronapthalen-1-ylamino)-3,5,6-trifluorobenzenesulfonamide' 354.347   1   ?       ? ? ? 
6 water       nat water                                                                              18.015    295 ?       ? ? ? 
# 
_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 BICINE                                                                             BCN 
5 '2-[(1S)-1,2,3,4-Tetrahydronapthalen-1-ylamino)-3,5,6-trifluorobenzenesulfonamide' OQT 
6 water                                                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  SER n 
1 66  PHE n 
1 67  LYS n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  THR n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 ALA n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 SER n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 ASN n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                            ? 'C3 H7 N O2' 89.093 
ARG 'L-peptide linking' y ARGININE                                                                           ? 'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                         ? 'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                    ? 'C4 H7 N O4' 
133.103 
BCN non-polymer         . BICINE                                                                             ? 'C6 H13 N O4' 
163.172 
CYS 'L-peptide linking' y CYSTEINE                                                                           ? 'C3 H7 N O2 S' 
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                               ? 'C2 H6 O S' 78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                          ? 'C5 H10 N2 O3' 
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                    ? 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                                            ? 'C2 H5 N O2' 75.067 
HIS 'L-peptide linking' y HISTIDINE                                                                          ? 'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                                              ? 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                         ? 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                            ? 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                                             ? 'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                                                                         ? 'C5 H11 N O2 S' 
149.211 
OQT non-polymer         . '2-[(1S)-1,2,3,4-Tetrahydronapthalen-1-ylamino)-3,5,6-trifluorobenzenesulfonamide' 
'2-[[(1~{S})-1,4-dihydronaphthalen-1-yl]amino]-3,5,6-tris(fluoranyl)benzenesulfonamide' 'C16 H13 F3 N2 O2 S' 354.347 
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 BCN 1   303 2   BCN BCN A . 
E 5 OQT 1   304 1   OQT V19 A . 
F 6 HOH 1   401 198 HOH HOH A . 
F 6 HOH 2   402 230 HOH HOH A . 
F 6 HOH 3   403 249 HOH HOH A . 
F 6 HOH 4   404 194 HOH HOH A . 
F 6 HOH 5   405 188 HOH HOH A . 
F 6 HOH 6   406 289 HOH HOH A . 
F 6 HOH 7   407 100 HOH HOH A . 
F 6 HOH 8   408 248 HOH HOH A . 
F 6 HOH 9   409 239 HOH HOH A . 
F 6 HOH 10  410 204 HOH HOH A . 
F 6 HOH 11  411 106 HOH HOH A . 
F 6 HOH 12  412 224 HOH HOH A . 
F 6 HOH 13  413 80  HOH HOH A . 
F 6 HOH 14  414 268 HOH HOH A . 
F 6 HOH 15  415 214 HOH HOH A . 
F 6 HOH 16  416 157 HOH HOH A . 
F 6 HOH 17  417 202 HOH HOH A . 
F 6 HOH 18  418 291 HOH HOH A . 
F 6 HOH 19  419 217 HOH HOH A . 
F 6 HOH 20  420 250 HOH HOH A . 
F 6 HOH 21  421 162 HOH HOH A . 
F 6 HOH 22  422 57  HOH HOH A . 
F 6 HOH 23  423 254 HOH HOH A . 
F 6 HOH 24  424 216 HOH HOH A . 
F 6 HOH 25  425 87  HOH HOH A . 
F 6 HOH 26  426 187 HOH HOH A . 
F 6 HOH 27  427 78  HOH HOH A . 
F 6 HOH 28  428 4   HOH HOH A . 
F 6 HOH 29  429 62  HOH HOH A . 
F 6 HOH 30  430 242 HOH HOH A . 
F 6 HOH 31  431 140 HOH HOH A . 
F 6 HOH 32  432 97  HOH HOH A . 
F 6 HOH 33  433 275 HOH HOH A . 
F 6 HOH 34  434 247 HOH HOH A . 
F 6 HOH 35  435 184 HOH HOH A . 
F 6 HOH 36  436 290 HOH HOH A . 
F 6 HOH 37  437 10  HOH HOH A . 
F 6 HOH 38  438 137 HOH HOH A . 
F 6 HOH 39  439 104 HOH HOH A . 
F 6 HOH 40  440 146 HOH HOH A . 
F 6 HOH 41  441 24  HOH HOH A . 
F 6 HOH 42  442 156 HOH HOH A . 
F 6 HOH 43  443 103 HOH HOH A . 
F 6 HOH 44  444 265 HOH HOH A . 
F 6 HOH 45  445 26  HOH HOH A . 
F 6 HOH 46  446 151 HOH HOH A . 
F 6 HOH 47  447 251 HOH HOH A . 
F 6 HOH 48  448 8   HOH HOH A . 
F 6 HOH 49  449 130 HOH HOH A . 
F 6 HOH 50  450 30  HOH HOH A . 
F 6 HOH 51  451 84  HOH HOH A . 
F 6 HOH 52  452 260 HOH HOH A . 
F 6 HOH 53  453 132 HOH HOH A . 
F 6 HOH 54  454 210 HOH HOH A . 
F 6 HOH 55  455 208 HOH HOH A . 
F 6 HOH 56  456 172 HOH HOH A . 
F 6 HOH 57  457 161 HOH HOH A . 
F 6 HOH 58  458 282 HOH HOH A . 
F 6 HOH 59  459 107 HOH HOH A . 
F 6 HOH 60  460 241 HOH HOH A . 
F 6 HOH 61  461 199 HOH HOH A . 
F 6 HOH 62  462 17  HOH HOH A . 
F 6 HOH 63  463 69  HOH HOH A . 
F 6 HOH 64  464 22  HOH HOH A . 
F 6 HOH 65  465 111 HOH HOH A . 
F 6 HOH 66  466 60  HOH HOH A . 
F 6 HOH 67  467 23  HOH HOH A . 
F 6 HOH 68  468 29  HOH HOH A . 
F 6 HOH 69  469 105 HOH HOH A . 
F 6 HOH 70  470 125 HOH HOH A . 
F 6 HOH 71  471 7   HOH HOH A . 
F 6 HOH 72  472 135 HOH HOH A . 
F 6 HOH 73  473 237 HOH HOH A . 
F 6 HOH 74  474 261 HOH HOH A . 
F 6 HOH 75  475 31  HOH HOH A . 
F 6 HOH 76  476 32  HOH HOH A . 
F 6 HOH 77  477 155 HOH HOH A . 
F 6 HOH 78  478 170 HOH HOH A . 
F 6 HOH 79  479 192 HOH HOH A . 
F 6 HOH 80  480 258 HOH HOH A . 
F 6 HOH 81  481 65  HOH HOH A . 
F 6 HOH 82  482 34  HOH HOH A . 
F 6 HOH 83  483 109 HOH HOH A . 
F 6 HOH 84  484 133 HOH HOH A . 
F 6 HOH 85  485 74  HOH HOH A . 
F 6 HOH 86  486 138 HOH HOH A . 
F 6 HOH 87  487 264 HOH HOH A . 
F 6 HOH 88  488 16  HOH HOH A . 
F 6 HOH 89  489 115 HOH HOH A . 
F 6 HOH 90  490 134 HOH HOH A . 
F 6 HOH 91  491 72  HOH HOH A . 
F 6 HOH 92  492 286 HOH HOH A . 
F 6 HOH 93  493 41  HOH HOH A . 
F 6 HOH 94  494 158 HOH HOH A . 
F 6 HOH 95  495 85  HOH HOH A . 
F 6 HOH 96  496 43  HOH HOH A . 
F 6 HOH 97  497 101 HOH HOH A . 
F 6 HOH 98  498 128 HOH HOH A . 
F 6 HOH 99  499 39  HOH HOH A . 
F 6 HOH 100 500 36  HOH HOH A . 
F 6 HOH 101 501 58  HOH HOH A . 
F 6 HOH 102 502 3   HOH HOH A . 
F 6 HOH 103 503 110 HOH HOH A . 
F 6 HOH 104 504 148 HOH HOH A . 
F 6 HOH 105 505 113 HOH HOH A . 
F 6 HOH 106 506 48  HOH HOH A . 
F 6 HOH 107 507 1   HOH HOH A . 
F 6 HOH 108 508 28  HOH HOH A . 
F 6 HOH 109 509 121 HOH HOH A . 
F 6 HOH 110 510 19  HOH HOH A . 
F 6 HOH 111 511 150 HOH HOH A . 
F 6 HOH 112 512 38  HOH HOH A . 
F 6 HOH 113 513 75  HOH HOH A . 
F 6 HOH 114 514 51  HOH HOH A . 
F 6 HOH 115 515 2   HOH HOH A . 
F 6 HOH 116 516 64  HOH HOH A . 
F 6 HOH 117 517 42  HOH HOH A . 
F 6 HOH 118 518 47  HOH HOH A . 
F 6 HOH 119 519 229 HOH HOH A . 
F 6 HOH 120 520 77  HOH HOH A . 
F 6 HOH 121 521 20  HOH HOH A . 
F 6 HOH 122 522 269 HOH HOH A . 
F 6 HOH 123 523 70  HOH HOH A . 
F 6 HOH 124 524 54  HOH HOH A . 
F 6 HOH 125 525 15  HOH HOH A . 
F 6 HOH 126 526 21  HOH HOH A . 
F 6 HOH 127 527 98  HOH HOH A . 
F 6 HOH 128 528 287 HOH HOH A . 
F 6 HOH 129 529 27  HOH HOH A . 
F 6 HOH 130 530 73  HOH HOH A . 
F 6 HOH 131 531 5   HOH HOH A . 
F 6 HOH 132 532 12  HOH HOH A . 
F 6 HOH 133 533 218 HOH HOH A . 
F 6 HOH 134 534 296 HOH HOH A . 
F 6 HOH 135 535 71  HOH HOH A . 
F 6 HOH 136 536 88  HOH HOH A . 
F 6 HOH 137 537 169 HOH HOH A . 
F 6 HOH 138 538 163 HOH HOH A . 
F 6 HOH 139 539 82  HOH HOH A . 
F 6 HOH 140 540 122 HOH HOH A . 
F 6 HOH 141 541 102 HOH HOH A . 
F 6 HOH 142 542 53  HOH HOH A . 
F 6 HOH 143 543 142 HOH HOH A . 
F 6 HOH 144 544 212 HOH HOH A . 
F 6 HOH 145 545 191 HOH HOH A . 
F 6 HOH 146 546 124 HOH HOH A . 
F 6 HOH 147 547 123 HOH HOH A . 
F 6 HOH 148 548 9   HOH HOH A . 
F 6 HOH 149 549 50  HOH HOH A . 
F 6 HOH 150 550 89  HOH HOH A . 
F 6 HOH 151 551 46  HOH HOH A . 
F 6 HOH 152 552 219 HOH HOH A . 
F 6 HOH 153 553 112 HOH HOH A . 
F 6 HOH 154 554 18  HOH HOH A . 
F 6 HOH 155 555 55  HOH HOH A . 
F 6 HOH 156 556 25  HOH HOH A . 
F 6 HOH 157 557 14  HOH HOH A . 
F 6 HOH 158 558 232 HOH HOH A . 
F 6 HOH 159 559 273 HOH HOH A . 
F 6 HOH 160 560 231 HOH HOH A . 
F 6 HOH 161 561 182 HOH HOH A . 
F 6 HOH 162 562 118 HOH HOH A . 
F 6 HOH 163 563 141 HOH HOH A . 
F 6 HOH 164 564 143 HOH HOH A . 
F 6 HOH 165 565 90  HOH HOH A . 
F 6 HOH 166 566 222 HOH HOH A . 
F 6 HOH 167 567 56  HOH HOH A . 
F 6 HOH 168 568 67  HOH HOH A . 
F 6 HOH 169 569 63  HOH HOH A . 
F 6 HOH 170 570 95  HOH HOH A . 
F 6 HOH 171 571 114 HOH HOH A . 
F 6 HOH 172 572 159 HOH HOH A . 
F 6 HOH 173 573 96  HOH HOH A . 
F 6 HOH 174 574 37  HOH HOH A . 
F 6 HOH 175 575 59  HOH HOH A . 
F 6 HOH 176 576 33  HOH HOH A . 
F 6 HOH 177 577 13  HOH HOH A . 
F 6 HOH 178 578 285 HOH HOH A . 
F 6 HOH 179 579 92  HOH HOH A . 
F 6 HOH 180 580 281 HOH HOH A . 
F 6 HOH 181 581 147 HOH HOH A . 
F 6 HOH 182 582 259 HOH HOH A . 
F 6 HOH 183 583 139 HOH HOH A . 
F 6 HOH 184 584 186 HOH HOH A . 
F 6 HOH 185 585 129 HOH HOH A . 
F 6 HOH 186 586 83  HOH HOH A . 
F 6 HOH 187 587 6   HOH HOH A . 
F 6 HOH 188 588 35  HOH HOH A . 
F 6 HOH 189 589 44  HOH HOH A . 
F 6 HOH 190 590 197 HOH HOH A . 
F 6 HOH 191 591 295 HOH HOH A . 
F 6 HOH 192 592 45  HOH HOH A . 
F 6 HOH 193 593 168 HOH HOH A . 
F 6 HOH 194 594 173 HOH HOH A . 
F 6 HOH 195 595 144 HOH HOH A . 
F 6 HOH 196 596 66  HOH HOH A . 
F 6 HOH 197 597 152 HOH HOH A . 
F 6 HOH 198 598 227 HOH HOH A . 
F 6 HOH 199 599 127 HOH HOH A . 
F 6 HOH 200 600 245 HOH HOH A . 
F 6 HOH 201 601 68  HOH HOH A . 
F 6 HOH 202 602 244 HOH HOH A . 
F 6 HOH 203 603 183 HOH HOH A . 
F 6 HOH 204 604 119 HOH HOH A . 
F 6 HOH 205 605 108 HOH HOH A . 
F 6 HOH 206 606 160 HOH HOH A . 
F 6 HOH 207 607 153 HOH HOH A . 
F 6 HOH 208 608 284 HOH HOH A . 
F 6 HOH 209 609 49  HOH HOH A . 
F 6 HOH 210 610 11  HOH HOH A . 
F 6 HOH 211 611 120 HOH HOH A . 
F 6 HOH 212 612 149 HOH HOH A . 
F 6 HOH 213 613 165 HOH HOH A . 
F 6 HOH 214 614 79  HOH HOH A . 
F 6 HOH 215 615 228 HOH HOH A . 
F 6 HOH 216 616 76  HOH HOH A . 
F 6 HOH 217 617 270 HOH HOH A . 
F 6 HOH 218 618 283 HOH HOH A . 
F 6 HOH 219 619 195 HOH HOH A . 
F 6 HOH 220 620 272 HOH HOH A . 
F 6 HOH 221 621 166 HOH HOH A . 
F 6 HOH 222 622 233 HOH HOH A . 
F 6 HOH 223 623 206 HOH HOH A . 
F 6 HOH 224 624 40  HOH HOH A . 
F 6 HOH 225 625 99  HOH HOH A . 
F 6 HOH 226 626 257 HOH HOH A . 
F 6 HOH 227 627 293 HOH HOH A . 
F 6 HOH 228 628 136 HOH HOH A . 
F 6 HOH 229 629 200 HOH HOH A . 
F 6 HOH 230 630 190 HOH HOH A . 
F 6 HOH 231 631 255 HOH HOH A . 
F 6 HOH 232 632 93  HOH HOH A . 
F 6 HOH 233 633 236 HOH HOH A . 
F 6 HOH 234 634 221 HOH HOH A . 
F 6 HOH 235 635 164 HOH HOH A . 
F 6 HOH 236 636 203 HOH HOH A . 
F 6 HOH 237 637 211 HOH HOH A . 
F 6 HOH 238 638 274 HOH HOH A . 
F 6 HOH 239 639 193 HOH HOH A . 
F 6 HOH 240 640 81  HOH HOH A . 
F 6 HOH 241 641 294 HOH HOH A . 
F 6 HOH 242 642 253 HOH HOH A . 
F 6 HOH 243 643 252 HOH HOH A . 
F 6 HOH 244 644 145 HOH HOH A . 
F 6 HOH 245 645 262 HOH HOH A . 
F 6 HOH 246 646 267 HOH HOH A . 
F 6 HOH 247 647 209 HOH HOH A . 
F 6 HOH 248 648 126 HOH HOH A . 
F 6 HOH 249 649 263 HOH HOH A . 
F 6 HOH 250 650 215 HOH HOH A . 
F 6 HOH 251 651 91  HOH HOH A . 
F 6 HOH 252 652 226 HOH HOH A . 
F 6 HOH 253 653 171 HOH HOH A . 
F 6 HOH 254 654 246 HOH HOH A . 
F 6 HOH 255 655 225 HOH HOH A . 
F 6 HOH 256 656 131 HOH HOH A . 
F 6 HOH 257 657 116 HOH HOH A . 
F 6 HOH 258 658 280 HOH HOH A . 
F 6 HOH 259 659 201 HOH HOH A . 
F 6 HOH 260 660 185 HOH HOH A . 
F 6 HOH 261 661 94  HOH HOH A . 
F 6 HOH 262 662 213 HOH HOH A . 
F 6 HOH 263 663 266 HOH HOH A . 
F 6 HOH 264 664 277 HOH HOH A . 
F 6 HOH 265 665 220 HOH HOH A . 
F 6 HOH 266 666 180 HOH HOH A . 
F 6 HOH 267 667 240 HOH HOH A . 
F 6 HOH 268 668 205 HOH HOH A . 
F 6 HOH 269 669 117 HOH HOH A . 
F 6 HOH 270 670 189 HOH HOH A . 
F 6 HOH 271 671 279 HOH HOH A . 
F 6 HOH 272 672 243 HOH HOH A . 
F 6 HOH 273 673 276 HOH HOH A . 
F 6 HOH 274 674 238 HOH HOH A . 
F 6 HOH 275 675 179 HOH HOH A . 
F 6 HOH 276 676 297 HOH HOH A . 
F 6 HOH 277 677 176 HOH HOH A . 
F 6 HOH 278 678 278 HOH HOH A . 
F 6 HOH 279 679 175 HOH HOH A . 
F 6 HOH 280 680 167 HOH HOH A . 
F 6 HOH 281 681 181 HOH HOH A . 
F 6 HOH 282 682 207 HOH HOH A . 
F 6 HOH 283 683 196 HOH HOH A . 
F 6 HOH 284 684 52  HOH HOH A . 
F 6 HOH 285 685 154 HOH HOH A . 
F 6 HOH 286 686 86  HOH HOH A . 
F 6 HOH 287 687 223 HOH HOH A . 
F 6 HOH 288 688 271 HOH HOH A . 
F 6 HOH 289 689 177 HOH HOH A . 
F 6 HOH 290 690 61  HOH HOH A . 
F 6 HOH 291 691 178 HOH HOH A . 
F 6 HOH 292 692 288 HOH HOH A . 
F 6 HOH 293 693 256 HOH HOH A . 
F 6 HOH 294 694 174 HOH HOH A . 
F 6 HOH 295 697 292 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   ? CE  ? A LYS 9   CE  
2  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
3  1 Y 1 A LYS 45  ? CD  ? A LYS 45  CD  
4  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
5  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
6  1 Y 1 A LYS 159 ? CD  ? A LYS 158 CD  
7  1 Y 1 A LYS 159 ? CE  ? A LYS 158 CE  
8  1 Y 1 A LYS 159 ? NZ  ? A LYS 158 NZ  
9  1 Y 1 A LYS 168 ? NZ  ? A LYS 167 NZ  
10 1 Y 1 A LEU 224 ? CD1 ? A LEU 223 CD1 
11 1 Y 1 A LYS 225 ? CE  ? A LYS 224 CE  
12 1 Y 1 A LYS 225 ? NZ  ? A LYS 224 NZ  
13 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
14 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
15 1 Y 1 A LYS 261 ? CG  ? A LYS 260 CG  
16 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
17 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
18 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.930 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YH8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.035 
_cell.length_a_esd                 ? 
_cell.length_b                     41.044 
_cell.length_b_esd                 ? 
_cell.length_c                     71.429 
_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                         6YH8 
_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                   6YH8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.05 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.90 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-21 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97630 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97630 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6YH8 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.200 
_reflns.d_resolution_low                 40.798 
_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                       71228 
_reflns.number_obs                       71228 
_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             96.500 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  5.100 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.038 
_reflns.pdbx_netI_over_av_sigmaI         5.700 
_reflns.pdbx_netI_over_sigmaI            19.900 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.049 
_reflns.pdbx_Rpim_I_all                  0.021 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         364422 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
1.200 1.260  ? 4.800  49610 ? ? ? 9967 93.100 ? ? ? ? 0.156 ? ? ? ? ? ? ? ? 5.000 0.156 ? ? 7.700  0.195 0.086 ? 1  1 ? ? ? 
1.260 1.340  ? 6.200  49536 ? ? ? 9618 94.800 ? ? ? ? 0.121 ? ? ? ? ? ? ? ? 5.200 0.121 ? ? 9.600  0.154 0.067 ? 2  1 ? ? ? 
1.340 1.430  ? 8.300  46711 ? ? ? 9137 95.700 ? ? ? ? 0.090 ? ? ? ? ? ? ? ? 5.100 0.090 ? ? 11.700 0.118 0.052 ? 3  1 ? ? ? 
1.430 1.550  ? 11.400 42938 ? ? ? 8579 96.700 ? ? ? ? 0.065 ? ? ? ? ? ? ? ? 5.000 0.065 ? ? 14.900 0.088 0.039 ? 4  1 ? ? ? 
1.550 1.700  ? 14.100 41457 ? ? ? 7940 96.800 ? ? ? ? 0.051 ? ? ? ? ? ? ? ? 5.200 0.051 ? ? 19.300 0.070 0.030 ? 5  1 ? ? ? 
1.700 1.900  ? 17.400 38265 ? ? ? 7281 98.100 ? ? ? ? 0.039 ? ? ? ? ? ? ? ? 5.300 0.039 ? ? 24.900 0.055 0.024 ? 6  1 ? ? ? 
1.900 2.190  ? 20.300 33475 ? ? ? 6450 98.400 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 5.200 0.033 ? ? 31.600 0.045 0.019 ? 7  1 ? ? ? 
2.190 2.680  ? 21.700 28724 ? ? ? 5512 98.800 ? ? ? ? 0.030 ? ? ? ? ? ? ? ? 5.200 0.030 ? ? 35.900 0.040 0.017 ? 8  1 ? ? ? 
2.680 3.790  ? 16.500 21425 ? ? ? 4309 99.500 ? ? ? ? 0.028 ? ? ? ? ? ? ? ? 5.000 0.028 ? ? 40.200 0.036 0.016 ? 9  1 ? ? ? 
3.790 40.798 ? 10.300 12281 ? ? ? 2435 99.400 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 5.000 0.038 ? ? 43.000 0.047 0.020 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.4000 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.1200 
_refine.aniso_B[2][2]                            -0.5900 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            0.2200 
_refine.B_iso_max                                86.570 
_refine.B_iso_mean                               17.2560 
_refine.B_iso_min                                5.240 
_refine.correlation_coeff_Fo_to_Fc               0.9760 
_refine.correlation_coeff_Fo_to_Fc_free          0.9650 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 6YH8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.2000 
_refine.ls_d_res_low                             39.5700 
_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                     63953 
_refine.ls_number_reflns_R_free                  7257 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.1400 
_refine.ls_percent_reflns_R_free                 10.2000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1393 
_refine.ls_R_factor_R_free                       0.1721 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1356 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4Q09 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0440 
_refine.pdbx_overall_ESU_R_Free                  0.0440 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0443 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.2000 
_refine_hist.d_res_low                        39.5700 
_refine_hist.number_atoms_solvent             297 
_refine_hist.number_atoms_total               2362 
_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           23.47 
_refine_hist.pdbx_B_iso_mean_solvent          29.99 
_refine_hist.pdbx_number_atoms_protein        2025 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_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' ? 0.015  0.012  2459 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.283  1.655  3369 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.308  5.000  316  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.858 23.934 122  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.602 15.000 400  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 17.410 15.000 9    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.154  0.200  300  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.016  0.020  1976 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 7.018  3.000  2459 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 25.588 5.000  157  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 16.291 5.000  2517 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2000 
_refine_ls_shell.d_res_low                        1.2310 
_refine_ls_shell.number_reflns_all                4984 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             500 
_refine_ls_shell.number_reflns_R_work             4484 
_refine_ls_shell.percent_reflns_obs               91.4200 
_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                  0.2090 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1640 
_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                     6YH8 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase XII with 2-[(1S)-1,2,3,4-Tetrahydronapthalen-1-ylamino)-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        6YH8 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6YH8 
_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 6YH8 SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YH8 LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YH8 THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YH8 ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YH8 SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YH8 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)' 510   ? 
1 MORE         3     ? 
1 'SSA (A^2)'  11330 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? SER A 134 ? ASP A 130 SER A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E OQT . N3 ? ? A ZN  301 A OQT 304 1_555 ? ? ? ? ? ? ? 1.898 ? ? 
# 
_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_555 105.6 ? 
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_555 111.1 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.6  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N3  ? E OQT .   ? A OQT 304 ? 1_555 110.7 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N3  ? E OQT .   ? A OQT 304 ? 1_555 116.3 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N3  ? E OQT .   ? A OQT 304 ? 1_555 112.8 ? 
# 
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 -3.57 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 14.30 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O THR A 91  ? O THR A 91  N PHE A 70  ? N PHE A 70  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 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 HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 4  'binding site for residue DMS A 302' 
AC3 Software A BCN 303 ? 8  'binding site for residue BCN A 303' 
AC4 Software A OQT 304 ? 15 'binding site for residue OQT A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  OQT E .   ? OQT A 304 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  PRO A 246 ? PRO A 247 . ? 1_555 ? 
9  AC3 8  LYS A 148 ? LYS A 149 . ? 1_555 ? 
10 AC3 8  LYS A 212 ? LYS A 213 . ? 1_555 ? 
11 AC3 8  GLU A 213 ? GLU A 214 . ? 1_555 ? 
12 AC3 8  PRO A 214 ? PRO A 215 . ? 1_555 ? 
13 AC3 8  HOH F .   ? HOH A 413 . ? 1_555 ? 
14 AC3 8  HOH F .   ? HOH A 475 . ? 1_555 ? 
15 AC3 8  HOH F .   ? HOH A 494 . ? 1_555 ? 
16 AC3 8  HOH F .   ? HOH A 537 . ? 1_555 ? 
17 AC4 15 ASN A 62  ? ASN A 62  . ? 1_555 ? 
18 AC4 15 LYS A 67  ? LYS A 67  . ? 1_555 ? 
19 AC4 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
20 AC4 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
21 AC4 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
22 AC4 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
23 AC4 15 VAL A 121 ? VAL A 121 . ? 1_555 ? 
24 AC4 15 LEU A 140 ? LEU A 141 . ? 1_555 ? 
25 AC4 15 VAL A 142 ? VAL A 143 . ? 1_555 ? 
26 AC4 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
27 AC4 15 THR A 198 ? THR A 199 . ? 1_555 ? 
28 AC4 15 THR A 199 ? THR A 200 . ? 1_555 ? 
29 AC4 15 VAL A 206 ? VAL A 207 . ? 1_555 ? 
30 AC4 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
31 AC4 15 HOH F .   ? HOH A 564 . ? 1_555 ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    34 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.80 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     403 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     441 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_565 
_pdbx_validate_symm_contact.dist              2.03 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 58  ? B CZ A ARG 58  ? B NH1 A ARG 58  ? B 123.64 120.30 3.34  0.50 N 
2 1 CB A ASN 253 ? B CA A ASN 253 ? B C   A ASN 253 ? B 130.57 110.40 20.17 2.00 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -143.12 56.39   
2 1 LEU A 57  ? ? -121.19 -61.28  
3 1 LYS A 76  ? ? -115.21 -104.53 
4 1 LYS A 111 ? ? 78.22   -3.68   
5 1 ASP A 175 ? A -55.85  109.53  
6 1 PHE A 176 ? ? -158.85 76.79   
7 1 ASN A 244 ? ? -93.81  48.40   
8 1 LYS A 252 ? ? 59.81   -129.31 
9 1 LYS A 252 ? ? 59.81   -142.62 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    HIS 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     4 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    A 
_pdbx_validate_planes.rmsd            0.073 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ASP 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              175 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             A 
_pdbx_validate_main_chain_plane.improper_torsion_angle   12.96 
# 
_pdbx_entry_details.entry_id                 6YH8 
_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         ? 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       697 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.68 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MET N    N  N N 264 
MET CA   C  N S 265 
MET C    C  N N 266 
MET O    O  N N 267 
MET CB   C  N N 268 
MET CG   C  N N 269 
MET SD   S  N N 270 
MET CE   C  N N 271 
MET OXT  O  N N 272 
MET H    H  N N 273 
MET H2   H  N N 274 
MET HA   H  N N 275 
MET HB2  H  N N 276 
MET HB3  H  N N 277 
MET HG2  H  N N 278 
MET HG3  H  N N 279 
MET HE1  H  N N 280 
MET HE2  H  N N 281 
MET HE3  H  N N 282 
MET HXT  H  N N 283 
OQT O24  O  N N 284 
OQT S2   S  N N 285 
OQT O1   O  N N 286 
OQT N3   N  N N 287 
OQT C4   C  Y N 288 
OQT C12  C  Y N 289 
OQT C10  C  Y N 290 
OQT F11  F  N N 291 
OQT C9   C  Y N 292 
OQT C7   C  Y N 293 
OQT F8   F  N N 294 
OQT C5   C  Y N 295 
OQT F6   F  N N 296 
OQT N13  N  N N 297 
OQT C14  C  N S 298 
OQT C23  C  N N 299 
OQT C22  C  N N 300 
OQT C21  C  N N 301 
OQT C20  C  Y N 302 
OQT C15  C  Y N 303 
OQT C19  C  Y N 304 
OQT C18  C  Y N 305 
OQT C17  C  Y N 306 
OQT C16  C  Y N 307 
OQT H1   H  N N 308 
OQT H2   H  N N 309 
OQT H3   H  N N 310 
OQT H4   H  N N 311 
OQT H5   H  N N 312 
OQT H6   H  N N 313 
OQT H7   H  N N 314 
OQT H8   H  N N 315 
OQT H9   H  N N 316 
OQT H10  H  N N 317 
OQT H11  H  N N 318 
OQT H12  H  N N 319 
OQT H13  H  N N 320 
PHE N    N  N N 321 
PHE CA   C  N S 322 
PHE C    C  N N 323 
PHE O    O  N N 324 
PHE CB   C  N N 325 
PHE CG   C  Y N 326 
PHE CD1  C  Y N 327 
PHE CD2  C  Y N 328 
PHE CE1  C  Y N 329 
PHE CE2  C  Y N 330 
PHE CZ   C  Y N 331 
PHE OXT  O  N N 332 
PHE H    H  N N 333 
PHE H2   H  N N 334 
PHE HA   H  N N 335 
PHE HB2  H  N N 336 
PHE HB3  H  N N 337 
PHE HD1  H  N N 338 
PHE HD2  H  N N 339 
PHE HE1  H  N N 340 
PHE HE2  H  N N 341 
PHE HZ   H  N N 342 
PHE HXT  H  N N 343 
PRO N    N  N N 344 
PRO CA   C  N S 345 
PRO C    C  N N 346 
PRO O    O  N N 347 
PRO CB   C  N N 348 
PRO CG   C  N N 349 
PRO CD   C  N N 350 
PRO OXT  O  N N 351 
PRO H    H  N N 352 
PRO HA   H  N N 353 
PRO HB2  H  N N 354 
PRO HB3  H  N N 355 
PRO HG2  H  N N 356 
PRO HG3  H  N N 357 
PRO HD2  H  N N 358 
PRO HD3  H  N N 359 
PRO HXT  H  N N 360 
SER N    N  N N 361 
SER CA   C  N S 362 
SER C    C  N N 363 
SER O    O  N N 364 
SER CB   C  N N 365 
SER OG   O  N N 366 
SER OXT  O  N N 367 
SER H    H  N N 368 
SER H2   H  N N 369 
SER HA   H  N N 370 
SER HB2  H  N N 371 
SER HB3  H  N N 372 
SER HG   H  N N 373 
SER HXT  H  N N 374 
THR N    N  N N 375 
THR CA   C  N S 376 
THR C    C  N N 377 
THR O    O  N N 378 
THR CB   C  N R 379 
THR OG1  O  N N 380 
THR CG2  C  N N 381 
THR OXT  O  N N 382 
THR H    H  N N 383 
THR H2   H  N N 384 
THR HA   H  N N 385 
THR HB   H  N N 386 
THR HG1  H  N N 387 
THR HG21 H  N N 388 
THR HG22 H  N N 389 
THR HG23 H  N N 390 
THR HXT  H  N N 391 
TRP N    N  N N 392 
TRP CA   C  N S 393 
TRP C    C  N N 394 
TRP O    O  N N 395 
TRP CB   C  N N 396 
TRP CG   C  Y N 397 
TRP CD1  C  Y N 398 
TRP CD2  C  Y N 399 
TRP NE1  N  Y N 400 
TRP CE2  C  Y N 401 
TRP CE3  C  Y N 402 
TRP CZ2  C  Y N 403 
TRP CZ3  C  Y N 404 
TRP CH2  C  Y N 405 
TRP OXT  O  N N 406 
TRP H    H  N N 407 
TRP H2   H  N N 408 
TRP HA   H  N N 409 
TRP HB2  H  N N 410 
TRP HB3  H  N N 411 
TRP HD1  H  N N 412 
TRP HE1  H  N N 413 
TRP HE3  H  N N 414 
TRP HZ2  H  N N 415 
TRP HZ3  H  N N 416 
TRP HH2  H  N N 417 
TRP HXT  H  N N 418 
TYR N    N  N N 419 
TYR CA   C  N S 420 
TYR C    C  N N 421 
TYR O    O  N N 422 
TYR CB   C  N N 423 
TYR CG   C  Y N 424 
TYR CD1  C  Y N 425 
TYR CD2  C  Y N 426 
TYR CE1  C  Y N 427 
TYR CE2  C  Y N 428 
TYR CZ   C  Y N 429 
TYR OH   O  N N 430 
TYR OXT  O  N N 431 
TYR H    H  N N 432 
TYR H2   H  N N 433 
TYR HA   H  N N 434 
TYR HB2  H  N N 435 
TYR HB3  H  N N 436 
TYR HD1  H  N N 437 
TYR HD2  H  N N 438 
TYR HE1  H  N N 439 
TYR HE2  H  N N 440 
TYR HH   H  N N 441 
TYR HXT  H  N N 442 
VAL N    N  N N 443 
VAL CA   C  N S 444 
VAL C    C  N N 445 
VAL O    O  N N 446 
VAL CB   C  N N 447 
VAL CG1  C  N N 448 
VAL CG2  C  N N 449 
VAL OXT  O  N N 450 
VAL H    H  N N 451 
VAL H2   H  N N 452 
VAL HA   H  N N 453 
VAL HB   H  N N 454 
VAL HG11 H  N N 455 
VAL HG12 H  N N 456 
VAL HG13 H  N N 457 
VAL HG21 H  N N 458 
VAL HG22 H  N N 459 
VAL HG23 H  N N 460 
VAL HXT  H  N N 461 
ZN  ZN   ZN N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MET N   CA   sing N N 250 
MET N   H    sing N N 251 
MET N   H2   sing N N 252 
MET CA  C    sing N N 253 
MET CA  CB   sing N N 254 
MET CA  HA   sing N N 255 
MET C   O    doub N N 256 
MET C   OXT  sing N N 257 
MET CB  CG   sing N N 258 
MET CB  HB2  sing N N 259 
MET CB  HB3  sing N N 260 
MET CG  SD   sing N N 261 
MET CG  HG2  sing N N 262 
MET CG  HG3  sing N N 263 
MET SD  CE   sing N N 264 
MET CE  HE1  sing N N 265 
MET CE  HE2  sing N N 266 
MET CE  HE3  sing N N 267 
MET OXT HXT  sing N N 268 
OQT C18 C19  doub Y N 269 
OQT C18 C17  sing Y N 270 
OQT C19 C20  sing Y N 271 
OQT C17 C16  doub Y N 272 
OQT C20 C21  sing N N 273 
OQT C20 C15  doub Y N 274 
OQT C21 C22  sing N N 275 
OQT C16 C15  sing Y N 276 
OQT C15 C14  sing N N 277 
OQT C22 C23  doub N N 278 
OQT C14 C23  sing N N 279 
OQT C14 N13  sing N N 280 
OQT N13 C12  sing N N 281 
OQT F11 C10  sing N N 282 
OQT O24 S2   doub N N 283 
OQT C12 C10  doub Y N 284 
OQT C12 C4   sing Y N 285 
OQT C10 C9   sing Y N 286 
OQT S2  C4   sing N N 287 
OQT S2  N3   sing N N 288 
OQT S2  O1   doub N N 289 
OQT C4  C5   doub Y N 290 
OQT C9  C7   doub Y N 291 
OQT C5  C7   sing Y N 292 
OQT C5  F6   sing N N 293 
OQT C7  F8   sing N N 294 
OQT N3  H1   sing N N 295 
OQT N3  H2   sing N N 296 
OQT C9  H3   sing N N 297 
OQT N13 H4   sing N N 298 
OQT C14 H5   sing N N 299 
OQT C23 H6   sing N N 300 
OQT C22 H7   sing N N 301 
OQT C21 H8   sing N N 302 
OQT C21 H9   sing N N 303 
OQT C19 H10  sing N N 304 
OQT C18 H11  sing N N 305 
OQT C17 H12  sing N N 306 
OQT C16 H13  sing N N 307 
PHE N   CA   sing N N 308 
PHE N   H    sing N N 309 
PHE N   H2   sing N N 310 
PHE CA  C    sing N N 311 
PHE CA  CB   sing N N 312 
PHE CA  HA   sing N N 313 
PHE C   O    doub N N 314 
PHE C   OXT  sing N N 315 
PHE CB  CG   sing N N 316 
PHE CB  HB2  sing N N 317 
PHE CB  HB3  sing N N 318 
PHE CG  CD1  doub Y N 319 
PHE CG  CD2  sing Y N 320 
PHE CD1 CE1  sing Y N 321 
PHE CD1 HD1  sing N N 322 
PHE CD2 CE2  doub Y N 323 
PHE CD2 HD2  sing N N 324 
PHE CE1 CZ   doub Y N 325 
PHE CE1 HE1  sing N N 326 
PHE CE2 CZ   sing Y N 327 
PHE CE2 HE2  sing N N 328 
PHE CZ  HZ   sing N N 329 
PHE OXT HXT  sing N N 330 
PRO N   CA   sing N N 331 
PRO N   CD   sing N N 332 
PRO N   H    sing N N 333 
PRO CA  C    sing N N 334 
PRO CA  CB   sing N N 335 
PRO CA  HA   sing N N 336 
PRO C   O    doub N N 337 
PRO C   OXT  sing N N 338 
PRO CB  CG   sing N N 339 
PRO CB  HB2  sing N N 340 
PRO CB  HB3  sing N N 341 
PRO CG  CD   sing N N 342 
PRO CG  HG2  sing N N 343 
PRO CG  HG3  sing N N 344 
PRO CD  HD2  sing N N 345 
PRO CD  HD3  sing N N 346 
PRO OXT HXT  sing N N 347 
SER N   CA   sing N N 348 
SER N   H    sing N N 349 
SER N   H2   sing N N 350 
SER CA  C    sing N N 351 
SER CA  CB   sing N N 352 
SER CA  HA   sing N N 353 
SER C   O    doub N N 354 
SER C   OXT  sing N N 355 
SER CB  OG   sing N N 356 
SER CB  HB2  sing N N 357 
SER CB  HB3  sing N N 358 
SER OG  HG   sing N N 359 
SER OXT HXT  sing N N 360 
THR N   CA   sing N N 361 
THR N   H    sing N N 362 
THR N   H2   sing N N 363 
THR CA  C    sing N N 364 
THR CA  CB   sing N N 365 
THR CA  HA   sing N N 366 
THR C   O    doub N N 367 
THR C   OXT  sing N N 368 
THR CB  OG1  sing N N 369 
THR CB  CG2  sing N N 370 
THR CB  HB   sing N N 371 
THR OG1 HG1  sing N N 372 
THR CG2 HG21 sing N N 373 
THR CG2 HG22 sing N N 374 
THR CG2 HG23 sing N N 375 
THR OXT HXT  sing N N 376 
TRP N   CA   sing N N 377 
TRP N   H    sing N N 378 
TRP N   H2   sing N N 379 
TRP CA  C    sing N N 380 
TRP CA  CB   sing N N 381 
TRP CA  HA   sing N N 382 
TRP C   O    doub N N 383 
TRP C   OXT  sing N N 384 
TRP CB  CG   sing N N 385 
TRP CB  HB2  sing N N 386 
TRP CB  HB3  sing N N 387 
TRP CG  CD1  doub Y N 388 
TRP CG  CD2  sing Y N 389 
TRP CD1 NE1  sing Y N 390 
TRP CD1 HD1  sing N N 391 
TRP CD2 CE2  doub Y N 392 
TRP CD2 CE3  sing Y N 393 
TRP NE1 CE2  sing Y N 394 
TRP NE1 HE1  sing N N 395 
TRP CE2 CZ2  sing Y N 396 
TRP CE3 CZ3  doub Y N 397 
TRP CE3 HE3  sing N N 398 
TRP CZ2 CH2  doub Y N 399 
TRP CZ2 HZ2  sing N N 400 
TRP CZ3 CH2  sing Y N 401 
TRP CZ3 HZ3  sing N N 402 
TRP CH2 HH2  sing N N 403 
TRP OXT HXT  sing N N 404 
TYR N   CA   sing N N 405 
TYR N   H    sing N N 406 
TYR N   H2   sing N N 407 
TYR CA  C    sing N N 408 
TYR CA  CB   sing N N 409 
TYR CA  HA   sing N N 410 
TYR C   O    doub N N 411 
TYR C   OXT  sing N N 412 
TYR CB  CG   sing N N 413 
TYR CB  HB2  sing N N 414 
TYR CB  HB3  sing N N 415 
TYR CG  CD1  doub Y N 416 
TYR CG  CD2  sing Y N 417 
TYR CD1 CE1  sing Y N 418 
TYR CD1 HD1  sing N N 419 
TYR CD2 CE2  doub Y N 420 
TYR CD2 HD2  sing N N 421 
TYR CE1 CZ   doub Y N 422 
TYR CE1 HE1  sing N N 423 
TYR CE2 CZ   sing Y N 424 
TYR CE2 HE2  sing N N 425 
TYR CZ  OH   sing N N 426 
TYR OH  HH   sing N N 427 
TYR OXT HXT  sing N N 428 
VAL N   CA   sing N N 429 
VAL N   H    sing N N 430 
VAL N   H2   sing N N 431 
VAL CA  C    sing N N 432 
VAL CA  CB   sing N N 433 
VAL CA  HA   sing N N 434 
VAL C   O    doub N N 435 
VAL C   OXT  sing N N 436 
VAL CB  CG1  sing N N 437 
VAL CB  CG2  sing N N 438 
VAL CB  HB   sing N N 439 
VAL CG1 HG11 sing N N 440 
VAL CG1 HG12 sing N N 441 
VAL CG1 HG13 sing N N 442 
VAL CG2 HG21 sing N N 443 
VAL CG2 HG22 sing N N 444 
VAL CG2 HG23 sing N N 445 
VAL OXT HXT  sing N N 446 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        OQT 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   OQT 
_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                    6YH8 
_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]   0.023790 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005902 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024364 
_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]   0.014424 
_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   A HIS A 1 4   ? 11.042  -0.941  7.363   0.50 31.56 ? 4   HIS A N   1 
ATOM   2    N  N   B HIS A 1 4   ? 11.630  -0.025  8.210   0.50 27.02 ? 4   HIS A N   1 
ATOM   3    C  CA  A HIS A 1 4   ? 10.191  -0.204  8.326   0.50 21.35 ? 4   HIS A CA  1 
ATOM   4    C  CA  B HIS A 1 4   ? 10.414  0.361   8.951   0.50 31.17 ? 4   HIS A CA  1 
ATOM   5    C  C   A HIS A 1 4   ? 9.545   -1.195  9.300   0.50 19.77 ? 4   HIS A C   1 
ATOM   6    C  C   B HIS A 1 4   ? 9.634   -0.913  9.310   0.50 27.37 ? 4   HIS A C   1 
ATOM   7    O  O   A HIS A 1 4   ? 9.849   -2.393  9.273   0.50 19.97 ? 4   HIS A O   1 
ATOM   8    O  O   B HIS A 1 4   ? 9.809   -2.022  8.785   0.50 27.89 ? 4   HIS A O   1 
ATOM   9    C  CB  A HIS A 1 4   ? 9.264   0.727   7.530   0.50 14.60 ? 4   HIS A CB  1 
ATOM   10   C  CB  B HIS A 1 4   ? 9.594   1.425   8.158   0.50 26.17 ? 4   HIS A CB  1 
ATOM   11   C  CG  A HIS A 1 4   ? 9.092   2.071   8.169   0.50 9.92  ? 4   HIS A CG  1 
ATOM   12   C  CG  B HIS A 1 4   ? 8.962   0.837   6.928   0.50 30.97 ? 4   HIS A CG  1 
ATOM   13   N  ND1 A HIS A 1 4   ? 9.622   2.265   9.386   0.50 18.66 ? 4   HIS A ND1 1 
ATOM   14   N  ND1 B HIS A 1 4   ? 8.028   1.519   6.161   0.50 39.07 ? 4   HIS A ND1 1 
ATOM   15   C  CD2 A HIS A 1 4   ? 8.071   2.939   8.062   0.50 18.44 ? 4   HIS A CD2 1 
ATOM   16   C  CD2 B HIS A 1 4   ? 9.109   -0.376  6.351   0.50 27.69 ? 4   HIS A CD2 1 
ATOM   17   C  CE1 A HIS A 1 4   ? 9.237   3.439   9.842   0.50 23.74 ? 4   HIS A CE1 1 
ATOM   18   C  CE1 B HIS A 1 4   ? 7.638   0.753   5.151   0.50 33.94 ? 4   HIS A CE1 1 
ATOM   19   N  NE2 A HIS A 1 4   ? 8.277   3.886   9.039   0.50 25.11 ? 4   HIS A NE2 1 
ATOM   20   N  NE2 B HIS A 1 4   ? 8.296   -0.417  5.248   0.50 27.11 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.674   -0.703  10.182  1.00 21.86 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 8.034   -1.670  11.032  1.00 18.16 ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 7.048   -2.500  10.234  1.00 17.33 ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.489   -2.076  9.182   1.00 19.54 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.404   -0.969  12.222  1.00 17.12 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 6.223   -0.140  11.853  1.00 15.10 ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 6.205   1.164   11.468  1.00 17.50 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.851   -0.593  11.790  1.00 12.76 ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.908   1.556   11.251  1.00 16.90 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 4.060   0.493   11.400  1.00 13.15 ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 4.203   -1.810  12.090  1.00 13.19 ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.675   0.421   11.315  1.00 13.42 ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.824   -1.894  12.010  1.00 13.34 ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 2.093   -0.778  11.616  1.00 14.50 ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.746   -3.654  10.807  1.00 15.24 ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.705   -4.501  10.238  1.00 17.55 ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.433   -5.630  11.228  1.00 15.07 ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.413   -5.406  12.432  1.00 14.79 ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 5.133   -6.835  10.720  1.00 19.60 ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.692   -7.937  11.585  1.00 18.17 ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.677   -9.144  11.627  1.00 18.83 ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 5.429   -10.199 12.299  1.00 22.00 ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 3.206   -8.265  11.306  1.00 18.25 ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 2.291   -7.148  11.738  1.00 13.13 ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.855   -7.096  13.051  1.00 11.64 ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.837   -6.172  10.866  1.00 13.71 ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 1.006   -6.101  13.498  1.00 10.49 ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.984   -5.167  11.298  1.00 12.02 ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.568   -5.131  12.618  1.00 9.84  ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.272  -4.159  13.080  1.00 10.88 ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.777   -9.064  10.874  1.00 24.48 ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.758   -10.193 10.850  1.00 18.26 ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.767   -10.349 11.986  1.00 19.79 ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.921   -9.643  12.974  1.00 19.53 ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.627   -11.348 11.721  1.00 21.51 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.668  -11.721 12.655  1.00 22.72 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.583  -10.533 12.942  1.00 18.28 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 12.023  -10.386 14.078  1.00 21.17 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 11.540  -12.787 12.004  1.00 26.05 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 12.578  -13.419 12.922  1.00 35.52 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 13.295  -14.631 12.323  1.00 40.97 ? 9   LYS A CD  1 
ATOM   62   N  N   . HIS A 1 10  ? 11.940  -9.780  11.885  1.00 20.68 ? 10  HIS A N   1 
ATOM   63   C  CA  . HIS A 1 10  ? 12.991  -8.806  12.058  1.00 20.83 ? 10  HIS A CA  1 
ATOM   64   C  C   . HIS A 1 10  ? 12.421  -7.408  12.157  1.00 20.46 ? 10  HIS A C   1 
ATOM   65   O  O   . HIS A 1 10  ? 13.187  -6.552  12.560  1.00 20.87 ? 10  HIS A O   1 
ATOM   66   C  CB  . HIS A 1 10  ? 13.904  -8.778  10.848  1.00 21.60 ? 10  HIS A CB  1 
ATOM   67   C  CG  . HIS A 1 10  ? 14.545  -10.111 10.690  1.00 21.14 ? 10  HIS A CG  1 
ATOM   68   N  ND1 . HIS A 1 10  ? 15.613  -10.590 11.469  1.00 21.66 ? 10  HIS A ND1 1 
ATOM   69   C  CD2 . HIS A 1 10  ? 14.208  -11.060 9.828   1.00 20.90 ? 10  HIS A CD2 1 
ATOM   70   C  CE1 . HIS A 1 10  ? 15.891  -11.826 11.092  1.00 20.61 ? 10  HIS A CE1 1 
ATOM   71   N  NE2 . HIS A 1 10  ? 15.083  -12.102 10.011  1.00 19.00 ? 10  HIS A NE2 1 
ATOM   72   N  N   . ASN A 1 11  ? 11.062  -7.233  12.073  1.00 21.35 ? 11  ASN A N   1 
ATOM   73   C  CA  . ASN A 1 11  ? 10.457  -5.892  12.194  1.00 19.62 ? 11  ASN A CA  1 
ATOM   74   C  C   . ASN A 1 11  ? 9.098   -5.872  12.907  1.00 17.68 ? 11  ASN A C   1 
ATOM   75   O  O   . ASN A 1 11  ? 8.432   -4.856  12.866  1.00 18.15 ? 11  ASN A O   1 
ATOM   76   C  CB  . ASN A 1 11  ? 10.272  -5.207  10.830  1.00 17.74 ? 11  ASN A CB  1 
ATOM   77   C  CG  . ASN A 1 11  ? 9.233   -5.831  9.910   1.00 19.13 ? 11  ASN A CG  1 
ATOM   78   O  OD1 . ASN A 1 11  ? 8.596   -6.835  10.229  1.00 22.31 ? 11  ASN A OD1 1 
ATOM   79   N  ND2 . ASN A 1 11  ? 8.949   -5.213  8.780   1.00 22.22 ? 11  ASN A ND2 1 
ATOM   80   N  N   . GLY A 1 12  ? 8.679   -7.017  13.491  1.00 17.60 ? 12  GLY A N   1 
ATOM   81   C  CA  . GLY A 1 12  ? 7.402   -7.210  14.104  1.00 16.67 ? 12  GLY A CA  1 
ATOM   82   C  C   . GLY A 1 12  ? 7.450   -6.606  15.464  1.00 13.61 ? 12  GLY A C   1 
ATOM   83   O  O   . GLY A 1 12  ? 8.352   -5.937  15.925  1.00 15.16 ? 12  GLY A O   1 
ATOM   84   N  N   . PRO A 1 13  ? 6.358   -6.891  16.195  1.00 13.83 ? 13  PRO A N   1 
ATOM   85   C  CA  . PRO A 1 13  ? 6.140   -6.300  17.521  1.00 14.24 ? 13  PRO A CA  1 
ATOM   86   C  C   . PRO A 1 13  ? 7.290   -6.319  18.517  1.00 14.69 ? 13  PRO A C   1 
ATOM   87   O  O   . PRO A 1 13  ? 7.367   -5.354  19.260  1.00 15.21 ? 13  PRO A O   1 
ATOM   88   C  CB  . PRO A 1 13  ? 4.943   -7.109  18.057  1.00 14.45 ? 13  PRO A CB  1 
ATOM   89   C  CG  . PRO A 1 13  ? 4.153   -7.384  16.805  1.00 15.88 ? 13  PRO A CG  1 
ATOM   90   C  CD  . PRO A 1 13  ? 5.194   -7.630  15.702  1.00 14.54 ? 13  PRO A CD  1 
ATOM   91   N  N   . GLU A 1 14  ? 8.116   -7.363  18.579  1.00 14.96 ? 14  GLU A N   1 
ATOM   92   C  CA  . GLU A 1 14  ? 9.204   -7.395  19.554  1.00 18.99 ? 14  GLU A CA  1 
ATOM   93   C  C   . GLU A 1 14  ? 10.307  -6.399  19.175  1.00 16.07 ? 14  GLU A C   1 
ATOM   94   O  O   . GLU A 1 14  ? 11.194  -6.228  20.005  1.00 17.55 ? 14  GLU A O   1 
ATOM   95   C  CB  . GLU A 1 14  ? 9.852   -8.778  19.684  1.00 21.62 ? 14  GLU A CB  1 
ATOM   96   C  CG  . GLU A 1 14  ? 8.843   -9.879  19.939  1.00 24.85 ? 14  GLU A CG  1 
ATOM   97   C  CD  . GLU A 1 14  ? 7.972   -9.804  21.207  1.00 43.21 ? 14  GLU A CD  1 
ATOM   98   O  OE1 . GLU A 1 14  ? 8.543   -9.689  22.315  1.00 50.31 ? 14  GLU A OE1 1 
ATOM   99   O  OE2 . GLU A 1 14  ? 6.682   -9.873  21.100  1.00 50.14 ? 14  GLU A OE2 1 
ATOM   100  N  N   . HIS A 1 15  ? 10.229  -5.788  17.984  1.00 15.00 ? 15  HIS A N   1 
ATOM   101  C  CA  . HIS A 1 15  ? 11.238  -4.842  17.561  1.00 15.47 ? 15  HIS A CA  1 
ATOM   102  C  C   . HIS A 1 15  ? 10.776  -3.397  17.697  1.00 14.81 ? 15  HIS A C   1 
ATOM   103  O  O   . HIS A 1 15  ? 11.607  -2.467  17.653  1.00 16.11 ? 15  HIS A O   1 
ATOM   104  C  CB  . HIS A 1 15  ? 11.572  -4.987  16.093  1.00 15.87 ? 15  HIS A CB  1 
ATOM   105  C  CG  . HIS A 1 15  ? 12.336  -6.239  15.895  1.00 17.20 ? 15  HIS A CG  1 
ATOM   106  N  ND1 . HIS A 1 15  ? 13.756  -6.301  16.035  1.00 18.48 ? 15  HIS A ND1 1 
ATOM   107  C  CD2 . HIS A 1 15  ? 11.887  -7.486  15.567  1.00 19.65 ? 15  HIS A CD2 1 
ATOM   108  C  CE1 . HIS A 1 15  ? 14.150  -7.542  15.755  1.00 21.27 ? 15  HIS A CE1 1 
ATOM   109  N  NE2 . HIS A 1 15  ? 13.039  -8.289  15.463  1.00 19.47 ? 15  HIS A NE2 1 
ATOM   110  N  N   . TRP A 1 16  ? 9.472   -3.166  17.838  1.00 13.15 ? 16  TRP A N   1 
ATOM   111  C  CA  . TRP A 1 16  ? 8.924   -1.833  17.728  1.00 12.66 ? 16  TRP A CA  1 
ATOM   112  C  C   . TRP A 1 16  ? 9.500   -0.864  18.754  1.00 13.18 ? 16  TRP A C   1 
ATOM   113  O  O   . TRP A 1 16  ? 9.593   0.348   18.494  1.00 14.31 ? 16  TRP A O   1 
ATOM   114  C  CB  . TRP A 1 16  ? 7.399   -1.896  17.841  1.00 11.34 ? 16  TRP A CB  1 
ATOM   115  C  CG  . TRP A 1 16  ? 6.757   -2.582  16.691  1.00 11.06 ? 16  TRP A CG  1 
ATOM   116  C  CD1 . TRP A 1 16  ? 7.317   -3.052  15.538  1.00 12.05 ? 16  TRP A CD1 1 
ATOM   117  C  CD2 . TRP A 1 16  ? 5.354   -2.892  16.600  1.00 10.53 ? 16  TRP A CD2 1 
ATOM   118  N  NE1 . TRP A 1 16  ? 6.353   -3.622  14.746  1.00 11.44 ? 16  TRP A NE1 1 
ATOM   119  C  CE2 . TRP A 1 16  ? 5.140   -3.561  15.376  1.00 11.14 ? 16  TRP A CE2 1 
ATOM   120  C  CE3 . TRP A 1 16  ? 4.269   -2.723  17.494  1.00 10.96 ? 16  TRP A CE3 1 
ATOM   121  C  CZ2 . TRP A 1 16  ? 3.858   -4.001  14.972  1.00 11.21 ? 16  TRP A CZ2 1 
ATOM   122  C  CZ3 . TRP A 1 16  ? 3.043   -3.177  17.110  1.00 11.09 ? 16  TRP A CZ3 1 
ATOM   123  C  CH2 . TRP A 1 16  ? 2.844   -3.777  15.874  1.00 11.59 ? 16  TRP A CH2 1 
ATOM   124  N  N   . HIS A 1 17  ? 9.880   -1.369  19.930  1.00 13.18 ? 17  HIS A N   1 
ATOM   125  C  CA  . HIS A 1 17  ? 10.364  -0.521  21.000  1.00 14.23 ? 17  HIS A CA  1 
ATOM   126  C  C   . HIS A 1 17  ? 11.605  0.272   20.585  1.00 16.08 ? 17  HIS A C   1 
ATOM   127  O  O   . HIS A 1 17  ? 11.872  1.311   21.194  1.00 18.20 ? 17  HIS A O   1 
ATOM   128  C  CB  . HIS A 1 17  ? 10.663  -1.301  22.287  1.00 15.14 ? 17  HIS A CB  1 
ATOM   129  C  CG  . HIS A 1 17  ? 11.869  -2.168  22.210  1.00 17.47 ? 17  HIS A CG  1 
ATOM   130  N  ND1 . HIS A 1 17  ? 13.080  -1.787  22.759  1.00 20.33 ? 17  HIS A ND1 1 
ATOM   131  C  CD2 . HIS A 1 17  ? 12.030  -3.351  21.639  1.00 18.34 ? 17  HIS A CD2 1 
ATOM   132  C  CE1 . HIS A 1 17  ? 13.901  -2.719  22.490  1.00 21.97 ? 17  HIS A CE1 1 
ATOM   133  N  NE2 . HIS A 1 17  ? 13.349  -3.682  21.823  1.00 18.44 ? 17  HIS A NE2 1 
ATOM   134  N  N   . LYS A 1 18  ? 12.404  -0.267  19.642  1.00 17.69 ? 18  LYS A N   1 
ATOM   135  C  CA  . LYS A 1 18  ? 13.588  0.492   19.297  1.00 18.74 ? 18  LYS A CA  1 
ATOM   136  C  C   . LYS A 1 18  ? 13.264  1.819   18.642  1.00 21.08 ? 18  LYS A C   1 
ATOM   137  O  O   . LYS A 1 18  ? 13.909  2.803   18.892  1.00 24.30 ? 18  LYS A O   1 
ATOM   138  C  CB  . LYS A 1 18  ? 14.524  -0.359  18.406  1.00 18.10 ? 18  LYS A CB  1 
ATOM   139  C  CG  . LYS A 1 18  ? 15.118  -1.570  19.139  1.00 20.46 ? 18  LYS A CG  1 
ATOM   140  C  CD  . LYS A 1 18  ? 15.758  -2.553  18.257  1.00 18.69 ? 18  LYS A CD  1 
ATOM   141  C  CE  . LYS A 1 18  ? 14.827  -3.511  17.573  1.00 21.20 ? 18  LYS A CE  1 
ATOM   142  N  NZ  . LYS A 1 18  ? 15.497  -4.287  16.493  1.00 19.84 ? 18  LYS A NZ  1 
ATOM   143  N  N   . ASP A 1 19  ? 12.266  1.877   17.755  1.00 17.81 ? 19  ASP A N   1 
ATOM   144  C  CA  . ASP A 1 19  ? 11.865  3.139   17.152  1.00 19.65 ? 19  ASP A CA  1 
ATOM   145  C  C   . ASP A 1 19  ? 10.846  3.863   18.027  1.00 19.75 ? 19  ASP A C   1 
ATOM   146  O  O   . ASP A 1 19  ? 10.731  5.068   17.958  1.00 22.22 ? 19  ASP A O   1 
ATOM   147  C  CB  . ASP A 1 19  ? 11.363  2.953   15.716  1.00 23.00 ? 19  ASP A CB  1 
ATOM   148  C  CG  . ASP A 1 19  ? 12.411  3.023   14.630  1.00 27.52 ? 19  ASP A CG  1 
ATOM   149  O  OD1 . ASP A 1 19  ? 13.490  3.511   14.888  1.00 39.11 ? 19  ASP A OD1 1 
ATOM   150  O  OD2 . ASP A 1 19  ? 12.115  2.538   13.543  1.00 48.17 ? 19  ASP A OD2 1 
ATOM   151  N  N   . PHE A 1 20  ? 10.081  3.116   18.813  1.00 18.28 ? 20  PHE A N   1 
ATOM   152  C  CA  . PHE A 1 20  ? 8.991   3.675   19.559  1.00 15.77 ? 20  PHE A CA  1 
ATOM   153  C  C   . PHE A 1 20  ? 9.086   3.222   21.003  1.00 14.38 ? 20  PHE A C   1 
ATOM   154  O  O   . PHE A 1 20  ? 8.461   2.212   21.372  1.00 14.64 ? 20  PHE A O   1 
ATOM   155  C  CB  . PHE A 1 20  ? 7.669   3.261   18.906  1.00 16.50 ? 20  PHE A CB  1 
ATOM   156  C  CG  . PHE A 1 20  ? 7.595   3.672   17.461  1.00 18.37 ? 20  PHE A CG  1 
ATOM   157  C  CD1 . PHE A 1 20  ? 7.285   4.987   17.126  1.00 22.47 ? 20  PHE A CD1 1 
ATOM   158  C  CD2 . PHE A 1 20  ? 8.004   2.774   16.471  1.00 21.79 ? 20  PHE A CD2 1 
ATOM   159  C  CE1 . PHE A 1 20  ? 7.329   5.383   15.787  1.00 22.93 ? 20  PHE A CE1 1 
ATOM   160  C  CE2 . PHE A 1 20  ? 8.041   3.167   15.141  1.00 26.92 ? 20  PHE A CE2 1 
ATOM   161  C  CZ  . PHE A 1 20  ? 7.701   4.451   14.825  1.00 21.84 ? 20  PHE A CZ  1 
ATOM   162  N  N   . PRO A 1 21  ? 9.943   3.840   21.838  1.00 18.38 ? 21  PRO A N   1 
ATOM   163  C  CA  . PRO A 1 21  ? 10.164  3.324   23.202  1.00 18.36 ? 21  PRO A CA  1 
ATOM   164  C  C   . PRO A 1 21  ? 8.915   3.212   24.089  1.00 15.59 ? 21  PRO A C   1 
ATOM   165  O  O   . PRO A 1 21  ? 8.963   2.417   25.043  1.00 16.63 ? 21  PRO A O   1 
ATOM   166  C  CB  . PRO A 1 21  ? 11.295  4.203   23.796  1.00 21.67 ? 21  PRO A CB  1 
ATOM   167  C  CG  . PRO A 1 21  ? 11.436  5.305   22.800  1.00 26.04 ? 21  PRO A CG  1 
ATOM   168  C  CD  . PRO A 1 21  ? 10.831  4.937   21.462  1.00 21.04 ? 21  PRO A CD  1 
ATOM   169  N  N   A ILE A 1 22  ? 7.843   3.959   23.774  0.50 15.85 ? 22  ILE A N   1 
ATOM   170  N  N   B ILE A 1 22  ? 7.862   3.961   23.735  0.50 15.71 ? 22  ILE A N   1 
ATOM   171  C  CA  A ILE A 1 22  ? 6.612   3.815   24.541  0.50 14.81 ? 22  ILE A CA  1 
ATOM   172  C  CA  B ILE A 1 22  ? 6.609   3.861   24.459  0.50 15.21 ? 22  ILE A CA  1 
ATOM   173  C  C   A ILE A 1 22  ? 6.032   2.400   24.383  0.50 12.84 ? 22  ILE A C   1 
ATOM   174  C  C   B ILE A 1 22  ? 6.022   2.441   24.347  0.50 13.13 ? 22  ILE A C   1 
ATOM   175  O  O   A ILE A 1 22  ? 5.122   2.041   25.127  0.50 13.09 ? 22  ILE A O   1 
ATOM   176  O  O   B ILE A 1 22  ? 5.135   2.100   25.129  0.50 13.45 ? 22  ILE A O   1 
ATOM   177  C  CB  A ILE A 1 22  ? 5.578   4.867   24.095  0.50 13.93 ? 22  ILE A CB  1 
ATOM   178  C  CB  B ILE A 1 22  ? 5.639   4.948   23.954  0.50 15.72 ? 22  ILE A CB  1 
ATOM   179  C  CG1 A ILE A 1 22  ? 4.513   5.220   25.136  0.50 14.63 ? 22  ILE A CG1 1 
ATOM   180  C  CG1 B ILE A 1 22  ? 4.528   5.277   24.964  0.50 17.08 ? 22  ILE A CG1 1 
ATOM   181  C  CG2 A ILE A 1 22  ? 4.893   4.420   22.796  0.50 17.21 ? 22  ILE A CG2 1 
ATOM   182  C  CG2 B ILE A 1 22  ? 5.072   4.534   22.587  0.50 13.40 ? 22  ILE A CG2 1 
ATOM   183  C  CD1 A ILE A 1 22  ? 3.652   6.349   24.645  0.50 12.66 ? 22  ILE A CD1 1 
ATOM   184  C  CD1 B ILE A 1 22  ? 5.046   5.776   26.311  0.50 18.24 ? 22  ILE A CD1 1 
ATOM   185  N  N   . ALA A 1 23  ? 6.565   1.583   23.450  1.00 12.77 ? 23  ALA A N   1 
ATOM   186  C  CA  . ALA A 1 23  ? 6.118   0.198   23.322  1.00 12.60 ? 23  ALA A CA  1 
ATOM   187  C  C   . ALA A 1 23  ? 6.235   -0.535  24.660  1.00 11.95 ? 23  ALA A C   1 
ATOM   188  O  O   . ALA A 1 23  ? 5.521   -1.532  24.842  1.00 13.06 ? 23  ALA A O   1 
ATOM   189  C  CB  . ALA A 1 23  ? 6.936   -0.540  22.245  1.00 12.80 ? 23  ALA A CB  1 
ATOM   190  N  N   . LYS A 1 24  ? 7.134   -0.068  25.556  1.00 13.96 ? 24  LYS A N   1 
ATOM   191  C  CA  . LYS A 1 24  ? 7.321   -0.651  26.885  1.00 13.42 ? 24  LYS A CA  1 
ATOM   192  C  C   . LYS A 1 24  ? 6.673   0.203   27.985  1.00 16.79 ? 24  LYS A C   1 
ATOM   193  O  O   . LYS A 1 24  ? 7.069   0.144   29.153  1.00 20.14 ? 24  LYS A O   1 
ATOM   194  C  CB  . LYS A 1 24  ? 8.809   -0.939  27.123  1.00 16.27 ? 24  LYS A CB  1 
ATOM   195  C  CG  . LYS A 1 24  ? 9.394   -1.924  26.124  1.00 16.43 ? 24  LYS A CG  1 
ATOM   196  C  CD  . LYS A 1 24  ? 10.853  -2.188  26.471  1.00 22.15 ? 24  LYS A CD  1 
ATOM   197  C  CE  . LYS A 1 24  ? 11.544  -3.207  25.599  1.00 26.12 ? 24  LYS A CE  1 
ATOM   198  N  NZ  . LYS A 1 24  ? 11.132  -4.587  25.935  1.00 32.59 ? 24  LYS A NZ  1 
ATOM   199  N  N   . GLY A 1 25  ? 5.683   0.991   27.590  1.00 15.43 ? 25  GLY A N   1 
ATOM   200  C  CA  . GLY A 1 25  ? 5.067   2.001   28.430  1.00 16.98 ? 25  GLY A CA  1 
ATOM   201  C  C   . GLY A 1 25  ? 4.132   1.381   29.455  1.00 15.10 ? 25  GLY A C   1 
ATOM   202  O  O   . GLY A 1 25  ? 3.918   0.160   29.575  1.00 15.85 ? 25  GLY A O   1 
ATOM   203  N  N   . GLU A 1 26  ? 3.450   2.304   30.111  1.00 16.62 ? 26  GLU A N   1 
ATOM   204  C  CA  . GLU A 1 26  ? 2.612   1.922   31.207  1.00 16.32 ? 26  GLU A CA  1 
ATOM   205  C  C   . GLU A 1 26  ? 1.159   1.664   30.823  1.00 15.17 ? 26  GLU A C   1 
ATOM   206  O  O   . GLU A 1 26  ? 0.381   1.173   31.626  1.00 15.53 ? 26  GLU A O   1 
ATOM   207  C  CB  . GLU A 1 26  ? 2.626   3.012   32.311  1.00 25.46 ? 26  GLU A CB  1 
ATOM   208  C  CG  . GLU A 1 26  ? 4.015   3.290   32.872  1.00 28.11 ? 26  GLU A CG  1 
ATOM   209  C  CD  . GLU A 1 26  ? 4.652   2.064   33.532  1.00 28.75 ? 26  GLU A CD  1 
ATOM   210  O  OE1 . GLU A 1 26  ? 3.918   1.353   34.264  1.00 30.09 ? 26  GLU A OE1 1 
ATOM   211  O  OE2 . GLU A 1 26  ? 5.873   1.791   33.298  1.00 38.63 ? 26  GLU A OE2 1 
ATOM   212  N  N   . ARG A 1 27  ? 0.740   1.974   29.602  1.00 11.75 ? 27  ARG A N   1 
ATOM   213  C  CA  . ARG A 1 27  ? -0.650  1.753   29.231  1.00 9.76  ? 27  ARG A CA  1 
ATOM   214  C  C   . ARG A 1 27  ? -0.711  1.293   27.781  1.00 9.27  ? 27  ARG A C   1 
ATOM   215  O  O   . ARG A 1 27  ? -1.435  1.844   26.966  1.00 9.64  ? 27  ARG A O   1 
ATOM   216  C  CB  . ARG A 1 27  ? -1.527  2.973   29.482  1.00 11.61 ? 27  ARG A CB  1 
ATOM   217  C  CG  . ARG A 1 27  ? -1.125  4.310   28.888  1.00 14.40 ? 27  ARG A CG  1 
ATOM   218  C  CD  . ARG A 1 27  ? -2.099  5.479   29.064  1.00 15.34 ? 27  ARG A CD  1 
ATOM   219  N  NE  . ARG A 1 27  ? -3.242  5.355   28.138  1.00 13.45 ? 27  ARG A NE  1 
ATOM   220  C  CZ  . ARG A 1 27  ? -4.218  6.273   28.112  1.00 12.95 ? 27  ARG A CZ  1 
ATOM   221  N  NH1 . ARG A 1 27  ? -4.171  7.313   28.926  1.00 14.44 ? 27  ARG A NH1 1 
ATOM   222  N  NH2 . ARG A 1 27  ? -5.230  6.139   27.274  1.00 13.59 ? 27  ARG A NH2 1 
ATOM   223  N  N   . GLN A 1 28  ? 0.007   0.201   27.508  1.00 9.47  ? 28  GLN A N   1 
ATOM   224  C  CA  . GLN A 1 28  ? 0.034   -0.331  26.134  1.00 8.36  ? 28  GLN A CA  1 
ATOM   225  C  C   . GLN A 1 28  ? -1.114  -1.298  25.891  1.00 7.39  ? 28  GLN A C   1 
ATOM   226  O  O   . GLN A 1 28  ? -1.623  -1.979  26.787  1.00 8.96  ? 28  GLN A O   1 
ATOM   227  C  CB  . GLN A 1 28  ? 1.385   -0.989  25.904  1.00 9.88  ? 28  GLN A CB  1 
ATOM   228  C  CG  . GLN A 1 28  ? 2.534   0.040   25.787  1.00 10.09 ? 28  GLN A CG  1 
ATOM   229  C  CD  . GLN A 1 28  ? 2.407   0.826   24.496  1.00 9.02  ? 28  GLN A CD  1 
ATOM   230  O  OE1 . GLN A 1 28  ? 2.582   0.264   23.441  1.00 9.87  ? 28  GLN A OE1 1 
ATOM   231  N  NE2 . GLN A 1 28  ? 2.043   2.115   24.580  1.00 10.27 ? 28  GLN A NE2 1 
ATOM   232  N  N   . SER A 1 29  ? -1.454  -1.398  24.608  1.00 7.17  ? 29  SER A N   1 
ATOM   233  C  CA  . SER A 1 29  ? -2.531  -2.267  24.149  1.00 6.76  ? 29  SER A CA  1 
ATOM   234  C  C   . SER A 1 29  ? -1.988  -3.161  23.051  1.00 6.23  ? 29  SER A C   1 
ATOM   235  O  O   . SER A 1 29  ? -0.999  -2.812  22.386  1.00 7.72  ? 29  SER A O   1 
ATOM   236  C  CB  . SER A 1 29  ? -3.642  -1.408  23.572  1.00 6.84  ? 29  SER A CB  1 
ATOM   237  O  OG  . SER A 1 29  ? -4.269  -0.671  24.618  1.00 7.35  ? 29  SER A OG  1 
ATOM   238  N  N   . PRO A 1 30  ? -2.655  -4.284  22.800  1.00 6.13  ? 30  PRO A N   1 
ATOM   239  C  CA  . PRO A 1 30  ? -3.831  -4.821  23.504  1.00 6.50  ? 30  PRO A CA  1 
ATOM   240  C  C   . PRO A 1 30  ? -3.415  -5.484  24.806  1.00 6.59  ? 30  PRO A C   1 
ATOM   241  O  O   . PRO A 1 30  ? -2.239  -5.510  25.161  1.00 7.48  ? 30  PRO A O   1 
ATOM   242  C  CB  . PRO A 1 30  ? -4.330  -5.852  22.500  1.00 6.03  ? 30  PRO A CB  1 
ATOM   243  C  CG  . PRO A 1 30  ? -3.070  -6.429  21.922  1.00 6.66  ? 30  PRO A CG  1 
ATOM   244  C  CD  . PRO A 1 30  ? -2.133  -5.225  21.755  1.00 6.78  ? 30  PRO A CD  1 
ATOM   245  N  N   . VAL A 1 31  ? -4.411  -6.046  25.494  1.00 7.02  ? 31  VAL A N   1 
ATOM   246  C  CA  . VAL A 1 31  ? -4.227  -6.794  26.728  1.00 7.57  ? 31  VAL A CA  1 
ATOM   247  C  C   . VAL A 1 31  ? -5.102  -8.018  26.673  1.00 6.95  ? 31  VAL A C   1 
ATOM   248  O  O   . VAL A 1 31  ? -6.058  -8.062  25.912  1.00 7.87  ? 31  VAL A O   1 
ATOM   249  C  CB  . VAL A 1 31  ? -4.555  -5.948  27.984  1.00 8.84  ? 31  VAL A CB  1 
ATOM   250  C  CG1 . VAL A 1 31  ? -3.625  -4.743  28.060  1.00 10.33 ? 31  VAL A CG1 1 
ATOM   251  C  CG2 . VAL A 1 31  ? -6.033  -5.486  27.994  1.00 9.46  ? 31  VAL A CG2 1 
ATOM   252  N  N   . ASP A 1 32  ? -4.761  -8.979  27.534  1.00 7.85  ? 32  ASP A N   1 
ATOM   253  C  CA  . ASP A 1 32  ? -5.684  -10.059 27.837  1.00 7.85  ? 32  ASP A CA  1 
ATOM   254  C  C   . ASP A 1 32  ? -6.746  -9.538  28.799  1.00 8.40  ? 32  ASP A C   1 
ATOM   255  O  O   . ASP A 1 32  ? -6.418  -8.925  29.825  1.00 11.13 ? 32  ASP A O   1 
ATOM   256  C  CB  . ASP A 1 32  ? -4.914  -11.224 28.436  1.00 10.62 ? 32  ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 32  ? -5.865  -12.373 28.717  1.00 10.16 ? 32  ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 32  ? -6.573  -12.850 27.799  1.00 9.88  ? 32  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 32  ? -5.916  -12.811 29.924  1.00 13.79 ? 32  ASP A OD2 1 
ATOM   260  N  N   . ILE A 1 33  ? -8.011  -9.831  28.493  1.00 8.23  ? 33  ILE A N   1 
ATOM   261  C  CA  . ILE A 1 33  ? -9.101  -9.438  29.367  1.00 8.80  ? 33  ILE A CA  1 
ATOM   262  C  C   . ILE A 1 33  ? -9.355  -10.682 30.198  1.00 9.02  ? 33  ILE A C   1 
ATOM   263  O  O   . ILE A 1 33  ? -9.949  -11.663 29.748  1.00 10.25 ? 33  ILE A O   1 
ATOM   264  C  CB  . ILE A 1 33  ? -10.317 -9.022  28.528  1.00 8.81  ? 33  ILE A CB  1 
ATOM   265  C  CG1 . ILE A 1 33  ? -9.940  -7.812  27.693  1.00 10.06 ? 33  ILE A CG1 1 
ATOM   266  C  CG2 . ILE A 1 33  ? -11.521 -8.773  29.471  1.00 10.71 ? 33  ILE A CG2 1 
ATOM   267  C  CD1 . ILE A 1 33  ? -10.955 -7.541  26.574  1.00 11.08 ? 33  ILE A CD1 1 
ATOM   268  N  N   A ASP A 1 34  ? -8.957  -10.616 31.468  0.50 11.46 ? 34  ASP A N   1 
ATOM   269  N  N   B ASP A 1 34  ? -9.081  -10.525 31.506  0.50 10.37 ? 34  ASP A N   1 
ATOM   270  C  CA  A ASP A 1 34  ? -9.278  -11.701 32.384  0.50 12.19 ? 34  ASP A CA  1 
ATOM   271  C  CA  B ASP A 1 34  ? -9.344  -11.565 32.496  0.50 12.41 ? 34  ASP A CA  1 
ATOM   272  C  C   A ASP A 1 34  ? -10.671 -11.394 32.926  0.50 11.22 ? 34  ASP A C   1 
ATOM   273  C  C   B ASP A 1 34  ? -10.767 -11.336 32.987  0.50 13.03 ? 34  ASP A C   1 
ATOM   274  O  O   A ASP A 1 34  ? -10.831 -10.462 33.728  0.50 13.68 ? 34  ASP A O   1 
ATOM   275  O  O   B ASP A 1 34  ? -11.059 -10.392 33.736  0.50 14.53 ? 34  ASP A O   1 
ATOM   276  C  CB  A ASP A 1 34  ? -8.229  -11.754 33.495  0.50 13.85 ? 34  ASP A CB  1 
ATOM   277  C  CB  B ASP A 1 34  ? -8.284  -11.553 33.599  0.50 13.60 ? 34  ASP A CB  1 
ATOM   278  C  CG  A ASP A 1 34  ? -8.396  -12.972 34.377  0.50 17.06 ? 34  ASP A CG  1 
ATOM   279  C  CG  B ASP A 1 34  ? -8.527  -12.555 34.711  0.50 14.17 ? 34  ASP A CG  1 
ATOM   280  O  OD1 A ASP A 1 34  ? -7.940  -14.048 33.954  0.50 20.47 ? 34  ASP A OD1 1 
ATOM   281  O  OD1 B ASP A 1 34  ? -9.665  -13.086 34.813  0.50 14.21 ? 34  ASP A OD1 1 
ATOM   282  O  OD2 A ASP A 1 34  ? -9.029  -12.846 35.446  0.50 18.06 ? 34  ASP A OD2 1 
ATOM   283  O  OD2 B ASP A 1 34  ? -7.562  -12.814 35.467  0.50 19.43 ? 34  ASP A OD2 1 
ATOM   284  N  N   . THR A 1 35  ? -11.688 -12.141 32.480  1.00 12.48 ? 35  THR A N   1 
ATOM   285  C  CA  . THR A 1 35  ? -13.093 -11.811 32.724  1.00 13.96 ? 35  THR A CA  1 
ATOM   286  C  C   . THR A 1 35  ? -13.472 -11.962 34.169  1.00 13.77 ? 35  THR A C   1 
ATOM   287  O  O   . THR A 1 35  ? -14.412 -11.294 34.608  1.00 16.15 ? 35  THR A O   1 
ATOM   288  C  CB  . THR A 1 35  ? -13.974 -12.735 31.894  1.00 15.32 ? 35  THR A CB  1 
ATOM   289  O  OG1 . THR A 1 35  ? -13.836 -14.055 32.374  1.00 16.64 ? 35  THR A OG1 1 
ATOM   290  C  CG2 . THR A 1 35  ? -13.777 -12.662 30.401  1.00 17.54 ? 35  THR A CG2 1 
ATOM   291  N  N   . HIS A 1 36  ? -12.744 -12.774 34.939  1.00 16.42 ? 36  HIS A N   1 
ATOM   292  C  CA  . HIS A 1 36  ? -13.081 -12.984 36.328  1.00 16.40 ? 36  HIS A CA  1 
ATOM   293  C  C   . HIS A 1 36  ? -12.601 -11.826 37.171  1.00 20.20 ? 36  HIS A C   1 
ATOM   294  O  O   . HIS A 1 36  ? -13.301 -11.519 38.163  1.00 23.88 ? 36  HIS A O   1 
ATOM   295  C  CB  . HIS A 1 36  ? -12.644 -14.402 36.732  1.00 19.05 ? 36  HIS A CB  1 
ATOM   296  C  CG  . HIS A 1 36  ? -13.546 -15.469 36.170  1.00 19.31 ? 36  HIS A CG  1 
ATOM   297  N  ND1 . HIS A 1 36  ? -14.904 -15.577 36.538  1.00 24.30 ? 36  HIS A ND1 1 
ATOM   298  C  CD2 . HIS A 1 36  ? -13.339 -16.396 35.187  1.00 20.88 ? 36  HIS A CD2 1 
ATOM   299  C  CE1 . HIS A 1 36  ? -15.477 -16.578 35.858  1.00 23.92 ? 36  HIS A CE1 1 
ATOM   300  N  NE2 . HIS A 1 36  ? -14.531 -17.061 34.999  1.00 28.45 ? 36  HIS A NE2 1 
ATOM   301  N  N   . THR A 1 37  ? -11.482 -11.204 36.762  1.00 18.68 ? 37  THR A N   1 
ATOM   302  C  CA  . THR A 1 37  ? -10.858 -10.065 37.421  1.00 18.86 ? 37  THR A CA  1 
ATOM   303  C  C   . THR A 1 37  ? -11.467 -8.709  37.026  1.00 17.93 ? 37  THR A C   1 
ATOM   304  O  O   . THR A 1 37  ? -11.320 -7.757  37.778  1.00 22.47 ? 37  THR A O   1 
ATOM   305  C  CB  . THR A 1 37  ? -9.347  -10.086 37.152  1.00 26.55 ? 37  THR A CB  1 
ATOM   306  O  OG1 . THR A 1 37  ? -8.904  -11.321 37.703  1.00 30.85 ? 37  THR A OG1 1 
ATOM   307  C  CG2 . THR A 1 37  ? -8.596  -8.945  37.818  1.00 22.44 ? 37  THR A CG2 1 
ATOM   308  N  N   . ALA A 1 38  ? -12.101 -8.620  35.876  1.00 16.47 ? 38  ALA A N   1 
ATOM   309  C  CA  . ALA A 1 38  ? -12.685 -7.352  35.467  1.00 14.84 ? 38  ALA A CA  1 
ATOM   310  C  C   . ALA A 1 38  ? -13.778 -7.006  36.468  1.00 19.39 ? 38  ALA A C   1 
ATOM   311  O  O   . ALA A 1 38  ? -14.496 -7.845  36.932  1.00 24.52 ? 38  ALA A O   1 
ATOM   312  C  CB  . ALA A 1 38  ? -13.218 -7.501  34.065  1.00 15.47 ? 38  ALA A CB  1 
ATOM   313  N  N   . LYS A 1 39  ? -13.816 -5.744  36.839  1.00 18.01 ? 39  LYS A N   1 
ATOM   314  C  CA  . LYS A 1 39  ? -14.746 -5.278  37.840  1.00 21.17 ? 39  LYS A CA  1 
ATOM   315  C  C   . LYS A 1 39  ? -16.021 -4.726  37.196  1.00 17.22 ? 39  LYS A C   1 
ATOM   316  O  O   . LYS A 1 39  ? -15.975 -3.807  36.424  1.00 15.62 ? 39  LYS A O   1 
ATOM   317  C  CB  . LYS A 1 39  ? -14.019 -4.236  38.698  1.00 28.16 ? 39  LYS A CB  1 
ATOM   318  C  CG  . LYS A 1 39  ? -14.807 -3.319  39.600  1.00 27.10 ? 39  LYS A CG  1 
ATOM   319  C  CD  . LYS A 1 39  ? -15.010 -4.006  40.939  1.00 26.18 ? 39  LYS A CD  1 
