data_5LL4
# 
_entry.id   5LL4 
# 
_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   5LL4         pdb_00005ll4 10.2210/pdb5ll4/pdb 
WWPDB D_1200000926 ?            ?                   
# 
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 2017-08-16 
2 'Structure model' 1 1 2024-01-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' diffrn_radiation_wavelength   
5 2 'Structure model' pdbx_initial_refinement_model 
6 2 'Structure model' struct_conn                   
# 
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' '_database_2.pdbx_DOI'                
2  2 'Structure model' '_database_2.pdbx_database_accession' 
3  2 'Structure model' '_struct_conn.pdbx_dist_value'        
4  2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
5  2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  2 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  2 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  2 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'     
12 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
13 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
14 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
15 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
16 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5LL4 
_pdbx_database_status.recvd_initial_deposition_date   2016-07-26 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_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            Chemistryselect 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2365-6549 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Combinatorial Design of Isoform-Selective N-Alkylated Benzimidazole-Based Inhibitors of Carbonic Anhydrases' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/slct.201700531 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'   1 ? 
primary 'Linkuviene, V.'     2 ? 
primary 'Smirnov, A.'        3 ? 
primary 'Milinaviciute, G.'  4 ? 
primary 'Timm, D.'           5 ? 
primary 'Kasiliauskaite, A.' 6 ? 
primary 'Manakova, E.'       7 ? 
primary 'Grazulis, S.'       8 ? 
primary 'Matulis, D.'        9 ? 
# 
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'                                29289.062 2   4.2.1.1 ? 'human carbonic anhydrase II' ? 
2 non-polymer syn 'ZINC ION'                                            65.409    2   ?       ? 
'4-(1H-benzimidazol-1-ylacetyl)benzenesulfonamide' ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                  78.133    2   ?       ? Zn ? 
4 non-polymer syn BICINE                                                163.172   2   ?       ? DMS ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                               106.120   1   ?       ? BCN ? 
6 non-polymer syn 'MALONIC ACID'                                        104.061   2   ?       ? PEG ? 
7 non-polymer syn '4-[2-(benzimidazol-1-yl)ethanoyl]benzenesulfonamide' 315.347   2   ?       ? DXX ? 
8 water       nat water                                                 18.015    652 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A,B 
_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 'DI(HYDROXYETHYL)ETHER'                               PEG 
6 'MALONIC ACID'                                        MLA 
7 '4-[2-(benzimidazol-1-yl)ethanoyl]benzenesulfonamide' 6YH 
8 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  ALA n 
1 66  PHE n 
1 67  ASN 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  ILE 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 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU 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 
6YH non-polymer         . '4-[2-(benzimidazol-1-yl)ethanoyl]benzenesulfonamide' ? 'C15 H13 N3 O3 S' 315.347 
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 
MLA non-polymer         . 'MALONIC ACID'                                        
'DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID; METHANEDICARBOXYLIC ACID' 'C3 H4 O4'        104.061 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                               ? 'C4 H10 O3'       106.120 
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   1   MET MET A . n 
A 1 2   SER 2   2   2   SER SER A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN 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  ILE 91  91  91  ILE ILE 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 PHE 130 131 131 PHE PHE 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 VAL 134 135 135 VAL VAL 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 LEU 203 204 204 LEU LEU 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 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   2   SER SER B . n 
B 1 3   HIS 3   3   3   HIS HIS B . n 
B 1 4   HIS 4   4   4   HIS HIS B . n 
B 1 5   TRP 5   5   5   TRP TRP B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   TYR 7   7   7   TYR TYR B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  HIS 10  10  10  HIS HIS B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  HIS 15  15  15  HIS HIS B . n 
B 1 16  TRP 16  16  16  TRP TRP B . n 
B 1 17  HIS 17  17  17  HIS HIS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  HIS 36  36  36  HIS HIS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  GLN 53  53  53  GLN GLN B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  PRO 83  83  83  PRO PRO B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  GLN 92  92  92  GLN GLN B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  TRP 97  97  97  TRP TRP B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 TRP 123 123 123 TRP TRP B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 LYS 126 127 127 LYS LYS B . n 
B 1 127 TYR 127 128 128 TYR TYR B . n 
B 1 128 GLY 128 129 129 GLY GLY B . n 
B 1 129 ASP 129 130 130 ASP ASP B . n 
B 1 130 PHE 130 131 131 PHE PHE B . n 
B 1 131 GLY 131 132 132 GLY GLY B . n 
B 1 132 LYS 132 133 133 LYS LYS B . n 
B 1 133 ALA 133 134 134 ALA ALA B . n 
B 1 134 VAL 134 135 135 VAL VAL B . n 
B 1 135 GLN 135 136 136 GLN GLN B . n 
B 1 136 GLN 136 137 137 GLN GLN B . n 
B 1 137 PRO 137 138 138 PRO PRO B . n 
B 1 138 ASP 138 139 139 ASP ASP B . n 
B 1 139 GLY 139 140 140 GLY GLY B . n 
B 1 140 LEU 140 141 141 LEU LEU B . n 
B 1 141 ALA 141 142 142 ALA ALA B . n 
B 1 142 VAL 142 143 143 VAL VAL B . n 
B 1 143 LEU 143 144 144 LEU LEU B . n 
B 1 144 GLY 144 145 145 GLY GLY B . n 
B 1 145 ILE 145 146 146 ILE ILE B . n 
B 1 146 PHE 146 147 147 PHE PHE B . n 
B 1 147 LEU 147 148 148 LEU LEU B . n 
B 1 148 LYS 148 149 149 LYS LYS B . n 
B 1 149 VAL 149 150 150 VAL VAL B . n 
B 1 150 GLY 150 151 151 GLY GLY B . n 
B 1 151 SER 151 152 152 SER SER B . n 
B 1 152 ALA 152 153 153 ALA ALA B . n 
B 1 153 LYS 153 154 154 LYS LYS B . n 
B 1 154 PRO 154 155 155 PRO PRO B . n 
B 1 155 GLY 155 156 156 GLY GLY B . n 
B 1 156 LEU 156 157 157 LEU LEU B . n 
B 1 157 GLN 157 158 158 GLN GLN B . n 
B 1 158 LYS 158 159 159 LYS LYS B . n 
B 1 159 VAL 159 160 160 VAL VAL B . n 
B 1 160 VAL 160 161 161 VAL VAL B . n 
B 1 161 ASP 161 162 162 ASP ASP B . n 
B 1 162 VAL 162 163 163 VAL VAL B . n 
B 1 163 LEU 163 164 164 LEU LEU B . n 
B 1 164 ASP 164 165 165 ASP ASP B . n 
B 1 165 SER 165 166 166 SER SER B . n 
B 1 166 ILE 166 167 167 ILE ILE B . n 
B 1 167 LYS 167 168 168 LYS LYS B . n 
B 1 168 THR 168 169 169 THR THR B . n 
B 1 169 LYS 169 170 170 LYS LYS B . n 
B 1 170 GLY 170 171 171 GLY GLY B . n 
B 1 171 LYS 171 172 172 LYS LYS B . n 
B 1 172 SER 172 173 173 SER SER B . n 
B 1 173 ALA 173 174 174 ALA ALA B . n 
B 1 174 ASP 174 175 175 ASP ASP B . n 
B 1 175 PHE 175 176 176 PHE PHE B . n 
B 1 176 THR 176 177 177 THR THR B . n 