ATOM   320  C  CE  . LYS A 1 39  ? -15.821 -3.199  41.913  1.00 27.24 ? 39  LYS A CE  1 
ATOM   321  N  NZ  . LYS A 1 39  ? -16.116 -3.999  43.120  1.00 29.02 ? 39  LYS A NZ  1 
ATOM   322  N  N   . TYR A 1 40  ? -17.187 -5.259  37.561  1.00 20.39 ? 40  TYR A N   1 
ATOM   323  C  CA  . TYR A 1 40  ? -18.431 -4.707  37.106  1.00 17.12 ? 40  TYR A CA  1 
ATOM   324  C  C   . TYR A 1 40  ? -18.523 -3.317  37.694  1.00 15.98 ? 40  TYR A C   1 
ATOM   325  O  O   . TYR A 1 40  ? -18.436 -3.116  38.919  1.00 18.43 ? 40  TYR A O   1 
ATOM   326  C  CB  . TYR A 1 40  ? -19.634 -5.559  37.533  1.00 22.93 ? 40  TYR A CB  1 
ATOM   327  C  CG  . TYR A 1 40  ? -20.967 -4.865  37.391  1.00 23.03 ? 40  TYR A CG  1 
ATOM   328  C  CD1 . TYR A 1 40  ? -21.369 -4.382  36.152  1.00 24.72 ? 40  TYR A CD1 1 
ATOM   329  C  CD2 . TYR A 1 40  ? -21.836 -4.689  38.476  1.00 34.43 ? 40  TYR A CD2 1 
ATOM   330  C  CE1 . TYR A 1 40  ? -22.552 -3.708  35.953  1.00 27.97 ? 40  TYR A CE1 1 
ATOM   331  C  CE2 . TYR A 1 40  ? -23.046 -4.035  38.287  1.00 36.15 ? 40  TYR A CE2 1 
ATOM   332  C  CZ  . TYR A 1 40  ? -23.417 -3.561  37.032  1.00 33.29 ? 40  TYR A CZ  1 
ATOM   333  O  OH  . TYR A 1 40  ? -24.601 -2.904  36.857  1.00 42.25 ? 40  TYR A OH  1 
ATOM   334  N  N   . ASP A 1 41  ? -18.793 -2.360  36.844  1.00 16.07 ? 41  ASP A N   1 
ATOM   335  C  CA  . ASP A 1 41  ? -18.913 -0.991  37.307  1.00 17.34 ? 41  ASP A CA  1 
ATOM   336  C  C   . ASP A 1 41  ? -20.321 -0.474  37.048  1.00 19.84 ? 41  ASP A C   1 
ATOM   337  O  O   . ASP A 1 41  ? -20.675 -0.070  35.948  1.00 19.26 ? 41  ASP A O   1 
ATOM   338  C  CB  . ASP A 1 41  ? -17.889 -0.068  36.667  1.00 21.43 ? 41  ASP A CB  1 
ATOM   339  C  CG  . ASP A 1 41  ? -17.943 1.335   37.229  1.00 27.10 ? 41  ASP A CG  1 
ATOM   340  O  OD1 . ASP A 1 41  ? -18.899 1.647   37.979  1.00 29.50 ? 41  ASP A OD1 1 
ATOM   341  O  OD2 . ASP A 1 41  ? -17.012 2.102   36.925  1.00 33.18 ? 41  ASP A OD2 1 
ATOM   342  N  N   . PRO A 1 42  ? -21.176 -0.424  38.103  1.00 25.90 ? 42  PRO A N   1 
ATOM   343  C  CA  . PRO A 1 42  ? -22.601 -0.058  37.969  1.00 34.40 ? 42  PRO A CA  1 
ATOM   344  C  C   . PRO A 1 42  ? -22.729 1.418   37.587  1.00 30.70 ? 42  PRO A C   1 
ATOM   345  O  O   . PRO A 1 42  ? -23.773 1.870   37.075  1.00 39.84 ? 42  PRO A O   1 
ATOM   346  C  CB  . PRO A 1 42  ? -23.193 -0.387  39.361  1.00 41.81 ? 42  PRO A CB  1 
ATOM   347  C  CG  . PRO A 1 42  ? -22.018 -0.164  40.303  1.00 34.05 ? 42  PRO A CG  1 
ATOM   348  C  CD  . PRO A 1 42  ? -20.849 -0.747  39.526  1.00 27.84 ? 42  PRO A CD  1 
ATOM   349  N  N   . SER A 1 43  ? -21.648 2.191   37.787  1.00 26.19 ? 43  SER A N   1 
ATOM   350  C  CA  . SER A 1 43  ? -21.719 3.598   37.361  1.00 31.21 ? 43  SER A CA  1 
ATOM   351  C  C   . SER A 1 43  ? -21.413 3.798   35.854  1.00 27.91 ? 43  SER A C   1 
ATOM   352  O  O   . SER A 1 43  ? -21.621 4.909   35.342  1.00 34.36 ? 43  SER A O   1 
ATOM   353  C  CB  . SER A 1 43  ? -20.828 4.455   38.190  1.00 40.72 ? 43  SER A CB  1 
ATOM   354  O  OG  . SER A 1 43  ? -19.507 4.345   37.715  1.00 37.31 ? 43  SER A OG  1 
ATOM   355  N  N   . LEU A 1 44  ? -20.983 2.771   35.111  1.00 24.38 ? 44  LEU A N   1 
ATOM   356  C  CA  . LEU A 1 44  ? -20.739 2.976   33.686  1.00 25.96 ? 44  LEU A CA  1 
ATOM   357  C  C   . LEU A 1 44  ? -22.100 3.194   33.040  1.00 31.97 ? 44  LEU A C   1 
ATOM   358  O  O   . LEU A 1 44  ? -23.107 2.666   33.494  1.00 30.16 ? 44  LEU A O   1 
ATOM   359  C  CB  . LEU A 1 44  ? -20.069 1.740   33.094  1.00 24.50 ? 44  LEU A CB  1 
ATOM   360  C  CG  . LEU A 1 44  ? -18.550 1.687   33.283  1.00 19.82 ? 44  LEU A CG  1 
ATOM   361  C  CD1 . LEU A 1 44  ? -18.005 0.316   33.005  1.00 21.51 ? 44  LEU A CD1 1 
ATOM   362  C  CD2 . LEU A 1 44  ? -17.775 2.729   32.457  1.00 19.81 ? 44  LEU A CD2 1 
ATOM   363  N  N   . LYS A 1 45  ? -22.127 3.923   31.920  1.00 31.27 ? 45  LYS A N   1 
ATOM   364  C  CA  . LYS A 1 45  ? -23.377 4.045   31.202  1.00 30.02 ? 45  LYS A CA  1 
ATOM   365  C  C   . LYS A 1 45  ? -23.376 3.167   29.966  1.00 24.57 ? 45  LYS A C   1 
ATOM   366  O  O   . LYS A 1 45  ? -22.366 2.521   29.575  1.00 28.87 ? 45  LYS A O   1 
ATOM   367  C  CB  . LYS A 1 45  ? -23.629 5.447   30.720  1.00 26.27 ? 45  LYS A CB  1 
ATOM   368  C  CG  . LYS A 1 45  ? -23.302 6.568   31.710  1.00 36.24 ? 45  LYS A CG  1 
ATOM   369  N  N   . PRO A 1 46  ? -24.598 2.959   29.428  1.00 25.30 ? 46  PRO A N   1 
ATOM   370  C  CA  . PRO A 1 46  ? -24.708 2.187   28.196  1.00 24.54 ? 46  PRO A CA  1 
ATOM   371  C  C   . PRO A 1 46  ? -23.922 3.016   27.229  1.00 18.89 ? 46  PRO A C   1 
ATOM   372  O  O   . PRO A 1 46  ? -23.919 4.229   27.305  1.00 23.39 ? 46  PRO A O   1 
ATOM   373  C  CB  . PRO A 1 46  ? -26.208 2.239   27.840  1.00 27.79 ? 46  PRO A CB  1 
ATOM   374  C  CG  . PRO A 1 46  ? -26.890 2.518   29.188  1.00 33.94 ? 46  PRO A CG  1 
ATOM   375  C  CD  . PRO A 1 46  ? -25.899 3.448   29.899  1.00 30.12 ? 46  PRO A CD  1 
ATOM   376  N  N   . LEU A 1 47  ? -23.363 2.278   26.308  1.00 22.37 ? 47  LEU A N   1 
ATOM   377  C  CA  . LEU A 1 47  ? -22.670 3.022   25.327  1.00 21.98 ? 47  LEU A CA  1 
ATOM   378  C  C   . LEU A 1 47  ? -23.742 3.610   24.420  1.00 22.75 ? 47  LEU A C   1 
ATOM   379  O  O   . LEU A 1 47  ? -24.773 2.949   24.244  1.00 27.37 ? 47  LEU A O   1 
ATOM   380  C  CB  . LEU A 1 47  ? -21.921 1.913   24.621  1.00 32.68 ? 47  LEU A CB  1 
ATOM   381  C  CG  . LEU A 1 47  ? -20.800 2.277   23.717  1.00 30.14 ? 47  LEU A CG  1 
ATOM   382  C  CD1 . LEU A 1 47  ? -19.755 3.075   24.513  1.00 28.04 ? 47  LEU A CD1 1 
ATOM   383  C  CD2 . LEU A 1 47  ? -20.233 0.943   23.270  1.00 33.16 ? 47  LEU A CD2 1 
ATOM   384  N  N   . SER A 1 48  ? -23.485 4.776   23.850  1.00 15.15 ? 48  SER A N   1 
ATOM   385  C  CA  . SER A 1 48  ? -24.350 5.282   22.812  1.00 14.95 ? 48  SER A CA  1 
ATOM   386  C  C   . SER A 1 48  ? -23.537 5.274   21.503  1.00 14.00 ? 48  SER A C   1 
ATOM   387  O  O   . SER A 1 48  ? -22.505 5.954   21.357  1.00 15.74 ? 48  SER A O   1 
ATOM   388  C  CB  . SER A 1 48  ? -24.698 6.720   23.200  1.00 18.10 ? 48  SER A CB  1 
ATOM   389  O  OG  . SER A 1 48  ? -25.348 7.360   22.146  1.00 22.60 ? 48  SER A OG  1 
ATOM   390  N  N   . VAL A 1 49  ? -23.959 4.465   20.543  1.00 16.55 ? 49  VAL A N   1 
ATOM   391  C  CA  . VAL A 1 49  ? -23.333 4.345   19.246  1.00 18.11 ? 49  VAL A CA  1 
ATOM   392  C  C   . VAL A 1 49  ? -24.341 4.904   18.251  1.00 20.34 ? 49  VAL A C   1 
ATOM   393  O  O   . VAL A 1 49  ? -25.363 4.312   17.989  1.00 26.46 ? 49  VAL A O   1 
ATOM   394  C  CB  . VAL A 1 49  ? -22.965 2.874   18.937  1.00 21.67 ? 49  VAL A CB  1 
ATOM   395  C  CG1 . VAL A 1 49  ? -22.127 2.754   17.657  1.00 31.02 ? 49  VAL A CG1 1 
ATOM   396  C  CG2 . VAL A 1 49  ? -22.252 2.213   20.117  1.00 23.00 ? 49  VAL A CG2 1 
ATOM   397  N  N   . SER A 1 50  ? -24.058 6.094   17.717  1.00 19.77 ? 50  SER A N   1 
ATOM   398  C  CA  . SER A 1 50  ? -25.026 6.802   16.913  1.00 20.51 ? 50  SER A CA  1 
ATOM   399  C  C   . SER A 1 50  ? -24.466 6.947   15.520  1.00 17.02 ? 50  SER A C   1 
ATOM   400  O  O   . SER A 1 50  ? -23.818 7.947   15.212  1.00 18.10 ? 50  SER A O   1 
ATOM   401  C  CB  . SER A 1 50  ? -25.414 8.139   17.455  1.00 22.12 ? 50  SER A CB  1 
ATOM   402  O  OG  . SER A 1 50  ? -26.051 7.977   18.708  1.00 32.53 ? 50  SER A OG  1 
ATOM   403  N  N   . TYR A 1 51  ? -24.674 5.903   14.715  1.00 19.58 ? 51  TYR A N   1 
ATOM   404  C  CA  . TYR A 1 51  ? -24.098 5.812   13.402  1.00 16.75 ? 51  TYR A CA  1 
ATOM   405  C  C   . TYR A 1 51  ? -25.062 6.135   12.262  1.00 17.73 ? 51  TYR A C   1 
ATOM   406  O  O   . TYR A 1 51  ? -24.645 6.006   11.101  1.00 18.72 ? 51  TYR A O   1 
ATOM   407  C  CB  . TYR A 1 51  ? -23.380 4.475   13.120  1.00 16.22 ? 51  TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 51  ? -22.101 4.184   13.906  1.00 14.44 ? 51  TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 51  ? -21.402 5.149   14.592  1.00 14.04 ? 51  TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 51  ? -21.581 2.900   13.896  1.00 14.05 ? 51  TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 51  ? -20.233 4.846   15.249  1.00 11.65 ? 51  TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 51  ? -20.416 2.557   14.575  1.00 13.87 ? 51  TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 51  ? -19.728 3.557   15.252  1.00 12.69 ? 51  TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 51  ? -18.596 3.212   15.916  1.00 12.93 ? 51  TYR A OH  1 
ATOM   415  N  N   . ASP A 1 52  ? -26.288 6.583   12.568  1.00 21.33 ? 52  ASP A N   1 
ATOM   416  C  CA  . ASP A 1 52  ? -27.262 6.886   11.509  1.00 24.15 ? 52  ASP A CA  1 
ATOM   417  C  C   . ASP A 1 52  ? -26.782 7.735   10.314  1.00 27.27 ? 52  ASP A C   1 
ATOM   418  O  O   . ASP A 1 52  ? -27.215 7.563   9.163   1.00 30.19 ? 52  ASP A O   1 
ATOM   419  C  CB  . ASP A 1 52  ? -28.569 7.364   12.126  1.00 33.43 ? 52  ASP A CB  1 
ATOM   420  C  CG  . ASP A 1 52  ? -28.469 8.492   13.153  1.00 39.23 ? 52  ASP A CG  1 
ATOM   421  O  OD1 . ASP A 1 52  ? -27.751 8.308   14.198  1.00 47.33 ? 52  ASP A OD1 1 
ATOM   422  O  OD2 . ASP A 1 52  ? -29.119 9.547   12.921  1.00 62.13 ? 52  ASP A OD2 1 
ATOM   423  N  N   . GLN A 1 53  ? -25.903 8.686   10.538  1.00 25.95 ? 53  GLN A N   1 
ATOM   424  C  CA  . GLN A 1 53  ? -25.606 9.578   9.405   1.00 29.38 ? 53  GLN A CA  1 
ATOM   425  C  C   . GLN A 1 53  ? -24.160 9.401   8.926   1.00 20.57 ? 53  GLN A C   1 
ATOM   426  O  O   . GLN A 1 53  ? -23.543 10.295  8.377   1.00 22.45 ? 53  GLN A O   1 
ATOM   427  C  CB  . GLN A 1 53  ? -25.792 11.045  9.801   1.00 35.47 ? 53  GLN A CB  1 
ATOM   428  C  CG  . GLN A 1 53  ? -27.242 11.512  9.853   1.00 45.91 ? 53  GLN A CG  1 
ATOM   429  C  CD  . GLN A 1 53  ? -27.923 11.361  8.517   1.00 50.85 ? 53  GLN A CD  1 
ATOM   430  O  OE1 . GLN A 1 53  ? -28.783 10.496  8.339   1.00 63.28 ? 53  GLN A OE1 1 
ATOM   431  N  NE2 . GLN A 1 53  ? -27.537 12.191  7.553   1.00 59.07 ? 53  GLN A NE2 1 
ATOM   432  N  N   . ALA A 1 54  ? -23.583 8.246   9.163   1.00 19.98 ? 54  ALA A N   1 
ATOM   433  C  CA  . ALA A 1 54  ? -22.201 8.029   8.800   1.00 15.48 ? 54  ALA A CA  1 
ATOM   434  C  C   . ALA A 1 54  ? -22.010 8.137   7.296   1.00 19.48 ? 54  ALA A C   1 
ATOM   435  O  O   . ALA A 1 54  ? -22.866 7.679   6.529   1.00 22.49 ? 54  ALA A O   1 
ATOM   436  C  CB  . ALA A 1 54  ? -21.705 6.652   9.273   1.00 18.67 ? 54  ALA A CB  1 
ATOM   437  N  N   . THR A 1 55  ? -20.913 8.772   6.889   1.00 17.03 ? 55  THR A N   1 
ATOM   438  C  CA  . THR A 1 55  ? -20.622 8.935   5.478   1.00 17.56 ? 55  THR A CA  1 
ATOM   439  C  C   . THR A 1 55  ? -19.251 8.343   5.240   1.00 14.69 ? 55  THR A C   1 
ATOM   440  O  O   . THR A 1 55  ? -18.274 8.972   5.540   1.00 16.19 ? 55  THR A O   1 
ATOM   441  C  CB  . THR A 1 55  ? -20.482 10.412  5.073   1.00 23.96 ? 55  THR A CB  1 
ATOM   442  O  OG1 . THR A 1 55  ? -21.774 10.982  5.226   1.00 29.05 ? 55  THR A OG1 1 
ATOM   443  C  CG2 . THR A 1 55  ? -20.123 10.500  3.599   1.00 26.68 ? 55  THR A CG2 1 
ATOM   444  N  N   . SER A 1 56  ? -19.196 7.113   4.714   1.00 16.98 ? 56  SER A N   1 
ATOM   445  C  CA  . SER A 1 56  ? -17.911 6.544   4.344   1.00 17.51 ? 56  SER A CA  1 
ATOM   446  C  C   . SER A 1 56  ? -17.422 7.237   3.065   1.00 17.55 ? 56  SER A C   1 
ATOM   447  O  O   . SER A 1 56  ? -18.234 7.685   2.242   1.00 21.25 ? 56  SER A O   1 
ATOM   448  C  CB  . SER A 1 56  ? -17.930 5.017   4.124   1.00 16.98 ? 56  SER A CB  1 
ATOM   449  O  OG  . SER A 1 56  ? -18.742 4.661   3.008   1.00 18.78 ? 56  SER A OG  1 
ATOM   450  N  N   . LEU A 1 57  ? -16.129 7.287   2.879   1.00 17.88 ? 57  LEU A N   1 
ATOM   451  C  CA  . LEU A 1 57  ? -15.585 7.951   1.710   1.00 19.80 ? 57  LEU A CA  1 
ATOM   452  C  C   . LEU A 1 57  ? -14.746 7.011   0.866   1.00 18.43 ? 57  LEU A C   1 
ATOM   453  O  O   . LEU A 1 57  ? -14.859 7.005   -0.350  1.00 19.48 ? 57  LEU A O   1 
ATOM   454  C  CB  . LEU A 1 57  ? -14.732 9.131   2.119   1.00 20.47 ? 57  LEU A CB  1 
ATOM   455  C  CG  . LEU A 1 57  ? -15.554 10.291  2.682   1.00 22.57 ? 57  LEU A CG  1 
ATOM   456  C  CD1 . LEU A 1 57  ? -14.617 11.369  3.202   1.00 25.37 ? 57  LEU A CD1 1 
ATOM   457  C  CD2 . LEU A 1 57  ? -16.530 10.857  1.611   1.00 29.66 ? 57  LEU A CD2 1 
ATOM   458  N  N   A ARG A 1 58  ? -13.702 6.533   1.518   0.50 10.13 ? 58  ARG A N   1 
ATOM   459  N  N   B ARG A 1 58  ? -13.857 6.252   1.537   0.50 15.67 ? 58  ARG A N   1 
ATOM   460  C  CA  A ARG A 1 58  ? -12.810 5.614   0.804   0.50 12.07 ? 58  ARG A CA  1 
ATOM   461  C  CA  B ARG A 1 58  ? -12.777 5.535   0.802   0.50 13.75 ? 58  ARG A CA  1 
ATOM   462  C  C   A ARG A 1 58  ? -12.561 4.379   1.664   0.50 9.90  ? 58  ARG A C   1 
ATOM   463  C  C   B ARG A 1 58  ? -12.089 4.376   1.546   0.50 13.63 ? 58  ARG A C   1 
ATOM   464  O  O   A ARG A 1 58  ? -12.943 4.289   2.844   0.50 9.03  ? 58  ARG A O   1 
ATOM   465  O  O   B ARG A 1 58  ? -11.966 4.421   2.746   0.50 10.40 ? 58  ARG A O   1 
ATOM   466  C  CB  A ARG A 1 58  ? -11.456 6.292   0.539   0.50 12.81 ? 58  ARG A CB  1 
ATOM   467  C  CB  B ARG A 1 58  ? -11.653 6.556   0.849   0.50 13.24 ? 58  ARG A CB  1 
ATOM   468  C  CG  A ARG A 1 58  ? -11.437 7.342   -0.568  0.50 13.00 ? 58  ARG A CG  1 
ATOM   469  C  CG  B ARG A 1 58  ? -11.419 7.328   -0.431  0.50 11.40 ? 58  ARG A CG  1 
ATOM   470  C  CD  A ARG A 1 58  ? -10.102 8.060   -0.782  0.50 19.16 ? 58  ARG A CD  1 
ATOM   471  C  CD  B ARG A 1 58  ? -9.924  7.179   -0.514  0.50 10.22 ? 58  ARG A CD  1 
ATOM   472  N  NE  A ARG A 1 58  ? -9.234  7.368   -1.731  0.50 17.17 ? 58  ARG A NE  1 
ATOM   473  N  NE  B ARG A 1 58  ? -9.152  7.291   0.708   0.50 8.99  ? 58  ARG A NE  1 
ATOM   474  C  CZ  A ARG A 1 58  ? -9.478  7.271   -3.042  0.50 13.65 ? 58  ARG A CZ  1 
ATOM   475  C  CZ  B ARG A 1 58  ? -7.822  7.398   0.707   0.50 9.95  ? 58  ARG A CZ  1 
ATOM   476  N  NH1 A ARG A 1 58  ? -8.667  6.550   -3.785  0.50 12.46 ? 58  ARG A NH1 1 
ATOM   477  N  NH1 B ARG A 1 58  ? -7.114  7.694   -0.365  0.50 9.18  ? 58  ARG A NH1 1 
ATOM   478  N  NH2 A ARG A 1 58  ? -10.536 7.836   -3.605  0.50 17.54 ? 58  ARG A NH2 1 
ATOM   479  N  NH2 B ARG A 1 58  ? -7.188  7.441   1.857   0.50 9.02  ? 58  ARG A NH2 1 
ATOM   480  N  N   A ILE A 1 59  ? -12.155 3.353   0.970   0.50 13.01 ? 59  ILE A N   1 
ATOM   481  N  N   B ILE A 1 59  ? -11.405 3.491   0.823   0.50 14.91 ? 59  ILE A N   1 
ATOM   482  C  CA  A ILE A 1 59  ? -11.497 2.258   1.647   0.50 11.58 ? 59  ILE A CA  1 
ATOM   483  C  CA  B ILE A 1 59  ? -10.811 2.323   1.443   0.50 15.49 ? 59  ILE A CA  1 
ATOM   484  C  C   A ILE A 1 59  ? -10.071 2.216   1.122   0.50 11.10 ? 59  ILE A C   1 
ATOM   485  C  C   B ILE A 1 59  ? -9.380  2.247   0.934   0.50 15.26 ? 59  ILE A C   1 
ATOM   486  O  O   A ILE A 1 59  ? -9.806  2.410   -0.073  0.50 16.34 ? 59  ILE A O   1 
ATOM   487  O  O   B ILE A 1 59  ? -9.077  2.467   -0.222  0.50 15.64 ? 59  ILE A O   1 
ATOM   488  C  CB  A ILE A 1 59  ? -12.243 0.951   1.359   0.50 11.58 ? 59  ILE A CB  1 
ATOM   489  C  CB  B ILE A 1 59  ? -11.621 1.039   1.196   0.50 14.87 ? 59  ILE A CB  1 
ATOM   490  C  CG1 A ILE A 1 59  ? -11.639 -0.205  2.162   0.50 12.28 ? 59  ILE A CG1 1 
ATOM   491  C  CG1 B ILE A 1 59  ? -11.146 -0.122  2.081   0.50 14.05 ? 59  ILE A CG1 1 
ATOM   492  C  CG2 A ILE A 1 59  ? -12.232 0.616   -0.146  0.50 12.89 ? 59  ILE A CG2 1 
ATOM   493  C  CG2 B ILE A 1 59  ? -11.600 0.606   -0.289  0.50 15.14 ? 59  ILE A CG2 1 
ATOM   494  C  CD1 A ILE A 1 59  ? -12.416 -1.517  1.981   0.50 13.85 ? 59  ILE A CD1 1 
ATOM   495  C  CD1 B ILE A 1 59  ? -12.067 -1.358  2.056   0.50 14.11 ? 59  ILE A CD1 1 
ATOM   496  N  N   A LEU A 1 60  ? -9.120  1.942   2.027   0.50 14.51 ? 60  LEU A N   1 
ATOM   497  N  N   B LEU A 1 60  ? -8.482  1.914   1.839   0.50 14.27 ? 60  LEU A N   1 
ATOM   498  C  CA  A LEU A 1 60  ? -7.714  2.096   1.736   0.50 10.54 ? 60  LEU A CA  1 
ATOM   499  C  CA  B LEU A 1 60  ? -7.067  2.042   1.606   0.50 17.40 ? 60  LEU A CA  1 
ATOM   500  C  C   A LEU A 1 60  ? -6.859  0.940   2.312   0.50 13.48 ? 60  LEU A C   1 
ATOM   501  C  C   B LEU A 1 60  ? -6.319  0.838   2.187   0.50 16.67 ? 60  LEU A C   1 
ATOM   502  O  O   A LEU A 1 60  ? -7.066  0.546   3.444   0.50 13.39 ? 60  LEU A O   1 
ATOM   503  O  O   B LEU A 1 60  ? -6.583  0.439   3.317   0.50 16.57 ? 60  LEU A O   1 
ATOM   504  C  CB  A LEU A 1 60  ? -7.293  3.385   2.451   0.50 12.73 ? 60  LEU A CB  1 
ATOM   505  C  CB  B LEU A 1 60  ? -6.704  3.316   2.369   0.50 19.31 ? 60  LEU A CB  1 
ATOM   506  C  CG  A LEU A 1 60  ? -5.784  3.550   2.537   0.50 11.06 ? 60  LEU A CG  1 
ATOM   507  C  CG  B LEU A 1 60  ? -5.239  3.618   2.361   0.50 15.70 ? 60  LEU A CG  1 
ATOM   508  C  CD1 A LEU A 1 60  ? -5.277  3.688   1.114   0.50 18.07 ? 60  LEU A CD1 1 
ATOM   509  C  CD1 B LEU A 1 60  ? -4.897  3.989   0.930   0.50 16.34 ? 60  LEU A CD1 1 
ATOM   510  C  CD2 A LEU A 1 60  ? -5.337  4.716   3.431   0.50 13.84 ? 60  LEU A CD2 1 
ATOM   511  C  CD2 B LEU A 1 60  ? -4.905  4.777   3.294   0.50 15.43 ? 60  LEU A CD2 1 
ATOM   512  N  N   A ASN A 1 61  ? -5.861  0.423   1.545   0.50 15.39 ? 61  ASN A N   1 
ATOM   513  N  N   B ASN A 1 61  ? -5.432  0.249   1.366   0.50 15.78 ? 61  ASN A N   1 
ATOM   514  C  CA  A ASN A 1 61  ? -4.848  -0.537  2.003   0.50 15.62 ? 61  ASN A CA  1 
ATOM   515  C  CA  B ASN A 1 61  ? -4.486  -0.754  1.831   0.50 16.07 ? 61  ASN A CA  1 
ATOM   516  C  C   A ASN A 1 61  ? -3.539  0.232   2.243   0.50 16.45 ? 61  ASN A C   1 
ATOM   517  C  C   B ASN A 1 61  ? -3.212  -0.003  2.186   0.50 17.90 ? 61  ASN A C   1 
ATOM   518  O  O   A ASN A 1 61  ? -3.060  0.857   1.296   0.50 15.74 ? 61  ASN A O   1 
ATOM   519  O  O   B ASN A 1 61  ? -2.506  0.481   1.310   0.50 18.28 ? 61  ASN A O   1 
ATOM   520  C  CB  A ASN A 1 61  ? -4.607  -1.623  0.923   0.50 16.85 ? 61  ASN A CB  1 
ATOM   521  C  CB  B ASN A 1 61  ? -4.195  -1.788  0.734   0.50 18.35 ? 61  ASN A CB  1 
ATOM   522  C  CG  A ASN A 1 61  ? -3.461  -2.574  1.235   0.50 16.56 ? 61  ASN A CG  1 
ATOM   523  C  CG  B ASN A 1 61  ? -3.178  -2.813  1.181   0.50 21.56 ? 61  ASN A CG  1 
ATOM   524  O  OD1 A ASN A 1 61  ? -2.525  -2.262  1.995   0.50 18.77 ? 61  ASN A OD1 1 
ATOM   525  O  OD1 B ASN A 1 61  ? -2.300  -2.504  2.026   0.50 18.72 ? 61  ASN A OD1 1 
ATOM   526  N  ND2 A ASN A 1 61  ? -3.582  -3.875  0.740   0.50 18.37 ? 61  ASN A ND2 1 
ATOM   527  N  ND2 B ASN A 1 61  ? -3.360  -4.092  0.726   0.50 19.15 ? 61  ASN A ND2 1 
ATOM   528  N  N   . ASN A 1 62  ? -2.972  0.211   3.473   1.00 16.11 ? 62  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 62  ? -1.797  1.006   3.831   1.00 18.43 ? 62  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 62  ? -0.549  0.146   4.063   1.00 17.68 ? 62  ASN A C   1 
ATOM   531  O  O   . ASN A 1 62  ? 0.541   0.571   4.545   1.00 22.77 ? 62  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 62  ? -1.987  1.907   5.045   1.00 16.62 ? 62  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 62  ? -1.966  1.103   6.317   1.00 16.08 ? 62  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 62  ? -2.118  -0.103  6.349   1.00 15.03 ? 62  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 62  ? -1.708  1.791   7.403   1.00 23.57 ? 62  ASN A ND2 1 
ATOM   536  N  N   . GLY A 1 63  ? -0.689  -1.125  3.724   1.00 15.63 ? 63  GLY A N   1 
ATOM   537  C  CA  . GLY A 1 63  ? 0.442   -2.008  3.856   1.00 16.26 ? 63  GLY A CA  1 
ATOM   538  C  C   . GLY A 1 63  ? 0.549   -2.691  5.220   1.00 15.74 ? 63  GLY A C   1 
ATOM   539  O  O   . GLY A 1 63  ? 1.369   -3.587  5.378   1.00 17.48 ? 63  GLY A O   1 
ATOM   540  N  N   . HIS A 1 64  ? -0.323  -2.345  6.150   1.00 13.61 ? 64  HIS A N   1 
ATOM   541  C  CA  . HIS A 1 64  ? -0.410  -3.022  7.454   1.00 13.35 ? 64  HIS A CA  1 
ATOM   542  C  C   . HIS A 1 64  ? -1.818  -3.566  7.725   1.00 11.29 ? 64  HIS A C   1 
ATOM   543  O  O   . HIS A 1 64  ? -1.954  -4.561  8.412   1.00 16.43 ? 64  HIS A O   1 
ATOM   544  C  CB  . HIS A 1 64  ? -0.080  -2.005  8.588   1.00 13.54 ? 64  HIS A CB  1 
ATOM   545  C  CG  . HIS A 1 64  ? 1.233   -1.310  8.388   1.00 16.71 ? 64  HIS A CG  1 
ATOM   546  N  ND1 . HIS A 1 64  ? 2.445   -1.991  8.532   1.00 18.74 ? 64  HIS A ND1 1 
ATOM   547  C  CD2 . HIS A 1 64  ? 1.554   -0.017  8.147   1.00 17.51 ? 64  HIS A CD2 1 
ATOM   548  C  CE1 . HIS A 1 64  ? 3.486   -1.166  8.353   1.00 18.59 ? 64  HIS A CE1 1 
ATOM   549  N  NE2 . HIS A 1 64  ? 2.940   0.068   8.041   1.00 20.26 ? 64  HIS A NE2 1 
ATOM   550  N  N   . SER A 1 65  ? -2.837  -2.909  7.214   1.00 11.37 ? 65  SER A N   1 
ATOM   551  C  CA  . SER A 1 65  ? -4.229  -3.303  7.336   1.00 10.95 ? 65  SER A CA  1 
ATOM   552  C  C   . SER A 1 65  ? -4.913  -2.618  6.154   1.00 11.55 ? 65  SER A C   1 
ATOM   553  O  O   . SER A 1 65  ? -4.249  -1.994  5.330   1.00 14.80 ? 65  SER A O   1 
ATOM   554  C  CB  . SER A 1 65  ? -4.789  -2.818  8.687   1.00 11.97 ? 65  SER A CB  1 
ATOM   555  O  OG  . SER A 1 65  ? -6.147  -3.177  8.860   1.00 15.29 ? 65  SER A OG  1 
ATOM   556  N  N   . PHE A 1 66  ? -6.236  -2.697  6.137   1.00 11.58 ? 66  PHE A N   1 
ATOM   557  C  CA  . PHE A 1 66  ? -7.044  -1.798  5.326   1.00 12.11 ? 66  PHE A CA  1 
ATOM   558  C  C   . PHE A 1 66  ? -8.019  -1.016  6.213   1.00 12.56 ? 66  PHE A C   1 
ATOM   559  O  O   . PHE A 1 66  ? -8.439  -1.534  7.251   1.00 12.53 ? 66  PHE A O   1 
ATOM   560  C  CB  . PHE A 1 66  ? -7.726  -2.569  4.179   1.00 13.89 ? 66  PHE A CB  1 
ATOM   561  C  CG  . PHE A 1 66  ? -8.869  -3.429  4.663   1.00 11.81 ? 66  PHE A CG  1 
ATOM   562  C  CD1 . PHE A 1 66  ? -10.144 -2.910  4.815   1.00 11.44 ? 66  PHE A CD1 1 
ATOM   563  C  CD2 . PHE A 1 66  ? -8.689  -4.764  5.014   1.00 12.37 ? 66  PHE A CD2 1 
ATOM   564  C  CE1 . PHE A 1 66  ? -11.204 -3.687  5.275   1.00 12.21 ? 66  PHE A CE1 1 
ATOM   565  C  CE2 . PHE A 1 66  ? -9.740  -5.568  5.450   1.00 12.25 ? 66  PHE A CE2 1 
ATOM   566  C  CZ  . PHE A 1 66  ? -11.010 -5.030  5.561   1.00 12.16 ? 66  PHE A CZ  1 
ATOM   567  N  N   A LYS A 1 67  ? -8.398  0.186   5.763   0.50 13.95 ? 67  LYS A N   1 
ATOM   568  N  N   B LYS A 1 67  ? -8.401  0.223   5.846   0.50 13.24 ? 67  LYS A N   1 
ATOM   569  C  CA  A LYS A 1 67  ? -9.251  1.042   6.579   0.50 15.71 ? 67  LYS A CA  1 
ATOM   570  C  CA  B LYS A 1 67  ? -9.430  0.928   6.603   0.50 13.37 ? 67  LYS A CA  1 
ATOM   571  C  C   A LYS A 1 67  ? -10.316 1.686   5.693   0.50 14.40 ? 67  LYS A C   1 
ATOM   572  C  C   B LYS A 1 67  ? -10.460 1.527   5.668   0.50 11.20 ? 67  LYS A C   1 
ATOM   573  O  O   A LYS A 1 67  ? -9.997  2.163   4.576   0.50 19.01 ? 67  LYS A O   1 
ATOM   574  O  O   B LYS A 1 67  ? -10.223 1.890   4.487   0.50 13.01 ? 67  LYS A O   1 
ATOM   575  C  CB  A LYS A 1 67  ? -8.430  2.053   7.385   0.50 21.58 ? 67  LYS A CB  1 
ATOM   576  C  CB  B LYS A 1 67  ? -8.998  2.141   7.432   0.50 10.06 ? 67  LYS A CB  1 
ATOM   577  C  CG  A LYS A 1 67  ? -8.044  3.361   6.716   0.50 17.76 ? 67  LYS A CG  1 
ATOM   578  C  CG  B LYS A 1 67  ? -7.838  2.906   6.880   0.50 16.28 ? 67  LYS A CG  1 
ATOM   579  C  CD  A LYS A 1 67  ? -7.519  4.342   7.795   0.50 18.68 ? 67  LYS A CD  1 
ATOM   580  C  CD  B LYS A 1 67  ? -7.417  4.086   7.795   0.50 13.56 ? 67  LYS A CD  1 
ATOM   581  C  CE  A LYS A 1 67  ? -6.354  5.234   7.388   0.50 25.99 ? 67  LYS A CE  1 
ATOM   582  C  CE  B LYS A 1 67  ? -6.455  5.037   7.110   0.50 12.52 ? 67  LYS A CE  1 
ATOM   583  N  NZ  A LYS A 1 67  ? -6.807  6.598   6.964   0.50 38.53 ? 67  LYS A NZ  1 
ATOM   584  N  NZ  B LYS A 1 67  ? -7.112  6.247   6.530   0.50 11.25 ? 67  LYS A NZ  1 
ATOM   585  N  N   A VAL A 1 68  ? -11.563 1.604   6.174   0.50 17.16 ? 68  VAL A N   1 
ATOM   586  N  N   B VAL A 1 68  ? -11.612 1.671   6.256   0.50 15.22 ? 68  VAL A N   1 
ATOM   587  C  CA  A VAL A 1 68  ? -12.745 2.264   5.623   0.50 14.36 ? 68  VAL A CA  1 
ATOM   588  C  CA  B VAL A 1 68  ? -12.564 2.500   5.594   0.50 16.62 ? 68  VAL A CA  1 
ATOM   589  C  C   A VAL A 1 68  ? -12.916 3.623   6.297   0.50 15.49 ? 68  VAL A C   1 
ATOM   590  C  C   B VAL A 1 68  ? -12.468 3.826   6.347   0.50 16.70 ? 68  VAL A C   1 
ATOM   591  O  O   A VAL A 1 68  ? -13.112 3.712   7.512   0.50 15.22 ? 68  VAL A O   1 
ATOM   592  O  O   B VAL A 1 68  ? -12.471 3.841   7.564   0.50 16.40 ? 68  VAL A O   1 
ATOM   593  C  CB  A VAL A 1 68  ? -14.078 1.502   5.768   0.50 16.12 ? 68  VAL A CB  1 
ATOM   594  C  CB  B VAL A 1 68  ? -13.915 1.782   5.673   0.50 18.33 ? 68  VAL A CB  1 
ATOM   595  C  CG1 A VAL A 1 68  ? -15.251 2.443   5.324   0.50 18.65 ? 68  VAL A CG1 1 
ATOM   596  C  CG1 B VAL A 1 68  ? -15.058 2.646   5.112   0.50 20.43 ? 68  VAL A CG1 1 
ATOM   597  C  CG2 A VAL A 1 68  ? -14.090 0.200   4.940   0.50 16.79 ? 68  VAL A CG2 1 
ATOM   598  C  CG2 B VAL A 1 68  ? -13.842 0.396   5.012   0.50 16.93 ? 68  VAL A CG2 1 
ATOM   599  N  N   A GLU A 1 69  ? -12.911 4.683   5.483   0.50 16.97 ? 69  GLU A N   1 
ATOM   600  N  N   B GLU A 1 69  ? -12.280 4.935   5.625   0.50 16.50 ? 69  GLU A N   1 
ATOM   601  C  CA  A GLU A 1 69  ? -12.802 6.030   6.022   0.50 13.89 ? 69  GLU A CA  1 
ATOM   602  C  CA  B GLU A 1 69  ? -12.297 6.236   6.293   0.50 14.92 ? 69  GLU A CA  1 
ATOM   603  C  C   A GLU A 1 69  ? -14.121 6.768   6.023   0.50 15.13 ? 69  GLU A C   1 
ATOM   604  C  C   B GLU A 1 69  ? -13.576 6.991   5.960   0.50 16.93 ? 69  GLU A C   1 
ATOM   605  O  O   A GLU A 1 69  ? -14.969 6.590   5.098   0.50 14.86 ? 69  GLU A O   1 
ATOM   606  O  O   B GLU A 1 69  ? -13.935 6.933   4.767   0.50 24.30 ? 69  GLU A O   1 
ATOM   607  C  CB  A GLU A 1 69  ? -11.945 6.925   5.163   0.50 11.27 ? 69  GLU A CB  1 
ATOM   608  C  CB  B GLU A 1 69  ? -11.212 7.086   5.663   0.50 17.88 ? 69  GLU A CB  1 
ATOM   609  C  CG  A GLU A 1 69  ? -10.561 6.549   5.333   0.50 14.95 ? 69  GLU A CG  1 
ATOM   610  C  CG  B GLU A 1 69  ? -9.922  6.324   5.687   0.50 18.67 ? 69  GLU A CG  1 
ATOM   611  C  CD  A GLU A 1 69  ? -9.691  6.761   4.153   0.50 17.36 ? 69  GLU A CD  1 
ATOM   612  C  CD  B GLU A 1 69  ? -9.193  6.876   4.525   0.50 18.80 ? 69  GLU A CD  1 
ATOM   613  O  OE1 A GLU A 1 69  ? -8.536  6.251   4.240   0.50 16.61 ? 69  GLU A OE1 1 
ATOM   614  O  OE1 B GLU A 1 69  ? -9.941  7.438   3.619   0.50 18.08 ? 69  GLU A OE1 1 
ATOM   615  O  OE2 A GLU A 1 69  ? -10.161 7.425   3.167   0.50 17.37 ? 69  GLU A OE2 1 
ATOM   616  O  OE2 B GLU A 1 69  ? -7.902  6.817   4.549   0.50 25.25 ? 69  GLU A OE2 1 
ATOM   617  N  N   . PHE A 1 70  ? -14.137 7.721   6.941   1.00 16.11 ? 70  PHE A N   1 
ATOM   618  C  CA  . PHE A 1 70  ? -15.391 8.446   7.002   1.00 15.57 ? 70  PHE A CA  1 
ATOM   619  C  C   . PHE A 1 70  ? -15.145 9.924   6.887   1.00 14.67 ? 70  PHE A C   1 
ATOM   620  O  O   . PHE A 1 70  ? -14.095 10.446  7.258   1.00 16.08 ? 70  PHE A O   1 
ATOM   621  C  CB  . PHE A 1 70  ? -16.133 8.136   8.311   1.00 14.62 ? 70  PHE A CB  1 
ATOM   622  C  CG  . PHE A 1 70  ? -16.666 6.722   8.276   1.00 15.06 ? 70  PHE A CG  1 
ATOM   623  C  CD1 . PHE A 1 70  ? -15.878 5.620   8.587   1.00 16.10 ? 70  PHE A CD1 1 
ATOM   624  C  CD2 . PHE A 1 70  ? -17.979 6.463   7.939   1.00 14.15 ? 70  PHE A CD2 1 
ATOM   625  C  CE1 . PHE A 1 70  ? -16.416 4.333   8.441   1.00 15.71 ? 70  PHE A CE1 1 
ATOM   626  C  CE2 . PHE A 1 70  ? -18.524 5.185   7.848   1.00 14.99 ? 70  PHE A CE2 1 
ATOM   627  C  CZ  . PHE A 1 70  ? -17.730 4.117   8.112   1.00 15.23 ? 70  PHE A CZ  1 
ATOM   628  N  N   A ASP A 1 71  ? -16.161 10.640  6.404   0.50 15.91 ? 71  ASP A N   1 
ATOM   629  N  N   B ASP A 1 71  ? -16.127 10.628  6.320   0.50 16.12 ? 71  ASP A N   1 
ATOM   630  C  CA  A ASP A 1 71  ? -16.131 12.092  6.459   0.50 14.37 ? 71  ASP A CA  1 
ATOM   631  C  CA  B ASP A 1 71  ? -16.187 12.072  6.467   0.50 15.57 ? 71  ASP A CA  1 
ATOM   632  C  C   A ASP A 1 71  ? -16.486 12.538  7.880   0.50 13.71 ? 71  ASP A C   1 
ATOM   633  C  C   B ASP A 1 71  ? -16.451 12.383  7.939   0.50 14.14 ? 71  ASP A C   1 
ATOM   634  O  O   A ASP A 1 71  ? -17.656 12.590  8.257   0.50 19.46 ? 71  ASP A O   1 
ATOM   635  O  O   B ASP A 1 71  ? -17.547 12.145  8.433   0.50 19.77 ? 71  ASP A O   1 
ATOM   636  C  CB  A ASP A 1 71  ? -17.057 12.666  5.386   0.50 17.97 ? 71  ASP A CB  1 
ATOM   637  C  CB  B ASP A 1 71  ? -17.371 12.626  5.673   0.50 20.17 ? 71  ASP A CB  1 
ATOM   638  C  CG  A ASP A 1 71  ? -17.078 14.185  5.378   0.50 18.24 ? 71  ASP A CG  1 
ATOM   639  C  CG  B ASP A 1 71  ? -17.531 14.127  5.857   0.50 24.38 ? 71  ASP A CG  1 
ATOM   640  O  OD1 A ASP A 1 71  ? -16.633 14.776  6.415   0.50 15.24 ? 71  ASP A OD1 1 
ATOM   641  O  OD1 B ASP A 1 71  ? -16.493 14.780  6.167   0.50 24.18 ? 71  ASP A OD1 1 
ATOM   642  O  OD2 A ASP A 1 71  ? -17.604 14.768  4.371   0.50 19.47 ? 71  ASP A OD2 1 
ATOM   643  O  OD2 B ASP A 1 71  ? -18.678 14.655  5.643   0.50 21.92 ? 71  ASP A OD2 1 
ATOM   644  N  N   . ASP A 1 72  ? -15.448 12.939  8.614   1.00 12.90 ? 72  ASP A N   1 
ATOM   645  C  CA  . ASP A 1 72  ? -15.599 13.327  10.008  1.00 12.40 ? 72  ASP A CA  1 
ATOM   646  C  C   . ASP A 1 72  ? -15.482 14.845  10.159  1.00 13.09 ? 72  ASP A C   1 
ATOM   647  O  O   . ASP A 1 72  ? -15.030 15.327  11.198  1.00 14.84 ? 72  ASP A O   1 
ATOM   648  C  CB  . ASP A 1 72  ? -14.593 12.615  10.898  1.00 12.36 ? 72  ASP A CB  1 
ATOM   649  C  CG  . ASP A 1 72  ? -13.161 12.906  10.512  1.00 12.02 ? 72  ASP A CG  1 
ATOM   650  O  OD1 . ASP A 1 72  ? -12.909 13.652  9.477   1.00 15.04 ? 72  ASP A OD1 1 
ATOM   651  O  OD2 . ASP A 1 72  ? -12.270 12.443  11.244  1.00 13.19 ? 72  ASP A OD2 1 
ATOM   652  N  N   . SER A 1 73  ? -15.859 15.597  9.123   1.00 14.80 ? 73  SER A N   1 
ATOM   653  C  CA  . SER A 1 73  ? -15.841 17.066  9.166   1.00 15.65 ? 73  SER A CA  1 
ATOM   654  C  C   . SER A 1 73  ? -17.103 17.644  9.825   1.00 16.17 ? 73  SER A C   1 
ATOM   655  O  O   . SER A 1 73  ? -17.175 18.858  9.981   1.00 15.51 ? 73  SER A O   1 
ATOM   656  C  CB  . SER A 1 73  ? -15.626 17.586  7.774   1.00 20.13 ? 73  SER A CB  1 
ATOM   657  O  OG  . SER A 1 73  ? -16.785 17.420  6.969   1.00 18.70 ? 73  SER A OG  1 
ATOM   658  N  N   . GLN A 1 74  ? -18.117 16.850  10.139  1.00 16.66 ? 74  GLN A N   1 
ATOM   659  C  CA  . GLN A 1 74  ? -19.401 17.270  10.722  1.00 19.84 ? 74  GLN A CA  1 
ATOM   660  C  C   . GLN A 1 74  ? -19.698 16.284  11.830  1.00 15.87 ? 74  GLN A C   1 
ATOM   661  O  O   . GLN A 1 74  ? -19.172 15.158  11.831  1.00 16.54 ? 74  GLN A O   1 
ATOM   662  C  CB  . GLN A 1 74  ? -20.563 17.288  9.687   1.00 22.15 ? 74  GLN A CB  1 
ATOM   663  C  CG  . GLN A 1 74  ? -20.455 18.351  8.601   1.00 26.81 ? 74  GLN A CG  1 
ATOM   664  C  CD  . GLN A 1 74  ? -21.425 18.145  7.451   1.00 29.87 ? 74  GLN A CD  1 
ATOM   665  O  OE1 . GLN A 1 74  ? -22.590 17.862  7.652   1.00 40.25 ? 74  GLN A OE1 1 
ATOM   666  N  NE2 . GLN A 1 74  ? -20.940 18.292  6.228   1.00 42.64 ? 74  GLN A NE2 1 
ATOM   667  N  N   . ASP A 1 75  ? -20.597 16.721  12.708  1.00 22.09 ? 75  ASP A N   1 
ATOM   668  C  CA  . ASP A 1 75  ? -21.128 15.981  13.816  1.00 20.71 ? 75  ASP A CA  1 
ATOM   669  C  C   . ASP A 1 75  ? -22.049 14.877  13.262  1.00 20.71 ? 75  ASP A C   1 
ATOM   670  O  O   . ASP A 1 75  ? -23.249 15.076  13.123  1.00 26.76 ? 75  ASP A O   1 
ATOM   671  C  CB  . ASP A 1 75  ? -21.841 17.023  14.704  1.00 21.97 ? 75  ASP A CB  1 
ATOM   672  C  CG  . ASP A 1 75  ? -22.452 16.384  15.934  1.00 32.71 ? 75  ASP A CG  1 
ATOM   673  O  OD1 . ASP A 1 75  ? -22.115 15.215  16.158  1.00 30.54 ? 75  ASP A OD1 1 
ATOM   674  O  OD2 . ASP A 1 75  ? -23.266 17.053  16.650  1.00 39.12 ? 75  ASP A OD2 1 
ATOM   675  N  N   . LYS A 1 76  ? -21.509 13.713  12.895  1.00 19.33 ? 76  LYS A N   1 
ATOM   676  C  CA  . LYS A 1 76  ? -22.279 12.644  12.259  1.00 22.87 ? 76  LYS A CA  1 
ATOM   677  C  C   . LYS A 1 76  ? -22.349 11.393  13.150  1.00 35.44 ? 76  LYS A C   1 
ATOM   678  O  O   . LYS A 1 76  ? -23.112 11.335  14.112  1.00 54.93 ? 76  LYS A O   1 
ATOM   679  C  CB  . LYS A 1 76  ? -21.849 12.382  10.796  1.00 20.66 ? 76  LYS A CB  1 
ATOM   680  C  CG  . LYS A 1 76  ? -22.269 13.461  9.791   1.00 28.06 ? 76  LYS A CG  1 
ATOM   681  C  CD  . LYS A 1 76  ? -21.705 13.233  8.383   1.00 33.64 ? 76  LYS A CD  1 
ATOM   682  C  CE  . LYS A 1 76  ? -22.149 14.214  7.299   1.00 36.74 ? 76  LYS A CE  1 
ATOM   683  N  NZ  . LYS A 1 76  ? -21.550 13.947  5.969   1.00 37.17 ? 76  LYS A NZ  1 
ATOM   684  N  N   . ALA A 1 77  ? -21.583 10.381  12.797  1.00 25.93 ? 77  ALA A N   1 
ATOM   685  C  CA  . ALA A 1 77  ? -21.411 9.069   13.473  1.00 18.94 ? 77  ALA A CA  1 
ATOM   686  C  C   . ALA A 1 77  ? -20.563 9.263   14.736  1.00 14.43 ? 77  ALA A C   1 
ATOM   687  O  O   . ALA A 1 77  ? -19.373 9.456   14.691  1.00 24.48 ? 77  ALA A O   1 
ATOM   688  C  CB  . ALA A 1 77  ? -20.776 8.081   12.526  1.00 21.08 ? 77  ALA A CB  1 
ATOM   689  N  N   . VAL A 1 78  ? -21.190 9.223   15.870  1.00 14.57 ? 78  VAL A N   1 
ATOM   690  C  CA  . VAL A 1 78  ? -20.540 9.532   17.117  1.00 15.64 ? 78  VAL A CA  1 
ATOM   691  C  C   . VAL A 1 78  ? -20.758 8.430   18.151  1.00 14.51 ? 78  VAL A C   1 
ATOM   692  O  O   . VAL A 1 78  ? -21.752 7.712   18.162  1.00 15.81 ? 78  VAL A O   1 
ATOM   693  C  CB  . VAL A 1 78  ? -20.967 10.889  17.672  1.00 22.91 ? 78  VAL A CB  1 
ATOM   694  C  CG1 . VAL A 1 78  ? -20.820 12.049  16.724  1.00 26.69 ? 78  VAL A CG1 1 
ATOM   695  C  CG2 . VAL A 1 78  ? -22.354 10.832  18.167  1.00 24.28 ? 78  VAL A CG2 1 
ATOM   696  N  N   . LEU A 1 79  ? -19.730 8.284   18.967  1.00 12.74 ? 79  LEU A N   1 
ATOM   697  C  CA  . LEU A 1 79  ? -19.719 7.442   20.132  1.00 12.04 ? 79  LEU A CA  1 
ATOM   698  C  C   . LEU A 1 79  ? -19.728 8.301   21.374  1.00 11.71 ? 79  LEU A C   1 
ATOM   699  O  O   . LEU A 1 79  ? -18.878 9.211   21.479  1.00 13.52 ? 79  LEU A O   1 
ATOM   700  C  CB  . LEU A 1 79  ? -18.471 6.550   20.003  1.00 12.77 ? 79  LEU A CB  1 
ATOM   701  C  CG  . LEU A 1 79  ? -18.281 5.513   21.094  1.00 13.26 ? 79  LEU A CG  1 
ATOM   702  C  CD1 . LEU A 1 79  ? -19.349 4.429   21.023  1.00 17.39 ? 79  LEU A CD1 1 
ATOM   703  C  CD2 . LEU A 1 79  ? -16.915 4.913   20.960  1.00 13.40 ? 79  LEU A CD2 1 
ATOM   704  N  N   . LYS A 1 80  ? -20.601 7.956   22.317  1.00 13.49 ? 80  LYS A N   1 
ATOM   705  C  CA  . LYS A 1 80  ? -20.574 8.651   23.605  1.00 14.25 ? 80  LYS A CA  1 
ATOM   706  C  C   . LYS A 1 80  ? -21.072 7.724   24.690  1.00 14.33 ? 80  LYS A C   1 
ATOM   707  O  O   . LYS A 1 80  ? -21.398 6.595   24.376  1.00 14.57 ? 80  LYS A O   1 
ATOM   708  C  CB  . LYS A 1 80  ? -21.334 9.968   23.554  1.00 18.39 ? 80  LYS A CB  1 
ATOM   709  C  CG  . LYS A 1 80  ? -22.776 9.807   23.191  1.00 23.51 ? 80  LYS A CG  1 
ATOM   710  C  CD  . LYS A 1 80  ? -23.375 11.205  23.161  1.00 30.53 ? 80  LYS A CD  1 
ATOM   711  C  CE  . LYS A 1 80  ? -24.266 11.494  24.350  1.00 39.54 ? 80  LYS A CE  1 
ATOM   712  N  NZ  . LYS A 1 80  ? -25.066 12.741  24.233  1.00 54.83 ? 80  LYS A NZ  1 
ATOM   713  N  N   . GLY A 1 81  ? -21.130 8.252   25.914  1.00 15.13 ? 81  GLY A N   1 
ATOM   714  C  CA  . GLY A 1 81  ? -21.543 7.449   27.041  1.00 16.66 ? 81  GLY A CA  1 
ATOM   715  C  C   . GLY A 1 81  ? -20.515 6.404   27.438  1.00 17.99 ? 81  GLY A C   1 
ATOM   716  O  O   . GLY A 1 81  ? -19.332 6.568   27.141  1.00 16.18 ? 81  GLY A O   1 
ATOM   717  N  N   . GLY A 1 82  ? -20.981 5.304   28.036  1.00 21.40 ? 82  GLY A N   1 
ATOM   718  C  CA  . GLY A 1 82  ? -20.054 4.331   28.555  1.00 27.01 ? 82  GLY A CA  1 
ATOM   719  C  C   . GLY A 1 82  ? -19.093 4.996   29.518  1.00 20.73 ? 82  GLY A C   1 
ATOM   720  O  O   . GLY A 1 82  ? -19.439 5.819   30.374  1.00 26.50 ? 82  GLY A O   1 
ATOM   721  N  N   . PRO A 1 83  ? -17.794 4.752   29.282  1.00 18.75 ? 83  PRO A N   1 
ATOM   722  C  CA  . PRO A 1 83  ? -16.763 5.376   30.096  1.00 19.07 ? 83  PRO A CA  1 
ATOM   723  C  C   . PRO A 1 83  ? -16.392 6.784   29.622  1.00 17.76 ? 83  PRO A C   1 
ATOM   724  O  O   . PRO A 1 83  ? -15.568 7.401   30.268  1.00 22.69 ? 83  PRO A O   1 
ATOM   725  C  CB  . PRO A 1 83  ? -15.551 4.443   29.927  1.00 18.82 ? 83  PRO A CB  1 
ATOM   726  C  CG  . PRO A 1 83  ? -15.757 3.967   28.497  1.00 15.57 ? 83  PRO A CG  1 
ATOM   727  C  CD  . PRO A 1 83  ? -17.259 3.888   28.208  1.00 15.84 ? 83  PRO A CD  1 
ATOM   728  N  N   . LEU A 1 84  ? -16.977 7.241   28.503  1.00 15.31 ? 84  LEU A N   1 
ATOM   729  C  CA  . LEU A 1 84  ? -16.460 8.432   27.860  1.00 14.29 ? 84  LEU A CA  1 
ATOM   730  C  C   . LEU A 1 84  ? -17.058 9.688   28.477  1.00 14.38 ? 84  LEU A C   1 
ATOM   731  O  O   . LEU A 1 84  ? -18.267 9.723   28.775  1.00 18.10 ? 84  LEU A O   1 
ATOM   732  C  CB  . LEU A 1 84  ? -16.809 8.356   26.379  1.00 12.24 ? 84  LEU A CB  1 
ATOM   733  C  CG  . LEU A 1 84  ? -16.227 7.123   25.678  1.00 11.66 ? 84  LEU A CG  1 
ATOM   734  C  CD1 . LEU A 1 84  ? -16.764 7.067   24.247  1.00 12.91 ? 84  LEU A CD1 1 
ATOM   735  C  CD2 . LEU A 1 84  ? -14.704 7.126   25.753  1.00 12.65 ? 84  LEU A CD2 1 
ATOM   736  N  N   . ASP A 1 85  ? -16.231 10.748  28.517  1.00 17.35 ? 85  ASP A N   1 
ATOM   737  C  CA  . ASP A 1 85  ? -16.755 12.080  28.819  1.00 18.43 ? 85  ASP A CA  1 
ATOM   738  C  C   . ASP A 1 85  ? -16.747 12.778  27.458  1.00 18.41 ? 85  ASP A C   1 
ATOM   739  O  O   . ASP A 1 85  ? -15.760 12.799  26.728  1.00 22.59 ? 85  ASP A O   1 
ATOM   740  C  CB  . ASP A 1 85  ? -15.896 12.828  29.852  1.00 21.50 ? 85  ASP A CB  1 
ATOM   741  C  CG  . ASP A 1 85  ? -16.013 12.318  31.300  1.00 28.86 ? 85  ASP A CG  1 
ATOM   742  O  OD1 . ASP A 1 85  ? -17.136 11.863  31.735  1.00 40.02 ? 85  ASP A OD1 1 
ATOM   743  O  OD2 . ASP A 1 85  ? -14.971 12.423  32.028  1.00 40.91 ? 85  ASP A OD2 1 
ATOM   744  N  N   . GLY A 1 86  ? -17.856 13.381  27.109  1.00 23.82 ? 86  GLY A N   1 
ATOM   745  C  CA  . GLY A 1 86  ? -17.933 14.071  25.838  1.00 19.71 ? 86  GLY A CA  1 
ATOM   746  C  C   . GLY A 1 86  ? -18.264 13.162  24.634  1.00 18.77 ? 86  GLY A C   1 
ATOM   747  O  O   . GLY A 1 86  ? -18.802 12.085  24.759  1.00 25.84 ? 86  GLY A O   1 
ATOM   748  N  N   A THR A 1 87  ? -18.061 13.697  23.411  0.50 16.37 ? 87  THR A N   1 
ATOM   749  N  N   B THR A 1 87  ? -17.897 13.622  23.455  0.50 13.96 ? 87  THR A N   1 
ATOM   750  C  CA  A THR A 1 87  ? -18.458 13.147  22.109  0.50 17.30 ? 87  THR A CA  1 
ATOM   751  C  CA  B THR A 1 87  ? -18.368 12.961  22.262  0.50 13.48 ? 87  THR A CA  1 
ATOM   752  C  C   A THR A 1 87  ? -17.213 12.740  21.320  0.50 13.64 ? 87  THR A C   1 
ATOM   753  C  C   B THR A 1 87  ? -17.171 12.690  21.383  0.50 11.30 ? 87  THR A C   1 
ATOM   754  O  O   A THR A 1 87  ? -16.253 13.527  21.173  0.50 13.70 ? 87  THR A O   1 
ATOM   755  O  O   B THR A 1 87  ? -16.249 13.521  21.233  0.50 12.16 ? 87  THR A O   1 
ATOM   756  C  CB  A THR A 1 87  ? -19.194 14.185  21.234  0.50 20.78 ? 87  THR A CB  1 
ATOM   757  C  CB  B THR A 1 87  ? -19.392 13.836  21.562  0.50 12.45 ? 87  THR A CB  1 
ATOM   758  O  OG1 A THR A 1 87  ? -20.301 14.779  21.923  0.50 25.38 ? 87  THR A OG1 1 
ATOM   759  O  OG1 B THR A 1 87  ? -18.787 15.120  21.412  0.50 13.04 ? 87  THR A OG1 1 
ATOM   760  C  CG2 A THR A 1 87  ? -19.753 13.598  19.947  0.50 21.57 ? 87  THR A CG2 1 
ATOM   761  C  CG2 B THR A 1 87  ? -20.633 13.953  22.409  0.50 14.15 ? 87  THR A CG2 1 
ATOM   762  N  N   . TYR A 1 88  ? -17.229 11.519  20.766  1.00 11.16 ? 88  TYR A N   1 
ATOM   763  C  CA  . TYR A 1 88  ? -16.120 11.037  19.967  1.00 9.45  ? 88  TYR A CA  1 
ATOM   764  C  C   . TYR A 1 88  ? -16.659 10.711  18.591  1.00 11.40 ? 88  TYR A C   1 
ATOM   765  O  O   . TYR A 1 88  ? -17.644 10.030  18.430  1.00 14.74 ? 88  TYR A O   1 
ATOM   766  C  CB  . TYR A 1 88  ? -15.519 9.811   20.600  1.00 10.28 ? 88  TYR A CB  1 
ATOM   767  C  CG  . TYR A 1 88  ? -14.704 10.029  21.845  1.00 8.65  ? 88  TYR A CG  1 
ATOM   768  C  CD1 . TYR A 1 88  ? -15.265 10.427  23.049  1.00 10.14 ? 88  TYR A CD1 1 
ATOM   769  C  CD2 . TYR A 1 88  ? -13.329 9.796   21.812  1.00 8.66  ? 88  TYR A CD2 1 
ATOM   770  C  CE1 . TYR A 1 88  ? -14.508 10.648  24.182  1.00 10.45 ? 88  TYR A CE1 1 
ATOM   771  C  CE2 . TYR A 1 88  ? -12.547 9.944   22.945  1.00 8.13  ? 88  TYR A CE2 1 
ATOM   772  C  CZ  . TYR A 1 88  ? -13.150 10.341  24.128  1.00 9.59  ? 88  TYR A CZ  1 
ATOM   773  O  OH  . TYR A 1 88  ? -12.388 10.469  25.241  1.00 10.17 ? 88  TYR A OH  1 
ATOM   774  N  N   . ARG A 1 89  ? -15.992 11.219  17.576  1.00 10.09 ? 89  ARG A N   1 
ATOM   775  C  CA  . ARG A 1 89  ? -16.511 11.111  16.223  1.00 10.23 ? 89  ARG A CA  1 
ATOM   776  C  C   . ARG A 1 89  ? -15.761 10.021  15.452  1.00 8.88  ? 89  ARG A C   1 
ATOM   777  O  O   . ARG A 1 89  ? -14.526 9.913   15.499  1.00 8.20  ? 89  ARG A O   1 
ATOM   778  C  CB  . ARG A 1 89  ? -16.201 12.429  15.575  1.00 11.95 ? 89  ARG A CB  1 
ATOM   779  C  CG  . ARG A 1 89  ? -16.953 12.568  14.260  1.00 14.15 ? 89  ARG A CG  1 
ATOM   780  C  CD  . ARG A 1 89  ? -16.704 13.986  13.726  1.00 14.41 ? 89  ARG A CD  1 
ATOM   781  N  NE  . ARG A 1 89  ? -17.407 14.982  14.534  1.00 15.18 ? 89  ARG A NE  1 
ATOM   782  C  CZ  . ARG A 1 89  ? -17.217 16.271  14.353  1.00 12.74 ? 89  ARG A CZ  1 
ATOM   783  N  NH1 . ARG A 1 89  ? -16.444 16.737  13.380  1.00 15.47 ? 89  ARG A NH1 1 
ATOM   784  N  NH2 . ARG A 1 89  ? -17.864 17.137  15.125  1.00 14.66 ? 89  ARG A NH2 1 
ATOM   785  N  N   . LEU A 1 90  ? -16.550 9.193   14.744  1.00 9.37  ? 90  LEU A N   1 
ATOM   786  C  CA  . LEU A 1 90  ? -15.966 8.085   13.992  1.00 9.05  ? 90  LEU A CA  1 
ATOM   787  C  C   . LEU A 1 90  ? -15.155 8.657   12.850  1.00 9.60  ? 90  LEU A C   1 
ATOM   788  O  O   . LEU A 1 90  ? -15.670 9.470   12.060  1.00 11.98 ? 90  LEU A O   1 
ATOM   789  C  CB  . LEU A 1 90  ? -17.076 7.205   13.411  1.00 10.31 ? 90  LEU A CB  1 
ATOM   790  C  CG  . LEU A 1 90  ? -16.665 6.040   12.503  1.00 11.43 ? 90  LEU A CG  1 
ATOM   791  C  CD1 . LEU A 1 90  ? -15.907 4.968   13.303  1.00 11.85 ? 90  LEU A CD1 1 
ATOM   792  C  CD2 . LEU A 1 90  ? -17.912 5.419   11.885  1.00 15.68 ? 90  LEU A CD2 1 
ATOM   793  N  N   . THR A 1 91  ? -13.926 8.178   12.706  1.00 9.12  ? 91  THR A N   1 
ATOM   794  C  CA  . THR A 1 91  ? -13.073 8.567   11.587  1.00 9.48  ? 91  THR A CA  1 
ATOM   795  C  C   . THR A 1 91  ? -12.730 7.423   10.638  1.00 9.31  ? 91  THR A C   1 
ATOM   796  O  O   . THR A 1 91  ? -12.626 7.633   9.443   1.00 11.00 ? 91  THR A O   1 
ATOM   797  C  CB  . THR A 1 91  ? -11.832 9.300   12.125  1.00 11.15 ? 91  THR A CB  1 
ATOM   798  O  OG1 . THR A 1 91  ? -11.160 9.897   11.018  1.00 15.84 ? 91  THR A OG1 1 
ATOM   799  C  CG2 . THR A 1 91  ? -10.924 8.430   12.952  1.00 12.45 ? 91  THR A CG2 1 
ATOM   800  N  N   . GLN A 1 92  ? -12.618 6.166   11.147  1.00 10.11 ? 92  GLN A N   1 
ATOM   801  C  CA  . GLN A 1 92  ? -12.307 5.043   10.280  1.00 10.84 ? 92  GLN A CA  1 
ATOM   802  C  C   . GLN A 1 92  ? -12.529 3.760   11.047  1.00 9.52  ? 92  GLN A C   1 
ATOM   803  O  O   . GLN A 1 92  ? -12.587 3.765   12.265  1.00 9.17  ? 92  GLN A O   1 
ATOM   804  C  CB  . GLN A 1 92  ? -10.878 5.090   9.819   1.00 12.09 ? 92  GLN A CB  1 
ATOM   805  C  CG  . GLN A 1 92  ? -9.830  5.214   10.943  1.00 12.54 ? 92  GLN A CG  1 
ATOM   806  C  CD  . GLN A 1 92  ? -9.126  3.932   11.253  1.00 12.19 ? 92  GLN A CD  1 
ATOM   807  O  OE1 . GLN A 1 92  ? -9.654  2.805   11.225  1.00 13.78 ? 92  GLN A OE1 1 
ATOM   808  N  NE2 . GLN A 1 92  ? -7.858  4.055   11.550  1.00 13.92 ? 92  GLN A NE2 1 
ATOM   809  N  N   . PHE A 1 93  ? -12.667 2.661   10.306  1.00 10.22 ? 93  PHE A N   1 
ATOM   810  C  CA  . PHE A 1 93  ? -12.517 1.358   10.929  1.00 9.20  ? 93  PHE A CA  1 
ATOM   811  C  C   . PHE A 1 93  ? -11.499 0.536   10.129  1.00 9.73  ? 93  PHE A C   1 
ATOM   812  O  O   . PHE A 1 93  ? -11.266 0.742   8.938   1.00 11.96 ? 93  PHE A O   1 
ATOM   813  C  CB  . PHE A 1 93  ? -13.864 0.658   11.135  1.00 10.62 ? 93  PHE A CB  1 
ATOM   814  C  CG  . PHE A 1 93  ? -14.540 0.218   9.869   1.00 11.52 ? 93  PHE A CG  1 
ATOM   815  C  CD1 . PHE A 1 93  ? -14.207 -0.939  9.196   1.00 12.11 ? 93  PHE A CD1 1 
ATOM   816  C  CD2 . PHE A 1 93  ? -15.664 0.920   9.463   1.00 12.58 ? 93  PHE A CD2 1 
ATOM   817  C  CE1 . PHE A 1 93  ? -14.825 -1.304  8.015   1.00 14.19 ? 93  PHE A CE1 1 
ATOM   818  C  CE2 . PHE A 1 93  ? -16.328 0.535   8.306   1.00 12.78 ? 93  PHE A CE2 1 
ATOM   819  C  CZ  . PHE A 1 93  ? -15.934 -0.582  7.600   1.00 14.83 ? 93  PHE A CZ  1 
ATOM   820  N  N   . HIS A 1 94  ? -10.969 -0.485  10.785  1.00 9.02  ? 94  HIS A N   1 
ATOM   821  C  CA  . HIS A 1 94  ? -10.029 -1.393  10.176  1.00 8.71  ? 94  HIS A CA  1 
ATOM   822  C  C   . HIS A 1 94  ? -10.065 -2.686  10.962  1.00 7.84  ? 94  HIS A C   1 
ATOM   823  O  O   . HIS A 1 94  ? -10.706 -2.777  12.000  1.00 8.74  ? 94  HIS A O   1 
ATOM   824  C  CB  . HIS A 1 94  ? -8.606  -0.833  10.107  1.00 10.13 ? 94  HIS A CB  1 
ATOM   825  C  CG  . HIS A 1 94  ? -8.094  -0.565  11.485  1.00 8.58  ? 94  HIS A CG  1 
ATOM   826  N  ND1 . HIS A 1 94  ? -8.316  0.605   12.201  1.00 9.06  ? 94  HIS A ND1 1 
ATOM   827  C  CD2 . HIS A 1 94  ? -7.424  -1.378  12.299  1.00 8.04  ? 94  HIS A CD2 1 
ATOM   828  C  CE1 . HIS A 1 94  ? -7.806  0.450   13.412  1.00 8.60  ? 94  HIS A CE1 1 
ATOM   829  N  NE2 . HIS A 1 94  ? -7.217  -0.761  13.536  1.00 7.44  ? 94  HIS A NE2 1 
ATOM   830  N  N   . PHE A 1 95  ? -9.329  -3.682  10.502  1.00 8.44  ? 95  PHE A N   1 
ATOM   831  C  CA  . PHE A 1 95  ? -9.280  -4.978  11.103  1.00 7.34  ? 95  PHE A CA  1 
ATOM   832  C  C   . PHE A 1 95  ? -7.854  -5.473  11.317  1.00 6.83  ? 95  PHE A C   1 
ATOM   833  O  O   . PHE A 1 95  ? -6.918  -5.020  10.683  1.00 8.43  ? 95  PHE A O   1 
ATOM   834  C  CB  . PHE A 1 95  ? -9.979  -6.025  10.203  1.00 8.29  ? 95  PHE A CB  1 
ATOM   835  C  CG  . PHE A 1 95  ? -11.429 -5.759  9.926   1.00 7.80  ? 95  PHE A CG  1 
ATOM   836  C  CD1 . PHE A 1 95  ? -11.796 -4.864  8.913   1.00 9.25  ? 95  PHE A CD1 1 
ATOM   837  C  CD2 . PHE A 1 95  ? -12.432 -6.444  10.612  1.00 8.86  ? 95  PHE A CD2 1 
ATOM   838  C  CE1 . PHE A 1 95  ? -13.117 -4.633  8.584   1.00 10.19 ? 95  PHE A CE1 1 
ATOM   839  C  CE2 . PHE A 1 95  ? -13.742 -6.217  10.254  1.00 9.38  ? 95  PHE A CE2 1 
ATOM   840  C  CZ  . PHE A 1 95  ? -14.093 -5.325  9.267   1.00 10.31 ? 95  PHE A CZ  1 
ATOM   841  N  N   . HIS A 1 96  ? -7.755  -6.448  12.209  1.00 7.14  ? 96  HIS A N   1 
ATOM   842  C  CA  . HIS A 1 96  ? -6.564  -7.266  12.369  1.00 6.95  ? 96  HIS A CA  1 
ATOM   843  C  C   . HIS A 1 96  ? -7.018  -8.716  12.274  1.00 6.14  ? 96  HIS A C   1 
ATOM   844  O  O   . HIS A 1 96  ? -8.094  -9.043  12.779  1.00 6.80  ? 96  HIS A O   1 
ATOM   845  C  CB  . HIS A 1 96  ? -5.896  -7.019  13.749  1.00 7.27  ? 96  HIS A CB  1 
ATOM   846  C  CG  . HIS A 1 96  ? -5.598  -5.606  14.011  1.00 6.63  ? 96  HIS A CG  1 
ATOM   847  N  ND1 . HIS A 1 96  ? -4.402  -5.015  13.799  1.00 7.82  ? 96  HIS A ND1 1 
ATOM   848  C  CD2 . HIS A 1 96  ? -6.416  -4.593  14.430  1.00 7.39  ? 96  HIS A CD2 1 
ATOM   849  C  CE1 . HIS A 1 96  ? -4.499  -3.719  14.094  1.00 7.62  ? 96  HIS A CE1 1 
ATOM   850  N  NE2 . HIS A 1 96  ? -5.703  -3.406  14.467  1.00 6.96  ? 96  HIS A NE2 1 
ATOM   851  N  N   . TRP A 1 97  ? -6.228  -9.583  11.635  1.00 6.40  ? 97  TRP A N   1 
ATOM   852  C  CA  . TRP A 1 97  ? -6.664  -10.938 11.452  1.00 6.99  ? 97  TRP A CA  1 
ATOM   853  C  C   . TRP A 1 97  ? -5.486  -11.871 11.336  1.00 7.42  ? 97  TRP A C   1 
ATOM   854  O  O   . TRP A 1 97  ? -4.317  -11.445 11.244  1.00 7.93  ? 97  TRP A O   1 
ATOM   855  C  CB  . TRP A 1 97  ? -7.585  -11.085 10.222  1.00 7.93  ? 97  TRP A CB  1 
ATOM   856  C  CG  . TRP A 1 97  ? -6.914  -10.695 8.943   1.00 7.85  ? 97  TRP A CG  1 
ATOM   857  C  CD1 . TRP A 1 97  ? -6.253  -11.544 8.102   1.00 9.50  ? 97  TRP A CD1 1 
ATOM   858  C  CD2 . TRP A 1 97  ? -6.842  -9.394  8.377   1.00 8.32  ? 97  TRP A CD2 1 
ATOM   859  N  NE1 . TRP A 1 97  ? -5.800  -10.844 7.012   1.00 11.42 ? 97  TRP A NE1 1 
ATOM   860  C  CE2 . TRP A 1 97  ? -6.125  -9.528  7.170   1.00 9.07  ? 97  TRP A CE2 1 
ATOM   861  C  CE3 . TRP A 1 97  ? -7.326  -8.121  8.749   1.00 8.25  ? 97  TRP A CE3 1 
ATOM   862  C  CZ2 . TRP A 1 97  ? -5.845  -8.422  6.340   1.00 10.32 ? 97  TRP A CZ2 1 
ATOM   863  C  CZ3 . TRP A 1 97  ? -7.047  -7.033  7.920   1.00 9.53  ? 97  TRP A CZ3 1 
ATOM   864  C  CH2 . TRP A 1 97  ? -6.363  -7.210  6.721   1.00 10.29 ? 97  TRP A CH2 1 
ATOM   865  N  N   . GLY A 1 98  ? -5.792  -13.172 11.356  1.00 7.66  ? 98  GLY A N   1 
ATOM   866  C  CA  . GLY A 1 98  ? -4.749  -14.181 11.406  1.00 8.30  ? 98  GLY A CA  1 
ATOM   867  C  C   . GLY A 1 98  ? -4.543  -14.935 10.090  1.00 9.13  ? 98  GLY A C   1 
ATOM   868  O  O   . GLY A 1 98  ? -5.286  -14.756 9.121   1.00 10.31 ? 98  GLY A O   1 
ATOM   869  N  N   . SER A 1 99  ? -3.514  -15.797 10.101  1.00 9.74  ? 99  SER A N   1 
ATOM   870  C  CA  . SER A 1 99  ? -3.322  -16.739 9.015   1.00 11.74 ? 99  SER A CA  1 
ATOM   871  C  C   . SER A 1 99  ? -4.204  -17.969 9.166   1.00 12.13 ? 99  SER A C   1 
ATOM   872  O  O   . SER A 1 99  ? -4.368  -18.716 8.214   1.00 15.84 ? 99  SER A O   1 
ATOM   873  C  CB  . SER A 1 99  ? -1.858  -17.099 8.950   1.00 13.64 ? 99  SER A CB  1 
ATOM   874  O  OG  . SER A 1 99  ? -1.422  -17.603 10.200  1.00 13.10 ? 99  SER A OG  1 
ATOM   875  N  N   . LEU A 1 100 ? -4.751  -18.211 10.363  1.00 12.15 ? 100 LEU A N   1 
ATOM   876  C  CA  . LEU A 1 100 ? -5.537  -19.371 10.749  1.00 13.72 ? 100 LEU A CA  1 
ATOM   877  C  C   . LEU A 1 100 ? -6.667  -18.841 11.569  1.00 11.40 ? 100 LEU A C   1 
ATOM   878  O  O   . LEU A 1 100 ? -6.508  -17.829 12.225  1.00 11.45 ? 100 LEU A O   1 
ATOM   879  C  CB  . LEU A 1 100 ? -4.763  -20.316 11.705  1.00 20.24 ? 100 LEU A CB  1 
ATOM   880  C  CG  . LEU A 1 100 ? -3.477  -20.835 11.127  1.00 19.98 ? 100 LEU A CG  1 
ATOM   881  C  CD1 . LEU A 1 100 ? -2.576  -21.532 12.122  1.00 22.61 ? 100 LEU A CD1 1 
ATOM   882  C  CD2 . LEU A 1 100 ? -3.885  -21.828 10.061  1.00 24.88 ? 100 LEU A CD2 1 
ATOM   883  N  N   . ASP A 1 101 ? -7.785  -19.598 11.655  1.00 11.89 ? 101 ASP A N   1 
ATOM   884  C  CA  . ASP A 1 101 ? -8.982  -19.095 12.315  1.00 11.58 ? 101 ASP A CA  1 
ATOM   885  C  C   . ASP A 1 101 ? -8.707  -19.023 13.822  1.00 11.58 ? 101 ASP A C   1 
ATOM   886  O  O   . ASP A 1 101 ? -9.381  -18.276 14.483  1.00 12.93 ? 101 ASP A O   1 
ATOM   887  C  CB  . ASP A 1 101 ? -10.180 -19.998 12.053  1.00 11.85 ? 101 ASP A CB  1 
ATOM   888  C  CG  . ASP A 1 101 ? -10.651 -20.043 10.621  1.00 13.65 ? 101 ASP A CG  1 
ATOM   889  O  OD1 . ASP A 1 101 ? -10.211 -19.223 9.775   1.00 14.36 ? 101 ASP A OD1 1 
ATOM   890  O  OD2 . ASP A 1 101 ? -11.445 -20.928 10.346  1.00 16.32 ? 101 ASP A OD2 1 
ATOM   891  N  N   . GLY A 1 102 ? -7.725  -19.777 14.325  1.00 13.33 ? 102 GLY A N   1 
ATOM   892  C  CA  . GLY A 1 102 ? -7.401  -19.770 15.734  1.00 12.85 ? 102 GLY A CA  1 
ATOM   893  C  C   . GLY A 1 102 ? -6.571  -18.604 16.274  1.00 10.51 ? 102 GLY A C   1 
ATOM   894  O  O   . GLY A 1 102 ? -6.180  -18.602 17.426  1.00 12.33 ? 102 GLY A O   1 
ATOM   895  N  N   . GLN A 1 103 ? -6.251  -17.612 15.434  1.00 9.91  ? 103 GLN A N   1 
ATOM   896  C  CA  . GLN A 1 103 ? -5.544  -16.431 15.917  1.00 7.92  ? 103 GLN A CA  1 
ATOM   897  C  C   . GLN A 1 103 ? -5.943  -15.282 15.021  1.00 7.49  ? 103 GLN A C   1 
ATOM   898  O  O   . GLN A 1 103 ? -6.461  -15.477 13.923  1.00 8.75  ? 103 GLN A O   1 
ATOM   899  C  CB  . GLN A 1 103 ? -4.050  -16.679 15.913  1.00 8.72  ? 103 GLN A CB  1 
ATOM   900  C  CG  . GLN A 1 103 ? -3.488  -16.903 14.494  1.00 10.46 ? 103 GLN A CG  1 
ATOM   901  C  CD  . GLN A 1 103 ? -2.112  -17.484 14.486  1.00 12.74 ? 103 GLN A CD  1 
ATOM   902  O  OE1 . GLN A 1 103 ? -1.218  -17.043 13.740  1.00 14.98 ? 103 GLN A OE1 1 
ATOM   903  N  NE2 . GLN A 1 103 ? -1.870  -18.420 15.332  1.00 19.42 ? 103 GLN A NE2 1 
ATOM   904  N  N   . GLY A 1 104 ? -5.595  -14.057 15.452  1.00 6.86  ? 104 GLY A N   1 
ATOM   905  C  CA  . GLY A 1 104 ? -5.872  -12.888 14.657  1.00 7.38  ? 104 GLY A CA  1 
ATOM   906  C  C   . GLY A 1 104 ? -6.311  -11.695 15.450  1.00 6.91  ? 104 GLY A C   1 
ATOM   907  O  O   . GLY A 1 104 ? -6.056  -10.568 15.086  1.00 7.91  ? 104 GLY A O   1 
ATOM   908  N  N   . SER A 1 105 ? -6.987  -11.931 16.595  1.00 6.50  ? 105 SER A N   1 
ATOM   909  C  CA  . SER A 1 105 ? -7.375  -10.801 17.432  1.00 5.98  ? 105 SER A CA  1 
ATOM   910  C  C   . SER A 1 105 ? -6.156  -10.239 18.165  1.00 6.47  ? 105 SER A C   1 
ATOM   911  O  O   . SER A 1 105 ? -5.151  -10.913 18.399  1.00 7.17  ? 105 SER A O   1 
ATOM   912  C  CB  . SER A 1 105 ? -8.514  -11.125 18.398  1.00 5.91  ? 105 SER A CB  1 
ATOM   913  O  OG  . SER A 1 105 ? -8.145  -12.110 19.360  1.00 6.56  ? 105 SER A OG  1 
ATOM   914  N  N   . GLU A 1 106 ? -6.306  -8.985  18.586  1.00 6.36  ? 106 GLU A N   1 
ATOM   915  C  CA  . GLU A 1 106 ? -5.283  -8.301  19.390  1.00 6.53  ? 106 GLU A CA  1 
ATOM   916  C  C   . GLU A 1 106 ? -5.602  -8.495  20.859  1.00 5.91  ? 106 GLU A C   1 
ATOM   917  O  O   . GLU A 1 106 ? -4.829  -9.062  21.623  1.00 6.71  ? 106 GLU A O   1 
ATOM   918  C  CB  . GLU A 1 106 ? -5.210  -6.847  18.977  1.00 6.59  ? 106 GLU A CB  1 
ATOM   919  C  CG  . GLU A 1 106 ? -4.849  -6.695  17.511  1.00 9.05  ? 106 GLU A CG  1 
ATOM   920  C  CD  . GLU A 1 106 ? -4.108  -5.442  17.245  1.00 7.22  ? 106 GLU A CD  1 
ATOM   921  O  OE1 . GLU A 1 106 ? -4.739  -4.361  17.448  1.00 7.72  ? 106 GLU A OE1 1 
ATOM   922  O  OE2 . GLU A 1 106 ? -2.931  -5.480  16.779  1.00 8.84  ? 106 GLU A OE2 1 
ATOM   923  N  N   . HIS A 1 107 ? -6.774  -8.041  21.282  1.00 5.58  ? 107 HIS A N   1 
ATOM   924  C  CA  . HIS A 1 107 ? -7.269  -8.423  22.598  1.00 5.43  ? 107 HIS A CA  1 
ATOM   925  C  C   . HIS A 1 107 ? -7.537  -9.914  22.622  1.00 6.15  ? 107 HIS A C   1 
ATOM   926  O  O   . HIS A 1 107 ? -7.890  -10.538 21.621  1.00 6.18  ? 107 HIS A O   1 
ATOM   927  C  CB  . HIS A 1 107 ? -8.479  -7.626  22.997  1.00 5.85  ? 107 HIS A CB  1 
ATOM   928  C  CG  . HIS A 1 107 ? -8.176  -6.185  23.144  1.00 5.45  ? 107 HIS A CG  1 
ATOM   929  N  ND1 . HIS A 1 107 ? -8.194  -5.281  22.087  1.00 6.30  ? 107 HIS A ND1 1 
ATOM   930  C  CD2 . HIS A 1 107 ? -7.719  -5.481  24.198  1.00 5.69  ? 107 HIS A CD2 1 
ATOM   931  C  CE1 . HIS A 1 107 ? -7.766  -4.100  22.522  1.00 5.86  ? 107 HIS A CE1 1 
ATOM   932  N  NE2 . HIS A 1 107 ? -7.459  -4.186  23.817  1.00 6.41  ? 107 HIS A NE2 1 
ATOM   933  N  N   . THR A 1 108 ? -7.429  -10.470 23.845  1.00 6.81  ? 108 THR A N   1 
ATOM   934  C  CA  . THR A 1 108 ? -7.800  -11.852 24.102  1.00 6.73  ? 108 THR A CA  1 
ATOM   935  C  C   . THR A 1 108 ? -8.767  -11.822 25.297  1.00 6.35  ? 108 THR A C   1 
ATOM   936  O  O   . THR A 1 108 ? -8.771  -10.880 26.063  1.00 7.16  ? 108 THR A O   1 
ATOM   937  C  CB  . THR A 1 108 ? -6.583  -12.759 24.315  1.00 7.70  ? 108 THR A CB  1 
ATOM   938  O  OG1 . THR A 1 108 ? -5.758  -12.277 25.365  1.00 8.29  ? 108 THR A OG1 1 
ATOM   939  C  CG2 . THR A 1 108 ? -5.756  -12.823 23.042  1.00 9.00  ? 108 THR A CG2 1 
ATOM   940  N  N   . VAL A 1 109 ? -9.508  -12.911 25.447  1.00 7.31  ? 109 VAL A N   1 
ATOM   941  C  CA  . VAL A 1 109 ? -10.501 -12.980 26.539  1.00 8.29  ? 109 VAL A CA  1 
ATOM   942  C  C   . VAL A 1 109 ? -10.208 -14.292 27.274  1.00 8.64  ? 109 VAL A C   1 
ATOM   943  O  O   . VAL A 1 109 ? -10.371 -15.393 26.709  1.00 8.39  ? 109 VAL A O   1 
ATOM   944  C  CB  . VAL A 1 109 ? -11.938 -12.999 25.968  1.00 8.76  ? 109 VAL A CB  1 
ATOM   945  C  CG1 . VAL A 1 109 ? -12.944 -13.104 27.144  1.00 11.15 ? 109 VAL A CG1 1 
ATOM   946  C  CG2 . VAL A 1 109 ? -12.194 -11.720 25.185  1.00 9.57  ? 109 VAL A CG2 1 
ATOM   947  N  N   . ASP A 1 110 ? -9.684  -14.183 28.492  1.00 9.21  ? 110 ASP A N   1 
ATOM   948  C  CA  . ASP A 1 110 ? -9.229  -15.383 29.213  1.00 10.35 ? 110 ASP A CA  1 
ATOM   949  C  C   . ASP A 1 110 ? -8.281  -16.199 28.324  1.00 9.82  ? 110 ASP A C   1 
ATOM   950  O  O   . ASP A 1 110 ? -8.331  -17.433 28.274  1.00 11.44 ? 110 ASP A O   1 
ATOM   951  C  CB  . ASP A 1 110 ? -10.388 -16.216 29.713  1.00 12.29 ? 110 ASP A CB  1 
ATOM   952  C  CG  . ASP A 1 110 ? -11.231 -15.415 30.732  1.00 12.74 ? 110 ASP A CG  1 
ATOM   953  O  OD1 . ASP A 1 110 ? -10.672 -14.584 31.431  1.00 13.93 ? 110 ASP A OD1 1 
ATOM   954  O  OD2 . ASP A 1 110 ? -12.420 -15.705 30.844  1.00 16.95 ? 110 ASP A OD2 1 
ATOM   955  N  N   . LYS A 1 111 ? -7.421  -15.494 27.607  1.00 9.46  ? 111 LYS A N   1 
ATOM   956  C  CA  . LYS A 1 111 ? -6.352  -16.016 26.759  1.00 9.63  ? 111 LYS A CA  1 
ATOM   957  C  C   . LYS A 1 111 ? -6.927  -16.511 25.433  1.00 9.98  ? 111 LYS A C   1 
ATOM   958  O  O   . LYS A 1 111 ? -6.146  -16.886 24.555  1.00 10.75 ? 111 LYS A O   1 
ATOM   959  C  CB  . LYS A 1 111 ? -5.403  -17.057 27.388  1.00 12.80 ? 111 LYS A CB  1 
ATOM   960  C  CG  . LYS A 1 111 ? -4.761  -16.545 28.679  1.00 16.93 ? 111 LYS A CG  1 
ATOM   961  C  CD  . LYS A 1 111 ? -3.843  -15.378 28.340  1.00 20.87 ? 111 LYS A CD  1 
ATOM   962  C  CE  . LYS A 1 111 ? -3.091  -14.771 29.517  1.00 23.29 ? 111 LYS A CE  1 
ATOM   963  N  NZ  . LYS A 1 111 ? -1.758  -15.350 29.617  1.00 24.69 ? 111 LYS A NZ  1 
ATOM   964  N  N   . LYS A 1 112 ? -8.240  -16.501 25.210  1.00 8.91  ? 112 LYS A N   1 
ATOM   965  C  CA  . LYS A 1 112 ? -8.769  -16.920 23.925  1.00 9.46  ? 112 LYS A CA  1 
ATOM   966  C  C   . LYS A 1 112 ? -8.467  -15.847 22.865  1.00 8.33  ? 112 LYS A C   1 
ATOM   967  O  O   . LYS A 1 112 ? -8.731  -14.670 23.062  1.00 7.71  ? 112 LYS A O   1 
ATOM   968  C  CB  . LYS A 1 112 ? -10.306 -17.043 24.005  1.00 10.52 ? 112 LYS A CB  1 
ATOM   969  C  CG  . LYS A 1 112 ? -11.031 -17.401 22.705  1.00 11.65 ? 112 LYS A CG  1 
ATOM   970  C  CD  . LYS A 1 112 ? -12.501 -17.413 22.801  1.00 14.93 ? 112 LYS A CD  1 
ATOM   971  C  CE  . LYS A 1 112 ? -13.168 -17.555 21.453  1.00 15.37 ? 112 LYS A CE  1 
ATOM   972  N  NZ  . LYS A 1 112 ? -13.012 -18.890 20.919  1.00 18.55 ? 112 LYS A NZ  1 
ATOM   973  N  N   A LYS A 1 113 ? -7.964  -16.334 21.716  0.50 8.27  ? 113 LYS A N   1 
ATOM   974  N  N   B LYS A 1 113 ? -7.966  -16.337 21.715  0.50 8.28  ? 113 LYS A N   1 
ATOM   975  C  CA  A LYS A 1 113 ? -7.780  -15.513 20.541  0.50 8.17  ? 113 LYS A CA  1 
ATOM   976  C  CA  B LYS A 1 113 ? -7.773  -15.518 20.538  0.50 8.19  ? 113 LYS A CA  1 
ATOM   977  C  C   A LYS A 1 113 ? -8.928  -15.764 19.582  0.50 8.29  ? 113 LYS A C   1 
ATOM   978  C  C   B LYS A 1 113 ? -8.920  -15.766 19.575  0.50 8.27  ? 113 LYS A C   1 
ATOM   979  O  O   A LYS A 1 113 ? -9.297  -16.910 19.311  0.50 11.10 ? 113 LYS A O   1 
ATOM   980  O  O   B LYS A 1 113 ? -9.300  -16.910 19.309  0.50 11.05 ? 113 LYS A O   1 
ATOM   981  C  CB  A LYS A 1 113 ? -6.500  -15.930 19.830  0.50 8.99  ? 113 LYS A CB  1 
ATOM   982  C  CB  B LYS A 1 113 ? -6.449  -15.884 19.876  0.50 8.88  ? 113 LYS A CB  1 
ATOM   983  C  CG  A LYS A 1 113 ? -5.232  -15.766 20.660  0.50 10.08 ? 113 LYS A CG  1 
ATOM   984  C  CG  B LYS A 1 113 ? -5.209  -15.448 20.657  0.50 10.02 ? 113 LYS A CG  1 
ATOM   985  C  CD  A LYS A 1 113 ? -4.027  -16.386 19.962  0.50 11.07 ? 113 LYS A CD  1 
ATOM   986  C  CD  B LYS A 1 113 ? -3.908  -16.036 20.105  0.50 10.83 ? 113 LYS A CD  1 
ATOM   987  C  CE  A LYS A 1 113 ? -2.702  -15.958 20.564  0.50 11.83 ? 113 LYS A CE  1 
ATOM   988  C  CE  B LYS A 1 113 ? -2.713  -15.446 20.830  0.50 13.30 ? 113 LYS A CE  1 
ATOM   989  N  NZ  A LYS A 1 113 ? -2.452  -16.587 21.883  0.50 13.91 ? 113 LYS A NZ  1 
ATOM   990  N  NZ  B LYS A 1 113 ? -1.526  -16.326 20.707  0.50 14.99 ? 113 LYS A NZ  1 
ATOM   991  N  N   . TYR A 1 114 ? -9.478  -14.672 19.054  1.00 6.77  ? 114 TYR A N   1 
ATOM   992  C  CA  . TYR A 1 114 ? -10.474 -14.762 18.005  1.00 6.89  ? 114 TYR A CA  1 
ATOM   993  C  C   . TYR A 1 114 ? -9.800  -14.730 16.634  1.00 6.70  ? 114 TYR A C   1 
ATOM   994  O  O   . TYR A 1 114 ? -8.594  -14.416 16.514  1.00 7.23  ? 114 TYR A O   1 
ATOM   995  C  CB  . TYR A 1 114 ? -11.498 -13.648 18.180  1.00 6.63  ? 114 TYR A CB  1 
ATOM   996  C  CG  . TYR A 1 114 ? -12.428 -13.860 19.319  1.00 6.61  ? 114 TYR A CG  1 
ATOM   997  C  CD1 . TYR A 1 114 ? -12.133 -13.470 20.622  1.00 8.77  ? 114 TYR A CD1 1 
ATOM   998  C  CD2 . TYR A 1 114 ? -13.654 -14.484 19.094  1.00 8.76  ? 114 TYR A CD2 1 
ATOM   999  C  CE1 . TYR A 1 114 ? -13.057 -13.643 21.653  1.00 11.16 ? 114 TYR A CE1 1 
ATOM   1000 C  CE2 . TYR A 1 114 ? -14.595 -14.689 20.116  1.00 12.24 ? 114 TYR A CE2 1 
ATOM   1001 C  CZ  . TYR A 1 114 ? -14.248 -14.279 21.388  1.00 12.64 ? 114 TYR A CZ  1 
ATOM   1002 O  OH  . TYR A 1 114 ? -15.119 -14.379 22.453  1.00 17.40 ? 114 TYR A OH  1 
ATOM   1003 N  N   . ALA A 1 115 ? -10.570 -15.007 15.580  1.00 7.05  ? 115 ALA A N   1 
ATOM   1004 C  CA  . ALA A 1 115 ? -10.026 -15.012 14.232  1.00 7.10  ? 115 ALA A CA  1 
ATOM   1005 C  C   . ALA A 1 115 ? -9.629  -13.644 13.751  1.00 6.86  ? 115 ALA A C   1 
ATOM   1006 O  O   . ALA A 1 115 ? -8.788  -13.496 12.862  1.00 7.81  ? 115 ALA A O   1 
ATOM   1007 C  CB  . ALA A 1 115 ? -11.064 -15.647 13.298  1.00 8.47  ? 115 ALA A CB  1 
ATOM   1008 N  N   . ALA A 1 116 ? -10.324 -12.606 14.258  1.00 6.73  ? 116 ALA A N   1 
ATOM   1009 C  CA  . ALA A 1 116 ? -10.002 -11.247 13.806  1.00 6.84  ? 116 ALA A CA  1 
ATOM   1010 C  C   . ALA A 1 116 ? -10.605 -10.299 14.817  1.00 6.03  ? 116 ALA A C   1 
ATOM   1011 O  O   . ALA A 1 116 ? -11.320 -10.690 15.753  1.00 6.51  ? 116 ALA A O   1 
ATOM   1012 C  CB  . ALA A 1 116 ? -10.568 -10.977 12.399  1.00 7.79  ? 116 ALA A CB  1 
ATOM   1013 N  N   . GLU A 1 117 ? -10.255 -9.016  14.649  1.00 6.50  ? 117 GLU A N   1 
ATOM   1014 C  CA  . GLU A 1 117 ? -10.770 -7.967  15.509  1.00 5.92  ? 117 GLU A CA  1 
ATOM   1015 C  C   . GLU A 1 117 ? -10.993 -6.719  14.656  1.00 5.73  ? 117 GLU A C   1 
ATOM   1016 O  O   . GLU A 1 117 ? -10.093 -6.324  13.904  1.00 7.41  ? 117 GLU A O   1 
ATOM   1017 C  CB  . GLU A 1 117 ? -9.803  -7.718  16.678  1.00 6.03  ? 117 GLU A CB  1 
ATOM   1018 C  CG  . GLU A 1 117 ? -10.284 -6.772  17.754  1.00 6.96  ? 117 GLU A CG  1 
ATOM   1019 C  CD  . GLU A 1 117 ? -9.371  -6.727  18.955  1.00 6.13  ? 117 GLU A CD  1 
ATOM   1020 O  OE1 . GLU A 1 117 ? -8.742  -7.739  19.261  1.00 7.11  ? 117 GLU A OE1 1 
ATOM   1021 O  OE2 . GLU A 1 117 ? -9.285  -5.653  19.585  1.00 7.69  ? 117 GLU A OE2 1 
ATOM   1022 N  N   . LEU A 1 118 ? -12.165 -6.138  14.824  1.00 6.23  ? 118 LEU A N   1 
ATOM   1023 C  CA  . LEU A 1 118 ? -12.545 -4.894  14.170  1.00 6.87  ? 118 LEU A CA  1 
ATOM   1024 C  C   . LEU A 1 118 ? -12.330 -3.762  15.150  1.00 6.17  ? 118 LEU A C   1 
ATOM   1025 O  O   . LEU A 1 118 ? -12.741 -3.828  16.304  1.00 5.95  ? 118 LEU A O   1 
ATOM   1026 C  CB  . LEU A 1 118 ? -14.036 -5.022  13.830  1.00 7.69  ? 118 LEU A CB  1 
ATOM   1027 C  CG  . LEU A 1 118 ? -14.796 -3.741  13.459  1.00 8.79  ? 118 LEU A CG  1 
ATOM   1028 C  CD1 . LEU A 1 118 ? -14.223 -3.051  12.236  1.00 9.37  ? 118 LEU A CD1 1 
ATOM   1029 C  CD2 . LEU A 1 118 ? -16.267 -4.102  13.225  1.00 10.91 ? 118 LEU A CD2 1 
ATOM   1030 N  N   . HIS A 1 119 ? -11.704 -2.692  14.652  1.00 5.73  ? 119 HIS A N   1 
ATOM   1031 C  CA  . HIS A 1 119 ? -11.449 -1.465  15.412  1.00 6.10  ? 119 HIS A CA  1 
ATOM   1032 C  C   . HIS A 1 119 ? -12.150 -0.296  14.742  1.00 6.24  ? 119 HIS A C   1 
ATOM   1033 O  O   . HIS A 1 119 ? -11.779 0.075   13.628  1.00 7.38  ? 119 HIS A O   1 
ATOM   1034 C  CB  . HIS A 1 119 ? -9.943  -1.185  15.483  1.00 6.60  ? 119 HIS A CB  1 
ATOM   1035 C  CG  . HIS A 1 119 ? -9.241  -2.148  16.369  1.00 5.95  ? 119 HIS A CG  1 
ATOM   1036 N  ND1 . HIS A 1 119 ? -7.866  -2.348  16.352  1.00 6.31  ? 119 HIS A ND1 1 
ATOM   1037 C  CD2 . HIS A 1 119 ? -9.771  -2.995  17.304  1.00 5.59  ? 119 HIS A CD2 1 
ATOM   1038 C  CE1 . HIS A 1 119 ? -7.588  -3.291  17.245  1.00 6.15  ? 119 HIS A CE1 1 
ATOM   1039 N  NE2 . HIS A 1 119 ? -8.723  -3.696  17.827  1.00 6.07  ? 119 HIS A NE2 1 
ATOM   1040 N  N   . LEU A 1 120 ? -13.156 0.264   15.422  1.00 6.31  ? 120 LEU A N   1 
ATOM   1041 C  CA  . LEU A 1 120 ? -13.823 1.495   15.002  1.00 6.81  ? 120 LEU A CA  1 
ATOM   1042 C  C   . LEU A 1 120 ? -13.212 2.631   15.793  1.00 5.98  ? 120 LEU A C   1 
ATOM   1043 O  O   . LEU A 1 120 ? -13.308 2.670   17.019  1.00 6.05  ? 120 LEU A O   1 
ATOM   1044 C  CB  . LEU A 1 120 ? -15.310 1.367   15.217  1.00 7.96  ? 120 LEU A CB  1 
ATOM   1045 C  CG  . LEU A 1 120 ? -15.976 0.318   14.337  1.00 8.82  ? 120 LEU A CG  1 
ATOM   1046 C  CD1 . LEU A 1 120 ? -16.833 -0.585  15.197  1.00 12.15 ? 120 LEU A CD1 1 
ATOM   1047 C  CD2 . LEU A 1 120 ? -16.840 0.991   13.273  1.00 12.23 ? 120 LEU A CD2 1 
ATOM   1048 N  N   . VAL A 1 121 ? -12.509 3.513   15.100  1.00 6.67  ? 121 VAL A N   1 
ATOM   1049 C  CA  . VAL A 1 121 ? -11.691 4.539   15.705  1.00 6.77  ? 121 VAL A CA  1 
ATOM   1050 C  C   . VAL A 1 121 ? -12.448 5.859   15.719  1.00 6.97  ? 121 VAL A C   1 
ATOM   1051 O  O   . VAL A 1 121 ? -12.912 6.324   14.684  1.00 7.96  ? 121 VAL A O   1 
ATOM   1052 C  CB  . VAL A 1 121 ? -10.374 4.668   14.908  1.00 8.05  ? 121 VAL A CB  1 
ATOM   1053 C  CG1 . VAL A 1 121 ? -9.464  5.765   15.514  1.00 9.94  ? 121 VAL A CG1 1 
ATOM   1054 C  CG2 . VAL A 1 121 ? -9.644  3.316   14.844  1.00 8.40  ? 121 VAL A CG2 1 
ATOM   1055 N  N   . HIS A 1 122 ? -12.438 6.500   16.879  1.00 6.48  ? 122 HIS A N   1 
ATOM   1056 C  CA  . HIS A 1 122 ? -13.148 7.745   17.093  1.00 6.79  ? 122 HIS A CA  1 
ATOM   1057 C  C   . HIS A 1 122 ? -12.250 8.734   17.829  1.00 7.18  ? 122 HIS A C   1 
ATOM   1058 O  O   . HIS A 1 122 ? -11.425 8.332   18.646  1.00 8.14  ? 122 HIS A O   1 
ATOM   1059 C  CB  . HIS A 1 122 ? -14.373 7.529   17.978  1.00 7.65  ? 122 HIS A CB  1 
ATOM   1060 C  CG  . HIS A 1 122 ? -15.268 6.402   17.592  1.00 6.89  ? 122 HIS A CG  1 
ATOM   1061 N  ND1 . HIS A 1 122 ? -14.918 5.078   17.821  1.00 7.00  ? 122 HIS A ND1 1 
ATOM   1062 C  CD2 . HIS A 1 122 ? -16.492 6.363   17.013  1.00 8.00  ? 122 HIS A CD2 1 
ATOM   1063 C  CE1 . HIS A 1 122 ? -15.910 4.331   17.388  1.00 8.20  ? 122 HIS A CE1 1 
ATOM   1064 N  NE2 . HIS A 1 122 ? -16.906 5.068   16.890  1.00 9.12  ? 122 HIS A NE2 1 
ATOM   1065 N  N   . TRP A 1 123 ? -12.406 10.024  17.543  1.00 6.97  ? 123 TRP A N   1 
ATOM   1066 C  CA  . TRP A 1 123 ? -11.599 11.044  18.209  1.00 7.05  ? 123 TRP A CA  1 
ATOM   1067 C  C   . TRP A 1 123 ? -12.492 11.981  18.999  1.00 7.36  ? 123 TRP A C   1 
ATOM   1068 O  O   . TRP A 1 123 ? -13.601 12.327  18.609  1.00 8.00  ? 123 TRP A O   1 
ATOM   1069 C  CB  . TRP A 1 123 ? -10.708 11.820  17.242  1.00 8.00  ? 123 TRP A CB  1 
ATOM   1070 C  CG  . TRP A 1 123 ? -11.396 12.422  16.063  1.00 8.85  ? 123 TRP A CG  1 
ATOM   1071 C  CD1 . TRP A 1 123 ? -11.682 11.797  14.874  1.00 10.35 ? 123 TRP A CD1 1 
ATOM   1072 C  CD2 . TRP A 1 123 ? -11.867 13.763  15.921  1.00 9.77  ? 123 TRP A CD2 1 
ATOM   1073 N  NE1 . TRP A 1 123 ? -12.280 12.637  14.000  1.00 11.44 ? 123 TRP A NE1 1 
ATOM   1074 C  CE2 . TRP A 1 123 ? -12.438 13.851  14.617  1.00 11.28 ? 123 TRP A CE2 1 
ATOM   1075 C  CE3 . TRP A 1 123 ? -11.885 14.884  16.754  1.00 10.19 ? 123 TRP A CE3 1 
ATOM   1076 C  CZ2 . TRP A 1 123 ? -12.992 15.017  14.120  1.00 13.70 ? 123 TRP A CZ2 1 
ATOM   1077 C  CZ3 . TRP A 1 123 ? -12.436 16.024  16.240  1.00 14.20 ? 123 TRP A CZ3 1 
ATOM   1078 C  CH2 . TRP A 1 123 ? -12.925 16.116  14.938  1.00 13.68 ? 123 TRP A CH2 1 
ATOM   1079 N  N   . ASN A 1 124 ? -11.935 12.435  20.125  1.00 6.83  ? 124 ASN A N   1 
ATOM   1080 C  CA  . ASN A 1 124 ? -12.666 13.307  21.036  1.00 7.88  ? 124 ASN A CA  1 
ATOM   1081 C  C   . ASN A 1 124 ? -12.785 14.677  20.417  1.00 8.06  ? 124 ASN A C   1 
ATOM   1082 O  O   . ASN A 1 124 ? -11.765 15.335  20.136  1.00 7.95  ? 124 ASN A O   1 
ATOM   1083 C  CB  . ASN A 1 124 ? -11.817 13.375  22.290  1.00 8.64  ? 124 ASN A CB  1 
ATOM   1084 C  CG  . ASN A 1 124 ? -12.535 14.007  23.458  1.00 9.99  ? 124 ASN A CG  1 
ATOM   1085 O  OD1 . ASN A 1 124 ? -13.377 14.910  23.254  1.00 10.70 ? 124 ASN A OD1 1 
ATOM   1086 N  ND2 . ASN A 1 124 ? -12.176 13.578  24.667  1.00 11.84 ? 124 ASN A ND2 1 
ATOM   1087 N  N   . THR A 1 125 ? -14.011 15.137  20.241  1.00 9.11  ? 125 THR A N   1 
ATOM   1088 C  CA  . THR A 1 125 ? -14.257 16.391  19.507  1.00 10.48 ? 125 THR A CA  1 
ATOM   1089 C  C   . THR A 1 125 ? -13.673 17.592  20.262  1.00 10.24 ? 125 THR A C   1 
ATOM   1090 O  O   . THR A 1 125 ? -13.484 18.635  19.611  1.00 11.23 ? 125 THR A O   1 
ATOM   1091 C  CB  . THR A 1 125 ? -15.743 16.573  19.169  1.00 13.35 ? 125 THR A CB  1 
ATOM   1092 O  OG1 . THR A 1 125 ? -16.452 16.589  20.406  1.00 16.07 ? 125 THR A OG1 1 
ATOM   1093 C  CG2 . THR A 1 125 ? -16.163 15.478  18.213  1.00 17.64 ? 125 THR A CG2 1 
ATOM   1094 N  N   A LYS A 1 126 ? -13.384 17.461  21.543  0.50 9.27  ? 127 LYS A N   1 
ATOM   1095 N  N   B LYS A 1 126 ? -13.390 17.471  21.565  0.50 10.27 ? 127 LYS A N   1 
ATOM   1096 C  CA  A LYS A 1 126 ? -12.820 18.647  22.210  0.50 11.72 ? 127 LYS A CA  1 
ATOM   1097 C  CA  B LYS A 1 126 ? -12.780 18.583  22.316  0.50 10.86 ? 127 LYS A CA  1 
ATOM   1098 C  C   A LYS A 1 126 ? -11.402 18.972  21.726  0.50 10.05 ? 127 LYS A C   1 
ATOM   1099 C  C   B LYS A 1 126 ? -11.395 18.952  21.759  0.50 10.19 ? 127 LYS A C   1 
ATOM   1100 O  O   A LYS A 1 126 ? -10.918 20.044  22.065  0.50 12.11 ? 127 LYS A O   1 
ATOM   1101 O  O   B LYS A 1 126 ? -10.925 20.042  22.059  0.50 13.19 ? 127 LYS A O   1 
ATOM   1102 C  CB  A LYS A 1 126 ? -12.941 18.492  23.715  0.50 14.12 ? 127 LYS A CB  1 
ATOM   1103 C  CB  B LYS A 1 126 ? -12.797 18.251  23.809  0.50 14.30 ? 127 LYS A CB  1 
ATOM   1104 C  CG  A LYS A 1 126 ? -11.886 17.629  24.324  0.50 13.82 ? 127 LYS A CG  1 
ATOM   1105 C  CG  B LYS A 1 126 ? -11.620 17.417  24.255  0.50 15.82 ? 127 LYS A CG  1 
ATOM   1106 C  CD  A LYS A 1 126 ? -12.278 17.426  25.767  0.50 18.15 ? 127 LYS A CD  1 
ATOM   1107 C  CD  B LYS A 1 126 ? -11.673 16.878  25.701  0.50 17.29 ? 127 LYS A CD  1 
ATOM   1108 C  CE  A LYS A 1 126 ? -11.296 16.507  26.430  0.50 15.02 ? 127 LYS A CE  1 
ATOM   1109 C  CE  B LYS A 1 126 ? -11.009 17.857  26.648  0.50 23.46 ? 127 LYS A CE  1 
ATOM   1110 N  NZ  A LYS A 1 126 ? -11.162 16.793  27.879  0.50 26.04 ? 127 LYS A NZ  1 
ATOM   1111 N  NZ  B LYS A 1 126 ? -11.840 19.059  26.863  0.50 36.40 ? 127 LYS A NZ  1 
ATOM   1112 N  N   . TYR A 1 127 ? -10.767 18.078  20.967  1.00 8.20  ? 128 TYR A N   1 
ATOM   1113 C  CA  . TYR A 1 127 ? -9.437  18.337  20.469  1.00 9.25  ? 128 TYR A CA  1 
ATOM   1114 C  C   . TYR A 1 127 ? -9.451  18.702  18.982  1.00 9.02  ? 128 TYR A C   1 
ATOM   1115 O  O   . TYR A 1 127 ? -8.383  18.932  18.390  1.00 10.16 ? 128 TYR A O   1 
ATOM   1116 C  CB  . TYR A 1 127 ? -8.520  17.136  20.711  1.00 9.45  ? 128 TYR A CB  1 
ATOM   1117 C  CG  . TYR A 1 127 ? -8.396  16.883  22.180  1.00 9.51  ? 128 TYR A CG  1 
ATOM   1118 C  CD1 . TYR A 1 127 ? -7.937  17.862  23.068  1.00 10.54 ? 128 TYR A CD1 1 
ATOM   1119 C  CD2 . TYR A 1 127 ? -8.715  15.632  22.682  1.00 9.15  ? 128 TYR A CD2 1 
ATOM   1120 C  CE1 . TYR A 1 127 ? -7.886  17.598  24.414  1.00 11.76 ? 128 TYR A CE1 1 
ATOM   1121 C  CE2 . TYR A 1 127 ? -8.573  15.334  24.040  1.00 9.73  ? 128 TYR A CE2 1 
ATOM   1122 C  CZ  . TYR A 1 127 ? -8.179  16.347  24.919  1.00 11.07 ? 128 TYR A CZ  1 
ATOM   1123 O  OH  . TYR A 1 127 ? -8.088  16.116  26.245  1.00 13.34 ? 128 TYR A OH  1 
ATOM   1124 N  N   . GLY A 1 128 ? -10.647 18.808  18.368  1.00 8.93  ? 129 GLY A N   1 
ATOM   1125 C  CA  . GLY A 1 128 ? -10.748 19.507  17.106  1.00 11.23 ? 129 GLY A CA  1 
ATOM   1126 C  C   . GLY A 1 128 ? -10.440 18.667  15.847  1.00 9.99  ? 129 GLY A C   1 
ATOM   1127 O  O   . GLY A 1 128 ? -11.096 18.823  14.820  1.00 12.65 ? 129 GLY A O   1 
ATOM   1128 N  N   A ASP A 1 129 ? -9.331  17.881  15.897  0.50 12.56 ? 130 ASP A N   1 
ATOM   1129 N  N   B ASP A 1 129 ? -9.559  17.671  15.931  0.50 10.83 ? 130 ASP A N   1 
ATOM   1130 C  CA  A ASP A 1 129 ? -8.849  17.008  14.823  0.50 12.65 ? 130 ASP A CA  1 
ATOM   1131 C  CA  B ASP A 1 129 ? -9.436  16.720  14.840  0.50 10.80 ? 130 ASP A CA  1 
ATOM   1132 C  C   A ASP A 1 129 ? -8.452  15.630  15.403  0.50 13.05 ? 130 ASP A C   1 
ATOM   1133 C  C   B ASP A 1 129 ? -8.528  15.615  15.375  0.50 12.43 ? 130 ASP A C   1 
ATOM   1134 O  O   A ASP A 1 129 ? -8.203  15.472  16.603  0.50 12.83 ? 130 ASP A O   1 
ATOM   1135 O  O   B ASP A 1 129 ? -7.889  15.688  16.439  0.50 11.86 ? 130 ASP A O   1 
ATOM   1136 C  CB  A ASP A 1 129 ? -7.855  17.682  13.850  0.50 11.56 ? 130 ASP A CB  1 
ATOM   1137 C  CB  B ASP A 1 129 ? -8.861  17.322  13.555  0.50 11.31 ? 130 ASP A CB  1 
ATOM   1138 C  CG  A ASP A 1 129 ? -6.448  18.042  14.336  0.50 12.72 ? 130 ASP A CG  1 
ATOM   1139 C  CG  B ASP A 1 129 ? -7.447  17.802  13.758  0.50 10.23 ? 130 ASP A CG  1 
ATOM   1140 O  OD1 A ASP A 1 129 ? -5.603  17.130  14.544  0.50 15.50 ? 130 ASP A OD1 1 
ATOM   1141 O  OD1 B ASP A 1 129 ? -6.854  17.445  14.787  0.50 13.66 ? 130 ASP A OD1 1 
ATOM   1142 O  OD2 A ASP A 1 129 ? -6.175  19.240  14.466  0.50 16.84 ? 130 ASP A OD2 1 
ATOM   1143 O  OD2 B ASP A 1 129 ? -6.976  18.523  12.908  0.50 13.13 ? 130 ASP A OD2 1 
ATOM   1144 N  N   . ALA A 1 130 ? -8.470  14.583  14.570  1.00 14.73 ? 131 ALA A N   1 
ATOM   1145 C  CA  . ALA A 1 130 ? -7.911  13.307  15.007  1.00 13.03 ? 131 ALA A CA  1 
ATOM   1146 C  C   . ALA A 1 130 ? -6.408  13.363  15.339  1.00 12.23 ? 131 ALA A C   1 
ATOM   1147 O  O   . ALA A 1 130 ? -5.928  12.681  16.258  1.00 11.36 ? 131 ALA A O   1 
ATOM   1148 C  CB  . ALA A 1 130 ? -8.188  12.191  14.011  1.00 15.71 ? 131 ALA A CB  1 
ATOM   1149 N  N   . GLY A 1 131 ? -5.661  14.181  14.573  1.00 14.49 ? 132 GLY A N   1 
ATOM   1150 C  CA  . GLY A 1 131 ? -4.229  14.207  14.825  1.00 15.92 ? 132 GLY A CA  1 
ATOM   1151 C  C   . GLY A 1 131 ? -3.913  14.837  16.188  1.00 13.78 ? 132 GLY A C   1 
ATOM   1152 O  O   . GLY A 1 131 ? -3.092  14.358  16.986  1.00 17.39 ? 132 GLY A O   1 
ATOM   1153 N  N   . LYS A 1 132 ? -4.514  16.007  16.475  1.00 14.13 ? 133 LYS A N   1 
ATOM   1154 C  CA  . LYS A 1 132 ? -4.342  16.598  17.803  1.00 13.45 ? 133 LYS A CA  1 
ATOM   1155 C  C   . LYS A 1 132 ? -4.857  15.695  18.900  1.00 11.46 ? 133 LYS A C   1 
ATOM   1156 O  O   . LYS A 1 132 ? -4.251  15.576  19.969  1.00 12.26 ? 133 LYS A O   1 
ATOM   1157 C  CB  . LYS A 1 132 ? -4.991  17.981  17.912  1.00 14.27 ? 133 LYS A CB  1 
ATOM   1158 C  CG  . LYS A 1 132 ? -4.213  19.125  17.277  1.00 27.05 ? 133 LYS A CG  1 
ATOM   1159 C  CD  . LYS A 1 132 ? -4.524  19.477  15.896  1.00 36.89 ? 133 LYS A CD  1 
ATOM   1160 C  CE  . LYS A 1 132 ? -3.434  20.305  15.295  1.00 41.91 ? 133 LYS A CE  1 
ATOM   1161 N  NZ  . LYS A 1 132 ? -2.171  19.536  15.420  1.00 66.03 ? 133 LYS A NZ  1 
ATOM   1162 N  N   . ALA A 1 133 ? -5.994  15.019  18.632  1.00 10.07 ? 134 ALA A N   1 
ATOM   1163 C  CA  . ALA A 1 133 ? -6.519  14.099  19.627  1.00 8.95  ? 134 ALA A CA  1 
ATOM   1164 C  C   . ALA A 1 133 ? -5.536  12.991  19.995  1.00 9.26  ? 134 ALA A C   1 
ATOM   1165 O  O   . ALA A 1 133 ? -5.467  12.559  21.147  1.00 9.94  ? 134 ALA A O   1 
ATOM   1166 C  CB  . ALA A 1 133 ? -7.840  13.511  19.152  1.00 9.12  ? 134 ALA A CB  1 
ATOM   1167 N  N   A SER A 1 134 ? -4.751  12.555  19.014  0.50 10.72 ? 135 SER A N   1 
ATOM   1168 N  N   B SER A 1 134 ? -4.733  12.525  19.040  0.50 11.11 ? 135 SER A N   1 
ATOM   1169 C  CA  A SER A 1 134 ? -3.827  11.456  19.219  0.50 11.14 ? 135 SER A CA  1 
ATOM   1170 C  CA  B SER A 1 134 ? -3.837  11.410  19.314  0.50 12.20 ? 135 SER A CA  1 
ATOM   1171 C  C   A SER A 1 134 ? -2.689  11.823  20.163  0.50 11.48 ? 135 SER A C   1 
ATOM   1172 C  C   B SER A 1 134 ? -2.701  11.807  20.255  0.50 12.71 ? 135 SER A C   1 
ATOM   1173 O  O   A SER A 1 134 ? -1.945  10.930  20.542  0.50 14.10 ? 135 SER A O   1 
ATOM   1174 O  O   B SER A 1 134 ? -1.984  10.943  20.749  0.50 13.72 ? 135 SER A O   1 
ATOM   1175 C  CB  A SER A 1 134 ? -3.264  11.006  17.896  0.50 12.38 ? 135 SER A CB  1 
ATOM   1176 C  CB  B SER A 1 134 ? -3.311  10.840  18.018  0.50 16.98 ? 135 SER A CB  1 
ATOM   1177 O  OG  A SER A 1 134 ? -2.208  11.858  17.468  0.50 12.04 ? 135 SER A OG  1 
ATOM   1178 O  OG  B SER A 1 134 ? -4.398  10.561  17.137  0.50 22.96 ? 135 SER A OG  1 
ATOM   1179 N  N   . GLN A 1 135 ? -2.547  13.111  20.518  1.00 12.04 ? 136 GLN A N   1 
ATOM   1180 C  CA  . GLN A 1 135 ? -1.525  13.582  21.452  1.00 13.17 ? 136 GLN A CA  1 
ATOM   1181 C  C   . GLN A 1 135 ? -2.062  13.695  22.876  1.00 12.67 ? 136 GLN A C   1 
ATOM   1182 O  O   . GLN A 1 135 ? -1.388  14.218  23.776  1.00 15.78 ? 136 GLN A O   1 
ATOM   1183 C  CB  . GLN A 1 135 ? -0.952  14.917  20.937  1.00 16.44 ? 136 GLN A CB  1 
ATOM   1184 C  CG  . GLN A 1 135 ? -0.505  14.821  19.508  1.00 20.16 ? 136 GLN A CG  1 
ATOM   1185 C  CD  . GLN A 1 135 ? 0.580   13.795  19.258  1.00 33.46 ? 136 GLN A CD  1 
ATOM   1186 O  OE1 . GLN A 1 135 ? 1.602   13.765  19.945  1.00 37.12 ? 136 GLN A OE1 1 
ATOM   1187 N  NE2 . GLN A 1 135 ? 0.362   12.945  18.263  1.00 37.92 ? 136 GLN A NE2 1 
ATOM   1188 N  N   . GLN A 1 136 ? -3.304  13.297  23.103  1.00 10.24 ? 137 GLN A N   1 
ATOM   1189 C  CA  . GLN A 1 136 ? -3.924  13.488  24.415  1.00 10.76 ? 137 GLN A CA  1 
ATOM   1190 C  C   . GLN A 1 136 ? -4.278  12.177  25.052  1.00 9.41  ? 137 GLN A C   1 
ATOM   1191 O  O   . GLN A 1 136 ? -4.657  11.222  24.365  1.00 9.25  ? 137 GLN A O   1 
ATOM   1192 C  CB  . GLN A 1 136 ? -5.221  14.292  24.285  1.00 11.13 ? 137 GLN A CB  1 
ATOM   1193 C  CG  . GLN A 1 136 ? -5.078  15.546  23.428  1.00 13.71 ? 137 GLN A CG  1 
ATOM   1194 C  CD  . GLN A 1 136 ? -4.087  16.494  23.985  1.00 15.94 ? 137 GLN A CD  1 
ATOM   1195 O  OE1 . GLN A 1 136 ? -3.869  16.570  25.180  1.00 17.09 ? 137 GLN A OE1 1 
ATOM   1196 N  NE2 . GLN A 1 136 ? -3.373  17.162  23.079  1.00 27.36 ? 137 GLN A NE2 1 
ATOM   1197 N  N   A PRO A 1 137 ? -4.310  12.082  26.388  0.50 9.69  ? 138 PRO A N   1 
ATOM   1198 N  N   B PRO A 1 137 ? -4.162  12.047  26.398  0.50 10.52 ? 138 PRO A N   1 
ATOM   1199 C  CA  A PRO A 1 137 ? -4.446  10.763  26.994  0.50 11.48 ? 138 PRO A CA  1 
ATOM   1200 C  CA  B PRO A 1 137 ? -4.490  10.787  27.073  0.50 11.89 ? 138 PRO A CA  1 
ATOM   1201 C  C   A PRO A 1 137 ? -5.892  10.285  26.955  0.50 10.82 ? 138 PRO A C   1 
ATOM   1202 C  C   B PRO A 1 137 ? -5.886  10.257  26.788  0.50 10.93 ? 138 PRO A C   1 
ATOM   1203 O  O   A PRO A 1 137 ? -6.114  9.125   27.237  0.50 12.89 ? 138 PRO A O   1 
ATOM   1204 O  O   B PRO A 1 137 ? -6.057  9.050   26.706  0.50 13.14 ? 138 PRO A O   1 
ATOM   1205 C  CB  A PRO A 1 137 ? -3.901  10.967  28.413  0.50 14.47 ? 138 PRO A CB  1 
ATOM   1206 C  CB  B PRO A 1 137 ? -4.361  11.108  28.566  0.50 14.01 ? 138 PRO A CB  1 
ATOM   1207 C  CG  A PRO A 1 137 ? -4.230  12.437  28.680  0.50 12.88 ? 138 PRO A CG  1 
ATOM   1208 C  CG  B PRO A 1 137 ? -3.224  12.104  28.547  0.50 15.26 ? 138 PRO A CG  1 
ATOM   1209 C  CD  A PRO A 1 137 ? -4.018  13.156  27.360  0.50 12.83 ? 138 PRO A CD  1 
ATOM   1210 C  CD  B PRO A 1 137 ? -3.478  12.984  27.322  0.50 11.98 ? 138 PRO A CD  1 
ATOM   1211 N  N   . ASP A 1 138 ? -6.832  11.177  26.615  1.00 9.70  ? 139 ASP A N   1 
ATOM   1212 C  CA  . ASP A 1 138 ? -8.230  10.833  26.373  1.00 9.84  ? 139 ASP A CA  1 
ATOM   1213 C  C   . ASP A 1 138 ? -8.639  11.284  24.975  1.00 8.73  ? 139 ASP A C   1 
ATOM   1214 O  O   . ASP A 1 138 ? -9.753  11.708  24.723  1.00 10.68 ? 139 ASP A O   1 
ATOM   1215 C  CB  . ASP A 1 138 ? -9.132  11.491  27.406  1.00 12.56 ? 139 ASP A CB  1 
ATOM   1216 C  CG  . ASP A 1 138 ? -9.063  12.995  27.417  1.00 12.87 ? 139 ASP A CG  1 
ATOM   1217 O  OD1 . ASP A 1 138 ? -8.115  13.606  26.803  1.00 12.78 ? 139 ASP A OD1 1 
ATOM   1218 O  OD2 . ASP A 1 138 ? -9.934  13.579  28.127  1.00 16.23 ? 139 ASP A OD2 1 
ATOM   1219 N  N   . GLY A 1 139 ? -7.694  11.168  24.031  1.00 7.48  ? 140 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 139 ? -7.975  11.689  22.701  1.00 7.93  ? 140 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 139 ? -8.809  10.778  21.811  1.00 5.97  ? 140 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 139 ? -9.547  11.290  20.963  1.00 6.94  ? 140 GLY A O   1 
ATOM   1223 N  N   . LEU A 1 140 ? -8.612  9.464   21.911  1.00 6.42  ? 141 LEU A N   1 
ATOM   1224 C  CA  . LEU A 1 140 ? -9.247  8.532   21.021  1.00 6.07  ? 141 LEU A CA  1 
ATOM   1225 C  C   . LEU A 1 140 ? -10.092 7.550   21.806  1.00 6.06  ? 141 LEU A C   1 
ATOM   1226 O  O   . LEU A 1 140 ? -9.756  7.228   22.947  1.00 6.89  ? 141 LEU A O   1 
ATOM   1227 C  CB  . LEU A 1 140 ? -8.253  7.764   20.168  1.00 7.29  ? 141 LEU A CB  1 
ATOM   1228 C  CG  . LEU A 1 140 ? -7.313  8.591   19.280  1.00 8.82  ? 141 LEU A CG  1 
ATOM   1229 C  CD1 . LEU A 1 140 ? -6.424  7.675   18.457  1.00 10.07 ? 141 LEU A CD1 1 
ATOM   1230 C  CD2 . LEU A 1 140 ? -8.044  9.575   18.379  1.00 9.82  ? 141 LEU A CD2 1 
ATOM   1231 N  N   . ALA A 1 141 ? -11.110 6.992   21.168  1.00 6.82  ? 142 ALA A N   1 
ATOM   1232 C  CA  . ALA A 1 141 ? -11.854 5.885   21.726  1.00 6.59  ? 142 ALA A CA  1 
ATOM   1233 C  C   . ALA A 1 141 ? -11.991 4.889   20.608  1.00 5.81  ? 142 ALA A C   1 
ATOM   1234 O  O   . ALA A 1 141 ? -12.399 5.223   19.482  1.00 7.04  ? 142 ALA A O   1 
ATOM   1235 C  CB  . ALA A 1 141 ? -13.203 6.307   22.196  1.00 8.22  ? 142 ALA A CB  1 
ATOM   1236 N  N   . VAL A 1 142 ? -11.564 3.641   20.891  1.00 6.31  ? 143 VAL A N   1 
ATOM   1237 C  CA  . VAL A 1 142 ? -11.656 2.578   19.899  1.00 5.94  ? 143 VAL A CA  1 
ATOM   1238 C  C   . VAL A 1 142 ? -12.656 1.559   20.403  1.00 5.27  ? 143 VAL A C   1 
ATOM   1239 O  O   . VAL A 1 142 ? -12.520 1.040   21.510  1.00 6.42  ? 143 VAL A O   1 
ATOM   1240 C  CB  . VAL A 1 142 ? -10.305 1.946   19.561  1.00 6.96  ? 143 VAL A CB  1 
ATOM   1241 C  CG1 . VAL A 1 142 ? -10.503 0.916   18.456  1.00 8.30  ? 143 VAL A CG1 1 
ATOM   1242 C  CG2 . VAL A 1 142 ? -9.340  2.996   19.079  1.00 8.51  ? 143 VAL A CG2 1 
ATOM   1243 N  N   . LEU A 1 143 ? -13.671 1.310   19.560  1.00 5.65  ? 144 LEU A N   1 
ATOM   1244 C  CA  . LEU A 1 143 ? -14.616 0.252   19.812  1.00 6.19  ? 144 LEU A CA  1 
ATOM   1245 C  C   . LEU A 1 143 ? -14.045 -0.983  19.146  1.00 6.01  ? 144 LEU A C   1 
ATOM   1246 O  O   . LEU A 1 143 ? -13.905 -1.014  17.920  1.00 7.52  ? 144 LEU A O   1 
ATOM   1247 C  CB  . LEU A 1 143 ? -15.990 0.689   19.253  1.00 8.01  ? 144 LEU A CB  1 
ATOM   1248 C  CG  . LEU A 1 143 ? -17.141 -0.266  19.443  1.00 10.06 ? 144 LEU A CG  1 
ATOM   1249 C  CD1 . LEU A 1 143 ? -17.361 -0.539  20.926  1.00 12.64 ? 144 LEU A CD1 1 
ATOM   1250 C  CD2 . LEU A 1 143 ? -18.400 0.337   18.813  1.00 11.90 ? 144 LEU A CD2 1 
ATOM   1251 N  N   . GLY A 1 144 ? -13.782 -2.002  19.935  1.00 6.04  ? 145 GLY A N   1 
ATOM   1252 C  CA  . GLY A 1 144 ? -13.196 -3.251  19.436  1.00 6.22  ? 145 GLY A CA  1 
ATOM   1253 C  C   . GLY A 1 144 ? -14.253 -4.345  19.459  1.00 5.61  ? 145 GLY A C   1 
ATOM   1254 O  O   . GLY A 1 144 ? -14.967 -4.491  20.428  1.00 6.86  ? 145 GLY A O   1 
ATOM   1255 N  N   . ILE A 1 145 ? -14.303 -5.073  18.356  1.00 5.24  ? 146 ILE A N   1 
ATOM   1256 C  CA  . ILE A 1 145 ? -15.319 -6.113  18.182  1.00 5.91  ? 146 ILE A CA  1 
ATOM   1257 C  C   . ILE A 1 145 ? -14.608 -7.354  17.663  1.00 5.80  ? 146 ILE A C   1 
ATOM   1258 O  O   . ILE A 1 145 ? -13.890 -7.306  16.668  1.00 6.48  ? 146 ILE A O   1 
ATOM   1259 C  CB  . ILE A 1 145 ? -16.411 -5.643  17.194  1.00 7.36  ? 146 ILE A CB  1 
ATOM   1260 C  CG1 . ILE A 1 145 ? -17.058 -4.373  17.740  1.00 8.94  ? 146 ILE A CG1 1 
ATOM   1261 C  CG2 . ILE A 1 145 ? -17.409 -6.756  16.978  1.00 8.70  ? 146 ILE A CG2 1 
ATOM   1262 C  CD1 . ILE A 1 145 ? -18.112 -3.782  16.835  1.00 9.46  ? 146 ILE A CD1 1 
ATOM   1263 N  N   . PHE A 1 146 ? -14.788 -8.472  18.355  1.00 5.79  ? 147 PHE A N   1 
ATOM   1264 C  CA  . PHE A 1 146 ? -14.167 -9.733  17.931  1.00 5.94  ? 147 PHE A CA  1 
ATOM   1265 C  C   . PHE A 1 146 ? -14.962 -10.339 16.787  1.00 6.32  ? 147 PHE A C   1 
ATOM   1266 O  O   . PHE A 1 146 ? -16.181 -10.230 16.723  1.00 7.64  ? 147 PHE A O   1 
ATOM   1267 C  CB  . PHE A 1 146 ? -14.183 -10.694 19.118  1.00 6.57  ? 147 PHE A CB  1 
ATOM   1268 C  CG  . PHE A 1 146 ? -13.326 -10.226 20.251  1.00 5.99  ? 147 PHE A CG  1 
ATOM   1269 C  CD1 . PHE A 1 146 ? -11.948 -10.067 20.069  1.00 6.46  ? 147 PHE A CD1 1 
ATOM   1270 C  CD2 . PHE A 1 146 ? -13.877 -9.980  21.509  1.00 7.01  ? 147 PHE A CD2 1 
ATOM   1271 C  CE1 . PHE A 1 146 ? -11.143 -9.690  21.127  1.00 7.09  ? 147 PHE A CE1 1 
ATOM   1272 C  CE2 . PHE A 1 146 ? -13.063 -9.605  22.578  1.00 7.18  ? 147 PHE A CE2 1 
ATOM   1273 C  CZ  . PHE A 1 146 ? -11.713 -9.451  22.372  1.00 6.93  ? 147 PHE A CZ  1 
ATOM   1274 N  N   . LEU A 1 147 ? -14.228 -11.042 15.928  1.00 6.21  ? 148 LEU A N   1 
ATOM   1275 C  CA  . LEU A 1 147 ? -14.829 -11.826 14.844  1.00 7.00  ? 148 LEU A CA  1 
ATOM   1276 C  C   . LEU A 1 147 ? -14.488 -13.282 15.063  1.00 6.88  ? 148 LEU A C   1 
ATOM   1277 O  O   . LEU A 1 147 ? -13.311 -13.643 15.270  1.00 7.47  ? 148 LEU A O   1 
ATOM   1278 C  CB  . LEU A 1 147 ? -14.207 -11.430 13.474  1.00 7.59  ? 148 LEU A CB  1 
ATOM   1279 C  CG  . LEU A 1 147 ? -14.778 -10.173 12.839  1.00 9.09  ? 148 LEU A CG  1 
ATOM   1280 C  CD1 . LEU A 1 147 ? -14.617 -8.899  13.692  1.00 11.03 ? 148 LEU A CD1 1 
ATOM   1281 C  CD2 . LEU A 1 147 ? -14.166 -9.954  11.434  1.00 10.70 ? 148 LEU A CD2 1 
ATOM   1282 N  N   . LYS A 1 148 ? -15.516 -14.133 14.989  1.00 7.27  ? 149 LYS A N   1 
ATOM   1283 C  CA  . LYS A 1 148 ? -15.295 -15.576 14.954  1.00 7.77  ? 149 LYS A CA  1 
ATOM   1284 C  C   . LYS A 1 148 ? -15.805 -16.082 13.615  1.00 8.76  ? 149 LYS A C   1 
ATOM   1285 O  O   . LYS A 1 148 ? -16.627 -15.430 12.958  1.00 9.89  ? 149 LYS A O   1 
ATOM   1286 C  CB  . LYS A 1 148 ? -16.028 -16.286 16.088  1.00 9.60  ? 149 LYS A CB  1 
ATOM   1287 C  CG  . LYS A 1 148 ? -17.534 -16.154 16.058  1.00 11.89 ? 149 LYS A CG  1 
ATOM   1288 C  CD  . LYS A 1 148 ? -18.174 -16.819 17.321  1.00 18.30 ? 149 LYS A CD  1 
ATOM   1289 C  CE  . LYS A 1 148 ? -19.602 -17.206 17.059  1.00 27.18 ? 149 LYS A CE  1 
ATOM   1290 N  NZ  . LYS A 1 148 ? -20.179 -17.831 18.272  1.00 35.16 ? 149 LYS A NZ  1 
ATOM   1291 N  N   . VAL A 1 149 ? -15.305 -17.235 13.193  1.00 9.52  ? 150 VAL A N   1 
ATOM   1292 C  CA  . VAL A 1 149 ? -15.701 -17.827 11.912  1.00 9.74  ? 150 VAL A CA  1 
ATOM   1293 C  C   . VAL A 1 149 ? -16.893 -18.743 12.127  1.00 9.72  ? 150 VAL A C   1 
ATOM   1294 O  O   . VAL A 1 149 ? -16.868 -19.689 12.922  1.00 10.99 ? 150 VAL A O   1 
ATOM   1295 C  CB  . VAL A 1 149 ? -14.497 -18.557 11.298  1.00 10.29 ? 150 VAL A CB  1 
ATOM   1296 C  CG1 . VAL A 1 149 ? -14.918 -19.328 10.049  1.00 12.15 ? 150 VAL A CG1 1 
ATOM   1297 C  CG2 . VAL A 1 149 ? -13.392 -17.587 10.994  1.00 12.60 ? 150 VAL A CG2 1 
ATOM   1298 N  N   . GLY A 1 150 ? -17.960 -18.484 11.383  1.00 9.68  ? 151 GLY A N   1 
ATOM   1299 C  CA  . GLY A 1 150 ? -19.176 -19.287 11.437  1.00 11.54 ? 151 GLY A CA  1 
ATOM   1300 C  C   . GLY A 1 150 ? -20.054 -18.845 10.306  1.00 10.59 ? 151 GLY A C   1 
ATOM   1301 O  O   . GLY A 1 150 ? -19.675 -18.915 9.140   1.00 12.09 ? 151 GLY A O   1 
ATOM   1302 N  N   A SER A 1 151 ? -21.263 -18.374 10.626  0.50 11.64 ? 152 SER A N   1 
ATOM   1303 N  N   B SER A 1 151 ? -21.224 -18.311 10.678  0.50 12.16 ? 152 SER A N   1 
ATOM   1304 C  CA  A SER A 1 151 ? -22.136 -17.850 9.570   0.50 13.21 ? 152 SER A CA  1 
ATOM   1305 C  CA  B SER A 1 151 ? -22.122 -17.692 9.701   0.50 13.27 ? 152 SER A CA  1 
ATOM   1306 C  C   A SER A 1 151 ? -21.605 -16.491 9.112   0.50 11.52 ? 152 SER A C   1 
ATOM   1307 C  C   B SER A 1 151 ? -21.426 -16.493 9.052   0.50 12.46 ? 152 SER A C   1 
ATOM   1308 O  O   A SER A 1 151 ? -21.015 -15.740 9.906   0.50 10.16 ? 152 SER A O   1 
ATOM   1309 O  O   B SER A 1 151 ? -20.554 -15.842 9.640   0.50 9.95  ? 152 SER A O   1 
ATOM   1310 C  CB  A SER A 1 151 ? -23.508 -17.698 10.089  0.50 16.95 ? 152 SER A CB  1 
ATOM   1311 C  CB  B SER A 1 151 ? -23.399 -17.281 10.361  0.50 16.40 ? 152 SER A CB  1 
ATOM   1312 O  OG  A SER A 1 151 ? -23.507 -16.694 11.086  0.50 17.85 ? 152 SER A OG  1 
ATOM   1313 O  OG  B SER A 1 151 ? -24.047 -18.414 10.938  0.50 18.63 ? 152 SER A OG  1 
ATOM   1314 N  N   . ALA A 1 152 ? -21.873 -16.156 7.838   1.00 11.58 ? 153 ALA A N   1 
ATOM   1315 C  CA  . ALA A 1 152 ? -21.480 -14.914 7.239   1.00 12.37 ? 153 ALA A CA  1 
ATOM   1316 C  C   . ALA A 1 152 ? -22.117 -13.706 7.929   1.00 11.43 ? 153 ALA A C   1 
ATOM   1317 O  O   . ALA A 1 152 ? -23.244 -13.801 8.435   1.00 13.96 ? 153 ALA A O   1 
ATOM   1318 C  CB  . ALA A 1 152 ? -21.870 -14.918 5.765   1.00 15.59 ? 153 ALA A CB  1 
ATOM   1319 N  N   . LYS A 1 153 ? -21.387 -12.579 7.888   1.00 11.99 ? 154 LYS A N   1 
ATOM   1320 C  CA  . LYS A 1 153 ? -21.979 -11.327 8.337   1.00 12.56 ? 154 LYS A CA  1 
ATOM   1321 C  C   . LYS A 1 153 ? -22.393 -10.574 7.070   1.00 11.98 ? 154 LYS A C   1 
ATOM   1322 O  O   . LYS A 1 153 ? -21.557 -10.107 6.297   1.00 12.52 ? 154 LYS A O   1 
ATOM   1323 C  CB  . LYS A 1 153 ? -20.951 -10.525 9.120   1.00 12.88 ? 154 LYS A CB  1 
ATOM   1324 C  CG  . LYS A 1 153 ? -21.486 -9.350  9.949   1.00 14.83 ? 154 LYS A CG  1 
ATOM   1325 C  CD  . LYS A 1 153 ? -22.461 -9.743  11.106  1.00 17.62 ? 154 LYS A CD  1 
ATOM   1326 C  CE  . LYS A 1 153 ? -22.653 -8.643  12.137  1.00 19.37 ? 154 LYS A CE  1 
ATOM   1327 N  NZ  . LYS A 1 153 ? -23.918 -8.978  12.834  1.00 30.19 ? 154 LYS A NZ  1 
ATOM   1328 N  N   . PRO A 1 154 ? -23.708 -10.461 6.783   1.00 13.18 ? 155 PRO A N   1 
ATOM   1329 C  CA  . PRO A 1 154 ? -24.133 -9.861  5.507   1.00 14.87 ? 155 PRO A CA  1 
ATOM   1330 C  C   . PRO A 1 154 ? -23.603 -8.422  5.358   1.00 14.18 ? 155 PRO A C   1 
ATOM   1331 O  O   . PRO A 1 154 ? -23.214 -8.051  4.265   1.00 15.98 ? 155 PRO A O   1 
ATOM   1332 C  CB  . PRO A 1 154 ? -25.659 -9.887  5.633   1.00 17.29 ? 155 PRO A CB  1 
ATOM   1333 C  CG  . PRO A 1 154 ? -25.945 -11.084 6.543   1.00 19.45 ? 155 PRO A CG  1 
ATOM   1334 C  CD  . PRO A 1 154 ? -24.829 -11.015 7.572   1.00 14.01 ? 155 PRO A CD  1 
ATOM   1335 N  N   . GLY A 1 155 ? -23.545 -7.677  6.478   1.00 14.82 ? 156 GLY A N   1 
ATOM   1336 C  CA  . GLY A 1 155 ? -23.171 -6.282  6.429   1.00 16.12 ? 156 GLY A CA  1 
ATOM   1337 C  C   . GLY A 1 155 ? -21.700 -6.099  6.169   1.00 14.90 ? 156 GLY A C   1 
ATOM   1338 O  O   . GLY A 1 155 ? -21.228 -4.986  5.948   1.00 18.69 ? 156 GLY A O   1 
ATOM   1339 N  N   . LEU A 1 156 ? -20.939 -7.178  6.233   1.00 14.58 ? 157 LEU A N   1 
ATOM   1340 C  CA  . LEU A 1 156 ? -19.532 -7.139  5.903   1.00 12.69 ? 157 LEU A CA  1 
ATOM   1341 C  C   . LEU A 1 156 ? -19.243 -7.321  4.419   1.00 14.26 ? 157 LEU A C   1 
ATOM   1342 O  O   . LEU A 1 156 ? -18.153 -7.048  3.935   1.00 13.39 ? 157 LEU A O   1 
ATOM   1343 C  CB  . LEU A 1 156 ? -18.734 -8.147  6.750   1.00 13.25 ? 157 LEU A CB  1 
ATOM   1344 C  CG  . LEU A 1 156 ? -17.200 -8.262  6.572   1.00 13.10 ? 157 LEU A CG  1 
ATOM   1345 C  CD1 . LEU A 1 156 ? -16.411 -6.964  6.929   1.00 15.75 ? 157 LEU A CD1 1 
ATOM   1346 C  CD2 . LEU A 1 156 ? -16.569 -9.418  7.342   1.00 14.01 ? 157 LEU A CD2 1 
ATOM   1347 N  N   . GLN A 1 157 ? -20.204 -7.908  3.686   1.00 14.09 ? 158 GLN A N   1 
ATOM   1348 C  CA  . GLN A 1 157 ? -19.866 -8.381  2.346   1.00 15.68 ? 158 GLN A CA  1 
ATOM   1349 C  C   . GLN A 1 157 ? -19.452 -7.242  1.407   1.00 14.43 ? 158 GLN A C   1 
ATOM   1350 O  O   . GLN A 1 157 ? -18.589 -7.455  0.573   1.00 14.14 ? 158 GLN A O   1 
ATOM   1351 C  CB  . GLN A 1 157 ? -21.048 -9.173  1.802   1.00 17.75 ? 158 GLN A CB  1 
ATOM   1352 C  CG  . GLN A 1 157 ? -20.688 -9.921  0.518   1.00 18.78 ? 158 GLN A CG  1 
ATOM   1353 C  CD  . GLN A 1 157 ? -19.613 -10.952 0.736   1.00 16.84 ? 158 GLN A CD  1 
ATOM   1354 O  OE1 . GLN A 1 157 ? -19.482 -11.516 1.839   1.00 16.58 ? 158 GLN A OE1 1 
ATOM   1355 N  NE2 . GLN A 1 157 ? -18.822 -11.232 -0.303  1.00 20.52 ? 158 GLN A NE2 1 
ATOM   1356 N  N   . LYS A 1 158 ? -20.005 -6.021  1.546   1.00 15.88 ? 159 LYS A N   1 
ATOM   1357 C  CA  . LYS A 1 158 ? -19.627 -4.935  0.664   1.00 14.91 ? 159 LYS A CA  1 
ATOM   1358 C  C   . LYS A 1 158 ? -18.139 -4.645  0.841   1.00 14.87 ? 159 LYS A C   1 
ATOM   1359 O  O   . LYS A 1 158 ? -17.492 -4.205  -0.109  1.00 16.20 ? 159 LYS A O   1 
ATOM   1360 C  CB  . LYS A 1 158 ? -20.582 -3.756  0.917   1.00 16.45 ? 159 LYS A CB  1 
ATOM   1361 C  CG  . LYS A 1 158 ? -21.955 -3.992  0.262   1.00 20.36 ? 159 LYS A CG  1 
ATOM   1362 N  N   . VAL A 1 159 ? -17.646 -4.796  2.079   1.00 13.52 ? 160 VAL A N   1 
ATOM   1363 C  CA  . VAL A 1 159 ? -16.239 -4.558  2.317   1.00 12.93 ? 160 VAL A CA  1 
ATOM   1364 C  C   . VAL A 1 159 ? -15.420 -5.659  1.645   1.00 13.58 ? 160 VAL A C   1 
ATOM   1365 O  O   . VAL A 1 159 ? -14.471 -5.432  0.907   1.00 14.20 ? 160 VAL A O   1 
ATOM   1366 C  CB  . VAL A 1 159 ? -15.936 -4.528  3.813   1.00 13.29 ? 160 VAL A CB  1 
ATOM   1367 C  CG1 . VAL A 1 159 ? -14.440 -4.553  4.058   1.00 14.67 ? 160 VAL A CG1 1 
ATOM   1368 C  CG2 . VAL A 1 159 ? -16.593 -3.339  4.479   1.00 15.85 ? 160 VAL A CG2 1 
ATOM   1369 N  N   . VAL A 1 160 ? -15.777 -6.918  1.890   1.00 13.26 ? 161 VAL A N   1 
ATOM   1370 C  CA  . VAL A 1 160 ? -14.995 -8.009  1.328   1.00 15.22 ? 161 VAL A CA  1 
ATOM   1371 C  C   . VAL A 1 160 ? -14.928 -7.926  -0.198  1.00 14.75 ? 161 VAL A C   1 
ATOM   1372 O  O   . VAL A 1 160 ? -13.921 -8.267  -0.778  1.00 16.14 ? 161 VAL A O   1 
ATOM   1373 C  CB  . VAL A 1 160 ? -15.586 -9.371  1.824   1.00 21.19 ? 161 VAL A CB  1 
ATOM   1374 C  CG1 . VAL A 1 160 ? -15.383 -10.588 0.924   1.00 22.14 ? 161 VAL A CG1 1 
ATOM   1375 C  CG2 . VAL A 1 160 ? -15.291 -9.526  3.309   1.00 22.18 ? 161 VAL A CG2 1 
ATOM   1376 N  N   . ASP A 1 161 ? -16.046 -7.533  -0.802  1.00 16.47 ? 162 ASP A N   1 
ATOM   1377 C  CA  . ASP A 1 161 ? -16.100 -7.599  -2.266  1.00 18.78 ? 162 ASP A CA  1 
ATOM   1378 C  C   . ASP A 1 161 ? -15.246 -6.517  -2.924  1.00 18.36 ? 162 ASP A C   1 
ATOM   1379 O  O   . ASP A 1 161 ? -14.920 -6.650  -4.104  1.00 24.48 ? 162 ASP A O   1 
ATOM   1380 C  CB  . ASP A 1 161 ? -17.551 -7.472  -2.671  1.00 20.94 ? 162 ASP A CB  1 
ATOM   1381 C  CG  . ASP A 1 161 ? -18.257 -8.840  -2.652  1.00 20.19 ? 162 ASP A CG  1 
ATOM   1382 O  OD1 . ASP A 1 161 ? -17.535 -9.895  -2.807  1.00 25.77 ? 162 ASP A OD1 1 
ATOM   1383 O  OD2 . ASP A 1 161 ? -19.501 -8.845  -2.467  1.00 26.08 ? 162 ASP A OD2 1 
ATOM   1384 N  N   . VAL A 1 162 ? -14.825 -5.463  -2.213  1.00 18.92 ? 163 VAL A N   1 
ATOM   1385 C  CA  . VAL A 1 162 ? -13.996 -4.409  -2.791  1.00 20.32 ? 163 VAL A CA  1 
ATOM   1386 C  C   . VAL A 1 162 ? -12.507 -4.731  -2.601  1.00 18.94 ? 163 VAL A C   1 
ATOM   1387 O  O   . VAL A 1 162 ? -11.653 -4.070  -3.163  1.00 20.39 ? 163 VAL A O   1 
ATOM   1388 C  CB  . VAL A 1 162 ? -14.429 -3.029  -2.230  1.00 23.15 ? 163 VAL A CB  1 
ATOM   1389 C  CG1 . VAL A 1 162 ? -13.823 -2.745  -0.891  1.00 21.49 ? 163 VAL A CG1 1 
ATOM   1390 C  CG2 . VAL A 1 162 ? -14.296 -1.822  -3.131  1.00 23.72 ? 163 VAL A CG2 1 
ATOM   1391 N  N   . LEU A 1 163 ? -12.172 -5.748  -1.784  1.00 17.77 ? 164 LEU A N   1 
ATOM   1392 C  CA  . LEU A 1 163 ? -10.771 -5.919  -1.446  1.00 15.87 ? 164 LEU A CA  1 
ATOM   1393 C  C   . LEU A 1 163 ? -9.864  -6.264  -2.619  1.00 17.00 ? 164 LEU A C   1 
ATOM   1394 O  O   . LEU A 1 163 ? -8.655  -5.948  -2.632  1.00 17.53 ? 164 LEU A O   1 
ATOM   1395 C  CB  . LEU A 1 163 ? -10.616 -6.957  -0.337  1.00 15.44 ? 164 LEU A CB  1 
ATOM   1396 C  CG  . LEU A 1 163 ? -11.237 -6.606  1.024   1.00 14.05 ? 164 LEU A CG  1 
ATOM   1397 C  CD1 . LEU A 1 163 ? -10.955 -7.741  2.004   1.00 16.48 ? 164 LEU A CD1 1 
ATOM   1398 C  CD2 . LEU A 1 163 ? -10.620 -5.301  1.543   1.00 14.50 ? 164 LEU A CD2 1 
ATOM   1399 N  N   . ASP A 1 164 ? -10.433 -6.926  -3.651  1.00 20.01 ? 165 ASP A N   1 
ATOM   1400 C  CA  . ASP A 1 164 ? -9.589  -7.286  -4.795  1.00 24.30 ? 165 ASP A CA  1 
ATOM   1401 C  C   . ASP A 1 164 ? -9.103  -6.013  -5.492  1.00 23.44 ? 165 ASP A C   1 
ATOM   1402 O  O   . ASP A 1 164 ? -8.104  -6.080  -6.215  1.00 31.25 ? 165 ASP A O   1 
ATOM   1403 C  CB  . ASP A 1 164 ? -10.306 -8.224  -5.773  1.00 29.47 ? 165 ASP A CB  1 
ATOM   1404 C  CG  . ASP A 1 164 ? -11.337 -7.469  -6.595  1.00 37.24 ? 165 ASP A CG  1 
ATOM   1405 O  OD1 . ASP A 1 164 ? -12.309 -6.945  -5.986  1.00 34.21 ? 165 ASP A OD1 1 
ATOM   1406 O  OD2 . ASP A 1 164 ? -11.153 -7.357  -7.819  1.00 49.55 ? 165 ASP A OD2 1 
ATOM   1407 N  N   . SER A 1 165 ? -9.797  -4.876  -5.299  1.00 20.76 ? 166 SER A N   1 
ATOM   1408 C  CA  . SER A 1 165 ? -9.438  -3.623  -5.950  1.00 22.51 ? 166 SER A CA  1 
ATOM   1409 C  C   . SER A 1 165 ? -8.406  -2.858  -5.123  1.00 20.47 ? 166 SER A C   1 
ATOM   1410 O  O   . SER A 1 165 ? -7.843  -1.862  -5.595  1.00 21.92 ? 166 SER A O   1 
ATOM   1411 C  CB  . SER A 1 165 ? -10.649 -2.764  -6.196  1.00 27.86 ? 166 SER A CB  1 
ATOM   1412 O  OG  . SER A 1 165 ? -11.068 -2.166  -4.976  1.00 24.48 ? 166 SER A OG  1 
ATOM   1413 N  N   . ILE A 1 166 ? -8.158  -3.326  -3.906  1.00 18.77 ? 167 ILE A N   1 
ATOM   1414 C  CA  . ILE A 1 166 ? -7.167  -2.704  -3.041  1.00 16.03 ? 167 ILE A CA  1 
ATOM   1415 C  C   . ILE A 1 166 ? -6.140  -3.726  -2.544  1.00 16.84 ? 167 ILE A C   1 
ATOM   1416 O  O   . ILE A 1 166 ? -5.698  -3.750  -1.382  1.00 17.72 ? 167 ILE A O   1 
ATOM   1417 C  CB  . ILE A 1 166 ? -7.743  -1.818  -1.912  1.00 18.75 ? 167 ILE A CB  1 
ATOM   1418 C  CG1 . ILE A 1 166 ? -8.679  -2.639  -1.015  1.00 15.57 ? 167 ILE A CG1 1 
ATOM   1419 C  CG2 . ILE A 1 166 ? -8.422  -0.606  -2.509  1.00 20.92 ? 167 ILE A CG2 1 
ATOM   1420 C  CD1 . ILE A 1 166 ? -8.576  -2.118  0.407   1.00 17.68 ? 167 ILE A CD1 1 
ATOM   1421 N  N   . LYS A 1 167 ? -5.702  -4.609  -3.442  1.00 16.40 ? 168 LYS A N   1 
ATOM   1422 C  CA  . LYS A 1 167 ? -4.961  -5.776  -3.044  1.00 15.35 ? 168 LYS A CA  1 
ATOM   1423 C  C   . LYS A 1 167 ? -3.627  -5.432  -2.398  1.00 15.99 ? 168 LYS A C   1 
ATOM   1424 O  O   . LYS A 1 167 ? -3.229  -6.068  -1.433  1.00 16.26 ? 168 LYS A O   1 
ATOM   1425 C  CB  . LYS A 1 167 ? -4.816  -6.715  -4.230  1.00 17.53 ? 168 LYS A CB  1 
ATOM   1426 C  CG  . LYS A 1 167 ? -3.999  -7.939  -3.865  1.00 18.71 ? 168 LYS A CG  1 
ATOM   1427 C  CD  . LYS A 1 167 ? -3.768  -8.763  -5.146  1.00 21.92 ? 168 LYS A CD  1 
ATOM   1428 C  CE  . LYS A 1 167 ? -2.898  -9.951  -4.894  1.00 27.92 ? 168 LYS A CE  1 
ATOM   1429 N  N   A THR A 1 168 ? -3.171  -4.265  -2.847  0.50 13.54 ? 169 THR A N   1 
ATOM   1430 N  N   B THR A 1 168 ? -2.775  -4.516  -2.939  0.50 21.06 ? 169 THR A N   1 
ATOM   1431 C  CA  A THR A 1 168 ? -1.801  -3.899  -2.594  0.50 14.17 ? 169 THR A CA  1 
ATOM   1432 C  CA  B THR A 1 168 ? -1.379  -4.328  -2.474  0.50 21.42 ? 169 THR A CA  1 
ATOM   1433 C  C   A THR A 1 168 ? -1.764  -2.546  -1.882  0.50 11.69 ? 169 THR A C   1 
ATOM   1434 C  C   B THR A 1 168 ? -1.135  -2.970  -1.793  0.50 20.15 ? 169 THR A C   1 
ATOM   1435 O  O   A THR A 1 168 ? -2.665  -1.704  -1.960  0.50 13.43 ? 169 THR A O   1 
ATOM   1436 O  O   B THR A 1 168 ? -1.925  -2.052  -1.972  0.50 23.53 ? 169 THR A O   1 
ATOM   1437 C  CB  A THR A 1 168 ? -0.881  -4.030  -3.820  0.50 16.00 ? 169 THR A CB  1 
ATOM   1438 C  CB  B THR A 1 168 ? -0.318  -4.479  -3.589  0.50 22.32 ? 169 THR A CB  1 
ATOM   1439 O  OG1 A THR A 1 168 ? -1.535  -3.276  -4.828  0.50 16.68 ? 169 THR A OG1 1 
ATOM   1440 O  OG1 B THR A 1 168 ? -0.657  -3.607  -4.660  0.50 22.14 ? 169 THR A OG1 1 
ATOM   1441 C  CG2 A THR A 1 168 ? -0.749  -5.469  -4.288  0.50 17.04 ? 169 THR A CG2 1 
ATOM   1442 C  CG2 B THR A 1 168 ? -0.261  -5.889  -4.147  0.50 23.29 ? 169 THR A CG2 1 
ATOM   1443 N  N   A LYS A 1 169 ? -0.691  -2.428  -1.129  0.50 14.66 ? 170 LYS A N   1 
ATOM   1444 N  N   B LYS A 1 169 ? -0.009  -2.840  -1.056  0.50 19.04 ? 170 LYS A N   1 
ATOM   1445 C  CA  A LYS A 1 169 ? -0.359  -1.259  -0.363  0.50 11.66 ? 170 LYS A CA  1 
ATOM   1446 C  CA  B LYS A 1 169 ? 0.357   -1.669  -0.264  0.50 19.90 ? 170 LYS A CA  1 
ATOM   1447 C  C   A LYS A 1 169 ? -0.511  0.000   -1.209  0.50 13.81 ? 170 LYS A C   1 
ATOM   1448 C  C   B LYS A 1 169 ? 0.338   -0.426  -1.141  0.50 18.35 ? 170 LYS A C   1 
ATOM   1449 O  O   A LYS A 1 169 ? 0.000   0.094   -2.333  0.50 15.39 ? 170 LYS A O   1 
ATOM   1450 O  O   B LYS A 1 169 ? 1.038   -0.364  -2.153  0.50 21.18 ? 170 LYS A O   1 
ATOM   1451 C  CB  A LYS A 1 169 ? 1.078   -1.394  0.107   0.50 12.22 ? 170 LYS A CB  1 
ATOM   1452 C  CB  B LYS A 1 169 ? 1.768   -1.791  0.320   0.50 21.53 ? 170 LYS A CB  1 
ATOM   1453 C  CG  A LYS A 1 169 ? 1.655   -0.141  0.765   0.50 16.47 ? 170 LYS A CG  1 
ATOM   1454 C  CG  B LYS A 1 169 ? 2.204   -0.619  1.195   0.50 20.30 ? 170 LYS A CG  1 
ATOM   1455 C  CD  A LYS A 1 169 ? 2.974   -0.405  1.442   0.50 16.89 ? 170 LYS A CD  1 
ATOM   1456 C  CD  B LYS A 1 169 ? 3.628   -0.745  1.701   0.50 23.95 ? 170 LYS A CD  1 
ATOM   1457 C  CE  A LYS A 1 169 ? 4.037   -1.026  0.545   0.50 20.58 ? 170 LYS A CE  1 
ATOM   1458 C  CE  B LYS A 1 169 ? 4.040   0.503   2.447   0.50 27.70 ? 170 LYS A CE  1 
ATOM   1459 N  NZ  A LYS A 1 169 ? 5.345   -1.229  1.221   0.50 22.22 ? 170 LYS A NZ  1 
ATOM   1460 N  NZ  B LYS A 1 169 ? 5.495   0.812   2.349   0.50 33.02 ? 170 LYS A NZ  1 
ATOM   1461 N  N   A GLY A 1 170 ? -1.291  0.948   -0.679  0.50 14.50 ? 171 GLY A N   1 
ATOM   1462 N  N   B GLY A 1 170 ? -0.401  0.580   -0.686  0.50 19.33 ? 171 GLY A N   1 
ATOM   1463 C  CA  A GLY A 1 170 ? -1.478  2.252   -1.292  0.50 13.85 ? 171 GLY A CA  1 
ATOM   1464 C  CA  B GLY A 1 170 ? -0.450  1.861   -1.374  0.50 20.83 ? 171 GLY A CA  1 
ATOM   1465 C  C   A GLY A 1 170 ? -2.717  2.372   -2.178  0.50 13.60 ? 171 GLY A C   1 
ATOM   1466 C  C   B GLY A 1 170 ? -1.677  2.010   -2.268  0.50 20.24 ? 171 GLY A C   1 
ATOM   1467 O  O   A GLY A 1 170 ? -3.062  3.494   -2.582  0.50 18.63 ? 171 GLY A O   1 
ATOM   1468 O  O   B GLY A 1 170 ? -1.903  3.108   -2.792  0.50 23.76 ? 171 GLY A O   1 
ATOM   1469 N  N   A LYS A 1 171 ? -3.320  1.236   -2.538  0.50 16.59 ? 172 LYS A N   1 
ATOM   1470 N  N   B LYS A 1 171 ? -2.487  0.946   -2.401  0.50 19.24 ? 172 LYS A N   1 
ATOM   1471 C  CA  A LYS A 1 171 ? -4.546  1.256   -3.322  0.50 17.03 ? 172 LYS A CA  1 
ATOM   1472 C  CA  B LYS A 1 171 ? -3.674  1.046   -3.243  0.50 20.84 ? 172 LYS A CA  1 
ATOM   1473 C  C   A LYS A 1 171 ? -5.698  1.704   -2.424  0.50 13.42 ? 172 LYS A C   1 
ATOM   1474 C  C   B LYS A 1 171 ? -4.857  1.557   -2.434  0.50 21.33 ? 172 LYS A C   1 
ATOM   1475 O  O   A LYS A 1 171 ? -5.796  1.275   -1.283  0.50 16.28 ? 172 LYS A O   1 
ATOM   1476 O  O   B LYS A 1 171 ? -5.037  1.194   -1.275  0.50 23.08 ? 172 LYS A O   1 
ATOM   1477 C  CB  A LYS A 1 171 ? -4.771  -0.097  -3.980  0.50 16.52 ? 172 LYS A CB  1 
ATOM   1478 C  CB  B LYS A 1 171 ? -4.047  -0.251  -3.962  0.50 19.04 ? 172 LYS A CB  1 
ATOM   1479 C  CG  A LYS A 1 171 ? -3.589  -0.612  -4.788  0.50 20.60 ? 172 LYS A CG  1 
ATOM   1480 C  CG  B LYS A 1 171 ? -3.125  -0.628  -5.123  0.50 26.63 ? 172 LYS A CG  1 
ATOM   1481 C  CD  A LYS A 1 171 ? -3.938  -1.498  -5.974  0.50 29.43 ? 172 LYS A CD  1 
ATOM   1482 C  CD  B LYS A 1 171 ? -3.665  -1.710  -6.091  0.50 28.27 ? 172 LYS A CD  1 
ATOM   1483 C  CE  A LYS A 1 171 ? -3.521  -0.924  -7.314  0.50 28.43 ? 172 LYS A CE  1 
ATOM   1484 C  CE  B LYS A 1 171 ? -4.785  -1.198  -6.983  0.50 31.52 ? 172 LYS A CE  1 
ATOM   1485 N  NZ  A LYS A 1 171 ? -4.613  -1.091  -8.306  0.50 37.55 ? 172 LYS A NZ  1 
ATOM   1486 N  NZ  B LYS A 1 171 ? -5.381  -2.235  -7.878  0.50 32.81 ? 172 LYS A NZ  1 
ATOM   1487 N  N   A SER A 1 172 ? -6.610  2.505   -2.985  0.50 14.48 ? 173 SER A N   1 
ATOM   1488 N  N   B SER A 1 172 ? -5.670  2.389   -3.089  0.50 19.38 ? 173 SER A N   1 
ATOM   1489 C  CA  A SER A 1 172 ? -7.853  2.983   -2.397  0.50 17.12 ? 173 SER A CA  1 
ATOM   1490 C  CA  B SER A 1 172 ? -6.891  2.890   -2.493  0.50 19.51 ? 173 SER A CA  1 
ATOM   1491 C  C   A SER A 1 172 ? -8.987  2.825   -3.407  0.50 14.11 ? 173 SER A C   1 
ATOM   1492 C  C   B SER A 1 172 ? -7.991  2.951   -3.563  0.50 20.26 ? 173 SER A C   1 
ATOM   1493 O  O   A SER A 1 172 ? -8.766  2.746   -4.637  0.50 17.29 ? 173 SER A O   1 
ATOM   1494 O  O   B SER A 1 172 ? -7.691  2.942   -4.773  0.50 22.75 ? 173 SER A O   1 
ATOM   1495 C  CB  A SER A 1 172 ? -7.727  4.425   -1.921  0.50 14.71 ? 173 SER A CB  1 
ATOM   1496 C  CB  B SER A 1 172 ? -6.629  4.226   -1.810  0.50 16.96 ? 173 SER A CB  1 
ATOM   1497 O  OG  A SER A 1 172 ? -7.411  5.354   -2.950  0.50 16.47 ? 173 SER A OG  1 
ATOM   1498 O  OG  B SER A 1 172 ? -6.093  5.198   -2.726  0.50 13.37 ? 173 SER A OG  1 
ATOM   1499 N  N   A ALA A 1 173 ? -10.214 2.778   -2.876  0.50 16.43 ? 174 ALA A N   1 
ATOM   1500 N  N   B ALA A 1 173 ? -9.253  3.043   -3.079  0.50 19.03 ? 174 ALA A N   1 
ATOM   1501 C  CA  A ALA A 1 173 ? -11.367 2.781   -3.762  0.50 15.60 ? 174 ALA A CA  1 
ATOM   1502 C  CA  B ALA A 1 173 ? -10.431 3.175   -3.947  0.50 20.25 ? 174 ALA A CA  1 
ATOM   1503 C  C   A ALA A 1 173 ? -12.465 3.655   -3.170  0.50 15.30 ? 174 ALA A C   1 
ATOM   1504 C  C   B ALA A 1 173 ? -11.541 3.929   -3.208  0.50 23.91 ? 174 ALA A C   1 
ATOM   1505 O  O   A ALA A 1 173 ? -12.643 3.740   -1.945  0.50 12.05 ? 174 ALA A O   1 
ATOM   1506 O  O   B ALA A 1 173 ? -11.552 3.953   -1.973  0.50 14.35 ? 174 ALA A O   1 
ATOM   1507 C  CB  A ALA A 1 173 ? -11.856 1.362   -3.924  0.50 17.76 ? 174 ALA A CB  1 
ATOM   1508 C  CB  B ALA A 1 173 ? -10.863 1.751   -4.300  0.50 17.93 ? 174 ALA A CB  1 
ATOM   1509 N  N   A ASP A 1 174 ? -13.216 4.238   -4.099  0.50 21.26 ? 175 ASP A N   1 
ATOM   1510 N  N   B ASP A 1 174 ? -12.532 4.450   -3.954  0.50 30.64 ? 175 ASP A N   1 
ATOM   1511 C  CA  A ASP A 1 174 ? -14.400 5.042   -3.739  0.50 25.64 ? 175 ASP A CA  1 
ATOM   1512 C  CA  B ASP A 1 174 ? -13.718 5.149   -3.364  0.50 40.07 ? 175 ASP A CA  1 
ATOM   1513 C  C   A ASP A 1 174 ? -15.284 4.144   -2.911  0.50 26.40 ? 175 ASP A C   1 
ATOM   1514 C  C   B ASP A 1 174 ? -14.611 4.090   -2.687  0.50 22.90 ? 175 ASP A C   1 
ATOM   1515 O  O   A ASP A 1 174 ? -15.489 2.993   -3.343  0.50 19.70 ? 175 ASP A O   1 
ATOM   1516 O  O   B ASP A 1 174 ? -14.468 2.904   -3.046  0.50 18.75 ? 175 ASP A O   1 
ATOM   1517 C  CB  A ASP A 1 174 ? -15.166 5.443   -4.981  0.50 33.50 ? 175 ASP A CB  1 
ATOM   1518 C  CB  B ASP A 1 174 ? -14.391 6.098   -4.375  0.50 50.76 ? 175 ASP A CB  1 
ATOM   1519 C  CG  A ASP A 1 174 ? -14.498 6.688   -5.470  0.50 38.07 ? 175 ASP A CG  1 
ATOM   1520 C  CG  B ASP A 1 174 ? -13.352 6.840   -5.199  0.50 55.92 ? 175 ASP A CG  1 
ATOM   1521 O  OD1 A ASP A 1 174 ? -14.129 7.517   -4.597  0.50 37.46 ? 175 ASP A OD1 1 
ATOM   1522 O  OD1 B ASP A 1 174 ? -12.677 7.797   -4.595  0.50 70.07 ? 175 ASP A OD1 1 
ATOM   1523 O  OD2 A ASP A 1 174 ? -14.307 6.815   -6.689  0.50 54.57 ? 175 ASP A OD2 1 
ATOM   1524 O  OD2 B ASP A 1 174 ? -13.195 6.426   -6.424  0.50 86.57 ? 175 ASP A OD2 1 
ATOM   1525 N  N   . PHE A 1 175 ? -15.350 4.464   -1.631  1.00 23.84 ? 176 PHE A N   1 
ATOM   1526 C  CA  . PHE A 1 175 ? -16.152 3.511   -0.857  1.00 26.98 ? 176 PHE A CA  1 
ATOM   1527 C  C   . PHE A 1 175 ? -17.257 4.213   -0.084  1.00 21.32 ? 176 PHE A C   1 
ATOM   1528 O  O   . PHE A 1 175 ? -17.038 4.527   1.063   1.00 23.56 ? 176 PHE A O   1 
ATOM   1529 C  CB  . PHE A 1 175 ? -15.237 2.675   0.048   1.00 25.97 ? 176 PHE A CB  1 
ATOM   1530 C  CG  . PHE A 1 175 ? -15.888 1.429   0.568   1.00 21.75 ? 176 PHE A CG  1 
ATOM   1531 C  CD1 . PHE A 1 175 ? -16.148 0.362   -0.266  1.00 22.25 ? 176 PHE A CD1 1 
ATOM   1532 C  CD2 . PHE A 1 175 ? -16.239 1.330   1.901   1.00 21.15 ? 176 PHE A CD2 1 
ATOM   1533 C  CE1 . PHE A 1 175 ? -16.762 -0.774  0.222   1.00 21.79 ? 176 PHE A CE1 1 
ATOM   1534 C  CE2 . PHE A 1 175 ? -16.780 0.153   2.402   1.00 23.28 ? 176 PHE A CE2 1 
ATOM   1535 C  CZ  . PHE A 1 175 ? -17.058 -0.876  1.566   1.00 20.66 ? 176 PHE A CZ  1 
ATOM   1536 N  N   . THR A 1 176 ? -18.346 4.618   -0.732  1.00 20.44 ? 177 THR A N   1 
ATOM   1537 C  CA  . THR A 1 176 ? -19.389 5.463   -0.182  1.00 20.74 ? 177 THR A CA  1 
ATOM   1538 C  C   . THR A 1 176 ? -20.584 4.643   0.249   1.00 14.32 ? 177 THR A C   1 
ATOM   1539 O  O   . THR A 1 176 ? -20.749 3.496   -0.232  1.00 19.84 ? 177 THR A O   1 
ATOM   1540 C  CB  . THR A 1 176 ? -19.814 6.522   -1.216  1.00 21.51 ? 177 THR A CB  1 
ATOM   1541 O  OG1 . THR A 1 176 ? -20.099 5.894   -2.463  1.00 23.34 ? 177 THR A OG1 1 
ATOM   1542 C  CG2 . THR A 1 176 ? -18.726 7.558   -1.444  1.00 27.49 ? 177 THR A CG2 1 
ATOM   1543 N  N   . ASN A 1 177 ? -21.390 5.186   1.157   1.00 18.14 ? 178 ASN A N   1 
ATOM   1544 C  CA  . ASN A 1 177 ? -22.665 4.656   1.573   1.00 20.34 ? 178 ASN A CA  1 
ATOM   1545 C  C   . ASN A 1 177 ? -22.521 3.323   2.278   1.00 21.85 ? 178 ASN A C   1 
ATOM   1546 O  O   . ASN A 1 177 ? -23.467 2.564   2.337   1.00 26.99 ? 178 ASN A O   1 
ATOM   1547 C  CB  . ASN A 1 177 ? -23.586 4.504   0.386   1.00 21.94 ? 178 ASN A CB  1 
ATOM   1548 C  CG  . ASN A 1 177 ? -23.798 5.877   -0.221  1.00 20.23 ? 178 ASN A CG  1 
ATOM   1549 O  OD1 . ASN A 1 177 ? -24.409 6.726   0.422   1.00 22.22 ? 178 ASN A OD1 1 
ATOM   1550 N  ND2 . ASN A 1 177 ? -23.220 6.142   -1.388  1.00 19.48 ? 178 ASN A ND2 1 
ATOM   1551 N  N   . PHE A 1 178 ? -21.351 3.073   2.868   1.00 18.32 ? 179 PHE A N   1 
ATOM   1552 C  CA  . PHE A 1 178 ? -21.202 1.875   3.694   1.00 16.28 ? 179 PHE A CA  1 
ATOM   1553 C  C   . PHE A 1 178 ? -21.676 2.154   5.109   1.00 15.88 ? 179 PHE A C   1 
ATOM   1554 O  O   . PHE A 1 178 ? -21.273 3.162   5.689   1.00 16.92 ? 179 PHE A O   1 
ATOM   1555 C  CB  . PHE A 1 178 ? -19.767 1.402   3.768   1.00 16.82 ? 179 PHE A CB  1 
ATOM   1556 C  CG  . PHE A 1 178 ? -19.664 0.186   4.625   1.00 16.61 ? 179 PHE A CG  1 
ATOM   1557 C  CD1 . PHE A 1 178 ? -20.048 -1.047  4.092   1.00 17.19 ? 179 PHE A CD1 1 
ATOM   1558 C  CD2 . PHE A 1 178 ? -19.324 0.250   5.990   1.00 13.42 ? 179 PHE A CD2 1 
ATOM   1559 C  CE1 . PHE A 1 178 ? -20.006 -2.203  4.852   1.00 17.48 ? 179 PHE A CE1 1 
ATOM   1560 C  CE2 . PHE A 1 178 ? -19.312 -0.926  6.737   1.00 13.94 ? 179 PHE A CE2 1 
ATOM   1561 C  CZ  . PHE A 1 178 ? -19.628 -2.142  6.182   1.00 14.66 ? 179 PHE A CZ  1 
ATOM   1562 N  N   . ASP A 1 179 ? -22.556 1.298   5.615   1.00 15.99 ? 180 ASP A N   1 
ATOM   1563 C  CA  . ASP A 1 179 ? -23.199 1.507   6.903   1.00 15.32 ? 180 ASP A CA  1 
ATOM   1564 C  C   . ASP A 1 179 ? -22.528 0.652   7.969   1.00 14.13 ? 180 ASP A C   1 
ATOM   1565 O  O   . ASP A 1 179 ? -22.683 -0.551  7.988   1.00 14.70 ? 180 ASP A O   1 
ATOM   1566 C  CB  . ASP A 1 179 ? -24.669 1.103   6.799   1.00 18.10 ? 180 ASP A CB  1 
ATOM   1567 C  CG  . ASP A 1 179 ? -25.465 1.489   8.019   1.00 19.99 ? 180 ASP A CG  1 
ATOM   1568 O  OD1 . ASP A 1 179 ? -24.868 1.774   9.075   1.00 18.82 ? 180 ASP A OD1 1 
ATOM   1569 O  OD2 . ASP A 1 179 ? -26.673 1.580   7.885   1.00 30.02 ? 180 ASP A OD2 1 
ATOM   1570 N  N   . PRO A 1 180 ? -21.724 1.237   8.869   1.00 12.57 ? 181 PRO A N   1 
ATOM   1571 C  CA  . PRO A 1 180 ? -21.025 0.413   9.855   1.00 12.23 ? 181 PRO A CA  1 
ATOM   1572 C  C   . PRO A 1 180 ? -21.938 -0.186  10.906  1.00 11.94 ? 181 PRO A C   1 
ATOM   1573 O  O   . PRO A 1 180 ? -21.542 -1.085  11.639  1.00 11.34 ? 181 PRO A O   1 
ATOM   1574 C  CB  . PRO A 1 180 ? -20.024 1.413   10.443  1.00 14.15 ? 181 PRO A CB  1 
ATOM   1575 C  CG  . PRO A 1 180 ? -20.740 2.755   10.310  1.00 15.12 ? 181 PRO A CG  1 
ATOM   1576 C  CD  . PRO A 1 180 ? -21.388 2.662   8.934   1.00 13.46 ? 181 PRO A CD  1 
ATOM   1577 N  N   . ARG A 1 181 ? -23.210 0.213   10.941  1.00 12.26 ? 182 ARG A N   1 
ATOM   1578 C  CA  . ARG A 1 181 ? -24.133 -0.469  11.857  1.00 12.83 ? 182 ARG A CA  1 
ATOM   1579 C  C   . ARG A 1 181 ? -24.236 -1.955  11.507  1.00 13.49 ? 182 ARG A C   1 
ATOM   1580 O  O   . ARG A 1 181 ? -24.606 -2.761  12.384  1.00 15.55 ? 182 ARG A O   1 
ATOM   1581 C  CB  . ARG A 1 181 ? -25.526 0.179   11.847  1.00 14.25 ? 182 ARG A CB  1 
ATOM   1582 C  CG  . ARG A 1 181 ? -25.448 1.610   12.357  1.00 15.97 ? 182 ARG A CG  1 
ATOM   1583 C  CD  . ARG A 1 181 ? -26.774 2.354   12.323  1.00 17.45 ? 182 ARG A CD  1 
ATOM   1584 N  NE  . ARG A 1 181 ? -27.146 2.567   10.941  1.00 19.05 ? 182 ARG A NE  1 
ATOM   1585 C  CZ  . ARG A 1 181 ? -28.190 3.340   10.643  1.00 19.82 ? 182 ARG A CZ  1 
ATOM   1586 N  NH1 . ARG A 1 181 ? -28.936 3.862   11.616  1.00 24.01 ? 182 ARG A NH1 1 
ATOM   1587 N  NH2 . ARG A 1 181 ? -28.490 3.561   9.393   1.00 22.91 ? 182 ARG A NH2 1 
ATOM   1588 N  N   . GLY A 1 182 ? -23.972 -2.331  10.248  1.00 14.51 ? 183 GLY A N   1 
ATOM   1589 C  CA  . GLY A 1 182 ? -24.096 -3.739  9.871   1.00 15.51 ? 183 GLY A CA  1 
ATOM   1590 C  C   . GLY A 1 182 ? -22.933 -4.580  10.379  1.00 16.03 ? 183 GLY A C   1 
ATOM   1591 O  O   . GLY A 1 182 ? -22.948 -5.763  10.122  1.00 16.67 ? 183 GLY A O   1 
ATOM   1592 N  N   . LEU A 1 183 ? -21.993 -3.972  11.132  1.00 13.52 ? 184 LEU A N   1 
ATOM   1593 C  CA  . LEU A 1 183 ? -20.860 -4.723  11.661  1.00 13.30 ? 184 LEU A CA  1 
ATOM   1594 C  C   . LEU A 1 183 ? -21.016 -4.933  13.181  1.00 11.59 ? 184 LEU A C   1 
ATOM   1595 O  O   . LEU A 1 183 ? -20.143 -5.523  13.800  1.00 13.29 ? 184 LEU A O   1 
ATOM   1596 C  CB  . LEU A 1 183 ? -19.569 -3.970  11.381  1.00 13.23 ? 184 LEU A CB  1 
ATOM   1597 C  CG  . LEU A 1 183 ? -19.235 -3.868  9.906   1.00 14.95 ? 184 LEU A CG  1 
ATOM   1598 C  CD1 . LEU A 1 183 ? -18.023 -3.037  9.716   1.00 17.24 ? 184 LEU A CD1 1 
ATOM   1599 C  CD2 . LEU A 1 183 ? -19.141 -5.167  9.173   1.00 16.42 ? 184 LEU A CD2 1 
ATOM   1600 N  N   . LEU A 1 184 ? -22.134 -4.491  13.787  1.00 12.76 ? 185 LEU A N   1 
ATOM   1601 C  CA  . LEU A 1 184 ? -22.249 -4.512  15.232  1.00 11.89 ? 185 LEU A CA  1 
ATOM   1602 C  C   . LEU A 1 184 ? -22.972 -5.764  15.696  1.00 15.72 ? 185 LEU A C   1 
ATOM   1603 O  O   . LEU A 1 184 ? -23.830 -6.234  15.011  1.00 23.56 ? 185 LEU A O   1 
ATOM   1604 C  CB  . LEU A 1 184 ? -23.015 -3.274  15.749  1.00 11.98 ? 185 LEU A CB  1 
ATOM   1605 C  CG  . LEU A 1 184 ? -22.409 -1.933  15.310  1.00 11.49 ? 185 LEU A CG  1 
ATOM   1606 C  CD1 . LEU A 1 184 ? -23.302 -0.803  15.792  1.00 13.37 ? 185 LEU A CD1 1 
ATOM   1607 C  CD2 . LEU A 1 184 ? -20.997 -1.833  15.876  1.00 13.15 ? 185 LEU A CD2 1 
ATOM   1608 N  N   . PRO A 1 185 ? -22.582 -6.366  16.816  1.00 12.41 ? 186 PRO A N   1 
ATOM   1609 C  CA  . PRO A 1 185 ? -23.361 -7.469  17.406  1.00 12.91 ? 186 PRO A CA  1 
ATOM   1610 C  C   . PRO A 1 185 ? -24.610 -6.918  18.082  1.00 15.37 ? 186 PRO A C   1 
ATOM   1611 O  O   . PRO A 1 185 ? -24.818 -5.718  18.181  1.00 17.92 ? 186 PRO A O   1 
ATOM   1612 C  CB  . PRO A 1 185 ? -22.373 -8.040  18.421  1.00 12.43 ? 186 PRO A CB  1 
ATOM   1613 C  CG  . PRO A 1 185 ? -21.625 -6.820  18.846  1.00 10.14 ? 186 PRO A CG  1 
ATOM   1614 C  CD  . PRO A 1 185 ? -21.468 -5.939  17.648  1.00 10.22 ? 186 PRO A CD  1 
ATOM   1615 N  N   . GLU A 1 186 ? -25.431 -7.842  18.569  1.00 16.14 ? 187 GLU A N   1 
ATOM   1616 C  CA  . GLU A 1 186 ? -26.689 -7.431  19.170  1.00 18.22 ? 187 GLU A CA  1 
ATOM   1617 C  C   . GLU A 1 186 ? -26.458 -6.633  20.438  1.00 15.36 ? 187 GLU A C   1 
ATOM   1618 O  O   . GLU A 1 186 ? -27.091 -5.595  20.685  1.00 18.20 ? 187 GLU A O   1 
ATOM   1619 C  CB  . GLU A 1 186 ? -27.491 -8.637  19.668  1.00 23.35 ? 187 GLU A CB  1 
ATOM   1620 C  CG  . GLU A 1 186 ? -28.320 -9.276  18.627  1.00 27.11 ? 187 GLU A CG  1 
ATOM   1621 C  CD  . GLU A 1 186 ? -28.979 -10.559 19.131  1.00 22.44 ? 187 GLU A CD  1 
ATOM   1622 O  OE1 . GLU A 1 186 ? -29.037 -10.739 20.329  1.00 31.62 ? 187 GLU A OE1 1 
ATOM   1623 O  OE2 . GLU A 1 186 ? -29.506 -11.274 18.308  1.00 31.90 ? 187 GLU A OE2 1 
ATOM   1624 N  N   . SER A 1 187 ? -25.591 -7.162  21.293  1.00 16.34 ? 188 SER A N   1 
ATOM   1625 C  CA  . SER A 1 187 ? -25.312 -6.593  22.586  1.00 15.00 ? 188 SER A CA  1 
ATOM   1626 C  C   . SER A 1 187 ? -24.189 -5.558  22.563  1.00 13.96 ? 188 SER A C   1 
ATOM   1627 O  O   . SER A 1 187 ? -23.148 -5.779  21.922  1.00 14.61 ? 188 SER A O   1 
ATOM   1628 C  CB  . SER A 1 187 ? -24.947 -7.681  23.542  1.00 17.02 ? 188 SER A CB  1 
ATOM   1629 O  OG  . SER A 1 187 ? -24.681 -7.188  24.836  1.00 17.35 ? 188 SER A OG  1 
ATOM   1630 N  N   . LEU A 1 188 ? -24.343 -4.486  23.352  1.00 14.97 ? 189 LEU A N   1 
ATOM   1631 C  CA  . LEU A 1 188 ? -23.292 -3.482  23.538  1.00 13.93 ? 189 LEU A CA  1 
ATOM   1632 C  C   . LEU A 1 188 ? -22.669 -3.653  24.919  1.00 13.15 ? 189 LEU A C   1 
ATOM   1633 O  O   . LEU A 1 188 ? -21.947 -2.775  25.378  1.00 15.48 ? 189 LEU A O   1 
ATOM   1634 C  CB  . LEU A 1 188 ? -23.803 -2.045  23.333  1.00 17.13 ? 189 LEU A CB  1 
ATOM   1635 C  CG  . LEU A 1 188 ? -24.225 -1.695  21.922  1.00 19.57 ? 189 LEU A CG  1 
ATOM   1636 C  CD1 . LEU A 1 188 ? -24.733 -0.282  21.818  1.00 21.32 ? 189 LEU A CD1 1 
ATOM   1637 C  CD2 . LEU A 1 188 ? -23.140 -2.028  20.918  1.00 21.61 ? 189 LEU A CD2 1 
ATOM   1638 N  N   . ASP A 1 189 ? -22.789 -4.846  25.530  1.00 13.96 ? 190 ASP A N   1 
ATOM   1639 C  CA  . ASP A 1 189 ? -22.045 -5.076  26.754  1.00 12.48 ? 190 ASP A CA  1 
ATOM   1640 C  C   . ASP A 1 189 ? -20.535 -5.012  26.446  1.00 10.40 ? 190 ASP A C   1 
ATOM   1641 O  O   . ASP A 1 189 ? -20.109 -5.536  25.420  1.00 10.30 ? 190 ASP A O   1 
ATOM   1642 C  CB  . ASP A 1 189 ? -22.327 -6.468  27.310  1.00 16.95 ? 190 ASP A CB  1 
ATOM   1643 C  CG  . ASP A 1 189 ? -23.693 -6.655  27.945  1.00 23.86 ? 190 ASP A CG  1 
ATOM   1644 O  OD1 . ASP A 1 189 ? -24.302 -5.642  28.139  1.00 26.86 ? 190 ASP A OD1 1 
ATOM   1645 O  OD2 . ASP A 1 189 ? -24.116 -7.828  28.221  1.00 33.34 ? 190 ASP A OD2 1 
ATOM   1646 N  N   . TYR A 1 190 ? -19.717 -4.455  27.352  1.00 9.52  ? 191 TYR A N   1 
ATOM   1647 C  CA  . TYR A 1 190 ? -18.322 -4.183  27.018  1.00 8.60  ? 191 TYR A CA  1 
ATOM   1648 C  C   . TYR A 1 190 ? -17.440 -4.217  28.242  1.00 8.38  ? 191 TYR A C   1 
ATOM   1649 O  O   . TYR A 1 190 ? -17.867 -4.092  29.404  1.00 9.81  ? 191 TYR A O   1 
ATOM   1650 C  CB  . TYR A 1 190 ? -18.218 -2.822  26.327  1.00 10.19 ? 191 TYR A CB  1 
ATOM   1651 C  CG  . TYR A 1 190 ? -18.625 -1.634  27.191  1.00 9.73  ? 191 TYR A CG  1 
ATOM   1652 C  CD1 . TYR A 1 190 ? -17.672 -1.061  28.053  1.00 11.01 ? 191 TYR A CD1 1 
ATOM   1653 C  CD2 . TYR A 1 190 ? -19.897 -1.097  27.131  1.00 11.42 ? 191 TYR A CD2 1 
ATOM   1654 C  CE1 . TYR A 1 190 ? -18.045 0.009   28.891  1.00 11.49 ? 191 TYR A CE1 1 
ATOM   1655 C  CE2 . TYR A 1 190 ? -20.240 -0.021  27.917  1.00 11.76 ? 191 TYR A CE2 1 
ATOM   1656 C  CZ  . TYR A 1 190 ? -19.323 0.501   28.806  1.00 12.15 ? 191 TYR A CZ  1 
ATOM   1657 O  OH  . TYR A 1 190 ? -19.654 1.524   29.653  1.00 14.18 ? 191 TYR A OH  1 
ATOM   1658 N  N   . TRP A 1 191 ? -16.155 -4.323  27.943  1.00 7.90  ? 192 TRP A N   1 
ATOM   1659 C  CA  . TRP A 1 191 ? -15.082 -4.081  28.865  1.00 7.80  ? 192 TRP A CA  1 
ATOM   1660 C  C   . TRP A 1 191 ? -14.394 -2.792  28.462  1.00 7.81  ? 192 TRP A C   1 
ATOM   1661 O  O   . TRP A 1 191 ? -14.327 -2.475  27.276  1.00 9.01  ? 192 TRP A O   1 
ATOM   1662 C  CB  . TRP A 1 191 ? -14.067 -5.214  28.879  1.00 8.56  ? 192 TRP A CB  1 
ATOM   1663 C  CG  . TRP A 1 191 ? -14.586 -6.548  29.300  1.00 8.80  ? 192 TRP A CG  1 
ATOM   1664 C  CD1 . TRP A 1 191 ? -14.868 -6.961  30.600  1.00 10.44 ? 192 TRP A CD1 1 
ATOM   1665 C  CD2 . TRP A 1 191 ? -14.883 -7.653  28.451  1.00 8.48  ? 192 TRP A CD2 1 
ATOM   1666 N  NE1 . TRP A 1 191 ? -15.276 -8.257  30.562  1.00 10.88 ? 192 TRP A NE1 1 
ATOM   1667 C  CE2 . TRP A 1 191 ? -15.294 -8.723  29.280  1.00 10.26 ? 192 TRP A CE2 1 
ATOM   1668 C  CE3 . TRP A 1 191 ? -14.787 -7.848  27.066  1.00 8.71  ? 192 TRP A CE3 1 
ATOM   1669 C  CZ2 . TRP A 1 191 ? -15.603 -9.979  28.757  1.00 10.76 ? 192 TRP A CZ2 1 
ATOM   1670 C  CZ3 . TRP A 1 191 ? -15.062 -9.110  26.567  1.00 10.26 ? 192 TRP A CZ3 1 
ATOM   1671 C  CH2 . TRP A 1 191 ? -15.475 -10.140 27.387  1.00 11.23 ? 192 TRP A CH2 1 
ATOM   1672 N  N   . THR A 1 192 ? -13.823 -2.065  29.416  1.00 8.14  ? 193 THR A N   1 
ATOM   1673 C  CA  . THR A 1 192 ? -13.096 -0.857  29.049  1.00 7.49  ? 193 THR A CA  1 
ATOM   1674 C  C   . THR A 1 192 ? -11.851 -0.666  29.915  1.00 7.83  ? 193 THR A C   1 
ATOM   1675 O  O   . THR A 1 192 ? -11.831 -1.079  31.087  1.00 9.18  ? 193 THR A O   1 
ATOM   1676 C  CB  . THR A 1 192 ? -14.017 0.355   29.169  1.00 8.26  ? 193 THR A CB  1 
ATOM   1677 O  OG1 . THR A 1 192 ? -13.353 1.534   28.737  1.00 8.52  ? 193 THR A OG1 1 
ATOM   1678 C  CG2 . THR A 1 192 ? -14.548 0.589   30.589  1.00 10.07 ? 193 THR A CG2 1 
ATOM   1679 N  N   . TYR A 1 193 ? -10.799 -0.083  29.321  1.00 7.49  ? 194 TYR A N   1 
ATOM   1680 C  CA  . TYR A 1 193 ? -9.577  0.195   30.045  1.00 7.89  ? 194 TYR A CA  1 
ATOM   1681 C  C   . TYR A 1 193 ? -8.814  1.236   29.239  1.00 7.90  ? 194 TYR A C   1 
ATOM   1682 O  O   . TYR A 1 193 ? -9.028  1.425   28.043  1.00 7.80  ? 194 TYR A O   1 
ATOM   1683 C  CB  . TYR A 1 193 ? -8.746  -1.090  30.237  1.00 9.24  ? 194 TYR A CB  1 
ATOM   1684 C  CG  . TYR A 1 193 ? -8.091  -1.586  28.963  1.00 7.71  ? 194 TYR A CG  1 
ATOM   1685 C  CD1 . TYR A 1 193 ? -8.763  -2.327  28.012  1.00 7.41  ? 194 TYR A CD1 1 
ATOM   1686 C  CD2 . TYR A 1 193 ? -6.779  -1.250  28.728  1.00 8.72  ? 194 TYR A CD2 1 
ATOM   1687 C  CE1 . TYR A 1 193 ? -8.136  -2.665  26.815  1.00 6.72  ? 194 TYR A CE1 1 
ATOM   1688 C  CE2 . TYR A 1 193 ? -6.112  -1.558  27.537  1.00 8.50  ? 194 TYR A CE2 1 
ATOM   1689 C  CZ  . TYR A 1 193 ? -6.829  -2.269  26.582  1.00 6.75  ? 194 TYR A CZ  1 
ATOM   1690 O  OH  . TYR A 1 193 ? -6.157  -2.578  25.410  1.00 7.23  ? 194 TYR A OH  1 
ATOM   1691 N  N   . PRO A 1 194 ? -7.850  1.943   29.901  1.00 7.82  ? 195 PRO A N   1 
ATOM   1692 C  CA  . PRO A 1 194 ? -7.036  2.934   29.226  1.00 8.27  ? 195 PRO A CA  1 
ATOM   1693 C  C   . PRO A 1 194 ? -5.844  2.279   28.549  1.00 7.10  ? 195 PRO A C   1 
ATOM   1694 O  O   . PRO A 1 194 ? -5.103  1.515   29.209  1.00 8.89  ? 195 PRO A O   1 
ATOM   1695 C  CB  . PRO A 1 194 ? -6.515  3.856   30.360  1.00 10.75 ? 195 PRO A CB  1 
ATOM   1696 C  CG  . PRO A 1 194 ? -6.553  2.953   31.574  1.00 11.35 ? 195 PRO A CG  1 
ATOM   1697 C  CD  . PRO A 1 194 ? -7.681  1.970   31.354  1.00 10.03 ? 195 PRO A CD  1 
ATOM   1698 N  N   . GLY A 1 195 ? -5.618  2.576   27.260  1.00 7.53  ? 196 GLY A N   1 
ATOM   1699 C  CA  . GLY A 1 195 ? -4.513  1.933   26.553  1.00 7.81  ? 196 GLY A CA  1 
ATOM   1700 C  C   . GLY A 1 195 ? -3.997  2.826   25.444  1.00 6.94  ? 196 GLY A C   1 
ATOM   1701 O  O   . GLY A 1 195 ? -3.852  4.041   25.594  1.00 7.60  ? 196 GLY A O   1 
ATOM   1702 N  N   . SER A 1 196 ? -3.579  2.172   24.373  1.00 6.76  ? 197 SER A N   1 
ATOM   1703 C  CA  . SER A 1 196 ? -2.759  2.787   23.356  1.00 7.56  ? 197 SER A CA  1 
ATOM   1704 C  C   . SER A 1 196 ? -3.178  2.338   21.949  1.00 6.70  ? 197 SER A C   1 
ATOM   1705 O  O   . SER A 1 196 ? -3.972  1.387   21.794  1.00 6.96  ? 197 SER A O   1 
ATOM   1706 C  CB  . SER A 1 196 ? -1.276  2.405   23.512  1.00 8.52  ? 197 SER A CB  1 
ATOM   1707 O  OG  . SER A 1 196 ? -1.062  1.056   23.173  1.00 7.65  ? 197 SER A OG  1 
ATOM   1708 N  N   . LEU A 1 197 ? -2.621  3.018   20.943  1.00 7.48  ? 198 LEU A N   1 
ATOM   1709 C  CA  . LEU A 1 197 ? -2.579  2.431   19.597  1.00 7.88  ? 198 LEU A CA  1 
ATOM   1710 C  C   . LEU A 1 197 ? -1.903  1.088   19.681  1.00 7.15  ? 198 LEU A C   1 
ATOM   1711 O  O   . LEU A 1 197 ? -0.982  0.908   20.477  1.00 7.98  ? 198 LEU A O   1 
ATOM   1712 C  CB  . LEU A 1 197 ? -1.758  3.302   18.649  1.00 10.50 ? 198 LEU A CB  1 
ATOM   1713 C  CG  . LEU A 1 197 ? -2.518  4.223   17.736  1.00 15.89 ? 198 LEU A CG  1 
ATOM   1714 C  CD1 . LEU A 1 197 ? -3.330  5.233   18.484  1.00 14.39 ? 198 LEU A CD1 1 
ATOM   1715 C  CD2 . LEU A 1 197 ? -1.511  4.922   16.821  1.00 18.12 ? 198 LEU A CD2 1 
ATOM   1716 N  N   . THR A 1 198 ? -2.258  0.172   18.787  1.00 8.06  ? 199 THR A N   1 
ATOM   1717 C  CA  . THR A 1 198 ? -1.650  -1.138  18.727  1.00 8.72  ? 199 THR A CA  1 
ATOM   1718 C  C   . THR A 1 198 ? -0.623  -1.228  17.596  1.00 8.58  ? 199 THR A C   1 
ATOM   1719 O  O   . THR A 1 198 ? -0.062  -2.288  17.369  1.00 9.54  ? 199 THR A O   1 
ATOM   1720 C  CB  . THR A 1 198 ? -2.639  -2.282  18.698  1.00 7.80  ? 199 THR A CB  1 
ATOM   1721 O  OG1 . THR A 1 198 ? -3.347  -2.130  17.465  1.00 7.78  ? 199 THR A OG1 1 
ATOM   1722 C  CG2 . THR A 1 198 ? -3.585  -2.268  19.861  1.00 8.61  ? 199 THR A CG2 1 
ATOM   1723 N  N   . THR A 1 199 ? -0.444  -0.132  16.855  1.00 9.34  ? 200 THR A N   1 
ATOM   1724 C  CA  . THR A 1 199 ? 0.569   -0.021  15.849  1.00 9.87  ? 200 THR A CA  1 
ATOM   1725 C  C   . THR A 1 199 ? 1.419   1.173   16.181  1.00 10.65 ? 200 THR A C   1 
ATOM   1726 O  O   . THR A 1 199 ? 0.940   2.147   16.749  1.00 10.87 ? 200 THR A O   1 
ATOM   1727 C  CB  . THR A 1 199 ? -0.050  0.173   14.455  1.00 10.16 ? 200 THR A CB  1 
ATOM   1728 O  OG1 . THR A 1 199 ? -0.893  1.331   14.453  1.00 12.13 ? 200 THR A OG1 1 
ATOM   1729 C  CG2 . THR A 1 199 ? -0.780  -1.051  13.971  1.00 12.02 ? 200 THR A CG2 1 