B 1 177 ASN 177 178 178 ASN ASN B . n 
B 1 178 PHE 178 179 179 PHE PHE B . n 
B 1 179 ASP 179 180 180 ASP ASP B . n 
B 1 180 PRO 180 181 181 PRO PRO B . n 
B 1 181 ARG 181 182 182 ARG ARG B . n 
B 1 182 GLY 182 183 183 GLY GLY B . n 
B 1 183 LEU 183 184 184 LEU LEU B . n 
B 1 184 LEU 184 185 185 LEU LEU B . n 
B 1 185 PRO 185 186 186 PRO PRO B . n 
B 1 186 GLU 186 187 187 GLU GLU B . n 
B 1 187 SER 187 188 188 SER SER B . n 
B 1 188 LEU 188 189 189 LEU LEU B . n 
B 1 189 ASP 189 190 190 ASP ASP B . n 
B 1 190 TYR 190 191 191 TYR TYR B . n 
B 1 191 TRP 191 192 192 TRP TRP B . n 
B 1 192 THR 192 193 193 THR THR B . n 
B 1 193 TYR 193 194 194 TYR TYR B . n 
B 1 194 PRO 194 195 195 PRO PRO B . n 
B 1 195 GLY 195 196 196 GLY GLY B . n 
B 1 196 SER 196 197 197 SER SER B . n 
B 1 197 LEU 197 198 198 LEU LEU B . n 
B 1 198 THR 198 199 199 THR THR B . n 
B 1 199 THR 199 200 200 THR THR B . n 
B 1 200 PRO 200 201 201 PRO PRO B . n 
B 1 201 PRO 201 202 202 PRO PRO B . n 
B 1 202 LEU 202 203 203 LEU LEU B . n 
B 1 203 LEU 203 204 204 LEU LEU B . n 
B 1 204 GLU 204 205 205 GLU GLU B . n 
B 1 205 CYS 205 206 206 CYS CYS B . n 
B 1 206 VAL 206 207 207 VAL VAL B . n 
B 1 207 THR 207 208 208 THR THR B . n 
B 1 208 TRP 208 209 209 TRP TRP B . n 
B 1 209 ILE 209 210 210 ILE ILE B . n 
B 1 210 VAL 210 211 211 VAL VAL B . n 
B 1 211 LEU 211 212 212 LEU LEU B . n 
B 1 212 LYS 212 213 213 LYS LYS B . n 
B 1 213 GLU 213 214 214 GLU GLU B . n 
B 1 214 PRO 214 215 215 PRO PRO B . n 
B 1 215 ILE 215 216 216 ILE ILE B . n 
B 1 216 SER 216 217 217 SER SER B . n 
B 1 217 VAL 217 218 218 VAL VAL B . n 
B 1 218 SER 218 219 219 SER SER B . n 
B 1 219 SER 219 220 220 SER SER B . n 
B 1 220 GLU 220 221 221 GLU GLU B . n 
B 1 221 GLN 221 222 222 GLN GLN B . n 
B 1 222 VAL 222 223 223 VAL VAL B . n 
B 1 223 LEU 223 224 224 LEU LEU B . n 
B 1 224 LYS 224 225 225 LYS LYS B . n 
B 1 225 PHE 225 226 226 PHE PHE B . n 
B 1 226 ARG 226 227 227 ARG ARG B . n 
B 1 227 LYS 227 228 228 LYS LYS B . n 
B 1 228 LEU 228 229 229 LEU LEU B . n 
B 1 229 ASN 229 230 230 ASN ASN B . n 
B 1 230 PHE 230 231 231 PHE PHE B . n 
B 1 231 ASN 231 232 232 ASN ASN B . n 
B 1 232 GLY 232 233 233 GLY GLY B . n 
B 1 233 GLU 233 234 234 GLU GLU B . n 
B 1 234 GLY 234 235 235 GLY GLY B . n 
B 1 235 GLU 235 236 236 GLU GLU B . n 
B 1 236 PRO 236 237 237 PRO PRO B . n 
B 1 237 GLU 237 238 238 GLU GLU B . n 
B 1 238 GLU 238 239 239 GLU GLU B . n 
B 1 239 LEU 239 240 240 LEU LEU B . n 
B 1 240 MET 240 241 241 MET MET B . n 
B 1 241 VAL 241 242 242 VAL VAL B . n 
B 1 242 ASP 242 243 243 ASP ASP B . n 
B 1 243 ASN 243 244 244 ASN ASN B . n 
B 1 244 TRP 244 245 245 TRP TRP B . n 
B 1 245 ARG 245 246 246 ARG ARG B . n 
B 1 246 PRO 246 247 247 PRO PRO B . n 
B 1 247 ALA 247 248 248 ALA ALA B . n 
B 1 248 GLN 248 249 249 GLN GLN B . n 
B 1 249 PRO 249 250 250 PRO PRO B . n 
B 1 250 LEU 250 251 251 LEU LEU B . n 
B 1 251 LYS 251 252 252 LYS LYS B . n 
B 1 252 ASN 252 253 253 ASN ASN B . n 
B 1 253 ARG 253 254 254 ARG ARG B . n 
B 1 254 GLN 254 255 255 GLN GLN B . n 
B 1 255 ILE 255 256 256 ILE ILE B . n 
B 1 256 LYS 256 257 257 LYS LYS B . n 
B 1 257 ALA 257 258 258 ALA ALA B . n 
B 1 258 SER 258 259 259 SER SER B . n 
B 1 259 PHE 259 260 260 PHE PHE B . n 
B 1 260 LYS 260 261 261 LYS LYS B . 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 
C 2 ZN  1   301 1   ZN  ZN  A . 
D 3 DMS 1   302 1   DMS DMS A . 
E 4 BCN 1   303 4   BCN BCN A . 
F 5 PEG 1   304 5   PEG PEG A . 
G 6 MLA 1   305 7   MLA DXX A . 
H 7 6YH 1   306 1   6YH E16 A . 
I 2 ZN  1   301 2   ZN  ZN  B . 
J 3 DMS 1   302 2   DMS DMS B . 
K 4 BCN 1   303 3   BCN BCN B . 
L 6 MLA 1   304 6   MLA DXX B . 
M 7 6YH 1   305 2   6YH E16 B . 
N 8 HOH 1   401 196 HOH HOH A . 
N 8 HOH 2   402 603 HOH HOH A . 
N 8 HOH 3   403 357 HOH HOH A . 
N 8 HOH 4   404 440 HOH HOH A . 
N 8 HOH 5   405 225 HOH HOH A . 
N 8 HOH 6   406 506 HOH HOH A . 
N 8 HOH 7   407 551 HOH HOH A . 
N 8 HOH 8   408 528 HOH HOH A . 
N 8 HOH 9   409 375 HOH HOH A . 
N 8 HOH 10  410 213 HOH HOH A . 
N 8 HOH 11  411 594 HOH HOH A . 
N 8 HOH 12  412 516 HOH HOH A . 
N 8 HOH 13  413 285 HOH HOH A . 
N 8 HOH 14  414 159 HOH HOH A . 
N 8 HOH 15  415 426 HOH HOH A . 
N 8 HOH 16  416 549 HOH HOH A . 
N 8 HOH 17  417 522 HOH HOH A . 
N 8 HOH 18  418 391 HOH HOH A . 
N 8 HOH 19  419 534 HOH HOH A . 
N 8 HOH 20  420 101 HOH HOH A . 
N 8 HOH 21  421 635 HOH HOH A . 
N 8 HOH 22  422 1   HOH HOH A . 
N 8 HOH 23  423 530 HOH HOH A . 
N 8 HOH 24  424 36  HOH HOH A . 
N 8 HOH 25  425 125 HOH HOH A . 
N 8 HOH 26  426 508 HOH HOH A . 
N 8 HOH 27  427 537 HOH HOH A . 
N 8 HOH 28  428 543 HOH HOH A . 
N 8 HOH 29  429 275 HOH HOH A . 
N 8 HOH 30  430 554 HOH HOH A . 
N 8 HOH 31  431 263 HOH HOH A . 
N 8 HOH 32  432 424 HOH HOH A . 
N 8 HOH 33  433 625 HOH HOH A . 
N 8 HOH 34  434 142 HOH HOH A . 
N 8 HOH 35  435 346 HOH HOH A . 
N 8 HOH 36  436 411 HOH HOH A . 
N 8 HOH 37  437 459 HOH HOH A . 
N 8 HOH 38  438 479 HOH HOH A . 
N 8 HOH 39  439 341 HOH HOH A . 
N 8 HOH 40  440 450 HOH HOH A . 
N 8 HOH 41  441 333 HOH HOH A . 
N 8 HOH 42  442 45  HOH HOH A . 
N 8 HOH 43  443 27  HOH HOH A . 
N 8 HOH 44  444 507 HOH HOH A . 
N 8 HOH 45  445 339 HOH HOH A . 
N 8 HOH 46  446 112 HOH HOH A . 
N 8 HOH 47  447 431 HOH HOH A . 
N 8 HOH 48  448 29  HOH HOH A . 
N 8 HOH 49  449 146 HOH HOH A . 
N 8 HOH 50  450 158 HOH HOH A . 
N 8 HOH 51  451 23  HOH HOH A . 
N 8 HOH 52  452 172 HOH HOH A . 
N 8 HOH 53  453 181 HOH HOH A . 
N 8 HOH 54  454 648 HOH HOH A . 
N 8 HOH 55  455 105 HOH HOH A . 
N 8 HOH 56  456 260 HOH HOH A . 
N 8 HOH 57  457 446 HOH HOH A . 
N 8 HOH 58  458 131 HOH HOH A . 
N 8 HOH 59  459 68  HOH HOH A . 
N 8 HOH 60  460 514 HOH HOH A . 
N 8 HOH 61  461 274 HOH HOH A . 
N 8 HOH 62  462 188 HOH HOH A . 
N 8 HOH 63  463 634 HOH HOH A . 
N 8 HOH 64  464 605 HOH HOH A . 
N 8 HOH 65  465 56  HOH HOH A . 
N 8 HOH 66  466 199 HOH HOH A . 
N 8 HOH 67  467 377 HOH HOH A . 
N 8 HOH 68  468 33  HOH HOH A . 
N 8 HOH 69  469 278 HOH HOH A . 
N 8 HOH 70  470 627 HOH HOH A . 
N 8 HOH 71  471 151 HOH HOH A . 
N 8 HOH 72  472 417 HOH HOH A . 
N 8 HOH 73  473 205 HOH HOH A . 
N 8 HOH 74  474 127 HOH HOH A . 
N 8 HOH 75  475 167 HOH HOH A . 
N 8 HOH 76  476 76  HOH HOH A . 
N 8 HOH 77  477 284 HOH HOH A . 
N 8 HOH 78  478 77  HOH HOH A . 
N 8 HOH 79  479 368 HOH HOH A . 
N 8 HOH 80  480 60  HOH HOH A . 