ATOM   1730 N  N   . PRO A 1 200 ? 2.692   1.197   15.738  1.00 11.38 ? 201 PRO A N   1 
ATOM   1731 C  CA  . PRO A 1 200 ? 3.533   2.423   15.814  1.00 11.24 ? 201 PRO A CA  1 
ATOM   1732 C  C   . PRO A 1 200 ? 2.736   3.589   15.230  1.00 11.51 ? 201 PRO A C   1 
ATOM   1733 O  O   . PRO A 1 200 ? 2.147   3.490   14.167  1.00 14.15 ? 201 PRO A O   1 
ATOM   1734 C  CB  . PRO A 1 200 ? 4.686   2.032   14.872  1.00 12.80 ? 201 PRO A CB  1 
ATOM   1735 C  CG  . PRO A 1 200 ? 4.879   0.566   15.125  1.00 14.25 ? 201 PRO A CG  1 
ATOM   1736 C  CD  . PRO A 1 200 ? 3.437   0.058   15.086  1.00 11.80 ? 201 PRO A CD  1 
ATOM   1737 N  N   . PRO A 1 201 ? 2.735   4.736   15.920  1.00 12.20 ? 202 PRO A N   1 
ATOM   1738 C  CA  . PRO A 1 201 ? 3.674   5.041   17.018  1.00 12.14 ? 202 PRO A CA  1 
ATOM   1739 C  C   . PRO A 1 201 ? 3.246   4.670   18.442  1.00 10.56 ? 202 PRO A C   1 
ATOM   1740 O  O   . PRO A 1 201 ? 3.909   5.061   19.421  1.00 11.81 ? 202 PRO A O   1 
ATOM   1741 C  CB  . PRO A 1 201 ? 3.867   6.570   16.887  1.00 15.51 ? 202 PRO A CB  1 
ATOM   1742 C  CG  . PRO A 1 201 ? 2.572   7.024   16.312  1.00 18.46 ? 202 PRO A CG  1 
ATOM   1743 C  CD  . PRO A 1 201 ? 2.082   5.943   15.387  1.00 15.23 ? 202 PRO A CD  1 
ATOM   1744 N  N   . LEU A 1 202 ? 2.172   3.884   18.579  1.00 10.23 ? 203 LEU A N   1 
ATOM   1745 C  CA  . LEU A 1 202 ? 1.851   3.280   19.884  1.00 9.62  ? 203 LEU A CA  1 
ATOM   1746 C  C   . LEU A 1 202 ? 1.418   4.318   20.918  1.00 9.26  ? 203 LEU A C   1 
ATOM   1747 O  O   . LEU A 1 202 ? 1.524   4.073   22.120  1.00 9.72  ? 203 LEU A O   1 
ATOM   1748 C  CB  . LEU A 1 202 ? 2.957   2.377   20.451  1.00 9.46  ? 203 LEU A CB  1 
ATOM   1749 C  CG  . LEU A 1 202 ? 3.312   1.224   19.495  1.00 9.83  ? 203 LEU A CG  1 
ATOM   1750 C  CD1 . LEU A 1 202 ? 4.592   0.560   19.971  1.00 12.44 ? 203 LEU A CD1 1 
ATOM   1751 C  CD2 . LEU A 1 202 ? 2.254   0.172   19.372  1.00 10.87 ? 203 LEU A CD2 1 
ATOM   1752 N  N   A ASN A 1 203 ? 0.858   5.434   20.449  0.50 10.58 ? 204 ASN A N   1 
ATOM   1753 N  N   B ASN A 1 203 ? 0.927   5.466   20.446  0.50 10.80 ? 204 ASN A N   1 
ATOM   1754 C  CA  A ASN A 1 203 ? 0.545   6.513   21.362  0.50 10.77 ? 204 ASN A CA  1 
ATOM   1755 C  CA  B ASN A 1 203 ? 0.525   6.572   21.296  0.50 10.84 ? 204 ASN A CA  1 
ATOM   1756 C  C   A ASN A 1 203 ? -0.416  6.036   22.438  0.50 9.48  ? 204 ASN A C   1 
ATOM   1757 C  C   B ASN A 1 203 ? -0.429  6.098   22.394  0.50 9.24  ? 204 ASN A C   1 
ATOM   1758 O  O   A ASN A 1 203 ? -1.357  5.309   22.195  0.50 9.16  ? 204 ASN A O   1 
ATOM   1759 O  O   B ASN A 1 203 ? -1.386  5.399   22.118  0.50 8.87  ? 204 ASN A O   1 
ATOM   1760 C  CB  A ASN A 1 203 ? -0.146  7.687   20.682  0.50 12.15 ? 204 ASN A CB  1 
ATOM   1761 C  CB  B ASN A 1 203 ? -0.215  7.631   20.475  0.50 13.15 ? 204 ASN A CB  1 
ATOM   1762 C  CG  A ASN A 1 203 ? 0.761   8.465   19.760  0.50 13.98 ? 204 ASN A CG  1 
ATOM   1763 C  CG  B ASN A 1 203 ? 0.579   8.189   19.312  0.50 17.45 ? 204 ASN A CG  1 
ATOM   1764 O  OD1 A ASN A 1 203 ? 1.893   8.059   19.437  0.50 16.56 ? 204 ASN A OD1 1 
ATOM   1765 O  OD1 B ASN A 1 203 ? 0.914   7.502   18.330  0.50 20.46 ? 204 ASN A OD1 1 
ATOM   1766 N  ND2 A ASN A 1 203 ? 0.213   9.562   19.242  0.50 16.94 ? 204 ASN A ND2 1 
ATOM   1767 N  ND2 B ASN A 1 203 ? 0.873   9.478   19.385  0.50 21.18 ? 204 ASN A ND2 1 
ATOM   1768 N  N   . GLU A 1 204 ? -0.221  6.543   23.639  1.00 10.66 ? 205 GLU A N   1 
ATOM   1769 C  CA  . GLU A 1 204 ? -1.037  6.188   24.794  1.00 9.41  ? 205 GLU A CA  1 
ATOM   1770 C  C   . GLU A 1 204 ? -2.182  7.177   24.917  1.00 10.13 ? 205 GLU A C   1 
ATOM   1771 O  O   . GLU A 1 204 ? -2.289  7.960   25.867  1.00 13.07 ? 205 GLU A O   1 
ATOM   1772 C  CB  . GLU A 1 204 ? -0.182  6.102   26.054  1.00 12.60 ? 205 GLU A CB  1 
ATOM   1773 C  CG  . GLU A 1 204 ? 0.715   4.868   25.955  1.00 12.19 ? 205 GLU A CG  1 
ATOM   1774 C  CD  . GLU A 1 204 ? 1.582   4.560   27.186  1.00 12.77 ? 205 GLU A CD  1 
ATOM   1775 O  OE1 . GLU A 1 204 ? 1.952   5.523   27.893  1.00 16.69 ? 205 GLU A OE1 1 
ATOM   1776 O  OE2 . GLU A 1 204 ? 1.989   3.397   27.347  1.00 13.45 ? 205 GLU A OE2 1 
ATOM   1777 N  N   . CYS A 1 205 ? -3.123  7.089   23.986  1.00 8.32  ? 206 CYS A N   1 
ATOM   1778 C  CA  . CYS A 1 205 ? -4.146  8.088   23.782  1.00 8.00  ? 206 CYS A CA  1 
ATOM   1779 C  C   . CYS A 1 205 ? -5.535  7.467   23.660  1.00 7.75  ? 206 CYS A C   1 
ATOM   1780 O  O   . CYS A 1 205 ? -6.465  8.181   23.300  1.00 9.22  ? 206 CYS A O   1 
ATOM   1781 C  CB  . CYS A 1 205 ? -3.895  8.948   22.556  1.00 9.35  ? 206 CYS A CB  1 
ATOM   1782 S  SG  . CYS A 1 205 ? -3.816  7.982   21.013  1.00 10.22 ? 206 CYS A SG  1 
ATOM   1783 N  N   . VAL A 1 206 ? -5.673  6.179   23.975  1.00 7.30  ? 207 VAL A N   1 
ATOM   1784 C  CA  . VAL A 1 206 ? -6.914  5.455   23.631  1.00 7.11  ? 207 VAL A CA  1 
ATOM   1785 C  C   . VAL A 1 206 ? -7.670  5.013   24.885  1.00 6.86  ? 207 VAL A C   1 
ATOM   1786 O  O   . VAL A 1 206 ? -7.121  4.333   25.741  1.00 8.95  ? 207 VAL A O   1 
ATOM   1787 C  CB  . VAL A 1 206 ? -6.618  4.198   22.795  1.00 7.15  ? 207 VAL A CB  1 
ATOM   1788 C  CG1 . VAL A 1 206 ? -7.961  3.504   22.431  1.00 7.67  ? 207 VAL A CG1 1 
ATOM   1789 C  CG2 . VAL A 1 206 ? -5.861  4.601   21.495  1.00 8.77  ? 207 VAL A CG2 1 
ATOM   1790 N  N   . THR A 1 207 ? -8.982  5.313   24.899  1.00 7.05  ? 208 THR A N   1 
ATOM   1791 C  CA  . THR A 1 207 ? -9.897  4.585   25.764  1.00 7.19  ? 208 THR A CA  1 
ATOM   1792 C  C   . THR A 1 207 ? -10.448 3.410   24.944  1.00 6.54  ? 208 THR A C   1 
ATOM   1793 O  O   . THR A 1 207 ? -11.106 3.609   23.934  1.00 6.81  ? 208 THR A O   1 
ATOM   1794 C  CB  . THR A 1 207 ? -11.073 5.458   26.222  1.00 7.32  ? 208 THR A CB  1 
ATOM   1795 O  OG1 . THR A 1 207 ? -10.584 6.579   26.966  1.00 9.19  ? 208 THR A OG1 1 
ATOM   1796 C  CG2 . THR A 1 207 ? -12.006 4.639   27.101  1.00 9.46  ? 208 THR A CG2 1 
ATOM   1797 N  N   . TRP A 1 208 ? -10.126 2.205   25.396  1.00 6.31  ? 209 TRP A N   1 
ATOM   1798 C  CA  . TRP A 1 208 ? -10.586 1.006   24.696  1.00 5.75  ? 209 TRP A CA  1 
ATOM   1799 C  C   . TRP A 1 208 ? -11.947 0.601   25.232  1.00 5.55  ? 209 TRP A C   1 
ATOM   1800 O  O   . TRP A 1 208 ? -12.147 0.546   26.457  1.00 6.86  ? 209 TRP A O   1 
ATOM   1801 C  CB  . TRP A 1 208 ? -9.563  -0.137  24.910  1.00 6.02  ? 209 TRP A CB  1 
ATOM   1802 C  CG  . TRP A 1 208 ? -8.457  -0.041  23.932  1.00 6.00  ? 209 TRP A CG  1 
ATOM   1803 C  CD1 . TRP A 1 208 ? -7.238  0.571   24.137  1.00 6.61  ? 209 TRP A CD1 1 
ATOM   1804 C  CD2 . TRP A 1 208 ? -8.494  -0.439  22.567  1.00 6.12  ? 209 TRP A CD2 1 
ATOM   1805 N  NE1 . TRP A 1 208 ? -6.493  0.558   22.961  1.00 7.21  ? 209 TRP A NE1 1 
ATOM   1806 C  CE2 . TRP A 1 208 ? -7.242  -0.087  22.011  1.00 6.72  ? 209 TRP A CE2 1 
ATOM   1807 C  CE3 . TRP A 1 208 ? -9.438  -1.114  21.812  1.00 6.61  ? 209 TRP A CE3 1 
ATOM   1808 C  CZ2 . TRP A 1 208 ? -6.935  -0.333  20.672  1.00 7.65  ? 209 TRP A CZ2 1 
ATOM   1809 C  CZ3 . TRP A 1 208 ? -9.127  -1.385  20.505  1.00 7.00  ? 209 TRP A CZ3 1 
ATOM   1810 C  CH2 . TRP A 1 208 ? -7.906  -0.997  19.939  1.00 7.45  ? 209 TRP A CH2 1 
ATOM   1811 N  N   . ILE A 1 209 ? -12.849 0.234   24.329  1.00 5.57  ? 210 ILE A N   1 
ATOM   1812 C  CA  . ILE A 1 209 ? -14.163 -0.272  24.641  1.00 5.86  ? 210 ILE A CA  1 
ATOM   1813 C  C   . ILE A 1 209 ? -14.280 -1.537  23.808  1.00 5.65  ? 210 ILE A C   1 
ATOM   1814 O  O   . ILE A 1 209 ? -14.400 -1.465  22.600  1.00 6.79  ? 210 ILE A O   1 
ATOM   1815 C  CB  . ILE A 1 209 ? -15.233 0.764   24.308  1.00 7.23  ? 210 ILE A CB  1 
ATOM   1816 C  CG1 . ILE A 1 209 ? -15.005 2.045   25.124  1.00 9.53  ? 210 ILE A CG1 1 
ATOM   1817 C  CG2 . ILE A 1 209 ? -16.593 0.138   24.562  1.00 8.71  ? 210 ILE A CG2 1 
ATOM   1818 C  CD1 . ILE A 1 209 ? -15.877 3.194   24.702  1.00 11.63 ? 210 ILE A CD1 1 
ATOM   1819 N  N   . VAL A 1 210 ? -14.201 -2.691  24.470  1.00 6.32  ? 211 VAL A N   1 
ATOM   1820 C  CA  . VAL A 1 210 ? -14.159 -3.975  23.765  1.00 6.13  ? 211 VAL A CA  1 
ATOM   1821 C  C   . VAL A 1 210 ? -15.473 -4.689  24.034  1.00 6.01  ? 211 VAL A C   1 
ATOM   1822 O  O   . VAL A 1 210 ? -15.825 -4.967  25.163  1.00 7.47  ? 211 VAL A O   1 
ATOM   1823 C  CB  . VAL A 1 210 ? -12.964 -4.832  24.223  1.00 6.99  ? 211 VAL A CB  1 
ATOM   1824 C  CG1 . VAL A 1 210 ? -12.997 -6.194  23.526  1.00 7.62  ? 211 VAL A CG1 1 
ATOM   1825 C  CG2 . VAL A 1 210 ? -11.668 -4.096  23.917  1.00 7.95  ? 211 VAL A CG2 1 
ATOM   1826 N  N   . LEU A 1 211 ? -16.238 -4.959  22.958  1.00 7.11  ? 212 LEU A N   1 
ATOM   1827 C  CA  . LEU A 1 211 ? -17.517 -5.624  23.125  1.00 7.43  ? 212 LEU A CA  1 
ATOM   1828 C  C   . LEU A 1 211 ? -17.341 -7.073  23.503  1.00 7.28  ? 212 LEU A C   1 
ATOM   1829 O  O   . LEU A 1 211 ? -16.512 -7.802  22.977  1.00 7.85  ? 212 LEU A O   1 
ATOM   1830 C  CB  . LEU A 1 211 ? -18.358 -5.490  21.857  1.00 8.87  ? 212 LEU A CB  1 
ATOM   1831 C  CG  . LEU A 1 211 ? -18.750 -4.083  21.463  1.00 9.17  ? 212 LEU A CG  1 
ATOM   1832 C  CD1 . LEU A 1 211 ? -19.803 -4.141  20.303  1.00 11.29 ? 212 LEU A CD1 1 
ATOM   1833 C  CD2 . LEU A 1 211 ? -19.263 -3.228  22.589  1.00 10.82 ? 212 LEU A CD2 1 
ATOM   1834 N  N   . LYS A 1 212 ? -18.188 -7.547  24.421  1.00 8.26  ? 213 LYS A N   1 
ATOM   1835 C  CA  . LYS A 1 212 ? -18.153 -8.946  24.800  1.00 9.01  ? 213 LYS A CA  1 
ATOM   1836 C  C   . LYS A 1 212 ? -18.636 -9.886  23.723  1.00 8.02  ? 213 LYS A C   1 
ATOM   1837 O  O   . LYS A 1 212 ? -18.108 -10.992 23.596  1.00 10.56 ? 213 LYS A O   1 
ATOM   1838 C  CB  . LYS A 1 212 ? -18.934 -9.165  26.077  1.00 11.42 ? 213 LYS A CB  1 
ATOM   1839 C  CG  . LYS A 1 212 ? -19.127 -10.625 26.483  1.00 15.16 ? 213 LYS A CG  1 
ATOM   1840 C  CD  . LYS A 1 212 ? -19.775 -10.799 27.831  1.00 25.82 ? 213 LYS A CD  1 
ATOM   1841 C  CE  . LYS A 1 212 ? -19.974 -12.242 28.238  1.00 28.94 ? 213 LYS A CE  1 
ATOM   1842 N  NZ  . LYS A 1 212 ? -20.982 -12.402 29.302  1.00 42.08 ? 213 LYS A NZ  1 
ATOM   1843 N  N   A GLU A 1 213 ? -19.613 -9.477  22.946  0.50 8.60  ? 214 GLU A N   1 
ATOM   1844 N  N   B GLU A 1 213 ? -19.678 -9.531  22.988  0.50 8.41  ? 214 GLU A N   1 
ATOM   1845 C  CA  A GLU A 1 213 ? -20.254 -10.381 22.013  0.50 8.92  ? 214 GLU A CA  1 
ATOM   1846 C  CA  B GLU A 1 213 ? -20.258 -10.439 22.012  0.50 8.93  ? 214 GLU A CA  1 
ATOM   1847 C  C   A GLU A 1 213 ? -19.507 -10.284 20.697  0.50 7.77  ? 214 GLU A C   1 
ATOM   1848 C  C   B GLU A 1 213 ? -19.497 -10.290 20.710  0.50 7.72  ? 214 GLU A C   1 
ATOM   1849 O  O   A GLU A 1 213 ? -19.446 -9.207  20.104  0.50 8.26  ? 214 GLU A O   1 
ATOM   1850 O  O   B GLU A 1 213 ? -19.434 -9.199  20.142  0.50 8.14  ? 214 GLU A O   1 
ATOM   1851 C  CB  A GLU A 1 213 ? -21.709 -9.936  21.848  0.50 10.24 ? 214 GLU A CB  1 
ATOM   1852 C  CB  B GLU A 1 213 ? -21.738 -10.137 21.757  0.50 9.24  ? 214 GLU A CB  1 
ATOM   1853 C  CG  A GLU A 1 213 ? -22.518 -10.920 21.041  0.50 11.72 ? 214 GLU A CG  1 
ATOM   1854 C  CG  B GLU A 1 213 ? -22.297 -10.977 20.638  0.50 11.30 ? 214 GLU A CG  1 
ATOM   1855 C  CD  A GLU A 1 213 ? -23.915 -10.387 20.737  0.50 13.52 ? 214 GLU A CD  1 
ATOM   1856 C  CD  B GLU A 1 213 ? -23.819 -10.931 20.505  0.50 12.95 ? 214 GLU A CD  1 
ATOM   1857 O  OE1 A GLU A 1 213 ? -24.550 -9.838  21.659  0.50 13.76 ? 214 GLU A OE1 1 
ATOM   1858 O  OE1 B GLU A 1 213 ? -24.415 -9.911  20.904  0.50 10.94 ? 214 GLU A OE1 1 
ATOM   1859 O  OE2 A GLU A 1 213 ? -24.359 -10.524 19.580  0.50 17.46 ? 214 GLU A OE2 1 
ATOM   1860 O  OE2 B GLU A 1 213 ? -24.397 -11.915 20.003  0.50 19.13 ? 214 GLU A OE2 1 
ATOM   1861 N  N   . PRO A 1 214 ? -18.920 -11.385 20.184  1.00 8.09  ? 215 PRO A N   1 
ATOM   1862 C  CA  . PRO A 1 214 ? -18.318 -11.328 18.861  1.00 8.09  ? 215 PRO A CA  1 
ATOM   1863 C  C   . PRO A 1 214 ? -19.352 -11.296 17.754  1.00 8.95  ? 215 PRO A C   1 
ATOM   1864 O  O   . PRO A 1 214 ? -20.526 -11.679 17.980  1.00 11.87 ? 215 PRO A O   1 
ATOM   1865 C  CB  . PRO A 1 214 ? -17.556 -12.670 18.747  1.00 9.47  ? 215 PRO A CB  1 
ATOM   1866 C  CG  . PRO A 1 214 ? -18.395 -13.612 19.617  1.00 13.48 ? 215 PRO A CG  1 
ATOM   1867 C  CD  . PRO A 1 214 ? -18.888 -12.739 20.799  1.00 10.97 ? 215 PRO A CD  1 
ATOM   1868 N  N   . ILE A 1 215 ? -18.951 -10.863 16.579  1.00 8.49  ? 216 ILE A N   1 
ATOM   1869 C  CA  . ILE A 1 215 ? -19.742 -11.110 15.390  1.00 9.05  ? 216 ILE A CA  1 
ATOM   1870 C  C   . ILE A 1 215 ? -19.199 -12.331 14.700  1.00 8.64  ? 216 ILE A C   1 
ATOM   1871 O  O   . ILE A 1 215 ? -18.032 -12.716 14.835  1.00 9.55  ? 216 ILE A O   1 
ATOM   1872 C  CB  . ILE A 1 215 ? -19.732 -9.886  14.450  1.00 10.59 ? 216 ILE A CB  1 
ATOM   1873 C  CG1 . ILE A 1 215 ? -18.330 -9.541  13.937  1.00 10.43 ? 216 ILE A CG1 1 
ATOM   1874 C  CG2 . ILE A 1 215 ? -20.419 -8.687  15.103  1.00 13.60 ? 216 ILE A CG2 1 
ATOM   1875 C  CD1 . ILE A 1 215 ? -18.378 -8.503  12.791  1.00 13.59 ? 216 ILE A CD1 1 
ATOM   1876 N  N   . SER A 1 216 ? -20.081 -12.991 13.933  1.00 9.84  ? 217 SER A N   1 
ATOM   1877 C  CA  A SER A 1 216 ? -19.716 -14.145 13.117  0.50 9.64  ? 217 SER A CA  1 
ATOM   1878 C  CA  B SER A 1 216 ? -19.670 -14.126 13.137  0.50 9.67  ? 217 SER A CA  1 
ATOM   1879 C  C   . SER A 1 216 ? -19.473 -13.677 11.705  1.00 9.23  ? 217 SER A C   1 
ATOM   1880 O  O   . SER A 1 216 ? -20.290 -12.938 11.170  1.00 10.27 ? 217 SER A O   1 
ATOM   1881 C  CB  A SER A 1 216 ? -20.783 -15.211 13.115  0.50 11.54 ? 217 SER A CB  1 
ATOM   1882 C  CB  B SER A 1 216 ? -20.690 -15.189 13.273  0.50 12.82 ? 217 SER A CB  1 
ATOM   1883 O  OG  A SER A 1 216 ? -20.881 -15.817 14.394  0.50 11.79 ? 217 SER A OG  1 
ATOM   1884 O  OG  B SER A 1 216 ? -20.373 -16.285 12.460  0.50 16.19 ? 217 SER A OG  1 
ATOM   1885 N  N   . VAL A 1 217 ? -18.364 -14.149 11.117  1.00 8.62  ? 218 VAL A N   1 
ATOM   1886 C  CA  . VAL A 1 217 ? -18.124 -13.943 9.706   1.00 9.26  ? 218 VAL A CA  1 
ATOM   1887 C  C   . VAL A 1 217 ? -17.886 -15.315 9.108   1.00 8.97  ? 218 VAL A C   1 
ATOM   1888 O  O   . VAL A 1 217 ? -17.526 -16.245 9.796   1.00 9.04  ? 218 VAL A O   1 
ATOM   1889 C  CB  . VAL A 1 217 ? -16.942 -13.005 9.472   1.00 9.87  ? 218 VAL A CB  1 
ATOM   1890 C  CG1 . VAL A 1 217 ? -17.192 -11.669 10.150  1.00 10.75 ? 218 VAL A CG1 1 
ATOM   1891 C  CG2 . VAL A 1 217 ? -15.642 -13.636 9.968   1.00 12.10 ? 218 VAL A CG2 1 
ATOM   1892 N  N   . SER A 1 218 ? -18.059 -15.453 7.789   1.00 9.76  ? 219 SER A N   1 
ATOM   1893 C  CA  . SER A 1 218 ? -17.862 -16.783 7.241   1.00 10.69 ? 219 SER A CA  1 
ATOM   1894 C  C   . SER A 1 218 ? -16.402 -17.015 6.918   1.00 9.49  ? 219 SER A C   1 
ATOM   1895 O  O   . SER A 1 218 ? -15.584 -16.098 6.753   1.00 10.53 ? 219 SER A O   1 
ATOM   1896 C  CB  . SER A 1 218 ? -18.692 -16.972 5.961   1.00 12.46 ? 219 SER A CB  1 
ATOM   1897 O  OG  . SER A 1 218 ? -18.218 -16.090 4.982   1.00 12.44 ? 219 SER A OG  1 
ATOM   1898 N  N   A SER A 1 219 ? -16.100 -18.311 6.750   0.50 10.58 ? 220 SER A N   1 
ATOM   1899 N  N   B SER A 1 219 ? -16.091 -18.298 6.716   0.50 10.72 ? 220 SER A N   1 
ATOM   1900 C  CA  A SER A 1 219 ? -14.770 -18.702 6.324   0.50 11.11 ? 220 SER A CA  1 
ATOM   1901 C  CA  B SER A 1 219 ? -14.738 -18.652 6.339   0.50 11.31 ? 220 SER A CA  1 
ATOM   1902 C  C   A SER A 1 219 ? -14.434 -17.962 5.026   0.50 11.86 ? 220 SER A C   1 
ATOM   1903 C  C   B SER A 1 219 ? -14.404 -18.010 4.987   0.50 12.36 ? 220 SER A C   1 
ATOM   1904 O  O   A SER A 1 219 ? -13.325 -17.444 4.877   0.50 13.43 ? 220 SER A O   1 
ATOM   1905 O  O   B SER A 1 219 ? -13.264 -17.605 4.754   0.50 12.54 ? 220 SER A O   1 
ATOM   1906 C  CB  A SER A 1 219 ? -14.665 -20.202 6.191   0.50 11.75 ? 220 SER A CB  1 
ATOM   1907 C  CB  B SER A 1 219 ? -14.608 -20.137 6.320   0.50 12.66 ? 220 SER A CB  1 
ATOM   1908 O  OG  A SER A 1 219 ? -15.633 -20.733 5.298   0.50 10.85 ? 220 SER A OG  1 
ATOM   1909 O  OG  B SER A 1 219 ? -13.287 -20.518 5.985   0.50 14.73 ? 220 SER A OG  1 
ATOM   1910 N  N   . GLU A 1 220 ? -15.396 -17.897 4.085   1.00 12.09 ? 221 GLU A N   1 
ATOM   1911 C  CA  . GLU A 1 220 ? -15.139 -17.247 2.812   1.00 14.18 ? 221 GLU A CA  1 
ATOM   1912 C  C   . GLU A 1 220 ? -14.824 -15.761 2.995   1.00 12.74 ? 221 GLU A C   1 
ATOM   1913 O  O   . GLU A 1 220 ? -13.987 -15.211 2.248   1.00 14.53 ? 221 GLU A O   1 
ATOM   1914 C  CB  . GLU A 1 220 ? -16.312 -17.380 1.839   1.00 16.36 ? 221 GLU A CB  1 
ATOM   1915 C  CG  . GLU A 1 220 ? -16.520 -18.860 1.408   1.00 21.77 ? 221 GLU A CG  1 
ATOM   1916 C  CD  . GLU A 1 220 ? -17.467 -19.651 2.319   1.00 22.99 ? 221 GLU A CD  1 
ATOM   1917 O  OE1 . GLU A 1 220 ? -17.886 -19.193 3.431   1.00 24.86 ? 221 GLU A OE1 1 
ATOM   1918 O  OE2 . GLU A 1 220 ? -17.817 -20.748 1.915   1.00 34.35 ? 221 GLU A OE2 1 
ATOM   1919 N  N   . GLN A 1 221 ? -15.495 -15.080 3.918   1.00 11.35 ? 222 GLN A N   1 
ATOM   1920 C  CA  . GLN A 1 221 ? -15.185 -13.678 4.156   1.00 11.28 ? 222 GLN A CA  1 
ATOM   1921 C  C   . GLN A 1 221 ? -13.778 -13.473 4.692   1.00 10.57 ? 222 GLN A C   1 
ATOM   1922 O  O   . GLN A 1 221 ? -13.008 -12.638 4.182   1.00 11.88 ? 222 GLN A O   1 
ATOM   1923 C  CB  . GLN A 1 221 ? -16.225 -13.116 5.108   1.00 11.14 ? 222 GLN A CB  1 
ATOM   1924 C  CG  . GLN A 1 221 ? -17.580 -12.985 4.417   1.00 11.33 ? 222 GLN A CG  1 
ATOM   1925 C  CD  . GLN A 1 221 ? -18.656 -12.444 5.299   1.00 10.41 ? 222 GLN A CD  1 
ATOM   1926 O  OE1 . GLN A 1 221 ? -18.763 -12.828 6.473   1.00 11.01 ? 222 GLN A OE1 1 
ATOM   1927 N  NE2 . GLN A 1 221 ? -19.483 -11.564 4.731   1.00 11.96 ? 222 GLN A NE2 1 
ATOM   1928 N  N   A VAL A 1 222 ? -13.370 -14.315 5.630   0.50 10.63 ? 223 VAL A N   1 
ATOM   1929 N  N   B VAL A 1 222 ? -13.378 -14.248 5.704   0.50 11.54 ? 223 VAL A N   1 
ATOM   1930 C  CA  A VAL A 1 222 ? -12.051 -14.060 6.179   0.50 10.32 ? 223 VAL A CA  1 
ATOM   1931 C  CA  B VAL A 1 222 ? -12.004 -14.125 6.187   0.50 11.98 ? 223 VAL A CA  1 
ATOM   1932 C  C   A VAL A 1 222 ? -10.940 -14.502 5.229   0.50 11.03 ? 223 VAL A C   1 
ATOM   1933 C  C   B VAL A 1 222 ? -10.977 -14.547 5.148   0.50 12.17 ? 223 VAL A C   1 
ATOM   1934 O  O   A VAL A 1 222 ? -9.888  -13.842 5.215   0.50 11.40 ? 223 VAL A O   1 
ATOM   1935 O  O   B VAL A 1 222 ? -9.880  -14.047 5.038   0.50 12.01 ? 223 VAL A O   1 
ATOM   1936 C  CB  A VAL A 1 222 ? -11.898 -14.657 7.584   0.50 11.34 ? 223 VAL A CB  1 
ATOM   1937 C  CB  B VAL A 1 222 ? -11.758 -14.896 7.494   0.50 15.32 ? 223 VAL A CB  1 
ATOM   1938 C  CG1 A VAL A 1 222 ? -11.799 -16.174 7.482   0.50 11.05 ? 223 VAL A CG1 1 
ATOM   1939 C  CG1 B VAL A 1 222 ? -10.386 -14.545 8.067   0.50 21.13 ? 223 VAL A CG1 1 
ATOM   1940 C  CG2 A VAL A 1 222 ? -10.719 -14.006 8.335   0.50 11.85 ? 223 VAL A CG2 1 
ATOM   1941 C  CG2 B VAL A 1 222 ? -12.831 -14.563 8.504   0.50 18.37 ? 223 VAL A CG2 1 
ATOM   1942 N  N   . LEU A 1 223 ? -11.216 -15.535 4.390   1.00 12.68 ? 224 LEU A N   1 
ATOM   1943 C  CA  . LEU A 1 223 ? -10.272 -15.877 3.337   1.00 14.15 ? 224 LEU A CA  1 
ATOM   1944 C  C   . LEU A 1 223 ? -10.020 -14.703 2.385   1.00 13.02 ? 224 LEU A C   1 
ATOM   1945 O  O   . LEU A 1 223 ? -8.913  -14.561 1.921   1.00 13.84 ? 224 LEU A O   1 
ATOM   1946 C  CB  . LEU A 1 223 ? -10.739 -17.109 2.579   1.00 15.04 ? 224 LEU A CB  1 
ATOM   1947 C  CG  . LEU A 1 223 ? -10.607 -18.376 3.423   1.00 18.22 ? 224 LEU A CG  1 
ATOM   1948 C  CD2 . LEU A 1 223 ? -9.144  -18.820 3.519   1.00 19.48 ? 224 LEU A CD2 1 
ATOM   1949 N  N   . LYS A 1 224 ? -11.018 -13.853 2.133   1.00 14.45 ? 225 LYS A N   1 
ATOM   1950 C  CA  . LYS A 1 224 ? -10.798 -12.677 1.296   1.00 13.84 ? 225 LYS A CA  1 
ATOM   1951 C  C   . LYS A 1 224 ? -9.838  -11.694 1.994   1.00 12.06 ? 225 LYS A C   1 
ATOM   1952 O  O   . LYS A 1 224 ? -8.976  -11.098 1.334   1.00 13.91 ? 225 LYS A O   1 
ATOM   1953 C  CB  . LYS A 1 224 ? -12.116 -12.135 0.738   1.00 17.02 ? 225 LYS A CB  1 
ATOM   1954 C  CG  . LYS A 1 224 ? -12.791 -13.115 -0.225  1.00 22.28 ? 225 LYS A CG  1 
ATOM   1955 C  CD  . LYS A 1 224 ? -14.010 -12.510 -0.847  1.00 32.87 ? 225 LYS A CD  1 
ATOM   1956 N  N   . PHE A 1 225 ? -9.932  -11.510 3.313   1.00 12.26 ? 226 PHE A N   1 
ATOM   1957 C  CA  . PHE A 1 225 ? -8.963  -10.667 4.018   1.00 12.04 ? 226 PHE A CA  1 
ATOM   1958 C  C   . PHE A 1 225 ? -7.575  -11.218 3.779   1.00 11.65 ? 226 PHE A C   1 
ATOM   1959 O  O   . PHE A 1 225 ? -6.623  -10.445 3.588   1.00 11.53 ? 226 PHE A O   1 
ATOM   1960 C  CB  . PHE A 1 225 ? -9.167  -10.680 5.534   1.00 11.96 ? 226 PHE A CB  1 
ATOM   1961 C  CG  . PHE A 1 225 ? -10.347 -9.955  6.113   1.00 11.67 ? 226 PHE A CG  1 
ATOM   1962 C  CD1 . PHE A 1 225 ? -11.342 -9.448  5.292   1.00 16.89 ? 226 PHE A CD1 1 
ATOM   1963 C  CD2 . PHE A 1 225 ? -10.469 -9.776  7.482   1.00 15.12 ? 226 PHE A CD2 1 
ATOM   1964 C  CE1 . PHE A 1 225 ? -12.431 -8.779  5.827   1.00 16.87 ? 226 PHE A CE1 1 
ATOM   1965 C  CE2 . PHE A 1 225 ? -11.559 -9.106  8.016   1.00 15.70 ? 226 PHE A CE2 1 
ATOM   1966 C  CZ  . PHE A 1 225 ? -12.538 -8.609  7.188   1.00 16.05 ? 226 PHE A CZ  1 
ATOM   1967 N  N   . ARG A 1 226 ? -7.422  -12.549 3.794   1.00 11.23 ? 227 ARG A N   1 
ATOM   1968 C  CA  . ARG A 1 226 ? -6.106  -13.165 3.731   1.00 12.15 ? 227 ARG A CA  1 
ATOM   1969 C  C   . ARG A 1 226 ? -5.514  -13.147 2.337   1.00 12.40 ? 227 ARG A C   1 
ATOM   1970 O  O   . ARG A 1 226 ? -4.375  -13.547 2.171   1.00 13.89 ? 227 ARG A O   1 
ATOM   1971 C  CB  . ARG A 1 226 ? -6.159  -14.600 4.270   1.00 12.79 ? 227 ARG A CB  1 
ATOM   1972 C  CG  . ARG A 1 226 ? -6.580  -14.704 5.733   1.00 12.20 ? 227 ARG A CG  1 
ATOM   1973 C  CD  . ARG A 1 226 ? -6.542  -16.141 6.137   1.00 13.76 ? 227 ARG A CD  1 
ATOM   1974 N  NE  . ARG A 1 226 ? -7.036  -16.292 7.517   1.00 11.70 ? 227 ARG A NE  1 
ATOM   1975 C  CZ  . ARG A 1 226 ? -7.914  -17.205 7.919   1.00 11.73 ? 227 ARG A CZ  1 
ATOM   1976 N  NH1 . ARG A 1 226 ? -8.328  -18.141 7.055   1.00 17.57 ? 227 ARG A NH1 1 
ATOM   1977 N  NH2 . ARG A 1 226 ? -8.340  -17.208 9.161   1.00 13.65 ? 227 ARG A NH2 1 
ATOM   1978 N  N   . LYS A 1 227 ? -6.263  -12.662 1.344   1.00 11.95 ? 228 LYS A N   1 
ATOM   1979 C  CA  . LYS A 1 227 ? -5.724  -12.517 -0.003  1.00 13.14 ? 228 LYS A CA  1 
ATOM   1980 C  C   . LYS A 1 227 ? -5.089  -11.144 -0.209  1.00 14.64 ? 228 LYS A C   1 
ATOM   1981 O  O   . LYS A 1 227 ? -4.398  -10.916 -1.206  1.00 15.65 ? 228 LYS A O   1 
ATOM   1982 C  CB  . LYS A 1 227 ? -6.844  -12.697 -1.030  1.00 14.08 ? 228 LYS A CB  1 
ATOM   1983 C  CG  . LYS A 1 227 ? -7.363  -14.107 -1.145  1.00 16.10 ? 228 LYS A CG  1 
ATOM   1984 C  CD  . LYS A 1 227 ? -8.389  -14.286 -2.247  1.00 20.93 ? 228 LYS A CD  1 
ATOM   1985 C  CE  . LYS A 1 227 ? -7.769  -14.374 -3.639  1.00 32.51 ? 228 LYS A CE  1 
ATOM   1986 N  NZ  . LYS A 1 227 ? -8.770  -14.558 -4.713  1.00 46.85 ? 228 LYS A NZ  1 
ATOM   1987 N  N   . LEU A 1 228 ? -5.294  -10.209 0.728   1.00 12.79 ? 229 LEU A N   1 
ATOM   1988 C  CA  . LEU A 1 228 ? -4.644  -8.923  0.669   1.00 13.79 ? 229 LEU A CA  1 
ATOM   1989 C  C   . LEU A 1 228 ? -3.149  -9.126  0.800   1.00 14.09 ? 229 LEU A C   1 
ATOM   1990 O  O   . LEU A 1 228 ? -2.630  -10.168 1.244   1.00 13.35 ? 229 LEU A O   1 
ATOM   1991 C  CB  . LEU A 1 228 ? -5.162  -7.970  1.757   1.00 14.81 ? 229 LEU A CB  1 
ATOM   1992 C  CG  . LEU A 1 228 ? -6.614  -7.521  1.606   1.00 15.21 ? 229 LEU A CG  1 
ATOM   1993 C  CD1 . LEU A 1 228 ? -7.114  -6.884  2.899   1.00 15.70 ? 229 LEU A CD1 1 
ATOM   1994 C  CD2 . LEU A 1 228 ? -6.732  -6.523  0.437   1.00 16.38 ? 229 LEU A CD2 1 
ATOM   1995 N  N   . ASN A 1 229 ? -2.447  -8.083  0.385   1.00 15.35 ? 230 ASN A N   1 
ATOM   1996 C  CA  . ASN A 1 229 ? -0.994  -8.138  0.399   1.00 15.80 ? 230 ASN A CA  1 
ATOM   1997 C  C   . ASN A 1 229 ? -0.392  -6.994  1.231   1.00 15.30 ? 230 ASN A C   1 
ATOM   1998 O  O   . ASN A 1 229 ? -0.862  -5.855  1.187   1.00 17.66 ? 230 ASN A O   1 
ATOM   1999 C  CB  . ASN A 1 229 ? -0.406  -7.916  -1.001  1.00 18.96 ? 230 ASN A CB  1 
ATOM   2000 C  CG  . ASN A 1 229 ? -0.477  -9.079  -1.955  1.00 19.47 ? 230 ASN A CG  1 
ATOM   2001 O  OD1 . ASN A 1 229 ? 0.022   -8.936  -3.070  1.00 23.42 ? 230 ASN A OD1 1 
ATOM   2002 N  ND2 . ASN A 1 229 ? -1.163  -10.176 -1.649  1.00 19.62 ? 230 ASN A ND2 1 
ATOM   2003 N  N   . PHE A 1 230 ? 0.690   -7.319  1.989   1.00 15.42 ? 231 PHE A N   1 
ATOM   2004 C  CA  . PHE A 1 230 ? 1.432   -6.253  2.658   1.00 16.35 ? 231 PHE A CA  1 
ATOM   2005 C  C   . PHE A 1 230 ? 2.344   -5.466  1.716   1.00 18.82 ? 231 PHE A C   1 
ATOM   2006 O  O   . PHE A 1 230 ? 2.597   -4.320  1.980   1.00 17.73 ? 231 PHE A O   1 
ATOM   2007 C  CB  . PHE A 1 230 ? 2.424   -6.861  3.650   1.00 17.10 ? 231 PHE A CB  1 
ATOM   2008 C  CG  . PHE A 1 230 ? 1.875   -7.469  4.931   1.00 16.10 ? 231 PHE A CG  1 
ATOM   2009 C  CD1 . PHE A 1 230 ? 1.148   -6.710  5.829   1.00 16.72 ? 231 PHE A CD1 1 
ATOM   2010 C  CD2 . PHE A 1 230 ? 2.222   -8.751  5.328   1.00 15.16 ? 231 PHE A CD2 1 
ATOM   2011 C  CE1 . PHE A 1 230 ? 0.730   -7.219  7.049   1.00 15.81 ? 231 PHE A CE1 1 
ATOM   2012 C  CE2 . PHE A 1 230 ? 1.808   -9.279  6.551   1.00 15.02 ? 231 PHE A CE2 1 
ATOM   2013 C  CZ  . PHE A 1 230 ? 1.036   -8.513  7.412   1.00 14.32 ? 231 PHE A CZ  1 
ATOM   2014 N  N   A ASN A 1 231 ? 2.674   -6.006  0.520   0.50 18.49 ? 232 ASN A N   1 
ATOM   2015 N  N   B ASN A 1 231 ? 3.005   -6.193  0.788   0.50 22.35 ? 232 ASN A N   1 
ATOM   2016 C  CA  A ASN A 1 231 ? 3.449   -5.342  -0.532  0.50 13.86 ? 232 ASN A CA  1 
ATOM   2017 C  CA  B ASN A 1 231 ? 4.019   -5.667  -0.132  0.50 21.06 ? 232 ASN A CA  1 
ATOM   2018 C  C   A ASN A 1 231 ? 2.519   -4.493  -1.416  0.50 13.18 ? 232 ASN A C   1 
ATOM   2019 C  C   B ASN A 1 231 ? 3.340   -4.738  -1.141  0.50 21.67 ? 232 ASN A C   1 
ATOM   2020 O  O   A ASN A 1 231 ? 1.310   -4.638  -1.576  0.50 14.11 ? 232 ASN A O   1 
ATOM   2021 O  O   B ASN A 1 231 ? 2.132   -4.773  -1.392  0.50 21.57 ? 232 ASN A O   1 
ATOM   2022 C  CB  A ASN A 1 231 ? 4.089   -6.440  -1.369  0.50 17.47 ? 232 ASN A CB  1 
ATOM   2023 C  CB  B ASN A 1 231 ? 4.752   -6.809  -0.859  0.50 20.38 ? 232 ASN A CB  1 
ATOM   2024 C  CG  A ASN A 1 231 ? 3.041   -7.399  -1.860  0.50 17.40 ? 232 ASN A CG  1 
ATOM   2025 C  CG  B ASN A 1 231 ? 3.835   -7.740  -1.623  0.50 21.43 ? 232 ASN A CG  1 
ATOM   2026 O  OD1 A ASN A 1 231 ? 2.664   -8.341  -1.128  0.50 19.85 ? 232 ASN A OD1 1 
ATOM   2027 O  OD1 B ASN A 1 231 ? 3.716   -7.690  -2.866  0.50 22.31 ? 232 ASN A OD1 1 
ATOM   2028 N  ND2 A ASN A 1 231 ? 2.602   -7.153  -3.105  0.50 15.28 ? 232 ASN A ND2 1 
ATOM   2029 N  ND2 B ASN A 1 231 ? 3.220   -8.651  -0.880  0.50 22.83 ? 232 ASN A ND2 1 
ATOM   2030 N  N   A GLY A 1 232 ? 3.195   -3.582  -2.153  0.50 14.21 ? 233 GLY A N   1 
ATOM   2031 N  N   B GLY A 1 232 ? 4.156   -3.878  -1.767  0.50 19.43 ? 233 GLY A N   1 
ATOM   2032 C  CA  A GLY A 1 232 ? 2.607   -2.796  -3.211  0.50 12.30 ? 233 GLY A CA  1 
ATOM   2033 C  CA  B GLY A 1 232 ? 3.669   -3.054  -2.876  0.50 29.09 ? 233 GLY A CA  1 
ATOM   2034 C  C   A GLY A 1 232 ? 2.673   -3.552  -4.524  0.50 13.61 ? 233 GLY A C   1 
ATOM   2035 C  C   B GLY A 1 232 ? 3.529   -3.923  -4.136  0.50 26.10 ? 233 GLY A C   1 
ATOM   2036 O  O   A GLY A 1 232 ? 3.386   -4.532  -4.637  0.50 17.06 ? 233 GLY A O   1 
ATOM   2037 O  O   B GLY A 1 232 ? 4.068   -5.052  -4.123  0.50 30.67 ? 233 GLY A O   1 
ATOM   2038 N  N   A GLU A 1 233 ? 1.902   -3.062  -5.500  0.50 11.48 ? 234 GLU A N   1 
ATOM   2039 N  N   B GLU A 1 233 ? 2.674   -3.456  -5.089  0.50 22.29 ? 234 GLU A N   1 
ATOM   2040 C  CA  A GLU A 1 233 ? 1.834   -3.626  -6.847  0.50 14.34 ? 234 GLU A CA  1 
ATOM   2041 C  CA  B GLU A 1 233 ? 2.530   -3.940  -6.462  0.50 22.14 ? 234 GLU A CA  1 
ATOM   2042 C  C   A GLU A 1 233 ? 3.233   -3.723  -7.426  0.50 15.34 ? 234 GLU A C   1 
ATOM   2043 C  C   B GLU A 1 233 ? 3.931   -4.037  -7.044  0.50 21.56 ? 234 GLU A C   1 
ATOM   2044 O  O   A GLU A 1 233 ? 4.036   -2.797  -7.326  0.50 18.00 ? 234 GLU A O   1 
ATOM   2045 O  O   B GLU A 1 233 ? 4.770   -3.137  -6.939  0.50 26.31 ? 234 GLU A O   1 
ATOM   2046 C  CB  A GLU A 1 233 ? 0.868   -2.815  -7.712  0.50 16.14 ? 234 GLU A CB  1 
ATOM   2047 C  CB  B GLU A 1 233 ? 1.604   -3.055  -7.327  0.50 20.67 ? 234 GLU A CB  1 
ATOM   2048 C  CG  A GLU A 1 233 ? 0.690   -3.326  -9.143  0.50 20.87 ? 234 GLU A CG  1 
ATOM   2049 C  CG  B GLU A 1 233 ? 1.125   -3.705  -8.645  0.50 26.90 ? 234 GLU A CG  1 
ATOM   2050 C  CD  A GLU A 1 233 ? -0.687  -3.041  -9.736  0.50 28.34 ? 234 GLU A CD  1 
ATOM   2051 C  CD  B GLU A 1 233 ? 0.428   -2.838  -9.699  0.50 30.50 ? 234 GLU A CD  1 
ATOM   2052 O  OE1 A GLU A 1 233 ? -1.656  -2.854  -8.952  0.50 36.76 ? 234 GLU A OE1 1 
ATOM   2053 O  OE1 B GLU A 1 233 ? -0.018  -1.689  -9.382  0.50 36.57 ? 234 GLU A OE1 1 
ATOM   2054 O  OE2 A GLU A 1 233 ? -0.796  -3.005  -10.982 0.50 32.99 ? 234 GLU A OE2 1 
ATOM   2055 O  OE2 B GLU A 1 233 ? 0.353   -3.311  -10.884 0.50 30.50 ? 234 GLU A OE2 1 
ATOM   2056 N  N   A GLY A 1 234 ? 3.489   -4.849  -8.088  0.50 18.78 ? 235 GLY A N   1 
ATOM   2057 N  N   B GLY A 1 234 ? 4.199   -5.206  -7.622  0.50 27.08 ? 235 GLY A N   1 
ATOM   2058 C  CA  A GLY A 1 234 ? 4.769   -4.993  -8.740  0.50 19.04 ? 235 GLY A CA  1 
ATOM   2059 C  CA  B GLY A 1 234 ? 5.483   -5.406  -8.258  0.50 28.39 ? 235 GLY A CA  1 
ATOM   2060 C  C   A GLY A 1 234 ? 5.898   -5.355  -7.778  0.50 19.45 ? 235 GLY A C   1 
ATOM   2061 C  C   B GLY A 1 234 ? 6.646   -5.650  -7.296  0.50 34.11 ? 235 GLY A C   1 
ATOM   2062 O  O   A GLY A 1 234 ? 7.051   -5.379  -8.196  0.50 26.31 ? 235 GLY A O   1 
ATOM   2063 O  O   B GLY A 1 234 ? 7.801   -5.456  -7.686  0.50 35.53 ? 235 GLY A O   1 
ATOM   2064 N  N   A GLU A 1 235 ? 5.583   -5.704  -6.538  0.50 20.06 ? 236 GLU A N   1 
ATOM   2065 N  N   B GLU A 1 235 ? 6.354   -6.025  -6.034  0.50 31.13 ? 236 GLU A N   1 
ATOM   2066 C  CA  A GLU A 1 235 ? 6.508   -6.248  -5.559  0.50 18.68 ? 236 GLU A CA  1 
ATOM   2067 C  CA  B GLU A 1 235 ? 7.330   -6.584  -5.095  0.50 26.80 ? 236 GLU A CA  1 
ATOM   2068 C  C   A GLU A 1 235 ? 6.038   -7.654  -5.224  0.50 15.62 ? 236 GLU A C   1 
ATOM   2069 C  C   B GLU A 1 235 ? 6.930   -8.017  -4.734  0.50 27.85 ? 236 GLU A C   1 
ATOM   2070 O  O   A GLU A 1 235 ? 4.882   -8.040  -5.419  0.50 21.53 ? 236 GLU A O   1 
ATOM   2071 O  O   B GLU A 1 235 ? 5.800   -8.464  -5.011  0.50 33.76 ? 236 GLU A O   1 
ATOM   2072 C  CB  A GLU A 1 235 ? 6.433   -5.448  -4.249  0.50 19.60 ? 236 GLU A CB  1 
ATOM   2073 C  CB  B GLU A 1 235 ? 7.403   -5.864  -3.737  0.50 26.90 ? 236 GLU A CB  1 
ATOM   2074 C  CG  A GLU A 1 235 ? 7.051   -4.059  -4.348  0.50 20.03 ? 236 GLU A CG  1 
ATOM   2075 C  CG  B GLU A 1 235 ? 8.026   -4.463  -3.799  0.50 31.44 ? 236 GLU A CG  1 
ATOM   2076 C  CD  A GLU A 1 235 ? 6.718   -3.060  -3.254  0.50 26.24 ? 236 GLU A CD  1 
ATOM   2077 C  CD  B GLU A 1 235 ? 7.832   -3.591  -2.566  0.50 41.58 ? 236 GLU A CD  1 
ATOM   2078 O  OE1 A GLU A 1 235 ? 5.994   -3.461  -2.275  0.50 21.10 ? 236 GLU A OE1 1 
ATOM   2079 O  OE1 B GLU A 1 235 ? 7.216   -4.073  -1.573  0.50 40.16 ? 236 GLU A OE1 1 
ATOM   2080 O  OE2 A GLU A 1 235 ? 7.145   -1.885  -3.374  0.50 32.72 ? 236 GLU A OE2 1 
ATOM   2081 O  OE2 B GLU A 1 235 ? 8.275   -2.418  -2.596  0.50 55.65 ? 236 GLU A OE2 1 
ATOM   2082 N  N   A PRO A 1 236 ? 6.984   -8.466  -4.713  0.50 12.78 ? 237 PRO A N   1 
ATOM   2083 N  N   B PRO A 1 236 ? 7.858   -8.763  -4.077  0.50 27.89 ? 237 PRO A N   1 
ATOM   2084 C  CA  A PRO A 1 236 ? 6.785   -9.859  -4.353  0.50 18.96 ? 237 PRO A CA  1 
ATOM   2085 C  CA  B PRO A 1 236 ? 7.702   -10.202 -3.817  0.50 23.91 ? 237 PRO A CA  1 
ATOM   2086 C  C   A PRO A 1 236 ? 5.589   -9.898  -3.402  0.50 16.48 ? 237 PRO A C   1 
ATOM   2087 C  C   B PRO A 1 236 ? 6.543   -10.384 -2.832  0.50 24.48 ? 237 PRO A C   1 
ATOM   2088 O  O   A PRO A 1 236 ? 5.462   -9.045  -2.512  0.50 19.45 ? 237 PRO A O   1 
ATOM   2089 O  O   B PRO A 1 236 ? 6.402   -9.634  -1.827  0.50 17.50 ? 237 PRO A O   1 
ATOM   2090 C  CB  A PRO A 1 236 ? 8.101   -10.296 -3.625  0.50 22.04 ? 237 PRO A CB  1 
ATOM   2091 C  CB  B PRO A 1 236 ? 8.892   -10.620 -2.936  0.50 24.73 ? 237 PRO A CB  1 
ATOM   2092 C  CG  A PRO A 1 236 ? 9.094   -9.118  -3.823  0.50 23.76 ? 237 PRO A CG  1 
ATOM   2093 C  CG  B PRO A 1 236 ? 9.943   -9.482  -3.227  0.50 28.62 ? 237 PRO A CG  1 
ATOM   2094 C  CD  A PRO A 1 236 ? 8.397   -8.080  -4.678  0.50 19.15 ? 237 PRO A CD  1 
ATOM   2095 C  CD  B PRO A 1 236 ? 9.163   -8.250  -3.647  0.50 30.70 ? 237 PRO A CD  1 
ATOM   2096 N  N   A GLU A 1 237 ? 4.749   -10.926 -3.603  0.50 17.18 ? 238 GLU A N   1 
ATOM   2097 N  N   B GLU A 1 237 ? 5.691   -11.388 -3.082  0.50 22.45 ? 238 GLU A N   1 
ATOM   2098 C  CA  A GLU A 1 237 ? 3.517   -11.024 -2.848  0.50 15.63 ? 238 GLU A CA  1 
ATOM   2099 C  CA  B GLU A 1 237 ? 4.382   -11.500 -2.438  0.50 17.99 ? 238 GLU A CA  1 
ATOM   2100 C  C   A GLU A 1 237 ? 3.773   -11.432 -1.391  0.50 12.50 ? 238 GLU A C   1 
ATOM   2101 C  C   B GLU A 1 237 ? 4.517   -12.026 -1.010  0.50 17.23 ? 238 GLU A C   1 
ATOM   2102 O  O   A GLU A 1 237 ? 4.478   -12.397 -1.097  0.50 12.58 ? 238 GLU A O   1 
ATOM   2103 O  O   B GLU A 1 237 ? 5.002   -13.115 -0.799  0.50 15.09 ? 238 GLU A O   1 
ATOM   2104 C  CB  A GLU A 1 237 ? 2.556   -12.029 -3.501  0.50 18.33 ? 238 GLU A CB  1 
ATOM   2105 C  CB  B GLU A 1 237 ? 3.418   -12.402 -3.241  0.50 18.73 ? 238 GLU A CB  1 
ATOM   2106 C  CG  A GLU A 1 237 ? 1.287   -12.122 -2.692  0.50 19.68 ? 238 GLU A CG  1 
ATOM   2107 C  CG  B GLU A 1 237 ? 2.021   -12.359 -2.644  0.50 23.62 ? 238 GLU A CG  1 
ATOM   2108 C  CD  A GLU A 1 237 ? 0.168   -12.918 -3.339  0.50 20.53 ? 238 GLU A CD  1 
ATOM   2109 C  CD  B GLU A 1 237 ? 0.898   -13.027 -3.421  0.50 24.06 ? 238 GLU A CD  1 
ATOM   2110 O  OE1 A GLU A 1 237 ? 0.480   -14.085 -3.706  0.50 20.06 ? 238 GLU A OE1 1 
ATOM   2111 O  OE1 B GLU A 1 237 ? 1.246   -13.813 -4.314  0.50 32.76 ? 238 GLU A OE1 1 
ATOM   2112 O  OE2 A GLU A 1 237 ? -0.966  -12.354 -3.521  0.50 17.02 ? 238 GLU A OE2 1 
ATOM   2113 O  OE2 B GLU A 1 237 ? -0.315  -12.728 -3.149  0.50 26.03 ? 238 GLU A OE2 1 
ATOM   2114 N  N   A GLU A 1 238 ? 3.284   -10.626 -0.466  0.50 11.38 ? 239 GLU A N   1 
ATOM   2115 N  N   B GLU A 1 238 ? 4.081   -11.229 -0.043  0.50 13.59 ? 239 GLU A N   1 
ATOM   2116 C  CA  A GLU A 1 238 ? 3.410   -10.932 0.983   0.50 12.29 ? 239 GLU A CA  1 
ATOM   2117 C  CA  B GLU A 1 238 ? 3.875   -11.578 1.398   0.50 12.38 ? 239 GLU A CA  1 
ATOM   2118 C  C   A GLU A 1 238 ? 1.983   -11.018 1.505   0.50 10.51 ? 239 GLU A C   1 
ATOM   2119 C  C   B GLU A 1 238 ? 2.418   -11.223 1.812   0.50 12.13 ? 239 GLU A C   1 
ATOM   2120 O  O   A GLU A 1 238 ? 1.331   -9.956  1.552   0.50 10.52 ? 239 GLU A O   1 
ATOM   2121 O  O   B GLU A 1 238 ? 2.159   -10.018 2.000   0.50 12.18 ? 239 GLU A O   1 
ATOM   2122 C  CB  A GLU A 1 238 ? 4.113   -9.794  1.719   0.50 13.53 ? 239 GLU A CB  1 
ATOM   2123 C  CB  B GLU A 1 238 ? 4.880   -10.829 2.281   0.50 12.09 ? 239 GLU A CB  1 
ATOM   2124 C  CG  A GLU A 1 238 ? 5.575   -9.689  1.361   0.50 16.90 ? 239 GLU A CG  1 
ATOM   2125 C  CG  B GLU A 1 238 ? 6.338   -11.213 2.054   0.50 14.10 ? 239 GLU A CG  1 
ATOM   2126 C  CD  A GLU A 1 238 ? 6.421   -8.753  2.202   0.50 20.83 ? 239 GLU A CD  1 
ATOM   2127 C  CD  B GLU A 1 238 ? 7.331   -10.506 2.968   0.50 14.63 ? 239 GLU A CD  1 
ATOM   2128 O  OE1 A GLU A 1 238 ? 6.006   -7.622  2.474   0.50 28.67 ? 239 GLU A OE1 1 
ATOM   2129 O  OE1 B GLU A 1 238 ? 7.238   -10.639 4.181   0.50 17.62 ? 239 GLU A OE1 1 
ATOM   2130 O  OE2 A GLU A 1 238 ? 7.598   -9.091  2.415   0.50 26.76 ? 239 GLU A OE2 1 
ATOM   2131 O  OE2 B GLU A 1 238 ? 8.195   -9.731  2.484   0.50 16.00 ? 239 GLU A OE2 1 
ATOM   2132 N  N   . LEU A 1 239 ? 1.485   -12.203 1.860   1.00 11.88 ? 240 LEU A N   1 
ATOM   2133 C  CA  . LEU A 1 239 ? 0.089   -12.086 2.225   1.00 10.98 ? 240 LEU A CA  1 
ATOM   2134 C  C   . LEU A 1 239 ? -0.064  -11.306 3.537   1.00 10.62 ? 240 LEU A C   1 
ATOM   2135 O  O   . LEU A 1 239 ? 0.710   -11.497 4.498   1.00 13.04 ? 240 LEU A O   1 
ATOM   2136 C  CB  . LEU A 1 239 ? -0.521  -13.468 2.405   1.00 12.01 ? 240 LEU A CB  1 
ATOM   2137 C  CG  . LEU A 1 239 ? -0.623  -14.337 1.166   1.00 12.36 ? 240 LEU A CG  1 
ATOM   2138 C  CD1 . LEU A 1 239 ? -1.302  -15.637 1.591   1.00 15.75 ? 240 LEU A CD1 1 
ATOM   2139 C  CD2 . LEU A 1 239 ? -1.394  -13.678 0.061   1.00 14.98 ? 240 LEU A CD2 1 
ATOM   2140 N  N   . MET A 1 240 ? -1.081  -10.443 3.539   1.00 11.95 ? 241 MET A N   1 
ATOM   2141 C  CA  . MET A 1 240 ? -1.384  -9.660  4.725   1.00 13.63 ? 241 MET A CA  1 
ATOM   2142 C  C   . MET A 1 240 ? -2.176  -10.580 5.656   1.00 10.73 ? 241 MET A C   1 
ATOM   2143 O  O   . MET A 1 240 ? -3.394  -10.712 5.538   1.00 11.60 ? 241 MET A O   1 
ATOM   2144 C  CB  . MET A 1 240 ? -2.235  -8.476  4.266   1.00 14.14 ? 241 MET A CB  1 
ATOM   2145 C  CG  . MET A 1 240 ? -2.546  -7.509  5.494   1.00 14.21 ? 241 MET A CG  1 
ATOM   2146 S  SD  . MET A 1 240 ? -3.511  -6.068  5.021   1.00 15.77 ? 241 MET A SD  1 
ATOM   2147 C  CE  . MET A 1 240 ? -2.213  -5.049  4.308   1.00 14.81 ? 241 MET A CE  1 
ATOM   2148 N  N   . VAL A 1 241 ? -1.438  -11.191 6.586   1.00 10.47 ? 242 VAL A N   1 
ATOM   2149 C  CA  . VAL A 1 241 ? -2.005  -12.092 7.589   1.00 10.05 ? 242 VAL A CA  1 
ATOM   2150 C  C   . VAL A 1 241 ? -1.190  -11.894 8.857   1.00 8.75  ? 242 VAL A C   1 
ATOM   2151 O  O   . VAL A 1 241 ? -0.036  -11.495 8.792   1.00 10.26 ? 242 VAL A O   1 
ATOM   2152 C  CB  . VAL A 1 241 ? -1.944  -13.567 7.165   1.00 11.28 ? 242 VAL A CB  1 
ATOM   2153 C  CG1 . VAL A 1 241 ? -2.866  -13.848 5.983   1.00 12.50 ? 242 VAL A CG1 1 
ATOM   2154 C  CG2 . VAL A 1 241 ? -0.514  -14.066 6.980   1.00 12.35 ? 242 VAL A CG2 1 
ATOM   2155 N  N   . ASP A 1 242 ? -1.822  -12.168 10.001  1.00 9.10  ? 243 ASP A N   1 
ATOM   2156 C  CA  . ASP A 1 242 ? -1.135  -12.046 11.271  1.00 9.59  ? 243 ASP A CA  1 
ATOM   2157 C  C   . ASP A 1 242 ? -0.656  -10.625 11.542  1.00 8.89  ? 243 ASP A C   1 
ATOM   2158 O  O   . ASP A 1 242 ? 0.463   -10.410 12.051  1.00 10.73 ? 243 ASP A O   1 
ATOM   2159 C  CB  . ASP A 1 242 ? -0.055  -13.114 11.499  1.00 10.07 ? 243 ASP A CB  1 
ATOM   2160 C  CG  . ASP A 1 242 ? -0.654  -14.502 11.596  1.00 9.80  ? 243 ASP A CG  1 
ATOM   2161 O  OD1 . ASP A 1 242 ? -1.691  -14.669 12.266  1.00 9.53  ? 243 ASP A OD1 1 
ATOM   2162 O  OD2 . ASP A 1 242 ? -0.064  -15.423 10.989  1.00 12.57 ? 243 ASP A OD2 1 
ATOM   2163 N  N   . ASN A 1 243 ? -1.532  -9.663  11.226  1.00 8.22  ? 244 ASN A N   1 
ATOM   2164 C  CA  . ASN A 1 243 ? -1.244  -8.249  11.457  1.00 8.02  ? 244 ASN A CA  1 
ATOM   2165 C  C   . ASN A 1 243 ? -1.791  -7.777  12.809  1.00 7.16  ? 244 ASN A C   1 
ATOM   2166 O  O   . ASN A 1 243 ? -2.437  -6.756  12.895  1.00 8.95  ? 244 ASN A O   1 
ATOM   2167 C  CB  . ASN A 1 243 ? -1.738  -7.385  10.306  1.00 9.23  ? 244 ASN A CB  1 
ATOM   2168 C  CG  . ASN A 1 243 ? -3.223  -7.535  10.051  1.00 8.57  ? 244 ASN A CG  1 
ATOM   2169 O  OD1 . ASN A 1 243 ? -3.859  -8.407  10.598  1.00 10.22 ? 244 ASN A OD1 1 
ATOM   2170 N  ND2 . ASN A 1 243 ? -3.769  -6.677  9.197   1.00 11.07 ? 244 ASN A ND2 1 
ATOM   2171 N  N   . TRP A 1 244 ? -1.501  -8.551  13.840  1.00 7.85  ? 245 TRP A N   1 
ATOM   2172 C  CA  . TRP A 1 244 ? -1.933  -8.306  15.221  1.00 7.36  ? 245 TRP A CA  1 
ATOM   2173 C  C   . TRP A 1 244 ? -0.713  -8.193  16.128  1.00 7.35  ? 245 TRP A C   1 
ATOM   2174 O  O   . TRP A 1 244 ? 0.244   -8.936  15.971  1.00 9.36  ? 245 TRP A O   1 
ATOM   2175 C  CB  . TRP A 1 244 ? -2.923  -9.386  15.687  1.00 7.30  ? 245 TRP A CB  1 
ATOM   2176 C  CG  . TRP A 1 244 ? -2.470  -10.793 15.523  1.00 7.19  ? 245 TRP A CG  1 
ATOM   2177 C  CD1 . TRP A 1 244 ? -2.582  -11.549 14.373  1.00 7.66  ? 245 TRP A CD1 1 
ATOM   2178 C  CD2 . TRP A 1 244 ? -1.863  -11.667 16.477  1.00 7.76  ? 245 TRP A CD2 1 
ATOM   2179 N  NE1 . TRP A 1 244 ? -2.093  -12.802 14.548  1.00 8.51  ? 245 TRP A NE1 1 
ATOM   2180 C  CE2 . TRP A 1 244 ? -1.612  -12.899 15.835  1.00 8.46  ? 245 TRP A CE2 1 
ATOM   2181 C  CE3 . TRP A 1 244 ? -1.529  -11.523 17.834  1.00 8.85  ? 245 TRP A CE3 1 
ATOM   2182 C  CZ2 . TRP A 1 244 ? -1.044  -13.981 16.531  1.00 9.21  ? 245 TRP A CZ2 1 
ATOM   2183 C  CZ3 . TRP A 1 244 ? -0.993  -12.607 18.513  1.00 11.29 ? 245 TRP A CZ3 1 
ATOM   2184 C  CH2 . TRP A 1 244 ? -0.737  -13.829 17.855  1.00 9.98  ? 245 TRP A CH2 1 
ATOM   2185 N  N   . ARG A 1 245 ? -0.843  -7.280  17.064  1.00 7.34  ? 246 ARG A N   1 
ATOM   2186 C  CA  . ARG A 1 245 ? 0.111   -7.169  18.172  1.00 7.76  ? 246 ARG A CA  1 
ATOM   2187 C  C   . ARG A 1 245 ? -0.369  -8.092  19.291  1.00 7.38  ? 246 ARG A C   1 
ATOM   2188 O  O   . ARG A 1 245 ? -1.549  -8.091  19.633  1.00 8.05  ? 246 ARG A O   1 
ATOM   2189 C  CB  . ARG A 1 245 ? 0.204   -5.727  18.655  1.00 7.80  ? 246 ARG A CB  1 
ATOM   2190 C  CG  . ARG A 1 245 ? 1.290   -5.506  19.697  1.00 8.10  ? 246 ARG A CG  1 
ATOM   2191 C  CD  . ARG A 1 245 ? 1.205   -4.136  20.280  1.00 9.00  ? 246 ARG A CD  1 
ATOM   2192 N  NE  . ARG A 1 245 ? 2.457   -3.856  21.006  1.00 9.92  ? 246 ARG A NE  1 
ATOM   2193 C  CZ  . ARG A 1 245 ? 2.668   -2.828  21.810  1.00 9.71  ? 246 ARG A CZ  1 
ATOM   2194 N  NH1 . ARG A 1 245 ? 1.688   -2.020  22.166  1.00 10.01 ? 246 ARG A NH1 1 
ATOM   2195 N  NH2 . ARG A 1 245 ? 3.900   -2.598  22.288  1.00 12.16 ? 246 ARG A NH2 1 
ATOM   2196 N  N   A PRO A 1 246 ? 0.506   -8.928  19.872  0.50 7.71  ? 247 PRO A N   1 
ATOM   2197 N  N   B PRO A 1 246 ? 0.560   -8.843  19.924  0.50 8.38  ? 247 PRO A N   1 
ATOM   2198 C  CA  A PRO A 1 246 ? 0.063   -9.730  21.008  0.50 8.36  ? 247 PRO A CA  1 
ATOM   2199 C  CA  B PRO A 1 246 ? 0.171   -9.688  21.052  0.50 8.79  ? 247 PRO A CA  1 
ATOM   2200 C  C   A PRO A 1 246 ? -0.241  -8.897  22.261  0.50 7.66  ? 247 PRO A C   1 
ATOM   2201 C  C   B PRO A 1 246 ? -0.218  -8.876  22.289  0.50 8.00  ? 247 PRO A C   1 
ATOM   2202 O  O   A PRO A 1 246 ? 0.157   -7.730  22.395  0.50 9.05  ? 247 PRO A O   1 
ATOM   2203 O  O   B PRO A 1 246 ? 0.151   -7.704  22.439  0.50 9.23  ? 247 PRO A O   1 
ATOM   2204 C  CB  A PRO A 1 246 ? 1.281   -10.663 21.265  0.50 10.82 ? 247 PRO A CB  1 
ATOM   2205 C  CB  B PRO A 1 246 ? 1.470   -10.474 21.373  0.50 11.53 ? 247 PRO A CB  1 
ATOM   2206 C  CG  A PRO A 1 246 ? 2.169   -10.542 20.066  0.50 10.12 ? 247 PRO A CG  1 
ATOM   2207 C  CG  B PRO A 1 246 ? 2.569   -9.666  20.804  0.50 12.80 ? 247 PRO A CG  1 
ATOM   2208 C  CD  A PRO A 1 246 ? 1.907   -9.186  19.468  0.50 9.01  ? 247 PRO A CD  1 
ATOM   2209 C  CD  B PRO A 1 246 ? 2.013   -8.887  19.637  0.50 10.56 ? 247 PRO A CD  1 
ATOM   2210 N  N   . ALA A 1 247 ? -0.871  -9.555  23.246  1.00 8.79  ? 248 ALA A N   1 
ATOM   2211 C  CA  . ALA A 1 247 ? -1.231  -8.902  24.509  1.00 8.97  ? 248 ALA A CA  1 
ATOM   2212 C  C   . ALA A 1 247 ? 0.033   -8.411  25.218  1.00 9.74  ? 248 ALA A C   1 
ATOM   2213 O  O   . ALA A 1 247 ? 1.076   -9.079  25.251  1.00 11.08 ? 248 ALA A O   1 
ATOM   2214 C  CB  . ALA A 1 247 ? -2.021  -9.913  25.338  1.00 11.76 ? 248 ALA A CB  1 
ATOM   2215 N  N   . GLN A 1 248 ? -0.131  -7.217  25.807  1.00 8.77  ? 249 GLN A N   1 
ATOM   2216 C  CA  . GLN A 1 248 ? 0.924   -6.497  26.532  1.00 9.31  ? 249 GLN A CA  1 
ATOM   2217 C  C   . GLN A 1 248 ? 0.600   -6.520  28.019  1.00 10.19 ? 249 GLN A C   1 
ATOM   2218 O  O   . GLN A 1 248 ? -0.557  -6.727  28.421  1.00 10.57 ? 249 GLN A O   1 
ATOM   2219 C  CB  . GLN A 1 248 ? 0.966   -5.064  26.002  1.00 10.60 ? 249 GLN A CB  1 
ATOM   2220 C  CG  . GLN A 1 248 ? 1.298   -4.996  24.494  1.00 11.39 ? 249 GLN A CG  1 
ATOM   2221 C  CD  . GLN A 1 248 ? 2.607   -5.674  24.187  1.00 12.37 ? 249 GLN A CD  1 
ATOM   2222 O  OE1 . GLN A 1 248 ? 3.658   -5.332  24.767  1.00 14.87 ? 249 GLN A OE1 1 
ATOM   2223 N  NE2 . GLN A 1 248 ? 2.604   -6.600  23.240  1.00 12.59 ? 249 GLN A NE2 1 
ATOM   2224 N  N   . PRO A 1 249 ? 1.589   -6.258  28.880  1.00 13.07 ? 250 PRO A N   1 
ATOM   2225 C  CA  . PRO A 1 249 ? 1.392   -6.257  30.323  1.00 14.71 ? 250 PRO A CA  1 
ATOM   2226 C  C   . PRO A 1 249 ? 0.315   -5.256  30.716  1.00 11.94 ? 250 PRO A C   1 
ATOM   2227 O  O   . PRO A 1 249 ? 0.374   -4.084  30.356  1.00 12.61 ? 250 PRO A O   1 
ATOM   2228 C  CB  . PRO A 1 249 ? 2.800   -5.837  30.841  1.00 18.12 ? 250 PRO A CB  1 
ATOM   2229 C  CG  . PRO A 1 249 ? 3.728   -6.253  29.819  1.00 20.24 ? 250 PRO A CG  1 
ATOM   2230 C  CD  . PRO A 1 249 ? 2.989   -6.030  28.517  1.00 15.92 ? 250 PRO A CD  1 
ATOM   2231 N  N   . LEU A 1 250 ? -0.532  -5.745  31.603  1.00 12.82 ? 251 LEU A N   1 
ATOM   2232 C  CA  . LEU A 1 250 ? -1.578  -4.870  32.132  1.00 12.20 ? 251 LEU A CA  1 
ATOM   2233 C  C   . LEU A 1 250 ? -1.047  -3.759  33.034  1.00 12.70 ? 251 LEU A C   1 
ATOM   2234 O  O   . LEU A 1 250 ? -1.585  -2.668  33.122  1.00 13.69 ? 251 LEU A O   1 
ATOM   2235 C  CB  . LEU A 1 250 ? -2.635  -5.703  32.875  1.00 14.48 ? 251 LEU A CB  1 
ATOM   2236 C  CG  . LEU A 1 250 ? -3.918  -4.988  33.289  1.00 15.05 ? 251 LEU A CG  1 
ATOM   2237 C  CD1 . LEU A 1 250 ? -4.721  -4.417  32.096  1.00 14.37 ? 251 LEU A CD1 1 
ATOM   2238 C  CD2 . LEU A 1 250 ? -4.797  -5.954  34.066  1.00 19.99 ? 251 LEU A CD2 1 
ATOM   2239 N  N   . LYS A 1 251 ? -0.000  -4.069  33.766  1.00 15.06 ? 252 LYS A N   1 
ATOM   2240 C  CA  . LYS A 1 251 ? 0.669   -3.047  34.617  1.00 15.71 ? 252 LYS A CA  1 
ATOM   2241 C  C   . LYS A 1 251 ? -0.335  -2.510  35.622  1.00 17.00 ? 252 LYS A C   1 
ATOM   2242 O  O   . LYS A 1 251 ? -1.100  -3.295  36.141  1.00 19.45 ? 252 LYS A O   1 
ATOM   2243 C  CB  . LYS A 1 251 ? 1.518   -2.031  33.828  1.00 17.59 ? 252 LYS A CB  1 
ATOM   2244 C  CG  . LYS A 1 251 ? 2.585   -2.691  32.974  1.00 21.77 ? 252 LYS A CG  1 
ATOM   2245 C  CD  . LYS A 1 251 ? 3.577   -1.755  32.376  1.00 24.76 ? 252 LYS A CD  1 
ATOM   2246 C  CE  . LYS A 1 251 ? 4.782   -2.466  31.789  1.00 31.39 ? 252 LYS A CE  1 
ATOM   2247 N  NZ  . LYS A 1 251 ? 5.650   -1.480  31.099  1.00 31.67 ? 252 LYS A NZ  1 
ATOM   2248 N  N   A ASN A 1 252 ? -0.500  -1.196  35.760  0.50 17.06 ? 253 ASN A N   1 
ATOM   2249 N  N   B ASN A 1 252 ? -0.267  -1.212  35.913  0.50 15.90 ? 253 ASN A N   1 
ATOM   2250 C  CA  A ASN A 1 252 ? -1.282  -0.868  36.991  0.50 22.94 ? 253 ASN A CA  1 
ATOM   2251 C  CA  B ASN A 1 252 ? -1.255  -0.776  36.924  0.50 20.13 ? 253 ASN A CA  1 
ATOM   2252 C  C   A ASN A 1 252 ? -2.800  -0.975  36.788  0.50 20.67 ? 253 ASN A C   1 
ATOM   2253 C  C   B ASN A 1 252 ? -2.472  -0.135  36.229  0.50 16.48 ? 253 ASN A C   1 
ATOM   2254 O  O   A ASN A 1 252 ? -3.601  -0.661  37.696  0.50 26.01 ? 253 ASN A O   1 
ATOM   2255 O  O   B ASN A 1 252 ? -2.637  1.096   36.159  0.50 14.21 ? 253 ASN A O   1 
ATOM   2256 C  CB  A ASN A 1 252 ? -0.981  0.589   37.345  0.50 24.11 ? 253 ASN A CB  1 
ATOM   2257 C  CB  B ASN A 1 252 ? -0.637  -0.509  38.310  0.50 24.26 ? 253 ASN A CB  1 
ATOM   2258 C  CG  A ASN A 1 252 ? -1.655  1.040   38.616  0.50 22.96 ? 253 ASN A CG  1 
ATOM   2259 C  CG  B ASN A 1 252 ? 0.451   -1.513  38.681  0.50 29.96 ? 253 ASN A CG  1 
ATOM   2260 O  OD1 A ASN A 1 252 ? -1.598  0.331   39.607  0.50 28.95 ? 253 ASN A OD1 1 
ATOM   2261 O  OD1 B ASN A 1 252 ? 0.238   -2.511  39.396  0.50 31.90 ? 253 ASN A OD1 1 
ATOM   2262 N  ND2 A ASN A 1 252 ? -2.286  2.203   38.591  0.50 21.77 ? 253 ASN A ND2 1 
ATOM   2263 N  ND2 B ASN A 1 252 ? 1.655   -1.260  38.194  0.50 37.92 ? 253 ASN A ND2 1 
ATOM   2264 N  N   A ARG A 1 253 ? -3.266  -1.548  35.655  0.50 15.69 ? 254 ARG A N   1 
ATOM   2265 N  N   B ARG A 1 253 ? -3.328  -1.045  35.723  0.50 14.81 ? 254 ARG A N   1 
ATOM   2266 C  CA  A ARG A 1 253 ? -4.574  -1.124  35.194  0.50 10.65 ? 254 ARG A CA  1 
ATOM   2267 C  CA  B ARG A 1 253 ? -4.607  -0.725  35.149  0.50 12.31 ? 254 ARG A CA  1 
ATOM   2268 C  C   A ARG A 1 253 ? -5.716  -2.025  35.605  0.50 12.83 ? 254 ARG A C   1 
ATOM   2269 C  C   B ARG A 1 253 ? -5.621  -1.738  35.665  0.50 11.99 ? 254 ARG A C   1 
ATOM   2270 O  O   A ARG A 1 253 ? -5.585  -3.246  35.685  0.50 17.57 ? 254 ARG A O   1 
ATOM   2271 O  O   B ARG A 1 253 ? -5.253  -2.844  36.043  0.50 17.39 ? 254 ARG A O   1 
ATOM   2272 C  CB  A ARG A 1 253 ? -4.676  -0.953  33.689  0.50 10.47 ? 254 ARG A CB  1 
ATOM   2273 C  CB  B ARG A 1 253 ? -4.474  -0.866  33.642  0.50 11.98 ? 254 ARG A CB  1 
ATOM   2274 C  CG  A ARG A 1 253 ? -3.708  0.114   33.203  0.50 10.60 ? 254 ARG A CG  1 
ATOM   2275 C  CG  B ARG A 1 253 ? -3.611  0.258   33.094  0.50 11.83 ? 254 ARG A CG  1 
ATOM   2276 C  CD  A ARG A 1 253 ? -3.565  0.172   31.691  0.50 9.96  ? 254 ARG A CD  1 
ATOM   2277 C  CD  B ARG A 1 253 ? -3.495  0.264   31.587  0.50 10.45 ? 254 ARG A CD  1 
ATOM   2278 N  NE  A ARG A 1 253 ? -2.753  -0.947  31.207  0.50 8.55  ? 254 ARG A NE  1 
ATOM   2279 N  NE  B ARG A 1 253 ? -2.707  -0.886  31.162  0.50 9.97  ? 254 ARG A NE  1 
ATOM   2280 C  CZ  A ARG A 1 253 ? -2.501  -1.205  29.915  0.50 7.50  ? 254 ARG A CZ  1 
ATOM   2281 C  CZ  B ARG A 1 253 ? -2.482  -1.200  29.885  0.50 8.16  ? 254 ARG A CZ  1 
ATOM   2282 N  NH1 A ARG A 1 253 ? -3.092  -0.501  28.951  0.50 8.25  ? 254 ARG A NH1 1 
ATOM   2283 N  NH1 B ARG A 1 253 ? -3.078  -0.512  28.914  0.50 8.66  ? 254 ARG A NH1 1 
ATOM   2284 N  NH2 A ARG A 1 253 ? -1.657  -2.185  29.601  0.50 8.76  ? 254 ARG A NH2 1 
ATOM   2285 N  NH2 B ARG A 1 253 ? -1.661  -2.205  29.596  0.50 9.50  ? 254 ARG A NH2 1 
ATOM   2286 N  N   . GLN A 1 254 ? -6.898  -1.344  35.664  1.00 14.15 ? 255 GLN A N   1 
ATOM   2287 C  CA  . GLN A 1 254 ? -8.052  -2.173  35.955  1.00 14.74 ? 255 GLN A CA  1 
ATOM   2288 C  C   . GLN A 1 254 ? -8.963  -2.173  34.733  1.00 14.35 ? 255 GLN A C   1 
ATOM   2289 O  O   . GLN A 1 254 ? -9.258  -1.131  34.149  1.00 16.15 ? 255 GLN A O   1 
ATOM   2290 C  CB  . GLN A 1 254 ? -8.889  -1.622  37.118  1.00 21.66 ? 255 GLN A CB  1 
ATOM   2291 C  CG  . GLN A 1 254 ? -8.248  -1.864  38.488  1.00 27.20 ? 255 GLN A CG  1 
ATOM   2292 C  CD  . GLN A 1 254 ? -9.271  -1.999  39.601  1.00 31.77 ? 255 GLN A CD  1 
ATOM   2293 N  N   . ILE A 1 255 ? -9.438  -3.338  34.355  1.00 11.25 ? 256 ILE A N   1 
ATOM   2294 C  CA  . ILE A 1 255 ? -10.417 -3.446  33.292  1.00 11.09 ? 256 ILE A CA  1 
ATOM   2295 C  C   . ILE A 1 255 ? -11.779 -3.455  33.975  1.00 11.66 ? 256 ILE A C   1 
ATOM   2296 O  O   . ILE A 1 255 ? -12.014 -4.194  34.924  1.00 13.03 ? 256 ILE A O   1 
ATOM   2297 C  CB  . ILE A 1 255 ? -10.189 -4.715  32.473  1.00 10.19 ? 256 ILE A CB  1 
ATOM   2298 C  CG1 . ILE A 1 255 ? -8.744  -4.722  31.923  1.00 11.79 ? 256 ILE A CG1 1 
ATOM   2299 C  CG2 . ILE A 1 255 ? -11.287 -4.834  31.387  1.00 11.99 ? 256 ILE A CG2 1 
ATOM   2300 C  CD1 . ILE A 1 255 ? -8.433  -5.951  31.084  1.00 14.93 ? 256 ILE A CD1 1 
ATOM   2301 N  N   . LYS A 1 256 ? -12.687 -2.606  33.478  1.00 9.81  ? 257 LYS A N   1 
ATOM   2302 C  CA  . LYS A 1 256 ? -14.015 -2.504  34.007  1.00 10.79 ? 257 LYS A CA  1 
ATOM   2303 C  C   . LYS A 1 256 ? -15.014 -3.134  33.060  1.00 11.68 ? 257 LYS A C   1 
ATOM   2304 O  O   . LYS A 1 256 ? -14.813 -3.046  31.849  1.00 12.86 ? 257 LYS A O   1 
ATOM   2305 C  CB  . LYS A 1 256 ? -14.357 -1.028  34.214  1.00 14.06 ? 257 LYS A CB  1 
ATOM   2306 C  CG  . LYS A 1 256 ? -13.454 -0.421  35.295  1.00 20.76 ? 257 LYS A CG  1 
ATOM   2307 C  CD  . LYS A 1 256 ? -13.624 1.015   35.540  1.00 26.79 ? 257 LYS A CD  1 
ATOM   2308 C  CE  . LYS A 1 256 ? -12.657 1.462   36.623  1.00 40.30 ? 257 LYS A CE  1 
ATOM   2309 N  NZ  . LYS A 1 256 ? -12.697 2.933   36.818  1.00 43.56 ? 257 LYS A NZ  1 
ATOM   2310 N  N   . ALA A 1 257 ? -16.055 -3.778  33.594  1.00 11.03 ? 258 ALA A N   1 
ATOM   2311 C  CA  . ALA A 1 257 ? -17.138 -4.398  32.829  1.00 12.03 ? 258 ALA A CA  1 
ATOM   2312 C  C   . ALA A 1 257 ? -18.391 -3.558  32.971  1.00 12.41 ? 258 ALA A C   1 
ATOM   2313 O  O   . ALA A 1 257 ? -18.716 -3.127  34.067  1.00 13.86 ? 258 ALA A O   1 
ATOM   2314 C  CB  . ALA A 1 257 ? -17.414 -5.824  33.265  1.00 14.06 ? 258 ALA A CB  1 
ATOM   2315 N  N   . SER A 1 258 ? -19.123 -3.457  31.872  1.00 12.36 ? 259 SER A N   1 
ATOM   2316 C  CA  . SER A 1 258 ? -20.407 -2.779  31.893  1.00 14.68 ? 259 SER A CA  1 
ATOM   2317 C  C   . SER A 1 258 ? -21.536 -3.669  32.390  1.00 15.20 ? 259 SER A C   1 
ATOM   2318 O  O   . SER A 1 258 ? -22.631 -3.139  32.471  1.00 20.06 ? 259 SER A O   1 
ATOM   2319 C  CB  . SER A 1 258 ? -20.745 -2.237  30.548  1.00 14.55 ? 259 SER A CB  1 
ATOM   2320 O  OG  . SER A 1 258 ? -21.101 -3.263  29.649  1.00 13.49 ? 259 SER A OG  1 
ATOM   2321 N  N   . PHE A 1 259 ? -21.264 -4.946  32.643  1.00 16.42 ? 260 PHE A N   1 
ATOM   2322 C  CA  . PHE A 1 259 ? -22.287 -5.950  32.809  1.00 18.29 ? 260 PHE A CA  1 
ATOM   2323 C  C   . PHE A 1 259 ? -21.809 -6.890  33.904  1.00 20.06 ? 260 PHE A C   1 
ATOM   2324 O  O   . PHE A 1 259 ? -20.590 -7.013  34.161  1.00 21.49 ? 260 PHE A O   1 
ATOM   2325 C  CB  . PHE A 1 259 ? -22.492 -6.747  31.523  1.00 18.89 ? 260 PHE A CB  1 
ATOM   2326 C  CG  . PHE A 1 259 ? -21.245 -7.471  31.066  1.00 16.22 ? 260 PHE A CG  1 
ATOM   2327 C  CD1 . PHE A 1 259 ? -20.239 -6.798  30.377  1.00 14.68 ? 260 PHE A CD1 1 
ATOM   2328 C  CD2 . PHE A 1 259 ? -21.011 -8.782  31.449  1.00 22.10 ? 260 PHE A CD2 1 
ATOM   2329 C  CE1 . PHE A 1 259 ? -19.039 -7.432  30.073  1.00 15.62 ? 260 PHE A CE1 1 
ATOM   2330 C  CE2 . PHE A 1 259 ? -19.825 -9.431  31.119  1.00 23.58 ? 260 PHE A CE2 1 
ATOM   2331 C  CZ  . PHE A 1 259 ? -18.826 -8.755  30.424  1.00 19.86 ? 260 PHE A CZ  1 
ATOM   2332 N  N   . LYS A 1 260 ? -22.813 -7.588  34.448  1.00 31.29 ? 261 LYS A N   1 
ATOM   2333 C  CA  . LYS A 1 260 ? -22.818 -8.821  35.255  1.00 50.70 ? 261 LYS A CA  1 
ATOM   2334 C  C   . LYS A 1 260 ? -23.094 -8.532  36.741  1.00 57.59 ? 261 LYS A C   1 
ATOM   2335 O  O   . LYS A 1 260 ? -23.890 -7.677  37.094  1.00 71.80 ? 261 LYS A O   1 
ATOM   2336 C  CB  . LYS A 1 260 ? -21.602 -9.734  35.032  1.00 57.62 ? 261 LYS A CB  1 
ATOM   2337 O  OXT . LYS A 1 260 ? -22.548 -9.158  37.647  1.00 74.79 ? 261 LYS A OXT 1 
HETATM 2338 ZN ZN  . ZN  B 2 .   ? -6.433  -1.664  15.135  1.00 6.74  ? 301 ZN  A ZN  1 
HETATM 2339 S  S   . DMS C 3 .   ? 1.542   -11.677 14.910  1.00 25.38 ? 302 DMS A S   1 
HETATM 2340 O  O   . DMS C 3 .   ? 2.061   -13.105 14.422  1.00 40.20 ? 302 DMS A O   1 
HETATM 2341 C  C1  . DMS C 3 .   ? 1.843   -11.654 16.632  1.00 24.13 ? 302 DMS A C1  1 
HETATM 2342 C  C2  . DMS C 3 .   ? 2.869   -10.614 14.537  1.00 29.49 ? 302 DMS A C2  1 
HETATM 2343 N  N1  . BCN D 4 .   ? -20.334 -14.787 23.398  1.00 39.23 ? 303 BCN A N1  1 
HETATM 2344 C  C1  . BCN D 4 .   ? -19.330 -14.166 24.326  1.00 33.99 ? 303 BCN A C1  1 
HETATM 2345 C  C2  . BCN D 4 .   ? -19.540 -14.989 25.603  1.00 38.29 ? 303 BCN A C2  1 
HETATM 2346 O  O21 . BCN D 4 .   ? -20.448 -15.844 25.536  1.00 45.25 ? 303 BCN A O21 1 
HETATM 2347 O  O22 . BCN D 4 .   ? -18.839 -14.783 26.610  1.00 43.77 ? 303 BCN A O22 1 
HETATM 2348 C  C3  . BCN D 4 .   ? -19.750 -15.600 22.320  1.00 24.76 ? 303 BCN A C3  1 
HETATM 2349 C  C4  . BCN D 4 .   ? -20.686 -16.531 21.597  1.00 45.48 ? 303 BCN A C4  1 
HETATM 2350 O  O4  . BCN D 4 .   ? -20.744 -16.214 20.223  1.00 48.26 ? 303 BCN A O4  1 
HETATM 2351 C  C5  . BCN D 4 .   ? -21.410 -13.871 22.987  1.00 27.03 ? 303 BCN A C5  1 
HETATM 2352 C  C6  . BCN D 4 .   ? -22.496 -13.579 24.006  1.00 43.08 ? 303 BCN A C6  1 
HETATM 2353 O  O6  . BCN D 4 .   ? -22.339 -12.275 24.578  1.00 44.39 ? 303 BCN A O6  1 
HETATM 2354 O  O24 . OQT E 5 .   ? -4.206  0.352   13.857  1.00 14.23 ? 304 OQT A O24 1 
HETATM 2355 S  S2  . OQT E 5 .   ? -4.422  0.604   15.309  1.00 11.73 ? 304 OQT A S2  1 
HETATM 2356 O  O1  . OQT E 5 .   ? -3.136  0.874   16.029  1.00 14.50 ? 304 OQT A O1  1 
HETATM 2357 N  N3  . OQT E 5 .   ? -5.203  -0.519  16.018  1.00 9.40  ? 304 OQT A N3  1 
HETATM 2358 C  C4  . OQT E 5 .   ? -5.317  2.110   15.464  1.00 10.78 ? 304 OQT A C4  1 
HETATM 2359 C  C12 . OQT E 5 .   ? -5.433  3.010   14.335  1.00 12.27 ? 304 OQT A C12 1 
HETATM 2360 C  C10 . OQT E 5 .   ? -5.937  4.275   14.624  1.00 14.36 ? 304 OQT A C10 1 
HETATM 2361 F  F11 . OQT E 5 .   ? -6.167  5.164   13.615  1.00 19.50 ? 304 OQT A F11 1 
HETATM 2362 C  C9  . OQT E 5 .   ? -6.256  4.755   15.852  1.00 15.24 ? 304 OQT A C9  1 
HETATM 2363 C  C7  . OQT E 5 .   ? -6.124  3.863   16.894  1.00 12.68 ? 304 OQT A C7  1 
HETATM 2364 F  F8  . OQT E 5 .   ? -6.455  4.248   18.174  1.00 15.28 ? 304 OQT A F8  1 
HETATM 2365 C  C5  . OQT E 5 .   ? -5.645  2.611   16.700  1.00 12.57 ? 304 OQT A C5  1 
HETATM 2366 F  F6  . OQT E 5 .   ? -5.453  1.738   17.760  1.00 15.67 ? 304 OQT A F6  1 
HETATM 2367 N  N13 . OQT E 5 .   ? -5.286  2.584   12.992  1.00 13.69 ? 304 OQT A N13 1 
HETATM 2368 C  C14 . OQT E 5 .   ? -4.797  3.351   11.867  1.00 14.94 ? 304 OQT A C14 1 
HETATM 2369 C  C23 . OQT E 5 .   ? -3.346  3.744   12.089  1.00 19.18 ? 304 OQT A C23 1 
HETATM 2370 C  C22 . OQT E 5 .   ? -2.642  4.449   10.892  1.00 25.64 ? 304 OQT A C22 1 
HETATM 2371 C  C21 . OQT E 5 .   ? -3.421  4.453   9.552   1.00 20.75 ? 304 OQT A C21 1 
HETATM 2372 C  C20 . OQT E 5 .   ? -4.220  3.214   9.385   1.00 16.65 ? 304 OQT A C20 1 
HETATM 2373 C  C15 . OQT E 5 .   ? -4.919  2.678   10.484  1.00 16.02 ? 304 OQT A C15 1 
HETATM 2374 C  C19 . OQT E 5 .   ? -4.305  2.577   8.131   1.00 18.20 ? 304 OQT A C19 1 
HETATM 2375 C  C18 . OQT E 5 .   ? -5.104  1.412   8.003   1.00 20.65 ? 304 OQT A C18 1 
HETATM 2376 C  C17 . OQT E 5 .   ? -5.767  0.825   9.090   1.00 17.64 ? 304 OQT A C17 1 
HETATM 2377 C  C16 . OQT E 5 .   ? -5.678  1.474   10.346  1.00 17.57 ? 304 OQT A C16 1 
HETATM 2378 O  O   . HOH F 6 .   ? -8.296  -15.400 32.820  1.00 31.04 ? 401 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? 6.872   -2.959  0.299   1.00 48.01 ? 402 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? -17.738 19.067  5.849   1.00 15.85 ? 403 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? -14.874 -10.165 37.334  1.00 29.84 ? 404 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? -25.432 -10.570 17.613  1.00 25.02 ? 405 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? 2.617   -14.707 -5.870  1.00 42.09 ? 406 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? -3.330  5.744   -2.457  1.00 31.52 ? 407 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? 10.998  -9.679  9.755   1.00 35.38 ? 408 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? -6.035  -11.345 36.465  1.00 55.07 ? 409 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? -9.713  15.794  29.441  1.00 27.44 ? 410 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? 9.967   -4.466  -7.573  1.00 24.25 ? 411 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? -13.739 -8.800  -5.494  1.00 32.15 ? 412 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? -16.607 -13.940 26.255  1.00 21.76 ? 413 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? -3.337  -19.840 6.344   1.00 40.35 ? 414 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? -12.225 10.721  5.756   1.00 26.96 ? 415 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? -20.001 8.652   30.130  1.00 38.45 ? 416 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? 0.042   20.537  15.094  1.00 39.07 ? 417 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? -10.333 -5.550  38.185  1.00 41.79 ? 418 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? -3.083  17.922  20.765  1.00 27.72 ? 419 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? 1.029   14.605  24.256  1.00 43.91 ? 420 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? -1.400  4.370   -4.919  1.00 53.95 ? 421 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? -6.125  -4.517  -6.435  1.00 31.94 ? 422 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? 11.599  -7.029  22.380  1.00 33.77 ? 423 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? -27.804 5.959   15.169  1.00 42.52 ? 424 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? -20.810 -6.712  -1.988  1.00 51.49 ? 425 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? 1.932   8.080   27.905  1.00 24.84 ? 426 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? -0.260  3.703   13.321  1.00 22.00 ? 427 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? -1.055  -4.122  15.529  1.00 9.78  ? 428 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? -23.984 8.618   20.358  1.00 23.98 ? 429 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? 5.677   -12.393 5.249   1.00 41.45 ? 430 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? -22.547 -14.879 16.127  1.00 34.31 ? 431 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? -16.672 -13.929 37.474  1.00 30.44 ? 432 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? 1.713   12.157  21.983  1.00 48.03 ? 433 HOH A O   1 
HETATM 2411 O  O   . HOH F 6 .   ? 1.889   2.643   5.356   1.00 47.01 ? 434 HOH A O   1 
HETATM 2412 O  O   . HOH F 6 .   ? -12.004 12.403  29.177  1.00 26.85 ? 435 HOH A O   1 
HETATM 2413 O  O   . HOH F 6 .   ? -1.021  -15.398 -5.393  1.00 36.90 ? 436 HOH A O   1 
HETATM 2414 O  O   . HOH F 6 .   ? 0.103   -1.100  -4.782  1.00 20.02 ? 437 HOH A O   1 
HETATM 2415 O  O   . HOH F 6 .   ? 4.639   -2.515  28.908  1.00 28.25 ? 438 HOH A O   1 
HETATM 2416 O  O   . HOH F 6 .   ? -25.017 9.645   12.820  1.00 35.09 ? 439 HOH A O   1 
HETATM 2417 O  O   . HOH F 6 .   ? 3.824   -12.245 11.905  1.00 41.34 ? 440 HOH A O   1 
HETATM 2418 O  O   . HOH F 6 .   ? -19.189 -20.783 5.072   1.00 26.26 ? 441 HOH A O   1 
HETATM 2419 O  O   . HOH F 6 .   ? -25.229 -15.405 7.766   1.00 30.40 ? 442 HOH A O   1 
HETATM 2420 O  O   . HOH F 6 .   ? -12.431 13.112  31.803  1.00 27.49 ? 443 HOH A O   1 
HETATM 2421 O  O   . HOH F 6 .   ? -11.986 9.337   3.198   1.00 24.78 ? 444 HOH A O   1 
HETATM 2422 O  O   . HOH F 6 .   ? -14.097 -16.488 28.955  1.00 22.76 ? 445 HOH A O   1 
HETATM 2423 O  O   . HOH F 6 .   ? -13.941 -21.707 3.513   1.00 47.37 ? 446 HOH A O   1 
HETATM 2424 O  O   . HOH F 6 .   ? 6.812   -2.978  6.711   1.00 50.75 ? 447 HOH A O   1 
HETATM 2425 O  O   . HOH F 6 .   ? -10.274 8.683   25.374  1.00 11.11 ? 448 HOH A O   1 
HETATM 2426 O  O   . HOH F 6 .   ? -25.735 -6.392  13.158  1.00 24.59 ? 449 HOH A O   1 
HETATM 2427 O  O   . HOH F 6 .   ? -4.536  -11.872 31.999  1.00 21.46 ? 450 HOH A O   1 
HETATM 2428 O  O   . HOH F 6 .   ? 2.873   -4.471  7.645   1.00 22.11 ? 451 HOH A O   1 
HETATM 2429 O  O   . HOH F 6 .   ? -11.097 -15.291 34.336  1.00 34.41 ? 452 HOH A O   1 
HETATM 2430 O  O   . HOH F 6 .   ? -8.741  5.930   28.791  1.00 22.96 ? 453 HOH A O   1 
HETATM 2431 O  O   . HOH F 6 .   ? -8.717  7.708   8.475   1.00 29.55 ? 454 HOH A O   1 
HETATM 2432 O  O   . HOH F 6 .   ? -19.803 15.866  19.047  1.00 29.30 ? 455 HOH A O   1 
HETATM 2433 O  O   . HOH F 6 .   ? 11.859  -0.336  16.046  1.00 27.01 ? 456 HOH A O   1 
HETATM 2434 O  O   . HOH F 6 .   ? -19.733 17.055  23.233  1.00 41.94 ? 457 HOH A O   1 
HETATM 2435 O  O   . HOH F 6 .   ? 0.824   7.204   29.661  1.00 38.13 ? 458 HOH A O   1 
HETATM 2436 O  O   . HOH F 6 .   ? -19.443 -4.225  41.151  1.00 39.19 ? 459 HOH A O   1 
HETATM 2437 O  O   . HOH F 6 .   ? 8.914   1.656   30.397  1.00 52.92 ? 460 HOH A O   1 
HETATM 2438 O  O   . HOH F 6 .   ? 6.767   -0.451  -1.128  1.00 40.26 ? 461 HOH A O   1 
HETATM 2439 O  O   . HOH F 6 .   ? -2.293  -8.690  29.037  1.00 12.29 ? 462 HOH A O   1 
HETATM 2440 O  O   . HOH F 6 .   ? -6.586  -14.863 31.533  1.00 24.20 ? 463 HOH A O   1 
HETATM 2441 O  O   . HOH F 6 .   ? -19.191 10.047  8.813   1.00 15.83 ? 464 HOH A O   1 
HETATM 2442 O  O   . HOH F 6 .   ? 0.195   1.047   34.311  1.00 37.14 ? 465 HOH A O   1 
HETATM 2443 O  O   . HOH F 6 .   ? 5.426   7.075   20.371  1.00 17.92 ? 466 HOH A O   1 
HETATM 2444 O  O   . HOH F 6 .   ? -10.191 -18.248 17.055  1.00 13.85 ? 467 HOH A O   1 
HETATM 2445 O  O   . HOH F 6 .   ? 4.484   -3.418  26.478  1.00 20.34 ? 468 HOH A O   1 
HETATM 2446 O  O   . HOH F 6 .   ? -1.871  -4.772  -7.047  1.00 38.62 ? 469 HOH A O   1 
HETATM 2447 O  O   . HOH F 6 .   ? 1.555   10.876  17.009  1.00 40.48 ? 470 HOH A O   1 
HETATM 2448 O  O   . HOH F 6 .   ? 3.849   5.029   29.747  1.00 22.34 ? 471 HOH A O   1 
HETATM 2449 O  O   . HOH F 6 .   ? -6.464  -5.266  37.243  1.00 21.07 ? 472 HOH A O   1 
HETATM 2450 O  O   . HOH F 6 .   ? -23.791 -3.305  29.389  1.00 36.68 ? 473 HOH A O   1 
HETATM 2451 O  O   . HOH F 6 .   ? -23.075 0.149   34.471  1.00 39.37 ? 474 HOH A O   1 
HETATM 2452 O  O   . HOH F 6 .   ? -17.087 -16.179 22.028  1.00 23.76 ? 475 HOH A O   1 
HETATM 2453 O  O   . HOH F 6 .   ? -0.829  9.209   27.765  1.00 22.95 ? 476 HOH A O   1 
HETATM 2454 O  O   . HOH F 6 .   ? -12.350 3.899   -6.869  1.00 40.80 ? 477 HOH A O   1 
HETATM 2455 O  O   . HOH F 6 .   ? 3.523   -9.008  26.397  1.00 41.46 ? 478 HOH A O   1 
HETATM 2456 O  O   . HOH F 6 .   ? -14.425 9.438   31.630  1.00 48.34 ? 479 HOH A O   1 
HETATM 2457 O  O   . HOH F 6 .   ? 0.540   -14.412 30.692  1.00 43.40 ? 480 HOH A O   1 
HETATM 2458 O  O   . HOH F 6 .   ? -3.560  -12.894 -2.968  1.00 22.97 ? 481 HOH A O   1 
HETATM 2459 O  O   . HOH F 6 .   ? -20.901 7.851   1.809   1.00 20.26 ? 482 HOH A O   1 
HETATM 2460 O  O   . HOH F 6 .   ? -15.429 8.886   -2.214  1.00 25.15 ? 483 HOH A O   1 
HETATM 2461 O  O   . HOH F 6 .   ? 2.736   -13.165 5.174   1.00 22.50 ? 484 HOH A O   1 
HETATM 2462 O  O   . HOH F 6 .   ? -18.432 -21.103 14.626  1.00 19.01 ? 485 HOH A O   1 
HETATM 2463 O  O   . HOH F 6 .   ? -13.786 14.623  6.218   1.00 37.79 ? 486 HOH A O   1 
HETATM 2464 O  O   . HOH F 6 .   ? -24.581 5.577   6.575   1.00 37.91 ? 487 HOH A O   1 
HETATM 2465 O  O   . HOH F 6 .   ? -7.806  -15.485 11.298  1.00 9.85  ? 488 HOH A O   1 
HETATM 2466 O  O   . HOH F 6 .   ? 8.216   -8.321  -0.292  1.00 41.65 ? 489 HOH A O   1 
HETATM 2467 O  O   . HOH F 6 .   ? 15.502  -2.432  14.509  1.00 21.03 ? 490 HOH A O   1 
HETATM 2468 O  O   . HOH F 6 .   ? -19.963 10.736  26.817  1.00 20.21 ? 491 HOH A O   1 
HETATM 2469 O  O   . HOH F 6 .   ? -19.427 15.004  16.543  1.00 23.44 ? 492 HOH A O   1 
HETATM 2470 O  O   . HOH F 6 .   ? -12.682 -22.411 12.269  1.00 21.96 ? 493 HOH A O   1 
HETATM 2471 O  O   . HOH F 6 .   ? -22.515 -9.661  25.330  1.00 25.78 ? 494 HOH A O   1 
HETATM 2472 O  O   . HOH F 6 .   ? -15.208 -21.848 13.050  1.00 14.40 ? 495 HOH A O   1 
HETATM 2473 O  O   . HOH F 6 .   ? -6.571  20.714  19.379  1.00 13.36 ? 496 HOH A O   1 
HETATM 2474 O  O   . HOH F 6 .   ? 13.646  0.322   24.394  1.00 28.82 ? 497 HOH A O   1 
HETATM 2475 O  O   . HOH F 6 .   ? -10.398 21.663  19.929  1.00 20.02 ? 498 HOH A O   1 
HETATM 2476 O  O   . HOH F 6 .   ? -17.996 10.699  11.335  1.00 18.20 ? 499 HOH A O   1 
HETATM 2477 O  O   . HOH F 6 .   ? -15.824 -12.275 24.365  1.00 13.30 ? 500 HOH A O   1 
HETATM 2478 O  O   . HOH F 6 .   ? 2.018   -15.639 9.235   1.00 20.41 ? 501 HOH A O   1 
HETATM 2479 O  O   . HOH F 6 .   ? -4.342  -13.487 17.970  1.00 8.52  ? 502 HOH A O   1 
HETATM 2480 O  O   . HOH F 6 .   ? -26.058 3.291   15.552  1.00 29.13 ? 503 HOH A O   1 
HETATM 2481 O  O   . HOH F 6 .   ? -4.057  -8.521  31.141  1.00 23.41 ? 504 HOH A O   1 
HETATM 2482 O  O   . HOH F 6 .   ? -12.743 -22.184 8.291   1.00 26.99 ? 505 HOH A O   1 
HETATM 2483 O  O   . HOH F 6 .   ? -13.397 14.121  27.127  1.00 26.87 ? 506 HOH A O   1 
HETATM 2484 O  O   . HOH F 6 .   ? -16.781 -8.374  20.314  1.00 8.11  ? 507 HOH A O   1 
HETATM 2485 O  O   . HOH F 6 .   ? -22.643 -5.896  2.677   1.00 19.66 ? 508 HOH A O   1 
HETATM 2486 O  O   . HOH F 6 .   ? -8.287  0.700   -6.456  1.00 31.61 ? 509 HOH A O   1 
HETATM 2487 O  O   . HOH F 6 .   ? -3.264  -11.151 20.788  1.00 9.07  ? 510 HOH A O   1 
HETATM 2488 O  O   . HOH F 6 .   ? -23.168 -11.096 17.179  1.00 26.78 ? 511 HOH A O   1 
HETATM 2489 O  O   . HOH F 6 .   ? -2.284  -3.497  11.340  1.00 15.81 ? 512 HOH A O   1 
HETATM 2490 O  O   . HOH F 6 .   ? -10.671 -19.761 7.120   1.00 27.50 ? 513 HOH A O   1 
HETATM 2491 O  O   . HOH F 6 .   ? -21.912 -18.284 13.552  1.00 21.65 ? 514 HOH A O   1 
HETATM 2492 O  O   . HOH F 6 .   ? -21.343 -7.156  23.568  1.00 12.83 ? 515 HOH A O   1 
HETATM 2493 O  O   . HOH F 6 .   ? -14.479 -18.445 18.632  1.00 14.80 ? 516 HOH A O   1 
HETATM 2494 O  O   . HOH F 6 .   ? 8.798   -3.831  21.054  1.00 16.09 ? 517 HOH A O   1 
HETATM 2495 O  O   . HOH F 6 .   ? -14.798 20.043  17.639  1.00 17.09 ? 518 HOH A O   1 
HETATM 2496 O  O   . HOH F 6 .   ? 3.436   9.940   18.124  1.00 38.10 ? 519 HOH A O   1 
HETATM 2497 O  O   . HOH F 6 .   ? -4.591  -15.805 0.588   1.00 23.29 ? 520 HOH A O   1 
HETATM 2498 O  O   . HOH F 6 .   ? -24.670 -7.716  9.005   1.00 17.06 ? 521 HOH A O   1 
HETATM 2499 O  O   . HOH F 6 .   ? -6.567  14.356  28.970  1.00 35.03 ? 522 HOH A O   1 
HETATM 2500 O  O   . HOH F 6 .   ? 1.520   -11.798 24.966  1.00 23.45 ? 523 HOH A O   1 
HETATM 2501 O  O   . HOH F 6 .   ? -23.025 -2.960  6.533   1.00 22.51 ? 524 HOH A O   1 
HETATM 2502 O  O   . HOH F 6 .   ? -21.672 5.711   4.677   1.00 20.82 ? 525 HOH A O   1 
HETATM 2503 O  O   . HOH F 6 .   ? -12.770 -16.777 26.576  1.00 14.82 ? 526 HOH A O   1 
HETATM 2504 O  O   . HOH F 6 .   ? 6.711   -1.340  -7.778  1.00 33.55 ? 527 HOH A O   1 
HETATM 2505 O  O   . HOH F 6 .   ? -20.004 13.796  28.818  1.00 44.09 ? 528 HOH A O   1 
HETATM 2506 O  O   . HOH F 6 .   ? -13.420 10.377  27.817  1.00 17.36 ? 529 HOH A O   1 
HETATM 2507 O  O   . HOH F 6 .   ? -12.856 -8.796  -3.288  1.00 28.60 ? 530 HOH A O   1 
HETATM 2508 O  O   . HOH F 6 .   ? -3.565  -15.864 24.323  1.00 12.75 ? 531 HOH A O   1 
HETATM 2509 O  O   . HOH F 6 .   ? -3.164  -13.232 25.090  1.00 10.98 ? 532 HOH A O   1 
HETATM 2510 O  O   . HOH F 6 .   ? -24.763 4.592   8.710   1.00 36.00 ? 533 HOH A O   1 
HETATM 2511 O  O   . HOH F 6 .   ? 10.019  -8.175  3.900   1.00 33.63 ? 534 HOH A O   1 
HETATM 2512 O  O   . HOH F 6 .   ? -15.940 15.915  23.674  1.00 18.73 ? 535 HOH A O   1 
HETATM 2513 O  O   . HOH F 6 .   ? -12.433 7.863   28.608  1.00 22.49 ? 536 HOH A O   1 
HETATM 2514 O  O   . HOH F 6 .   ? -21.663 -14.165 18.525  1.00 38.43 ? 537 HOH A O   1 
HETATM 2515 O  O   . HOH F 6 .   ? 2.453   -4.675  -12.110 1.00 29.47 ? 538 HOH A O   1 
HETATM 2516 O  O   . HOH F 6 .   ? -18.087 3.980   -3.682  1.00 36.11 ? 539 HOH A O   1 
HETATM 2517 O  O   . HOH F 6 .   ? -25.758 6.319   27.004  1.00 30.99 ? 540 HOH A O   1 
HETATM 2518 O  O   . HOH F 6 .   ? -8.366  -15.299 36.624  1.00 28.13 ? 541 HOH A O   1 
HETATM 2519 O  O   . HOH F 6 .   ? 8.218   -9.469  16.735  1.00 22.46 ? 542 HOH A O   1 
HETATM 2520 O  O   . HOH F 6 .   ? 10.647  -10.850 16.474  1.00 25.09 ? 543 HOH A O   1 
HETATM 2521 O  O   . HOH F 6 .   ? 0.333   -19.752 10.609  1.00 35.80 ? 544 HOH A O   1 
HETATM 2522 O  O   . HOH F 6 .   ? -1.091  -17.736 17.940  1.00 32.49 ? 545 HOH A O   1 
HETATM 2523 O  O   . HOH F 6 .   ? -18.495 -3.779  -2.700  1.00 28.87 ? 546 HOH A O   1 
HETATM 2524 O  O   . HOH F 6 .   ? 13.207  -5.790  24.463  1.00 29.27 ? 547 HOH A O   1 
HETATM 2525 O  O   . HOH F 6 .   ? -17.775 20.687  7.927   1.00 12.64 ? 548 HOH A O   1 
HETATM 2526 O  O   . HOH F 6 .   ? -13.674 19.911  15.144  1.00 16.20 ? 549 HOH A O   1 
HETATM 2527 O  O   . HOH F 6 .   ? -7.143  -8.611  32.530  1.00 17.91 ? 550 HOH A O   1 
HETATM 2528 O  O   . HOH F 6 .   ? -8.038  -22.111 10.386  1.00 17.90 ? 551 HOH A O   1 
HETATM 2529 O  O   . HOH F 6 .   ? -13.172 -0.657  -6.111  1.00 35.76 ? 552 HOH A O   1 
HETATM 2530 O  O   . HOH F 6 .   ? 11.335  1.325   26.128  1.00 27.65 ? 553 HOH A O   1 
HETATM 2531 O  O   . HOH F 6 .   ? -16.131 -9.830  32.897  1.00 17.32 ? 554 HOH A O   1 
HETATM 2532 O  O   . HOH F 6 .   ? 2.723   -11.606 9.439   1.00 21.57 ? 555 HOH A O   1 
HETATM 2533 O  O   . HOH F 6 .   ? -13.151 -18.491 14.548  1.00 14.11 ? 556 HOH A O   1 
HETATM 2534 O  O   . HOH F 6 .   ? 5.126   -4.931  20.954  1.00 15.69 ? 557 HOH A O   1 
HETATM 2535 O  O   . HOH F 6 .   ? -23.791 -17.757 6.476   1.00 36.39 ? 558 HOH A O   1 
HETATM 2536 O  O   . HOH F 6 .   ? -12.448 16.166  8.220   1.00 35.84 ? 559 HOH A O   1 
HETATM 2537 O  O   . HOH F 6 .   ? -24.174 -0.057  1.457   1.00 29.96 ? 560 HOH A O   1 
HETATM 2538 O  O   . HOH F 6 .   ? -6.614  6.502   10.756  1.00 25.29 ? 561 HOH A O   1 
HETATM 2539 O  O   . HOH F 6 .   ? -12.462 -18.282 32.079  1.00 27.56 ? 562 HOH A O   1 
HETATM 2540 O  O   . HOH F 6 .   ? -22.513 15.313  18.992  1.00 46.63 ? 563 HOH A O   1 
HETATM 2541 O  O   . HOH F 6 .   ? -3.512  -0.938  11.396  1.00 24.94 ? 564 HOH A O   1 
HETATM 2542 O  O   . HOH F 6 .   ? -0.329  10.626  23.066  1.00 25.00 ? 565 HOH A O   1 
HETATM 2543 O  O   . HOH F 6 .   ? -10.757 1.187   33.365  1.00 27.52 ? 566 HOH A O   1 
HETATM 2544 O  O   . HOH F 6 .   ? -23.141 -13.261 11.282  1.00 19.85 ? 567 HOH A O   1 
HETATM 2545 O  O   . HOH F 6 .   ? 15.813  3.149   21.026  1.00 36.11 ? 568 HOH A O   1 
HETATM 2546 O  O   . HOH F 6 .   ? -7.121  -16.703 1.202   1.00 20.58 ? 569 HOH A O   1 
HETATM 2547 O  O   . HOH F 6 .   ? -0.342  -8.481  32.495  1.00 25.18 ? 570 HOH A O   1 
HETATM 2548 O  O   . HOH F 6 .   ? 1.764   -6.301  34.241  1.00 28.36 ? 571 HOH A O   1 
HETATM 2549 O  O   . HOH F 6 .   ? -16.523 -15.049 32.718  1.00 45.58 ? 572 HOH A O   1 
HETATM 2550 O  O   . HOH F 6 .   ? -6.553  -8.324  -7.156  1.00 38.26 ? 573 HOH A O   1 
HETATM 2551 O  O   . HOH F 6 .   ? -11.640 2.872   30.641  1.00 20.34 ? 574 HOH A O   1 
HETATM 2552 O  O   . HOH F 6 .   ? -8.826  -5.777  35.814  1.00 19.54 ? 575 HOH A O   1 
HETATM 2553 O  O   . HOH F 6 .   ? -23.680 -0.787  3.929   1.00 27.81 ? 576 HOH A O   1 
HETATM 2554 O  O   . HOH F 6 .   ? 1.471   -1.501  29.357  1.00 14.95 ? 577 HOH A O   1 
HETATM 2555 O  O   . HOH F 6 .   ? -1.769  0.537   10.027  1.00 32.54 ? 578 HOH A O   1 
HETATM 2556 O  O   . HOH F 6 .   ? -5.688  17.419  27.287  1.00 32.57 ? 579 HOH A O   1 
HETATM 2557 O  O   . HOH F 6 .   ? -17.076 -22.856 3.788   1.00 37.33 ? 580 HOH A O   1 
HETATM 2558 O  O   . HOH F 6 .   ? -10.248 20.797  24.802  1.00 22.82 ? 581 HOH A O   1 
HETATM 2559 O  O   . HOH F 6 .   ? -0.231  -16.299 27.320  1.00 42.81 ? 582 HOH A O   1 
HETATM 2560 O  O   . HOH F 6 .   ? -23.729 -0.722  26.437  1.00 22.34 ? 583 HOH A O   1 
HETATM 2561 O  O   . HOH F 6 .   ? -6.110  -19.693 23.760  1.00 30.18 ? 584 HOH A O   1 
HETATM 2562 O  O   . HOH F 6 .   ? 1.705   8.747   23.625  1.00 21.32 ? 585 HOH A O   1 
HETATM 2563 O  O   . HOH F 6 .   ? -0.014  -14.262 22.131  1.00 21.63 ? 586 HOH A O   1 
HETATM 2564 O  O   . HOH F 6 .   ? -1.847  -12.274 22.752  1.00 10.78 ? 587 HOH A O   1 
HETATM 2565 O  O   . HOH F 6 .   ? -22.723 -11.718 13.923  1.00 22.31 ? 588 HOH A O   1 
HETATM 2566 O  O   . HOH F 6 .   ? -11.021 9.661   8.045   1.00 21.48 ? 589 HOH A O   1 
HETATM 2567 O  O   . HOH F 6 .   ? 13.210  -3.733  13.403  1.00 27.03 ? 590 HOH A O   1 
HETATM 2568 O  O   . HOH F 6 .   ? 8.268   -6.039  0.354   1.00 35.15 ? 591 HOH A O   1 
HETATM 2569 O  O   . HOH F 6 .   ? -22.133 3.814   -2.997  1.00 24.77 ? 592 HOH A O   1 
HETATM 2570 O  O   . HOH F 6 .   ? 14.168  5.701   19.425  1.00 34.76 ? 593 HOH A O   1 
HETATM 2571 O  O   . HOH F 6 .   ? 8.523   3.443   27.784  1.00 36.48 ? 594 HOH A O   1 
HETATM 2572 O  O   . HOH F 6 .   ? 3.709   4.203   10.674  1.00 58.57 ? 595 HOH A O   1 
HETATM 2573 O  O   . HOH F 6 .   ? 4.580   -6.717  7.811   1.00 28.13 ? 596 HOH A O   1 
HETATM 2574 O  O   . HOH F 6 .   ? 4.685   -12.820 -5.905  1.00 27.96 ? 597 HOH A O   1 
HETATM 2575 O  O   . HOH F 6 .   ? -6.750  1.533   34.892  1.00 26.48 ? 598 HOH A O   1 
HETATM 2576 O  O   . HOH F 6 .   ? -8.238  -19.880 26.569  1.00 25.27 ? 599 HOH A O   1 
HETATM 2577 O  O   . HOH F 6 .   ? -16.661 0.390   -4.219  1.00 47.90 ? 600 HOH A O   1 
HETATM 2578 O  O   . HOH F 6 .   ? 7.766   6.115   21.667  1.00 20.03 ? 601 HOH A O   1 
HETATM 2579 O  O   . HOH F 6 .   ? -24.624 12.030  6.198   1.00 28.45 ? 602 HOH A O   1 
HETATM 2580 O  O   . HOH F 6 .   ? -21.061 -19.572 6.565   1.00 24.01 ? 603 HOH A O   1 
HETATM 2581 O  O   . HOH F 6 .   ? -2.368  -18.095 30.672  1.00 40.34 ? 604 HOH A O   1 
HETATM 2582 O  O   . HOH F 6 .   ? -12.203 16.349  11.018  1.00 21.82 ? 605 HOH A O   1 
HETATM 2583 O  O   . HOH F 6 .   ? -4.836  -13.258 34.258  1.00 38.39 ? 606 HOH A O   1 
HETATM 2584 O  O   . HOH F 6 .   ? -27.620 2.444   23.374  1.00 41.50 ? 607 HOH A O   1 
HETATM 2585 O  O   . HOH F 6 .   ? 4.252   -3.089  4.625   1.00 42.27 ? 608 HOH A O   1 
HETATM 2586 O  O   . HOH F 6 .   ? -10.187 14.504  11.985  1.00 22.17 ? 609 HOH A O   1 
HETATM 2587 O  O   . HOH F 6 .   ? -7.906  -19.357 21.579  1.00 16.03 ? 610 HOH A O   1 
HETATM 2588 O  O   . HOH F 6 .   ? 6.438   -10.955 15.062  1.00 37.97 ? 611 HOH A O   1 
HETATM 2589 O  O   . HOH F 6 .   ? 5.419   -7.272  22.315  1.00 30.43 ? 612 HOH A O   1 
HETATM 2590 O  O   . HOH F 6 .   ? -4.710  3.373   -5.806  1.00 27.95 ? 613 HOH A O   1 
HETATM 2591 O  O   . HOH F 6 .   ? -26.672 -3.872  25.220  1.00 26.20 ? 614 HOH A O   1 
HETATM 2592 O  O   . HOH F 6 .   ? -21.519 19.581  12.115  1.00 27.45 ? 615 HOH A O   1 
HETATM 2593 O  O   . HOH F 6 .   ? -9.231  -7.864  34.004  1.00 21.50 ? 616 HOH A O   1 
HETATM 2594 O  O   . HOH F 6 .   ? -7.357  16.490  10.632  1.00 27.93 ? 617 HOH A O   1 
HETATM 2595 O  O   . HOH F 6 .   ? 4.837   -0.892  36.155  1.00 49.18 ? 618 HOH A O   1 
HETATM 2596 O  O   . HOH F 6 .   ? 10.398  -2.628  13.673  1.00 27.83 ? 619 HOH A O   1 
HETATM 2597 O  O   . HOH F 6 .   ? -6.348  14.780  11.607  1.00 24.90 ? 620 HOH A O   1 
HETATM 2598 O  O   . HOH F 6 .   ? -23.375 8.261   3.493   1.00 27.64 ? 621 HOH A O   1 
HETATM 2599 O  O   . HOH F 6 .   ? -18.133 -8.976  34.646  1.00 28.62 ? 622 HOH A O   1 
HETATM 2600 O  O   . HOH F 6 .   ? 8.924   -4.613  23.630  1.00 27.48 ? 623 HOH A O   1 
HETATM 2601 O  O   . HOH F 6 .   ? -12.671 -17.165 16.784  1.00 12.30 ? 624 HOH A O   1 
HETATM 2602 O  O   . HOH F 6 .   ? 10.529  -7.080  -8.398  1.00 30.47 ? 625 HOH A O   1 
HETATM 2603 O  O   . HOH F 6 .   ? -2.469  -14.792 32.779  1.00 33.79 ? 626 HOH A O   1 
HETATM 2604 O  O   . HOH F 6 .   ? -0.650  8.427   15.573  1.00 41.58 ? 627 HOH A O   1 
HETATM 2605 O  O   . HOH F 6 .   ? -1.109  11.317  25.356  1.00 29.40 ? 628 HOH A O   1 
HETATM 2606 O  O   . HOH F 6 .   ? 10.605  5.368   12.659  1.00 35.59 ? 629 HOH A O   1 
HETATM 2607 O  O   . HOH F 6 .   ? -15.040 -16.110 25.294  1.00 37.59 ? 630 HOH A O   1 
HETATM 2608 O  O   . HOH F 6 .   ? 1.384   -9.929  28.472  1.00 43.39 ? 631 HOH A O   1 
HETATM 2609 O  O   . HOH F 6 .   ? -16.898 19.738  21.506  1.00 46.57 ? 632 HOH A O   1 
HETATM 2610 O  O   . HOH F 6 .   ? 6.678   -5.958  6.399   1.00 31.21 ? 633 HOH A O   1 
HETATM 2611 O  O   . HOH F 6 .   ? -2.732  6.019   -0.354  1.00 31.54 ? 634 HOH A O   1 
HETATM 2612 O  O   . HOH F 6 .   ? -9.141  9.565   -6.189  1.00 45.07 ? 635 HOH A O   1 
HETATM 2613 O  O   . HOH F 6 .   ? -25.010 11.087  19.697  1.00 31.14 ? 636 HOH A O   1 
HETATM 2614 O  O   . HOH F 6 .   ? 4.046   8.751   22.190  1.00 25.75 ? 637 HOH A O   1 
HETATM 2615 O  O   . HOH F 6 .   ? -11.992 12.990  5.885   1.00 65.70 ? 638 HOH A O   1 
HETATM 2616 O  O   . HOH F 6 .   ? 1.047   3.018   1.983   1.00 28.52 ? 639 HOH A O   1 
HETATM 2617 O  O   . HOH F 6 .   ? -1.132  -13.038 26.940  1.00 25.57 ? 640 HOH A O   1 
HETATM 2618 O  O   . HOH F 6 .   ? -23.587 -3.506  3.658   1.00 32.90 ? 641 HOH A O   1 
HETATM 2619 O  O   . HOH F 6 .   ? 14.684  0.086   15.043  1.00 28.81 ? 642 HOH A O   1 
HETATM 2620 O  O   . HOH F 6 .   ? 9.842   -0.062  14.715  1.00 32.06 ? 643 HOH A O   1 
HETATM 2621 O  O   . HOH F 6 .   ? 14.205  -3.745  10.440  1.00 43.66 ? 644 HOH A O   1 
HETATM 2622 O  O   . HOH F 6 .   ? -27.645 5.002   25.243  1.00 40.25 ? 645 HOH A O   1 
HETATM 2623 O  O   . HOH F 6 .   ? 3.260   2.584   0.021   1.00 33.65 ? 646 HOH A O   1 
HETATM 2624 O  O   . HOH F 6 .   ? -5.195  12.645  11.225  1.00 34.98 ? 647 HOH A O   1 
HETATM 2625 O  O   . HOH F 6 .   ? -1.949  -12.085 31.378  1.00 32.45 ? 648 HOH A O   1 
HETATM 2626 O  O   . HOH F 6 .   ? -24.803 8.676   26.398  1.00 52.83 ? 649 HOH A O   1 
HETATM 2627 O  O   . HOH F 6 .   ? 12.113  -6.895  7.640   1.00 42.63 ? 650 HOH A O   1 
HETATM 2628 O  O   . HOH F 6 .   ? -1.732  -17.403 25.502  1.00 28.42 ? 651 HOH A O   1 
HETATM 2629 O  O   . HOH F 6 .   ? -24.112 13.726  20.708  1.00 35.56 ? 652 HOH A O   1 
HETATM 2630 O  O   . HOH F 6 .   ? 3.041   -13.562 7.971   1.00 28.68 ? 653 HOH A O   1 
HETATM 2631 O  O   . HOH F 6 .   ? -0.181  2.480   10.880  1.00 50.47 ? 654 HOH A O   1 
HETATM 2632 O  O   . HOH F 6 .   ? -4.577  20.310  21.180  1.00 31.05 ? 655 HOH A O   1 
HETATM 2633 O  O   . HOH F 6 .   ? -26.934 -6.545  7.969   1.00 40.26 ? 656 HOH A O   1 
HETATM 2634 O  O   . HOH F 6 .   ? -10.058 5.070   30.498  1.00 29.53 ? 657 HOH A O   1 
HETATM 2635 O  O   . HOH F 6 .   ? -16.456 -17.623 24.117  1.00 35.39 ? 658 HOH A O   1 
HETATM 2636 O  O   . HOH F 6 .   ? -2.300  -17.313 5.234   1.00 46.82 ? 659 HOH A O   1 
HETATM 2637 O  O   . HOH F 6 .   ? -9.672  1.563   38.878  1.00 32.56 ? 660 HOH A O   1 
HETATM 2638 O  O   . HOH F 6 .   ? -16.730 -17.883 20.131  1.00 24.38 ? 661 HOH A O   1 
HETATM 2639 O  O   . HOH F 6 .   ? 4.089   -11.684 23.420  1.00 33.68 ? 662 HOH A O   1 
HETATM 2640 O  O   . HOH F 6 .   ? -1.408  4.388   1.817   1.00 30.83 ? 663 HOH A O   1 
HETATM 2641 O  O   . HOH F 6 .   ? -5.348  -12.766 -5.478  1.00 35.35 ? 664 HOH A O   1 
HETATM 2642 O  O   . HOH F 6 .   ? -26.941 -10.531 14.849  1.00 31.01 ? 665 HOH A O   1 
HETATM 2643 O  O   . HOH F 6 .   ? 4.447   -13.085 21.661  1.00 43.03 ? 666 HOH A O   1 
HETATM 2644 O  O   . HOH F 6 .   ? -17.634 -12.105 31.502  1.00 34.45 ? 667 HOH A O   1 
HETATM 2645 O  O   . HOH F 6 .   ? 15.512  -1.280  25.936  1.00 24.95 ? 668 HOH A O   1 
HETATM 2646 O  O   . HOH F 6 .   ? -15.114 20.942  22.772  1.00 31.81 ? 669 HOH A O   1 
HETATM 2647 O  O   . HOH F 6 .   ? -0.679  -19.853 6.831   1.00 38.98 ? 670 HOH A O   1 
HETATM 2648 O  O   . HOH F 6 .   ? -10.737 -10.990 -3.125  1.00 42.83 ? 671 HOH A O   1 
HETATM 2649 O  O   . HOH F 6 .   ? -4.093  8.514   9.422   1.00 32.42 ? 672 HOH A O   1 
HETATM 2650 O  O   . HOH F 6 .   ? -0.445  18.337  20.380  1.00 42.60 ? 673 HOH A O   1 
HETATM 2651 O  O   . HOH F 6 .   ? -4.586  -9.454  33.544  1.00 37.10 ? 674 HOH A O   1 
HETATM 2652 O  O   . HOH F 6 .   ? -1.680  3.145   -6.981  1.00 36.60 ? 675 HOH A O   1 
HETATM 2653 O  O   . HOH F 6 .   ? -4.150  10.814  12.426  1.00 36.18 ? 676 HOH A O   1 
HETATM 2654 O  O   . HOH F 6 .   ? 2.189   -14.183 20.506  1.00 32.71 ? 677 HOH A O   1 
HETATM 2655 O  O   . HOH F 6 .   ? -7.262  -10.250 -4.335  1.00 33.53 ? 678 HOH A O   1 
HETATM 2656 O  O   . HOH F 6 .   ? -17.511 -21.126 17.383  1.00 23.65 ? 679 HOH A O   1 
HETATM 2657 O  O   . HOH F 6 .   ? -8.431  -17.673 -1.066  1.00 53.80 ? 680 HOH A O   1 
HETATM 2658 O  O   . HOH F 6 .   ? -8.605  14.562  10.180  1.00 18.83 ? 681 HOH A O   1 
HETATM 2659 O  O   . HOH F 6 .   ? -1.003  6.431   13.447  1.00 32.01 ? 682 HOH A O   1 
HETATM 2660 O  O   . HOH F 6 .   ? -8.807  3.191   34.617  1.00 26.74 ? 683 HOH A O   1 
HETATM 2661 O  O   . HOH F 6 .   ? -0.934  -11.067 28.914  1.00 19.04 ? 684 HOH A O   1 
HETATM 2662 O  O   . HOH F 6 .   ? 2.600   9.463   26.038  1.00 36.05 ? 685 HOH A O   1 
HETATM 2663 O  O   . HOH F 6 .   ? -3.819  -15.466 -2.215  1.00 31.16 ? 686 HOH A O   1 
HETATM 2664 O  O   . HOH F 6 .   ? -15.939 17.637  25.897  1.00 36.98 ? 687 HOH A O   1 
HETATM 2665 O  O   . HOH F 6 .   ? -9.817  16.997  9.732   1.00 34.71 ? 688 HOH A O   1 
HETATM 2666 O  O   . HOH F 6 .   ? 11.592  -9.487  -0.686  1.00 32.12 ? 689 HOH A O   1 
HETATM 2667 O  O   . HOH F 6 .   ? -12.642 -19.453 26.147  1.00 22.33 ? 690 HOH A O   1 
HETATM 2668 O  O   . HOH F 6 .   ? -18.169 13.428  -0.263  1.00 28.80 ? 691 HOH A O   1 
HETATM 2669 O  O   . HOH F 6 .   ? -2.930  -19.836 26.711  1.00 34.53 ? 692 HOH A O   1 
HETATM 2670 O  O   . HOH F 6 .   ? -2.247  -9.197  34.583  1.00 34.83 ? 693 HOH A O   1 
HETATM 2671 O  O   . HOH F 6 .   ? -17.398 11.120  -1.939  1.00 26.33 ? 694 HOH A O   1 
HETATM 2672 O  O   . HOH F 6 .   ? -1.399  8.601   10.326  1.00 50.87 ? 697 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   A HIS A 4   ? 0.3667 0.4318 0.4005 0.0334  0.0601  -0.0038 4   HIS A N   
2    N  N   B HIS A 4   ? 0.2951 0.3486 0.3828 -0.1904 0.0969  0.0895  4   HIS A N   
3    C  CA  A HIS A 4   ? 0.1650 0.3261 0.3201 0.0044  0.0439  0.1055  4   HIS A CA  
4    C  CA  B HIS A 4   ? 0.3846 0.4795 0.3201 -0.0454 0.1001  0.0955  4   HIS A CA  
5    C  C   A HIS A 4   ? 0.1833 0.2477 0.3202 0.0034  0.0294  0.0787  4   HIS A C   
6    C  C   B HIS A 4   ? 0.2849 0.4530 0.3021 -0.0120 0.0848  0.0403  4   HIS A C   
7    O  O   A HIS A 4   ? 0.2425 0.2343 0.2821 -0.0343 0.1076  0.0952  4   HIS A O   
8    O  O   B HIS A 4   ? 0.3143 0.3793 0.3661 -0.0762 0.0029  0.0697  4   HIS A O   
9    C  CB  A HIS A 4   ? 0.1185 0.1564 0.2798 -0.0497 -0.0095 0.0035  4   HIS A CB  
10   C  CB  B HIS A 4   ? 0.1304 0.6336 0.2303 -0.1257 0.0092  0.0917  4   HIS A CB  
11   C  CG  A HIS A 4   ? 0.0884 0.0987 0.1899 0.0279  0.0083  0.0923  4   HIS A CG  
12   C  CG  B HIS A 4   ? 0.3318 0.5222 0.3228 0.0011  -0.0754 0.0151  4   HIS A CG  
13   N  ND1 A HIS A 4   ? 0.2701 0.2033 0.2356 -0.0731 0.0119  0.0524  4   HIS A ND1 
14   N  ND1 B HIS A 4   ? 0.2610 0.6673 0.5560 0.0281  -0.1256 0.0403  4   HIS A ND1 
15   C  CD2 A HIS A 4   ? 0.1445 0.2623 0.2939 0.1280  -0.0346 0.0239  4   HIS A CD2 
16   C  CD2 B HIS A 4   ? 0.3644 0.3818 0.3059 -0.1304 -0.0387 0.1354  4   HIS A CD2 
17   C  CE1 A HIS A 4   ? 0.3207 0.2762 0.3053 0.0018  0.0275  0.0223  4   HIS A CE1 
18   C  CE1 B HIS A 4   ? 0.3386 0.5069 0.4439 0.1667  -0.0925 0.0694  4   HIS A CE1 
19   N  NE2 A HIS A 4   ? 0.3191 0.3078 0.3271 0.0294  0.0193  -0.0290 4   HIS A NE2 
20   N  NE2 B HIS A 4   ? 0.4393 0.2732 0.3176 -0.0107 -0.0795 0.0432  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1588 0.2878 0.3841 -0.0669 0.0902  0.0612  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1576 0.2022 0.3301 -0.0179 0.0704  0.0514  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1155 0.2106 0.3325 0.0124  0.1262  0.0283  5   TRP A C   
24   O  O   . TRP A 5   ? 0.1408 0.2673 0.3344 -0.0163 0.1119  0.0410  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1243 0.1802 0.3459 -0.0001 0.0190  0.0152  5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1103 0.1949 0.2685 -0.0127 0.0381  0.0364  5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.1592 0.2104 0.2954 -0.0184 0.0047  0.0412  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.0933 0.1805 0.2111 0.0111  0.0247  -0.0037 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.1587 0.2202 0.2631 0.0052  0.0514  0.0660  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1023 0.2020 0.1954 0.0163  0.0422  0.0137  5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.0955 0.2103 0.1953 -0.0252 0.0496  -0.0236 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1082 0.2423 0.1593 0.0262  -0.0008 -0.0300 5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.0951 0.2406 0.1711 -0.0062 0.0739  -0.0562 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.0933 0.2609 0.1969 0.0070  0.0417  -0.0661 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1489 0.1687 0.2613 0.0127  0.1097  -0.0017 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1711 0.1887 0.3070 -0.0220 0.1226  -0.0320 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1003 0.1866 0.2856 0.0068  0.0995  -0.0155 6   GLY A C   
38   O  O   . GLY A 6   ? 0.0935 0.1822 0.2864 0.0091  0.1107  -0.0157 6   GLY A O   
39   N  N   . TYR A 7   ? 0.1714 0.1958 0.3775 -0.0321 0.1715  -0.0653 7   TYR A N   
40   C  CA  . TYR A 7   ? 0.1448 0.1467 0.3990 -0.0340 0.1729  -0.0678 7   TYR A CA  
41   C  C   . TYR A 7   ? 0.1429 0.1782 0.3944 -0.0136 0.1235  -0.0268 7   TYR A C   
42   O  O   . TYR A 7   ? 0.1579 0.1881 0.4900 -0.0029 0.1048  -0.0132 7   TYR A O   
43   C  CB  . TYR A 7   ? 0.1479 0.1976 0.3479 -0.0192 0.1870  -0.1007 7   TYR A CB  
44   C  CG  . TYR A 7   ? 0.0911 0.1767 0.2309 -0.0187 0.0697  -0.0736 7   TYR A CG  
45   C  CD1 . TYR A 7   ? 0.0811 0.1570 0.2040 -0.0132 0.0661  -0.0473 7   TYR A CD1 
46   C  CD2 . TYR A 7   ? 0.1123 0.2040 0.2048 -0.0381 0.0878  -0.0497 7   TYR A CD2 
47   C  CE1 . TYR A 7   ? 0.0633 0.1531 0.1823 -0.0148 0.0466  -0.0312 7   TYR A CE1 
48   C  CE2 . TYR A 7   ? 0.1088 0.1850 0.1629 -0.0389 0.0679  -0.0345 7   TYR A CE2 
49   C  CZ  . TYR A 7   ? 0.0721 0.1416 0.1601 -0.0353 0.0594  -0.0402 7   TYR A CZ  
50   O  OH  . TYR A 7   ? 0.1098 0.1313 0.1723 -0.0040 0.0421  -0.0218 7   TYR A OH  
51   N  N   . GLY A 8   ? 0.1791 0.2418 0.5092 0.0132  0.1928  -0.0816 8   GLY A N   
52   C  CA  . GLY A 8   ? 0.1141 0.1979 0.3818 -0.0047 0.0889  -0.0555 8   GLY A CA  
53   C  C   . GLY A 8   ? 0.1553 0.2672 0.3292 -0.0601 0.1406  -0.0703 8   GLY A C   
54   O  O   . GLY A 8   ? 0.1393 0.2477 0.3552 -0.0150 0.1295  -0.0810 8   GLY A O   
55   N  N   . LYS A 9   ? 0.0947 0.3097 0.4128 -0.0399 0.0908  -0.0911 9   LYS A N   
56   C  CA  . LYS A 9   ? 0.1845 0.2332 0.4454 -0.0227 0.0347  -0.0502 9   LYS A CA  
57   C  C   . LYS A 9   ? 0.1894 0.1983 0.3069 -0.0091 0.0841  -0.0506 9   LYS A C   
58   O  O   . LYS A 9   ? 0.1389 0.3142 0.3514 -0.0317 0.0599  -0.0030 9   LYS A O   
59   C  CB  . LYS A 9   ? 0.1212 0.4440 0.4247 0.0074  0.0819  -0.0842 9   LYS A CB  
60   C  CG  . LYS A 9   ? 0.2599 0.4600 0.6298 0.1018  0.0367  -0.0036 9   LYS A CG  
61   C  CD  . LYS A 9   ? 0.5310 0.4985 0.5272 0.0425  0.2135  -0.0315 9   LYS A CD  
62   N  N   . HIS A 10  ? 0.1442 0.1980 0.4437 0.0135  0.1150  0.0151  10  HIS A N   
63   C  CA  . HIS A 10  ? 0.1703 0.1723 0.4487 0.0155  0.1456  0.0509  10  HIS A CA  
64   C  C   . HIS A 10  ? 0.1217 0.2029 0.4527 0.0730  0.1752  0.0533  10  HIS A C   
65   O  O   . HIS A 10  ? 0.1669 0.1947 0.4313 0.0617  0.1399  0.0491  10  HIS A O   
66   C  CB  . HIS A 10  ? 0.2165 0.1896 0.4147 0.0162  0.1612  0.0280  10  HIS A CB  
67   C  CG  . HIS A 10  ? 0.2377 0.2044 0.3612 0.0323  0.0506  0.0600  10  HIS A CG  
68   N  ND1 . HIS A 10  ? 0.2075 0.2153 0.4002 0.0447  0.0608  0.0207  10  HIS A ND1 
69   C  CD2 . HIS A 10  ? 0.2144 0.1796 0.4001 0.0418  0.1989  -0.0307 10  HIS A CD2 
70   C  CE1 . HIS A 10  ? 0.1992 0.2340 0.3498 0.0888  -0.0019 0.0089  10  HIS A CE1 
71   N  NE2 . HIS A 10  ? 0.1432 0.2779 0.3008 0.0320  0.0274  0.0010  10  HIS A NE2 
72   N  N   . ASN A 11  ? 0.1170 0.2120 0.4820 0.0520  0.1835  0.0794  11  ASN A N   
73   C  CA  . ASN A 11  ? 0.1782 0.2030 0.3644 0.0704  0.1615  0.0712  11  ASN A CA  
74   C  C   . ASN A 11  ? 0.1399 0.1652 0.3665 0.0241  0.1156  0.0343  11  ASN A C   
75   O  O   . ASN A 11  ? 0.1468 0.1846 0.3583 0.0410  0.1420  0.0336  11  ASN A O   
76   C  CB  . ASN A 11  ? 0.1374 0.2023 0.3345 0.0247  0.1780  0.0331  11  ASN A CB  
77   C  CG  . ASN A 11  ? 0.1412 0.2315 0.3541 0.0044  0.2037  -0.0252 11  ASN A CG  
78   O  OD1 . ASN A 11  ? 0.2165 0.2255 0.4057 -0.0276 0.1753  -0.0126 11  ASN A OD1 
79   N  ND2 . ASN A 11  ? 0.2188 0.2583 0.3673 0.0038  0.1851  0.0136  11  ASN A ND2 
80   N  N   . GLY A 12  ? 0.1085 0.1967 0.3635 0.0584  0.1612  0.0739  12  GLY A N   
81   C  CA  . GLY A 12  ? 0.1100 0.2072 0.3161 0.0086  0.1434  0.0089  12  GLY A CA  
82   C  C   . GLY A 12  ? 0.0444 0.1327 0.3398 0.0241  0.1102  0.0419  12  GLY A C   
83   O  O   . GLY A 12  ? 0.0824 0.1493 0.3444 0.0115  0.0732  0.0420  12  GLY A O   
84   N  N   . PRO A 13  ? 0.0579 0.1554 0.3122 0.0084  0.1223  -0.0068 13  PRO A N   
85   C  CA  . PRO A 13  ? 0.0947 0.1321 0.3143 -0.0051 0.0835  0.0080  13  PRO A CA  
86   C  C   . PRO A 13  ? 0.1166 0.1394 0.3021 0.0152  0.0908  0.0106  13  PRO A C   
87   O  O   . PRO A 13  ? 0.0653 0.1737 0.3391 0.0024  0.0756  -0.0152 13  PRO A O   
88   C  CB  . PRO A 13  ? 0.1003 0.1625 0.2863 -0.0165 0.1107  -0.0330 13  PRO A CB  
89   C  CG  . PRO A 13  ? 0.1530 0.1788 0.2716 -0.0339 0.1214  -0.0350 13  PRO A CG  
90   C  CD  . PRO A 13  ? 0.0899 0.2043 0.2583 -0.0006 0.0867  0.0130  13  PRO A CD  
91   N  N   . GLU A 14  ? 0.1190 0.1357 0.3136 0.0176  0.1125  0.0429  14  GLU A N   
92   C  CA  . GLU A 14  ? 0.1866 0.1629 0.3720 0.0267  0.0446  0.0439  14  GLU A CA  
93   C  C   . GLU A 14  ? 0.1291 0.1696 0.3116 0.0789  0.0513  0.0383  14  GLU A C   
94   O  O   . GLU A 14  ? 0.1238 0.2056 0.3376 0.0561  0.0455  0.0736  14  GLU A O   
95   C  CB  . GLU A 14  ? 0.2070 0.1751 0.4395 0.0281  0.0227  0.1059  14  GLU A CB  
96   C  CG  . GLU A 14  ? 0.2995 0.2155 0.4292 -0.0388 0.0515  0.0411  14  GLU A CG  
97   C  CD  . GLU A 14  ? 0.6132 0.7077 0.3206 -0.0438 0.0368  0.0751  14  GLU A CD  
98   O  OE1 . GLU A 14  ? 0.7287 0.6988 0.4840 -0.0334 -0.1687 0.0107  14  GLU A OE1 
99   O  OE2 . GLU A 14  ? 0.7136 0.8124 0.3792 0.0065  0.0782  0.1713  14  GLU A OE2 
100  N  N   . HIS A 15  ? 0.0644 0.1680 0.3374 0.0352  0.0773  0.0456  15  HIS A N   
101  C  CA  . HIS A 15  ? 0.0423 0.1717 0.3738 0.0245  0.0754  0.0142  15  HIS A CA  
102  C  C   . HIS A 15  ? 0.0315 0.1534 0.3777 0.0149  0.0195  0.0223  15  HIS A C   
103  O  O   . HIS A 15  ? 0.0387 0.1919 0.3813 -0.0012 0.0317  0.0612  15  HIS A O   
104  C  CB  . HIS A 15  ? 0.0703 0.1899 0.3426 0.0478  0.0899  0.0451  15  HIS A CB  
105  C  CG  . HIS A 15  ? 0.1024 0.1852 0.3658 0.0533  0.1209  0.0534  15  HIS A CG  
106  N  ND1 . HIS A 15  ? 0.0999 0.2270 0.3750 0.0817  0.1174  0.0601  15  HIS A ND1 
107  C  CD2 . HIS A 15  ? 0.1462 0.2032 0.3972 0.0653  0.1048  -0.0071 15  HIS A CD2 
108  C  CE1 . HIS A 15  ? 0.2238 0.2429 0.3416 0.0878  0.0336  0.0490  15  HIS A CE1 
109  N  NE2 . HIS A 15  ? 0.1547 0.2316 0.3533 0.0914  0.0794  0.0363  15  HIS A NE2 
110  N  N   . TRP A 16  ? 0.0454 0.1423 0.3118 0.0287  0.0576  0.0318  16  TRP A N   
111  C  CA  . TRP A 16  ? 0.0181 0.1454 0.3175 0.0190  0.0358  0.0263  16  TRP A CA  
112  C  C   . TRP A 16  ? 0.0263 0.1533 0.3210 0.0179  0.0036  0.0430  16  TRP A C   
113  O  O   . TRP A 16  ? 0.0532 0.1347 0.3559 -0.0053 0.0131  0.0341  16  TRP A O   
114  C  CB  . TRP A 16  ? 0.0166 0.1641 0.2500 0.0165  0.0250  0.0058  16  TRP A CB  
115  C  CG  . TRP A 16  ? 0.0432 0.1208 0.2563 -0.0046 0.0287  -0.0091 16  TRP A CG  
116  C  CD1 . TRP A 16  ? 0.0818 0.1227 0.2532 0.0027  0.0670  -0.0048 16  TRP A CD1 
117  C  CD2 . TRP A 16  ? 0.0446 0.1139 0.2416 -0.0153 0.0388  0.0048  16  TRP A CD2 
118  N  NE1 . TRP A 16  ? 0.0788 0.1400 0.2158 0.0068  0.0737  0.0051  16  TRP A NE1 
119  C  CE2 . TRP A 16  ? 0.0597 0.1389 0.2247 0.0026  0.0559  0.0098  16  TRP A CE2 
120  C  CE3 . TRP A 16  ? 0.0366 0.1116 0.2683 -0.0047 0.0473  -0.0013 16  TRP A CE3 
121  C  CZ2 . TRP A 16  ? 0.0579 0.1448 0.2233 -0.0245 0.0792  0.0021  16  TRP A CZ2 
122  C  CZ3 . TRP A 16  ? 0.0564 0.1323 0.2326 -0.0288 0.0568  -0.0220 16  TRP A CZ3 
123  C  CH2 . TRP A 16  ? 0.0775 0.1405 0.2223 -0.0159 0.0771  -0.0252 16  TRP A CH2 
124  N  N   . HIS A 17  ? 0.0420 0.1509 0.3076 0.0036  -0.0029 0.0241  17  HIS A N   
125  C  CA  . HIS A 17  ? 0.0407 0.1760 0.3240 -0.0122 0.0031  0.0281  17  HIS A CA  
126  C  C   . HIS A 17  ? 0.0370 0.1948 0.3789 -0.0306 -0.0244 0.0514  17  HIS A C   
127  O  O   . HIS A 17  ? 0.0727 0.1838 0.4352 -0.0077 -0.0237 0.0432  17  HIS A O   
128  C  CB  . HIS A 17  ? 0.0518 0.1996 0.3236 0.0160  0.0000  0.0436  17  HIS A CB  
129  C  CG  . HIS A 17  ? 0.0741 0.1773 0.4124 0.0197  -0.0242 0.0637  17  HIS A CG  
130  N  ND1 . HIS A 17  ? 0.0840 0.2812 0.4072 0.0011  -0.0292 0.0858  17  HIS A ND1 
131  C  CD2 . HIS A 17  ? 0.0790 0.2303 0.3874 0.0561  0.0480  0.0480  17  HIS A CD2 
132  C  CE1 . HIS A 17  ? 0.0831 0.2638 0.4879 0.0019  0.0143  0.0469  17  HIS A CE1 
133  N  NE2 . HIS A 17  ? 0.0851 0.2308 0.3848 0.0315  0.0099  0.1009  17  HIS A NE2 
134  N  N   . LYS A 18  ? 0.0854 0.1917 0.3949 0.0026  -0.0053 0.0806  18  LYS A N   
135  C  CA  . LYS A 18  ? 0.0773 0.2433 0.3914 -0.0160 0.0052  0.0951  18  LYS A CA  
136  C  C   . LYS A 18  ? 0.1009 0.2111 0.4889 -0.0244 -0.0163 0.0913  18  LYS A C   
137  O  O   . LYS A 18  ? 0.1176 0.2297 0.5759 -0.0379 -0.0493 0.0863  18  LYS A O   
138  C  CB  . LYS A 18  ? 0.0231 0.2271 0.4373 -0.0069 0.0038  0.0932  18  LYS A CB  
139  C  CG  . LYS A 18  ? 0.0687 0.2380 0.4705 0.0298  0.0300  0.0961  18  LYS A CG  
140  C  CD  . LYS A 18  ? 0.1001 0.2352 0.3747 0.0335  0.0347  0.1217  18  LYS A CD  
141  C  CE  . LYS A 18  ? 0.0728 0.2671 0.4656 0.0222  0.0547  0.1317  18  LYS A CE  
142  N  NZ  . LYS A 18  ? 0.0678 0.2896 0.3962 0.0554  0.0699  0.1638  18  LYS A NZ  
143  N  N   . ASP A 19  ? 0.0435 0.2226 0.4105 0.0100  0.0162  0.0927  19  ASP A N   
144  C  CA  . ASP A 19  ? 0.1076 0.1963 0.4428 -0.0148 0.0471  0.0826  19  ASP A CA  
145  C  C   . ASP A 19  ? 0.0617 0.1848 0.5039 -0.0323 0.0275  0.0488  19  ASP A C   
146  O  O   . ASP A 19  ? 0.1358 0.1767 0.5316 -0.0252 0.0467  0.0635  19  ASP A O   
147  C  CB  . ASP A 19  ? 0.0858 0.3180 0.4702 -0.0174 -0.0234 0.0889  19  ASP A CB  
148  C  CG  . ASP A 19  ? 0.2605 0.3996 0.3856 0.0211  0.0034  0.0680  19  ASP A CG  
149  O  OD1 . ASP A 19  ? 0.2669 0.6991 0.5199 -0.0548 -0.0061 0.0345  19  ASP A OD1 
150  O  OD2 . ASP A 19  ? 0.5845 0.6338 0.6117 0.0529  -0.0996 -0.0761 19  ASP A OD2 
151  N  N   . PHE A 20  ? 0.0782 0.1958 0.4206 0.0002  0.0111  0.0792  20  PHE A N   
152  C  CA  . PHE A 20  ? 0.0579 0.1806 0.3604 -0.0019 -0.0209 0.0408  20  PHE A CA  
153  C  C   . PHE A 20  ? 0.0166 0.1743 0.3552 -0.0070 -0.0008 0.0259  20  PHE A C   
154  O  O   . PHE A 20  ? 0.0728 0.1471 0.3362 -0.0106 -0.0043 0.0175  20  PHE A O   
155  C  CB  . PHE A 20  ? 0.0506 0.2537 0.3225 -0.0130 -0.0156 0.0464  20  PHE A CB  
156  C  CG  . PHE A 20  ? 0.0836 0.2816 0.3327 -0.0326 0.0176  0.0842  20  PHE A CG  
157  C  CD1 . PHE A 20  ? 0.1122 0.3294 0.4123 0.0098  -0.0062 0.1197  20  PHE A CD1 
158  C  CD2 . PHE A 20  ? 0.1170 0.3619 0.3489 0.0049  0.0030  0.0680  20  PHE A CD2 
159  C  CE1 . PHE A 20  ? 0.1225 0.3883 0.3605 0.0285  0.0257  0.0762  20  PHE A CE1 
160  C  CE2 . PHE A 20  ? 0.2637 0.3875 0.3716 -0.0109 0.0089  0.1229  20  PHE A CE2 
161  C  CZ  . PHE A 20  ? 0.1049 0.4003 0.3246 0.0138  0.0228  0.1132  20  PHE A CZ  
162  N  N   . PRO A 21  ? 0.1048 0.2071 0.3865 -0.0156 -0.0527 0.0586  21  PRO A N   
163  C  CA  . PRO A 21  ? 0.0906 0.2448 0.3622 -0.0603 -0.0231 0.0374  21  PRO A CA  
164  C  C   . PRO A 21  ? 0.0599 0.1683 0.3641 -0.0234 -0.0314 0.0055  21  PRO A C   
165  O  O   . PRO A 21  ? 0.0743 0.2054 0.3520 -0.0111 -0.0533 0.0223  21  PRO A O   
166  C  CB  . PRO A 21  ? 0.0816 0.3380 0.4038 -0.0796 -0.0623 0.0413  21  PRO A CB  
167  C  CG  . PRO A 21  ? 0.2330 0.3064 0.4499 -0.1165 -0.1032 0.0293  21  PRO A CG  
168  C  CD  . PRO A 21  ? 0.1421 0.2595 0.3976 -0.0573 -0.0201 0.0739  21  PRO A CD  
169  N  N   A ILE A 22  ? 0.0710 0.1455 0.3858 -0.0278 -0.0546 -0.0142 22  ILE A N   
170  N  N   B ILE A 22  ? 0.0705 0.1515 0.3750 -0.0241 -0.0525 -0.0196 22  ILE A N   
171  C  CA  A ILE A 22  ? 0.0820 0.1412 0.3395 -0.0291 -0.0630 0.0013  22  ILE A CA  
172  C  CA  B ILE A 22  ? 0.0949 0.1647 0.3181 -0.0233 -0.0502 -0.0107 22  ILE A CA  
173  C  C   A ILE A 22  ? 0.0617 0.1313 0.2948 -0.0130 -0.0383 -0.0181 22  ILE A C   
174  C  C   B ILE A 22  ? 0.0587 0.1498 0.2902 -0.0020 -0.0416 -0.0225 22  ILE A C   
175  O  O   A ILE A 22  ? 0.0575 0.1425 0.2974 0.0027  -0.0270 -0.0281 22  ILE A O   
176  O  O   B ILE A 22  ? 0.0584 0.1538 0.2987 -0.0098 -0.0326 -0.0386 22  ILE A O   
177  C  CB  A ILE A 22  ? 0.0707 0.1192 0.3392 -0.0201 -0.0417 -0.0225 22  ILE A CB  
178  C  CB  B ILE A 22  ? 0.1019 0.1970 0.2984 0.0275  -0.0442 -0.0524 22  ILE A CB  
179  C  CG1 A ILE A 22  ? 0.1197 0.1466 0.2897 0.0142  -0.0595 -0.0398 22  ILE A CG1 
180  C  CG1 B ILE A 22  ? 0.1754 0.2041 0.2693 0.0085  -0.0176 -0.0647 22  ILE A CG1 
181  C  CG2 A ILE A 22  ? 0.1400 0.1736 0.3403 -0.0100 -0.1034 0.0011  22  ILE A CG2 
182  C  CG2 B ILE A 22  ? 0.0852 0.1438 0.2799 -0.0357 -0.0233 -0.0350 22  ILE A CG2 
183  C  CD1 A ILE A 22  ? 0.0902 0.1234 0.2673 -0.0044 0.0001  -0.0117 22  ILE A CD1 
184  C  CD1 B ILE A 22  ? 0.1807 0.2131 0.2994 0.0179  -0.0395 -0.0806 22  ILE A CD1 
185  N  N   . ALA A 23  ? 0.0678 0.1319 0.2856 -0.0055 -0.0346 -0.0086 23  ALA A N   
186  C  CA  . ALA A 23  ? 0.0699 0.1349 0.2737 0.0009  -0.0179 -0.0036 23  ALA A CA  
187  C  C   . ALA A 23  ? 0.0606 0.1414 0.2521 0.0016  -0.0152 -0.0412 23  ALA A C   
188  O  O   . ALA A 23  ? 0.0829 0.1562 0.2570 -0.0077 -0.0111 -0.0165 23  ALA A O   
189  C  CB  . ALA A 23  ? 0.0509 0.1673 0.2681 0.0177  -0.0352 -0.0345 23  ALA A CB  
190  N  N   . LYS A 24  ? 0.0754 0.1839 0.2711 0.0144  -0.0487 -0.0151 24  LYS A N   
191  C  CA  . LYS A 24  ? 0.0644 0.2037 0.2416 -0.0004 -0.0406 -0.0336 24  LYS A CA  
192  C  C   . LYS A 24  ? 0.1393 0.1921 0.3066 0.0279  -0.0615 -0.0547 24  LYS A C   
193  O  O   . LYS A 24  ? 0.1186 0.3143 0.3323 0.0036  -0.0880 -0.0037 24  LYS A O   
194  C  CB  . LYS A 24  ? 0.0784 0.2194 0.3201 0.0399  -0.0373 0.0135  24  LYS A CB  
195  C  CG  . LYS A 24  ? 0.1116 0.2552 0.2572 0.0516  0.0027  0.0259  24  LYS A CG  
196  C  CD  . LYS A 24  ? 0.1246 0.2971 0.4198 0.0337  -0.0186 0.0583  24  LYS A CD  
197  C  CE  . LYS A 24  ? 0.2086 0.3943 0.3895 0.1075  0.0642  0.1242  24  LYS A CE  
198  N  NZ  . LYS A 24  ? 0.2415 0.4251 0.5718 -0.0341 0.1424  0.0234  24  LYS A NZ  
199  N  N   . GLY A 25  ? 0.0992 0.1873 0.2996 0.0258  -0.0343 -0.0406 25  GLY A N   
200  C  CA  . GLY A 25  ? 0.1170 0.2240 0.3043 -0.0093 -0.0305 -0.0721 25  GLY A CA  
201  C  C   . GLY A 25  ? 0.1269 0.2269 0.2199 0.0436  -0.0683 -0.0563 25  GLY A C   
202  O  O   . GLY A 25  ? 0.1242 0.2417 0.2362 0.0370  -0.0606 -0.0628 25  GLY A O   
203  N  N   . GLU A 26  ? 0.1158 0.2868 0.2287 0.0480  -0.0700 -0.0967 26  GLU A N   
204  C  CA  . GLU A 26  ? 0.1333 0.2857 0.2011 0.0342  -0.0766 -0.0895 26  GLU A CA  
205  C  C   . GLU A 26  ? 0.1237 0.2466 0.2060 0.0431  -0.0674 -0.0588 26  GLU A C   
206  O  O   . GLU A 26  ? 0.1989 0.2359 0.1552 0.0219  -0.0838 -0.0563 26  GLU A O   
207  C  CB  . GLU A 26  ? 0.3060 0.3400 0.3213 0.0544  -0.0412 -0.1735 26  GLU A CB  
208  C  CG  . GLU A 26  ? 0.3123 0.3829 0.3730 0.0326  -0.0403 -0.0850 26  GLU A CG  
209  C  CD  . GLU A 26  ? 0.2869 0.5195 0.2857 -0.0542 -0.1335 0.0062  26  GLU A CD  
210  O  OE1 . GLU A 26  ? 0.3176 0.5001 0.3254 -0.0892 -0.0697 -0.0561 26  GLU A OE1 
211  O  OE2 . GLU A 26  ? 0.3601 0.5392 0.5685 0.1222  -0.1076 -0.0140 26  GLU A OE2 
212  N  N   . ARG A 27  ? 0.1252 0.1581 0.1633 0.0276  -0.0428 -0.0668 27  ARG A N   
213  C  CA  . ARG A 27  ? 0.1039 0.1358 0.1310 0.0083  -0.0345 -0.0390 27  ARG A CA  
214  C  C   . ARG A 27  ? 0.0966 0.1388 0.1170 0.0222  -0.0234 -0.0324 27  ARG A C   
215  O  O   . ARG A 27  ? 0.1003 0.1397 0.1261 0.0204  -0.0297 -0.0305 27  ARG A O   
216  C  CB  . ARG A 27  ? 0.1357 0.1582 0.1472 0.0313  -0.0219 -0.0513 27  ARG A CB  
217  C  CG  . ARG A 27  ? 0.1554 0.2055 0.1861 0.0083  -0.0507 -0.0266 27  ARG A CG  
218  C  CD  . ARG A 27  ? 0.1908 0.2439 0.1481 0.0394  -0.0332 -0.0237 27  ARG A CD  
219  N  NE  . ARG A 27  ? 0.1974 0.1696 0.1441 0.0332  -0.0195 -0.0291 27  ARG A NE  
220  C  CZ  . ARG A 27  ? 0.1679 0.1846 0.1395 0.0509  -0.0115 -0.0352 27  ARG A CZ  
221  N  NH1 . ARG A 27  ? 0.1581 0.2224 0.1683 0.0605  0.0029  -0.0956 27  ARG A NH1 
222  N  NH2 . ARG A 27  ? 0.1570 0.1935 0.1658 0.0155  -0.0120 -0.0411 27  ARG A NH2 
223  N  N   . GLN A 28  ? 0.0892 0.1354 0.1351 0.0137  -0.0256 -0.0486 28  GLN A N   
224  C  CA  . GLN A 28  ? 0.0685 0.1152 0.1339 0.0044  -0.0136 -0.0396 28  GLN A CA  
225  C  C   . GLN A 28  ? 0.0581 0.1064 0.1159 0.0069  -0.0097 -0.0251 28  GLN A C   
226  O  O   . GLN A 28  ? 0.0951 0.1378 0.1073 0.0006  -0.0173 -0.0192 28  GLN A O   
227  C  CB  . GLN A 28  ? 0.0446 0.1512 0.1796 0.0122  -0.0241 -0.0377 28  GLN A CB  
228  C  CG  . GLN A 28  ? 0.0797 0.1318 0.1720 -0.0016 -0.0267 -0.0401 28  GLN A CG  
229  C  CD  . GLN A 28  ? 0.0304 0.1449 0.1673 -0.0163 -0.0092 -0.0345 28  GLN A CD  
230  O  OE1 . GLN A 28  ? 0.0588 0.1351 0.1810 -0.0040 -0.0189 -0.0369 28  GLN A OE1 
231  N  NE2 . GLN A 28  ? 0.0568 0.1383 0.1951 0.0061  -0.0247 -0.0372 28  GLN A NE2 
232  N  N   . SER A 29  ? 0.0460 0.1125 0.1137 0.0021  -0.0074 -0.0326 29  SER A N   
233  C  CA  . SER A 29  ? 0.0457 0.1021 0.1089 0.0077  -0.0150 -0.0283 29  SER A CA  
234  C  C   . SER A 29  ? 0.0517 0.0931 0.0920 -0.0084 -0.0017 -0.0092 29  SER A C   
235  O  O   . SER A 29  ? 0.0594 0.1087 0.1252 -0.0100 0.0097  -0.0179 29  SER A O   
236  C  CB  . SER A 29  ? 0.0429 0.1021 0.1149 0.0194  -0.0039 -0.0333 29  SER A CB  
237  O  OG  . SER A 29  ? 0.0624 0.1032 0.1136 0.0027  0.0091  -0.0280 29  SER A OG  
238  N  N   . PRO A 30  ? 0.0348 0.0965 0.1018 0.0015  0.0039  -0.0212 30  PRO A N   
239  C  CA  . PRO A 30  ? 0.0465 0.1132 0.0870 -0.0210 -0.0025 -0.0038 30  PRO A CA  
240  C  C   . PRO A 30  ? 0.0703 0.0989 0.0811 0.0096  -0.0110 -0.0172 30  PRO A C   
241  O  O   . PRO A 30  ? 0.0690 0.1124 0.1028 0.0168  -0.0146 -0.0138 30  PRO A O   
242  C  CB  . PRO A 30  ? 0.0225 0.1073 0.0994 0.0012  0.0029  -0.0183 30  PRO A CB  
243  C  CG  . PRO A 30  ? 0.0264 0.1091 0.1175 0.0027  0.0111  -0.0157 30  PRO A CG  
244  C  CD  . PRO A 30  ? 0.0415 0.1005 0.1154 0.0063  0.0100  -0.0237 30  PRO A CD  
245  N  N   . VAL A 31  ? 0.0913 0.1050 0.0705 0.0071  0.0095  0.0000  31  VAL A N   
246  C  CA  . VAL A 31  ? 0.0946 0.1158 0.0773 0.0201  -0.0049 0.0001  31  VAL A CA  
247  C  C   . VAL A 31  ? 0.0538 0.1182 0.0917 0.0308  0.0063  0.0006  31  VAL A C   
248  O  O   . VAL A 31  ? 0.0642 0.1341 0.1007 0.0192  0.0016  0.0066  31  VAL A O   
249  C  CB  . VAL A 31  ? 0.1177 0.1159 0.1019 0.0050  0.0162  -0.0147 31  VAL A CB  
250  C  CG1 . VAL A 31  ? 0.1046 0.1394 0.1486 -0.0055 0.0100  -0.0061 31  VAL A CG1 
251  C  CG2 . VAL A 31  ? 0.1219 0.1378 0.0998 0.0261  0.0222  -0.0189 31  VAL A CG2 
252  N  N   . ASP A 32  ? 0.0963 0.1098 0.0919 0.0183  -0.0144 -0.0018 32  ASP A N   
253  C  CA  . ASP A 32  ? 0.0832 0.1087 0.1064 0.0228  0.0013  0.0060  32  ASP A CA  
254  C  C   . ASP A 32  ? 0.1201 0.1268 0.0721 0.0337  -0.0041 0.0059  32  ASP A C   
255  O  O   . ASP A 32  ? 0.1217 0.1918 0.1094 0.0106  -0.0032 -0.0248 32  ASP A O   
256  C  CB  . ASP A 32  ? 0.1645 0.1145 0.1245 0.0377  -0.0150 0.0080  32  ASP A CB  
257  C  CG  . ASP A 32  ? 0.1493 0.1185 0.1181 0.0425  -0.0047 0.0092  32  ASP A CG  
258  O  OD1 . ASP A 32  ? 0.1490 0.1217 0.1046 0.0102  0.0032  0.0091  32  ASP A OD1 
259  O  OD2 . ASP A 32  ? 0.2232 0.1777 0.1229 -0.0077 -0.0164 0.0262  32  ASP A OD2 
260  N  N   . ILE A 33  ? 0.1018 0.1209 0.0899 0.0231  0.0133  -0.0016 33  ILE A N   
261  C  CA  . ILE A 33  ? 0.1042 0.1333 0.0967 0.0276  0.0218  0.0126  33  ILE A CA  
262  C  C   . ILE A 33  ? 0.1157 0.1279 0.0990 0.0216  0.0353  0.0061  33  ILE A C   
263  O  O   . ILE A 33  ? 0.1509 0.1245 0.1142 0.0186  0.0209  0.0212  33  ILE A O   
264  C  CB  . ILE A 33  ? 0.0922 0.1354 0.1073 0.0218  0.0286  0.0248  33  ILE A CB  
265  C  CG1 . ILE A 33  ? 0.1423 0.1219 0.1182 0.0178  0.0011  0.0370  33  ILE A CG1 
266  C  CG2 . ILE A 33  ? 0.0992 0.1700 0.1376 0.0352  0.0419  0.0072  33  ILE A CG2 
267  C  CD1 . ILE A 33  ? 0.0863 0.1758 0.1587 0.0209  0.0044  0.0529  33  ILE A CD1 
268  N  N   A ASP A 34  ? 0.1874 0.1521 0.0960 0.0390  0.0148  0.0375  34  ASP A N   
269  N  N   B ASP A 34  ? 0.1493 0.1668 0.0781 0.0343  0.0542  0.0203  34  ASP A N   
270  C  CA  A ASP A 34  ? 0.2074 0.1692 0.0866 0.0540  0.0544  0.0412  34  ASP A CA  
271  C  CA  B ASP A 34  ? 0.1827 0.1583 0.1306 0.0370  0.0374  0.0513  34  ASP A CA  
272  C  C   A ASP A 34  ? 0.2029 0.1654 0.0581 0.0593  0.0408  0.0461  34  ASP A C   
273  C  C   B ASP A 34  ? 0.1914 0.1925 0.1112 0.0541  0.0355  0.0310  34  ASP A C   
274  O  O   A ASP A 34  ? 0.2237 0.2096 0.0864 0.0647  0.0532  0.0025  34  ASP A O   
275  O  O   B ASP A 34  ? 0.2513 0.1940 0.1068 0.0762  0.0500  0.0300  34  ASP A O   
276  C  CB  A ASP A 34  ? 0.2684 0.1646 0.0933 0.0754  0.0227  0.0111  34  ASP A CB  
277  C  CB  B ASP A 34  ? 0.2220 0.1707 0.1240 0.0530  0.0184  0.0490  34  ASP A CB  
278  C  CG  A ASP A 34  ? 0.2965 0.1957 0.1561 0.0504  0.0452  0.0340  34  ASP A CG  
279  C  CG  B ASP A 34  ? 0.2125 0.1911 0.1349 0.0256  0.0095  0.0525  34  ASP A CG  
280  O  OD1 A ASP A 34  ? 0.4083 0.2046 0.1646 0.0836  0.0211  0.0198  34  ASP A OD1 
281  O  OD1 B ASP A 34  ? 0.2037 0.1945 0.1418 0.0274  -0.0127 0.0666  34  ASP A OD1 
282  O  OD2 A ASP A 34  ? 0.2452 0.2319 0.2092 0.0588  0.0736  0.0201  34  ASP A OD2 
283  O  OD2 B ASP A 34  ? 0.2451 0.3194 0.1738 0.0521  -0.0125 0.1154  34  ASP A OD2 
284  N  N   . THR A 35  ? 0.1808 0.1770 0.1163 0.0497  0.0429  0.0627  35  THR A N   
285  C  CA  . THR A 35  ? 0.2037 0.2123 0.1145 0.0851  0.0760  0.0581  35  THR A CA  
286  C  C   . THR A 35  ? 0.2225 0.1746 0.1260 0.0624  0.0979  0.0451  35  THR A C   
287  O  O   . THR A 35  ? 0.2299 0.2308 0.1531 0.0774  0.1042  0.0311  35  THR A O   
288  C  CB  . THR A 35  ? 0.1904 0.2129 0.1787 0.0586  0.0989  0.0681  35  THR A CB  
289  O  OG1 . THR A 35  ? 0.2653 0.2082 0.1587 0.0632  0.0895  0.0703  35  THR A OG1 
290  C  CG2 . THR A 35  ? 0.2549 0.2583 0.1534 0.0883  0.0806  0.0834  35  THR A CG2 
291  N  N   . HIS A 36  ? 0.3291 0.1804 0.1142 0.0895  0.0868  0.0600  36  HIS A N   
292  C  CA  . HIS A 36  ? 0.2895 0.2143 0.1193 0.0372  0.0551  0.0972  36  HIS A CA  
293  C  C   . HIS A 36  ? 0.3640 0.2911 0.1124 0.0290  0.0497  0.0420  36  HIS A C   
294  O  O   . HIS A 36  ? 0.3642 0.4077 0.1355 0.0966  0.0496  0.0322  36  HIS A O   
295  C  CB  . HIS A 36  ? 0.3727 0.2030 0.1483 0.0245  0.0094  0.0906  36  HIS A CB  
296  C  CG  . HIS A 36  ? 0.3892 0.2158 0.1286 0.0097  -0.0172 0.0528  36  HIS A CG  
297  N  ND1 . HIS A 36  ? 0.4256 0.2734 0.2244 -0.0258 -0.0668 0.0595  36  HIS A ND1 
298  C  CD2 . HIS A 36  ? 0.4471 0.1839 0.1623 0.0584  -0.0760 0.0502  36  HIS A CD2 
299  C  CE1 . HIS A 36  ? 0.3955 0.2555 0.2577 -0.0181 -0.0706 0.0445  36  HIS A CE1 
300  N  NE2 . HIS A 36  ? 0.5224 0.1954 0.3631 0.0782  -0.0099 0.0372  36  HIS A NE2 
301  N  N   . THR A 37  ? 0.3495 0.1991 0.1609 0.0828  0.0838  0.0139  37  THR A N   
302  C  CA  . THR A 37  ? 0.3752 0.2121 0.1293 0.0784  0.0423  0.0614  37  THR A CA  
303  C  C   . THR A 37  ? 0.2983 0.2366 0.1465 0.1220  0.0199  0.0111  37  THR A C   
304  O  O   . THR A 37  ? 0.4442 0.2385 0.1711 0.1027  0.0001  0.0122  37  THR A O   
305  C  CB  . THR A 37  ? 0.3811 0.3100 0.3174 0.1233  -0.1172 0.0063  37  THR A CB  
306  O  OG1 . THR A 37  ? 0.3940 0.2877 0.4904 0.0719  0.0125  0.0919  37  THR A OG1 
307  C  CG2 . THR A 37  ? 0.2639 0.4056 0.1830 0.1010  -0.0255 0.0163  37  THR A CG2 
308  N  N   . ALA A 38  ? 0.2820 0.2168 0.1269 0.1083  0.0446  0.0434  38  ALA A N   
309  C  CA  . ALA A 38  ? 0.2458 0.2007 0.1173 0.1011  0.0455  0.0477  38  ALA A CA  
310  C  C   . ALA A 38  ? 0.3213 0.2011 0.2145 0.0853  0.1135  0.0324  38  ALA A C   
311  O  O   . ALA A 38  ? 0.4005 0.2153 0.3157 0.0954  0.1863  0.0536  38  ALA A O   
312  C  CB  . ALA A 38  ? 0.2424 0.2096 0.1356 0.0609  0.0411  0.0171  38  ALA A CB  
313  N  N   . LYS A 39  ? 0.3229 0.2399 0.1213 0.1351  0.0556  0.0081  39  LYS A N   
314  C  CA  . LYS A 39  ? 0.3468 0.3206 0.1368 0.1870  0.0397  -0.0152 39  LYS A CA  
315  C  C   . LYS A 39  ? 0.2658 0.2256 0.1628 0.1056  0.0853  0.0395  39  LYS A C   
316  O  O   . LYS A 39  ? 0.2198 0.2606 0.1129 0.1052  0.0447  0.0245  39  LYS A O   
317  C  CB  . LYS A 39  ? 0.4510 0.4568 0.1622 0.2037  -0.0357 -0.0801 39  LYS A CB  
318  C  CG  . LYS A 39  ? 0.3984 0.4506 0.1807 0.0759  0.0575  -0.0485 39  LYS A CG  
319  C  CD  . LYS A 39  ? 0.2046 0.5495 0.2408 0.1597  0.0700  0.0797  39  LYS A CD  
320  C  CE  . LYS A 39  ? 0.2518 0.5387 0.2444 0.0435  0.0800  0.0141  39  LYS A CE  
321  N  NZ  . LYS A 39  ? 0.2153 0.6042 0.2831 0.0500  0.0633  0.1206  39  LYS A NZ  
322  N  N   . TYR A 40  ? 0.2746 0.3263 0.1738 0.0998  0.0941  0.0491  40  TYR A N   
323  C  CA  . TYR A 40  ? 0.2273 0.2951 0.1281 0.0278  0.1118  0.0073  40  TYR A CA  
324  C  C   . TYR A 40  ? 0.1828 0.2915 0.1329 0.0173  0.0549  -0.0053 40  TYR A C   
325  O  O   . TYR A 40  ? 0.2299 0.3418 0.1287 0.0643  0.0549  -0.0108 40  TYR A O   
326  C  CB  . TYR A 40  ? 0.2893 0.3582 0.2236 -0.0247 0.1763  0.0312  40  TYR A CB  
327  C  CG  . TYR A 40  ? 0.2809 0.3628 0.2315 -0.0626 0.0708  -0.0182 40  TYR A CG  
328  C  CD1 . TYR A 40  ? 0.3826 0.3154 0.2414 -0.0624 0.0691  -0.0436 40  TYR A CD1 
329  C  CD2 . TYR A 40  ? 0.4233 0.5877 0.2973 0.0038  0.1473  -0.0316 40  TYR A CD2 
330  C  CE1 . TYR A 40  ? 0.3103 0.5704 0.1821 -0.0394 0.0780  0.0856  40  TYR A CE1 
331  C  CE2 . TYR A 40  ? 0.4928 0.5841 0.2967 0.0776  0.0677  -0.0027 40  TYR A CE2 
332  C  CZ  . TYR A 40  ? 0.2930 0.7531 0.2188 -0.0335 0.0614  -0.0177 40  TYR A CZ  
333  O  OH  . TYR A 40  ? 0.3564 0.7478 0.5012 0.0241  0.0861  -0.0693 40  TYR A OH  
334  N  N   . ASP A 41  ? 0.1816 0.2360 0.1930 0.0613  0.0782  0.0000  41  ASP A N   
335  C  CA  . ASP A 41  ? 0.2412 0.2390 0.1785 0.0454  -0.0240 -0.0134 41  ASP A CA  
336  C  C   . ASP A 41  ? 0.2505 0.3406 0.1629 0.1122  0.0262  -0.0006 41  ASP A C   
337  O  O   . ASP A 41  ? 0.2347 0.3247 0.1725 0.0930  0.0524  0.0094  41  ASP A O   
338  C  CB  . ASP A 41  ? 0.2856 0.2350 0.2937 0.0207  0.0005  0.0020  41  ASP A CB  
339  C  CG  . ASP A 41  ? 0.3962 0.2952 0.3380 -0.0200 -0.0644 -0.0741 41  ASP A CG  
340  O  OD1 . ASP A 41  ? 0.4403 0.3576 0.3229 0.0812  -0.0701 -0.1150 41  ASP A OD1 
341  O  OD2 . ASP A 41  ? 0.3781 0.3996 0.4830 -0.0859 -0.1865 0.0933  41  ASP A OD2 
342  N  N   . PRO A 42  ? 0.2843 0.4976 0.2021 0.1264  0.0516  -0.0083 42  PRO A N   
343  C  CA  . PRO A 42  ? 0.3319 0.5249 0.4503 0.2091  -0.0088 -0.0111 42  PRO A CA  
344  C  C   . PRO A 42  ? 0.3486 0.5314 0.2864 0.1652  0.1155  0.0153  42  PRO A C   
345  O  O   . PRO A 42  ? 0.4073 0.6690 0.4376 0.1747  0.0368  0.0692  42  PRO A O   
346  C  CB  . PRO A 42  ? 0.4552 0.8181 0.3153 -0.0524 0.1708  0.0697  42  PRO A CB  
347  C  CG  . PRO A 42  ? 0.4159 0.6664 0.2116 0.1421  0.2619  -0.0609 42  PRO A CG  
348  C  CD  . PRO A 42  ? 0.3758 0.5184 0.1634 0.2096  0.1674  0.0443  42  PRO A CD  
349  N  N   . SER A 43  ? 0.2856 0.4245 0.2850 0.2019  0.0911  -0.0500 43  SER A N   
350  C  CA  . SER A 43  ? 0.5197 0.3974 0.2689 0.1500  0.0134  -0.1039 43  SER A CA  
351  C  C   . SER A 43  ? 0.4279 0.3129 0.3195 0.1539  0.0735  -0.0105 43  SER A C   
352  O  O   . SER A 43  ? 0.4635 0.3317 0.5103 0.1240  -0.0748 0.0193  43  SER A O   
353  C  CB  . SER A 43  ? 0.5915 0.5132 0.4423 0.1032  -0.0697 -0.1064 43  SER A CB  
354  O  OG  . SER A 43  ? 0.5459 0.5905 0.2811 0.0223  -0.1243 -0.1319 43  SER A OG  
355  N  N   . LEU A 44  ? 0.2624 0.4010 0.2628 0.1003  0.0368  -0.0593 44  LEU A N   
356  C  CA  . LEU A 44  ? 0.1838 0.4977 0.3050 0.1092  0.0177  0.0128  44  LEU A CA  
357  C  C   . LEU A 44  ? 0.1191 0.6363 0.4595 -0.0254 0.0134  0.1456  44  LEU A C   
358  O  O   . LEU A 44  ? 0.2189 0.5572 0.3697 -0.1038 -0.0336 0.1342  44  LEU A O   
359  C  CB  . LEU A 44  ? 0.2036 0.5224 0.2049 0.0883  0.0585  0.0462  44  LEU A CB  
360  C  CG  . LEU A 44  ? 0.2068 0.3578 0.1885 0.1003  0.0495  0.0646  44  LEU A CG  
361  C  CD1 . LEU A 44  ? 0.2273 0.3371 0.2529 0.0600  0.0536  0.0020  44  LEU A CD1 
362  C  CD2 . LEU A 44  ? 0.2432 0.2396 0.2700 0.0850  0.0434  0.0115  44  LEU A CD2 
363  N  N   . LYS A 45  ? 0.1750 0.4890 0.5241 -0.0704 -0.0566 0.1411  45  LYS A N   
364  C  CA  . LYS A 45  ? 0.3109 0.4532 0.3766 0.0710  -0.1092 0.0020  45  LYS A CA  
365  C  C   . LYS A 45  ? 0.2284 0.4696 0.2357 0.1144  -0.0111 0.0508  45  LYS A C   
366  O  O   . LYS A 45  ? 0.1676 0.5794 0.3501 -0.0293 0.0644  -0.0801 45  LYS A O   
367  C  CB  . LYS A 45  ? 0.3231 0.4111 0.2638 0.1224  0.0528  -0.0252 45  LYS A CB  
368  C  CG  . LYS A 45  ? 0.3265 0.8078 0.2425 0.0130  0.0063  -0.2413 45  LYS A CG  
369  N  N   . PRO A 46  ? 0.1725 0.5202 0.2685 -0.0441 0.0473  0.0199  46  PRO A N   
370  C  CA  . PRO A 46  ? 0.1986 0.4572 0.2767 -0.0606 0.0334  0.0540  46  PRO A CA  
371  C  C   . PRO A 46  ? 0.0922 0.3669 0.2586 0.0276  0.0736  0.0285  46  PRO A C   
372  O  O   . PRO A 46  ? 0.1118 0.4198 0.3572 -0.0245 0.0261  0.1011  46  PRO A O   
373  C  CB  . PRO A 46  ? 0.1702 0.4858 0.3998 -0.0856 0.0856  0.0124  46  PRO A CB  
374  C  CG  . PRO A 46  ? 0.2690 0.5460 0.4745 -0.0139 0.1348  -0.2002 46  PRO A CG  
375  C  CD  . PRO A 46  ? 0.3301 0.4417 0.3725 0.0477  0.1110  -0.1548 46  PRO A CD  
376  N  N   . LEU A 47  ? 0.0972 0.3544 0.3983 0.0084  0.0907  0.0439  47  LEU A N   
377  C  CA  . LEU A 47  ? 0.1200 0.3055 0.4095 -0.0434 0.0344  0.1191  47  LEU A CA  
378  C  C   . LEU A 47  ? 0.0936 0.2515 0.5193 -0.0402 0.0407  0.1538  47  LEU A C   
379  O  O   . LEU A 47  ? 0.0917 0.3272 0.6210 -0.0804 -0.0348 0.2367  47  LEU A O   
380  C  CB  . LEU A 47  ? 0.3121 0.3410 0.5886 0.0919  -0.0190 0.1471  47  LEU A CB  
381  C  CG  . LEU A 47  ? 0.1540 0.3273 0.6637 -0.0661 -0.1353 0.0678  47  LEU A CG  
382  C  CD1 . LEU A 47  ? 0.1122 0.2732 0.6801 -0.0849 -0.1016 0.0860  47  LEU A CD1 
383  C  CD2 . LEU A 47  ? 0.2127 0.2572 0.7900 -0.0952 -0.1849 0.0566  47  LEU A CD2 
384  N  N   . SER A 48  ? 0.0721 0.2396 0.2637 -0.0150 0.0374  0.0881  48  SER A N   
385  C  CA  . SER A 48  ? 0.0895 0.2322 0.2463 0.0351  0.0374  0.0451  48  SER A CA  
386  C  C   . SER A 48  ? 0.0552 0.2283 0.2486 -0.0184 0.0201  0.0242  48  SER A C   
387  O  O   . SER A 48  ? 0.1028 0.2237 0.2713 -0.0499 0.0398  0.0020  48  SER A O   
388  C  CB  . SER A 48  ? 0.1179 0.2350 0.3349 0.0308  0.0272  0.0424  48  SER A CB  
389  O  OG  . SER A 48  ? 0.1806 0.3138 0.3642 0.0516  0.0359  0.0906  48  SER A OG  
390  N  N   . VAL A 49  ? 0.1080 0.2433 0.2773 -0.0622 0.0097  0.0413  49  VAL A N   
391  C  CA  . VAL A 49  ? 0.1605 0.2368 0.2909 -0.0855 0.0435  0.0194  49  VAL A CA  
392  C  C   . VAL A 49  ? 0.1698 0.2498 0.3534 -0.0488 0.0249  0.0026  49  VAL A C   
393  O  O   . VAL A 49  ? 0.2339 0.3871 0.3842 -0.1443 -0.0386 0.0220  49  VAL A O   
394  C  CB  . VAL A 49  ? 0.1931 0.2548 0.3755 -0.1176 0.0719  -0.0050 49  VAL A CB  
395  C  CG1 . VAL A 49  ? 0.3937 0.3971 0.3877 -0.0972 0.1797  0.1011  49  VAL A CG1 
396  C  CG2 . VAL A 49  ? 0.2346 0.2340 0.4054 -0.0748 0.0862  0.0223  49  VAL A CG2 
397  N  N   . SER A 50  ? 0.1735 0.2287 0.3488 -0.1066 -0.0525 0.0010  50  SER A N   
398  C  CA  . SER A 50  ? 0.1539 0.2422 0.3832 -0.0706 -0.0326 0.0195  50  SER A CA  
399  C  C   . SER A 50  ? 0.1140 0.2329 0.2998 -0.0257 -0.0873 -0.0034 50  SER A C   
400  O  O   . SER A 50  ? 0.1578 0.2201 0.3098 -0.0381 -0.0723 0.0304  50  SER A O   
401  C  CB  . SER A 50  ? 0.2104 0.2623 0.3677 -0.0223 0.0020  -0.0001 50  SER A CB  
402  O  OG  . SER A 50  ? 0.3475 0.4464 0.4422 -0.1400 0.0552  -0.0650 50  SER A OG  
403  N  N   . TYR A 51  ? 0.1839 0.2335 0.3265 -0.0669 -0.0719 -0.0181 51  TYR A N   
404  C  CA  . TYR A 51  ? 0.1197 0.1799 0.3368 -0.0289 -0.0701 0.0181  51  TYR A CA  
405  C  C   . TYR A 51  ? 0.1262 0.2350 0.3123 -0.0594 -0.0243 0.0621  51  TYR A C   
406  O  O   . TYR A 51  ? 0.2054 0.2169 0.2891 -0.0193 -0.0724 0.0479  51  TYR A O   
407  C  CB  . TYR A 51  ? 0.1467 0.2033 0.2664 -0.0011 -0.0803 -0.0053 51  TYR A CB  
408  C  CG  . TYR A 51  ? 0.1360 0.1628 0.2498 -0.0372 -0.0673 0.0277  51  TYR A CG  
409  C  CD1 . TYR A 51  ? 0.1130 0.1639 0.2565 -0.0509 -0.0435 0.0343  51  TYR A CD1 
410  C  CD2 . TYR A 51  ? 0.1347 0.1544 0.2446 -0.0350 -0.0325 0.0231  51  TYR A CD2 
411  C  CE1 . TYR A 51  ? 0.1061 0.1444 0.1920 -0.0242 -0.0212 0.0128  51  TYR A CE1 
412  C  CE2 . TYR A 51  ? 0.1742 0.1321 0.2206 -0.0296 -0.0682 -0.0023 51  TYR A CE2 
413  C  CZ  . TYR A 51  ? 0.1302 0.1317 0.2203 -0.0408 -0.0475 0.0108  51  TYR A CZ  
414  O  OH  . TYR A 51  ? 0.1473 0.1437 0.2004 -0.0315 -0.0465 0.0171  51  TYR A OH  
415  N  N   . ASP A 52  ? 0.0886 0.2822 0.4394 -0.0736 -0.0653 0.0443  52  ASP A N   
416  C  CA  . ASP A 52  ? 0.1836 0.2658 0.4682 -0.0566 -0.0895 0.1014  52  ASP A CA  
417  C  C   . ASP A 52  ? 0.2289 0.3169 0.4902 -0.0189 -0.1073 0.0978  52  ASP A C   
418  O  O   . ASP A 52  ? 0.2732 0.3667 0.5071 -0.0142 -0.1533 0.1593  52  ASP A O   
419  C  CB  . ASP A 52  ? 0.2251 0.3767 0.6684 0.0027  -0.0759 0.0914  52  ASP A CB  
420  C  CG  . ASP A 52  ? 0.1846 0.4144 0.8915 -0.0241 0.0276  0.0168  52  ASP A CG  
421  O  OD1 . ASP A 52  ? 0.2998 0.5774 0.9210 -0.0231 0.0129  -0.0960 52  ASP A OD1 
422  O  OD2 . ASP A 52  ? 0.6167 0.5126 1.2312 0.1203  0.0641  0.2608  52  ASP A OD2 
423  N  N   . GLN A 53  ? 0.1936 0.2230 0.5693 0.0044  -0.0648 0.1348  53  GLN A N   
424  C  CA  . GLN A 53  ? 0.2979 0.2103 0.6082 -0.0015 -0.0586 0.1530  53  GLN A CA  
425  C  C   . GLN A 53  ? 0.3491 0.1981 0.2345 -0.0259 -0.0572 0.0632  53  GLN A C   
426  O  O   . GLN A 53  ? 0.2477 0.2290 0.3763 -0.0321 -0.0952 0.0941  53  GLN A O   
427  C  CB  . GLN A 53  ? 0.5449 0.3054 0.4975 0.0119  -0.0641 0.0692  53  GLN A CB  
428  C  CG  . GLN A 53  ? 0.5650 0.5725 0.6070 -0.0214 -0.0615 0.2001  53  GLN A CG  
429  C  CD  . GLN A 53  ? 0.5307 0.6980 0.7033 -0.0030 -0.1161 0.1085  53  GLN A CD  
430  O  OE1 . GLN A 53  ? 0.6016 0.4503 1.3523 0.1099  -0.1364 0.1432  53  GLN A OE1 
431  N  NE2 . GLN A 53  ? 0.5927 0.6786 0.9731 -0.0587 -0.1008 0.3009  53  GLN A NE2 
432  N  N   . ALA A 54  ? 0.2272 0.1842 0.3479 -0.0800 -0.0928 0.0649  54  ALA A N   
433  C  CA  . ALA A 54  ? 0.2052 0.1557 0.2271 -0.0592 -0.1036 0.0146  54  ALA A CA  
434  C  C   . ALA A 54  ? 0.3075 0.1998 0.2329 -0.0499 -0.0898 -0.0161 54  ALA A C   
435  O  O   . ALA A 54  ? 0.3245 0.2416 0.2885 -0.0914 -0.1167 -0.0326 54  ALA A O   
436  C  CB  . ALA A 54  ? 0.2619 0.1526 0.2948 0.0002  -0.0444 -0.0008 54  ALA A CB  
437  N  N   . THR A 55  ? 0.3188 0.1439 0.1845 -0.0189 -0.0972 0.0259  55  THR A N   
438  C  CA  . THR A 55  ? 0.3240 0.1785 0.1647 0.0168  -0.0929 0.0272  55  THR A CA  
439  C  C   . THR A 55  ? 0.3240 0.1122 0.1218 -0.0067 -0.0951 0.0331  55  THR A C   
440  O  O   . THR A 55  ? 0.3446 0.1296 0.1409 -0.0125 -0.0906 0.0078  55  THR A O   
441  C  CB  . THR A 55  ? 0.4775 0.2194 0.2133 0.0381  -0.0648 0.0685  55  THR A CB  
442  O  OG1 . THR A 55  ? 0.5050 0.2210 0.3778 0.0282  -0.1437 0.0326  55  THR A OG1 
443  C  CG2 . THR A 55  ? 0.6330 0.1976 0.1831 0.1641  -0.0583 0.0641  55  THR A CG2 
444  N  N   . SER A 56  ? 0.3856 0.1054 0.1542 -0.0179 -0.1184 0.0186  56  SER A N   
445  C  CA  . SER A 56  ? 0.4127 0.1134 0.1393 -0.0016 -0.0725 0.0163  56  SER A CA  
446  C  C   . SER A 56  ? 0.4423 0.1054 0.1192 0.0120  -0.0713 0.0046  56  SER A C   
447  O  O   . SER A 56  ? 0.5552 0.1228 0.1293 0.0469  -0.1260 0.0326  56  SER A O   
448  C  CB  . SER A 56  ? 0.3792 0.1260 0.1401 -0.0175 -0.1094 0.0074  56  SER A CB  
449  O  OG  . SER A 56  ? 0.4222 0.1361 0.1554 -0.0147 -0.1443 0.0160  56  SER A OG  
450  N  N   . LEU A 57  ? 0.4415 0.1351 0.1026 0.0367  -0.0254 0.0138  57  LEU A N   
451  C  CA  . LEU A 57  ? 0.5181 0.1170 0.1172 0.0280  -0.0301 0.0266  57  LEU A CA  
452  C  C   . LEU A 57  ? 0.4902 0.1073 0.1027 0.0331  -0.0377 0.0399  57  LEU A C   
453  O  O   . LEU A 57  ? 0.5068 0.1337 0.0994 0.0216  -0.0464 0.0309  57  LEU A O   
454  C  CB  . LEU A 57  ? 0.5195 0.1243 0.1337 0.0002  0.0065  -0.0029 57  LEU A CB  
455  C  CG  . LEU A 57  ? 0.5651 0.1217 0.1706 0.0763  -0.0793 -0.0046 57  LEU A CG  
456  C  CD1 . LEU A 57  ? 0.5956 0.1859 0.1823 0.0044  -0.0449 -0.0311 57  LEU A CD1 
457  C  CD2 . LEU A 57  ? 0.7097 0.1863 0.2308 0.1691  -0.1324 0.0105  57  LEU A CD2 
458  N  N   A ARG A 58  ? 0.1533 0.0872 0.1444 -0.0306 -0.0124 0.0337  58  ARG A N   
459  N  N   B ARG A 58  ? 0.4646 0.0538 0.0766 -0.0079 -0.0322 0.0279  58  ARG A N   
460  C  CA  A ARG A 58  ? 0.1281 0.1512 0.1791 0.0366  -0.0006 0.0701  58  ARG A CA  
461  C  CA  B ARG A 58  ? 0.3107 0.1278 0.0838 -0.0712 -0.0399 0.0480  58  ARG A CA  
462  C  C   A ARG A 58  ? 0.1302 0.1242 0.1217 -0.0386 0.0019  0.0691  58  ARG A C   
463  C  C   B ARG A 58  ? 0.3637 0.0901 0.0639 -0.0563 -0.0034 0.0173  58  ARG A C   
464  O  O   A ARG A 58  ? 0.1302 0.0974 0.1155 -0.0273 0.0217  0.0326  58  ARG A O   
465  O  O   B ARG A 58  ? 0.1633 0.1714 0.0603 -0.0312 0.0156  0.0358  58  ARG A O   
466  C  CB  A ARG A 58  ? 0.0861 0.2730 0.1277 0.0008  0.0820  0.0545  58  ARG A CB  
467  C  CB  B ARG A 58  ? 0.2561 0.1032 0.1438 -0.0113 0.0450  0.0344  58  ARG A CB  
468  C  CG  A ARG A 58  ? 0.0612 0.2643 0.1684 0.0351  0.0685  0.0744  58  ARG A CG  
469  C  CG  B ARG A 58  ? 0.1021 0.1218 0.2090 -0.0205 0.0491  0.0576  58  ARG A CG  
470  C  CD  A ARG A 58  ? 0.1948 0.2564 0.2769 0.0175  0.0834  0.0151  58  ARG A CD  
471  C  CD  B ARG A 58  ? 0.0728 0.1712 0.1444 -0.0672 0.0266  0.0534  58  ARG A CD  
472  N  NE  A ARG A 58  ? 0.1468 0.2579 0.2475 -0.0723 0.0963  0.0337  58  ARG A NE  
473  N  NE  B ARG A 58  ? 0.0469 0.1430 0.1517 -0.0138 0.0185  -0.0022 58  ARG A NE  
474  C  CZ  A ARG A 58  ? 0.1309 0.1404 0.2472 0.0230  0.0731  0.0594  58  ARG A CZ  
475  C  CZ  B ARG A 58  ? 0.0458 0.1883 0.1439 -0.0178 0.0193  0.0787  58  ARG A CZ  
476  N  NH1 A ARG A 58  ? 0.1405 0.1518 0.1812 -0.0219 0.0700  0.0328  58  ARG A NH1 
477  N  NH1 B ARG A 58  ? 0.0860 0.1379 0.1249 -0.0493 0.0256  0.0248  58  ARG A NH1 
478  N  NH2 A ARG A 58  ? 0.2267 0.2415 0.1984 0.1035  0.0582  0.0624  58  ARG A NH2 
479  N  NH2 B ARG A 58  ? 0.0579 0.1382 0.1465 -0.0170 0.0149  0.0358  58  ARG A NH2 
480  N  N   A ILE A 59  ? 0.2300 0.1665 0.0976 -0.0176 0.0206  0.0298  59  ILE A N   