N 8 HOH 81  481 124 HOH HOH A . 
N 8 HOH 82  482 300 HOH HOH A . 
N 8 HOH 83  483 621 HOH HOH A . 
N 8 HOH 84  484 297 HOH HOH A . 
N 8 HOH 85  485 119 HOH HOH A . 
N 8 HOH 86  486 130 HOH HOH A . 
N 8 HOH 87  487 531 HOH HOH A . 
N 8 HOH 88  488 311 HOH HOH A . 
N 8 HOH 89  489 547 HOH HOH A . 
N 8 HOH 90  490 524 HOH HOH A . 
N 8 HOH 91  491 365 HOH HOH A . 
N 8 HOH 92  492 608 HOH HOH A . 
N 8 HOH 93  493 81  HOH HOH A . 
N 8 HOH 94  494 26  HOH HOH A . 
N 8 HOH 95  495 232 HOH HOH A . 
N 8 HOH 96  496 4   HOH HOH A . 
N 8 HOH 97  497 5   HOH HOH A . 
N 8 HOH 98  498 643 HOH HOH A . 
N 8 HOH 99  499 303 HOH HOH A . 
N 8 HOH 100 500 493 HOH HOH A . 
N 8 HOH 101 501 3   HOH HOH A . 
N 8 HOH 102 502 595 HOH HOH A . 
N 8 HOH 103 503 179 HOH HOH A . 
N 8 HOH 104 504 597 HOH HOH A . 
N 8 HOH 105 505 187 HOH HOH A . 
N 8 HOH 106 506 496 HOH HOH A . 
N 8 HOH 107 507 210 HOH HOH A . 
N 8 HOH 108 508 12  HOH HOH A . 
N 8 HOH 109 509 121 HOH HOH A . 
N 8 HOH 110 510 546 HOH HOH A . 
N 8 HOH 111 511 31  HOH HOH A . 
N 8 HOH 112 512 176 HOH HOH A . 
N 8 HOH 113 513 14  HOH HOH A . 
N 8 HOH 114 514 435 HOH HOH A . 
N 8 HOH 115 515 175 HOH HOH A . 
N 8 HOH 116 516 486 HOH HOH A . 
N 8 HOH 117 517 156 HOH HOH A . 
N 8 HOH 118 518 184 HOH HOH A . 
N 8 HOH 119 519 600 HOH HOH A . 
N 8 HOH 120 520 521 HOH HOH A . 
N 8 HOH 121 521 379 HOH HOH A . 
N 8 HOH 122 522 370 HOH HOH A . 
N 8 HOH 123 523 622 HOH HOH A . 
N 8 HOH 124 524 53  HOH HOH A . 
N 8 HOH 125 525 267 HOH HOH A . 
N 8 HOH 126 526 647 HOH HOH A . 
N 8 HOH 127 527 2   HOH HOH A . 
N 8 HOH 128 528 197 HOH HOH A . 
N 8 HOH 129 529 79  HOH HOH A . 
N 8 HOH 130 530 43  HOH HOH A . 
N 8 HOH 131 531 138 HOH HOH A . 
N 8 HOH 132 532 236 HOH HOH A . 
N 8 HOH 133 533 324 HOH HOH A . 
N 8 HOH 134 534 288 HOH HOH A . 
N 8 HOH 135 535 25  HOH HOH A . 
N 8 HOH 136 536 523 HOH HOH A . 
N 8 HOH 137 537 344 HOH HOH A . 
N 8 HOH 138 538 410 HOH HOH A . 
N 8 HOH 139 539 201 HOH HOH A . 
N 8 HOH 140 540 252 HOH HOH A . 
N 8 HOH 141 541 204 HOH HOH A . 
N 8 HOH 142 542 64  HOH HOH A . 
N 8 HOH 143 543 67  HOH HOH A . 
N 8 HOH 144 544 104 HOH HOH A . 
N 8 HOH 145 545 103 HOH HOH A . 
N 8 HOH 146 546 9   HOH HOH A . 
N 8 HOH 147 547 58  HOH HOH A . 
N 8 HOH 148 548 380 HOH HOH A . 
N 8 HOH 149 549 141 HOH HOH A . 
N 8 HOH 150 550 106 HOH HOH A . 
N 8 HOH 151 551 7   HOH HOH A . 
N 8 HOH 152 552 134 HOH HOH A . 
N 8 HOH 153 553 63  HOH HOH A . 
N 8 HOH 154 554 207 HOH HOH A . 
N 8 HOH 155 555 18  HOH HOH A . 
N 8 HOH 156 556 221 HOH HOH A . 
N 8 HOH 157 557 71  HOH HOH A . 