481  N  N   B ILE A 59  ? 0.4457 0.0864 0.0342 -0.0154 -0.0281 0.0269  59  ILE A N   
482  C  CA  A ILE A 59  ? 0.1683 0.1460 0.1256 -0.0353 0.0527  0.0530  59  ILE A CA  
483  C  CA  B ILE A 59  ? 0.4153 0.0802 0.0928 -0.0122 -0.0534 0.0149  59  ILE A CA  
484  C  C   A ILE A 59  ? 0.1557 0.1664 0.0996 -0.0200 0.0243  0.0288  59  ILE A C   
485  C  C   B ILE A 59  ? 0.4102 0.0798 0.0899 -0.0337 -0.0709 0.0358  59  ILE A C   
486  O  O   A ILE A 59  ? 0.2964 0.2414 0.0829 -0.0087 0.0154  0.0254  59  ILE A O   
487  O  O   B ILE A 59  ? 0.4124 0.0998 0.0820 -0.0464 -0.0625 0.0282  59  ILE A O   
488  C  CB  A ILE A 59  ? 0.1867 0.1373 0.1158 -0.0154 0.0089  0.0434  59  ILE A CB  
489  C  CB  B ILE A 59  ? 0.4087 0.0827 0.0735 -0.0061 -0.0586 0.0017  59  ILE A CB  
490  C  CG1 A ILE A 59  ? 0.2211 0.1244 0.1211 -0.0249 0.0099  0.0434  59  ILE A CG1 
491  C  CG1 B ILE A 59  ? 0.3508 0.0834 0.0996 -0.0132 -0.0760 0.0000  59  ILE A CG1 
492  C  CG2 A ILE A 59  ? 0.2227 0.1437 0.1231 -0.0016 -0.0023 0.0192  59  ILE A CG2 
493  C  CG2 B ILE A 59  ? 0.3948 0.1243 0.0560 -0.0100 -0.0880 0.0179  59  ILE A CG2 
494  C  CD1 A ILE A 59  ? 0.2382 0.1359 0.1522 -0.0377 -0.0455 0.0318  59  ILE A CD1 
495  C  CD1 B ILE A 59  ? 0.3698 0.0751 0.0912 -0.0077 -0.0807 0.0057  59  ILE A CD1 
496  N  N   A LEU A 60  ? 0.1154 0.2399 0.1962 -0.0489 -0.0168 0.0133  60  LEU A N   
497  N  N   B LEU A 60  ? 0.3662 0.1125 0.0633 -0.1070 -0.0772 0.0429  60  LEU A N   
498  C  CA  A LEU A 60  ? 0.0942 0.2013 0.1049 -0.0479 -0.0509 0.0372  60  LEU A CA  
499  C  CA  B LEU A 60  ? 0.3927 0.1427 0.1256 -0.0983 -0.0557 0.0873  60  LEU A CA  
500  C  C   A LEU A 60  ? 0.1761 0.1737 0.1624 -0.0691 -0.0809 0.0397  60  LEU A C   
501  C  C   B LEU A 60  ? 0.3652 0.1758 0.0924 -0.0644 0.0032  0.0732  60  LEU A C   
502  O  O   A LEU A 60  ? 0.1340 0.2263 0.1483 -0.0636 -0.0548 0.0339  60  LEU A O   
503  O  O   B LEU A 60  ? 0.3037 0.2390 0.0868 -0.0674 -0.0141 0.0880  60  LEU A O   
504  C  CB  A LEU A 60  ? 0.0581 0.1903 0.2353 0.0256  -0.0365 -0.0145 60  LEU A CB  
505  C  CB  B LEU A 60  ? 0.2653 0.1825 0.2858 -0.1324 -0.0886 0.0561  60  LEU A CB  
506  C  CG  A LEU A 60  ? 0.0651 0.0511 0.3040 -0.0326 -0.0052 0.0336  60  LEU A CG  
507  C  CG  B LEU A 60  ? 0.2427 0.2007 0.1530 -0.0826 0.0122  0.0387  60  LEU A CG  
508  C  CD1 A LEU A 60  ? 0.2609 0.1572 0.2685 0.0609  -0.0287 -0.0044 60  LEU A CD1 
509  C  CD1 B LEU A 60  ? 0.2130 0.2201 0.1877 -0.1830 0.0241  0.0744  60  LEU A CD1 
510  C  CD2 A LEU A 60  ? 0.1091 0.1536 0.2630 -0.0427 0.0637  -0.0478 60  LEU A CD2 
511  C  CD2 B LEU A 60  ? 0.2707 0.2196 0.0960 -0.0762 0.0151  0.0307  60  LEU A CD2 
512  N  N   A ASN A 61  ? 0.2927 0.1909 0.1012 -0.0974 0.0023  0.0514  61  ASN A N   
513  N  N   B ASN A 61  ? 0.4003 0.1401 0.0591 -0.1062 -0.0096 -0.0099 61  ASN A N   
514  C  CA  A ASN A 61  ? 0.2939 0.1958 0.1037 -0.0634 0.0234  -0.0451 61  ASN A CA  
515  C  CA  B ASN A 61  ? 0.3961 0.1380 0.0764 -0.1204 0.0320  -0.0120 61  ASN A CA  
516  C  C   A ASN A 61  ? 0.3046 0.2251 0.0952 -0.1089 0.0605  0.0023  61  ASN A C   
517  C  C   B ASN A 61  ? 0.3987 0.1745 0.1070 -0.1499 0.0471  -0.0009 61  ASN A C   
518  O  O   A ASN A 61  ? 0.3037 0.1558 0.1383 -0.0854 0.0650  0.0190  61  ASN A O   
519  O  O   B ASN A 61  ? 0.4760 0.1371 0.0813 -0.1032 0.0687  0.0222  61  ASN A O   
520  C  CB  A ASN A 61  ? 0.4296 0.1050 0.1055 -0.0536 0.0554  0.0141  61  ASN A CB  
521  C  CB  B ASN A 61  ? 0.4478 0.1572 0.0922 -0.1390 0.0647  -0.0381 61  ASN A CB  
522  C  CG  A ASN A 61  ? 0.3356 0.1896 0.1040 -0.0529 0.0966  -0.0365 61  ASN A CG  
523  C  CG  B ASN A 61  ? 0.4242 0.3145 0.0805 -0.0766 0.0433  -0.0278 61  ASN A CG  
524  O  OD1 A ASN A 61  ? 0.3727 0.1682 0.1723 -0.1013 0.0541  -0.0236 61  ASN A OD1 
525  O  OD1 B ASN A 61  ? 0.4032 0.1694 0.1386 -0.1188 0.0200  -0.0216 61  ASN A OD1 
526  N  ND2 A ASN A 61  ? 0.3968 0.1233 0.1779 -0.1307 0.1139  -0.0454 61  ASN A ND2 
527  N  ND2 B ASN A 61  ? 0.3985 0.1533 0.1758 -0.1248 0.0832  0.0093  61  ASN A ND2 
528  N  N   . ASN A 62  ? 0.3495 0.1506 0.1118 -0.1183 0.0263  0.0035  62  ASN A N   
529  C  CA  . ASN A 62  ? 0.3556 0.1633 0.1813 -0.1232 0.0275  -0.0377 62  ASN A CA  
530  C  C   . ASN A 62  ? 0.3037 0.2075 0.1605 -0.1212 0.0936  -0.0478 62  ASN A C   
531  O  O   . ASN A 62  ? 0.3204 0.2746 0.2702 -0.1584 0.1122  -0.1105 62  ASN A O   
532  C  CB  . ASN A 62  ? 0.2906 0.1854 0.1555 -0.1087 0.0205  -0.0141 62  ASN A CB  
533  C  CG  . ASN A 62  ? 0.2597 0.1870 0.1641 -0.0107 0.0057  -0.0291 62  ASN A CG  
534  O  OD1 . ASN A 62  ? 0.2300 0.2029 0.1383 -0.0499 0.0647  -0.0303 62  ASN A OD1 
535  N  ND2 . ASN A 62  ? 0.3740 0.3198 0.2018 0.0076  0.0071  -0.1147 62  ASN A ND2 
536  N  N   . GLY A 63  ? 0.2725 0.1816 0.1397 -0.0708 0.0974  -0.0204 63  GLY A N   
537  C  CA  . GLY A 63  ? 0.2701 0.1859 0.1617 -0.1002 0.1043  -0.0326 63  GLY A CA  
538  C  C   . GLY A 63  ? 0.2316 0.1982 0.1684 -0.0726 0.1079  -0.0427 63  GLY A C   
539  O  O   . GLY A 63  ? 0.1859 0.2258 0.2524 -0.0713 0.1142  -0.0668 63  GLY A O   
540  N  N   . HIS A 64  ? 0.2207 0.1572 0.1392 -0.0782 0.1074  -0.0269 64  HIS A N   
541  C  CA  . HIS A 64  ? 0.1941 0.1875 0.1254 -0.0684 0.0822  -0.0163 64  HIS A CA  
542  C  C   . HIS A 64  ? 0.1615 0.1426 0.1247 -0.0444 0.0615  -0.0122 64  HIS A C   
543  O  O   . HIS A 64  ? 0.1585 0.2074 0.2583 -0.0617 0.0261  0.0880  64  HIS A O   
544  C  CB  . HIS A 64  ? 0.1485 0.2181 0.1479 -0.0553 0.0297  -0.0229 64  HIS A CB  
545  C  CG  . HIS A 64  ? 0.1791 0.2132 0.2425 -0.0609 0.0439  -0.0140 64  HIS A CG  
546  N  ND1 . HIS A 64  ? 0.2075 0.2645 0.2402 -0.0391 0.0377  -0.0462 64  HIS A ND1 
547  C  CD2 . HIS A 64  ? 0.2343 0.2183 0.2128 -0.0538 0.0457  0.0058  64  HIS A CD2 
548  C  CE1 . HIS A 64  ? 0.1901 0.2494 0.2669 -0.0346 0.0838  -0.0063 64  HIS A CE1 
549  N  NE2 . HIS A 64  ? 0.2169 0.2576 0.2951 -0.0339 0.0544  0.0189  64  HIS A NE2 
550  N  N   . SER A 65  ? 0.1646 0.1603 0.1071 -0.0493 0.0469  0.0121  65  SER A N   
551  C  CA  . SER A 65  ? 0.1595 0.1488 0.1078 -0.0479 0.0326  0.0205  65  SER A CA  
552  C  C   . SER A 65  ? 0.1707 0.1650 0.1033 -0.0548 0.0239  0.0209  65  SER A C   
553  O  O   . SER A 65  ? 0.2347 0.2081 0.1195 -0.0710 0.0436  0.0293  65  SER A O   
554  C  CB  . SER A 65  ? 0.1525 0.1975 0.1048 -0.0436 0.0454  0.0365  65  SER A CB  
555  O  OG  . SER A 65  ? 0.1674 0.2733 0.1404 -0.0585 0.0361  0.0731  65  SER A OG  
556  N  N   . PHE A 66  ? 0.1713 0.1763 0.0922 -0.0375 0.0055  0.0300  66  PHE A N   
557  C  CA  . PHE A 66  ? 0.2174 0.1582 0.0847 -0.0435 -0.0087 0.0314  66  PHE A CA  
558  C  C   . PHE A 66  ? 0.2548 0.1446 0.0776 -0.0311 -0.0058 0.0119  66  PHE A C   
559  O  O   . PHE A 66  ? 0.2561 0.1347 0.0852 -0.0355 0.0044  0.0160  66  PHE A O   
560  C  CB  . PHE A 66  ? 0.2353 0.2084 0.0841 -0.0602 -0.0197 0.0150  66  PHE A CB  
561  C  CG  . PHE A 66  ? 0.1983 0.1703 0.0802 -0.0122 0.0206  -0.0320 66  PHE A CG  
562  C  CD1 . PHE A 66  ? 0.1773 0.1836 0.0735 -0.0315 -0.0048 -0.0158 66  PHE A CD1 
563  C  CD2 . PHE A 66  ? 0.1944 0.1642 0.1114 -0.0212 0.0339  -0.0380 66  PHE A CD2 
564  C  CE1 . PHE A 66  ? 0.1822 0.1601 0.1215 -0.0222 0.0031  -0.0151 66  PHE A CE1 
565  C  CE2 . PHE A 66  ? 0.1836 0.1492 0.1327 -0.0293 0.0037  -0.0299 66  PHE A CE2 
566  C  CZ  . PHE A 66  ? 0.1869 0.1652 0.1098 -0.0163 -0.0069 -0.0331 66  PHE A CZ  
567  N  N   A LYS A 67  ? 0.3053 0.1578 0.0669 -0.0363 -0.0282 0.0419  67  LYS A N   
568  N  N   B LYS A 67  ? 0.2242 0.1746 0.1042 -0.0174 -0.0107 0.0593  67  LYS A N   
569  C  CA  A LYS A 67  ? 0.4227 0.1262 0.0481 -0.0106 -0.0572 0.0167  67  LYS A CA  
570  C  CA  B LYS A 67  ? 0.2423 0.1556 0.1102 -0.0305 -0.0359 0.0157  67  LYS A CA  
571  C  C   A LYS A 67  ? 0.3815 0.0637 0.1019 -0.0425 -0.0706 0.0070  67  LYS A C   
572  C  C   B LYS A 67  ? 0.2869 0.1043 0.0344 -0.0500 -0.0208 0.0357  67  LYS A C   
573  O  O   A LYS A 67  ? 0.4582 0.1516 0.1124 -0.0375 -0.0575 0.0255  67  LYS A O   
574  O  O   B LYS A 67  ? 0.2810 0.1801 0.0333 -0.0227 0.0225  0.0198  67  LYS A O   
575  C  CB  A LYS A 67  ? 0.3995 0.1945 0.2258 -0.0800 -0.1499 0.0639  67  LYS A CB  
576  C  CB  B LYS A 67  ? 0.1644 0.1500 0.0678 -0.0062 0.0216  0.0237  67  LYS A CB  
577  C  CG  A LYS A 67  ? 0.3173 0.1591 0.1983 -0.0274 -0.0881 0.0075  67  LYS A CG  
578  C  CG  B LYS A 67  ? 0.1865 0.2348 0.1972 -0.1316 -0.0268 -0.0190 67  LYS A CG  
579  C  CD  A LYS A 67  ? 0.3843 0.1364 0.1890 -0.0836 -0.0701 0.0300  67  LYS A CD  
580  C  CD  B LYS A 67  ? 0.2083 0.1886 0.1185 -0.0596 0.0194  -0.0117 67  LYS A CD  
581  C  CE  A LYS A 67  ? 0.3811 0.3691 0.2373 -0.0609 0.0440  0.1641  67  LYS A CE  
582  C  CE  B LYS A 67  ? 0.1278 0.1494 0.1985 -0.0301 -0.0319 0.0236  67  LYS A CE  
583  N  NZ  A LYS A 67  ? 0.5471 0.2964 0.6204 -0.0033 0.0167  0.0593  67  LYS A NZ  
584  N  NZ  B LYS A 67  ? 0.0967 0.1739 0.1568 0.0062  0.0064  0.0152  67  LYS A NZ  
585  N  N   A VAL A 68  ? 0.3887 0.1430 0.1204 0.0436  -0.0564 0.0230  68  VAL A N   
586  N  N   B VAL A 68  ? 0.3624 0.1128 0.1031 0.0442  0.0001  -0.0053 68  VAL A N   
587  C  CA  A VAL A 68  ? 0.3700 0.1286 0.0469 0.0697  -0.0352 0.0181  68  VAL A CA  
588  C  CA  B VAL A 68  ? 0.4688 0.1037 0.0590 0.0824  -0.0456 -0.0050 68  VAL A CA  
589  C  C   A VAL A 68  ? 0.3149 0.1523 0.1213 0.0639  -0.0455 -0.0181 68  VAL A C   
590  C  C   B VAL A 68  ? 0.4897 0.0676 0.0773 0.0253  -0.0039 0.0245  68  VAL A C   
591  O  O   A VAL A 68  ? 0.3467 0.1143 0.1172 0.0312  -0.0469 0.0003  68  VAL A O   
592  O  O   B VAL A 68  ? 0.4827 0.0585 0.0818 0.0414  -0.0623 0.0029  68  VAL A O   
593  C  CB  A VAL A 68  ? 0.3740 0.0845 0.1539 0.0706  -0.0752 0.0384  68  VAL A CB  
594  C  CB  B VAL A 68  ? 0.4744 0.0911 0.1308 0.0798  -0.0428 -0.0624 68  VAL A CB  
595  C  CG1 A VAL A 68  ? 0.3838 0.1685 0.1561 0.0872  -0.0754 -0.0113 68  VAL A CG1 
596  C  CG1 B VAL A 68  ? 0.5064 0.1141 0.1559 0.0862  -0.0827 0.0069  68  VAL A CG1 
597  C  CG2 A VAL A 68  ? 0.3614 0.1452 0.1314 0.0258  -0.0065 0.0053  68  VAL A CG2 
598  C  CG2 B VAL A 68  ? 0.5021 0.0820 0.0590 0.0323  -0.0688 -0.0314 68  VAL A CG2 
599  N  N   A GLU A 69  ? 0.3912 0.1486 0.1049 0.0759  -0.0352 -0.0242 69  GLU A N   
600  N  N   B GLU A 69  ? 0.5457 0.0646 0.0165 0.0331  -0.0427 0.0143  69  GLU A N   
601  C  CA  A GLU A 69  ? 0.3380 0.1421 0.0474 0.0544  -0.0248 0.0074  69  GLU A CA  
602  C  CA  B GLU A 69  ? 0.4030 0.0415 0.1222 -0.0290 -0.0308 0.0068  69  GLU A CA  
603  C  C   A GLU A 69  ? 0.3427 0.1062 0.1261 0.0476  -0.0212 -0.0064 69  GLU A C   
604  C  C   B GLU A 69  ? 0.4796 0.1134 0.0503 0.0334  -0.0514 0.0249  69  GLU A C   
605  O  O   A GLU A 69  ? 0.4190 0.0685 0.0771 0.0403  -0.0346 -0.0122 69  GLU A O   
606  O  O   B GLU A 69  ? 0.6059 0.2454 0.0718 0.0414  -0.0854 0.0034  69  GLU A O   
607  C  CB  A GLU A 69  ? 0.1506 0.1272 0.1503 0.0296  -0.1015 0.0009  69  GLU A CB  
608  C  CB  B GLU A 69  ? 0.3486 0.1641 0.1667 0.0355  0.0300  0.0480  69  GLU A CB  
609  C  CG  A GLU A 69  ? 0.1508 0.2437 0.1736 0.0582  -0.0979 0.0315  69  GLU A CG  
610  C  CG  B GLU A 69  ? 0.3687 0.1592 0.1814 0.0347  0.1459  0.0695  69  GLU A CG  
611  C  CD  A GLU A 69  ? 0.2789 0.2303 0.1503 0.0358  -0.0713 0.0292  69  GLU A CD  
612  C  CD  B GLU A 69  ? 0.3344 0.1685 0.2116 0.0320  0.1394  0.1009  69  GLU A CD  
613  O  OE1 A GLU A 69  ? 0.2823 0.2640 0.0848 0.0490  -0.0175 -0.0511 69  GLU A OE1 
614  O  OE1 B GLU A 69  ? 0.2509 0.2182 0.2176 0.0516  0.1040  0.0147  69  GLU A OE1 
615  O  OE2 A GLU A 69  ? 0.2634 0.2429 0.1537 0.0006  -0.0436 0.0641  69  GLU A OE2 
616  O  OE2 B GLU A 69  ? 0.3499 0.2231 0.3864 0.2054  0.1430  0.1542  69  GLU A OE2 
617  N  N   . PHE A 70  ? 0.4134 0.1028 0.0958 0.0145  -0.0407 0.0077  70  PHE A N   
618  C  CA  . PHE A 70  ? 0.3452 0.0926 0.1538 -0.0155 -0.0608 0.0082  70  PHE A CA  
619  C  C   . PHE A 70  ? 0.3143 0.0931 0.1498 0.0023  -0.0726 0.0013  70  PHE A C   
620  O  O   . PHE A 70  ? 0.3163 0.1159 0.1786 0.0035  -0.0752 0.0115  70  PHE A O   
621  C  CB  . PHE A 70  ? 0.3310 0.1098 0.1146 -0.0020 -0.0718 0.0142  70  PHE A CB  
622  C  CG  . PHE A 70  ? 0.3198 0.1078 0.1448 0.0053  -0.0929 0.0267  70  PHE A CG  
623  C  CD1 . PHE A 70  ? 0.3371 0.1168 0.1577 0.0284  -0.0707 0.0474  70  PHE A CD1 
624  C  CD2 . PHE A 70  ? 0.3064 0.1089 0.1224 0.0195  -0.0710 0.0190  70  PHE A CD2 
625  C  CE1 . PHE A 70  ? 0.2776 0.1354 0.1838 0.0193  -0.0167 0.0688  70  PHE A CE1 
626  C  CE2 . PHE A 70  ? 0.3343 0.1086 0.1268 0.0228  -0.0497 0.0319  70  PHE A CE2 
627  C  CZ  . PHE A 70  ? 0.3120 0.1350 0.1316 0.0455  -0.0249 0.0023  70  PHE A CZ  
628  N  N   A ASP A 71  ? 0.3404 0.0897 0.1743 -0.0040 -0.1100 0.0272  71  ASP A N   
629  N  N   B ASP A 71  ? 0.3455 0.0827 0.1843 -0.0103 -0.1196 0.0177  71  ASP A N   
630  C  CA  A ASP A 71  ? 0.3017 0.0866 0.1578 0.0190  -0.0659 0.0111  71  ASP A CA  
631  C  CA  B ASP A 71  ? 0.3112 0.0814 0.1990 0.0183  -0.0801 0.0163  71  ASP A CA  
632  C  C   A ASP A 71  ? 0.2750 0.0852 0.1609 -0.0245 -0.0469 0.0082  71  ASP A C   
633  C  C   B ASP A 71  ? 0.2893 0.0345 0.2134 -0.0199 -0.0644 0.0003  71  ASP A C   
634  O  O   A ASP A 71  ? 0.2364 0.2158 0.2872 -0.0805 -0.0731 0.0143  71  ASP A O   
635  O  O   B ASP A 71  ? 0.3449 0.0866 0.3195 -0.0628 -0.0022 0.0050  71  ASP A O   
636  C  CB  A ASP A 71  ? 0.3362 0.1227 0.2239 0.0190  -0.1198 0.0280  71  ASP A CB  
637  C  CB  B ASP A 71  ? 0.3529 0.1454 0.2680 0.0044  -0.1524 0.0444  71  ASP A CB  
638  C  CG  A ASP A 71  ? 0.3022 0.1282 0.2626 -0.0298 -0.1305 0.0134  71  ASP A CG  
639  C  CG  B ASP A 71  ? 0.3723 0.1727 0.3811 0.0359  -0.2120 -0.0055 71  ASP A CG  
640  O  OD1 A ASP A 71  ? 0.2639 0.1028 0.2122 -0.0053 -0.1013 0.0346  71  ASP A OD1 
641  O  OD1 B ASP A 71  ? 0.3403 0.1341 0.4445 0.0037  -0.1097 0.0838  71  ASP A OD1 
642  O  OD2 A ASP A 71  ? 0.3538 0.1545 0.2313 0.0168  -0.1030 0.0073  71  ASP A OD2 
643  O  OD2 B ASP A 71  ? 0.2737 0.1832 0.3758 -0.0397 -0.1185 0.0422  71  ASP A OD2 
644  N  N   . ASP A 72  ? 0.2535 0.0798 0.1568 -0.0018 -0.0482 0.0009  72  ASP A N   
645  C  CA  . ASP A 72  ? 0.2165 0.0876 0.1670 -0.0156 -0.0044 0.0005  72  ASP A CA  
646  C  C   . ASP A 72  ? 0.2236 0.0845 0.1891 -0.0249 -0.0013 0.0299  72  ASP A C   
647  O  O   . ASP A 72  ? 0.2750 0.0966 0.1921 -0.0176 -0.0039 -0.0006 72  ASP A O   
648  C  CB  . ASP A 72  ? 0.1873 0.1197 0.1626 -0.0102 0.0031  0.0071  72  ASP A CB  
649  C  CG  . ASP A 72  ? 0.1984 0.1294 0.1289 -0.0012 -0.0258 0.0162  72  ASP A CG  
650  O  OD1 . ASP A 72  ? 0.2226 0.1827 0.1661 -0.0252 -0.0391 0.0551  72  ASP A OD1 
651  O  OD2 . ASP A 72  ? 0.1839 0.1612 0.1560 -0.0107 -0.0337 0.0160  72  ASP A OD2 
652  N  N   . SER A 73  ? 0.2708 0.0843 0.2073 -0.0164 -0.0147 0.0342  73  SER A N   
653  C  CA  . SER A 73  ? 0.2751 0.0827 0.2366 -0.0230 -0.0089 0.0344  73  SER A CA  
654  C  C   . SER A 73  ? 0.2632 0.1058 0.2452 -0.0438 0.0058  -0.0036 73  SER A C   
655  O  O   . SER A 73  ? 0.2619 0.1073 0.2199 -0.0057 0.0002  0.0168  73  SER A O   
656  C  CB  . SER A 73  ? 0.3665 0.1104 0.2879 -0.0462 0.0039  0.0787  73  SER A CB  
657  O  OG  . SER A 73  ? 0.3207 0.1392 0.2506 0.0121  0.0253  0.0566  73  SER A OG  
658  N  N   . GLN A 74  ? 0.2451 0.1291 0.2587 -0.0081 0.0353  0.0268  74  GLN A N   
659  C  CA  . GLN A 74  ? 0.2390 0.1825 0.3323 0.0105  0.0359  0.0522  74  GLN A CA  
660  C  C   . GLN A 74  ? 0.1748 0.2079 0.2203 -0.0243 0.0179  -0.0002 74  GLN A C   
661  O  O   . GLN A 74  ? 0.2187 0.1625 0.2471 -0.0361 -0.0824 0.0505  74  GLN A O   
662  C  CB  . GLN A 74  ? 0.2104 0.2218 0.4095 0.0118  -0.0198 0.1051  74  GLN A CB  
663  C  CG  . GLN A 74  ? 0.2832 0.2963 0.4391 0.0011  -0.0341 0.1246  74  GLN A CG  
664  C  CD  . GLN A 74  ? 0.4248 0.3262 0.3838 -0.0842 -0.0294 0.1280  74  GLN A CD  
665  O  OE1 . GLN A 74  ? 0.4307 0.4590 0.6395 -0.0018 -0.0212 0.2818  74  GLN A OE1 
666  N  NE2 . GLN A 74  ? 0.8247 0.4578 0.3375 -0.1805 0.0632  -0.0130 74  GLN A NE2 
667  N  N   . ASP A 75  ? 0.2834 0.2800 0.2758 -0.0762 0.0732  -0.0642 75  ASP A N   
668  C  CA  . ASP A 75  ? 0.2072 0.2985 0.2813 -0.0840 -0.0012 -0.0326 75  ASP A CA  
669  C  C   . ASP A 75  ? 0.2006 0.2795 0.3066 -0.0574 -0.0579 -0.0048 75  ASP A C   
670  O  O   . ASP A 75  ? 0.2602 0.3166 0.4398 -0.0443 -0.1186 0.0442  75  ASP A O   
671  C  CB  . ASP A 75  ? 0.3021 0.2755 0.2570 0.0012  -0.0419 0.0121  75  ASP A CB  
672  C  CG  . ASP A 75  ? 0.4902 0.3592 0.3933 0.0491  -0.0078 0.1741  75  ASP A CG  
673  O  OD1 . ASP A 75  ? 0.2707 0.3268 0.5629 0.0044  -0.0451 0.1658  75  ASP A OD1 
674  O  OD2 . ASP A 75  ? 0.4720 0.4609 0.5534 0.1172  0.0965  0.1697  75  ASP A OD2 
675  N  N   . LYS A 76  ? 0.2511 0.2016 0.2819 -0.0447 -0.0933 0.0671  76  LYS A N   
676  C  CA  . LYS A 76  ? 0.3389 0.1483 0.3816 -0.0175 -0.0556 0.0290  76  LYS A CA  
677  C  C   . LYS A 76  ? 0.6203 0.2355 0.4908 0.0710  -0.0129 0.1311  76  LYS A C   
678  O  O   . LYS A 76  ? 0.6951 0.7411 0.6506 -0.1951 0.0450  0.3510  76  LYS A O   
679  C  CB  . LYS A 76  ? 0.2850 0.1606 0.3393 -0.0197 -0.1046 0.0091  76  LYS A CB  
680  C  CG  . LYS A 76  ? 0.4590 0.2658 0.3412 0.0313  -0.0759 0.0585  76  LYS A CG  
681  C  CD  . LYS A 76  ? 0.7458 0.2184 0.3138 -0.0785 -0.0476 -0.0104 76  LYS A CD  
682  C  CE  . LYS A 76  ? 0.7559 0.2764 0.3635 -0.0721 0.0591  0.0131  76  LYS A CE  
683  N  NZ  . LYS A 76  ? 0.6276 0.4288 0.3558 0.1246  0.0794  0.2165  76  LYS A NZ  
684  N  N   . ALA A 77  ? 0.2754 0.2379 0.4719 0.0111  -0.1803 0.0651  77  ALA A N   
685  C  CA  . ALA A 77  ? 0.1645 0.2353 0.3198 -0.0229 -0.1205 0.0449  77  ALA A CA  
686  C  C   . ALA A 77  ? 0.1282 0.1617 0.2582 -0.0113 -0.0589 0.0234  77  ALA A C   
687  O  O   . ALA A 77  ? 0.1411 0.3340 0.4551 -0.0231 -0.0812 -0.0812 77  ALA A O   
688  C  CB  . ALA A 77  ? 0.3019 0.1976 0.3014 0.0278  -0.1247 0.0048  77  ALA A CB  
689  N  N   . VAL A 78  ? 0.1561 0.1638 0.2336 -0.0369 -0.0722 0.0252  78  VAL A N   
690  C  CA  . VAL A 78  ? 0.1966 0.1516 0.2460 -0.0412 -0.0950 0.0456  78  VAL A CA  
691  C  C   . VAL A 78  ? 0.1300 0.1568 0.2644 -0.0434 -0.0586 0.0410  78  VAL A C   
692  O  O   . VAL A 78  ? 0.1199 0.1624 0.3184 -0.0435 -0.0727 0.0432  78  VAL A O   
693  C  CB  . VAL A 78  ? 0.3231 0.1947 0.3527 -0.0082 -0.1163 -0.0077 78  VAL A CB  
694  C  CG1 . VAL A 78  ? 0.3870 0.1779 0.4493 0.0141  -0.1613 0.0440  78  VAL A CG1 
695  C  CG2 . VAL A 78  ? 0.3162 0.2205 0.3856 -0.0142 -0.0646 0.0386  78  VAL A CG2 
696  N  N   . LEU A 79  ? 0.1216 0.1493 0.2131 -0.0238 -0.0495 0.0275  79  LEU A N   
697  C  CA  . LEU A 79  ? 0.0983 0.1597 0.1994 -0.0179 0.0053  0.0117  79  LEU A CA  
698  C  C   . LEU A 79  ? 0.0951 0.1363 0.2136 -0.0254 0.0179  -0.0008 79  LEU A C   
699  O  O   . LEU A 79  ? 0.1211 0.1451 0.2475 -0.0260 0.0133  -0.0265 79  LEU A O   
700  C  CB  . LEU A 79  ? 0.0969 0.1673 0.2210 -0.0129 0.0000  0.0298  79  LEU A CB  
701  C  CG  . LEU A 79  ? 0.1300 0.1504 0.2236 0.0294  0.0138  0.0098  79  LEU A CG  
702  C  CD1 . LEU A 79  ? 0.1310 0.1583 0.3713 0.0082  0.0288  0.0675  79  LEU A CD1 
703  C  CD2 . LEU A 79  ? 0.1332 0.1610 0.2149 0.0458  0.0414  0.0089  79  LEU A CD2 
704  N  N   . LYS A 80  ? 0.1192 0.1789 0.2146 -0.0216 0.0316  -0.0032 80  LYS A N   
705  C  CA  . LYS A 80  ? 0.1311 0.1764 0.2338 -0.0264 0.0405  0.0091  80  LYS A CA  
706  C  C   . LYS A 80  ? 0.1039 0.1803 0.2604 0.0037  0.0869  0.0042  80  LYS A C   
707  O  O   . LYS A 80  ? 0.1055 0.1706 0.2775 -0.0230 0.0298  0.0199  80  LYS A O   
708  C  CB  . LYS A 80  ? 0.2211 0.1842 0.2933 0.0001  0.0431  0.0494  80  LYS A CB  
709  C  CG  . LYS A 80  ? 0.1797 0.2395 0.4742 -0.0434 0.0964  0.1010  80  LYS A CG  
710  C  CD  . LYS A 80  ? 0.2151 0.3526 0.5923 0.0857  0.0054  0.0293  80  LYS A CD  
711  C  CE  . LYS A 80  ? 0.4667 0.3643 0.6714 0.2002  0.1026  0.0795  80  LYS A CE  
712  N  NZ  . LYS A 80  ? 0.5949 0.5152 0.9730 0.3290  -0.0841 -0.0102 80  LYS A NZ  
713  N  N   . GLY A 81  ? 0.1340 0.1895 0.2513 0.0343  0.0914  0.0171  81  GLY A N   
714  C  CA  . GLY A 81  ? 0.1356 0.1818 0.3155 0.0281  0.1232  0.0637  81  GLY A CA  
715  C  C   . GLY A 81  ? 0.1502 0.1863 0.3471 0.0372  0.1254  0.0544  81  GLY A C   
716  O  O   . GLY A 81  ? 0.1614 0.1851 0.2683 -0.0034 0.1094  0.0100  81  GLY A O   
717  N  N   . GLY A 82  ? 0.1854 0.2168 0.4108 0.0244  0.1374  0.1038  82  GLY A N   
718  C  CA  . GLY A 82  ? 0.2415 0.1937 0.5911 0.0649  0.1306  0.0792  82  GLY A CA  
719  C  C   . GLY A 82  ? 0.2640 0.2161 0.3075 0.1025  0.1461  0.0815  82  GLY A C   
720  O  O   . GLY A 82  ? 0.3336 0.3174 0.3560 0.1337  0.1803  0.0531  82  GLY A O   
721  N  N   . PRO A 83  ? 0.2109 0.1637 0.3379 0.0822  0.1051  0.0619  83  PRO A N   
722  C  CA  . PRO A 83  ? 0.2605 0.2214 0.2428 0.1131  0.0670  0.0225  83  PRO A CA  
723  C  C   . PRO A 83  ? 0.1714 0.2339 0.2694 0.1126  0.0520  -0.0111 83  PRO A C   
724  O  O   . PRO A 83  ? 0.2796 0.3582 0.2242 0.0765  0.0096  -0.0174 83  PRO A O   
725  C  CB  . PRO A 83  ? 0.2556 0.2283 0.2310 0.1158  0.0394  0.0043  83  PRO A CB  
726  C  CG  . PRO A 83  ? 0.1896 0.2058 0.1960 0.0423  0.0436  0.0359  83  PRO A CG  
727  C  CD  . PRO A 83  ? 0.1556 0.1561 0.2903 0.0290  0.0795  0.0408  83  PRO A CD  
728  N  N   . LEU A 84  ? 0.1697 0.1606 0.2514 0.0760  0.0749  0.0102  84  LEU A N   
729  C  CA  . LEU A 84  ? 0.1804 0.1532 0.2094 0.0424  0.0517  -0.0219 84  LEU A CA  
730  C  C   . LEU A 84  ? 0.1687 0.1980 0.1795 0.0491  0.0644  -0.0340 84  LEU A C   
731  O  O   . LEU A 84  ? 0.1923 0.2313 0.2642 0.0665  0.1011  -0.0485 84  LEU A O   
732  C  CB  . LEU A 84  ? 0.1100 0.1392 0.2160 0.0385  0.0609  -0.0068 84  LEU A CB  
733  C  CG  . LEU A 84  ? 0.0949 0.1523 0.1958 0.0553  0.0518  0.0004  84  LEU A CG  
734  C  CD1 . LEU A 84  ? 0.1291 0.1681 0.1932 0.0253  0.0392  -0.0168 84  LEU A CD1 
735  C  CD2 . LEU A 84  ? 0.1115 0.1516 0.2175 0.0275  0.0168  -0.0513 84  LEU A CD2 
736  N  N   . ASP A 85  ? 0.2173 0.1688 0.2732 0.0420  0.0639  -0.0399 85  ASP A N   
737  C  CA  . ASP A 85  ? 0.2325 0.1894 0.2784 0.0566  0.0826  -0.0334 85  ASP A CA  
738  C  C   . ASP A 85  ? 0.2021 0.1728 0.3245 0.0243  0.0761  0.0148  85  ASP A C   
739  O  O   . ASP A 85  ? 0.2902 0.2967 0.2714 0.0759  0.0988  -0.0267 85  ASP A O   
740  C  CB  . ASP A 85  ? 0.3272 0.2626 0.2270 0.0517  0.1181  -0.0337 85  ASP A CB  
741  C  CG  . ASP A 85  ? 0.3871 0.3650 0.3445 0.0758  0.2116  0.0971  85  ASP A CG  
742  O  OD1 . ASP A 85  ? 0.4674 0.6593 0.3938 -0.0300 0.2461  0.1132  85  ASP A OD1 
743  O  OD2 . ASP A 85  ? 0.5510 0.3944 0.6089 0.1324  -0.0173 -0.0575 85  ASP A OD2 
744  N  N   . GLY A 86  ? 0.2514 0.2887 0.3650 0.0480  0.0629  0.1195  86  GLY A N   
745  C  CA  . GLY A 86  ? 0.2523 0.2189 0.2776 -0.0416 -0.0002 0.0473  86  GLY A CA  
746  C  C   . GLY A 86  ? 0.1621 0.2254 0.3258 -0.0412 0.0098  0.0186  86  GLY A C   
747  O  O   . GLY A 86  ? 0.3185 0.3095 0.3537 -0.1412 -0.0583 0.1125  86  GLY A O   
748  N  N   A THR A 87  ? 0.1832 0.1496 0.2891 0.0050  0.0330  -0.0273 87  THR A N   
749  N  N   B THR A 87  ? 0.0967 0.1580 0.2757 0.0279  0.0234  -0.0168 87  THR A N   
750  C  CA  A THR A 87  ? 0.1082 0.2232 0.3258 0.0166  0.0100  -0.0588 87  THR A CA  
751  C  CA  B THR A 87  ? 0.0917 0.1545 0.2658 0.0282  0.0317  -0.0196 87  THR A CA  
752  C  C   A THR A 87  ? 0.0881 0.1295 0.3005 -0.0152 0.0018  -0.0342 87  THR A C   
753  C  C   B THR A 87  ? 0.0642 0.1231 0.2422 0.0023  0.0092  -0.0148 87  THR A C   
754  O  O   A THR A 87  ? 0.0840 0.1102 0.3264 0.0025  0.0356  -0.0205 87  THR A O   
755  O  O   B THR A 87  ? 0.0827 0.1142 0.2649 0.0000  0.0452  -0.0198 87  THR A O   
756  C  CB  A THR A 87  ? 0.1244 0.2884 0.3768 0.0403  -0.0315 -0.0737 87  THR A CB  
757  C  CB  B THR A 87  ? 0.0691 0.1524 0.2517 0.0140  0.0248  -0.0386 87  THR A CB  
758  O  OG1 A THR A 87  ? 0.2333 0.2885 0.4425 0.1092  0.0257  -0.0464 87  THR A OG1 
759  O  OG1 B THR A 87  ? 0.1106 0.1482 0.2365 0.0002  0.0044  0.0114  87  THR A OG1 
760  C  CG2 A THR A 87  ? 0.1001 0.3313 0.3882 0.0610  0.0111  -0.1392 87  THR A CG2 
761  C  CG2 B THR A 87  ? 0.0462 0.1654 0.3262 0.0397  0.0369  0.0054  87  THR A CG2 
762  N  N   . TYR A 88  ? 0.0633 0.1210 0.2396 0.0059  0.0131  -0.0195 88  TYR A N   
763  C  CA  . TYR A 88  ? 0.0674 0.1037 0.1881 -0.0121 0.0153  -0.0058 88  TYR A CA  
764  C  C   . TYR A 88  ? 0.0693 0.1369 0.2269 -0.0011 -0.0350 0.0128  88  TYR A C   
765  O  O   . TYR A 88  ? 0.0888 0.2249 0.2463 -0.0525 -0.0381 0.0357  88  TYR A O   
766  C  CB  . TYR A 88  ? 0.1075 0.1130 0.1702 0.0089  0.0113  -0.0074 88  TYR A CB  
767  C  CG  . TYR A 88  ? 0.0866 0.0854 0.1568 0.0058  0.0196  -0.0183 88  TYR A CG  
768  C  CD1 . TYR A 88  ? 0.1183 0.1195 0.1475 0.0185  0.0370  -0.0006 88  TYR A CD1 
769  C  CD2 . TYR A 88  ? 0.0903 0.0800 0.1588 0.0150  0.0062  0.0047  88  TYR A CD2 
770  C  CE1 . TYR A 88  ? 0.1179 0.1245 0.1546 0.0044  0.0435  -0.0060 88  TYR A CE1 
771  C  CE2 . TYR A 88  ? 0.0782 0.0876 0.1432 -0.0026 0.0272  -0.0038 88  TYR A CE2 
772  C  CZ  . TYR A 88  ? 0.1276 0.0982 0.1387 0.0162  0.0238  -0.0236 88  TYR A CZ  
773  O  OH  . TYR A 88  ? 0.1150 0.1372 0.1340 -0.0013 0.0264  -0.0254 88  TYR A OH  
774  N  N   . ARG A 89  ? 0.1040 0.1042 0.1753 0.0012  -0.0127 -0.0257 89  ARG A N   
775  C  CA  . ARG A 89  ? 0.1412 0.0809 0.1665 0.0015  -0.0192 0.0036  89  ARG A CA  
776  C  C   . ARG A 89  ? 0.1208 0.0852 0.1313 -0.0001 -0.0319 0.0172  89  ARG A C   
777  O  O   . ARG A 89  ? 0.1116 0.0854 0.1145 0.0025  -0.0170 0.0047  89  ARG A O   
778  C  CB  . ARG A 89  ? 0.1412 0.1039 0.2091 -0.0111 -0.0512 0.0328  89  ARG A CB  
779  C  CG  . ARG A 89  ? 0.2223 0.1292 0.1861 0.0057  -0.0500 0.0372  89  ARG A CG  
780  C  CD  . ARG A 89  ? 0.2204 0.1367 0.1905 0.0378  -0.0131 0.0435  89  ARG A CD  
781  N  NE  . ARG A 89  ? 0.2350 0.1418 0.2001 0.0273  -0.0223 0.0396  89  ARG A NE  
782  C  CZ  . ARG A 89  ? 0.2149 0.1375 0.1315 0.0186  -0.0143 0.0269  89  ARG A CZ  
783  N  NH1 . ARG A 89  ? 0.2457 0.1515 0.1906 0.0114  0.0196  0.0293  89  ARG A NH1 
784  N  NH2 . ARG A 89  ? 0.2279 0.1492 0.1799 0.0184  0.0268  0.0228  89  ARG A NH2 
785  N  N   . LEU A 90  ? 0.1197 0.0824 0.1540 -0.0165 -0.0348 0.0210  90  LEU A N   
786  C  CA  . LEU A 90  ? 0.1228 0.0908 0.1302 -0.0175 -0.0283 0.0283  90  LEU A CA  
787  C  C   . LEU A 90  ? 0.1421 0.1014 0.1213 -0.0190 -0.0323 0.0302  90  LEU A C   
788  O  O   . LEU A 90  ? 0.1727 0.1423 0.1402 -0.0110 -0.0274 0.0609  90  LEU A O   
789  C  CB  . LEU A 90  ? 0.1531 0.1016 0.1369 -0.0344 -0.0328 0.0167  90  LEU A CB  
790  C  CG  . LEU A 90  ? 0.2034 0.1021 0.1287 -0.0324 -0.0499 0.0083  90  LEU A CG  
791  C  CD1 . LEU A 90  ? 0.2234 0.0992 0.1277 -0.0168 -0.0456 -0.0015 90  LEU A CD1 
792  C  CD2 . LEU A 90  ? 0.2481 0.1515 0.1960 -0.0536 -0.1064 0.0136  90  LEU A CD2 
793  N  N   . THR A 91  ? 0.1543 0.0992 0.0930 -0.0105 -0.0100 0.0066  91  THR A N   
794  C  CA  . THR A 91  ? 0.1559 0.1012 0.1030 -0.0064 0.0097  0.0025  91  THR A CA  
795  C  C   . THR A 91  ? 0.1841 0.0831 0.0864 -0.0105 0.0057  0.0226  91  THR A C   
796  O  O   . THR A 91  ? 0.2442 0.0890 0.0847 -0.0105 -0.0055 0.0249  91  THR A O   
797  C  CB  . THR A 91  ? 0.1806 0.1152 0.1279 -0.0422 -0.0044 0.0207  91  THR A CB  
798  O  OG1 . THR A 91  ? 0.2522 0.2006 0.1489 -0.0900 0.0160  0.0305  91  THR A OG1 
799  C  CG2 . THR A 91  ? 0.1908 0.1356 0.1465 -0.0244 -0.0208 0.0044  91  THR A CG2 
800  N  N   . GLN A 92  ? 0.2255 0.0730 0.0857 -0.0027 -0.0122 0.0122  92  GLN A N   
801  C  CA  . GLN A 92  ? 0.2399 0.0822 0.0895 -0.0016 0.0092  0.0223  92  GLN A CA  
802  C  C   . GLN A 92  ? 0.2046 0.0870 0.0701 -0.0049 0.0071  0.0129  92  GLN A C   
803  O  O   . GLN A 92  ? 0.1963 0.0856 0.0667 0.0040  0.0055  0.0135  92  GLN A O   
804  C  CB  . GLN A 92  ? 0.2518 0.0974 0.1102 -0.0179 0.0304  0.0111  92  GLN A CB  
805  C  CG  . GLN A 92  ? 0.2270 0.1005 0.1491 -0.0111 0.0281  0.0051  92  GLN A CG  
806  C  CD  . GLN A 92  ? 0.2069 0.1332 0.1231 -0.0109 0.0669  0.0076  92  GLN A CD  
807  O  OE1 . GLN A 92  ? 0.3124 0.0982 0.1129 0.0109  -0.0121 0.0167  92  GLN A OE1 
808  N  NE2 . GLN A 92  ? 0.1689 0.1449 0.2152 -0.0116 0.0636  0.0596  92  GLN A NE2 
809  N  N   . PHE A 93  ? 0.2275 0.0809 0.0800 0.0023  -0.0242 0.0124  93  PHE A N   
810  C  CA  . PHE A 93  ? 0.1911 0.0829 0.0754 0.0041  -0.0167 0.0154  93  PHE A CA  
811  C  C   . PHE A 93  ? 0.2284 0.0851 0.0563 -0.0081 -0.0143 0.0115  93  PHE A C   
812  O  O   . PHE A 93  ? 0.2936 0.0999 0.0610 0.0126  -0.0046 0.0089  93  PHE A O   
813  C  CB  . PHE A 93  ? 0.2020 0.1071 0.0942 -0.0108 -0.0502 0.0168  93  PHE A CB  
814  C  CG  . PHE A 93  ? 0.2601 0.0863 0.0913 0.0110  -0.0673 0.0128  93  PHE A CG  
815  C  CD1 . PHE A 93  ? 0.2602 0.0949 0.1050 0.0222  -0.0537 0.0018  93  PHE A CD1 
816  C  CD2 . PHE A 93  ? 0.2512 0.1306 0.0960 0.0198  -0.0824 0.0293  93  PHE A CD2 
817  C  CE1 . PHE A 93  ? 0.3027 0.0964 0.1401 0.0293  -0.0878 -0.0160 93  PHE A CE1 
818  C  CE2 . PHE A 93  ? 0.2709 0.0982 0.1164 0.0044  -0.0885 0.0124  93  PHE A CE2 
819  C  CZ  . PHE A 93  ? 0.3300 0.0924 0.1411 0.0354  -0.0956 0.0121  93  PHE A CZ  
820  N  N   . HIS A 94  ? 0.1914 0.0696 0.0816 0.0036  -0.0122 0.0000  94  HIS A N   
821  C  CA  . HIS A 94  ? 0.1751 0.0942 0.0615 -0.0022 -0.0018 0.0245  94  HIS A CA  
822  C  C   . HIS A 94  ? 0.1636 0.0737 0.0603 -0.0114 -0.0177 0.0006  94  HIS A C   
823  O  O   . HIS A 94  ? 0.1696 0.0888 0.0735 -0.0033 0.0017  0.0161  94  HIS A O   
824  C  CB  . HIS A 94  ? 0.2206 0.0999 0.0642 -0.0282 -0.0059 0.0066  94  HIS A CB  
825  C  CG  . HIS A 94  ? 0.1759 0.0888 0.0614 -0.0334 0.0133  0.0115  94  HIS A CG  
826  N  ND1 . HIS A 94  ? 0.1841 0.0915 0.0685 -0.0288 0.0015  0.0085  94  HIS A ND1 
827  C  CD2 . HIS A 94  ? 0.1382 0.1095 0.0577 -0.0314 0.0255  0.0000  94  HIS A CD2 
828  C  CE1 . HIS A 94  ? 0.1558 0.0949 0.0760 -0.0208 0.0032  0.0263  94  HIS A CE1 
829  N  NE2 . HIS A 94  ? 0.1311 0.0994 0.0522 -0.0265 0.0106  0.0099  94  HIS A NE2 
830  N  N   . PHE A 95  ? 0.1631 0.0793 0.0782 -0.0076 -0.0069 0.0031  95  PHE A N   
831  C  CA  . PHE A 95  ? 0.1146 0.0684 0.0958 -0.0197 0.0053  0.0057  95  PHE A CA  
832  C  C   . PHE A 95  ? 0.1071 0.0852 0.0672 -0.0196 0.0242  -0.0023 95  PHE A C   
833  O  O   . PHE A 95  ? 0.1273 0.1069 0.0861 -0.0317 0.0267  0.0111  95  PHE A O   
834  C  CB  . PHE A 95  ? 0.1222 0.0863 0.1064 -0.0205 -0.0183 -0.0026 95  PHE A CB  
835  C  CG  . PHE A 95  ? 0.1191 0.0890 0.0881 -0.0208 -0.0062 -0.0106 95  PHE A CG  
836  C  CD1 . PHE A 95  ? 0.1584 0.1036 0.0893 -0.0226 -0.0194 -0.0168 95  PHE A CD1 
837  C  CD2 . PHE A 95  ? 0.1146 0.1082 0.1139 -0.0414 0.0108  -0.0355 95  PHE A CD2 
838  C  CE1 . PHE A 95  ? 0.1640 0.1225 0.1007 -0.0183 -0.0214 -0.0290 95  PHE A CE1 
839  C  CE2 . PHE A 95  ? 0.1209 0.1179 0.1176 -0.0259 0.0089  -0.0342 95  PHE A CE2 
840  C  CZ  . PHE A 95  ? 0.1228 0.1385 0.1306 -0.0136 -0.0114 -0.0402 95  PHE A CZ  
841  N  N   . HIS A 96  ? 0.1249 0.0784 0.0678 -0.0018 0.0195  -0.0034 96  HIS A N   
842  C  CA  . HIS A 96  ? 0.1073 0.0789 0.0778 -0.0098 0.0293  0.0071  96  HIS A CA  
843  C  C   . HIS A 96  ? 0.0893 0.0872 0.0567 -0.0109 0.0251  0.0035  96  HIS A C   
844  O  O   . HIS A 96  ? 0.0879 0.0902 0.0802 -0.0140 0.0282  -0.0013 96  HIS A O   
845  C  CB  . HIS A 96  ? 0.1142 0.0867 0.0754 -0.0161 0.0285  -0.0145 96  HIS A CB  
846  C  CG  . HIS A 96  ? 0.0814 0.0955 0.0750 -0.0083 0.0195  -0.0109 96  HIS A CG  
847  N  ND1 . HIS A 96  ? 0.0912 0.0958 0.1098 -0.0207 0.0292  -0.0187 96  HIS A ND1 
848  C  CD2 . HIS A 96  ? 0.1150 0.0820 0.0834 -0.0043 0.0179  -0.0184 96  HIS A CD2 
849  C  CE1 . HIS A 96  ? 0.0893 0.0912 0.1091 -0.0064 0.0392  -0.0204 96  HIS A CE1 
850  N  NE2 . HIS A 96  ? 0.0818 0.1005 0.0820 -0.0147 0.0398  -0.0140 96  HIS A NE2 
851  N  N   . TRP A 97  ? 0.0906 0.0802 0.0723 -0.0100 0.0245  -0.0027 97  TRP A N   
852  C  CA  . TRP A 97  ? 0.0942 0.0796 0.0917 -0.0129 0.0314  -0.0136 97  TRP A CA  
853  C  C   . TRP A 97  ? 0.1025 0.0924 0.0872 -0.0118 0.0337  -0.0173 97  TRP A C   
854  O  O   . TRP A 97  ? 0.1008 0.1048 0.0957 -0.0067 0.0425  -0.0102 97  TRP A O   
855  C  CB  . TRP A 97  ? 0.1259 0.1028 0.0727 -0.0228 0.0236  -0.0048 97  TRP A CB  
856  C  CG  . TRP A 97  ? 0.1177 0.0944 0.0860 -0.0283 0.0303  -0.0075 97  TRP A CG  
857  C  CD1 . TRP A 97  ? 0.1699 0.1132 0.0780 -0.0210 0.0427  -0.0168 97  TRP A CD1 
858  C  CD2 . TRP A 97  ? 0.1417 0.1026 0.0717 -0.0150 0.0270  -0.0057 97  TRP A CD2 
859  N  NE1 . TRP A 97  ? 0.2478 0.1010 0.0852 -0.0277 0.0612  -0.0098 97  TRP A NE1 
860  C  CE2 . TRP A 97  ? 0.1670 0.1009 0.0766 -0.0299 0.0416  -0.0127 97  TRP A CE2 
861  C  CE3 . TRP A 97  ? 0.1505 0.0859 0.0771 -0.0220 0.0190  -0.0083 97  TRP A CE3 
862  C  CZ2 . TRP A 97  ? 0.1967 0.1220 0.0735 -0.0308 0.0403  -0.0053 97  TRP A CZ2 
863  C  CZ3 . TRP A 97  ? 0.1787 0.1098 0.0734 -0.0252 0.0222  0.0043  97  TRP A CZ3 
864  C  CH2 . TRP A 97  ? 0.1969 0.1082 0.0857 -0.0283 0.0292  -0.0039 97  TRP A CH2 
865  N  N   . GLY A 98  ? 0.1260 0.0823 0.0829 -0.0011 0.0293  -0.0168 98  GLY A N   
866  C  CA  . GLY A 98  ? 0.1131 0.1129 0.0895 0.0134  0.0386  -0.0164 98  GLY A CA  
867  C  C   . GLY A 98  ? 0.1287 0.1105 0.1076 -0.0038 0.0435  -0.0252 98  GLY A C   
868  O  O   . GLY A 98  ? 0.1690 0.1046 0.1183 -0.0203 0.0315  -0.0179 98  GLY A O   
869  N  N   . SER A 99  ? 0.1415 0.1042 0.1242 -0.0013 0.0607  -0.0302 99  SER A N   
870  C  CA  . SER A 99  ? 0.1786 0.1129 0.1544 -0.0027 0.0579  -0.0526 99  SER A CA  
871  C  C   . SER A 99  ? 0.1606 0.1197 0.1806 0.0044  0.0290  -0.0548 99  SER A C   
872  O  O   . SER A 99  ? 0.2500 0.1456 0.2062 -0.0211 0.0102  -0.0738 99  SER A O   
873  C  CB  . SER A 99  ? 0.1808 0.1552 0.1824 0.0070  0.0647  -0.0486 99  SER A CB  
874  O  OG  . SER A 99  ? 0.1708 0.1177 0.2094 0.0143  0.0730  -0.0356 99  SER A OG  
875  N  N   . LEU A 100 ? 0.1290 0.1222 0.2102 -0.0178 0.0429  -0.0365 100 LEU A N   
876  C  CA  . LEU A 100 ? 0.1631 0.0921 0.2661 -0.0100 0.0620  -0.0309 100 LEU A CA  
877  C  C   . LEU A 100 ? 0.1444 0.1091 0.1797 -0.0137 0.0118  -0.0329 100 LEU A C   
878  O  O   . LEU A 100 ? 0.1584 0.0981 0.1786 -0.0119 0.0177  -0.0290 100 LEU A O   
879  C  CB  . LEU A 100 ? 0.2250 0.1332 0.4108 0.0559  0.0574  0.0279  100 LEU A CB  
880  C  CG  . LEU A 100 ? 0.2454 0.2413 0.2724 0.0255  0.0736  0.0605  100 LEU A CG  
881  C  CD1 . LEU A 100 ? 0.1511 0.3175 0.3906 0.0642  0.0168  -0.0116 100 LEU A CD1 
882  C  CD2 . LEU A 100 ? 0.3164 0.2978 0.3313 0.0724  0.1671  -0.1173 100 LEU A CD2 
883  N  N   . ASP A 101 ? 0.1258 0.0960 0.2298 -0.0115 0.0283  -0.0291 101 ASP A N   
884  C  CA  . ASP A 101 ? 0.1410 0.1209 0.1781 -0.0174 0.0205  -0.0025 101 ASP A CA  
885  C  C   . ASP A 101 ? 0.1538 0.0956 0.1907 -0.0096 0.0054  0.0022  101 ASP A C   
886  O  O   . ASP A 101 ? 0.1848 0.1313 0.1753 0.0120  0.0143  0.0058  101 ASP A O   
887  C  CB  . ASP A 101 ? 0.1520 0.1263 0.1721 -0.0288 -0.0114 0.0070  101 ASP A CB  
888  C  CG  . ASP A 101 ? 0.1752 0.1638 0.1795 -0.0407 0.0062  -0.0036 101 ASP A CG  
889  O  OD1 . ASP A 101 ? 0.1933 0.1568 0.1956 -0.0388 0.0161  0.0038  101 ASP A OD1 
890  O  OD2 . ASP A 101 ? 0.2420 0.1830 0.1949 -0.0779 -0.0170 0.0067  101 ASP A OD2 
891  N  N   . GLY A 102 ? 0.1716 0.1053 0.2296 -0.0193 -0.0190 0.0318  102 GLY A N   
892  C  CA  . GLY A 102 ? 0.1296 0.1279 0.2309 -0.0418 -0.0041 0.0455  102 GLY A CA  
893  C  C   . GLY A 102 ? 0.1240 0.1107 0.1645 -0.0061 0.0132  0.0258  102 GLY A C   
894  O  O   . GLY A 102 ? 0.1504 0.1432 0.1747 -0.0156 0.0102  0.0352  102 GLY A O   
895  N  N   . GLN A 103 ? 0.1272 0.1044 0.1448 -0.0221 0.0225  0.0116  103 GLN A N   
896  C  CA  . GLN A 103 ? 0.0827 0.0981 0.1200 -0.0087 0.0384  0.0060  103 GLN A CA  
897  C  C   . GLN A 103 ? 0.0832 0.1025 0.0990 -0.0124 0.0473  0.0001  103 GLN A C   
898  O  O   . GLN A 103 ? 0.1211 0.0987 0.1124 -0.0119 0.0285  -0.0039 103 GLN A O   
899  C  CB  . GLN A 103 ? 0.0939 0.1124 0.1249 -0.0010 0.0402  0.0096  103 GLN A CB  
900  C  CG  . GLN A 103 ? 0.1484 0.1152 0.1339 0.0281  0.0590  -0.0131 103 GLN A CG  
901  C  CD  . GLN A 103 ? 0.1836 0.1215 0.1789 0.0521  0.0627  0.0268  103 GLN A CD  
902  O  OE1 . GLN A 103 ? 0.1762 0.1849 0.2080 0.0165  0.0737  0.0248  103 GLN A OE1 
903  N  NE2 . GLN A 103 ? 0.2114 0.2218 0.3045 0.1245  0.1606  0.1337  103 GLN A NE2 
904  N  N   . GLY A 104 ? 0.0624 0.0912 0.1069 0.0082  0.0398  -0.0070 104 GLY A N   
905  C  CA  . GLY A 104 ? 0.0815 0.1041 0.0949 0.0091  0.0222  -0.0013 104 GLY A CA  
906  C  C   . GLY A 104 ? 0.0719 0.0980 0.0928 0.0022  0.0264  0.0017  104 GLY A C   
907  O  O   . GLY A 104 ? 0.0989 0.1052 0.0964 -0.0078 0.0267  -0.0034 104 GLY A O   
908  N  N   . SER A 105 ? 0.0697 0.1015 0.0757 -0.0005 0.0190  -0.0111 105 SER A N   
909  C  CA  . SER A 105 ? 0.0596 0.0944 0.0732 -0.0089 0.0277  -0.0078 105 SER A CA  
910  C  C   . SER A 105 ? 0.0773 0.0811 0.0870 -0.0029 0.0114  0.0005  105 SER A C   
911  O  O   . SER A 105 ? 0.0750 0.1048 0.0926 0.0026  0.0085  -0.0026 105 SER A O   
912  C  CB  . SER A 105 ? 0.0375 0.0933 0.0937 -0.0141 0.0161  0.0117  105 SER A CB  
913  O  OG  . SER A 105 ? 0.0688 0.0839 0.0965 -0.0086 0.0257  0.0055  105 SER A OG  
914  N  N   . GLU A 106 ? 0.0811 0.0841 0.0764 -0.0038 0.0117  -0.0138 106 GLU A N   
915  C  CA  . GLU A 106 ? 0.0633 0.0991 0.0856 -0.0198 0.0277  -0.0179 106 GLU A CA  
916  C  C   . GLU A 106 ? 0.0405 0.0955 0.0886 -0.0048 0.0196  -0.0146 106 GLU A C   
917  O  O   . GLU A 106 ? 0.0534 0.1071 0.0945 0.0044  0.0204  -0.0110 106 GLU A O   
918  C  CB  . GLU A 106 ? 0.0687 0.1052 0.0764 -0.0108 0.0275  -0.0081 106 GLU A CB  
919  C  CG  . GLU A 106 ? 0.1428 0.1043 0.0967 -0.0270 0.0712  -0.0015 106 GLU A CG  
920  C  CD  . GLU A 106 ? 0.0642 0.1087 0.1012 -0.0129 0.0376  -0.0116 106 GLU A CD  
921  O  OE1 . GLU A 106 ? 0.0651 0.1030 0.1252 -0.0153 0.0251  -0.0060 106 GLU A OE1 
922  O  OE2 . GLU A 106 ? 0.0682 0.1336 0.1340 -0.0016 0.0419  -0.0151 106 GLU A OE2 
923  N  N   . HIS A 107 ? 0.0476 0.0893 0.0750 -0.0034 0.0263  -0.0055 107 HIS A N   
924  C  CA  . HIS A 107 ? 0.0472 0.0929 0.0664 0.0039  0.0244  -0.0094 107 HIS A CA  
925  C  C   . HIS A 107 ? 0.0680 0.0886 0.0769 0.0044  0.0149  0.0009  107 HIS A C   
926  O  O   . HIS A 107 ? 0.0554 0.0859 0.0936 -0.0003 0.0125  -0.0020 107 HIS A O   
927  C  CB  . HIS A 107 ? 0.0588 0.0897 0.0739 0.0103  0.0244  -0.0100 107 HIS A CB  
928  C  CG  . HIS A 107 ? 0.0490 0.0857 0.0725 0.0189  0.0162  -0.0074 107 HIS A CG  
929  N  ND1 . HIS A 107 ? 0.0790 0.0815 0.0788 0.0129  0.0057  -0.0003 107 HIS A ND1 
930  C  CD2 . HIS A 107 ? 0.0516 0.0915 0.0730 0.0194  0.0141  -0.0146 107 HIS A CD2 
931  C  CE1 . HIS A 107 ? 0.0502 0.0890 0.0834 0.0107  0.0098  -0.0046 107 HIS A CE1 
932  N  NE2 . HIS A 107 ? 0.0688 0.0947 0.0798 0.0206  0.0065  -0.0171 107 HIS A NE2 
933  N  N   . THR A 108 ? 0.0843 0.0917 0.0827 0.0149  0.0175  0.0063  108 THR A N   
934  C  CA  . THR A 108 ? 0.0766 0.0804 0.0987 0.0126  0.0261  0.0006  108 THR A CA  
935  C  C   . THR A 108 ? 0.0671 0.0945 0.0797 0.0114  0.0006  0.0033  108 THR A C   
936  O  O   . THR A 108 ? 0.0834 0.1003 0.0883 0.0050  0.0137  0.0065  108 THR A O   
937  C  CB  . THR A 108 ? 0.0849 0.1152 0.0922 0.0252  0.0067  0.0000  108 THR A CB  
938  O  OG1 . THR A 108 ? 0.0922 0.1197 0.1031 0.0313  -0.0046 -0.0059 108 THR A OG1 
939  C  CG2 . THR A 108 ? 0.0991 0.1466 0.0961 0.0190  0.0176  0.0070  108 THR A CG2 
940  N  N   . VAL A 109 ? 0.0787 0.1064 0.0927 0.0100  0.0204  0.0157  109 VAL A N   
941  C  CA  . VAL A 109 ? 0.0978 0.1197 0.0974 0.0197  0.0328  0.0263  109 VAL A CA  
942  C  C   . VAL A 109 ? 0.1238 0.1110 0.0935 0.0080  0.0359  0.0150  109 VAL A C   
943  O  O   . VAL A 109 ? 0.0945 0.1154 0.1089 0.0062  0.0245  0.0148  109 VAL A O   
944  C  CB  . VAL A 109 ? 0.0944 0.1218 0.1167 0.0042  0.0232  0.0245  109 VAL A CB  
945  C  CG1 . VAL A 109 ? 0.1204 0.1442 0.1590 0.0214  0.0622  0.0297  109 VAL A CG1 
946  C  CG2 . VAL A 109 ? 0.1028 0.1219 0.1391 0.0158  0.0363  0.0342  109 VAL A CG2 
947  N  N   . ASP A 110 ? 0.1499 0.1152 0.0850 0.0182  0.0251  0.0266  110 ASP A N   
948  C  CA  . ASP A 110 ? 0.1573 0.1055 0.1302 0.0283  0.0288  0.0348  110 ASP A CA  
949  C  C   . ASP A 110 ? 0.1596 0.1036 0.1100 0.0229  0.0075  0.0223  110 ASP A C   
950  O  O   . ASP A 110 ? 0.1971 0.1106 0.1271 0.0313  0.0219  0.0287  110 ASP A O   
951  C  CB  . ASP A 110 ? 0.1940 0.1474 0.1254 0.0228  0.0709  0.0500  110 ASP A CB  
952  C  CG  . ASP A 110 ? 0.2253 0.1590 0.0996 0.0216  0.0318  0.0266  110 ASP A CG  
953  O  OD1 . ASP A 110 ? 0.2362 0.1539 0.1393 0.0354  0.0665  0.0265  110 ASP A OD1 
954  O  OD2 . ASP A 110 ? 0.2429 0.2207 0.1804 0.0463  0.0601  0.0449  110 ASP A OD2 
955  N  N   . LYS A 111 ? 0.1019 0.1410 0.1166 0.0299  0.0079  0.0217  111 LYS A N   
956  C  CA  . LYS A 111 ? 0.0987 0.1324 0.1346 0.0433  0.0105  0.0267  111 LYS A CA  
957  C  C   . LYS A 111 ? 0.1414 0.1212 0.1167 0.0263  0.0271  0.0136  111 LYS A C   
958  O  O   . LYS A 111 ? 0.1277 0.1481 0.1326 0.0318  0.0315  -0.0032 111 LYS A O   
959  C  CB  . LYS A 111 ? 0.1606 0.1699 0.1559 0.0832  -0.0083 0.0146  111 LYS A CB  
960  C  CG  . LYS A 111 ? 0.2269 0.2464 0.1699 0.1038  -0.0372 0.0083  111 LYS A CG  
961  C  CD  . LYS A 111 ? 0.2141 0.3273 0.2516 0.0593  -0.0351 -0.0351 111 LYS A CD  
962  C  CE  . LYS A 111 ? 0.2785 0.3759 0.2305 0.1059  -0.0585 -0.0369 111 LYS A CE  
963  N  NZ  . LYS A 111 ? 0.1632 0.3785 0.3963 -0.0043 -0.0143 0.1576  111 LYS A NZ  
964  N  N   . LYS A 112 ? 0.1366 0.0944 0.1076 0.0140  0.0022  0.0194  112 LYS A N   
965  C  CA  . LYS A 112 ? 0.1333 0.1279 0.0983 -0.0004 0.0186  0.0142  112 LYS A CA  
966  C  C   . LYS A 112 ? 0.1028 0.1012 0.1123 0.0263  0.0027  0.0088  112 LYS A C   
967  O  O   . LYS A 112 ? 0.0872 0.0965 0.1091 0.0055  0.0062  -0.0009 112 LYS A O   
968  C  CB  . LYS A 112 ? 0.1298 0.1360 0.1340 -0.0041 0.0142  -0.0108 112 LYS A CB  
969  C  CG  . LYS A 112 ? 0.1062 0.1813 0.1552 -0.0151 0.0129  -0.0290 112 LYS A CG  
970  C  CD  . LYS A 112 ? 0.1136 0.2614 0.1923 -0.0003 0.0012  0.0009  112 LYS A CD  
971  C  CE  . LYS A 112 ? 0.1326 0.2481 0.2031 -0.0040 -0.0042 0.0027  112 LYS A CE  
972  N  NZ  . LYS A 112 ? 0.2188 0.2181 0.2680 0.0017  -0.0004 0.0774  112 LYS A NZ  
973  N  N   A LYS A 113 ? 0.1107 0.1000 0.1035 0.0153  0.0114  0.0119  113 LYS A N   
974  N  N   B LYS A 113 ? 0.1111 0.1010 0.1024 0.0143  0.0105  0.0109  113 LYS A N   
975  C  CA  A LYS A 113 ? 0.0942 0.1070 0.1091 0.0227  0.0117  0.0209  113 LYS A CA  
976  C  CA  B LYS A 113 ? 0.0982 0.1061 0.1068 0.0215  0.0084  0.0190  113 LYS A CA  
977  C  C   A LYS A 113 ? 0.1134 0.0869 0.1148 0.0002  0.0065  0.0110  113 LYS A C   
978  C  C   B LYS A 113 ? 0.1127 0.0872 0.1142 -0.0003 0.0049  0.0108  113 LYS A C   
979  O  O   A LYS A 113 ? 0.1721 0.0945 0.1551 -0.0118 -0.0307 0.0111  113 LYS A O   
980  O  O   B LYS A 113 ? 0.1713 0.0942 0.1542 -0.0122 -0.0317 0.0122  113 LYS A O   
981  C  CB  A LYS A 113 ? 0.0946 0.1341 0.1129 0.0279  0.0083  0.0004  113 LYS A CB  
982  C  CB  B LYS A 113 ? 0.1014 0.1373 0.0985 0.0217  0.0072  -0.0063 113 LYS A CB  
983  C  CG  A LYS A 113 ? 0.0793 0.1378 0.1659 0.0124  0.0023  0.0114  113 LYS A CG  
984  C  CG  B LYS A 113 ? 0.1125 0.1745 0.0936 0.0295  -0.0092 -0.0140 113 LYS A CG  
985  C  CD  A LYS A 113 ? 0.1037 0.1627 0.1541 0.0097  0.0086  -0.0314 113 LYS A CD  
986  C  CD  B LYS A 113 ? 0.0987 0.1470 0.1657 0.0241  -0.0146 -0.0225 113 LYS A CD  
987  C  CE  A LYS A 113 ? 0.0866 0.1867 0.1760 -0.0069 0.0293  -0.0197 113 LYS A CE  
988  C  CE  B LYS A 113 ? 0.0590 0.2362 0.2102 -0.0016 -0.0043 -0.0021 113 LYS A CE  
989  N  NZ  A LYS A 113 ? 0.0416 0.2503 0.2365 -0.0005 -0.0146 0.0216  113 LYS A NZ  
990  N  NZ  B LYS A 113 ? 0.0725 0.2261 0.2709 0.0034  0.0034  0.0130  113 LYS A NZ  
991  N  N   . TYR A 114 ? 0.0638 0.0972 0.0964 0.0060  0.0185  0.0100  114 TYR A N   
992  C  CA  . TYR A 114 ? 0.0644 0.1003 0.0969 0.0032  0.0106  0.0071  114 TYR A CA  
993  C  C   . TYR A 114 ? 0.0755 0.0773 0.1018 -0.0040 0.0080  0.0052  114 TYR A C   
994  O  O   . TYR A 114 ? 0.0752 0.0987 0.1007 -0.0062 0.0127  -0.0060 114 TYR A O   
995  C  CB  . TYR A 114 ? 0.0466 0.1043 0.1008 0.0001  0.0236  -0.0015 114 TYR A CB  
996  C  CG  . TYR A 114 ? 0.0502 0.0908 0.1102 0.0132  0.0262  0.0140  114 TYR A CG  
997  C  CD1 . TYR A 114 ? 0.1100 0.1100 0.1133 0.0209  0.0298  -0.0016 114 TYR A CD1 
998  C  CD2 . TYR A 114 ? 0.0567 0.1028 0.1733 -0.0058 0.0372  0.0348  114 TYR A CD2 
999  C  CE1 . TYR A 114 ? 0.1791 0.1263 0.1186 0.0346  0.0579  0.0179  114 TYR A CE1 
1000 C  CE2 . TYR A 114 ? 0.1357 0.1465 0.1830 -0.0073 0.0828  0.0252  114 TYR A CE2 
1001 C  CZ  . TYR A 114 ? 0.1662 0.1594 0.1547 0.0154  0.0785  0.0192  114 TYR A CZ  
1002 O  OH  . TYR A 114 ? 0.2021 0.2596 0.1996 0.0140  0.1187  0.0298  114 TYR A OH  
1003 N  N   . ALA A 115 ? 0.0965 0.0807 0.0906 -0.0204 0.0055  0.0037  115 ALA A N   
1004 C  CA  . ALA A 115 ? 0.1053 0.0719 0.0924 -0.0151 0.0106  -0.0070 115 ALA A CA  
1005 C  C   . ALA A 115 ? 0.0957 0.0782 0.0868 -0.0097 0.0150  -0.0064 115 ALA A C   
1006 O  O   . ALA A 115 ? 0.1115 0.0852 0.1001 -0.0071 0.0231  -0.0089 115 ALA A O   
1007 C  CB  . ALA A 115 ? 0.1148 0.1024 0.1048 -0.0033 -0.0055 -0.0199 115 ALA A CB  
1008 N  N   . ALA A 116 ? 0.1134 0.0602 0.0822 -0.0049 0.0011  -0.0044 116 ALA A N   
1009 C  CA  . ALA A 116 ? 0.1093 0.0735 0.0772 -0.0059 0.0175  0.0030  116 ALA A CA  
1010 C  C   . ALA A 116 ? 0.0741 0.0757 0.0791 -0.0065 0.0076  0.0011  116 ALA A C   
1011 O  O   . ALA A 116 ? 0.0782 0.0868 0.0825 -0.0107 0.0133  0.0029  116 ALA A O   
1012 C  CB  . ALA A 116 ? 0.0996 0.1127 0.0834 -0.0031 0.0097  -0.0018 116 ALA A CB  
1013 N  N   . GLU A 117 ? 0.0904 0.0719 0.0845 -0.0015 0.0137  -0.0018 117 GLU A N   
1014 C  CA  . GLU A 117 ? 0.0847 0.0751 0.0651 -0.0004 0.0061  -0.0006 117 GLU A CA  
1015 C  C   . GLU A 117 ? 0.0782 0.0791 0.0605 -0.0059 0.0212  0.0006  117 GLU A C   
1016 O  O   . GLU A 117 ? 0.0829 0.1051 0.0935 -0.0032 0.0377  0.0176  117 GLU A O   
1017 C  CB  . GLU A 117 ? 0.0667 0.0969 0.0656 -0.0040 0.0126  -0.0027 117 GLU A CB  
1018 C  CG  . GLU A 117 ? 0.0845 0.1067 0.0730 0.0042  0.0035  -0.0067 117 GLU A CG  
1019 C  CD  . GLU A 117 ? 0.0640 0.0884 0.0804 -0.0051 0.0085  0.0054  117 GLU A CD  
1020 O  OE1 . GLU A 117 ? 0.0582 0.1143 0.0974 0.0029  0.0046  0.0025  117 GLU A OE1 
1021 O  OE2 . GLU A 117 ? 0.1115 0.1021 0.0785 -0.0100 -0.0096 -0.0004 117 GLU A OE2 
1022 N  N   . LEU A 118 ? 0.0877 0.0732 0.0759 0.0071  0.0055  0.0002  118 LEU A N   
1023 C  CA  . LEU A 118 ? 0.1082 0.0667 0.0859 0.0055  -0.0053 0.0026  118 LEU A CA  
1024 C  C   . LEU A 118 ? 0.0872 0.0811 0.0660 -0.0048 0.0037  0.0096  118 LEU A C   
1025 O  O   . LEU A 118 ? 0.0726 0.0834 0.0700 -0.0076 0.0138  0.0082  118 LEU A O   
1026 C  CB  . LEU A 118 ? 0.1088 0.0746 0.1086 -0.0006 -0.0168 0.0073  118 LEU A CB  
1027 C  CG  . LEU A 118 ? 0.1371 0.0858 0.1112 0.0150  -0.0308 0.0088  118 LEU A CG  
1028 C  CD1 . LEU A 118 ? 0.1386 0.0885 0.1289 0.0000  -0.0514 0.0329  118 LEU A CD1 
1029 C  CD2 . LEU A 118 ? 0.1383 0.1366 0.1397 0.0179  -0.0547 -0.0136 118 LEU A CD2 
1030 N  N   . HIS A 119 ? 0.0845 0.0656 0.0676 -0.0049 -0.0035 0.0072  119 HIS A N   
1031 C  CA  . HIS A 119 ? 0.0839 0.0710 0.0770 -0.0052 0.0024  -0.0002 119 HIS A CA  
1032 C  C   . HIS A 119 ? 0.0994 0.0764 0.0613 -0.0120 -0.0021 0.0026  119 HIS A C   
1033 O  O   . HIS A 119 ? 0.1234 0.0952 0.0617 0.0032  0.0079  0.0089  119 HIS A O   
1034 C  CB  . HIS A 119 ? 0.0766 0.0886 0.0852 0.0006  0.0127  0.0026  119 HIS A CB  
1035 C  CG  . HIS A 119 ? 0.0688 0.0908 0.0664 -0.0044 0.0223  0.0025  119 HIS A CG  
1036 N  ND1 . HIS A 119 ? 0.0709 0.0963 0.0727 0.0114  0.0120  -0.0038 119 HIS A ND1 
1037 C  CD2 . HIS A 119 ? 0.0710 0.0752 0.0660 0.0006  0.0139  0.0006  119 HIS A CD2 
1038 C  CE1 . HIS A 119 ? 0.0732 0.0915 0.0688 -0.0153 0.0124  0.0031  119 HIS A CE1 
1039 N  NE2 . HIS A 119 ? 0.0642 0.0924 0.0739 0.0002  0.0100  0.0064  119 HIS A NE2 
1040 N  N   . LEU A 120 ? 0.0813 0.0876 0.0707 0.0040  -0.0039 0.0063  120 LEU A N   
1041 C  CA  . LEU A 120 ? 0.0974 0.0796 0.0815 -0.0079 -0.0152 0.0124  120 LEU A CA  
1042 C  C   . LEU A 120 ? 0.0703 0.0778 0.0793 -0.0027 -0.0049 0.0148  120 LEU A C   
1043 O  O   . LEU A 120 ? 0.0750 0.0791 0.0757 -0.0122 0.0033  0.0050  120 LEU A O   
1044 C  CB  . LEU A 120 ? 0.0946 0.0928 0.1150 -0.0156 -0.0168 -0.0089 120 LEU A CB  
1045 C  CG  . LEU A 120 ? 0.1376 0.0848 0.1125 -0.0234 -0.0484 0.0190  120 LEU A CG  
1046 C  CD1 . LEU A 120 ? 0.1671 0.1277 0.1667 -0.0779 0.0002  -0.0178 120 LEU A CD1 
1047 C  CD2 . LEU A 120 ? 0.1687 0.1346 0.1614 0.0128  -0.0883 -0.0054 120 LEU A CD2 
1048 N  N   . VAL A 121 ? 0.0991 0.0721 0.0823 -0.0086 0.0067  0.0121  121 VAL A N   
1049 C  CA  . VAL A 121 ? 0.0987 0.0685 0.0901 -0.0096 0.0113  0.0030  121 VAL A CA  
1050 C  C   . VAL A 121 ? 0.1046 0.0633 0.0967 -0.0126 -0.0151 0.0029  121 VAL A C   
1051 O  O   . VAL A 121 ? 0.1271 0.0834 0.0920 -0.0025 -0.0107 0.0135  121 VAL A O   
1052 C  CB  . VAL A 121 ? 0.1247 0.0755 0.1054 -0.0230 0.0385  0.0036  121 VAL A CB  
1053 C  CG1 . VAL A 121 ? 0.1073 0.1085 0.1615 -0.0308 0.0308  -0.0074 121 VAL A CG1 
1054 C  CG2 . VAL A 121 ? 0.0940 0.1100 0.1150 -0.0005 0.0407  0.0010  121 VAL A CG2 
1055 N  N   . HIS A 122 ? 0.0763 0.0750 0.0949 -0.0133 -0.0027 -0.0025 122 HIS A N   
1056 C  CA  . HIS A 122 ? 0.0798 0.0697 0.1080 -0.0069 -0.0029 0.0002  122 HIS A CA  
1057 C  C   . HIS A 122 ? 0.1048 0.0764 0.0915 -0.0085 -0.0071 0.0002  122 HIS A C   
1058 O  O   . HIS A 122 ? 0.1071 0.0791 0.1230 -0.0103 -0.0179 0.0069  122 HIS A O   
1059 C  CB  . HIS A 122 ? 0.0875 0.0748 0.1283 -0.0037 0.0129  -0.0052 122 HIS A CB  
1060 C  CG  . HIS A 122 ? 0.0751 0.0849 0.1019 -0.0092 -0.0078 0.0133  122 HIS A CG  
1061 N  ND1 . HIS A 122 ? 0.0732 0.0811 0.1115 -0.0086 0.0050  0.0121  122 HIS A ND1 
1062 C  CD2 . HIS A 122 ? 0.0773 0.1046 0.1222 -0.0201 -0.0093 0.0136  122 HIS A CD2 
1063 C  CE1 . HIS A 122 ? 0.0644 0.1050 0.1419 -0.0102 0.0066  -0.0058 122 HIS A CE1 
1064 N  NE2 . HIS A 122 ? 0.0836 0.1079 0.1550 -0.0234 -0.0234 0.0134  122 HIS A NE2 
1065 N  N   . TRP A 123 ? 0.0903 0.0710 0.1034 -0.0152 -0.0018 0.0002  123 TRP A N   
1066 C  CA  . TRP A 123 ? 0.0917 0.0773 0.0987 -0.0125 0.0003  -0.0063 123 TRP A CA  
1067 C  C   . TRP A 123 ? 0.0656 0.0885 0.1254 -0.0115 -0.0035 -0.0018 123 TRP A C   
1068 O  O   . TRP A 123 ? 0.0649 0.0863 0.1526 -0.0053 -0.0013 -0.0092 123 TRP A O   
1069 C  CB  . TRP A 123 ? 0.1071 0.0989 0.0978 -0.0194 0.0100  0.0115  123 TRP A CB  
1070 C  CG  . TRP A 123 ? 0.1338 0.0850 0.1173 -0.0297 -0.0091 0.0027  123 TRP A CG  
1071 C  CD1 . TRP A 123 ? 0.1785 0.1028 0.1119 -0.0265 -0.0287 0.0097  123 TRP A CD1 
1072 C  CD2 . TRP A 123 ? 0.1909 0.0872 0.0931 -0.0258 -0.0083 0.0100  123 TRP A CD2 
1073 N  NE1 . TRP A 123 ? 0.2124 0.0869 0.1353 -0.0160 -0.0458 0.0065  123 TRP A NE1 
1074 C  CE2 . TRP A 123 ? 0.2064 0.0894 0.1328 -0.0188 -0.0379 0.0128  123 TRP A CE2 
1075 C  CE3 . TRP A 123 ? 0.1804 0.0719 0.1347 -0.0430 0.0059  0.0032  123 TRP A CE3 
1076 C  CZ2 . TRP A 123 ? 0.2824 0.0901 0.1480 -0.0144 -0.0392 0.0189  123 TRP A CZ2 
1077 C  CZ3 . TRP A 123 ? 0.2954 0.0785 0.1654 -0.0521 -0.0362 0.0232  123 TRP A CZ3 
1078 C  CH2 . TRP A 123 ? 0.2648 0.0780 0.1771 -0.0128 -0.0269 0.0097  123 TRP A CH2 
1079 N  N   . ASN A 124 ? 0.0700 0.0820 0.1073 -0.0068 0.0033  -0.0119 124 ASN A N   
1080 C  CA  . ASN A 124 ? 0.1001 0.0721 0.1270 0.0042  0.0044  -0.0250 124 ASN A CA  
1081 C  C   . ASN A 124 ? 0.1059 0.0797 0.1204 -0.0020 0.0067  -0.0212 124 ASN A C   
1082 O  O   . ASN A 124 ? 0.0992 0.0809 0.1219 -0.0005 0.0140  -0.0139 124 ASN A O   
1083 C  CB  . ASN A 124 ? 0.1112 0.1023 0.1148 -0.0071 0.0167  -0.0160 124 ASN A CB  
1084 C  CG  . ASN A 124 ? 0.1476 0.0888 0.1430 -0.0088 0.0412  -0.0108 124 ASN A CG  
1085 O  OD1 . ASN A 124 ? 0.1444 0.1071 0.1549 0.0032  0.0343  -0.0255 124 ASN A OD1 
1086 N  ND2 . ASN A 124 ? 0.1794 0.1246 0.1458 -0.0042 0.0114  -0.0138 124 ASN A ND2 
1087 N  N   . THR A 125 ? 0.1142 0.0872 0.1446 0.0170  0.0110  -0.0146 125 THR A N   
1088 C  CA  . THR A 125 ? 0.1120 0.0897 0.1966 0.0005  -0.0223 0.0013  125 THR A CA  
1089 C  C   . THR A 125 ? 0.1249 0.0963 0.1676 0.0195  0.0088  -0.0152 125 THR A C   
1090 O  O   . THR A 125 ? 0.1371 0.1073 0.1822 0.0241  -0.0043 0.0072  125 THR A O   
1091 C  CB  . THR A 125 ? 0.1276 0.1534 0.2261 0.0022  -0.0594 0.0087  125 THR A CB  
1092 O  OG1 . THR A 125 ? 0.1394 0.1600 0.3112 0.0479  0.0122  -0.0011 125 THR A OG1 
1093 C  CG2 . THR A 125 ? 0.1876 0.1653 0.3172 -0.0337 -0.0983 -0.0105 125 THR A CG2 
1094 N  N   A LYS A 126 ? 0.1064 0.0878 0.1582 0.0168  0.0427  -0.0310 127 LYS A N   
1095 N  N   B LYS A 126 ? 0.1384 0.0807 0.1710 0.0210  0.0477  -0.0407 127 LYS A N   
1096 C  CA  A LYS A 126 ? 0.1402 0.1399 0.1651 -0.0222 0.0461  -0.0571 127 LYS A CA  
1097 C  CA  B LYS A 126 ? 0.1573 0.1121 0.1430 -0.0050 0.0513  -0.0440 127 LYS A CA  
1098 C  C   A LYS A 126 ? 0.1337 0.0847 0.1633 -0.0050 0.0350  -0.0263 127 LYS A C   
1099 C  C   B LYS A 126 ? 0.1446 0.0732 0.1693 0.0050  0.0347  -0.0197 127 LYS A C   
1100 O  O   A LYS A 126 ? 0.1558 0.1120 0.1922 -0.0237 0.0507  -0.0537 127 LYS A O   
1101 O  O   B LYS A 126 ? 0.1741 0.1025 0.2244 -0.0198 0.0516  -0.0500 127 LYS A O   
1102 C  CB  A LYS A 126 ? 0.1770 0.1819 0.1775 -0.0222 0.0133  -0.0079 127 LYS A CB  
1103 C  CB  B LYS A 126 ? 0.2764 0.1181 0.1488 -0.0343 0.0294  -0.0383 127 LYS A CB  
1104 C  CG  A LYS A 126 ? 0.1543 0.1883 0.1825 -0.0080 -0.0080 -0.0489 127 LYS A CG  
1105 C  CG  B LYS A 126 ? 0.2816 0.1906 0.1289 -0.0064 0.0488  -0.0186 127 LYS A CG  
1106 C  CD  A LYS A 126 ? 0.2096 0.2743 0.2058 0.0440  0.0261  -0.0278 127 LYS A CD  
1107 C  CD  B LYS A 126 ? 0.3520 0.1599 0.1452 0.0460  0.0179  0.0019  127 LYS A CD  
1108 C  CE  A LYS A 126 ? 0.0989 0.2309 0.2409 0.0141  0.0295  -0.0429 127 LYS A CE  
1109 C  CE  B LYS A 126 ? 0.4211 0.3483 0.1218 -0.0589 0.0867  -0.0653 127 LYS A CE  
1110 N  NZ  A LYS A 126 ? 0.3684 0.4397 0.1812 0.0553  0.0256  0.0622  127 LYS A NZ  
1111 N  NZ  B LYS A 126 ? 0.5323 0.4594 0.3914 0.0535  0.0500  0.0092  127 LYS A NZ  
1112 N  N   . TYR A 127 ? 0.1100 0.0854 0.1161 -0.0001 0.0105  -0.0118 128 TYR A N   
1113 C  CA  . TYR A 127 ? 0.1097 0.1091 0.1326 0.0067  0.0100  -0.0048 128 TYR A CA  
1114 C  C   . TYR A 127 ? 0.1204 0.0872 0.1349 -0.0080 0.0177  -0.0172 128 TYR A C   
1115 O  O   . TYR A 127 ? 0.1221 0.1122 0.1517 -0.0122 0.0165  0.0047  128 TYR A O   
1116 C  CB  . TYR A 127 ? 0.1106 0.1009 0.1475 0.0106  0.0164  -0.0143 128 TYR A CB  
1117 C  CG  . TYR A 127 ? 0.1278 0.0982 0.1354 0.0171  0.0006  -0.0199 128 TYR A CG  
1118 C  CD1 . TYR A 127 ? 0.1550 0.1030 0.1424 0.0228  -0.0200 -0.0167 128 TYR A CD1 
1119 C  CD2 . TYR A 127 ? 0.1102 0.1005 0.1367 0.0076  0.0148  -0.0159 128 TYR A CD2 
1120 C  CE1 . TYR A 127 ? 0.1651 0.1481 0.1336 0.0059  -0.0117 -0.0326 128 TYR A CE1 
1121 C  CE2 . TYR A 127 ? 0.1116 0.1316 0.1264 0.0107  0.0198  -0.0322 128 TYR A CE2 
1122 C  CZ  . TYR A 127 ? 0.1454 0.1391 0.1361 0.0245  0.0046  -0.0379 128 TYR A CZ  
1123 O  OH  . TYR A 127 ? 0.2059 0.1749 0.1259 0.0443  -0.0043 -0.0430 128 TYR A OH  
1124 N  N   . GLY A 128 ? 0.1280 0.0888 0.1224 0.0079  0.0024  0.0000  129 GLY A N   
1125 C  CA  . GLY A 128 ? 0.1841 0.1275 0.1152 -0.0055 0.0266  0.0110  129 GLY A CA  
1126 C  C   . GLY A 128 ? 0.1490 0.1173 0.1131 -0.0081 0.0184  0.0164  129 GLY A C   
1127 O  O   . GLY A 128 ? 0.2261 0.1314 0.1230 -0.0051 -0.0024 0.0155  129 GLY A O   
1128 N  N   A ASP A 129 ? 0.2142 0.1252 0.1378 0.0433  0.0301  0.0148  130 ASP A N   
1129 N  N   B ASP A 129 ? 0.1995 0.1120 0.0999 0.0146  0.0414  0.0089  130 ASP A N   
1130 C  CA  A ASP A 129 ? 0.2701 0.1147 0.0957 0.0339  0.0567  0.0482  130 ASP A CA  
1131 C  CA  B ASP A 129 ? 0.1738 0.1321 0.1043 0.0201  0.0591  0.0015  130 ASP A CA  
1132 C  C   A ASP A 129 ? 0.2716 0.1215 0.1027 0.0458  0.0070  0.0321  130 ASP A C   
1133 C  C   B ASP A 129 ? 0.2406 0.1523 0.0795 0.0440  0.0587  0.0147  130 ASP A C   
1134 O  O   A ASP A 129 ? 0.2470 0.1523 0.0881 0.0252  0.0712  0.0555  130 ASP A O   
1135 O  O   B ASP A 129 ? 0.2385 0.1317 0.0806 0.0567  0.0675  0.0108  130 ASP A O   
1136 C  CB  A ASP A 129 ? 0.2079 0.1428 0.0884 0.0502  0.0308  0.0513  130 ASP A CB  
1137 C  CB  B ASP A 129 ? 0.1017 0.1846 0.1435 -0.0127 0.0501  0.0287  130 ASP A CB  
1138 C  CG  A ASP A 129 ? 0.1791 0.1992 0.1050 0.0775  0.0650  0.0269  130 ASP A CG  
1139 C  CG  B ASP A 129 ? 0.1078 0.1247 0.1563 -0.0134 0.0521  0.0018  130 ASP A CG  
1140 O  OD1 A ASP A 129 ? 0.2285 0.2084 0.1522 0.0877  0.0096  0.0508  130 ASP A OD1 
1141 O  OD1 B ASP A 129 ? 0.1303 0.1647 0.2242 -0.0190 0.0193  0.0355  130 ASP A OD1 
1142 O  OD2 A ASP A 129 ? 0.1493 0.2403 0.2504 0.0196  0.0043  0.0926  130 ASP A OD2 
1143 O  OD2 B ASP A 129 ? 0.1555 0.1697 0.1735 -0.0133 0.0827  0.0155  130 ASP A OD2 
1144 N  N   . ALA A 130 ? 0.3180 0.1294 0.1123 0.0586  0.0630  0.0143  131 ALA A N   
1145 C  CA  . ALA A 130 ? 0.2386 0.1393 0.1170 0.0465  0.0468  0.0110  131 ALA A CA  
1146 C  C   . ALA A 130 ? 0.2257 0.1235 0.1156 0.0176  0.0571  0.0013  131 ALA A C   
1147 O  O   . ALA A 130 ? 0.1849 0.1420 0.1046 -0.0068 0.0469  -0.0026 131 ALA A O   
1148 C  CB  . ALA A 130 ? 0.2788 0.1419 0.1761 0.0050  0.1041  -0.0147 131 ALA A CB  
1149 N  N   . GLY A 131 ? 0.2685 0.1477 0.1341 0.0208  0.0856  0.0200  132 GLY A N   
1150 C  CA  . GLY A 131 ? 0.2377 0.1747 0.1925 0.0254  0.1230  0.0351  132 GLY A CA  
1151 C  C   . GLY A 131 ? 0.1790 0.1242 0.2202 -0.0223 0.1056  0.0380  132 GLY A C   
1152 O  O   . GLY A 131 ? 0.2085 0.1701 0.2821 0.0276  0.1100  0.0249  132 GLY A O   
1153 N  N   . LYS A 132 ? 0.1827 0.1251 0.2292 -0.0058 0.1184  0.0466  133 LYS A N   
1154 C  CA  . LYS A 132 ? 0.1507 0.1274 0.2329 -0.0029 0.0842  0.0268  133 LYS A CA  
1155 C  C   . LYS A 132 ? 0.1432 0.0985 0.1935 -0.0137 0.0489  -0.0055 133 LYS A C   
1156 O  O   . LYS A 132 ? 0.1134 0.1376 0.2149 -0.0358 0.0359  -0.0115 133 LYS A O   
1157 C  CB  . LYS A 132 ? 0.1595 0.1398 0.2428 0.0094  0.0535  0.0106  133 LYS A CB  
1158 C  CG  . LYS A 132 ? 0.3570 0.1473 0.5236 -0.0197 0.0432  0.1271  133 LYS A CG  
1159 C  CD  . LYS A 132 ? 0.2966 0.5576 0.5474 0.0489  -0.0583 -0.0228 133 LYS A CD  
1160 C  CE  . LYS A 132 ? 0.2819 0.5820 0.7282 -0.1153 -0.1852 -0.0293 133 LYS A CE  
1161 N  NZ  . LYS A 132 ? 0.3933 0.8738 1.2417 0.0505  -0.2415 -0.1081 133 LYS A NZ  
1162 N  N   . ALA A 133 ? 0.1373 0.0933 0.1522 -0.0245 0.0535  -0.0094 134 ALA A N   
1163 C  CA  . ALA A 133 ? 0.1129 0.1112 0.1159 -0.0135 0.0245  0.0046  134 ALA A CA  
1164 C  C   . ALA A 133 ? 0.1105 0.1170 0.1240 -0.0144 0.0312  -0.0054 134 ALA A C   
1165 O  O   . ALA A 133 ? 0.1033 0.1549 0.1195 -0.0154 0.0102  0.0025  134 ALA A O   
1166 C  CB  . ALA A 133 ? 0.1314 0.1154 0.0996 -0.0322 0.0192  0.0016  134 ALA A CB  
1167 N  N   A SER A 134 ? 0.1282 0.1095 0.1694 -0.0082 0.0584  -0.0231 135 SER A N   
1168 N  N   B SER A 134 ? 0.1407 0.1193 0.1623 -0.0147 0.0610  -0.0227 135 SER A N   
1169 C  CA  A SER A 134 ? 0.1276 0.1333 0.1625 0.0001  0.0685  -0.0075 135 SER A CA  
1170 C  CA  B SER A 134 ? 0.1488 0.1580 0.1566 0.0009  0.0646  -0.0035 135 SER A CA  
1171 C  C   A SER A 134 ? 0.1000 0.1426 0.1935 0.0027  0.0705  0.0161  135 SER A C   
1172 C  C   B SER A 134 ? 0.1342 0.1476 0.2010 -0.0196 0.0655  0.0215  135 SER A C   
1173 O  O   A SER A 134 ? 0.1289 0.1600 0.2469 0.0332  0.0756  0.0237  135 SER A O   
1174 O  O   B SER A 134 ? 0.1640 0.1611 0.1961 0.0021  0.0638  0.0203  135 SER A O   
1175 C  CB  A SER A 134 ? 0.1257 0.1554 0.1892 0.0410  0.0782  -0.0178 135 SER A CB  
1176 C  CB  B SER A 134 ? 0.2568 0.2071 0.1813 0.0569  0.0930  -0.0099 135 SER A CB  
1177 O  OG  A SER A 134 ? 0.1174 0.1849 0.1551 0.0672  0.1136  0.0021  135 SER A OG  
1178 O  OG  B SER A 134 ? 0.2904 0.2998 0.2821 0.0239  0.0736  0.0252  135 SER A OG  
1179 N  N   . GLN A 135 ? 0.1134 0.1575 0.1864 -0.0350 0.0514  0.0044  136 GLN A N   
1180 C  CA  . GLN A 135 ? 0.0703 0.1824 0.2476 -0.0185 0.0428  0.0066  136 GLN A CA  
1181 C  C   . GLN A 135 ? 0.0872 0.1749 0.2193 -0.0160 0.0010  -0.0121 136 GLN A C   
1182 O  O   . GLN A 135 ? 0.1194 0.2249 0.2554 -0.0538 -0.0436 0.0041  136 GLN A O   
1183 C  CB  . GLN A 135 ? 0.1186 0.2049 0.3010 -0.0631 0.0555  0.0011  136 GLN A CB  
1184 C  CG  . GLN A 135 ? 0.1776 0.2887 0.2997 -0.0480 0.0533  0.1120  136 GLN A CG  
1185 C  CD  . GLN A 135 ? 0.3180 0.4248 0.5287 0.0406  0.0833  0.0914  136 GLN A CD  
1186 O  OE1 . GLN A 135 ? 0.2606 0.5188 0.6308 0.0904  0.0901  0.1936  136 GLN A OE1 
1187 N  NE2 . GLN A 135 ? 0.3514 0.5704 0.5188 0.0445  0.0927  0.0648  136 GLN A NE2 
1188 N  N   . GLN A 136 ? 0.0944 0.1374 0.1571 -0.0080 0.0258  0.0058  137 GLN A N   
1189 C  CA  . GLN A 136 ? 0.1376 0.1417 0.1297 0.0135  0.0029  -0.0242 137 GLN A CA  
1190 C  C   . GLN A 136 ? 0.0818 0.1613 0.1143 0.0020  0.0051  -0.0291 137 GLN A C   
1191 O  O   . GLN A 136 ? 0.1104 0.1332 0.1080 0.0113  -0.0027 -0.0214 137 GLN A O   
1192 C  CB  . GLN A 136 ? 0.1412 0.1373 0.1442 0.0135  -0.0032 -0.0247 137 GLN A CB  
1193 C  CG  . GLN A 136 ? 0.2093 0.1861 0.1254 0.0430  0.0018  0.0001  137 GLN A CG  
1194 C  CD  . GLN A 136 ? 0.1861 0.1906 0.2289 0.0256  0.0114  0.0675  137 GLN A CD  
1195 O  OE1 . GLN A 136 ? 0.2755 0.1599 0.2139 -0.0069 -0.0149 -0.0534 137 GLN A OE1 
1196 N  NE2 . GLN A 136 ? 0.3449 0.2846 0.4101 -0.0129 0.1203  0.1561  137 GLN A NE2 
1197 N  N   A PRO A 137 ? 0.0739 0.1843 0.1100 0.0227  -0.0221 -0.0106 138 PRO A N   
1198 N  N   B PRO A 137 ? 0.1306 0.1545 0.1146 0.0059  -0.0187 -0.0472 138 PRO A N   
1199 C  CA  A PRO A 137 ? 0.1490 0.1937 0.0933 0.0178  -0.0228 0.0049  138 PRO A CA  
1200 C  CA  B PRO A 137 ? 0.1511 0.1749 0.1258 0.0278  -0.0217 -0.0051 138 PRO A CA  
1201 C  C   A PRO A 137 ? 0.1405 0.1975 0.0730 0.0269  0.0062  0.0057  138 PRO A C   
1202 C  C   B PRO A 137 ? 0.1379 0.1912 0.0863 0.0265  0.0120  0.0110  138 PRO A C   
1203 O  O   A PRO A 137 ? 0.1544 0.1894 0.1461 0.0326  0.0193  0.0289  138 PRO A O   
1204 O  O   B PRO A 137 ? 0.1504 0.1736 0.1751 0.0510  0.0102  0.0341  138 PRO A O   
1205 C  CB  A PRO A 137 ? 0.2127 0.2439 0.0931 0.0549  -0.0274 -0.0440 138 PRO A CB  
1206 C  CB  B PRO A 137 ? 0.1365 0.2709 0.1251 0.0283  -0.0292 -0.0188 138 PRO A CB  
1207 C  CG  A PRO A 137 ? 0.1219 0.2670 0.1005 0.0548  -0.0168 -0.0702 138 PRO A CG  
1208 C  CG  B PRO A 137 ? 0.1650 0.2643 0.1507 0.0152  -0.0285 -0.0350 138 PRO A CG  
1209 C  CD  A PRO A 137 ? 0.0938 0.2526 0.1411 0.0080  -0.0077 -0.0574 138 PRO A CD  
1210 C  CD  B PRO A 137 ? 0.0987 0.2117 0.1447 0.0079  -0.0554 -0.0598 138 PRO A CD  
1211 N  N   . ASP A 138 ? 0.1150 0.1527 0.1007 0.0021  0.0008  -0.0111 139 ASP A N   
1212 C  CA  . ASP A 138 ? 0.1086 0.1743 0.0910 -0.0006 0.0130  0.0069  139 ASP A CA  
1213 C  C   . ASP A 138 ? 0.1003 0.1345 0.0969 -0.0089 0.0088  0.0030  139 ASP A C   
1214 O  O   . ASP A 138 ? 0.1280 0.1480 0.1297 0.0167  0.0021  0.0006  139 ASP A O   
1215 C  CB  . ASP A 138 ? 0.1790 0.2051 0.0930 0.0197  0.0367  0.0003  139 ASP A CB  
1216 C  CG  . ASP A 138 ? 0.1553 0.2225 0.1112 0.0305  0.0153  -0.0201 139 ASP A CG  
1217 O  OD1 . ASP A 138 ? 0.1945 0.1503 0.1407 0.0328  0.0040  -0.0329 139 ASP A OD1 
1218 O  OD2 . ASP A 138 ? 0.1755 0.2570 0.1841 0.0264  0.0355  -0.0627 139 ASP A OD2 
1219 N  N   . GLY A 139 ? 0.0904 0.1133 0.0806 -0.0151 0.0072  -0.0107 140 GLY A N   
1220 C  CA  . GLY A 139 ? 0.0939 0.1186 0.0888 -0.0201 0.0013  -0.0021 140 GLY A CA  
1221 C  C   . GLY A 139 ? 0.0651 0.0902 0.0716 -0.0038 0.0173  0.0025  140 GLY A C   
1222 O  O   . GLY A 139 ? 0.0915 0.0879 0.0841 0.0100  0.0039  -0.0030 140 GLY A O   
1223 N  N   . LEU A 140 ? 0.0682 0.0860 0.0895 -0.0065 0.0083  -0.0079 141 LEU A N   
1224 C  CA  . LEU A 140 ? 0.0599 0.0739 0.0966 -0.0008 0.0122  -0.0138 141 LEU A CA  
1225 C  C   . LEU A 140 ? 0.0649 0.0696 0.0954 0.0092  0.0020  -0.0019 141 LEU A C   
1226 O  O   . LEU A 140 ? 0.0802 0.0825 0.0987 0.0033  -0.0010 0.0054  141 LEU A O   
1227 C  CB  . LEU A 140 ? 0.0825 0.0929 0.1017 0.0083  0.0211  -0.0120 141 LEU A CB  
1228 C  CG  . LEU A 140 ? 0.0863 0.1046 0.1442 0.0201  0.0374  -0.0026 141 LEU A CG  
1229 C  CD1 . LEU A 140 ? 0.1240 0.1369 0.1219 0.0309  0.0394  -0.0153 141 LEU A CD1 
1230 C  CD2 . LEU A 140 ? 0.1231 0.1262 0.1240 0.0095  0.0373  0.0115  141 LEU A CD2 
1231 N  N   . ALA A 141 ? 0.0842 0.0648 0.1102 -0.0111 -0.0019 -0.0107 142 ALA A N   
1232 C  CA  . ALA A 141 ? 0.0707 0.0746 0.1050 -0.0093 0.0075  -0.0073 142 ALA A CA  
1233 C  C   . ALA A 141 ? 0.0451 0.0901 0.0852 -0.0089 0.0030  -0.0001 142 ALA A C   
1234 O  O   . ALA A 141 ? 0.0847 0.0849 0.0976 -0.0119 -0.0067 0.0110  142 ALA A O   
1235 C  CB  . ALA A 141 ? 0.0802 0.1012 0.1308 -0.0026 0.0219  0.0063  142 ALA A CB  
1236 N  N   . VAL A 142 ? 0.0646 0.0832 0.0917 0.0009  0.0100  -0.0053 143 VAL A N   
1237 C  CA  . VAL A 142 ? 0.0617 0.0842 0.0797 -0.0084 0.0171  -0.0005 143 VAL A CA  
1238 C  C   . VAL A 142 ? 0.0538 0.0798 0.0666 -0.0006 0.0175  0.0000  143 VAL A C   
1239 O  O   . VAL A 142 ? 0.0769 0.0973 0.0697 -0.0005 0.0072  0.0076  143 VAL A O   
1240 C  CB  . VAL A 142 ? 0.0612 0.1130 0.0902 0.0064  0.0139  -0.0020 143 VAL A CB  
1241 C  CG1 . VAL A 142 ? 0.0849 0.1290 0.1012 0.0189  0.0094  -0.0209 143 VAL A CG1 
1242 C  CG2 . VAL A 142 ? 0.0623 0.1660 0.0951 -0.0098 0.0226  0.0158  143 VAL A CG2 
1243 N  N   . LEU A 143 ? 0.0453 0.0833 0.0861 -0.0044 0.0078  0.0089  144 LEU A N   
1244 C  CA  . LEU A 143 ? 0.0576 0.0802 0.0973 -0.0170 -0.0054 -0.0013 144 LEU A CA  
1245 C  C   . LEU A 143 ? 0.0672 0.0838 0.0773 -0.0184 0.0060  0.0070  144 LEU A C   
1246 O  O   . LEU A 143 ? 0.1054 0.0978 0.0825 -0.0129 0.0163  0.0129  144 LEU A O   
1247 C  CB  . LEU A 143 ? 0.0635 0.1349 0.1059 -0.0049 0.0046  0.0250  144 LEU A CB  
1248 C  CG  . LEU A 143 ? 0.0744 0.1465 0.1614 -0.0164 -0.0009 0.0278  144 LEU A CG  
1249 C  CD1 . LEU A 143 ? 0.1012 0.2156 0.1632 -0.0354 -0.0006 0.0544  144 LEU A CD1 
1250 C  CD2 . LEU A 143 ? 0.0572 0.2226 0.1723 -0.0046 -0.0010 0.0251  144 LEU A CD2 
1251 N  N   . GLY A 144 ? 0.0596 0.0757 0.0942 -0.0027 0.0096  0.0111  145 GLY A N   
1252 C  CA  . GLY A 144 ? 0.0525 0.0843 0.0994 -0.0048 0.0121  -0.0055 145 GLY A CA  
1253 C  C   . GLY A 144 ? 0.0610 0.0867 0.0655 -0.0114 0.0078  0.0122  145 GLY A C   
1254 O  O   . GLY A 144 ? 0.0775 0.1017 0.0816 -0.0168 0.0214  -0.0013 145 GLY A O   
1255 N  N   . ILE A 145 ? 0.0436 0.0736 0.0818 -0.0064 0.0020  -0.0020 146 ILE A N   
1256 C  CA  . ILE A 145 ? 0.0357 0.0788 0.1098 -0.0071 -0.0031 -0.0010 146 ILE A CA  
1257 C  C   . ILE A 145 ? 0.0447 0.0775 0.0982 -0.0050 0.0064  0.0093  146 ILE A C   
1258 O  O   . ILE A 145 ? 0.0669 0.0782 0.1010 -0.0126 0.0120  0.0044  146 ILE A O   
1259 C  CB  . ILE A 145 ? 0.0718 0.0863 0.1215 0.0008  -0.0192 0.0099  146 ILE A CB  
1260 C  CG1 . ILE A 145 ? 0.0757 0.1044 0.1594 0.0316  -0.0214 0.0047  146 ILE A CG1 
1261 C  CG2 . ILE A 145 ? 0.0584 0.1168 0.1553 -0.0060 -0.0131 -0.0072 146 ILE A CG2 
1262 C  CD1 . ILE A 145 ? 0.0901 0.1060 0.1634 0.0239  -0.0301 0.0105  146 ILE A CD1 
1263 N  N   . PHE A 146 ? 0.0567 0.0741 0.0892 -0.0003 -0.0032 0.0024  147 PHE A N   
1264 C  CA  . PHE A 146 ? 0.0727 0.0728 0.0800 0.0108  -0.0075 -0.0010 147 PHE A CA  
1265 C  C   . PHE A 146 ? 0.0719 0.0737 0.0947 -0.0125 -0.0033 -0.0077 147 PHE A C   
1266 O  O   . PHE A 146 ? 0.0696 0.1030 0.1177 -0.0037 -0.0060 -0.0131 147 PHE A O   
1267 C  CB  . PHE A 146 ? 0.0692 0.0831 0.0972 -0.0111 -0.0086 0.0159  147 PHE A CB  
1268 C  CG  . PHE A 146 ? 0.0624 0.0723 0.0926 0.0055  -0.0025 -0.0009 147 PHE A CG  
1269 C  CD1 . PHE A 146 ? 0.0578 0.0848 0.1030 0.0058  -0.0026 -0.0030 147 PHE A CD1 
1270 C  CD2 . PHE A 146 ? 0.0847 0.0888 0.0927 0.0051  0.0025  0.0200  147 PHE A CD2 
1271 C  CE1 . PHE A 146 ? 0.0816 0.0974 0.0902 0.0021  0.0065  -0.0042 147 PHE A CE1 
1272 C  CE2 . PHE A 146 ? 0.0741 0.0963 0.1025 -0.0102 0.0144  0.0161  147 PHE A CE2 
1273 C  CZ  . PHE A 146 ? 0.0708 0.0957 0.0969 -0.0084 0.0128  0.0137  147 PHE A CZ  
1274 N  N   . LEU A 147 ? 0.0769 0.0719 0.0872 -0.0069 -0.0015 -0.0023 148 LEU A N   
1275 C  CA  . LEU A 147 ? 0.1031 0.0744 0.0883 -0.0206 -0.0052 -0.0034 148 LEU A CA  
1276 C  C   . LEU A 147 ? 0.0823 0.0829 0.0961 -0.0160 -0.0042 0.0099  148 LEU A C   
1277 O  O   . LEU A 147 ? 0.0734 0.0890 0.1215 -0.0092 0.0030  -0.0013 148 LEU A O   
1278 C  CB  . LEU A 147 ? 0.0969 0.1008 0.0906 -0.0073 -0.0029 0.0053  148 LEU A CB  
1279 C  CG  . LEU A 147 ? 0.1457 0.0818 0.1177 -0.0187 -0.0290 0.0126  148 LEU A CG  
1280 C  CD1 . LEU A 147 ? 0.2157 0.0996 0.1039 -0.0215 -0.0412 -0.0018 148 LEU A CD1 
1281 C  CD2 . LEU A 147 ? 0.1772 0.1266 0.1027 -0.0268 -0.0369 0.0291  148 LEU A CD2 
1282 N  N   . LYS A 148 ? 0.0879 0.0717 0.1165 -0.0201 -0.0064 0.0044  149 LYS A N   
1283 C  CA  . LYS A 148 ? 0.0920 0.0788 0.1244 0.0052  -0.0097 0.0058  149 LYS A CA  
1284 C  C   . LYS A 148 ? 0.1168 0.0834 0.1327 -0.0021 -0.0175 0.0058  149 LYS A C   
1285 O  O   . LYS A 148 ? 0.1350 0.1244 0.1164 0.0261  -0.0328 -0.0089 149 LYS A O   
1286 C  CB  . LYS A 148 ? 0.1261 0.1028 0.1356 -0.0054 0.0084  0.0245  149 LYS A CB  
1287 C  CG  . LYS A 148 ? 0.1240 0.1485 0.1793 -0.0173 0.0241  0.0198  149 LYS A CG  
1288 C  CD  . LYS A 148 ? 0.2083 0.2378 0.2494 -0.0298 0.0442  0.0847  149 LYS A CD  
1289 C  CE  . LYS A 148 ? 0.2649 0.4275 0.3405 -0.1109 0.0582  0.1112  149 LYS A CE  
1290 N  NZ  . LYS A 148 ? 0.3599 0.5089 0.4672 -0.0807 0.1460  0.2242  149 LYS A NZ  
1291 N  N   . VAL A 149 ? 0.1366 0.0793 0.1459 -0.0158 -0.0120 -0.0140 150 VAL A N   
1292 C  CA  . VAL A 149 ? 0.1473 0.0863 0.1364 -0.0103 -0.0084 -0.0080 150 VAL A CA  
1293 C  C   . VAL A 149 ? 0.1533 0.0996 0.1163 -0.0165 -0.0276 0.0024  150 VAL A C   
1294 O  O   . VAL A 149 ? 0.1634 0.1091 0.1449 -0.0066 -0.0204 0.0185  150 VAL A O   
1295 C  CB  . VAL A 149 ? 0.1529 0.0964 0.1416 0.0008  -0.0137 -0.0185 150 VAL A CB  
1296 C  CG1 . VAL A 149 ? 0.1597 0.1645 0.1373 0.0053  -0.0166 -0.0225 150 VAL A CG1 
1297 C  CG2 . VAL A 149 ? 0.1554 0.1587 0.1646 -0.0212 0.0259  -0.0290 150 VAL A CG2 
1298 N  N   . GLY A 150 ? 0.1384 0.0981 0.1314 -0.0184 -0.0208 -0.0029 151 GLY A N   
1299 C  CA  . GLY A 150 ? 0.1469 0.1375 0.1539 -0.0416 -0.0379 0.0148  151 GLY A CA  
1300 C  C   . GLY A 150 ? 0.1311 0.1137 0.1574 -0.0308 -0.0334 0.0018  151 GLY A C   
1301 O  O   . GLY A 150 ? 0.1724 0.1167 0.1702 -0.0314 -0.0248 -0.0025 151 GLY A O   
1302 N  N   A SER A 151 ? 0.1231 0.1226 0.1964 -0.0163 -0.0483 0.0093  152 SER A N   
1303 N  N   B SER A 151 ? 0.1246 0.1268 0.2108 -0.0171 -0.0403 0.0017  152 SER A N   
1304 C  CA  A SER A 151 ? 0.1314 0.1215 0.2492 -0.0071 -0.0749 0.0100  152 SER A CA  
1305 C  CA  B SER A 151 ? 0.1527 0.1209 0.2307 -0.0326 -0.0669 -0.0044 152 SER A CA  
1306 C  C   A SER A 151 ? 0.1628 0.0931 0.1817 0.0043  -0.0567 -0.0251 152 SER A C   
1307 C  C   B SER A 151 ? 0.1633 0.1264 0.1837 -0.0262 -0.0498 -0.0054 152 SER A C   
1308 O  O   A SER A 151 ? 0.1001 0.1300 0.1560 -0.0023 -0.0304 -0.0299 152 SER A O   
1309 O  O   B SER A 151 ? 0.1268 0.1131 0.1381 -0.0181 -0.0100 -0.0110 152 SER A O   
1310 C  CB  A SER A 151 ? 0.1311 0.2442 0.2689 0.0471  -0.0911 0.0023  152 SER A CB  
1311 C  CB  B SER A 151 ? 0.2020 0.1577 0.2635 -0.0574 -0.0074 -0.0381 152 SER A CB  
1312 O  OG  A SER A 151 ? 0.1225 0.2780 0.2776 0.0145  -0.0023 -0.0114 152 SER A OG  
1313 O  OG  B SER A 151 ? 0.1543 0.2685 0.2848 -0.0513 0.0314  0.0529  152 SER A OG  
1314 N  N   . ALA A 152 ? 0.1513 0.1136 0.1751 -0.0080 -0.0554 -0.0182 153 ALA A N   
1315 C  CA  . ALA A 152 ? 0.1908 0.1204 0.1587 -0.0044 -0.0641 -0.0084 153 ALA A CA  
1316 C  C   . ALA A 152 ? 0.1768 0.1186 0.1386 -0.0064 -0.0688 -0.0043 153 ALA A C   
1317 O  O   . ALA A 152 ? 0.1865 0.1195 0.2245 -0.0065 -0.0506 -0.0141 153 ALA A O   
1318 C  CB  . ALA A 152 ? 0.2971 0.1511 0.1439 0.0155  -0.0738 -0.0139 153 ALA A CB  
1319 N  N   . LYS A 153 ? 0.1878 0.0971 0.1707 -0.0006 -0.0893 0.0023  154 LYS A N   
1320 C  CA  . LYS A 153 ? 0.2037 0.1040 0.1696 0.0139  -0.0771 -0.0031 154 LYS A CA  
1321 C  C   . LYS A 153 ? 0.1953 0.1052 0.1545 0.0107  -0.0611 -0.0127 154 LYS A C   
1322 O  O   . LYS A 153 ? 0.1899 0.1337 0.1521 0.0024  -0.0872 -0.0083 154 LYS A O   
1323 C  CB  . LYS A 153 ? 0.2060 0.0999 0.1836 -0.0044 -0.0771 0.0025  154 LYS A CB  
1324 C  CG  . LYS A 153 ? 0.2060 0.1084 0.2492 0.0031  -0.0921 -0.0320 154 LYS A CG  
1325 C  CD  . LYS A 153 ? 0.3087 0.1503 0.2103 0.0061  -0.0394 -0.0196 154 LYS A CD  
1326 C  CE  . LYS A 153 ? 0.2779 0.1432 0.3150 0.0745  -0.1594 -0.0763 154 LYS A CE  
1327 N  NZ  . LYS A 153 ? 0.4376 0.2806 0.4289 0.0438  -0.0096 -0.0424 154 LYS A NZ  
1328 N  N   . PRO A 154 ? 0.2070 0.1201 0.1738 0.0064  -0.0822 -0.0217 155 PRO A N   
1329 C  CA  . PRO A 154 ? 0.2096 0.1395 0.2159 0.0077  -0.1142 0.0156  155 PRO A CA  
1330 C  C   . PRO A 154 ? 0.2209 0.1603 0.1574 0.0113  -0.0989 0.0040  155 PRO A C   
1331 O  O   . PRO A 154 ? 0.2671 0.1731 0.1671 0.0129  -0.1042 0.0102  155 PRO A O   
1332 C  CB  . PRO A 154 ? 0.2009 0.1867 0.2694 0.0381  -0.1248 0.0110  155 PRO A CB  
1333 C  CG  . PRO A 154 ? 0.2294 0.2405 0.2693 0.0313  -0.1177 0.0402  155 PRO A CG  
1334 C  CD  . PRO A 154 ? 0.1886 0.1653 0.1786 0.0100  -0.0568 -0.0038 155 PRO A CD  
1335 N  N   . GLY A 155 ? 0.2579 0.1085 0.1965 0.0331  -0.1087 -0.0023 156 GLY A N   
1336 C  CA  . GLY A 155 ? 0.2699 0.1170 0.2254 0.0124  -0.1005 0.0010  156 GLY A CA  
1337 C  C   . GLY A 155 ? 0.2971 0.0969 0.1722 0.0084  -0.0728 0.0223  156 GLY A C   
1338 O  O   . GLY A 155 ? 0.3100 0.0992 0.3007 0.0164  -0.0769 0.0305  156 GLY A O   
1339 N  N   . LEU A 156 ? 0.2329 0.1293 0.1919 0.0142  -0.0826 -0.0129 157 LEU A N   
1340 C  CA  . LEU A 156 ? 0.2321 0.1079 0.1421 -0.0022 -0.0858 0.0013  157 LEU A CA  
1341 C  C   . LEU A 156 ? 0.2588 0.1258 0.1573 -0.0312 -0.0807 -0.0187 157 LEU A C   
1342 O  O   . LEU A 156 ? 0.2494 0.1316 0.1278 0.0017  -0.0839 -0.0030 157 LEU A O   
1343 C  CB  . LEU A 156 ? 0.2084 0.1274 0.1678 -0.0080 -0.0804 0.0209  157 LEU A CB  
1344 C  CG  . LEU A 156 ? 0.2078 0.1416 0.1482 -0.0091 -0.0644 -0.0008 157 LEU A CG  
1345 C  CD1 . LEU A 156 ? 0.2794 0.1615 0.1576 -0.0591 -0.0710 0.0078  157 LEU A CD1 
1346 C  CD2 . LEU A 156 ? 0.2056 0.1734 0.1532 -0.0196 -0.0504 0.0395  157 LEU A CD2 
1347 N  N   . GLN A 157 ? 0.2724 0.1062 0.1566 -0.0252 -0.0999 -0.0011 158 GLN A N   
1348 C  CA  . GLN A 157 ? 0.3054 0.1569 0.1336 -0.0547 -0.0959 -0.0032 158 GLN A CA  
1349 C  C   . GLN A 157 ? 0.2545 0.1518 0.1417 0.0001  -0.0826 -0.0102 158 GLN A C   
1350 O  O   . GLN A 157 ? 0.2536 0.1405 0.1430 -0.0062 -0.0660 -0.0188 158 GLN A O   
1351 C  CB  . GLN A 157 ? 0.3468 0.1573 0.1703 -0.0524 -0.1072 -0.0277 158 GLN A CB  
1352 C  CG  . GLN A 157 ? 0.3647 0.1591 0.1899 -0.0168 -0.0826 -0.0378 158 GLN A CG  
1353 C  CD  . GLN A 157 ? 0.3653 0.1424 0.1321 -0.0334 -0.1010 -0.0146 158 GLN A CD  
1354 O  OE1 . GLN A 157 ? 0.3512 0.1378 0.1409 -0.0225 -0.0917 -0.0004 158 GLN A OE1 
1355 N  NE2 . GLN A 157 ? 0.4591 0.1571 0.1635 -0.0351 -0.1088 -0.0316 158 GLN A NE2 
1356 N  N   . LYS A 158 ? 0.3149 0.1449 0.1437 0.0137  -0.1165 -0.0021 159 LYS A N   
1357 C  CA  . LYS A 158 ? 0.2635 0.1538 0.1491 0.0201  -0.0985 0.0051  159 LYS A CA  
1358 C  C   . LYS A 158 ? 0.2843 0.1312 0.1494 0.0015  -0.0951 0.0144  159 LYS A C   
1359 O  O   . LYS A 158 ? 0.3106 0.1453 0.1596 -0.0275 -0.0809 0.0082  159 LYS A O   
1360 C  CB  . LYS A 158 ? 0.2795 0.1620 0.1834 0.0212  -0.0603 0.0207  159 LYS A CB  
1361 C  CG  . LYS A 158 ? 0.2900 0.2386 0.2451 -0.0222 -0.0704 0.0099  159 LYS A CG  
1362 N  N   . VAL A 159 ? 0.2628 0.1191 0.1319 0.0187  -0.0789 -0.0105 160 VAL A N   
1363 C  CA  . VAL A 159 ? 0.2693 0.1100 0.1120 -0.0223 -0.0425 0.0064  160 VAL A CA  
1364 C  C   . VAL A 159 ? 0.2491 0.1314 0.1354 0.0092  -0.0672 0.0008  160 VAL A C   
1365 O  O   . VAL A 159 ? 0.2473 0.1302 0.1619 0.0054  -0.0643 -0.0070 160 VAL A O   
1366 C  CB  . VAL A 159 ? 0.2678 0.1129 0.1244 -0.0006 -0.0693 -0.0162 160 VAL A CB  
1367 C  CG1 . VAL A 159 ? 0.2478 0.1809 0.1286 -0.0631 -0.0583 0.0144  160 VAL A CG1 
1368 C  CG2 . VAL A 159 ? 0.3385 0.1439 0.1200 0.0264  -0.0845 -0.0344 160 VAL A CG2 
1369 N  N   . VAL A 160 ? 0.2888 0.1028 0.1120 -0.0085 -0.0500 -0.0079 161 VAL A N   
1370 C  CA  . VAL A 160 ? 0.3148 0.1167 0.1469 0.0252  -0.0527 0.0208  161 VAL A CA  
1371 C  C   . VAL A 160 ? 0.3162 0.0904 0.1539 -0.0047 -0.0361 -0.0099 161 VAL A C   
1372 O  O   . VAL A 160 ? 0.3151 0.1383 0.1597 -0.0226 -0.0348 -0.0217 161 VAL A O   
1373 C  CB  . VAL A 160 ? 0.4850 0.1405 0.1797 0.0364  0.0826  0.0207  161 VAL A CB  
1374 C  CG1 . VAL A 160 ? 0.3991 0.1834 0.2587 -0.0739 -0.0006 -0.0476 161 VAL A CG1 
1375 C  CG2 . VAL A 160 ? 0.5180 0.1467 0.1781 0.0760  0.0750  0.0381  161 VAL A CG2 
1376 N  N   . ASP A 161 ? 0.3453 0.1470 0.1333 -0.0209 -0.0788 -0.0016 162 ASP A N   
1377 C  CA  . ASP A 161 ? 0.3895 0.1802 0.1439 -0.0449 -0.0675 -0.0042 162 ASP A CA  
1378 C  C   . ASP A 161 ? 0.3707 0.1923 0.1346 -0.0507 -0.0725 -0.0215 162 ASP A C   
1379 O  O   . ASP A 161 ? 0.4734 0.3087 0.1481 -0.0829 -0.0387 -0.0098 162 ASP A O   
1380 C  CB  . ASP A 161 ? 0.4487 0.2262 0.1206 -0.0513 -0.0986 -0.0081 162 ASP A CB  
1381 C  CG  . ASP A 161 ? 0.3810 0.2267 0.1596 -0.0253 -0.0055 -0.0274 162 ASP A CG  
1382 O  OD1 . ASP A 161 ? 0.4057 0.3121 0.2613 0.0118  -0.0732 -0.0497 162 ASP A OD1 
1383 O  OD2 . ASP A 161 ? 0.3890 0.3239 0.2780 -0.0006 -0.0904 -0.0507 162 ASP A OD2 
1384 N  N   . VAL A 162 ? 0.4029 0.1731 0.1429 -0.0842 -0.1179 0.0299  163 VAL A N   
1385 C  CA  . VAL A 162 ? 0.4251 0.1739 0.1730 -0.0825 -0.1052 0.0296  163 VAL A CA  
1386 C  C   . VAL A 162 ? 0.4336 0.1869 0.0992 -0.0661 -0.0430 0.0352  163 VAL A C   
1387 O  O   . VAL A 162 ? 0.5140 0.1676 0.0930 -0.0688 -0.0149 0.0125  163 VAL A O   
1388 C  CB  . VAL A 162 ? 0.4765 0.1678 0.2354 -0.0417 -0.0880 0.0326  163 VAL A CB  
1389 C  CG1 . VAL A 162 ? 0.4433 0.1237 0.2494 -0.0425 -0.0895 -0.0015 163 VAL A CG1 
1390 C  CG2 . VAL A 162 ? 0.4080 0.2422 0.2509 0.0287  -0.0011 0.0895  163 VAL A CG2 
1391 N  N   . LEU A 163 ? 0.3860 0.1828 0.1062 -0.0395 -0.0263 0.0231  164 LEU A N   
1392 C  CA  . LEU A 163 ? 0.3727 0.1402 0.0902 -0.0310 0.0168  0.0156  164 LEU A CA  
1393 C  C   . LEU A 163 ? 0.3793 0.1505 0.1161 -0.0370 0.0163  0.0100  164 LEU A C   
1394 O  O   . LEU A 163 ? 0.3850 0.1624 0.1186 -0.0381 0.0511  0.0131  164 LEU A O   
1395 C  CB  . LEU A 163 ? 0.3427 0.1397 0.1042 -0.0106 -0.0003 0.0132  164 LEU A CB  
1396 C  CG  . LEU A 163 ? 0.3093 0.1267 0.0978 -0.0317 0.0037  0.0227  164 LEU A CG  
1397 C  CD1 . LEU A 163 ? 0.3396 0.1484 0.1380 -0.0084 0.0088  0.0446  164 LEU A CD1 
1398 C  CD2 . LEU A 163 ? 0.2904 0.1639 0.0964 -0.0389 -0.0143 0.0083  164 LEU A CD2 
1399 N  N   . ASP A 164 ? 0.4888 0.1502 0.1213 -0.0701 0.0266  -0.0206 165 ASP A N   
1400 C  CA  . ASP A 164 ? 0.6100 0.1763 0.1370 -0.0687 0.0592  -0.0580 165 ASP A CA  
1401 C  C   . ASP A 164 ? 0.5923 0.2143 0.0842 -0.0504 0.0072  0.0005  165 ASP A C   
1402 O  O   . ASP A 164 ? 0.6450 0.2588 0.2836 -0.0778 0.0925  -0.0201 165 ASP A O   
1403 C  CB  . ASP A 164 ? 0.6481 0.2630 0.2088 -0.0996 -0.0005 -0.0854 165 ASP A CB  
1404 C  CG  . ASP A 164 ? 0.7491 0.4779 0.1881 -0.0591 0.0011  -0.0659 165 ASP A CG  
1405 O  OD1 . ASP A 164 ? 0.7149 0.3319 0.2531 -0.1955 -0.0199 -0.0255 165 ASP A OD1 
1406 O  OD2 . ASP A 164 ? 0.8609 0.8340 0.1878 -0.1505 0.1022  -0.1703 165 ASP A OD2 
1407 N  N   . SER A 165 ? 0.5112 0.1912 0.0863 -0.0732 -0.0151 0.0142  166 SER A N   
1408 C  CA  . SER A 165 ? 0.5521 0.2008 0.1023 -0.1062 -0.0201 0.0054  166 SER A CA  
1409 C  C   . SER A 165 ? 0.5110 0.1652 0.1016 -0.0801 0.0017  0.0141  166 SER A C   
1410 O  O   . SER A 165 ? 0.5772 0.1741 0.0816 -0.0908 0.0131  0.0388  166 SER A O   
1411 C  CB  . SER A 165 ? 0.6041 0.2135 0.2411 -0.0658 0.1575  0.0268  166 SER A CB  
1412 O  OG  . SER A 165 ? 0.5554 0.1909 0.1839 -0.0046 0.0210  0.0265  166 SER A OG  
1413 N  N   . ILE A 166 ? 0.4476 0.1759 0.0895 -0.0754 0.0060  0.0001  167 ILE A N   
1414 C  CA  . ILE A 166 ? 0.3260 0.1611 0.1220 -0.0560 0.0390  0.0186  167 ILE A CA  
1415 C  C   . ILE A 166 ? 0.3972 0.1373 0.1054 -0.0374 -0.0111 -0.0084 167 ILE A C   
1416 O  O   . ILE A 166 ? 0.4070 0.1769 0.0892 -0.0791 0.0228  0.0058  167 ILE A O   
1417 C  CB  . ILE A 166 ? 0.4589 0.1488 0.1046 -0.0585 0.0248  -0.0004 167 ILE A CB  
1418 C  CG1 . ILE A 166 ? 0.3098 0.1709 0.1107 -0.0412 0.0033  -0.0102 167 ILE A CG1 
1419 C  CG2 . ILE A 166 ? 0.5123 0.1349 0.1475 -0.0716 -0.0276 0.0223  167 ILE A CG2 
1420 C  CD1 . ILE A 166 ? 0.4022 0.1576 0.1119 -0.0095 0.0024  -0.0132 167 ILE A CD1 
1421 N  N   . LYS A 167 ? 0.3607 0.1462 0.1164 -0.0351 0.0343  0.0077  168 LYS A N   
1422 C  CA  . LYS A 167 ? 0.2953 0.1766 0.1115 -0.0347 0.0568  -0.0300 168 LYS A CA  
1423 C  C   . LYS A 167 ? 0.3441 0.1626 0.1008 -0.0740 0.0257  -0.0085 168 LYS A C   
1424 O  O   . LYS A 167 ? 0.3307 0.1841 0.1028 -0.0743 0.0287  -0.0106 168 LYS A O   
1425 C  CB  . LYS A 167 ? 0.3651 0.1711 0.1297 -0.0285 0.0365  -0.0429 168 LYS A CB  
1426 C  CG  . LYS A 167 ? 0.3313 0.1874 0.1923 -0.0068 0.0452  -0.0599 168 LYS A CG  
1427 C  CD  . LYS A 167 ? 0.3802 0.2153 0.2374 0.0206  0.0039  -0.0928 168 LYS A CD  
1428 C  CE  . LYS A 167 ? 0.4086 0.3854 0.2669 0.1061  -0.0128 -0.1294 168 LYS A CE  
1429 N  N   A THR A 168 ? 0.2111 0.1419 0.1614 -0.0316 0.0629  -0.0040 169 THR A N   
1430 N  N   B THR A 168 ? 0.4382 0.1889 0.1730 -0.1254 0.0590  -0.0136 169 THR A N   
1431 C  CA  A THR A 168 ? 0.1952 0.1558 0.1875 -0.0261 0.0611  0.0116  169 THR A CA  
1432 C  CA  B THR A 168 ? 0.4355 0.1445 0.2340 -0.0744 0.0577  -0.0417 169 THR A CA  
1433 C  C   A THR A 168 ? 0.2118 0.1509 0.0814 0.0215  0.0729  0.0381  169 THR A C   
1434 C  C   B THR A 168 ? 0.3747 0.1771 0.2138 -0.1832 0.0882  -0.0303 169 THR A C   
1435 O  O   A THR A 168 ? 0.2053 0.1386 0.1665 -0.0076 0.1069  0.0491  169 THR A O   
1436 O  O   B THR A 168 ? 0.5190 0.1822 0.1929 -0.1030 0.0314  -0.0351 169 THR A O   
1437 C  CB  A THR A 168 ? 0.2748 0.1694 0.1636 -0.0272 0.0700  0.0015  169 THR A CB  
1438 C  CB  B THR A 168 ? 0.4706 0.1504 0.2269 -0.0937 0.0622  -0.0172 169 THR A CB  
1439 O  OG1 A THR A 168 ? 0.3471 0.2185 0.0680 -0.0578 0.1044  0.0245  169 THR A OG1 
1440 O  OG1 B THR A 168 ? 0.4886 0.1976 0.1551 -0.1347 0.0926  -0.0132 169 THR A OG1 
1441 C  CG2 A THR A 168 ? 0.3299 0.1946 0.1230 0.0436  0.1327  -0.0061 169 THR A CG2 
1442 C  CG2 B THR A 168 ? 0.4975 0.1641 0.2232 -0.0891 0.0403  -0.0402 169 THR A CG2 
1443 N  N   A LYS A 169 ? 0.2221 0.1991 0.1358 -0.0663 0.0748  0.0027  170 LYS A N   
1444 N  N   B LYS A 169 ? 0.4265 0.1620 0.1349 -0.0942 0.0929  -0.0212 170 LYS A N   
1445 C  CA  A LYS A 169 ? 0.1338 0.1195 0.1897 -0.0128 0.1251  0.0120  170 LYS A CA  
1446 C  CA  B LYS A 169 ? 0.4140 0.1576 0.1844 -0.1307 0.0781  -0.0110 170 LYS A CA  
1447 C  C   A LYS A 169 ? 0.1951 0.1954 0.1342 -0.0359 0.0989  0.0678  170 LYS A C   
1448 C  C   B LYS A 169 ? 0.3594 0.1961 0.1419 -0.1781 0.0589  0.0074  170 LYS A C   
1449 O  O   A LYS A 169 ? 0.2300 0.2508 0.1039 -0.0992 0.0736  0.0122  170 LYS A O   
1450 O  O   B LYS A 169 ? 0.4213 0.2927 0.0906 -0.1740 0.0606  0.0190  170 LYS A O   
1451 C  CB  A LYS A 169 ? 0.1123 0.1451 0.2069 -0.0046 0.1446  -0.0041 170 LYS A CB  
1452 C  CB  B LYS A 169 ? 0.4412 0.1697 0.2071 -0.0372 0.1018  -0.0597 170 LYS A CB  
1453 C  CG  A LYS A 169 ? 0.1060 0.2552 0.2643 -0.0724 0.1317  -0.0596 170 LYS A CG  
1454 C  CG  B LYS A 169 ? 0.4194 0.1976 0.1541 -0.1317 0.0326  0.0239  170 LYS A CG  
1455 C  CD  A LYS A 169 ? 0.1668 0.2180 0.2568 -0.0570 0.0948  -0.0553 170 LYS A CD  
1456 C  CD  B LYS A 169 ? 0.4154 0.2874 0.2072 -0.1115 0.0541  -0.0131 170 LYS A CD  
1457 C  CE  A LYS A 169 ? 0.1021 0.3331 0.3466 0.0029  0.1074  -0.0172 170 LYS A CE  
1458 C  CE  B LYS A 169 ? 0.3862 0.3444 0.3219 -0.1858 -0.0779 -0.0151 170 LYS A CE  
1459 N  NZ  A LYS A 169 ? 0.1675 0.4250 0.2518 -0.0136 0.0996  -0.0016 170 LYS A NZ  
1460 N  NZ  B LYS A 169 ? 0.3280 0.5004 0.4263 -0.0761 -0.1054 -0.0432 170 LYS A NZ  
1461 N  N   A GLY A 170 ? 0.2581 0.1411 0.1518 -0.0754 0.0666  0.0421  171 GLY A N   
1462 N  N   B GLY A 170 ? 0.4387 0.1720 0.1236 -0.1596 0.0396  0.0119  171 GLY A N   
1463 C  CA  A GLY A 170 ? 0.1640 0.1597 0.2027 -0.1017 -0.0430 0.0762  171 GLY A CA  
1464 C  CA  B GLY A 170 ? 0.4416 0.1885 0.1613 -0.1878 -0.0617 0.0554  171 GLY A CA  
1465 C  C   A GLY A 170 ? 0.0860 0.1855 0.2452 -0.0254 0.0040  0.0335  171 GLY A C   
1466 C  C   B GLY A 170 ? 0.4523 0.1879 0.1288 -0.1280 -0.0474 0.0480  171 GLY A C   
1467 O  O   A GLY A 170 ? 0.2409 0.1750 0.2918 -0.0391 0.0361  0.0916  171 GLY A O   
1468 O  O   B GLY A 170 ? 0.5157 0.1433 0.2438 -0.1638 -0.0738 0.0709  171 GLY A O   
1469 N  N   A LYS A 171 ? 0.3528 0.1588 0.1186 -0.0956 0.0201  0.0700  172 LYS A N   
1470 N  N   B LYS A 171 ? 0.4947 0.1859 0.0506 -0.1459 0.0017  0.0283  172 LYS A N   
1471 C  CA  A LYS A 171 ? 0.3050 0.1894 0.1527 -0.0987 0.0484  -0.0064 172 LYS A CA  
1472 C  CA  B LYS A 171 ? 0.4738 0.1280 0.1901 -0.0631 -0.0158 0.0122  172 LYS A CA  
1473 C  C   A LYS A 171 ? 0.2940 0.1667 0.0491 -0.0269 -0.0099 0.0484  172 LYS A C   
1474 C  C   B LYS A 171 ? 0.4776 0.2227 0.1100 -0.1199 0.0145  0.0241  172 LYS A C   
1475 O  O   A LYS A 171 ? 0.4177 0.1503 0.0504 -0.0501 0.0378  0.0466  172 LYS A O   
1476 O  O   B LYS A 171 ? 0.5529 0.2239 0.1003 -0.0895 0.0266  0.0173  172 LYS A O   
1477 C  CB  A LYS A 171 ? 0.3309 0.1975 0.0994 -0.1066 0.1185  -0.0073 172 LYS A CB  
1478 C  CB  B LYS A 171 ? 0.4203 0.1663 0.1368 -0.1065 -0.0665 0.0318  172 LYS A CB  
1479 C  CG  A LYS A 171 ? 0.3891 0.2720 0.1215 -0.0863 0.1296  -0.0149 172 LYS A CG  
1480 C  CG  B LYS A 171 ? 0.6035 0.2753 0.1330 -0.1007 0.0031  -0.0229 172 LYS A CG  
1481 C  CD  A LYS A 171 ? 0.4603 0.4315 0.2265 -0.0414 0.0455  -0.1094 172 LYS A CD  
1482 C  CD  B LYS A 171 ? 0.6838 0.1692 0.2212 -0.0974 0.0139  -0.0120 172 LYS A CD  
1483 C  CE  A LYS A 171 ? 0.3317 0.4765 0.2721 0.1912  0.0289  0.0057  172 LYS A CE  
1484 C  CE  B LYS A 171 ? 0.8103 0.2276 0.1597 -0.0925 -0.0253 0.0718  172 LYS A CE  
1485 N  NZ  A LYS A 171 ? 0.5490 0.5736 0.3040 0.1256  -0.0625 -0.0259 172 LYS A NZ  
1486 N  NZ  B LYS A 171 ? 0.8338 0.1791 0.2336 -0.1567 0.0907  0.0249  172 LYS A NZ  
1487 N  N   A SER A 172 ? 0.2514 0.1749 0.1240 -0.0225 0.0300  0.0763  173 SER A N   
1488 N  N   B SER A 172 ? 0.4028 0.1641 0.1694 -0.1219 -0.0337 -0.0398 173 SER A N   
1489 C  CA  A SER A 172 ? 0.3264 0.2046 0.1195 -0.0094 0.0706  -0.0146 173 SER A CA  
1490 C  CA  B SER A 172 ? 0.4461 0.1497 0.1455 -0.0337 -0.0318 -0.0005 173 SER A CA  
1491 C  C   A SER A 172 ? 0.2460 0.1416 0.1484 -0.0087 0.0854  0.0610  173 SER A C   
1492 C  C   B SER A 172 ? 0.4986 0.1500 0.1212 -0.0078 -0.0381 0.0078  173 SER A C   
1493 O  O   A SER A 172 ? 0.3486 0.1879 0.1203 0.0538  0.0365  0.0579  173 SER A O   
1494 O  O   B SER A 172 ? 0.5327 0.1965 0.1351 -0.0201 0.0547  -0.0211 173 SER A O   
1495 C  CB  A SER A 172 ? 0.2935 0.1813 0.0842 0.0179  0.0309  0.0219  173 SER A CB  
1496 C  CB  B SER A 172 ? 0.3642 0.1295 0.1507 -0.0840 0.0021  0.0277  173 SER A CB  
1497 O  OG  A SER A 172 ? 0.3529 0.1477 0.1252 0.0619  0.0491  0.0394  173 SER A OG  
1498 O  OG  B SER A 172 ? 0.1927 0.1338 0.1816 0.0152  0.0478  0.0377  173 SER A OG  
1499 N  N   A ALA A 173 ? 0.2180 0.2205 0.1859 0.0508  0.0508  0.0508  174 ALA A N   
1500 N  N   B ALA A 173 ? 0.4811 0.1165 0.1254 0.0420  -0.0155 -0.0122 174 ALA A N   
1501 C  CA  A ALA A 173 ? 0.2425 0.2534 0.0967 0.0809  0.0479  0.0512  174 ALA A CA  
1502 C  CA  B ALA A 173 ? 0.5177 0.1667 0.0850 0.0817  -0.0325 0.0391  174 ALA A CA  
1503 C  C   A ALA A 173 ? 0.1264 0.2582 0.1967 0.0776  -0.0261 0.0456  174 ALA A C   
1504 C  C   B ALA A 173 ? 0.5659 0.2726 0.0699 0.0685  0.0205  0.0166  174 ALA A C   
1505 O  O   A ALA A 173 ? 0.0514 0.2081 0.1982 -0.0545 -0.0305 0.0622  174 ALA A O   
1506 O  O   B ALA A 173 ? 0.3746 0.1182 0.0525 0.0565  -0.0551 0.0161  174 ALA A O   
1507 C  CB  A ALA A 173 ? 0.3652 0.1990 0.1105 0.1177  0.0261  -0.0190 174 ALA A CB  
1508 C  CB  B ALA A 173 ? 0.4132 0.2006 0.0675 0.0601  0.0053  0.0158  174 ALA A CB  
1509 N  N   A ASP A 174 ? 0.3436 0.2811 0.1829 0.0936  -0.0523 0.1093  175 ASP A N   
1510 N  N   B ASP A 174 ? 0.5559 0.2719 0.3365 0.0394  -0.0979 0.0198  175 ASP A N   
1511 C  CA  A ASP A 174 ? 0.4484 0.2760 0.2498 0.1678  -0.0003 0.0949  175 ASP A CA  
1512 C  CA  B ASP A 174 ? 0.8606 0.3145 0.3472 -0.0883 0.0113  0.1182  175 ASP A CA  
1513 C  C   A ASP A 174 ? 0.4612 0.3532 0.1886 0.0980  -0.0072 -0.0072 175 ASP A C   
1514 C  C   B ASP A 174 ? 0.5126 0.1354 0.2220 0.0866  -0.0541 0.0001  175 ASP A C   
1515 O  O   A ASP A 174 ? 0.0284 0.4648 0.2554 -0.0022 0.0357  0.1003  175 ASP A O   
1516 O  O   B ASP A 174 ? 0.4368 0.1701 0.1055 0.1024  -0.0798 -0.0077 175 ASP A O   
1517 C  CB  A ASP A 174 ? 0.5253 0.4918 0.2557 0.1453  -0.0544 0.1148  175 ASP A CB  
1518 C  CB  B ASP A 174 ? 0.9874 0.4512 0.4900 0.1280  -0.5128 0.1826  175 ASP A CB  
1519 C  CG  A ASP A 174 ? 0.5187 0.4539 0.4739 0.1576  0.0475  0.0575  175 ASP A CG  
1520 C  CG  B ASP A 174 ? 1.1179 0.6128 0.3939 0.0074  0.0316  -0.0513 175 ASP A CG  
1521 O  OD1 A ASP A 174 ? 0.5633 0.6074 0.2525 0.0869  0.0596  -0.0089 175 ASP A OD1 
1522 O  OD1 B ASP A 174 ? 1.1957 0.7682 0.6985 -0.1388 0.0723  -0.0570 175 ASP A OD1 
1523 O  OD2 A ASP A 174 ? 0.8960 0.7336 0.4440 0.3012  0.0511  -0.0264 175 ASP A OD2 
1524 O  OD2 B ASP A 174 ? 1.6671 1.2182 0.4038 0.1058  0.0779  -0.0385 175 ASP A OD2 
1525 N  N   . PHE A 175 ? 0.5096 0.2269 0.1692 0.0564  -0.0520 -0.0458 176 PHE A N   
1526 C  CA  . PHE A 175 ? 0.5395 0.2192 0.2663 0.0100  -0.0978 -0.0375 176 PHE A CA  
1527 C  C   . PHE A 175 ? 0.4800 0.1483 0.1817 -0.0234 -0.1283 0.0214  176 PHE A C   
1528 O  O   . PHE A 175 ? 0.5521 0.1595 0.1835 0.0178  -0.1672 0.0187  176 PHE A O   
1529 C  CB  . PHE A 175 ? 0.5784 0.1671 0.2410 0.0125  -0.0699 0.0111  176 PHE A CB  
1530 C  CG  . PHE A 175 ? 0.5159 0.1504 0.1600 0.0380  -0.0741 -0.0051 176 PHE A CG  
1531 C  CD1 . PHE A 175 ? 0.5329 0.1261 0.1865 0.0621  -0.0785 -0.0033 176 PHE A CD1 
1532 C  CD2 . PHE A 175 ? 0.4991 0.1491 0.1554 0.0286  -0.0955 -0.0144 176 PHE A CD2 
1533 C  CE1 . PHE A 175 ? 0.5235 0.1249 0.1795 0.0628  -0.0811 -0.0172 176 PHE A CE1 
1534 C  CE2 . PHE A 175 ? 0.5396 0.1360 0.2087 0.0177  -0.1657 0.0015  176 PHE A CE2 
1535 C  CZ  . PHE A 175 ? 0.4886 0.1311 0.1653 0.0204  -0.1093 0.0013  176 PHE A CZ  
1536 N  N   . THR A 176 ? 0.4919 0.1533 0.1314 0.0305  -0.1252 0.0122  177 THR A N   
1537 C  CA  . THR A 176 ? 0.4250 0.1713 0.1918 -0.0333 -0.0862 0.0087  177 THR A CA  
1538 C  C   . THR A 176 ? 0.3192 0.1217 0.1032 0.0211  -0.1131 0.0347  177 THR A C   
1539 O  O   . THR A 176 ? 0.4643 0.1349 0.1546 -0.0141 -0.1421 0.0260  177 THR A O   
1540 C  CB  . THR A 176 ? 0.4345 0.1638 0.2191 -0.0423 -0.1578 0.0021  177 THR A CB  
1541 O  OG1 . THR A 176 ? 0.5578 0.1967 0.1323 0.0156  -0.1460 0.0464  177 THR A OG1 
1542 C  CG2 . THR A 176 ? 0.4943 0.2285 0.3218 -0.0368 -0.1749 0.1550  177 THR A CG2 
1543 N  N   . ASN A 177 ? 0.4225 0.1474 0.1192 0.0093  -0.1085 0.0186  178 ASN A N   
1544 C  CA  . ASN A 177 ? 0.4111 0.1846 0.1770 -0.0023 -0.1178 0.0324  178 ASN A CA  
1545 C  C   . ASN A 177 ? 0.4333 0.1545 0.2425 -0.0442 -0.1733 0.0242  178 ASN A C   
1546 O  O   . ASN A 177 ? 0.4732 0.2377 0.3145 -0.0674 -0.1664 0.0884  178 ASN A O   
1547 C  CB  . ASN A 177 ? 0.4329 0.1767 0.2239 -0.0033 -0.1716 0.0571  178 ASN A CB  
1548 C  CG  . ASN A 177 ? 0.4655 0.1492 0.1540 -0.0003 -0.1106 0.0120  178 ASN A CG  
1549 O  OD1 . ASN A 177 ? 0.4662 0.1737 0.2042 0.0225  -0.0548 0.0368  178 ASN A OD1 
1550 N  ND2 . ASN A 177 ? 0.4119 0.1683 0.1600 -0.0192 -0.1398 0.0672  178 ASN A ND2 
1551 N  N   . PHE A 178 ? 0.4448 0.1030 0.1483 -0.0067 -0.1636 0.0559  179 PHE A N   
1552 C  CA  . PHE A 178 ? 0.3642 0.1046 0.1496 -0.0275 -0.1023 0.0632  179 PHE A CA  
1553 C  C   . PHE A 178 ? 0.3508 0.1016 0.1509 -0.0125 -0.1139 0.0311  179 PHE A C   
1554 O  O   . PHE A 178 ? 0.3577 0.1219 0.1632 -0.0289 -0.1264 0.0257  179 PHE A O   
1555 C  CB  . PHE A 178 ? 0.3806 0.1303 0.1281 0.0009  -0.0588 0.0359  179 PHE A CB  
1556 C  CG  . PHE A 178 ? 0.3630 0.1210 0.1471 -0.0185 -0.0881 0.0337  179 PHE A CG  
1557 C  CD1 . PHE A 178 ? 0.3736 0.1182 0.1615 -0.0132 -0.0480 0.0192  179 PHE A CD1 
1558 C  CD2 . PHE A 178 ? 0.2464 0.1220 0.1414 0.0144  -0.0554 0.0306  179 PHE A CD2 
1559 C  CE1 . PHE A 178 ? 0.3722 0.1228 0.1690 -0.0084 -0.0505 0.0185  179 PHE A CE1 
1560 C  CE2 . PHE A 178 ? 0.2595 0.1161 0.1539 0.0026  -0.0819 0.0318  179 PHE A CE2 
1561 C  CZ  . PHE A 178 ? 0.2852 0.1172 0.1547 0.0168  -0.0446 0.0127  179 PHE A CZ  
1562 N  N   . ASP A 179 ? 0.2961 0.1377 0.1739 -0.0032 -0.1195 0.0476  180 ASP A N   
1563 C  CA  . ASP A 179 ? 0.2380 0.1493 0.1947 0.0055  -0.1137 0.0326  180 ASP A CA  
1564 C  C   . ASP A 179 ? 0.2483 0.1134 0.1749 -0.0166 -0.1053 0.0292  180 ASP A C   
1565 O  O   . ASP A 179 ? 0.2585 0.1122 0.1879 -0.0209 -0.0968 0.0099  180 ASP A O   
1566 C  CB  . ASP A 179 ? 0.2484 0.1989 0.2405 -0.0347 -0.1420 0.0839  180 ASP A CB  
1567 C  CG  . ASP A 179 ? 0.2329 0.2416 0.2851 -0.0316 -0.1182 0.0754  180 ASP A CG  
1568 O  OD1 . ASP A 179 ? 0.2967 0.1441 0.2741 -0.0033 -0.1342 0.0436  180 ASP A OD1 
1569 O  OD2 . ASP A 179 ? 0.2221 0.4868 0.4319 -0.0474 -0.1400 0.0324  180 ASP A OD2 
1570 N  N   . PRO A 180 ? 0.1983 0.1128 0.1665 0.0063  -0.0927 0.0143  181 PRO A N   
1571 C  CA  . PRO A 180 ? 0.1638 0.1405 0.1603 -0.0133 -0.0841 0.0308  181 PRO A CA  
1572 C  C   . PRO A 180 ? 0.1714 0.1116 0.1706 -0.0011 -0.0566 0.0267  181 PRO A C   
1573 O  O   . PRO A 180 ? 0.1594 0.1219 0.1495 0.0098  -0.0549 0.0134  181 PRO A O   
1574 C  CB  . PRO A 180 ? 0.1919 0.1470 0.1988 -0.0263 -0.0844 0.0175  181 PRO A CB  
1575 C  CG  . PRO A 180 ? 0.2527 0.1372 0.1845 -0.0366 -0.0974 0.0156  181 PRO A CG  
1576 C  CD  . PRO A 180 ? 0.2025 0.1371 0.1718 -0.0425 -0.0862 0.0256  181 PRO A CD  
1577 N  N   . ARG A 181 ? 0.1636 0.1320 0.1703 -0.0041 -0.0649 0.0118  182 ARG A N   
1578 C  CA  . ARG A 181 ? 0.1264 0.1283 0.2328 -0.0040 -0.0643 -0.0038 182 ARG A CA  
1579 C  C   . ARG A 181 ? 0.1755 0.1300 0.2069 0.0108  -0.1086 0.0118  182 ARG A C   
1580 O  O   . ARG A 181 ? 0.2062 0.1450 0.2397 -0.0147 -0.1086 0.0463  182 ARG A O   
1581 C  CB  . ARG A 181 ? 0.1229 0.1454 0.2732 -0.0002 -0.0345 0.0140  182 ARG A CB  
1582 C  CG  . ARG A 181 ? 0.1703 0.1375 0.2989 0.0141  -0.0208 0.0078  182 ARG A CG  
1583 C  CD  . ARG A 181 ? 0.1122 0.1942 0.3565 -0.0027 0.0058  0.0502  182 ARG A CD  
1584 N  NE  . ARG A 181 ? 0.1703 0.1650 0.3886 -0.0485 -0.0629 0.0930  182 ARG A NE  
1585 C  CZ  . ARG A 181 ? 0.1929 0.1947 0.3655 -0.0122 0.0279  0.1331  182 ARG A CZ  
1586 N  NH1 . ARG A 181 ? 0.1756 0.2755 0.4610 -0.0203 0.0597  0.1150  182 ARG A NH1 
1587 N  NH2 . ARG A 181 ? 0.2074 0.2699 0.3930 -0.0142 -0.0418 0.1407  182 ARG A NH2 
1588 N  N   . GLY A 182 ? 0.2256 0.1307 0.1952 0.0121  -0.1197 0.0078  183 GLY A N   
1589 C  CA  . GLY A 182 ? 0.2282 0.1236 0.2376 -0.0127 -0.1525 0.0185  183 GLY A CA  
1590 C  C   . GLY A 182 ? 0.2543 0.1217 0.2332 0.0093  -0.1395 0.0050  183 GLY A C   
1591 O  O   . GLY A 182 ? 0.2762 0.1112 0.2460 0.0096  -0.1441 -0.0012 183 GLY A O   
1592 N  N   . LEU A 183 ? 0.2225 0.1158 0.1754 0.0051  -0.1056 0.0120  184 LEU A N   
1593 C  CA  . LEU A 183 ? 0.2105 0.1342 0.1606 0.0182  -0.0939 0.0010  184 LEU A CA  
1594 C  C   . LEU A 183 ? 0.1662 0.1177 0.1562 -0.0009 -0.0754 0.0127  184 LEU A C   
1595 O  O   . LEU A 183 ? 0.1857 0.1391 0.1802 0.0182  -0.0673 0.0362  184 LEU A O   
1596 C  CB  . LEU A 183 ? 0.1938 0.1778 0.1309 0.0431  -0.0576 0.0162  184 LEU A CB  
1597 C  CG  . LEU A 183 ? 0.2727 0.1637 0.1316 0.0483  -0.0690 0.0097  184 LEU A CG  
1598 C  CD1 . LEU A 183 ? 0.2683 0.2051 0.1815 0.0628  -0.0506 0.0493  184 LEU A CD1 
1599 C  CD2 . LEU A 183 ? 0.2597 0.1857 0.1782 0.0650  -0.0487 -0.0099 184 LEU A CD2 
1600 N  N   . LEU A 184 ? 0.1595 0.1418 0.1837 -0.0018 -0.0565 0.0275  185 LEU A N   
1601 C  CA  . LEU A 184 ? 0.1306 0.1377 0.1835 -0.0321 -0.0599 0.0306  185 LEU A CA  
1602 C  C   . LEU A 184 ? 0.2375 0.1491 0.2105 -0.0835 -0.1109 0.0370  185 LEU A C   
1603 O  O   . LEU A 184 ? 0.3110 0.2232 0.3611 -0.1421 -0.2373 0.1207  185 LEU A O   
1604 C  CB  . LEU A 184 ? 0.1001 0.1567 0.1981 -0.0253 -0.0278 0.0373  185 LEU A CB  
1605 C  CG  . LEU A 184 ? 0.0912 0.1432 0.2022 -0.0189 -0.0293 0.0106  185 LEU A CG  
1606 C  CD1 . LEU A 184 ? 0.1021 0.1649 0.2408 0.0071  -0.0084 0.0395  185 LEU A CD1 
1607 C  CD2 . LEU A 184 ? 0.0748 0.1840 0.2408 0.0087  -0.0257 0.0077  185 LEU A CD2 
1608 N  N   . PRO A 185 ? 0.1165 0.1531 0.2018 -0.0229 -0.0601 0.0434  186 PRO A N   
1609 C  CA  . PRO A 185 ? 0.1405 0.1383 0.2116 -0.0278 -0.0549 0.0500  186 PRO A CA  
1610 C  C   . PRO A 185 ? 0.0815 0.1307 0.3719 -0.0278 -0.0727 0.0663  186 PRO A C   
1611 O  O   . PRO A 185 ? 0.0769 0.1298 0.4741 -0.0105 -0.0548 0.0878  186 PRO A O   
1612 C  CB  . PRO A 185 ? 0.0886 0.1605 0.2231 -0.0127 -0.0319 0.0546  186 PRO A CB  
1613 C  CG  . PRO A 185 ? 0.0424 0.1678 0.1749 0.0337  -0.0122 0.0106  186 PRO A CG  
1614 C  CD  . PRO A 185 ? 0.1139 0.1418 0.1324 0.0103  -0.0384 -0.0002 186 PRO A CD  
1615 N  N   . GLU A 186 ? 0.0969 0.1641 0.3523 -0.0434 -0.0717 0.0877  187 GLU A N   
1616 C  CA  . GLU A 186 ? 0.0976 0.1938 0.4009 -0.0405 -0.0400 0.0767  187 GLU A CA  
1617 C  C   . GLU A 186 ? 0.0454 0.1793 0.3589 0.0331  0.0089  0.0815  187 GLU A C   
1618 O  O   . GLU A 186 ? 0.0527 0.2017 0.4372 0.0447  0.0223  0.0583  187 GLU A O   
1619 C  CB  . GLU A 186 ? 0.1568 0.2066 0.5238 -0.0655 -0.0796 0.1254  187 GLU A CB  
1620 C  CG  . GLU A 186 ? 0.2194 0.2984 0.5122 -0.0541 -0.0849 0.1226  187 GLU A CG  
1621 C  CD  . GLU A 186 ? 0.1460 0.2534 0.4533 -0.0044 -0.0356 0.0580  187 GLU A CD  
1622 O  OE1 . GLU A 186 ? 0.3321 0.3928 0.4765 -0.0907 -0.0754 0.1215  187 GLU A OE1 
1623 O  OE2 . GLU A 186 ? 0.2077 0.3750 0.6293 -0.0234 -0.0664 -0.0630 187 GLU A OE2 
1624 N  N   . SER A 187 ? 0.0547 0.2216 0.3443 -0.0541 -0.0323 0.1064  188 SER A N   
1625 C  CA  . SER A 187 ? 0.0228 0.2108 0.3365 0.0038  0.0286  0.0802  188 SER A CA  
1626 C  C   . SER A 187 ? 0.0551 0.1945 0.2807 -0.0182 0.0441  0.0398  188 SER A C   
1627 O  O   . SER A 187 ? 0.0511 0.2233 0.2808 -0.0161 0.0367  0.0336  188 SER A O   
1628 C  CB  . SER A 187 ? 0.0653 0.2863 0.2949 0.0110  0.0452  0.1117  188 SER A CB  
1629 O  OG  . SER A 187 ? 0.0839 0.2398 0.3357 -0.0208 0.0359  0.1004  188 SER A OG  
1630 N  N   . LEU A 188 ? 0.0707 0.1687 0.3294 -0.0074 0.0303  0.0264  189 LEU A N   
1631 C  CA  . LEU A 188 ? 0.0768 0.1683 0.2840 -0.0108 0.0165  0.0100  189 LEU A CA  
1632 C  C   . LEU A 188 ? 0.0678 0.1764 0.2552 0.0074  0.0536  0.0044  189 LEU A C   
1633 O  O   . LEU A 188 ? 0.1240 0.1989 0.2652 -0.0207 0.0569  -0.0369 189 LEU A O   
1634 C  CB  . LEU A 188 ? 0.1368 0.1804 0.3338 0.0003  0.0796  0.0260  189 LEU A CB  
1635 C  CG  . LEU A 188 ? 0.1159 0.2017 0.4259 -0.0079 -0.0111 0.0803  189 LEU A CG  
1636 C  CD1 . LEU A 188 ? 0.1448 0.2136 0.4517 -0.0036 -0.0100 0.1047  189 LEU A CD1 
1637 C  CD2 . LEU A 188 ? 0.0854 0.3468 0.3885 0.0277  -0.0088 0.1138  189 LEU A CD2 
1638 N  N   . ASP A 189 ? 0.0757 0.1967 0.2578 0.0294  0.0599  0.0270  190 ASP A N   
1639 C  CA  . ASP A 189 ? 0.0833 0.1836 0.2071 -0.0144 0.0849  0.0036  190 ASP A CA  
1640 C  C   . ASP A 189 ? 0.0702 0.1470 0.1781 -0.0141 0.0556  0.0002  190 ASP A C   
1641 O  O   . ASP A 189 ? 0.0848 0.1385 0.1682 -0.0018 0.0477  -0.0029 190 ASP A O   
1642 C  CB  . ASP A 189 ? 0.1588 0.2400 0.2453 -0.1037 0.0673  0.0633  190 ASP A CB  
1643 C  CG  . ASP A 189 ? 0.1620 0.4201 0.3243 -0.1099 0.1103  0.0518  190 ASP A CG  
1644 O  OD1 . ASP A 189 ? 0.2112 0.4620 0.3474 -0.0565 0.1001  0.0046  190 ASP A OD1 
1645 O  OD2 . ASP A 189 ? 0.4552 0.4461 0.3653 -0.0851 -0.0416 0.0084  190 ASP A OD2 
1646 N  N   . TYR A 190 ? 0.0745 0.1486 0.1388 -0.0065 0.0706  0.0178  191 TYR A N   
1647 C  CA  . TYR A 190 ? 0.0617 0.1421 0.1229 -0.0044 0.0480  0.0216  191 TYR A CA  
1648 C  C   . TYR A 190 ? 0.0860 0.1297 0.1028 -0.0075 0.0507  0.0160  191 TYR A C   
1649 O  O   . TYR A 190 ? 0.1136 0.1566 0.1025 0.0044  0.0605  0.0161  191 TYR A O   
1650 C  CB  . TYR A 190 ? 0.1123 0.1341 0.1409 0.0057  0.0535  0.0273  191 TYR A CB  
1651 C  CG  . TYR A 190 ? 0.1147 0.1286 0.1265 0.0020  0.0512  0.0298  191 TYR A CG  
1652 C  CD1 . TYR A 190 ? 0.1445 0.1373 0.1365 -0.0107 0.0490  0.0189  191 TYR A CD1 
1653 C  CD2 . TYR A 190 ? 0.1323 0.1487 0.1530 0.0447  0.0864  0.0233  191 TYR A CD2 
1654 C  CE1 . TYR A 190 ? 0.1317 0.1418 0.1630 -0.0008 0.0587  0.0182  191 TYR A CE1 
1655 C  CE2 . TYR A 190 ? 0.1443 0.1728 0.1297 0.0160  0.0565  0.0033  191 TYR A CE2 
1656 C  CZ  . TYR A 190 ? 0.1615 0.1621 0.1381 0.0256  0.0425  -0.0089 191 TYR A CZ  
1657 O  OH  . TYR A 190 ? 0.2009 0.1688 0.1692 0.0425  0.0576  -0.0201 191 TYR A OH  
1658 N  N   . TRP A 191 ? 0.0804 0.1168 0.1030 0.0001  0.0351  0.0108  192 TRP A N   
1659 C  CA  . TRP A 191 ? 0.0728 0.1285 0.0951 0.0053  0.0353  0.0078  192 TRP A CA  
1660 C  C   . TRP A 191 ? 0.0987 0.1298 0.0682 0.0095  0.0364  0.0065  192 TRP A C   
1661 O  O   . TRP A 191 ? 0.1383 0.1358 0.0683 -0.0051 0.0279  0.0051  192 TRP A O   
1662 C  CB  . TRP A 191 ? 0.0866 0.1385 0.1003 0.0143  0.0484  0.0069  192 TRP A CB  
1663 C  CG  . TRP A 191 ? 0.0937 0.1378 0.1027 0.0356  0.0406  0.0199  192 TRP A CG  
1664 C  CD1 . TRP A 191 ? 0.1587 0.1314 0.1064 0.0257  0.0482  0.0217  192 TRP A CD1 
1665 C  CD2 . TRP A 191 ? 0.0795 0.1359 0.1069 0.0299  0.0348  0.0176  192 TRP A CD2 
1666 N  NE1 . TRP A 191 ? 0.1458 0.1393 0.1282 0.0135  0.0521  0.0299  192 TRP A NE1 
1667 C  CE2 . TRP A 191 ? 0.1219 0.1286 0.1395 0.0209  0.0315  0.0174  192 TRP A CE2 
1668 C  CE3 . TRP A 191 ? 0.0739 0.1441 0.1131 0.0315  0.0302  0.0058  192 TRP A CE3 
1669 C  CZ2 . TRP A 191 ? 0.1018 0.1418 0.1653 0.0089  0.0044  0.0239  192 TRP A CZ2 
1670 C  CZ3 . TRP A 191 ? 0.0700 0.1527 0.1670 0.0261  0.0295  -0.0100 192 TRP A CZ3 
1671 C  CH2 . TRP A 191 ? 0.1134 0.1366 0.1764 0.0084  0.0197  -0.0174 192 TRP A CH2 
1672 N  N   . THR A 192 ? 0.1037 0.1270 0.0784 0.0050  0.0260  0.0075  193 THR A N   
1673 C  CA  . THR A 192 ? 0.0973 0.1166 0.0707 0.0103  0.0212  -0.0094 193 THR A CA  
1674 C  C   . THR A 192 ? 0.1149 0.1107 0.0719 0.0099  0.0137  0.0049  193 THR A C   
1675 O  O   . THR A 192 ? 0.1340 0.1515 0.0633 0.0179  0.0234  0.0013  193 THR A O   
1676 C  CB  . THR A 192 ? 0.1186 0.1152 0.0798 0.0239  0.0286  0.0043  193 THR A CB  
1677 O  OG1 . THR A 192 ? 0.1033 0.1134 0.1070 0.0309  0.0208  -0.0058 193 THR A OG1 
1678 C  CG2 . THR A 192 ? 0.1408 0.1480 0.0940 0.0679  0.0432  -0.0003 193 THR A CG2 
1679 N  N   . TYR A 193 ? 0.0854 0.1201 0.0791 0.0177  0.0053  -0.0071 194 TYR A N   
1680 C  CA  . TYR A 193 ? 0.1018 0.1271 0.0709 0.0096  0.0013  -0.0062 194 TYR A CA  
1681 C  C   . TYR A 193 ? 0.1191 0.1025 0.0785 0.0237  -0.0055 -0.0140 194 TYR A C   
1682 O  O   . TYR A 193 ? 0.1016 0.1206 0.0739 0.0234  0.0009  -0.0080 194 TYR A O   
1683 C  CB  . TYR A 193 ? 0.1235 0.1397 0.0877 0.0383  0.0179  -0.0184 194 TYR A CB  
1684 C  CG  . TYR A 193 ? 0.0930 0.1182 0.0816 0.0256  0.0055  -0.0047 194 TYR A CG  
1685 C  CD1 . TYR A 193 ? 0.1146 0.1012 0.0658 0.0297  0.0035  -0.0063 194 TYR A CD1 
1686 C  CD2 . TYR A 193 ? 0.0866 0.1323 0.1125 0.0274  -0.0156 -0.0122 194 TYR A CD2 
1687 C  CE1 . TYR A 193 ? 0.0736 0.1001 0.0815 0.0223  0.0055  -0.0004 194 TYR A CE1 
1688 C  CE2 . TYR A 193 ? 0.1179 0.1125 0.0926 0.0254  -0.0150 -0.0203 194 TYR A CE2 
1689 C  CZ  . TYR A 193 ? 0.0732 0.1012 0.0818 0.0256  -0.0038 -0.0055 194 TYR A CZ  
1690 O  OH  . TYR A 193 ? 0.0701 0.1115 0.0930 0.0110  0.0025  -0.0168 194 TYR A OH  
1691 N  N   . PRO A 194 ? 0.0858 0.1338 0.0775 0.0289  -0.0047 -0.0230 195 PRO A N   
1692 C  CA  . PRO A 194 ? 0.0963 0.1116 0.1062 0.0264  0.0103  -0.0402 195 PRO A CA  
1693 C  C   . PRO A 194 ? 0.0784 0.0976 0.0937 0.0272  -0.0081 -0.0296 195 PRO A C   
1694 O  O   . PRO A 194 ? 0.1071 0.1347 0.0960 0.0435  -0.0248 -0.0250 195 PRO A O   
1695 C  CB  . PRO A 194 ? 0.1361 0.1448 0.1274 0.0254  -0.0262 -0.0458 195 PRO A CB  
1696 C  CG  . PRO A 194 ? 0.1283 0.1790 0.1240 0.0218  -0.0143 -0.0458 195 PRO A CG  
1697 C  CD  . PRO A 194 ? 0.1216 0.1834 0.0762 0.0170  -0.0006 -0.0122 195 PRO A CD  
1698 N  N   . GLY A 195 ? 0.0816 0.1132 0.0913 0.0181  -0.0129 -0.0281 196 GLY A N   
1699 C  CA  . GLY A 195 ? 0.0702 0.1197 0.1067 0.0221  -0.0040 -0.0177 196 GLY A CA  
1700 C  C   . GLY A 195 ? 0.0503 0.0940 0.1193 0.0187  -0.0141 -0.0275 196 GLY A C   
1701 O  O   . GLY A 195 ? 0.0818 0.0906 0.1161 0.0118  -0.0179 -0.0238 196 GLY A O   
1702 N  N   . SER A 196 ? 0.0552 0.0951 0.1066 0.0120  -0.0004 -0.0185 197 SER A N   
1703 C  CA  . SER A 196 ? 0.0536 0.1091 0.1244 -0.0023 0.0091  -0.0168 197 SER A CA  
1704 C  C   . SER A 196 ? 0.0357 0.0994 0.1195 0.0083  -0.0066 -0.0109 197 SER A C   
1705 O  O   . SER A 196 ? 0.0410 0.1044 0.1188 0.0033  -0.0038 -0.0185 197 SER A O   
1706 C  CB  . SER A 196 ? 0.0575 0.0967 0.1693 0.0087  -0.0300 -0.0267 197 SER A CB  
1707 O  OG  . SER A 196 ? 0.0522 0.1025 0.1361 0.0069  -0.0011 -0.0230 197 SER A OG  
1708 N  N   . LEU A 197 ? 0.0552 0.1018 0.1273 0.0052  0.0109  -0.0212 198 LEU A N   
1709 C  CA  . LEU A 197 ? 0.0644 0.1052 0.1297 -0.0117 0.0190  -0.0289 198 LEU A CA  
1710 C  C   . LEU A 197 ? 0.0508 0.1080 0.1125 -0.0223 0.0190  -0.0127 198 LEU A C   
1711 O  O   . LEU A 197 ? 0.0588 0.1228 0.1216 -0.0027 0.0093  -0.0254 198 LEU A O   
1712 C  CB  . LEU A 197 ? 0.1067 0.1283 0.1639 -0.0066 0.0419  -0.0137 198 LEU A CB  
1713 C  CG  . LEU A 197 ? 0.1140 0.1939 0.2958 0.0304  0.0785  0.0644  198 LEU A CG  
1714 C  CD1 . LEU A 197 ? 0.1653 0.1852 0.1963 -0.0059 0.0524  -0.0111 198 LEU A CD1 
1715 C  CD2 . LEU A 197 ? 0.1168 0.2423 0.3294 0.0220  0.1032  0.0697  198 LEU A CD2 
1716 N  N   . THR A 198 ? 0.0551 0.1142 0.1370 0.0031  0.0021  -0.0333 199 THR A N   
1717 C  CA  . THR A 198 ? 0.0512 0.1220 0.1579 0.0032  0.0220  -0.0396 199 THR A CA  
1718 C  C   . THR A 198 ? 0.0275 0.1337 0.1647 0.0021  0.0190  -0.0262 199 THR A C   
1719 O  O   . THR A 198 ? 0.0421 0.1313 0.1889 0.0027  0.0356  -0.0245 199 THR A O   
1720 C  CB  . THR A 198 ? 0.0516 0.1292 0.1156 -0.0087 0.0156  -0.0242 199 THR A CB  
1721 O  OG1 . THR A 198 ? 0.0665 0.1118 0.1173 -0.0127 0.0113  0.0026  199 THR A OG1 
1722 C  CG2 . THR A 198 ? 0.0710 0.1360 0.1200 0.0145  0.0219  -0.0088 199 THR A CG2 
1723 N  N   . THR A 199 ? 0.0685 0.1330 0.1535 -0.0060 0.0357  -0.0189 200 THR A N   
1724 C  CA  . THR A 199 ? 0.0590 0.1368 0.1791 0.0058  0.0474  -0.0282 200 THR A CA  
1725 C  C   . THR A 199 ? 0.0991 0.1397 0.1659 -0.0006 0.0242  -0.0248 200 THR A C   
1726 O  O   . THR A 199 ? 0.0894 0.1354 0.1883 -0.0133 0.0324  -0.0417 200 THR A O   
1727 C  CB  . THR A 199 ? 0.0629 0.1531 0.1700 -0.0211 0.0540  -0.0178 200 THR A CB  
1728 O  OG1 . THR A 199 ? 0.1308 0.1419 0.1883 -0.0132 0.0255  -0.0049 200 THR A OG1 
1729 C  CG2 . THR A 199 ? 0.1577 0.1418 0.1573 -0.0331 0.0291  -0.0209 200 THR A CG2 
1730 N  N   . PRO A 200 ? 0.0893 0.1402 0.2029 -0.0118 0.0363  -0.0210 201 PRO A N   
1731 C  CA  . PRO A 200 ? 0.0622 0.1516 0.2134 -0.0206 0.0240  0.0040  201 PRO A CA  
1732 C  C   . PRO A 200 ? 0.0978 0.1511 0.1884 -0.0178 0.0111  0.0010  201 PRO A C   
1733 O  O   . PRO A 200 ? 0.1276 0.1987 0.2114 -0.0015 -0.0052 -0.0089 201 PRO A O   
1734 C  CB  . PRO A 200 ? 0.0807 0.1905 0.2149 -0.0111 0.0236  -0.0111 201 PRO A CB  
1735 C  CG  . PRO A 200 ? 0.0999 0.1806 0.2611 -0.0323 0.0279  -0.0124 201 PRO A CG  
1736 C  CD  . PRO A 200 ? 0.0763 0.1780 0.1940 0.0026  0.0337  -0.0390 201 PRO A CD  
1737 N  N   . PRO A 201 ? 0.0782 0.1720 0.2131 -0.0245 0.0132  -0.0187 202 PRO A N   
1738 C  CA  . PRO A 201 ? 0.1404 0.1389 0.1818 -0.0271 0.0106  -0.0121 202 PRO A CA  
1739 C  C   . PRO A 201 ? 0.0764 0.1200 0.2046 0.0002  0.0245  -0.0034 202 PRO A C   
1740 O  O   . PRO A 201 ? 0.0901 0.1424 0.2161 -0.0200 0.0124  -0.0147 202 PRO A O   
1741 C  CB  . PRO A 201 ? 0.1716 0.1432 0.2744 -0.0271 -0.0051 0.0152  202 PRO A CB  
1742 C  CG  . PRO A 201 ? 0.2228 0.1866 0.2920 0.0071  -0.0452 -0.0082 202 PRO A CG  
1743 C  CD  . PRO A 201 ? 0.1761 0.1438 0.2588 -0.0083 -0.0064 0.0095  202 PRO A CD  
1744 N  N   . LEU A 202 ? 0.0736 0.1037 0.2115 -0.0015 0.0117  0.0114  203 LEU A N   
1745 C  CA  . LEU A 202 ? 0.0714 0.1031 0.1911 0.0039  -0.0013 -0.0274 203 LEU A CA  
1746 C  C   . LEU A 202 ? 0.0465 0.1185 0.1868 -0.0075 0.0072  -0.0231 203 LEU A C   
1747 O  O   . LEU A 202 ? 0.0681 0.1307 0.1707 -0.0078 -0.0122 -0.0362 203 LEU A O   
1748 C  CB  . LEU A 202 ? 0.0503 0.1230 0.1861 0.0094  0.0020  -0.0296 203 LEU A CB  
1749 C  CG  . LEU A 202 ? 0.0424 0.1356 0.1954 -0.0024 0.0206  -0.0302 203 LEU A CG  
1750 C  CD1 . LEU A 202 ? 0.0437 0.1626 0.2663 0.0062  0.0096  -0.0341 203 LEU A CD1 
1751 C  CD2 . LEU A 202 ? 0.0584 0.1398 0.2149 -0.0108 -0.0046 -0.0287 203 LEU A CD2 
1752 N  N   A ASN A 203 ? 0.0710 0.1140 0.2169 0.0055  0.0061  -0.0263 204 ASN A N   
1753 N  N   B ASN A 203 ? 0.0954 0.0969 0.2180 -0.0005 0.0080  -0.0345 204 ASN A N   
1754 C  CA  A ASN A 203 ? 0.0820 0.1147 0.2125 -0.0089 0.0183  -0.0247 204 ASN A CA  
1755 C  CA  B ASN A 203 ? 0.1003 0.1051 0.2066 0.0001  0.0347  -0.0233 204 ASN A CA  
1756 C  C   A ASN A 203 ? 0.0457 0.1103 0.2043 0.0120  0.0110  -0.0530 204 ASN A C   
1757 C  C   B ASN A 203 ? 0.0563 0.0994 0.1954 0.0129  0.0159  -0.0453 204 ASN A C   
1758 O  O   A ASN A 203 ? 0.0674 0.1060 0.1747 -0.0013 -0.0033 -0.0303 204 ASN A O   
1759 O  O   B ASN A 203 ? 0.0845 0.1107 0.1419 -0.0020 -0.0113 -0.0325 204 ASN A O   
1760 C  CB  A ASN A 203 ? 0.0782 0.1186 0.2646 -0.0125 -0.0074 -0.0190 204 ASN A CB  
1761 C  CB  B ASN A 203 ? 0.1757 0.1027 0.2211 0.0308  0.0514  -0.0058 204 ASN A CB  
1762 C  CG  A ASN A 203 ? 0.1296 0.1240 0.2773 -0.0214 0.0044  -0.0344 204 ASN A CG  
1763 C  CG  B ASN A 203 ? 0.2224 0.1414 0.2992 0.0516  0.1155  0.0080  204 ASN A CG  
1764 O  OD1 A ASN A 203 ? 0.1513 0.2052 0.2726 -0.0022 0.0318  -0.0149 204 ASN A OD1 
1765 O  OD1 B ASN A 203 ? 0.3440 0.1776 0.2558 0.1017  0.1567  0.0578  204 ASN A OD1 
1766 N  ND2 A ASN A 203 ? 0.1989 0.1606 0.2842 0.0130  0.0285  0.0018  204 ASN A ND2 
1767 N  ND2 B ASN A 203 ? 0.3114 0.1780 0.3152 -0.0557 0.0441  0.0718  204 ASN A ND2 
1768 N  N   . GLU A 204 ? 0.0785 0.1295 0.1969 -0.0041 0.0048  -0.0513 205 GLU A N   
1769 C  CA  . GLU A 204 ? 0.0825 0.1247 0.1503 0.0125  -0.0253 -0.0519 205 GLU A CA  
1770 C  C   . GLU A 204 ? 0.1124 0.1098 0.1627 0.0147  -0.0361 -0.0405 205 GLU A C   
1771 O  O   . GLU A 204 ? 0.1552 0.1691 0.1724 0.0485  -0.0529 -0.0693 205 GLU A O   
1772 C  CB  . GLU A 204 ? 0.1097 0.1641 0.2049 0.0458  -0.0739 -0.0583 205 GLU A CB  
1773 C  CG  . GLU A 204 ? 0.0974 0.1539 0.2119 0.0293  -0.0518 -0.0365 205 GLU A CG  
1774 C  CD  . GLU A 204 ? 0.1200 0.1627 0.2024 0.0100  -0.0544 -0.0389 205 GLU A CD  
1775 O  OE1 . GLU A 204 ? 0.1588 0.1879 0.2873 0.0310  -0.1138 -0.0677 205 GLU A OE1 
1776 O  OE2 . GLU A 204 ? 0.0955 0.1639 0.2516 0.0107  -0.0641 -0.0465 205 GLU A OE2 
1777 N  N   . CYS A 205 ? 0.0672 0.0948 0.1541 -0.0024 -0.0248 -0.0145 206 CYS A N   
1778 C  CA  . CYS A 205 ? 0.0785 0.0990 0.1264 0.0086  -0.0074 -0.0159 206 CYS A CA  
1779 C  C   . CYS A 205 ? 0.0736 0.0902 0.1306 0.0110  -0.0010 -0.0189 206 CYS A C   
1780 O  O   . CYS A 205 ? 0.0878 0.0899 0.1725 0.0071  -0.0381 -0.0061 206 CYS A O   
1781 C  CB  . CYS A 205 ? 0.1138 0.1179 0.1237 -0.0042 0.0109  -0.0162 206 CYS A CB  
1782 S  SG  . CYS A 205 ? 0.1116 0.1345 0.1421 0.0084  -0.0011 -0.0209 206 CYS A SG  
1783 N  N   . VAL A 206 ? 0.0667 0.0921 0.1184 -0.0020 -0.0050 -0.0138 207 VAL A N   
1784 C  CA  . VAL A 206 ? 0.0728 0.0983 0.0990 -0.0048 -0.0095 -0.0144 207 VAL A CA  
1785 C  C   . VAL A 206 ? 0.0743 0.0872 0.0990 0.0138  -0.0082 -0.0167 207 VAL A C   
1786 O  O   . VAL A 206 ? 0.0974 0.1258 0.1168 0.0173  -0.0172 0.0044  207 VAL A O   
1787 C  CB  . VAL A 206 ? 0.0466 0.0913 0.1333 -0.0008 0.0036  -0.0210 207 VAL A CB  
1788 C  CG1 . VAL A 206 ? 0.0572 0.0996 0.1347 0.0003  -0.0223 -0.0252 207 VAL A CG1 
1789 C  CG2 . VAL A 206 ? 0.0658 0.1243 0.1429 0.0037  0.0186  -0.0167 207 VAL A CG2 
1790 N  N   . THR A 207 ? 0.0671 0.0899 0.1109 0.0019  -0.0013 -0.0142 208 THR A N   
1791 C  CA  . THR A 207 ? 0.0712 0.1005 0.1016 0.0055  -0.0057 -0.0117 208 THR A CA  
1792 C  C   . THR A 207 ? 0.0811 0.0863 0.0809 0.0044  -0.0013 -0.0005 208 THR A C   
1793 O  O   . THR A 207 ? 0.0829 0.0919 0.0839 0.0091  0.0026  -0.0021 208 THR A O   
1794 C  CB  . THR A 207 ? 0.0790 0.0904 0.1089 0.0072  0.0043  -0.0096 208 THR A CB  
1795 O  OG1 . THR A 207 ? 0.1252 0.1050 0.1188 0.0009  0.0138  -0.0290 208 THR A OG1 
1796 C  CG2 . THR A 207 ? 0.0967 0.1245 0.1382 0.0091  0.0391  0.0128  208 THR A CG2 
1797 N  N   . TRP A 208 ? 0.0717 0.0811 0.0869 0.0125  0.0044  -0.0076 209 TRP A N   
1798 C  CA  . TRP A 208 ? 0.0491 0.0857 0.0836 0.0065  0.0097  -0.0085 209 TRP A CA  
1799 C  C   . TRP A 208 ? 0.0500 0.0927 0.0678 0.0122  0.0122  0.0055  209 TRP A C   
1800 O  O   . TRP A 208 ? 0.0805 0.1078 0.0725 0.0051  0.0149  0.0050  209 TRP A O   
1801 C  CB  . TRP A 208 ? 0.0561 0.0991 0.0737 0.0121  0.0042  -0.0018 209 TRP A CB  
1802 C  CG  . TRP A 208 ? 0.0541 0.0860 0.0879 0.0100  0.0025  -0.0049 209 TRP A CG  
1803 C  CD1 . TRP A 208 ? 0.0550 0.0899 0.1062 0.0035  -0.0010 -0.0032 209 TRP A CD1 
1804 C  CD2 . TRP A 208 ? 0.0518 0.0829 0.0976 0.0127  0.0052  -0.0122 209 TRP A CD2 
1805 N  NE1 . TRP A 208 ? 0.0360 0.1100 0.1278 0.0021  0.0121  -0.0168 209 TRP A NE1 
1806 C  CE2 . TRP A 208 ? 0.0538 0.0868 0.1147 0.0179  0.0109  -0.0134 209 TRP A CE2 
1807 C  CE3 . TRP A 208 ? 0.0829 0.0888 0.0796 0.0089  -0.0127 -0.0098 209 TRP A CE3 
1808 C  CZ2 . TRP A 208 ? 0.0604 0.1125 0.1179 0.0326  0.0190  -0.0216 209 TRP A CZ2 
1809 C  CZ3 . TRP A 208 ? 0.0761 0.1005 0.0893 0.0135  0.0153  -0.0047 209 TRP A CZ3 
1810 C  CH2 . TRP A 208 ? 0.0834 0.0992 0.1005 0.0249  0.0279  -0.0181 209 TRP A CH2 
1811 N  N   . ILE A 209 ? 0.0425 0.0939 0.0750 0.0009  0.0166  0.0067  210 ILE A N   
1812 C  CA  . ILE A 209 ? 0.0401 0.0917 0.0910 0.0033  0.0256  0.0070  210 ILE A CA  
1813 C  C   . ILE A 209 ? 0.0482 0.0930 0.0735 0.0077  0.0142  0.0087  210 ILE A C   
1814 O  O   . ILE A 209 ? 0.0866 0.0973 0.0739 0.0033  0.0175  0.0040  210 ILE A O   
1815 C  CB  . ILE A 209 ? 0.0551 0.0933 0.1263 0.0087  0.0400  0.0173  210 ILE A CB  
1816 C  CG1 . ILE A 209 ? 0.1152 0.0856 0.1613 0.0315  0.0234  -0.0120 210 ILE A CG1 
1817 C  CG2 . ILE A 209 ? 0.0450 0.1342 0.1517 0.0102  0.0362  0.0297  210 ILE A CG2 
1818 C  CD1 . ILE A 209 ? 0.1091 0.1103 0.2224 0.0363  0.0188  -0.0012 210 ILE A CD1 
1819 N  N   . VAL A 210 ? 0.0604 0.0859 0.0940 0.0110  0.0316  0.0075  211 VAL A N   
1820 C  CA  . VAL A 210 ? 0.0709 0.0892 0.0728 -0.0015 0.0260  0.0096  211 VAL A CA  
1821 C  C   . VAL A 210 ? 0.0626 0.0829 0.0825 0.0060  0.0364  0.0117  211 VAL A C   
1822 O  O   . VAL A 210 ? 0.0899 0.1073 0.0868 -0.0010 0.0490  0.0109  211 VAL A O   
1823 C  CB  . VAL A 210 ? 0.0586 0.1019 0.1048 0.0013  0.0194  0.0082  211 VAL A CB  
1824 C  CG1 . VAL A 210 ? 0.0921 0.0906 0.1067 0.0120  0.0097  0.0053  211 VAL A CG1 
1825 C  CG2 . VAL A 210 ? 0.0789 0.1082 0.1150 -0.0115 0.0362  0.0084  211 VAL A CG2 
1826 N  N   . LEU A 211 ? 0.0395 0.1227 0.1078 -0.0071 0.0174  0.0111  212 LEU A N   
1827 C  CA  . LEU A 211 ? 0.0491 0.1114 0.1219 -0.0137 0.0234  0.0201  212 LEU A CA  
1828 C  C   . LEU A 211 ? 0.0611 0.0954 0.1201 -0.0179 0.0185  0.0058  212 LEU A C   
1829 O  O   . LEU A 211 ? 0.0676 0.1194 0.1111 0.0022  0.0168  0.0132  212 LEU A O   
1830 C  CB  . LEU A 211 ? 0.0617 0.1365 0.1388 -0.0132 0.0027  0.0300  212 LEU A CB  
1831 C  CG  . LEU A 211 ? 0.0761 0.1299 0.1425 -0.0083 0.0021  0.0193  212 LEU A CG  
1832 C  CD1 . LEU A 211 ? 0.0603 0.1952 0.1735 -0.0121 -0.0066 0.0376  212 LEU A CD1 
1833 C  CD2 . LEU A 211 ? 0.0924 0.1640 0.1549 -0.0051 0.0298  0.0103  212 LEU A CD2 
1834 N  N   . LYS A 212 ? 0.0710 0.1240 0.1190 -0.0178 0.0231  0.0179  213 LYS A N   
1835 C  CA  . LYS A 212 ? 0.0985 0.1333 0.1103 -0.0119 0.0247  0.0230  213 LYS A CA  
1836 C  C   . LYS A 212 ? 0.0790 0.1152 0.1103 -0.0207 0.0181  0.0367  213 LYS A C   
1837 O  O   . LYS A 212 ? 0.1113 0.1209 0.1690 -0.0006 -0.0069 0.0242  213 LYS A O   
1838 C  CB  . LYS A 212 ? 0.1466 0.1596 0.1278 -0.0456 0.0444  0.0266  213 LYS A CB  
1839 C  CG  . LYS A 212 ? 0.1967 0.1804 0.1989 -0.0258 0.0409  0.0610  213 LYS A CG  
1840 C  CD  . LYS A 212 ? 0.4271 0.3281 0.2260 -0.1389 0.0876  0.0787  213 LYS A CD  
1841 C  CE  . LYS A 212 ? 0.4219 0.3413 0.3362 -0.0709 0.0812  0.1373  213 LYS A CE  
1842 N  NZ  . LYS A 212 ? 0.4942 0.6621 0.4427 -0.1195 0.1263  0.2061  213 LYS A NZ  
1843 N  N   A GLU A 213 ? 0.0428 0.1375 0.1463 -0.0193 0.0091  0.0184  214 GLU A N   
1844 N  N   B GLU A 213 ? 0.0608 0.1310 0.1279 -0.0097 0.0155  0.0190  214 GLU A N   
1845 C  CA  A GLU A 213 ? 0.0642 0.1177 0.1568 -0.0134 0.0137  0.0139  214 GLU A CA  
1846 C  CA  B GLU A 213 ? 0.0753 0.1157 0.1483 -0.0115 0.0125  0.0175  214 GLU A CA  
1847 C  C   A GLU A 213 ? 0.0546 0.0994 0.1412 -0.0138 0.0029  0.0210  214 GLU A C   
1848 C  C   B GLU A 213 ? 0.0568 0.0992 0.1372 -0.0133 0.0027  0.0223  214 GLU A C   
1849 O  O   A GLU A 213 ? 0.0649 0.1053 0.1438 -0.0100 -0.0009 0.0292  214 GLU A O   
1850 O  O   B GLU A 213 ? 0.0606 0.1044 0.1444 -0.0149 0.0031  0.0298  214 GLU A O   
1851 C  CB  A GLU A 213 ? 0.0683 0.1531 0.1676 -0.0018 0.0144  0.0098  214 GLU A CB  
1852 C  CB  B GLU A 213 ? 0.0820 0.1296 0.1394 -0.0156 -0.0046 0.0395  214 GLU A CB  
1853 C  CG  A GLU A 213 ? 0.0587 0.1856 0.2009 -0.0119 0.0067  -0.0072 214 GLU A CG  
1854 C  CG  B GLU A 213 ? 0.0766 0.1466 0.2060 -0.0238 -0.0436 0.0124  214 GLU A CG  
1855 C  CD  A GLU A 213 ? 0.0694 0.1612 0.2831 0.0026  0.0034  -0.0335 214 GLU A CD  
1856 C  CD  B GLU A 213 ? 0.0773 0.1538 0.2610 -0.0190 -0.0375 0.0024  214 GLU A CD  
1857 O  OE1 A GLU A 213 ? 0.1538 0.1884 0.1806 -0.0348 0.0166  0.0065  214 GLU A OE1 
1858 O  OE1 B GLU A 213 ? 0.0696 0.1731 0.1727 -0.0136 -0.0052 0.0053  214 GLU A OE1 
1859 O  OE2 A GLU A 213 ? 0.1337 0.2212 0.3086 -0.0270 -0.0468 0.0116  214 GLU A OE2 
1860 O  OE2 B GLU A 213 ? 0.1902 0.1502 0.3866 -0.0717 -0.0829 0.0189  214 GLU A OE2 
1861 N  N   . PRO A 214 ? 0.0869 0.1050 0.1155 -0.0133 -0.0033 0.0194  215 PRO A N   
1862 C  CA  . PRO A 214 ? 0.0764 0.1179 0.1127 0.0021  -0.0004 0.0088  215 PRO A CA  
1863 C  C   . PRO A 214 ? 0.0681 0.1226 0.1492 0.0074  -0.0083 0.0059  215 PRO A C   
1864 O  O   . PRO A 214 ? 0.0888 0.1866 0.1757 -0.0417 -0.0244 0.0405  215 PRO A O   
1865 C  CB  . PRO A 214 ? 0.0946 0.0884 0.1769 -0.0082 -0.0087 -0.0011 215 PRO A CB  
1866 C  CG  . PRO A 214 ? 0.1404 0.1662 0.2056 0.0089  0.0301  0.0186  215 PRO A CG  
1867 C  CD  . PRO A 214 ? 0.1455 0.0906 0.1807 0.0036  0.0285  0.0255  215 PRO A CD  
1868 N  N   . ILE A 215 ? 0.0935 0.1017 0.1273 -0.0055 -0.0187 -0.0105 216 ILE A N   
1869 C  CA  . ILE A 215 ? 0.1040 0.1060 0.1338 0.0002  -0.0292 -0.0238 216 ILE A CA  
1870 C  C   . ILE A 215 ? 0.0917 0.1146 0.1217 0.0137  -0.0299 -0.0155 216 ILE A C   
1871 O  O   . ILE A 215 ? 0.0899 0.1061 0.1668 0.0044  -0.0265 -0.0159 216 ILE A O   
1872 C  CB  . ILE A 215 ? 0.1285 0.1192 0.1546 0.0247  -0.0419 -0.0054 216 ILE A CB  
1873 C  CG1 . ILE A 215 ? 0.1538 0.1039 0.1385 -0.0017 -0.0181 0.0051  216 ILE A CG1 
1874 C  CG2 . ILE A 215 ? 0.2330 0.1186 0.1650 0.0604  -0.0682 -0.0286 216 ILE A CG2 
1875 C  CD1 . ILE A 215 ? 0.2564 0.1037 0.1561 -0.0254 -0.0321 0.0124  216 ILE A CD1 
1876 N  N   . SER A 216 ? 0.1095 0.1062 0.1579 -0.0042 -0.0260 -0.0189 217 SER A N   
1877 C  CA  A SER A 216 ? 0.1199 0.1014 0.1449 -0.0006 -0.0245 -0.0130 217 SER A CA  
1878 C  CA  B SER A 216 ? 0.1177 0.1001 0.1498 -0.0066 -0.0243 -0.0147 217 SER A CA  
1879 C  C   . SER A 216 ? 0.1166 0.0861 0.1479 -0.0040 -0.0365 -0.0068 217 SER A C   
1880 O  O   . SER A 216 ? 0.0985 0.1292 0.1625 0.0060  -0.0298 0.0053  217 SER A O   
1881 C  CB  A SER A 216 ? 0.1994 0.0696 0.1692 -0.0234 0.0239  -0.0079 217 SER A CB  
1882 C  CB  B SER A 216 ? 0.1545 0.1226 0.2100 -0.0348 -0.0288 0.0062  217 SER A CB  
1883 O  OG  A SER A 216 ? 0.1659 0.1347 0.1472 -0.0253 -0.0059 -0.0107 217 SER A OG  
1884 O  OG  B SER A 216 ? 0.2120 0.1664 0.2366 -0.0002 -0.0395 -0.0110 217 SER A OG  
1885 N  N   . VAL A 217 ? 0.1103 0.0861 0.1311 -0.0149 -0.0230 -0.0131 218 VAL A N   
1886 C  CA  . VAL A 217 ? 0.1258 0.0888 0.1371 -0.0122 -0.0162 -0.0048 218 VAL A CA  
1887 C  C   . VAL A 217 ? 0.1210 0.0816 0.1383 -0.0212 -0.0245 0.0042  218 VAL A C   
1888 O  O   . VAL A 217 ? 0.1280 0.0971 0.1183 -0.0160 -0.0231 0.0040  218 VAL A O   
1889 C  CB  . VAL A 217 ? 0.1328 0.0881 0.1542 -0.0223 -0.0201 -0.0063 218 VAL A CB  
1890 C  CG1 . VAL A 217 ? 0.1739 0.0938 0.1407 -0.0089 -0.0370 -0.0093 218 VAL A CG1 
1891 C  CG2 . VAL A 217 ? 0.1400 0.1068 0.2128 -0.0310 -0.0376 0.0243  218 VAL A CG2 
1892 N  N   . SER A 218 ? 0.1515 0.0933 0.1262 -0.0182 -0.0341 -0.0108 219 SER A N   
1893 C  CA  . SER A 218 ? 0.1572 0.1008 0.1480 -0.0154 -0.0241 -0.0230 219 SER A CA  
1894 C  C   . SER A 218 ? 0.1554 0.0927 0.1123 -0.0207 -0.0251 -0.0051 219 SER A C   
1895 O  O   . SER A 218 ? 0.1744 0.1001 0.1256 -0.0298 -0.0194 -0.0006 219 SER A O   
1896 C  CB  . SER A 218 ? 0.2322 0.1071 0.1341 -0.0170 -0.0432 0.0011  219 SER A CB  
1897 O  OG  . SER A 218 ? 0.1972 0.1210 0.1546 -0.0307 -0.0488 -0.0052 219 SER A OG  
1898 N  N   A SER A 219 ? 0.1646 0.0947 0.1428 -0.0029 -0.0239 -0.0033 220 SER A N   
1899 N  N   B SER A 219 ? 0.1710 0.0927 0.1437 -0.0071 -0.0290 -0.0079 220 SER A N   
1900 C  CA  A SER A 219 ? 0.1632 0.0974 0.1615 -0.0220 -0.0034 0.0103  220 SER A CA  
1901 C  CA  B SER A 219 ? 0.1762 0.0834 0.1701 -0.0294 0.0034  0.0012  220 SER A CA  
1902 C  C   A SER A 219 ? 0.2114 0.0768 0.1626 -0.0194 -0.0094 0.0079  220 SER A C   
1903 C  C   B SER A 219 ? 0.2073 0.0886 0.1736 -0.0336 -0.0119 0.0108  220 SER A C   
1904 O  O   A SER A 219 ? 0.2087 0.1096 0.1918 -0.0122 0.0189  0.0154  220 SER A O   
1905 O  O   B SER A 219 ? 0.2098 0.0805 0.1860 -0.0196 0.0158  0.0100  220 SER A O   
1906 C  CB  A SER A 219 ? 0.1745 0.1100 0.1617 -0.0114 0.0089  0.0000  220 SER A CB  
1907 C  CB  B SER A 219 ? 0.1843 0.0931 0.2037 -0.0143 0.0095  -0.0022 220 SER A CB  
1908 O  OG  A SER A 219 ? 0.1893 0.0555 0.1675 0.0008  0.0025  -0.0188 220 SER A OG  
1909 O  OG  B SER A 219 ? 0.1952 0.1409 0.2236 0.0023  0.0301  0.0089  220 SER A OG  
1910 N  N   . GLU A 220 ? 0.2132 0.1119 0.1344 -0.0078 -0.0035 -0.0171 221 GLU A N   
1911 C  CA  . GLU A 220 ? 0.2353 0.1256 0.1778 -0.0089 0.0027  -0.0032 221 GLU A CA  
1912 C  C   . GLU A 220 ? 0.2301 0.1204 0.1335 0.0050  -0.0102 0.0064  221 GLU A C   
1913 O  O   . GLU A 220 ? 0.2610 0.1492 0.1418 0.0013  0.0299  -0.0194 221 GLU A O   
1914 C  CB  . GLU A 220 ? 0.2833 0.1823 0.1561 -0.0351 -0.0194 -0.0478 221 GLU A CB  
1915 C  CG  . GLU A 220 ? 0.3806 0.2033 0.2432 -0.0672 -0.0408 -0.0782 221 GLU A CG  
1916 C  CD  . GLU A 220 ? 0.3006 0.2438 0.3291 -0.0847 -0.0433 -0.0982 221 GLU A CD  
1917 O  OE1 . GLU A 220 ? 0.3444 0.2461 0.3542 -0.1441 -0.0044 -0.0976 221 GLU A OE1 
1918 O  OE2 . GLU A 220 ? 0.5128 0.3186 0.4736 -0.1932 0.1204  -0.1923 221 GLU A OE2 
1919 N  N   . GLN A 221 ? 0.2039 0.0946 0.1329 -0.0139 -0.0278 -0.0094 222 GLN A N   
1920 C  CA  . GLN A 221 ? 0.1858 0.0939 0.1488 -0.0183 -0.0066 -0.0044 222 GLN A CA  
1921 C  C   . GLN A 221 ? 0.1631 0.0827 0.1558 -0.0074 -0.0071 0.0063  222 GLN A C   
1922 O  O   . GLN A 221 ? 0.2081 0.1125 0.1305 -0.0281 0.0041  0.0147  222 GLN A O   
1923 C  CB  . GLN A 221 ? 0.1849 0.1211 0.1172 -0.0013 -0.0221 -0.0133 222 GLN A CB  
1924 C  CG  . GLN A 221 ? 0.1969 0.1143 0.1193 -0.0017 -0.0355 -0.0098 222 GLN A CG  
1925 C  CD  . GLN A 221 ? 0.1910 0.0721 0.1324 -0.0100 -0.0252 -0.0034 222 GLN A CD  
1926 O  OE1 . GLN A 221 ? 0.1822 0.1037 0.1324 -0.0075 -0.0376 0.0098  222 GLN A OE1 
1927 N  NE2 . GLN A 221 ? 0.2042 0.1028 0.1474 -0.0172 -0.0622 0.0163  222 GLN A NE2 
1928 N  N   A VAL A 222 ? 0.1603 0.1198 0.1237 -0.0085 -0.0135 0.0094  223 VAL A N   
1929 N  N   B VAL A 222 ? 0.1781 0.1173 0.1429 -0.0301 0.0032  0.0318  223 VAL A N   
1930 C  CA  A VAL A 222 ? 0.1540 0.1150 0.1233 -0.0085 0.0078  0.0254  223 VAL A CA  
1931 C  CA  B VAL A 222 ? 0.1624 0.1515 0.1412 -0.0150 0.0455  0.0381  223 VAL A CA  
1932 C  C   A VAL A 222 ? 0.1896 0.1209 0.1085 -0.0097 0.0187  0.0135  223 VAL A C   
1933 C  C   B VAL A 222 ? 0.1997 0.1264 0.1363 -0.0310 0.0540  0.0114  223 VAL A C   
1934 O  O   A VAL A 222 ? 0.2120 0.1057 0.1154 -0.0295 0.0099  0.0221  223 VAL A O   
1935 O  O   B VAL A 222 ? 0.1538 0.1434 0.1592 -0.0004 0.0348  0.0221  223 VAL A O   
1936 C  CB  A VAL A 222 ? 0.1763 0.1358 0.1186 -0.0013 -0.0147 0.0170  223 VAL A CB  
1937 C  CB  B VAL A 222 ? 0.2260 0.2195 0.1367 -0.0221 0.0505  0.0584  223 VAL A CB  
1938 C  CG1 A VAL A 222 ? 0.1494 0.1286 0.1419 -0.0155 -0.0282 0.0326  223 VAL A CG1 
1939 C  CG1 B VAL A 222 ? 0.2606 0.3710 0.1711 -0.0233 0.0040  0.0560  223 VAL A CG1 
1940 C  CG2 A VAL A 222 ? 0.1791 0.1267 0.1444 -0.0064 -0.0100 -0.0055 223 VAL A CG2 
1941 C  CG2 B VAL A 222 ? 0.1678 0.3003 0.2299 -0.0544 0.0798  0.0466  223 VAL A CG2 