N 8 HOH 158 558 460 HOH HOH A . 
N 8 HOH 159 559 87  HOH HOH A . 
N 8 HOH 160 560 48  HOH HOH A . 
N 8 HOH 161 561 186 HOH HOH A . 
N 8 HOH 162 562 552 HOH HOH A . 
N 8 HOH 163 563 75  HOH HOH A . 
N 8 HOH 164 564 286 HOH HOH A . 
N 8 HOH 165 565 388 HOH HOH A . 
N 8 HOH 166 566 20  HOH HOH A . 
N 8 HOH 167 567 290 HOH HOH A . 
N 8 HOH 168 568 289 HOH HOH A . 
N 8 HOH 169 569 40  HOH HOH A . 
N 8 HOH 170 570 41  HOH HOH A . 
N 8 HOH 171 571 328 HOH HOH A . 
N 8 HOH 172 572 180 HOH HOH A . 
N 8 HOH 173 573 504 HOH HOH A . 
N 8 HOH 174 574 78  HOH HOH A . 
N 8 HOH 175 575 215 HOH HOH A . 
N 8 HOH 176 576 372 HOH HOH A . 
N 8 HOH 177 577 132 HOH HOH A . 
N 8 HOH 178 578 419 HOH HOH A . 
N 8 HOH 179 579 170 HOH HOH A . 
N 8 HOH 180 580 152 HOH HOH A . 
N 8 HOH 181 581 174 HOH HOH A . 
N 8 HOH 182 582 72  HOH HOH A . 
N 8 HOH 183 583 150 HOH HOH A . 
N 8 HOH 184 584 330 HOH HOH A . 
N 8 HOH 185 585 244 HOH HOH A . 
N 8 HOH 186 586 98  HOH HOH A . 
N 8 HOH 187 587 153 HOH HOH A . 
N 8 HOH 188 588 165 HOH HOH A . 
N 8 HOH 189 589 412 HOH HOH A . 
N 8 HOH 190 590 89  HOH HOH A . 
N 8 HOH 191 591 133 HOH HOH A . 
N 8 HOH 192 592 630 HOH HOH A . 
N 8 HOH 193 593 517 HOH HOH A . 
N 8 HOH 194 594 157 HOH HOH A . 
N 8 HOH 195 595 182 HOH HOH A . 
N 8 HOH 196 596 154 HOH HOH A . 
N 8 HOH 197 597 306 HOH HOH A . 
N 8 HOH 198 598 337 HOH HOH A . 
N 8 HOH 199 599 237 HOH HOH A . 
N 8 HOH 200 600 452 HOH HOH A . 
N 8 HOH 201 601 633 HOH HOH A . 
N 8 HOH 202 602 162 HOH HOH A . 
N 8 HOH 203 603 253 HOH HOH A . 
N 8 HOH 204 604 485 HOH HOH A . 
N 8 HOH 205 605 17  HOH HOH A . 
N 8 HOH 206 606 475 HOH HOH A . 
N 8 HOH 207 607 93  HOH HOH A . 
N 8 HOH 208 608 553 HOH HOH A . 
N 8 HOH 209 609 91  HOH HOH A . 
N 8 HOH 210 610 218 HOH HOH A . 
N 8 HOH 211 611 24  HOH HOH A . 
N 8 HOH 212 612 84  HOH HOH A . 
N 8 HOH 213 613 326 HOH HOH A . 
N 8 HOH 214 614 334 HOH HOH A . 
N 8 HOH 215 615 441 HOH HOH A . 
N 8 HOH 216 616 520 HOH HOH A . 
N 8 HOH 217 617 279 HOH HOH A . 
N 8 HOH 218 618 529 HOH HOH A . 
N 8 HOH 219 619 61  HOH HOH A . 
N 8 HOH 220 620 273 HOH HOH A . 
N 8 HOH 221 621 550 HOH HOH A . 
N 8 HOH 222 622 62  HOH HOH A . 
N 8 HOH 223 623 298 HOH HOH A . 
N 8 HOH 224 624 335 HOH HOH A . 
N 8 HOH 225 625 38  HOH HOH A . 
N 8 HOH 226 626 203 HOH HOH A . 
N 8 HOH 227 627 646 HOH HOH A . 
N 8 HOH 228 628 636 HOH HOH A . 
N 8 HOH 229 629 148 HOH HOH A . 
N 8 HOH 230 630 272 HOH HOH A . 
N 8 HOH 231 631 598 HOH HOH A . 
N 8 HOH 232 632 533 HOH HOH A . 
N 8 HOH 233 633 256 HOH HOH A . 
N 8 HOH 234 634 470 HOH HOH A . 