1942 N  N   . LEU A 223 ? 0.2408 0.1152 0.1259 -0.0136 0.0223  0.0084  224 LEU A N   
1943 C  CA  . LEU A 223 ? 0.2195 0.1270 0.1911 -0.0188 0.0522  -0.0057 224 LEU A CA  
1944 C  C   . LEU A 223 ? 0.1946 0.1558 0.1442 -0.0336 0.0407  -0.0092 224 LEU A C   
1945 O  O   . LEU A 223 ? 0.1782 0.1753 0.1722 -0.0008 0.0523  -0.0068 224 LEU A O   
1946 C  CB  . LEU A 223 ? 0.2471 0.1476 0.1768 -0.0023 0.0269  -0.0248 224 LEU A CB  
1947 C  CG  . LEU A 223 ? 0.2658 0.1842 0.2421 -0.0543 0.0166  0.0022  224 LEU A CG  
1948 C  CD2 . LEU A 223 ? 0.2685 0.2221 0.2496 -0.0386 0.0177  0.0027  224 LEU A CD2 
1949 N  N   . LYS A 224 ? 0.2608 0.1411 0.1470 0.0074  0.0136  0.0173  225 LYS A N   
1950 C  CA  . LYS A 224 ? 0.2222 0.1867 0.1170 -0.0167 0.0482  0.0083  225 LYS A CA  
1951 C  C   . LYS A 224 ? 0.1811 0.1661 0.1110 0.0135  0.0423  -0.0063 225 LYS A C   
1952 O  O   . LYS A 224 ? 0.2330 0.1701 0.1254 -0.0195 0.0549  -0.0005 225 LYS A O   
1953 C  CB  . LYS A 224 ? 0.2453 0.2409 0.1603 0.0189  0.0200  0.0497  225 LYS A CB  
1954 C  CG  . LYS A 224 ? 0.2556 0.3783 0.2126 -0.0256 -0.0068 0.0175  225 LYS A CG  
1955 C  CD  . LYS A 224 ? 0.3305 0.5593 0.3592 0.0204  -0.0886 0.0150  225 LYS A CD  
1956 N  N   . PHE A 225 ? 0.2237 0.1312 0.1110 -0.0174 0.0495  0.0098  226 PHE A N   
1957 C  CA  . PHE A 225 ? 0.2240 0.1291 0.1045 -0.0141 0.0662  -0.0087 226 PHE A CA  
1958 C  C   . PHE A 225 ? 0.2185 0.1401 0.0842 -0.0339 0.0516  -0.0001 226 PHE A C   
1959 O  O   . PHE A 225 ? 0.1923 0.1345 0.1114 -0.0375 0.0435  -0.0194 226 PHE A O   
1960 C  CB  . PHE A 225 ? 0.2207 0.1321 0.1018 -0.0038 0.0642  0.0209  226 PHE A CB  
1961 C  CG  . PHE A 225 ? 0.2069 0.0992 0.1373 -0.0316 0.0624  -0.0116 226 PHE A CG  
1962 C  CD1 . PHE A 225 ? 0.2879 0.2159 0.1380 0.0339  0.0506  0.0337  226 PHE A CD1 
1963 C  CD2 . PHE A 225 ? 0.2263 0.1933 0.1548 -0.0316 0.0326  -0.0450 226 PHE A CD2 
1964 C  CE1 . PHE A 225 ? 0.2696 0.1918 0.1794 0.0171  0.0563  0.0328  226 PHE A CE1 
1965 C  CE2 . PHE A 225 ? 0.2069 0.1994 0.1902 -0.0067 0.0220  -0.0495 226 PHE A CE2 
1966 C  CZ  . PHE A 225 ? 0.2489 0.1458 0.2152 -0.0182 0.0037  -0.0646 226 PHE A CZ  
1967 N  N   . ARG A 226 ? 0.1935 0.1238 0.1091 -0.0146 0.0496  -0.0053 227 ARG A N   
1968 C  CA  . ARG A 226 ? 0.2067 0.1347 0.1203 -0.0232 0.0659  0.0066  227 ARG A CA  
1969 C  C   . ARG A 226 ? 0.2149 0.1415 0.1148 -0.0285 0.0586  0.0139  227 ARG A C   
1970 O  O   . ARG A 226 ? 0.2076 0.1789 0.1414 -0.0315 0.0467  -0.0132 227 ARG A O   
1971 C  CB  . ARG A 226 ? 0.2495 0.1324 0.1041 0.0032  0.0436  0.0172  227 ARG A CB  
1972 C  CG  . ARG A 226 ? 0.2289 0.1277 0.1071 -0.0219 0.0489  0.0140  227 ARG A CG  
1973 C  CD  . ARG A 226 ? 0.2679 0.1298 0.1251 0.0023  0.0546  0.0198  227 ARG A CD  
1974 N  NE  . ARG A 226 ? 0.2248 0.1211 0.0985 -0.0366 0.0139  0.0127  227 ARG A NE  
1975 C  CZ  . ARG A 226 ? 0.1917 0.1286 0.1254 -0.0342 0.0299  -0.0242 227 ARG A CZ  
1976 N  NH1 . ARG A 226 ? 0.2979 0.1801 0.1894 -0.0696 -0.0265 -0.0607 227 ARG A NH1 
1977 N  NH2 . ARG A 226 ? 0.2395 0.1406 0.1384 -0.0641 0.0522  -0.0059 227 ARG A NH2 
1978 N  N   . LYS A 227 ? 0.2113 0.1521 0.0904 -0.0341 0.0385  -0.0181 228 LYS A N   
1979 C  CA  . LYS A 227 ? 0.2463 0.1621 0.0908 -0.0413 0.0498  -0.0234 228 LYS A CA  
1980 C  C   . LYS A 227 ? 0.3142 0.1575 0.0843 -0.0354 0.0583  -0.0074 228 LYS A C   
1981 O  O   . LYS A 227 ? 0.3128 0.1861 0.0957 -0.0659 0.0659  -0.0244 228 LYS A O   
1982 C  CB  . LYS A 227 ? 0.2335 0.2023 0.0992 -0.0469 0.0487  -0.0205 228 LYS A CB  
1983 C  CG  . LYS A 227 ? 0.2434 0.2114 0.1569 -0.0631 0.0458  -0.0368 228 LYS A CG  
1984 C  CD  . LYS A 227 ? 0.3054 0.2710 0.2188 -0.0737 -0.0258 -0.0182 228 LYS A CD  
1985 C  CE  . LYS A 227 ? 0.5141 0.4873 0.2336 -0.1078 0.0247  -0.0540 228 LYS A CE  
1986 N  NZ  . LYS A 227 ? 0.6366 0.6827 0.4606 -0.1287 -0.0871 -0.2130 228 LYS A NZ  
1987 N  N   . LEU A 228 ? 0.2570 0.1329 0.0958 -0.0342 0.0561  -0.0125 229 LEU A N   
1988 C  CA  . LEU A 228 ? 0.2863 0.1295 0.1082 -0.0325 0.0446  -0.0195 229 LEU A CA  
1989 C  C   . LEU A 228 ? 0.2966 0.1505 0.0881 -0.0498 0.0612  -0.0192 229 LEU A C   
1990 O  O   . LEU A 228 ? 0.2404 0.1485 0.1182 -0.0425 0.0807  -0.0144 229 LEU A O   
1991 C  CB  . LEU A 228 ? 0.3072 0.1611 0.0944 -0.0536 0.0915  -0.0155 229 LEU A CB  
1992 C  CG  . LEU A 228 ? 0.3069 0.1708 0.1001 -0.0355 0.0583  0.0067  229 LEU A CG  
1993 C  CD1 . LEU A 228 ? 0.3161 0.1714 0.1091 -0.0608 0.0536  -0.0194 229 LEU A CD1 
1994 C  CD2 . LEU A 228 ? 0.3009 0.1939 0.1275 -0.0434 0.0429  0.0348  229 LEU A CD2 
1995 N  N   . ASN A 229 ? 0.2952 0.1801 0.1080 -0.0823 0.0732  -0.0201 230 ASN A N   
1996 C  CA  . ASN A 229 ? 0.2949 0.2034 0.1021 -0.0863 0.0943  -0.0532 230 ASN A CA  
1997 C  C   . ASN A 229 ? 0.2457 0.1879 0.1477 -0.1030 0.1068  -0.0372 230 ASN A C   
1998 O  O   . ASN A 229 ? 0.3692 0.1795 0.1222 -0.1037 0.0995  -0.0323 230 ASN A O   
1999 C  CB  . ASN A 229 ? 0.3630 0.2357 0.1217 -0.1250 0.1122  -0.0375 230 ASN A CB  
2000 C  CG  . ASN A 229 ? 0.4085 0.2270 0.1042 -0.0895 0.0854  -0.0337 230 ASN A CG  
2001 O  OD1 . ASN A 229 ? 0.5105 0.2526 0.1268 -0.0675 0.1307  -0.0305 230 ASN A OD1 
2002 N  ND2 . ASN A 229 ? 0.3490 0.2191 0.1772 -0.0928 0.0780  -0.0444 230 ASN A ND2 
2003 N  N   . PHE A 230 ? 0.2522 0.2089 0.1247 -0.1172 0.1174  -0.0502 231 PHE A N   
2004 C  CA  . PHE A 230 ? 0.2498 0.2212 0.1500 -0.1516 0.0956  -0.0311 231 PHE A CA  
2005 C  C   . PHE A 230 ? 0.3726 0.1834 0.1592 -0.1190 0.1606  -0.0299 231 PHE A C   
2006 O  O   . PHE A 230 ? 0.3078 0.1998 0.1661 -0.1231 0.1326  -0.0383 231 PHE A O   
2007 C  CB  . PHE A 230 ? 0.2737 0.2288 0.1471 -0.1348 0.1316  -0.0694 231 PHE A CB  
2008 C  CG  . PHE A 230 ? 0.2382 0.2140 0.1594 -0.1262 0.1135  -0.0526 231 PHE A CG  
2009 C  CD1 . PHE A 230 ? 0.2854 0.2237 0.1262 -0.1140 0.1167  -0.0582 231 PHE A CD1 
2010 C  CD2 . PHE A 230 ? 0.2265 0.2172 0.1323 -0.1137 0.0660  -0.0507 231 PHE A CD2 
2011 C  CE1 . PHE A 230 ? 0.2570 0.1953 0.1482 -0.0937 0.1201  -0.0433 231 PHE A CE1 
2012 C  CE2 . PHE A 230 ? 0.2537 0.1973 0.1197 -0.0816 0.0722  -0.0540 231 PHE A CE2 
2013 C  CZ  . PHE A 230 ? 0.2168 0.1938 0.1335 -0.0919 0.0728  -0.0461 231 PHE A CZ  
2014 N  N   A ASN A 231 ? 0.2977 0.2794 0.1254 -0.1004 0.1359  -0.0554 232 ASN A N   
2015 N  N   B ASN A 231 ? 0.4481 0.2031 0.1981 -0.1031 0.1109  -0.1014 232 ASN A N   
2016 C  CA  A ASN A 231 ? 0.1890 0.1794 0.1584 -0.0506 0.0693  -0.0319 232 ASN A CA  
2017 C  CA  B ASN A 231 ? 0.3633 0.2148 0.2219 -0.0767 0.1687  -0.0642 232 ASN A CA  
2018 C  C   A ASN A 231 ? 0.1371 0.2841 0.0793 -0.0255 0.0284  -0.0461 232 ASN A C   
2019 C  C   B ASN A 231 ? 0.4510 0.1286 0.2438 -0.0782 0.1778  -0.0125 232 ASN A C   
2020 O  O   A ASN A 231 ? 0.1833 0.2320 0.1209 -0.0732 0.0445  -0.0353 232 ASN A O   
2021 O  O   B ASN A 231 ? 0.4530 0.1911 0.1753 -0.1217 0.1112  -0.0352 232 ASN A O   
2022 C  CB  A ASN A 231 ? 0.2430 0.1650 0.2557 -0.0465 0.1356  -0.0374 232 ASN A CB  
2023 C  CB  B ASN A 231 ? 0.4242 0.1962 0.1541 -0.0936 0.1770  -0.0440 232 ASN A CB  
2024 C  CG  A ASN A 231 ? 0.2943 0.1361 0.2306 -0.0178 0.0625  -0.0103 232 ASN A CG  
2025 C  CG  B ASN A 231 ? 0.3043 0.3252 0.1849 -0.0727 0.1679  -0.0753 232 ASN A CG  
2026 O  OD1 A ASN A 231 ? 0.4044 0.1551 0.1948 -0.0820 0.1749  -0.0772 232 ASN A OD1 
2027 O  OD1 B ASN A 231 ? 0.3463 0.2940 0.2075 -0.0436 0.1362  -0.1101 232 ASN A OD1 
2028 N  ND2 A ASN A 231 ? 0.1585 0.2057 0.2164 0.0348  0.1503  -0.0241 232 ASN A ND2 
2029 N  ND2 B ASN A 231 ? 0.3838 0.3245 0.1592 -0.1597 0.0822  -0.0796 232 ASN A ND2 
2030 N  N   A GLY A 232 ? 0.1449 0.2070 0.1879 0.0653  -0.0044 0.0231  233 GLY A N   
2031 N  N   B GLY A 232 ? 0.3206 0.1849 0.2326 -0.0820 0.1641  -0.0993 233 GLY A N   
2032 C  CA  A GLY A 232 ? 0.0888 0.2272 0.1514 0.0244  0.0365  0.0463  233 GLY A CA  
2033 C  CA  B GLY A 232 ? 0.5292 0.3441 0.2317 0.0012  0.0063  -0.1385 233 GLY A CA  
2034 C  C   A GLY A 232 ? 0.1243 0.2072 0.1855 0.0469  0.0052  0.0569  233 GLY A C   
2035 C  C   B GLY A 232 ? 0.4624 0.2955 0.2338 -0.0653 0.0653  -0.1093 233 GLY A C   
2036 O  O   A GLY A 232 ? 0.1298 0.2587 0.2596 0.0855  0.1089  0.0910  233 GLY A O   
2037 O  O   B GLY A 232 ? 0.5757 0.1904 0.3991 -0.1342 0.1052  -0.0310 233 GLY A O   
2038 N  N   A GLU A 233 ? 0.0500 0.2121 0.1741 0.0563  0.0282  0.0262  234 GLU A N   
2039 N  N   B GLU A 233 ? 0.4156 0.2746 0.1566 -0.1240 0.0876  -0.0809 234 GLU A N   
2040 C  CA  A GLU A 233 ? 0.1645 0.2206 0.1597 0.0378  0.0065  0.0512  234 GLU A CA  
2041 C  CA  B GLU A 233 ? 0.3608 0.3229 0.1574 -0.0798 0.1372  -0.1099 234 GLU A CA  
2042 C  C   A GLU A 233 ? 0.2489 0.1867 0.1471 0.0606  0.1024  0.0730  234 GLU A C   
2043 C  C   B GLU A 233 ? 0.3588 0.2837 0.1767 -0.0942 0.1077  -0.0724 234 GLU A C   
2044 O  O   A GLU A 233 ? 0.2839 0.1904 0.2095 0.0780  0.0436  0.0697  234 GLU A O   
2045 O  O   B GLU A 233 ? 0.3590 0.4805 0.1601 -0.2067 0.1568  -0.0571 234 GLU A O   
2046 C  CB  A GLU A 233 ? 0.1412 0.2679 0.2042 0.0275  -0.0517 0.0160  234 GLU A CB  
2047 C  CB  B GLU A 233 ? 0.2834 0.3917 0.1100 -0.1372 0.1485  -0.0196 234 GLU A CB  
2048 C  CG  A GLU A 233 ? 0.3069 0.3609 0.1252 -0.0384 -0.0443 0.0958  234 GLU A CG  
2049 C  CG  B GLU A 233 ? 0.2025 0.5413 0.2782 -0.1257 0.0543  -0.1187 234 GLU A CG  
2050 C  CD  A GLU A 233 ? 0.3441 0.4974 0.2353 -0.0116 -0.0768 0.0653  234 GLU A CD  
2051 C  CD  B GLU A 233 ? 0.3290 0.5576 0.2724 -0.1575 0.0741  -0.0739 234 GLU A CD  
2052 O  OE1 A GLU A 233 ? 0.5019 0.5643 0.3305 -0.0832 0.0738  0.1404  234 GLU A OE1 
2053 O  OE1 B GLU A 233 ? 0.4789 0.5331 0.3776 -0.1147 0.1030  0.0483  234 GLU A OE1 
2054 O  OE2 A GLU A 233 ? 0.6128 0.3806 0.2602 -0.1531 -0.1641 0.0998  234 GLU A OE2 
2055 O  OE2 B GLU A 233 ? 0.1832 0.6327 0.3430 -0.1372 0.0668  -0.1362 234 GLU A OE2 
2056 N  N   A GLY A 234 ? 0.3396 0.2428 0.1313 0.1265  0.0890  0.0364  235 GLY A N   
2057 N  N   B GLY A 234 ? 0.4686 0.2746 0.2858 -0.0502 0.1333  -0.0640 235 GLY A N   
2058 C  CA  A GLY A 234 ? 0.3148 0.2376 0.1712 0.1267  0.0725  0.1004  235 GLY A CA  
2059 C  CA  B GLY A 234 ? 0.3813 0.3327 0.3647 -0.0750 0.0642  -0.0741 235 GLY A CA  
2060 C  C   A GLY A 234 ? 0.2605 0.2724 0.2060 0.1410  0.0759  0.0534  235 GLY A C   
2061 C  C   B GLY A 234 ? 0.5687 0.4060 0.3213 -0.1574 -0.0062 0.0264  235 GLY A C   
2062 O  O   A GLY A 234 ? 0.2658 0.4086 0.3252 0.2174  0.1543  0.0868  235 GLY A O   
2063 O  O   B GLY A 234 ? 0.7028 0.3160 0.3313 -0.0819 0.2638  -0.0400 235 GLY A O   
2064 N  N   A GLU A 235 ? 0.2928 0.2068 0.2625 0.1621  0.1125  0.1129  236 GLU A N   
2065 N  N   B GLU A 235 ? 0.5357 0.3563 0.2908 -0.1559 0.1030  -0.0789 236 GLU A N   
2066 C  CA  A GLU A 235 ? 0.3227 0.1439 0.2433 0.1149  0.0864  0.1228  236 GLU A CA  
2067 C  CA  B GLU A 235 ? 0.4368 0.2191 0.3622 -0.1012 0.1625  -0.0537 236 GLU A CA  
2068 C  C   A GLU A 235 ? 0.1625 0.1812 0.2497 0.0995  0.0848  0.1354  236 GLU A C   
2069 C  C   B GLU A 235 ? 0.4688 0.1963 0.3929 -0.0519 0.1580  -0.0681 236 GLU A C   
2070 O  O   A GLU A 235 ? 0.1159 0.4143 0.2879 0.1142  0.0686  0.1639  236 GLU A O   
2071 O  O   B GLU A 235 ? 0.5911 0.2295 0.4622 -0.1258 0.1736  -0.0462 236 GLU A O   
2072 C  CB  A GLU A 235 ? 0.2449 0.1975 0.3024 0.1414  0.0530  0.0730  236 GLU A CB  
2073 C  CB  B GLU A 235 ? 0.4683 0.2455 0.3082 -0.1280 0.1997  -0.0132 236 GLU A CB  
2074 C  CG  A GLU A 235 ? 0.2692 0.2023 0.2896 0.1016  0.1139  0.0646  236 GLU A CG  
2075 C  CG  B GLU A 235 ? 0.5289 0.1631 0.5026 -0.0595 0.1541  -0.0193 236 GLU A CG  
2076 C  CD  A GLU A 235 ? 0.3982 0.3421 0.2566 0.0758  0.1854  0.0268  236 GLU A CD  
2077 C  CD  B GLU A 235 ? 0.5574 0.4635 0.5590 -0.0199 0.0651  -0.1762 236 GLU A CD  
2078 O  OE1 A GLU A 235 ? 0.0824 0.4147 0.3045 0.0354  0.0901  0.0317  236 GLU A OE1 
2079 O  OE1 B GLU A 235 ? 0.4983 0.3330 0.6947 -0.0601 0.0700  -0.1540 236 GLU A OE1 
2080 O  OE2 A GLU A 235 ? 0.4426 0.3240 0.4764 0.0549  0.1829  -0.0740 236 GLU A OE2 
2081 O  OE2 B GLU A 235 ? 0.7371 0.5253 0.8522 -0.1072 -0.0608 -0.1288 236 GLU A OE2 
2082 N  N   A PRO A 236 ? 0.0769 0.2566 0.1522 0.0753  0.0668  0.1030  237 PRO A N   
2083 N  N   B PRO A 236 ? 0.4930 0.2426 0.3242 -0.0873 0.1022  -0.0286 237 PRO A N   
2084 C  CA  A PRO A 236 ? 0.1087 0.3010 0.3107 0.0055  0.0800  0.1495  237 PRO A CA  
2085 C  CA  B PRO A 236 ? 0.2768 0.2687 0.3630 -0.0450 0.2639  -0.0143 237 PRO A CA  
2086 C  C   A PRO A 236 ? 0.0673 0.2690 0.2900 0.0886  0.0451  0.1882  237 PRO A C   
2087 C  C   B PRO A 236 ? 0.4277 0.3111 0.1912 0.0034  0.2588  -0.0866 237 PRO A C   
2088 O  O   A PRO A 236 ? 0.1016 0.3224 0.3152 0.0787  0.0813  0.1152  237 PRO A O   
2089 O  O   B PRO A 236 ? 0.3028 0.1503 0.2116 -0.1071 0.1989  -0.0790 237 PRO A O   
2090 C  CB  A PRO A 236 ? 0.1410 0.3278 0.3686 0.0811  0.0565  0.0908  237 PRO A CB  
2091 C  CB  B PRO A 236 ? 0.3896 0.2868 0.2633 -0.0832 0.1861  -0.0498 237 PRO A CB  
2092 C  CG  A PRO A 236 ? 0.3789 0.2337 0.2900 0.0336  0.0557  0.0502  237 PRO A CG  
2093 C  CG  B PRO A 236 ? 0.5190 0.3326 0.2357 -0.1416 0.1786  0.0766  237 PRO A CG  
2094 C  CD  A PRO A 236 ? 0.1302 0.4096 0.1878 -0.0406 0.0318  0.0529  237 PRO A CD  
2095 C  CD  B PRO A 236 ? 0.5153 0.3316 0.3195 -0.0882 0.1030  -0.0335 237 PRO A CD  
2096 N  N   A GLU A 237 ? 0.2308 0.2299 0.1920 0.0731  0.1439  0.0166  238 GLU A N   
2097 N  N   B GLU A 237 ? 0.4551 0.2258 0.1721 -0.0236 0.1663  -0.0141 238 GLU A N   
2098 C  CA  A GLU A 237 ? 0.1424 0.3110 0.1403 0.0358  0.0588  -0.0041 238 GLU A CA  
2099 C  CA  B GLU A 237 ? 0.3735 0.1870 0.1231 -0.0798 0.0988  -0.0449 238 GLU A CA  
2100 C  C   A GLU A 237 ? 0.0870 0.2362 0.1518 0.0489  0.0292  -0.0348 238 GLU A C   
2101 C  C   B GLU A 237 ? 0.3157 0.2117 0.1274 -0.1045 0.0577  -0.0508 238 GLU A C   
2102 O  O   A GLU A 237 ? 0.0741 0.2438 0.1600 0.0555  0.0608  0.0084  238 GLU A O   
2103 O  O   B GLU A 237 ? 0.1940 0.2566 0.1228 -0.0952 0.0506  -0.0850 238 GLU A O   
2104 C  CB  A GLU A 237 ? 0.0350 0.2780 0.3833 0.0746  0.0373  -0.0619 238 GLU A CB  
2105 C  CB  B GLU A 237 ? 0.4254 0.1843 0.1019 -0.0392 -0.0049 -0.0181 238 GLU A CB  
2106 C  CG  A GLU A 237 ? 0.0538 0.3264 0.3675 0.0285  0.0773  -0.0839 238 GLU A CG  
2107 C  CG  B GLU A 237 ? 0.4024 0.2666 0.2285 -0.0655 -0.0089 -0.0710 238 GLU A CG  
2108 C  CD  A GLU A 237 ? 0.2155 0.2133 0.3512 -0.0284 0.0319  -0.0397 238 GLU A CD  
2109 C  CD  B GLU A 237 ? 0.4025 0.3880 0.1238 -0.0496 -0.0290 -0.0201 238 GLU A CD  
2110 O  OE1 A GLU A 237 ? 0.2329 0.2615 0.2678 -0.0214 0.0440  -0.0890 238 GLU A OE1 
2111 O  OE1 B GLU A 237 ? 0.5247 0.4668 0.2531 0.0063  -0.0601 -0.1304 238 GLU A OE1 
2112 O  OE2 A GLU A 237 ? 0.2303 0.2016 0.2149 -0.0100 0.0286  -0.0904 238 GLU A OE2 
2113 O  OE2 B GLU A 237 ? 0.4512 0.3553 0.1827 -0.0421 0.0958  -0.0195 238 GLU A OE2 
2114 N  N   A GLU A 238 ? 0.0832 0.2421 0.1071 -0.0195 0.0767  -0.0289 239 GLU A N   
2115 N  N   B GLU A 238 ? 0.2024 0.2055 0.1082 -0.1028 0.0540  -0.0368 239 GLU A N   
2116 C  CA  A GLU A 238 ? 0.1210 0.2316 0.1145 -0.0197 0.0771  -0.0104 239 GLU A CA  
2117 C  CA  B GLU A 238 ? 0.1265 0.2154 0.1285 -0.0891 0.0479  -0.0189 239 GLU A CA  
2118 C  C   A GLU A 238 ? 0.1197 0.1701 0.1094 -0.0306 0.0780  -0.0100 239 GLU A C   
2119 C  C   B GLU A 238 ? 0.1228 0.2176 0.1204 -0.0864 0.0359  -0.0461 239 GLU A C   
2120 O  O   A GLU A 238 ? 0.1195 0.1493 0.1308 -0.0638 0.0478  -0.0168 239 GLU A O   
2121 O  O   B GLU A 238 ? 0.1109 0.2051 0.1466 -0.0547 -0.0065 -0.0027 239 GLU A O   
2122 C  CB  A GLU A 238 ? 0.1661 0.2219 0.1262 -0.0231 0.1042  -0.0292 239 GLU A CB  
2123 C  CB  B GLU A 238 ? 0.0757 0.2021 0.1815 -0.0372 0.0625  -0.0722 239 GLU A CB  
2124 C  CG  A GLU A 238 ? 0.1628 0.2759 0.2034 0.0096  0.1028  -0.0464 239 GLU A CG  
2125 C  CG  B GLU A 238 ? 0.0973 0.2308 0.2075 0.0173  0.0601  -0.0409 239 GLU A CG  
2126 C  CD  A GLU A 238 ? 0.0762 0.3520 0.3634 -0.0565 0.1215  -0.0488 239 GLU A CD  
2127 C  CD  B GLU A 238 ? 0.1643 0.2400 0.1514 -0.0190 0.0285  0.0296  239 GLU A CD  
2128 O  OE1 A GLU A 238 ? 0.0842 0.4173 0.5877 0.0805  0.0088  -0.0751 239 GLU A OE1 
2129 O  OE1 B GLU A 238 ? 0.1667 0.3605 0.1424 -0.0377 0.0326  -0.0042 239 GLU A OE1 
2130 O  OE2 A GLU A 238 ? 0.0516 0.4376 0.5276 -0.0729 0.1205  -0.0277 239 GLU A OE2 
2131 O  OE2 B GLU A 238 ? 0.1441 0.2814 0.1826 -0.0456 0.0397  -0.0149 239 GLU A OE2 
2132 N  N   . LEU A 239 ? 0.1462 0.1813 0.1240 -0.0630 0.0773  -0.0262 240 LEU A N   
2133 C  CA  . LEU A 239 ? 0.1322 0.1671 0.1179 -0.0489 0.0641  -0.0410 240 LEU A CA  
2134 C  C   . LEU A 239 ? 0.1491 0.1540 0.1005 -0.0478 0.0774  -0.0092 240 LEU A C   
2135 O  O   . LEU A 239 ? 0.1848 0.1982 0.1123 -0.0523 0.0678  -0.0195 240 LEU A O   
2136 C  CB  . LEU A 239 ? 0.1428 0.1509 0.1628 -0.0315 0.0200  -0.0344 240 LEU A CB  
2137 C  CG  . LEU A 239 ? 0.1176 0.1664 0.1857 -0.0096 0.0234  -0.0536 240 LEU A CG  
2138 C  CD1 . LEU A 239 ? 0.1664 0.1289 0.3031 -0.0013 -0.0039 -0.0499 240 LEU A CD1 
2139 C  CD2 . LEU A 239 ? 0.2368 0.1709 0.1613 0.0154  0.0289  -0.0414 240 LEU A CD2 
2140 N  N   . MET A 240 ? 0.1823 0.1486 0.1233 -0.0310 0.0971  -0.0158 241 MET A N   
2141 C  CA  . MET A 240 ? 0.2551 0.1688 0.0939 -0.0423 0.1077  -0.0089 241 MET A CA  
2142 C  C   . MET A 240 ? 0.1530 0.1506 0.1042 -0.0622 0.0725  -0.0402 241 MET A C   
2143 O  O   . MET A 240 ? 0.1649 0.1730 0.1028 -0.0463 0.0510  -0.0107 241 MET A O   
2144 C  CB  . MET A 240 ? 0.2312 0.1753 0.1306 -0.0159 0.1138  -0.0222 241 MET A CB  
2145 C  CG  . MET A 240 ? 0.2829 0.1454 0.1116 -0.0615 0.0974  -0.0188 241 MET A CG  
2146 S  SD  . MET A 240 ? 0.3186 0.1385 0.1420 -0.0547 0.0955  -0.0151 241 MET A SD  
2147 C  CE  . MET A 240 ? 0.2552 0.1578 0.1496 -0.0642 0.0870  -0.0132 241 MET A CE  
2148 N  N   . VAL A 241 ? 0.1705 0.1463 0.0809 -0.0378 0.0701  -0.0240 242 VAL A N   
2149 C  CA  . VAL A 241 ? 0.1702 0.1174 0.0944 -0.0279 0.0658  -0.0200 242 VAL A CA  
2150 C  C   . VAL A 241 ? 0.1116 0.0992 0.1213 -0.0187 0.0768  -0.0257 242 VAL A C   
2151 O  O   . VAL A 241 ? 0.1142 0.1555 0.1202 -0.0314 0.0763  -0.0305 242 VAL A O   
2152 C  CB  . VAL A 241 ? 0.1710 0.1246 0.1331 -0.0267 0.0479  -0.0414 242 VAL A CB  
2153 C  CG1 . VAL A 241 ? 0.1778 0.1575 0.1398 -0.0571 0.0496  -0.0331 242 VAL A CG1 
2154 C  CG2 . VAL A 241 ? 0.1691 0.1386 0.1615 -0.0264 0.0934  -0.0201 242 VAL A CG2 
2155 N  N   . ASP A 242 ? 0.1499 0.1075 0.0883 -0.0156 0.0622  -0.0240 243 ASP A N   
2156 C  CA  . ASP A 242 ? 0.1318 0.1104 0.1221 -0.0008 0.0529  -0.0250 243 ASP A CA  
2157 C  C   . ASP A 242 ? 0.1069 0.1288 0.1021 -0.0302 0.0567  -0.0157 243 ASP A C   
2158 O  O   . ASP A 242 ? 0.1136 0.1327 0.1613 -0.0190 0.0482  -0.0358 243 ASP A O   
2159 C  CB  . ASP A 242 ? 0.1121 0.1155 0.1551 -0.0185 0.0728  -0.0223 243 ASP A CB  
2160 C  CG  . ASP A 242 ? 0.1276 0.1079 0.1368 -0.0039 0.0648  -0.0241 243 ASP A CG  
2161 O  OD1 . ASP A 242 ? 0.1319 0.1032 0.1269 -0.0080 0.0541  -0.0142 243 ASP A OD1 
2162 O  OD2 . ASP A 242 ? 0.1643 0.1245 0.1888 0.0036  0.0862  -0.0401 243 ASP A OD2 
2163 N  N   . ASN A 243 ? 0.1082 0.0990 0.1051 -0.0157 0.0714  -0.0204 244 ASN A N   
2164 C  CA  . ASN A 243 ? 0.1014 0.0944 0.1089 -0.0156 0.0630  -0.0168 244 ASN A CA  
2165 C  C   . ASN A 243 ? 0.0640 0.1045 0.1035 -0.0199 0.0477  -0.0234 244 ASN A C   
2166 O  O   . ASN A 243 ? 0.1275 0.1177 0.0947 0.0146  0.0523  -0.0175 244 ASN A O   
2167 C  CB  . ASN A 243 ? 0.1062 0.1395 0.1049 -0.0171 0.0740  -0.0074 244 ASN A CB  
2168 C  CG  . ASN A 243 ? 0.1173 0.1170 0.0913 -0.0489 0.0639  -0.0089 244 ASN A CG  
2169 O  OD1 . ASN A 243 ? 0.1384 0.1188 0.1311 -0.0409 0.0596  0.0137  244 ASN A OD1 
2170 N  ND2 . ASN A 243 ? 0.1612 0.1382 0.1211 -0.0472 0.0293  0.0086  244 ASN A ND2 
2171 N  N   . TRP A 244 ? 0.0989 0.1077 0.0915 -0.0099 0.0523  -0.0167 245 TRP A N   
2172 C  CA  . TRP A 244 ? 0.0710 0.1098 0.0989 -0.0201 0.0440  -0.0301 245 TRP A CA  
2173 C  C   . TRP A 244 ? 0.0705 0.1031 0.1054 -0.0175 0.0369  -0.0207 245 TRP A C   
2174 O  O   . TRP A 244 ? 0.0899 0.1218 0.1438 0.0096  0.0311  -0.0352 245 TRP A O   
2175 C  CB  . TRP A 244 ? 0.0764 0.0969 0.1037 -0.0146 0.0388  -0.0187 245 TRP A CB  
2176 C  CG  . TRP A 244 ? 0.0678 0.1067 0.0987 -0.0136 0.0422  -0.0079 245 TRP A CG  
2177 C  CD1 . TRP A 244 ? 0.0942 0.0978 0.0990 -0.0074 0.0406  -0.0131 245 TRP A CD1 
2178 C  CD2 . TRP A 244 ? 0.0789 0.1114 0.1045 0.0076  0.0372  -0.0159 245 TRP A CD2 
2179 N  NE1 . TRP A 244 ? 0.1109 0.0996 0.1129 -0.0157 0.0422  -0.0186 245 TRP A NE1 
2180 C  CE2 . TRP A 244 ? 0.0921 0.1003 0.1289 -0.0063 0.0283  -0.0152 245 TRP A CE2 
2181 C  CE3 . TRP A 244 ? 0.0867 0.1399 0.1098 0.0127  0.0461  -0.0055 245 TRP A CE3 
2182 C  CZ2 . TRP A 244 ? 0.0863 0.1133 0.1503 -0.0066 0.0311  -0.0122 245 TRP A CZ2 
2183 C  CZ3 . TRP A 244 ? 0.1333 0.1242 0.1713 0.0291  0.0259  0.0044  245 TRP A CZ3 
2184 C  CH2 . TRP A 244 ? 0.0851 0.1358 0.1584 0.0060  0.0346  0.0016  245 TRP A CH2 
2185 N  N   . ARG A 245 ? 0.0584 0.1098 0.1105 -0.0165 0.0283  -0.0297 246 ARG A N   
2186 C  CA  . ARG A 245 ? 0.0560 0.1200 0.1188 0.0050  0.0124  -0.0239 246 ARG A CA  
2187 C  C   . ARG A 245 ? 0.0566 0.1134 0.1104 0.0087  0.0310  -0.0363 246 ARG A C   
2188 O  O   . ARG A 245 ? 0.0608 0.1246 0.1202 -0.0077 0.0346  -0.0234 246 ARG A O   
2189 C  CB  . ARG A 245 ? 0.0453 0.1249 0.1263 -0.0063 0.0199  -0.0232 246 ARG A CB  
2190 C  CG  . ARG A 245 ? 0.0396 0.1222 0.1459 -0.0216 0.0216  -0.0348 246 ARG A CG  
2191 C  CD  . ARG A 245 ? 0.0554 0.1200 0.1664 -0.0108 0.0082  -0.0412 246 ARG A CD  
2192 N  NE  . ARG A 245 ? 0.0502 0.1410 0.1859 -0.0156 0.0104  -0.0464 246 ARG A NE  
2193 C  CZ  . ARG A 245 ? 0.0653 0.1524 0.1513 -0.0117 0.0135  -0.0436 246 ARG A CZ  
2194 N  NH1 . ARG A 245 ? 0.0615 0.1593 0.1595 -0.0201 0.0383  -0.0345 246 ARG A NH1 
2195 N  NH2 . ARG A 245 ? 0.0840 0.1668 0.2112 -0.0461 -0.0115 -0.0282 246 ARG A NH2 
2196 N  N   A PRO A 246 ? 0.0611 0.1070 0.1247 0.0008  0.0320  -0.0170 247 PRO A N   
2197 N  N   B PRO A 246 ? 0.0814 0.1159 0.1210 0.0164  0.0341  -0.0203 247 PRO A N   
2198 C  CA  A PRO A 246 ? 0.0869 0.1080 0.1227 0.0015  0.0138  -0.0077 247 PRO A CA  
2199 C  CA  B PRO A 246 ? 0.0859 0.1174 0.1307 0.0130  0.0103  -0.0069 247 PRO A CA  
2200 C  C   A PRO A 246 ? 0.0436 0.1231 0.1243 0.0158  0.0054  -0.0139 247 PRO A C   
2201 C  C   B PRO A 246 ? 0.0474 0.1246 0.1319 0.0164  0.0086  -0.0106 247 PRO A C   
2202 O  O   A PRO A 246 ? 0.0969 0.1195 0.1273 0.0047  0.0066  -0.0168 247 PRO A O   
2203 O  O   B PRO A 246 ? 0.0928 0.1215 0.1363 0.0054  0.0031  -0.0131 247 PRO A O   
2204 C  CB  A PRO A 246 ? 0.1060 0.1426 0.1624 0.0367  0.0359  -0.0121 247 PRO A CB  
2205 C  CB  B PRO A 246 ? 0.1088 0.1434 0.1858 0.0514  0.0215  -0.0011 247 PRO A CB  
2206 C  CG  A PRO A 246 ? 0.0892 0.1173 0.1779 0.0368  0.0387  -0.0018 247 PRO A CG  
2207 C  CG  B PRO A 246 ? 0.1463 0.1351 0.2049 0.0418  0.0340  -0.0024 247 PRO A CG  
2208 C  CD  A PRO A 246 ? 0.0554 0.1082 0.1787 0.0220  0.0160  -0.0103 247 PRO A CD  
2209 C  CD  B PRO A 246 ? 0.0895 0.1738 0.1377 0.0498  0.0466  -0.0416 247 PRO A CD  
2210 N  N   . ALA A 247 ? 0.0721 0.1304 0.1312 0.0176  0.0148  -0.0039 248 ALA A N   
2211 C  CA  . ALA A 247 ? 0.0822 0.1310 0.1275 0.0088  0.0087  -0.0178 248 ALA A CA  
2212 C  C   . ALA A 247 ? 0.1032 0.1390 0.1277 0.0333  -0.0102 -0.0189 248 ALA A C   
2213 O  O   . ALA A 247 ? 0.1079 0.1534 0.1597 0.0361  -0.0146 -0.0074 248 ALA A O   
2214 C  CB  . ALA A 247 ? 0.1484 0.1460 0.1524 0.0035  0.0376  0.0115  248 ALA A CB  
2215 N  N   . GLN A 248 ? 0.0888 0.1154 0.1290 0.0081  -0.0110 -0.0096 249 GLN A N   
2216 C  CA  . GLN A 248 ? 0.0547 0.1599 0.1390 0.0222  -0.0157 -0.0097 249 GLN A CA  
2217 C  C   . GLN A 248 ? 0.0980 0.1496 0.1394 0.0487  -0.0306 -0.0134 249 GLN A C   
2218 O  O   . GLN A 248 ? 0.1115 0.1526 0.1376 0.0284  -0.0102 -0.0055 249 GLN A O   
2219 C  CB  . GLN A 248 ? 0.0947 0.1347 0.1735 -0.0093 -0.0172 -0.0128 249 GLN A CB  
2220 C  CG  . GLN A 248 ? 0.1206 0.1572 0.1548 0.0136  0.0016  -0.0130 249 GLN A CG  
2221 C  CD  . GLN A 248 ? 0.0800 0.1897 0.2002 -0.0199 0.0053  -0.0198 249 GLN A CD  
2222 O  OE1 . GLN A 248 ? 0.0883 0.2433 0.2334 -0.0309 -0.0005 -0.0476 249 GLN A OE1 
2223 N  NE2 . GLN A 248 ? 0.1141 0.1820 0.1824 -0.0049 -0.0005 -0.0140 249 GLN A NE2 
2224 N  N   . PRO A 249 ? 0.1111 0.2244 0.1610 0.0545  -0.0499 -0.0210 250 PRO A N   
2225 C  CA  . PRO A 249 ? 0.1531 0.2574 0.1484 0.0946  -0.0606 -0.0250 250 PRO A CA  
2226 C  C   . PRO A 249 ? 0.1212 0.1671 0.1652 0.0392  -0.0590 0.0120  250 PRO A C   
2227 O  O   . PRO A 249 ? 0.1399 0.1762 0.1631 0.0537  -0.0365 0.0071  250 PRO A O   
2228 C  CB  . PRO A 249 ? 0.1449 0.3394 0.2040 0.0801  -0.0765 -0.0289 250 PRO A CB  
2229 C  CG  . PRO A 249 ? 0.2236 0.3683 0.1772 0.0646  -0.0709 -0.0343 250 PRO A CG  
2230 C  CD  . PRO A 249 ? 0.0816 0.3328 0.1903 0.0524  -0.0537 -0.0345 250 PRO A CD  
2231 N  N   . LEU A 250 ? 0.1597 0.2066 0.1208 0.0640  -0.0296 -0.0019 251 LEU A N   
2232 C  CA  . LEU A 250 ? 0.1487 0.1667 0.1480 0.0392  -0.0286 -0.0187 251 LEU A CA  
2233 C  C   . LEU A 250 ? 0.1707 0.1627 0.1493 0.0646  -0.0546 -0.0151 251 LEU A C   
2234 O  O   . LEU A 250 ? 0.1901 0.1637 0.1662 0.0479  -0.0802 -0.0296 251 LEU A O   
2235 C  CB  . LEU A 250 ? 0.2267 0.1508 0.1727 0.0399  0.0207  0.0027  251 LEU A CB  
2236 C  CG  . LEU A 250 ? 0.2046 0.2246 0.1425 0.0185  0.0178  -0.0254 251 LEU A CG  
2237 C  CD1 . LEU A 250 ? 0.1412 0.2351 0.1697 0.0099  -0.0006 -0.0234 251 LEU A CD1 
2238 C  CD2 . LEU A 250 ? 0.3434 0.2352 0.1811 -0.0089 0.0807  -0.0273 251 LEU A CD2 
2239 N  N   . LYS A 251 ? 0.2046 0.1985 0.1691 0.0842  -0.0933 -0.0376 252 LYS A N   
2240 C  CA  . LYS A 251 ? 0.2353 0.2167 0.1448 0.0774  -0.0705 -0.0511 252 LYS A CA  
2241 C  C   . LYS A 251 ? 0.2157 0.2408 0.1895 0.0422  -0.0564 -0.0635 252 LYS A C   
2242 O  O   . LYS A 251 ? 0.2484 0.3101 0.1807 0.0255  0.0134  -0.0376 252 LYS A O   
2243 C  CB  . LYS A 251 ? 0.2361 0.2122 0.2200 0.0166  -0.1015 -0.0546 252 LYS A CB  
2244 C  CG  . LYS A 251 ? 0.3028 0.2647 0.2597 0.0974  -0.0688 -0.0563 252 LYS A CG  
2245 C  CD  . LYS A 251 ? 0.3434 0.3380 0.2593 0.0277  -0.0560 -0.1142 252 LYS A CD  
2246 C  CE  . LYS A 251 ? 0.3723 0.4018 0.4184 0.0455  0.0323  -0.0596 252 LYS A CE  
2247 N  NZ  . LYS A 251 ? 0.2561 0.4018 0.5454 0.0837  -0.0344 0.0086  252 LYS A NZ  
2248 N  N   A ASN A 252 ? 0.2499 0.2449 0.1533 0.0536  -0.0908 -0.0683 253 ASN A N   
2249 N  N   B ASN A 252 ? 0.1481 0.2448 0.2112 0.1065  -0.1049 -0.0817 253 ASN A N   
2250 C  CA  A ASN A 252 ? 0.2318 0.3750 0.2648 0.0510  -0.0394 -0.1248 253 ASN A CA  
2251 C  CA  B ASN A 252 ? 0.1627 0.3513 0.2508 0.0831  -0.0600 -0.0707 253 ASN A CA  
2252 C  C   A ASN A 252 ? 0.2010 0.3870 0.1974 0.1282  -0.0308 -0.0914 253 ASN A C   
2253 C  C   B ASN A 252 ? 0.2679 0.1951 0.1633 0.0509  -0.0765 0.0350  253 ASN A C   
2254 O  O   A ASN A 252 ? 0.3052 0.5331 0.1498 0.1685  -0.0179 -0.0565 253 ASN A O   
2255 O  O   B ASN A 252 ? 0.1694 0.1912 0.1794 0.0749  -0.0165 -0.0289 253 ASN A O   
2256 C  CB  A ASN A 252 ? 0.3361 0.3786 0.2015 0.0060  -0.0540 -0.1018 253 ASN A CB  
2257 C  CB  B ASN A 252 ? 0.1785 0.4771 0.2661 -0.0163 -0.1072 -0.0139 253 ASN A CB  
2258 C  CG  A ASN A 252 ? 0.3306 0.3638 0.1778 0.0065  -0.0231 -0.0395 253 ASN A CG  
2259 C  CG  B ASN A 252 ? 0.2971 0.5164 0.3250 0.0587  -0.0789 0.0402  253 ASN A CG  
2260 O  OD1 A ASN A 252 ? 0.4235 0.5131 0.1635 -0.0131 0.0533  -0.0077 253 ASN A OD1 
2261 O  OD1 B ASN A 252 ? 0.3100 0.5858 0.3164 -0.0035 -0.0120 0.0937  253 ASN A OD1 
2262 N  ND2 A ASN A 252 ? 0.1878 0.3693 0.2702 0.0104  -0.0375 -0.0419 253 ASN A ND2 
2263 N  ND2 B ASN A 252 ? 0.3754 0.6815 0.3838 -0.1091 -0.1445 0.0534  253 ASN A ND2 
2264 N  N   A ARG A 253 ? 0.2154 0.2361 0.1448 0.1010  -0.0103 -0.0231 254 ARG A N   
2265 N  N   B ARG A 253 ? 0.1743 0.2784 0.1102 0.0775  -0.0245 -0.0527 254 ARG A N   
2266 C  CA  A ARG A 253 ? 0.1730 0.1167 0.1150 0.0532  0.0111  -0.0350 254 ARG A CA  
2267 C  CA  B ARG A 253 ? 0.1790 0.2285 0.0602 0.0321  -0.0331 0.0002  254 ARG A CA  
2268 C  C   A ARG A 253 ? 0.1909 0.1655 0.1311 0.0376  0.0291  0.0108  254 ARG A C   
2269 C  C   B ARG A 253 ? 0.2000 0.1867 0.0687 0.0294  -0.0069 -0.0209 254 ARG A C   
2270 O  O   A ARG A 253 ? 0.2374 0.1714 0.2588 0.0761  0.0452  0.0253  254 ARG A O   
2271 O  O   B ARG A 253 ? 0.3041 0.1860 0.1705 0.0387  0.0151  0.0129  254 ARG A O   
2272 C  CB  A ARG A 253 ? 0.1716 0.1168 0.1096 0.0156  0.0181  -0.0253 254 ARG A CB  
2273 C  CB  B ARG A 253 ? 0.1678 0.2264 0.0608 0.0120  -0.0370 -0.0121 254 ARG A CB  
2274 C  CG  A ARG A 253 ? 0.1631 0.1292 0.1104 0.0000  0.0046  -0.0236 254 ARG A CG  
2275 C  CG  B ARG A 253 ? 0.1497 0.2044 0.0952 0.0264  -0.0208 -0.0065 254 ARG A CG  
2276 C  CD  A ARG A 253 ? 0.1357 0.1326 0.1100 0.0325  0.0065  -0.0282 254 ARG A CD  
2277 C  CD  B ARG A 253 ? 0.1465 0.1577 0.0928 0.0422  -0.0196 -0.0250 254 ARG A CD  
2278 N  NE  A ARG A 253 ? 0.1042 0.1207 0.1000 0.0271  -0.0110 -0.0198 254 ARG A NE  
2279 N  NE  B ARG A 253 ? 0.1262 0.1497 0.1031 0.0412  -0.0239 -0.0176 254 ARG A NE  
2280 C  CZ  A ARG A 253 ? 0.0705 0.1155 0.0991 0.0088  -0.0144 -0.0140 254 ARG A CZ  
2281 C  CZ  B ARG A 253 ? 0.0780 0.1261 0.1059 0.0140  -0.0209 -0.0138 254 ARG A CZ  
2282 N  NH1 A ARG A 253 ? 0.0735 0.1302 0.1097 0.0127  -0.0214 -0.0085 254 ARG A NH1 
2283 N  NH1 B ARG A 253 ? 0.0710 0.1372 0.1206 0.0182  -0.0265 -0.0083 254 ARG A NH1 
2284 N  NH2 A ARG A 253 ? 0.0942 0.1243 0.1143 0.0226  -0.0267 -0.0226 254 ARG A NH2 
2285 N  NH2 B ARG A 253 ? 0.1025 0.1316 0.1269 0.0248  -0.0295 -0.0240 254 ARG A NH2 
2286 N  N   . GLN A 254 ? 0.1812 0.2199 0.1364 0.0254  -0.0266 -0.0622 255 GLN A N   
2287 C  CA  . GLN A 254 ? 0.2146 0.2408 0.1046 0.0207  -0.0237 -0.0398 255 GLN A CA  
2288 C  C   . GLN A 254 ? 0.2082 0.1932 0.1439 -0.0083 -0.0388 0.0047  255 GLN A C   
2289 O  O   . GLN A 254 ? 0.2202 0.1867 0.2068 0.0044  -0.0514 -0.0089 255 GLN A O   
2290 C  CB  . GLN A 254 ? 0.3462 0.3257 0.1509 0.0747  -0.0099 -0.1039 255 GLN A CB  
2291 C  CG  . GLN A 254 ? 0.3883 0.4655 0.1795 0.1260  0.0156  -0.0641 255 GLN A CG  
2292 C  CD  . GLN A 254 ? 0.3600 0.5568 0.2902 0.1357  0.0403  -0.0361 255 GLN A CD  
2293 N  N   . ILE A 255 ? 0.1641 0.1662 0.0972 0.0190  0.0021  -0.0072 256 ILE A N   
2294 C  CA  . ILE A 255 ? 0.1613 0.1640 0.0960 0.0454  -0.0030 -0.0058 256 ILE A CA  
2295 C  C   . ILE A 255 ? 0.1915 0.1595 0.0919 0.0482  0.0248  0.0244  256 ILE A C   
2296 O  O   . ILE A 255 ? 0.2007 0.1804 0.1138 0.0522  0.0582  0.0321  256 ILE A O   
2297 C  CB  . ILE A 255 ? 0.1164 0.1706 0.1003 0.0378  0.0119  -0.0127 256 ILE A CB  
2298 C  CG1 . ILE A 255 ? 0.1224 0.1806 0.1451 0.0398  0.0245  -0.0298 256 ILE A CG1 
2299 C  CG2 . ILE A 255 ? 0.1568 0.1764 0.1224 0.0234  -0.0095 -0.0122 256 ILE A CG2 
2300 C  CD1 . ILE A 255 ? 0.2291 0.1795 0.1586 0.0369  0.0214  -0.0497 256 ILE A CD1 
2301 N  N   . LYS A 256 ? 0.1131 0.1732 0.0866 0.0244  0.0193  0.0111  257 LYS A N   
2302 C  CA  . LYS A 256 ? 0.1332 0.1851 0.0915 0.0251  0.0545  0.0261  257 LYS A CA  
2303 C  C   . LYS A 256 ? 0.1703 0.1870 0.0863 0.0181  0.0413  0.0168  257 LYS A C   
2304 O  O   . LYS A 256 ? 0.1903 0.2145 0.0836 -0.0120 0.0551  0.0060  257 LYS A O   
2305 C  CB  . LYS A 256 ? 0.2008 0.1974 0.1360 0.0423  0.0178  -0.0290 257 LYS A CB  
2306 C  CG  . LYS A 256 ? 0.2563 0.3042 0.2281 0.0526  -0.0212 -0.0872 257 LYS A CG  
2307 C  CD  . LYS A 256 ? 0.4482 0.3192 0.2504 0.0199  -0.0410 -0.0967 257 LYS A CD  
2308 C  CE  . LYS A 256 ? 0.4775 0.6190 0.4346 -0.1072 -0.0330 -0.2800 257 LYS A CE  
2309 N  NZ  . LYS A 256 ? 0.5167 0.5946 0.5438 -0.1637 -0.0803 -0.1920 257 LYS A NZ  
2310 N  N   . ALA A 257 ? 0.1369 0.1913 0.0908 0.0468  0.0543  0.0212  258 ALA A N   
2311 C  CA  . ALA A 257 ? 0.1372 0.2091 0.1106 0.0194  0.0514  0.0447  258 ALA A CA  
2312 C  C   . ALA A 257 ? 0.1697 0.1988 0.1031 0.0387  0.0760  0.0139  258 ALA A C   
2313 O  O   . ALA A 257 ? 0.1899 0.2336 0.1032 0.0344  0.0826  0.0088  258 ALA A O   
2314 C  CB  . ALA A 257 ? 0.1633 0.2118 0.1591 0.0299  0.0895  0.0395  258 ALA A CB  
2315 N  N   . SER A 258 ? 0.1575 0.1924 0.1197 0.0313  0.0585  0.0217  259 SER A N   
2316 C  CA  . SER A 258 ? 0.1637 0.2190 0.1750 0.0321  0.0741  0.0337  259 SER A CA  
2317 C  C   . SER A 258 ? 0.1370 0.2456 0.1951 0.0227  0.1057  -0.0067 259 SER A C   
2318 O  O   . SER A 258 ? 0.1714 0.3664 0.2242 0.0621  0.1210  0.0330  259 SER A O   
2319 C  CB  . SER A 258 ? 0.2020 0.1885 0.1624 -0.0111 0.0548  0.0400  259 SER A CB  
2320 O  OG  . SER A 258 ? 0.1339 0.2187 0.1600 0.0198  0.0863  0.0157  259 SER A OG  
2321 N  N   . PHE A 259 ? 0.1321 0.2606 0.2310 -0.0181 0.0871  -0.0161 260 PHE A N   
2322 C  CA  . PHE A 259 ? 0.1572 0.2457 0.2922 -0.0269 0.0653  0.0447  260 PHE A CA  
2323 C  C   . PHE A 259 ? 0.1851 0.3544 0.2227 -0.0432 0.1306  0.0601  260 PHE A C   
2324 O  O   . PHE A 259 ? 0.2789 0.2842 0.2535 -0.0509 0.0596  0.1186  260 PHE A O   
2325 C  CB  . PHE A 259 ? 0.1549 0.3146 0.2482 0.0148  0.0793  0.0408  260 PHE A CB  
2326 C  CG  . PHE A 259 ? 0.1487 0.2120 0.2555 -0.0208 0.0815  0.0469  260 PHE A CG  
2327 C  CD1 . PHE A 259 ? 0.1511 0.2233 0.1834 -0.0122 0.0807  0.0387  260 PHE A CD1 
2328 C  CD2 . PHE A 259 ? 0.3160 0.2146 0.3091 -0.0381 0.0798  0.0901  260 PHE A CD2 
2329 C  CE1 . PHE A 259 ? 0.1585 0.1834 0.2516 -0.0072 0.0623  0.0279  260 PHE A CE1 
2330 C  CE2 . PHE A 259 ? 0.2755 0.3055 0.3148 -0.0197 0.0256  0.0806  260 PHE A CE2 
2331 C  CZ  . PHE A 259 ? 0.2299 0.1911 0.3335 0.0195  0.0396  0.0259  260 PHE A CZ  
2332 N  N   . LYS A 260 ? 0.4209 0.4330 0.3349 -0.1734 0.2102  0.1397  261 LYS A N   
2333 C  CA  . LYS A 260 ? 0.7713 0.7170 0.4382 -0.0269 0.2432  0.4014  261 LYS A CA  
2334 C  C   . LYS A 260 ? 0.9337 0.6524 0.6021 -0.0173 0.1199  0.1639  261 LYS A C   
2335 O  O   . LYS A 260 ? 0.8386 0.7596 1.1300 0.1707  0.0571  0.3008  261 LYS A O   
2336 C  CB  . LYS A 260 ? 1.0524 0.7653 0.3717 0.1599  0.3287  0.4889  261 LYS A CB  
2337 O  OXT . LYS A 260 ? 1.3213 0.7189 0.8016 0.0361  0.2558  0.2301  261 LYS A OXT 
2338 ZN ZN  . ZN  B .   ? 0.0838 0.0890 0.0831 -0.0117 0.0210  -0.0052 301 ZN  A ZN  
2339 S  S   . DMS C .   ? 0.2267 0.4032 0.3344 -0.0265 0.0610  -0.0754 302 DMS A S   
2340 O  O   . DMS C .   ? 0.4219 0.4912 0.6143 0.0546  0.2041  -0.1550 302 DMS A O   
2341 C  C1  . DMS C .   ? 0.2865 0.3332 0.2972 0.0447  0.0749  -0.1112 302 DMS A C1  
2342 C  C2  . DMS C .   ? 0.4595 0.1841 0.4770 -0.0496 0.0447  0.0562  302 DMS A C2  
2343 N  N1  . BCN D .   ? 0.4449 0.5702 0.4753 -0.0206 -0.0058 0.0694  303 BCN A N1  
2344 C  C1  . BCN D .   ? 0.1821 0.6169 0.4923 -0.0726 -0.0379 0.1893  303 BCN A C1  
2345 C  C2  . BCN D .   ? 0.3036 0.5067 0.6445 -0.2748 -0.0036 0.2223  303 BCN A C2  
2346 O  O21 . BCN D .   ? 0.4730 0.7831 0.4633 -0.4925 -0.0502 0.1737  303 BCN A O21 
2347 O  O22 . BCN D .   ? 0.5866 0.5457 0.5308 -0.1226 -0.0204 0.2237  303 BCN A O22 
2348 C  C3  . BCN D .   ? 0.1570 0.3162 0.4674 -0.0794 0.0576  0.1688  303 BCN A C3  
2349 C  C4  . BCN D .   ? 0.5360 0.5274 0.6646 -0.1885 -0.1063 0.0734  303 BCN A C4  
2350 O  O4  . BCN D .   ? 0.8277 0.3967 0.6092 -0.2126 0.0212  0.1450  303 BCN A O4  
2351 C  C5  . BCN D .   ? 0.3273 0.3371 0.3624 -0.1410 0.0334  0.1663  303 BCN A C5  
2352 C  C6  . BCN D .   ? 0.6170 0.3993 0.6204 -0.0211 0.1888  0.0238  303 BCN A C6  
2353 O  O6  . BCN D .   ? 0.5157 0.2879 0.8832 -0.0732 0.0875  0.1252  303 BCN A O6  
2354 O  O24 . OQT E .   ? 0.1998 0.1795 0.1614 -0.0001 0.0602  -0.0165 304 OQT A O24 
2355 S  S2  . OQT E .   ? 0.1031 0.1503 0.1923 -0.0239 0.0122  0.0144  304 OQT A S2  
2356 O  O1  . OQT E .   ? 0.1254 0.1824 0.2430 -0.0417 -0.0150 0.0269  304 OQT A O1  
2357 N  N3  . OQT E .   ? 0.1089 0.1001 0.1482 -0.0572 -0.0053 -0.0053 304 OQT A N3  
2358 C  C4  . OQT E .   ? 0.0637 0.1647 0.1811 -0.0278 0.0330  -0.0143 304 OQT A C4  
2359 C  C12 . OQT E .   ? 0.1186 0.1717 0.1758 0.0078  0.0297  -0.0064 304 OQT A C12 
2360 C  C10 . OQT E .   ? 0.1997 0.1567 0.1894 0.0238  0.0077  0.0044  304 OQT A C10 
2361 F  F11 . OQT E .   ? 0.3738 0.1780 0.1890 0.0433  0.0175  -0.0076 304 OQT A F11 
2362 C  C9  . OQT E .   ? 0.1687 0.2348 0.1754 0.0242  -0.0172 -0.0089 304 OQT A C9  
2363 C  C7  . OQT E .   ? 0.1485 0.1869 0.1465 0.0259  0.0099  -0.0451 304 OQT A C7  
2364 F  F8  . OQT E .   ? 0.1410 0.2621 0.1773 -0.0216 0.0226  -0.0474 304 OQT A F8  
2365 C  C5  . OQT E .   ? 0.1497 0.1584 0.1694 0.0041  0.0086  -0.0214 304 OQT A C5  
2366 F  F6  . OQT E .   ? 0.2217 0.2182 0.1554 -0.0622 -0.0130 -0.0065 304 OQT A F6  
2367 N  N13 . OQT E .   ? 0.1701 0.1663 0.1839 -0.0122 0.0564  0.0061  304 OQT A N13 
2368 C  C14 . OQT E .   ? 0.1693 0.2276 0.1708 -0.0201 0.0722  -0.0044 304 OQT A C14 
2369 C  C23 . OQT E .   ? 0.2055 0.2851 0.2383 -0.0814 0.0271  0.0118  304 OQT A C23 
2370 C  C22 . OQT E .   ? 0.3055 0.4405 0.2282 -0.1153 0.0289  0.0639  304 OQT A C22 
2371 C  C21 . OQT E .   ? 0.2593 0.2442 0.2850 -0.0741 0.0015  0.0048  304 OQT A C21 
2372 C  C20 . OQT E .   ? 0.2016 0.2266 0.2044 -0.0467 0.0829  0.0143  304 OQT A C20 
2373 C  C15 . OQT E .   ? 0.1698 0.2463 0.1927 -0.0216 0.0945  -0.0263 304 OQT A C15 
2374 C  C19 . OQT E .   ? 0.2082 0.2727 0.2108 0.0266  0.1005  -0.0118 304 OQT A C19 
2375 C  C18 . OQT E .   ? 0.2078 0.2825 0.2942 -0.0146 0.0849  0.0888  304 OQT A C18 
2376 C  C17 . OQT E .   ? 0.2301 0.2369 0.2033 0.0083  0.0743  0.0075  304 OQT A C17 
2377 C  C16 . OQT E .   ? 0.2392 0.2048 0.2235 -0.0040 0.0283  -0.0162 304 OQT A C16 
2378 O  O   . HOH F .   ? 0.4935 0.3829 0.3028 0.0906  0.0139  0.1133  401 HOH A O   
2379 O  O   . HOH F .   ? 0.2758 0.7559 0.7923 -0.1012 -0.0098 0.2570  402 HOH A O   
2380 O  O   . HOH F .   ? 0.2524 0.1410 0.2089 -0.0283 -0.0384 -0.0198 403 HOH A O   
2381 O  O   . HOH F .   ? 0.5323 0.2691 0.3325 -0.0797 0.0657  0.0562  404 HOH A O   
2382 O  O   . HOH F .   ? 0.2007 0.2782 0.4716 -0.0436 -0.0350 0.0585  405 HOH A O   
2383 O  O   . HOH F .   ? 0.6099 0.5209 0.4685 0.0570  -0.2037 0.1036  406 HOH A O   
2384 O  O   . HOH F .   ? 0.2382 0.2606 0.6988 0.0142  0.1953  0.1816  407 HOH A O   
2385 O  O   . HOH F .   ? 0.2535 0.3872 0.7034 -0.0588 0.1256  -0.2350 408 HOH A O   
2386 O  O   . HOH F .   ? 0.6901 0.7637 0.6384 -0.3025 -0.0616 0.0864  409 HOH A O   
2387 O  O   . HOH F .   ? 0.4574 0.3272 0.2581 -0.0496 0.1481  -0.0915 410 HOH A O   
2388 O  O   . HOH F .   ? 0.2588 0.3142 0.3483 0.0258  0.0563  -0.0137 411 HOH A O   
2389 O  O   . HOH F .   ? 0.7161 0.3240 0.1815 -0.1594 0.0641  -0.0537 412 HOH A O   
2390 O  O   . HOH F .   ? 0.2110 0.2791 0.3365 0.0320  0.0993  0.1078  413 HOH A O   
2391 O  O   . HOH F .   ? 0.5517 0.7999 0.1815 0.0872  0.1533  -0.0422 414 HOH A O   
2392 O  O   . HOH F .   ? 0.2539 0.3950 0.3755 -0.0310 0.1398  -0.0913 415 HOH A O   
2393 O  O   . HOH F .   ? 0.4263 0.5710 0.4637 0.1293  0.1195  0.0842  416 HOH A O   
2394 O  O   . HOH F .   ? 0.3391 0.3982 0.7471 0.0670  0.0427  0.0152  417 HOH A O   
2395 O  O   . HOH F .   ? 0.5077 0.8222 0.2581 -0.1327 0.1205  -0.1948 418 HOH A O   
2396 O  O   . HOH F .   ? 0.3120 0.2590 0.4823 -0.0974 -0.0549 -0.0763 419 HOH A O   
2397 O  O   . HOH F .   ? 0.3105 0.8376 0.5202 -0.0601 0.0203  -0.1441 420 HOH A O   
2398 O  O   . HOH F .   ? 0.8953 0.7662 0.3885 -0.4787 -0.0170 0.2098  421 HOH A O   
2399 O  O   . HOH F .   ? 0.4709 0.3965 0.3459 -0.0068 0.0071  0.0829  422 HOH A O   
2400 O  O   . HOH F .   ? 0.3867 0.4196 0.4767 -0.0933 -0.0053 0.0510  423 HOH A O   
2401 O  O   . HOH F .   ? 0.4621 0.5201 0.6335 -0.0925 -0.1048 0.1495  424 HOH A O   
2402 O  O   . HOH F .   ? 0.6090 0.5134 0.8340 0.2318  -0.2153 0.0177  425 HOH A O   
2403 O  O   . HOH F .   ? 0.3376 0.2381 0.3680 -0.0551 -0.0480 -0.0594 426 HOH A O   
2404 O  O   . HOH F .   ? 0.2481 0.2377 0.3501 -0.0145 -0.0414 0.0444  427 HOH A O   
2405 O  O   . HOH F .   ? 0.1037 0.1293 0.1386 -0.0071 0.0433  -0.0105 428 HOH A O   
2406 O  O   . HOH F .   ? 0.1999 0.2952 0.4161 0.0196  -0.0179 -0.0278 429 HOH A O   
2407 O  O   . HOH F .   ? 0.3516 0.5583 0.6649 -0.0540 0.3040  -0.0806 430 HOH A O   
2408 O  O   . HOH F .   ? 0.5556 0.4096 0.3385 -0.0435 0.1147  -0.0107 431 HOH A O   
2409 O  O   . HOH F .   ? 0.5198 0.3286 0.3082 -0.0849 -0.0659 0.1092  432 HOH A O   
2410 O  O   . HOH F .   ? 0.3195 0.6143 0.8912 0.0071  0.0994  0.1322  433 HOH A O   
2411 O  O   . HOH F .   ? 0.6090 0.5649 0.6121 -0.1195 -0.0890 -0.0100 434 HOH A O   
2412 O  O   . HOH F .   ? 0.3067 0.4542 0.2592 -0.1140 0.1307  -0.1786 435 HOH A O   
2413 O  O   . HOH F .   ? 0.5876 0.3820 0.4324 0.0422  0.0735  0.0439  436 HOH A O   
2414 O  O   . HOH F .   ? 0.3391 0.2301 0.1915 -0.0955 0.0889  0.0212  437 HOH A O   
2415 O  O   . HOH F .   ? 0.3780 0.2341 0.4613 0.0009  0.0754  -0.1175 438 HOH A O   
2416 O  O   . HOH F .   ? 0.4074 0.3589 0.5668 0.0402  -0.1040 0.1129  439 HOH A O   
2417 O  O   . HOH F .   ? 0.5019 0.6651 0.4038 -0.0930 0.1253  -0.1536 440 HOH A O   
2418 O  O   . HOH F .   ? 0.3364 0.2518 0.4095 -0.1050 0.0834  -0.0671 441 HOH A O   
2419 O  O   . HOH F .   ? 0.2000 0.4222 0.5327 -0.1398 -0.0348 -0.1139 442 HOH A O   
2420 O  O   . HOH F .   ? 0.4058 0.3502 0.2886 -0.1596 0.0811  -0.1054 443 HOH A O   
2421 O  O   . HOH F .   ? 0.3529 0.3395 0.2490 -0.0127 0.0129  -0.0474 444 HOH A O   
2422 O  O   . HOH F .   ? 0.2531 0.3591 0.2527 -0.0558 0.0891  0.0201  445 HOH A O   
2423 O  O   . HOH F .   ? 0.5766 0.6996 0.5236 -0.1394 0.1385  -0.2346 446 HOH A O   
2424 O  O   . HOH F .   ? 1.0297 0.5712 0.3274 0.3546  0.0954  0.0232  447 HOH A O   
2425 O  O   . HOH F .   ? 0.1507 0.1341 0.1375 -0.0001 0.0151  -0.0060 448 HOH A O   
2426 O  O   . HOH F .   ? 0.1798 0.4567 0.2977 0.0839  0.0300  -0.0512 449 HOH A O   
2427 O  O   . HOH F .   ? 0.3533 0.3050 0.1570 -0.0043 -0.0641 -0.0060 450 HOH A O   
2428 O  O   . HOH F .   ? 0.2404 0.2393 0.3604 -0.0200 0.0436  -0.0615 451 HOH A O   
2429 O  O   . HOH F .   ? 0.4274 0.4672 0.4128 0.2331  -0.1451 -0.1005 452 HOH A O   
2430 O  O   . HOH F .   ? 0.2620 0.2676 0.3426 0.0505  -0.0974 -0.0529 453 HOH A O   
2431 O  O   . HOH F .   ? 0.3879 0.2751 0.4597 0.0794  0.2490  0.1391  454 HOH A O   
2432 O  O   . HOH F .   ? 0.2706 0.3804 0.4622 0.0369  0.0304  0.0715  455 HOH A O   
2433 O  O   . HOH F .   ? 0.1609 0.2996 0.5657 0.0434  0.1084  0.0519  456 HOH A O   
2434 O  O   . HOH F .   ? 0.3671 0.5371 0.6893 0.1243  -0.0096 -0.2457 457 HOH A O   
2435 O  O   . HOH F .   ? 0.4894 0.4980 0.4615 -0.0010 -0.0737 -0.2020 458 HOH A O   
2436 O  O   . HOH F .   ? 0.7115 0.5370 0.2404 -0.0445 0.1869  0.0660  459 HOH A O   
2437 O  O   . HOH F .   ? 0.4711 1.1896 0.3502 0.0807  0.0015  -0.1965 460 HOH A O   
2438 O  O   . HOH F .   ? 0.8194 0.3440 0.3662 -0.0785 0.1710  -0.0013 461 HOH A O   
2439 O  O   . HOH F .   ? 0.1297 0.1879 0.1493 0.0139  -0.0476 0.0002  462 HOH A O   
2440 O  O   . HOH F .   ? 0.4760 0.2344 0.2092 -0.0062 0.0399  0.0610  463 HOH A O   
2441 O  O   . HOH F .   ? 0.2520 0.1507 0.1988 -0.0416 -0.0884 0.0310  464 HOH A O   
2442 O  O   . HOH F .   ? 0.7628 0.2868 0.3615 0.0042  -0.0701 0.0301  465 HOH A O   
2443 O  O   . HOH F .   ? 0.1427 0.2013 0.3369 -0.0323 -0.0403 0.0033  466 HOH A O   
2444 O  O   . HOH F .   ? 0.1809 0.1377 0.2077 -0.0251 -0.0133 0.0190  467 HOH A O   
2445 O  O   . HOH F .   ? 0.2225 0.2342 0.3162 -0.0464 -0.0435 -0.0222 468 HOH A O   
2446 O  O   . HOH F .   ? 0.8514 0.3677 0.2481 -0.2441 -0.0788 -0.0370 469 HOH A O   
2447 O  O   . HOH F .   ? 0.6211 0.5274 0.3895 -0.0991 0.0016  -0.0234 470 HOH A O   
2448 O  O   . HOH F .   ? 0.2444 0.2480 0.3564 0.0417  -0.1801 -0.0987 471 HOH A O   
2449 O  O   . HOH F .   ? 0.3443 0.2708 0.1852 0.0916  -0.0034 0.0073  472 HOH A O   
2450 O  O   . HOH F .   ? 0.2766 0.5784 0.5388 0.1278  0.0616  -0.1298 473 HOH A O   
2451 O  O   . HOH F .   ? 0.2864 0.8911 0.3182 0.0363  0.0111  0.1481  474 HOH A O   
2452 O  O   . HOH F .   ? 0.2725 0.2795 0.3509 -0.0082 0.1439  0.1339  475 HOH A O   
2453 O  O   . HOH F .   ? 0.2182 0.3091 0.3446 0.0659  -0.0927 -0.1669 476 HOH A O   
2454 O  O   . HOH F .   ? 0.7808 0.6088 0.1605 0.0930  0.0100  0.0810  477 HOH A O   
2455 O  O   . HOH F .   ? 0.3523 0.3832 0.8399 0.0288  -0.1731 -0.0279 478 HOH A O   
2456 O  O   . HOH F .   ? 0.8323 0.2661 0.7384 -0.0417 0.1538  -0.1197 479 HOH A O   
2457 O  O   . HOH F .   ? 0.6572 0.3347 0.6572 0.0312  -0.1654 0.0110  480 HOH A O   
2458 O  O   . HOH F .   ? 0.3542 0.2875 0.2312 -0.0435 0.1177  -0.1113 481 HOH A O   
2459 O  O   . HOH F .   ? 0.4509 0.1319 0.1870 0.0000  -0.1789 0.0135  482 HOH A O   
2460 O  O   . HOH F .   ? 0.4947 0.2428 0.2181 -0.0300 -0.0612 0.1153  483 HOH A O   
2461 O  O   . HOH F .   ? 0.3343 0.3335 0.1872 0.0039  0.0215  0.0485  484 HOH A O   
2462 O  O   . HOH F .   ? 0.2313 0.2101 0.2810 0.0021  0.0381  0.0837  485 HOH A O   
2463 O  O   . HOH F .   ? 0.4907 0.2946 0.6506 -0.0298 0.0577  -0.0756 486 HOH A O   
2464 O  O   . HOH F .   ? 0.4759 0.5006 0.4639 -0.0863 -0.1738 0.0796  487 HOH A O   
2465 O  O   . HOH F .   ? 0.1273 0.1261 0.1207 -0.0244 0.0326  -0.0192 488 HOH A O   
2466 O  O   . HOH F .   ? 0.2748 0.6309 0.6768 -0.3158 0.3328  -0.1719 489 HOH A O   
2467 O  O   . HOH F .   ? 0.1584 0.2645 0.3761 0.0384  -0.0150 0.1246  490 HOH A O   
2468 O  O   . HOH F .   ? 0.2073 0.2023 0.3583 0.0037  0.1046  -0.0176 491 HOH A O   
2469 O  O   . HOH F .   ? 0.2291 0.3835 0.2780 -0.0549 -0.0018 0.0336  492 HOH A O   
2470 O  O   . HOH F .   ? 0.3449 0.2459 0.2434 -0.0570 0.0561  0.0072  493 HOH A O   
2471 O  O   . HOH F .   ? 0.1594 0.3541 0.4659 -0.0203 0.0297  0.0013  494 HOH A O   
2472 O  O   . HOH F .   ? 0.1971 0.1285 0.2215 -0.0052 -0.0397 0.0228  495 HOH A O   
2473 O  O   . HOH F .   ? 0.1588 0.1877 0.1613 0.0167  0.0150  0.0065  496 HOH A O   
2474 O  O   . HOH F .   ? 0.1890 0.3319 0.5740 -0.0443 -0.0385 0.0820  497 HOH A O   
2475 O  O   . HOH F .   ? 0.3421 0.2056 0.2130 0.0250  0.0603  0.0047  498 HOH A O   
2476 O  O   . HOH F .   ? 0.2434 0.2307 0.2176 0.0000  -0.0992 0.0299  499 HOH A O   
2477 O  O   . HOH F .   ? 0.1037 0.2138 0.1877 0.0339  0.0081  0.0115  500 HOH A O   
2478 O  O   . HOH F .   ? 0.1878 0.3334 0.2542 0.0108  0.1005  -0.0245 501 HOH A O   
2479 O  O   . HOH F .   ? 0.0861 0.1208 0.1167 0.0163  0.0111  -0.0149 502 HOH A O   
2480 O  O   . HOH F .   ? 0.0945 0.4887 0.5236 -0.0285 0.0021  -0.1638 503 HOH A O   
2481 O  O   . HOH F .   ? 0.2284 0.4414 0.2195 0.0587  -0.0375 -0.1172 504 HOH A O   
2482 O  O   . HOH F .   ? 0.4799 0.2413 0.3044 -0.0065 -0.1254 -0.0080 505 HOH A O   
2483 O  O   . HOH F .   ? 0.5284 0.2430 0.2494 -0.0753 0.1732  -0.0460 506 HOH A O   
2484 O  O   . HOH F .   ? 0.0692 0.1084 0.1305 -0.0077 0.0278  0.0047  507 HOH A O   
2485 O  O   . HOH F .   ? 0.2847 0.2073 0.2550 -0.0053 -0.0623 0.0609  508 HOH A O   
2486 O  O   . HOH F .   ? 0.7164 0.2631 0.2216 -0.0320 0.0602  0.0601  509 HOH A O   
2487 O  O   . HOH F .   ? 0.0802 0.1397 0.1247 0.0206  0.0241  -0.0024 510 HOH A O   
2488 O  O   . HOH F .   ? 0.3142 0.3523 0.3510 -0.0351 -0.1218 0.0027  511 HOH A O   
2489 O  O   . HOH F .   ? 0.1833 0.2421 0.1754 0.0372  0.0291  -0.0188 512 HOH A O   
2490 O  O   . HOH F .   ? 0.3953 0.3718 0.2779 -0.0049 -0.0188 -0.0653 513 HOH A O   
2491 O  O   . HOH F .   ? 0.2513 0.2526 0.3186 -0.0372 0.0296  -0.0423 514 HOH A O   
2492 O  O   . HOH F .   ? 0.0796 0.1585 0.2495 0.0134  0.0149  -0.0226 515 HOH A O   
2493 O  O   . HOH F .   ? 0.1850 0.2014 0.1759 -0.0147 -0.0208 -0.0005 516 HOH A O   
2494 O  O   . HOH F .   ? 0.0825 0.1671 0.3617 -0.0145 0.0142  0.0261  517 HOH A O   
2495 O  O   . HOH F .   ? 0.2035 0.2325 0.2132 -0.0178 -0.0494 -0.0036 518 HOH A O   
2496 O  O   . HOH F .   ? 0.4228 0.3528 0.6720 -0.0527 -0.0331 0.0933  519 HOH A O   
2497 O  O   . HOH F .   ? 0.2821 0.2582 0.3445 0.0027  0.0529  -0.1005 520 HOH A O   
2498 O  O   . HOH F .   ? 0.2330 0.1912 0.2240 0.0464  -0.0770 -0.0179 521 HOH A O   
2499 O  O   . HOH F .   ? 0.4199 0.4426 0.4686 0.0582  -0.0390 -0.0124 522 HOH A O   
2500 O  O   . HOH F .   ? 0.2883 0.1946 0.4080 0.0878  -0.0653 -0.0270 523 HOH A O   
2501 O  O   . HOH F .   ? 0.3486 0.1633 0.3432 0.0136  -0.1068 -0.0253 524 HOH A O   
2502 O  O   . HOH F .   ? 0.4329 0.1390 0.2191 -0.0177 -0.1523 0.0232  525 HOH A O   
2503 O  O   . HOH F .   ? 0.1442 0.1763 0.2426 -0.0221 0.0688  0.0166  526 HOH A O   
2504 O  O   . HOH F .   ? 0.4156 0.5856 0.2735 -0.1581 0.0762  -0.0401 527 HOH A O   
2505 O  O   . HOH F .   ? 0.4595 0.6314 0.5844 0.1752  0.1270  -0.0554 528 HOH A O   
2506 O  O   . HOH F .   ? 0.1943 0.2854 0.1799 0.0369  0.0581  -0.0464 529 HOH A O   
2507 O  O   . HOH F .   ? 0.6157 0.2360 0.2348 -0.1254 0.0803  -0.0621 530 HOH A O   
2508 O  O   . HOH F .   ? 0.1240 0.1591 0.2014 0.0408  0.0196  0.0127  531 HOH A O   
2509 O  O   . HOH F .   ? 0.1082 0.1518 0.1571 0.0305  -0.0153 0.0142  532 HOH A O   
2510 O  O   . HOH F .   ? 0.5708 0.2450 0.5520 -0.0160 -0.0670 -0.0633 533 HOH A O   
2511 O  O   . HOH F .   ? 0.3891 0.4151 0.4736 -0.0038 0.0337  -0.0313 534 HOH A O   
2512 O  O   . HOH F .   ? 0.2028 0.1761 0.3328 -0.0013 0.0441  -0.0352 535 HOH A O   
2513 O  O   . HOH F .   ? 0.2872 0.2877 0.2797 0.0766  0.0939  -0.0163 536 HOH A O   
2514 O  O   . HOH F .   ? 0.4481 0.4308 0.5812 -0.0187 -0.1305 0.0320  537 HOH A O   
2515 O  O   . HOH F .   ? 0.3565 0.4508 0.3125 -0.0263 0.1570  -0.1546 538 HOH A O   
2516 O  O   . HOH F .   ? 0.6692 0.5295 0.1735 0.1750  -0.2484 -0.0732 539 HOH A O   
2517 O  O   . HOH F .   ? 0.1948 0.4607 0.5219 0.1166  -0.0220 -0.0320 540 HOH A O   
2518 O  O   . HOH F .   ? 0.3434 0.3231 0.4025 0.0190  -0.0051 0.1599  541 HOH A O   
2519 O  O   . HOH F .   ? 0.2918 0.2703 0.2911 0.1001  -0.0236 -0.0555 542 HOH A O   
2520 O  O   . HOH F .   ? 0.2640 0.1582 0.5309 -0.0151 0.1080  0.0076  543 HOH A O   
2521 O  O   . HOH F .   ? 0.4196 0.3123 0.6282 0.1615  0.0158  0.0079  544 HOH A O   
2522 O  O   . HOH F .   ? 0.5263 0.3648 0.3434 0.1614  -0.1024 -0.0244 545 HOH A O   
2523 O  O   . HOH F .   ? 0.3697 0.4916 0.2358 -0.1102 -0.1064 0.1297  546 HOH A O   
2524 O  O   . HOH F .   ? 0.2418 0.3367 0.5335 0.0386  0.1373  0.1204  547 HOH A O   
2525 O  O   . HOH F .   ? 0.1813 0.1118 0.1873 -0.0392 -0.0320 0.0058  548 HOH A O   
2526 O  O   . HOH F .   ? 0.2653 0.1330 0.2172 0.0115  -0.0700 -0.0044 549 HOH A O   
2527 O  O   . HOH F .   ? 0.2310 0.2901 0.1593 0.0536  0.0087  -0.0304 550 HOH A O   
2528 O  O   . HOH F .   ? 0.3457 0.1516 0.1827 -0.0285 -0.0233 -0.0270 551 HOH A O   
2529 O  O   . HOH F .   ? 0.6174 0.2818 0.4597 0.0331  0.1119  -0.1074 552 HOH A O   
2530 O  O   . HOH F .   ? 0.1374 0.4090 0.5043 0.0054  -0.0609 0.1087  553 HOH A O   
2531 O  O   . HOH F .   ? 0.2509 0.2030 0.2040 0.0403  0.0779  0.1050  554 HOH A O   
2532 O  O   . HOH F .   ? 0.2400 0.2707 0.3087 -0.0311 0.0439  0.0148  555 HOH A O   
2533 O  O   . HOH F .   ? 0.2057 0.1424 0.1882 0.0150  0.0000  0.0242  556 HOH A O   
2534 O  O   . HOH F .   ? 0.0508 0.2079 0.3375 0.0132  0.0263  -0.0724 557 HOH A O   
2535 O  O   . HOH F .   ? 0.4879 0.4472 0.4475 -0.2120 -0.2785 -0.0842 558 HOH A O   
2536 O  O   . HOH F .   ? 0.4428 0.2490 0.6700 0.0247  -0.0389 0.0677  559 HOH A O   
2537 O  O   . HOH F .   ? 0.3732 0.4602 0.3049 0.0507  -0.0272 0.1489  560 HOH A O   
2538 O  O   . HOH F .   ? 0.4487 0.2575 0.2548 -0.0314 0.0272  0.0623  561 HOH A O   
2539 O  O   . HOH F .   ? 0.3235 0.2647 0.4591 -0.0590 0.0064  0.1472  562 HOH A O   
2540 O  O   . HOH F .   ? 0.4309 0.4659 0.8748 -0.0539 0.0496  -0.0162 563 HOH A O   
2541 O  O   . HOH F .   ? 0.3945 0.3107 0.2424 0.0939  -0.0681 -0.0832 564 HOH A O   
2542 O  O   . HOH F .   ? 0.3218 0.2606 0.3676 0.0164  -0.0468 -0.0405 565 HOH A O   
2543 O  O   . HOH F .   ? 0.3245 0.3064 0.4148 0.0749  0.1373  -0.0068 566 HOH A O   
2544 O  O   . HOH F .   ? 0.1886 0.2873 0.2782 0.0115  -0.0657 -0.0179 567 HOH A O   
2545 O  O   . HOH F .   ? 0.3753 0.5098 0.4870 -0.2392 0.0619  -0.0267 568 HOH A O   
2546 O  O   . HOH F .   ? 0.2620 0.2041 0.3159 -0.0188 0.0715  -0.0257 569 HOH A O   
2547 O  O   . HOH F .   ? 0.4148 0.2181 0.3237 0.1050  -0.0162 0.0677  570 HOH A O   
2548 O  O   . HOH F .   ? 0.4685 0.3836 0.2253 0.2559  -0.0748 -0.0200 571 HOH A O   
2549 O  O   . HOH F .   ? 0.4137 0.7886 0.5295 -0.0080 0.1175  0.1541  572 HOH A O   
2550 O  O   . HOH F .   ? 0.6515 0.3785 0.4238 0.0287  -0.0154 -0.1182 573 HOH A O   
2551 O  O   . HOH F .   ? 0.2736 0.2389 0.2603 0.0524  -0.0750 -0.0813 574 HOH A O   
2552 O  O   . HOH F .   ? 0.3285 0.2265 0.1874 0.0569  -0.0300 0.0427  575 HOH A O   
2553 O  O   . HOH F .   ? 0.5781 0.1925 0.2860 -0.0946 -0.2205 -0.0195 576 HOH A O   
2554 O  O   . HOH F .   ? 0.1197 0.2544 0.1941 -0.0013 -0.0674 0.0348  577 HOH A O   
2555 O  O   . HOH F .   ? 0.6690 0.3966 0.1707 0.1524  0.0229  0.0051  578 HOH A O   
2556 O  O   . HOH F .   ? 0.3420 0.5565 0.3389 0.0067  -0.1050 -0.1658 579 HOH A O   
2557 O  O   . HOH F .   ? 0.5321 0.4288 0.4576 -0.0414 -0.0272 0.0172  580 HOH A O   
2558 O  O   . HOH F .   ? 0.4339 0.1913 0.2419 -0.0066 -0.0477 0.0069  581 HOH A O   
2559 O  O   . HOH F .   ? 0.2520 0.7777 0.5970 0.0421  0.0100  -0.1402 582 HOH A O   
2560 O  O   . HOH F .   ? 0.2227 0.2775 0.3488 -0.0022 0.0587  -0.0037 583 HOH A O   
2561 O  O   . HOH F .   ? 0.5554 0.2472 0.3439 0.1952  -0.1527 -0.1273 584 HOH A O   
2562 O  O   . HOH F .   ? 0.2127 0.2658 0.3315 -0.1075 0.0394  -0.1223 585 HOH A O   
2563 O  O   . HOH F .   ? 0.2043 0.2699 0.3475 0.1254  0.0064  0.0001  586 HOH A O   
2564 O  O   . HOH F .   ? 0.0890 0.1257 0.1947 0.0184  -0.0064 -0.0138 587 HOH A O   
2565 O  O   . HOH F .   ? 0.1962 0.3774 0.2742 0.1068  -0.0849 -0.0575 588 HOH A O   
2566 O  O   . HOH F .   ? 0.1693 0.4376 0.2094 -0.0815 -0.0079 0.0682  589 HOH A O   
2567 O  O   . HOH F .   ? 0.1842 0.3173 0.5254 -0.0163 0.0604  0.0573  590 HOH A O   
2568 O  O   . HOH F .   ? 0.4930 0.3850 0.4577 -0.0194 -0.0249 -0.0389 591 HOH A O   
2569 O  O   . HOH F .   ? 0.3298 0.4655 0.1457 0.1151  -0.1310 -0.0155 592 HOH A O   
2570 O  O   . HOH F .   ? 0.2906 0.2481 0.7821 -0.1153 0.1819  0.0366  593 HOH A O   
2571 O  O   . HOH F .   ? 0.3980 0.5024 0.4855 0.1304  -0.0803 -0.0635 594 HOH A O   
2572 O  O   . HOH F .   ? 0.9508 0.6516 0.6230 0.1311  0.1348  0.0516  595 HOH A O   
2573 O  O   . HOH F .   ? 0.4176 0.2927 0.3583 0.0219  0.2055  -0.0685 596 HOH A O   
2574 O  O   . HOH F .   ? 0.4167 0.3630 0.2825 0.1313  0.0522  -0.0756 597 HOH A O   
2575 O  O   . HOH F .   ? 0.3964 0.2989 0.3107 0.1038  0.0987  0.0006  598 HOH A O   
2576 O  O   . HOH F .   ? 0.3971 0.2742 0.2890 0.0589  -0.0248 -0.0403 599 HOH A O   
2577 O  O   . HOH F .   ? 0.7095 0.4629 0.6475 0.1834  -0.2285 0.1805  600 HOH A O   
2578 O  O   . HOH F .   ? 0.1442 0.1652 0.4516 -0.0026 -0.0502 0.0311  601 HOH A O   
2579 O  O   . HOH F .   ? 0.5141 0.3287 0.2382 -0.1001 -0.0482 -0.0021 602 HOH A O   
2580 O  O   . HOH F .   ? 0.3146 0.3396 0.2579 0.0190  -0.0893 -0.0093 603 HOH A O   
2581 O  O   . HOH F .   ? 0.3527 0.6303 0.5499 -0.0257 -0.1079 0.2912  604 HOH A O   
2582 O  O   . HOH F .   ? 0.3184 0.2757 0.2350 -0.0292 -0.0209 -0.0355 605 HOH A O   
2583 O  O   . HOH F .   ? 0.4744 0.7047 0.2795 -0.0052 -0.0872 0.2007  606 HOH A O   
2584 O  O   . HOH F .   ? 0.3030 0.4847 0.7893 0.2749  0.1067  0.2128  607 HOH A O   
2585 O  O   . HOH F .   ? 0.1961 0.6355 0.7745 -0.0775 0.2643  0.0460  608 HOH A O   
2586 O  O   . HOH F .   ? 0.3872 0.2576 0.1976 0.1119  0.0052  0.0212  609 HOH A O   
2587 O  O   . HOH F .   ? 0.2669 0.1468 0.1953 0.0438  0.0279  -0.0138 610 HOH A O   
2588 O  O   . HOH F .   ? 0.2414 0.4202 0.7810 0.0034  -0.1314 -0.0173 611 HOH A O   
2589 O  O   . HOH F .   ? 0.3112 0.4159 0.4291 0.1537  0.0996  0.0772  612 HOH A O   
2590 O  O   . HOH F .   ? 0.4902 0.3475 0.2242 -0.0972 0.0421  0.1241  613 HOH A O   
2591 O  O   . HOH F .   ? 0.1758 0.3538 0.4657 0.0771  0.1149  0.0912  614 HOH A O   
2592 O  O   . HOH F .   ? 0.3896 0.1964 0.4568 0.0355  0.1101  0.1076  615 HOH A O   
2593 O  O   . HOH F .   ? 0.3151 0.2407 0.2612 0.0467  0.0702  0.0344  616 HOH A O   
2594 O  O   . HOH F .   ? 0.4949 0.3450 0.2211 0.0291  0.0602  -0.0032 617 HOH A O   
2595 O  O   . HOH F .   ? 0.7368 0.4788 0.6531 0.1064  -0.2743 -0.0961 618 HOH A O   
2596 O  O   . HOH F .   ? 0.2279 0.2359 0.5935 -0.0260 -0.0066 0.0206  619 HOH A O   
2597 O  O   . HOH F .   ? 0.3495 0.4111 0.1855 -0.0043 0.1005  0.0756  620 HOH A O   
2598 O  O   . HOH F .   ? 0.5365 0.2974 0.2162 0.0671  -0.1430 0.0044  621 HOH A O   
2599 O  O   . HOH F .   ? 0.5032 0.2484 0.3360 0.0666  0.1762  0.0565  622 HOH A O   
2600 O  O   . HOH F .   ? 0.2246 0.4210 0.3984 0.0127  -0.0278 -0.1018 623 HOH A O   
2601 O  O   . HOH F .   ? 0.1443 0.1454 0.1778 -0.0079 -0.0214 -0.0046 624 HOH A O   
2602 O  O   . HOH F .   ? 0.1905 0.6670 0.3001 -0.0107 0.0605  -0.1243 625 HOH A O   
2603 O  O   . HOH F .   ? 0.3873 0.5126 0.3838 0.0089  -0.0320 -0.0495 626 HOH A O   
2604 O  O   . HOH F .   ? 0.4172 0.5865 0.5759 0.0618  -0.0980 -0.1237 627 HOH A O   
2605 O  O   . HOH F .   ? 0.2153 0.4664 0.4354 0.1197  0.0159  0.0507  628 HOH A O   
2606 O  O   . HOH F .   ? 0.3323 0.4235 0.5963 0.0094  0.0805  0.1280  629 HOH A O   
2607 O  O   . HOH F .   ? 0.3495 0.6418 0.4369 0.2503  -0.0963 -0.1886 630 HOH A O   
2608 O  O   . HOH F .   ? 0.6485 0.5727 0.4273 0.3068  -0.1808 -0.0921 631 HOH A O   
2609 O  O   . HOH F .   ? 0.5287 0.5368 0.7040 0.0661  0.0504  -0.0553 632 HOH A O   
2610 O  O   . HOH F .   ? 0.3579 0.4628 0.3653 0.0559  0.0922  0.0511  633 HOH A O   
2611 O  O   . HOH F .   ? 0.2235 0.2744 0.7005 0.0215  0.0902  0.0431  634 HOH A O   
2612 O  O   . HOH F .   ? 0.6115 0.7031 0.3977 -0.0425 -0.1150 0.2011  635 HOH A O   
2613 O  O   . HOH F .   ? 0.3328 0.3234 0.5271 0.0571  0.0278  0.0672  636 HOH A O   
2614 O  O   . HOH F .   ? 0.3305 0.2630 0.3849 -0.0673 0.0926  -0.0838 637 HOH A O   
2615 O  O   . HOH F .   ? 0.7141 0.7253 1.0569 -0.1544 0.0153  -0.1208 638 HOH A O   
2616 O  O   . HOH F .   ? 0.4161 0.3367 0.3310 0.0581  0.0948  0.0780  639 HOH A O   
2617 O  O   . HOH F .   ? 0.3188 0.2800 0.3726 0.1011  -0.2076 -0.0662 640 HOH A O   
2618 O  O   . HOH F .   ? 0.4792 0.2801 0.4909 0.0762  -0.0060 0.0209  641 HOH A O   
2619 O  O   . HOH F .   ? 0.3035 0.3367 0.4544 0.0908  0.0793  0.1233  642 HOH A O   
2620 O  O   . HOH F .   ? 0.2828 0.2953 0.6399 0.0603  -0.0381 -0.0433 643 HOH A O   
2621 O  O   . HOH F .   ? 0.2626 0.9602 0.4359 -0.0628 0.0427  0.1110  644 HOH A O   
2622 O  O   . HOH F .   ? 0.2636 0.5586 0.7070 -0.0560 -0.0436 0.1699  645 HOH A O   
2623 O  O   . HOH F .   ? 0.3561 0.3225 0.6001 -0.0094 0.1620  0.1448  646 HOH A O   
2624 O  O   . HOH F .   ? 0.3729 0.5032 0.4531 0.0304  0.1708  0.0305  647 HOH A O   
2625 O  O   . HOH F .   ? 0.4755 0.4583 0.2990 -0.0017 -0.0571 0.0105  648 HOH A O   
2626 O  O   . HOH F .   ? 0.2403 0.8047 0.9622 0.0620  0.1055  0.2825  649 HOH A O   
2627 O  O   . HOH F .   ? 0.3115 0.7771 0.5310 -0.0812 0.0961  -0.1159 650 HOH A O   
2628 O  O   . HOH F .   ? 0.2953 0.3384 0.4461 0.1421  -0.0615 0.0223  651 HOH A O   
2629 O  O   . HOH F .   ? 0.2903 0.3488 0.7122 0.0089  -0.0066 0.0950  652 HOH A O   
2630 O  O   . HOH F .   ? 0.3657 0.4449 0.2790 -0.1815 -0.0077 0.0488  653 HOH A O   
2631 O  O   . HOH F .   ? 0.5921 0.6395 0.6862 0.3049  -0.3659 -0.2348 654 HOH A O   
2632 O  O   . HOH F .   ? 0.3336 0.3711 0.4752 0.0158  -0.1815 -0.0803 655 HOH A O   
2633 O  O   . HOH F .   ? 0.3508 0.5254 0.6535 0.1681  0.0214  0.1957  656 HOH A O   
2634 O  O   . HOH F .   ? 0.2931 0.3484 0.4804 -0.0886 -0.0535 -0.0961 657 HOH A O   
2635 O  O   . HOH F .   ? 0.3647 0.3935 0.5863 -0.0669 -0.0151 0.0831  658 HOH A O   
2636 O  O   . HOH F .   ? 0.8034 0.4660 0.5096 0.0813  -0.1272 0.1166  659 HOH A O   
2637 O  O   . HOH F .   ? 0.6706 0.3041 0.2624 -0.0255 -0.0714 -0.0630 660 HOH A O   
2638 O  O   . HOH F .   ? 0.2776 0.3637 0.2849 -0.0532 0.0255  -0.0436 661 HOH A O   
2639 O  O   . HOH F .   ? 0.3276 0.3538 0.5983 0.1084  0.0290  -0.0143 662 HOH A O   
2640 O  O   . HOH F .   ? 0.3015 0.4831 0.3867 -0.0170 0.1361  -0.0254 663 HOH A O   
2641 O  O   . HOH F .   ? 0.4913 0.3778 0.4739 0.0179  0.0093  -0.0294 664 HOH A O   
2642 O  O   . HOH F .   ? 0.2594 0.3653 0.5536 0.1256  -0.0885 -0.1638 665 HOH A O   
2643 O  O   . HOH F .   ? 0.4174 0.4806 0.7371 0.1995  0.2528  0.2100  666 HOH A O   
2644 O  O   . HOH F .   ? 0.2498 0.3216 0.7377 -0.0669 0.0136  0.1033  667 HOH A O   
2645 O  O   . HOH F .   ? 0.2906 0.3673 0.2901 -0.0095 0.0069  0.0046  668 HOH A O   
2646 O  O   . HOH F .   ? 0.4119 0.2851 0.5118 0.1542  0.1321  0.0305  669 HOH A O   
2647 O  O   . HOH F .   ? 0.5000 0.4798 0.5011 -0.0041 -0.0469 0.0671  670 HOH A O   
2648 O  O   . HOH F .   ? 0.7097 0.4106 0.5070 0.1927  0.0193  0.1165  671 HOH A O   
2649 O  O   . HOH F .   ? 0.4016 0.3410 0.4891 0.0526  0.0813  -0.0478 672 HOH A O   
2650 O  O   . HOH F .   ? 0.4707 0.4978 0.6500 -0.0842 0.0687  0.0660  673 HOH A O   
2651 O  O   . HOH F .   ? 0.5831 0.3270 0.4994 -0.1688 -0.0644 0.0385  674 HOH A O   
2652 O  O   . HOH F .   ? 0.4334 0.5572 0.3998 -0.0652 0.1410  0.1839  675 HOH A O   
2653 O  O   . HOH F .   ? 0.4188 0.4913 0.4647 0.0183  -0.0084 0.0286  676 HOH A O   
2654 O  O   . HOH F .   ? 0.2935 0.3157 0.6336 0.0942  0.0507  0.0680  677 HOH A O   
2655 O  O   . HOH F .   ? 0.5613 0.2891 0.4234 0.0307  -0.0819 -0.0544 678 HOH A O   
2656 O  O   . HOH F .   ? 0.2773 0.2663 0.3549 0.0079  -0.0223 0.0467  679 HOH A O   
2657 O  O   . HOH F .   ? 0.7758 0.7665 0.5018 -0.2991 -0.0762 -0.1415 680 HOH A O   
2658 O  O   . HOH F .   ? 0.2136 0.2528 0.2492 0.0089  0.0510  -0.0188 681 HOH A O   
2659 O  O   . HOH F .   ? 0.3016 0.4073 0.5072 0.0229  -0.1041 0.0385  682 HOH A O   
2660 O  O   . HOH F .   ? 0.4703 0.3328 0.2129 0.0281  0.0748  -0.1054 683 HOH A O   
2661 O  O   . HOH F .   ? 0.2143 0.2716 0.2377 0.0686  -0.0447 0.0075  684 HOH A O   
2662 O  O   . HOH F .   ? 0.4493 0.4200 0.5005 -0.0913 -0.0510 -0.2573 685 HOH A O   
2663 O  O   . HOH F .   ? 0.4564 0.3756 0.3518 -0.1574 0.0693  -0.1228 686 HOH A O   
2664 O  O   . HOH F .   ? 0.3107 0.5544 0.5400 -0.0166 0.0469  -0.3138 687 HOH A O   
2665 O  O   . HOH F .   ? 0.3199 0.4892 0.5098 -0.0433 0.1158  -0.2027 688 HOH A O   
2666 O  O   . HOH F .   ? 0.3236 0.4784 0.4183 -0.0649 -0.1182 0.0974  689 HOH A O   
2667 O  O   . HOH F .   ? 0.2764 0.1875 0.3843 -0.0008 0.1338  -0.0161 690 HOH A O   
2668 O  O   . HOH F .   ? 0.4813 0.3461 0.2667 0.0424  -0.1401 -0.0519 691 HOH A O   
2669 O  O   . HOH F .   ? 0.4599 0.3860 0.4661 0.1323  -0.0831 -0.0704 692 HOH A O   
2670 O  O   . HOH F .   ? 0.5003 0.3424 0.4807 0.0218  0.1232  0.0215  693 HOH A O   
2671 O  O   . HOH F .   ? 0.4320 0.3553 0.2133 0.0316  -0.1167 -0.0033 694 HOH A O   
2672 O  O   . HOH F .   ? 0.3168 0.9972 0.6189 0.2182  0.1360  -0.0952 697 HOH A O   
# 