N 8 HOH 235 635 19  HOH HOH A . 
N 8 HOH 236 636 363 HOH HOH A . 
N 8 HOH 237 637 386 HOH HOH A . 
N 8 HOH 238 638 355 HOH HOH A . 
N 8 HOH 239 639 500 HOH HOH A . 
N 8 HOH 240 640 307 HOH HOH A . 
N 8 HOH 241 641 532 HOH HOH A . 
N 8 HOH 242 642 540 HOH HOH A . 
N 8 HOH 243 643 465 HOH HOH A . 
N 8 HOH 244 644 558 HOH HOH A . 
N 8 HOH 245 645 439 HOH HOH A . 
N 8 HOH 246 646 364 HOH HOH A . 
N 8 HOH 247 647 277 HOH HOH A . 
N 8 HOH 248 648 393 HOH HOH A . 
N 8 HOH 249 649 544 HOH HOH A . 
N 8 HOH 250 650 384 HOH HOH A . 
N 8 HOH 251 651 373 HOH HOH A . 
N 8 HOH 252 652 308 HOH HOH A . 
N 8 HOH 253 653 416 HOH HOH A . 
N 8 HOH 254 654 607 HOH HOH A . 
N 8 HOH 255 655 313 HOH HOH A . 
N 8 HOH 256 656 15  HOH HOH A . 
N 8 HOH 257 657 468 HOH HOH A . 
N 8 HOH 258 658 437 HOH HOH A . 
N 8 HOH 259 659 392 HOH HOH A . 
N 8 HOH 260 660 645 HOH HOH A . 
N 8 HOH 261 661 436 HOH HOH A . 
N 8 HOH 262 662 526 HOH HOH A . 
N 8 HOH 263 663 102 HOH HOH A . 
N 8 HOH 264 664 457 HOH HOH A . 
N 8 HOH 265 665 245 HOH HOH A . 
N 8 HOH 266 666 173 HOH HOH A . 
N 8 HOH 267 667 356 HOH HOH A . 
N 8 HOH 268 668 623 HOH HOH A . 
N 8 HOH 269 669 612 HOH HOH A . 
N 8 HOH 270 670 406 HOH HOH A . 
N 8 HOH 271 671 400 HOH HOH A . 
N 8 HOH 272 672 353 HOH HOH A . 
N 8 HOH 273 673 525 HOH HOH A . 
N 8 HOH 274 674 477 HOH HOH A . 
N 8 HOH 275 675 519 HOH HOH A . 
N 8 HOH 276 676 616 HOH HOH A . 
N 8 HOH 277 677 638 HOH HOH A . 
N 8 HOH 278 678 503 HOH HOH A . 
N 8 HOH 279 679 536 HOH HOH A . 
N 8 HOH 280 680 652 HOH HOH A . 
N 8 HOH 281 681 34  HOH HOH A . 
N 8 HOH 282 682 502 HOH HOH A . 
N 8 HOH 283 683 390 HOH HOH A . 
N 8 HOH 284 684 166 HOH HOH A . 
N 8 HOH 285 685 471 HOH HOH A . 
N 8 HOH 286 686 476 HOH HOH A . 
N 8 HOH 287 687 428 HOH HOH A . 
N 8 HOH 288 688 490 HOH HOH A . 
N 8 HOH 289 689 347 HOH HOH A . 
N 8 HOH 290 690 192 HOH HOH A . 
N 8 HOH 291 691 320 HOH HOH A . 
N 8 HOH 292 692 111 HOH HOH A . 
N 8 HOH 293 693 361 HOH HOH A . 
N 8 HOH 294 694 535 HOH HOH A . 
N 8 HOH 295 695 350 HOH HOH A . 
N 8 HOH 296 696 343 HOH HOH A . 
N 8 HOH 297 697 331 HOH HOH A . 
N 8 HOH 298 698 596 HOH HOH A . 
N 8 HOH 299 699 631 HOH HOH A . 
N 8 HOH 300 700 527 HOH HOH A . 
N 8 HOH 301 701 257 HOH HOH A . 
N 8 HOH 302 702 318 HOH HOH A . 
N 8 HOH 303 703 545 HOH HOH A . 
N 8 HOH 304 704 198 HOH HOH A . 
N 8 HOH 305 705 281 HOH HOH A . 
N 8 HOH 306 706 282 HOH HOH A . 
N 8 HOH 307 707 480 HOH HOH A . 
N 8 HOH 308 708 382 HOH HOH A . 
N 8 HOH 309 709 548 HOH HOH A . 
N 8 HOH 310 710 617 HOH HOH A . 
N 8 HOH 311 711 509 HOH HOH A . 
N 8 HOH 312 712 626 HOH HOH A . 
N 8 HOH 313 713 395 HOH HOH A . 
N 8 HOH 314 714 644 HOH HOH A . 
N 8 HOH 315 715 248 HOH HOH A . 
N 8 HOH 316 716 434 HOH HOH A . 
N 8 HOH 317 717 513 HOH HOH A . 
N 8 HOH 318 718 632 HOH HOH A . 
N 8 HOH 319 719 358 HOH HOH A . 
N 8 HOH 320 720 492 HOH HOH A . 
N 8 HOH 321 721 474 HOH HOH A . 
N 8 HOH 322 722 52  HOH HOH A . 
N 8 HOH 323 723 345 HOH HOH A . 
N 8 HOH 324 724 599 HOH HOH A . 
N 8 HOH 325 725 444 HOH HOH A . 
N 8 HOH 326 726 432 HOH HOH A . 
N 8 HOH 327 727 360 HOH HOH A . 
N 8 HOH 328 728 397 HOH HOH A . 
N 8 HOH 329 729 542 HOH HOH A . 
N 8 HOH 330 730 433 HOH HOH A . 
N 8 HOH 331 731 511 HOH HOH A . 
N 8 HOH 332 732 515 HOH HOH A . 
N 8 HOH 333 733 512 HOH HOH A . 
N 8 HOH 334 734 637 HOH HOH A . 
N 8 HOH 335 735 427 HOH HOH A . 
N 8 HOH 336 736 501 HOH HOH A . 
N 8 HOH 337 737 602 HOH HOH A . 
N 8 HOH 338 738 425 HOH HOH A . 
N 8 HOH 339 739 505 HOH HOH A . 
N 8 HOH 340 740 510 HOH HOH A . 
N 8 HOH 341 741 362 HOH HOH A . 
N 8 HOH 342 742 518 HOH HOH A . 
N 8 HOH 343 743 407 HOH HOH A . 
N 8 HOH 344 744 575 HOH HOH A . 
N 8 HOH 345 745 296 HOH HOH A . 
O 8 HOH 1   601 601 HOH HOH B . 
O 8 HOH 2   602 371 HOH HOH B . 
O 8 HOH 3   603 413 HOH HOH B . 
O 8 HOH 4   604 568 HOH HOH B . 
O 8 HOH 5   605 387 HOH HOH B . 
O 8 HOH 6   606 270 HOH HOH B . 
O 8 HOH 7   607 250 HOH HOH B . 
O 8 HOH 8   608 234 HOH HOH B . 
O 8 HOH 9   609 194 HOH HOH B . 
O 8 HOH 10  610 559 HOH HOH B . 
O 8 HOH 11  611 642 HOH HOH B . 
O 8 HOH 12  612 195 HOH HOH B . 
O 8 HOH 13  613 611 HOH HOH B . 
O 8 HOH 14  614 233 HOH HOH B . 
O 8 HOH 15  615 283 HOH HOH B . 
O 8 HOH 16  616 367 HOH HOH B . 
O 8 HOH 17  617 587 HOH HOH B . 
O 8 HOH 18  618 541 HOH HOH B . 
O 8 HOH 19  619 455 HOH HOH B . 
O 8 HOH 20  620 13  HOH HOH B . 
O 8 HOH 21  621 239 HOH HOH B . 
O 8 HOH 22  622 555 HOH HOH B . 
O 8 HOH 23  623 576 HOH HOH B . 
O 8 HOH 24  624 302 HOH HOH B . 
O 8 HOH 25  625 88  HOH HOH B . 
O 8 HOH 26  626 46  HOH HOH B . 
O 8 HOH 27  627 629 HOH HOH B . 
O 8 HOH 28  628 454 HOH HOH B . 
O 8 HOH 29  629 190 HOH HOH B . 
O 8 HOH 30  630 403 HOH HOH B . 
O 8 HOH 31  631 453 HOH HOH B . 
O 8 HOH 32  632 117 HOH HOH B . 
O 8 HOH 33  633 579 HOH HOH B . 
O 8 HOH 34  634 149 HOH HOH B . 
O 8 HOH 35  635 624 HOH HOH B . 
O 8 HOH 36  636 39  HOH HOH B . 
O 8 HOH 37  637 82  HOH HOH B . 
O 8 HOH 38  638 447 HOH HOH B . 
O 8 HOH 39  639 577 HOH HOH B . 
O 8 HOH 40  640 217 HOH HOH B . 
O 8 HOH 41  641 280 HOH HOH B . 
O 8 HOH 42  642 115 HOH HOH B . 
O 8 HOH 43  643 65  HOH HOH B . 
O 8 HOH 44  644 374 HOH HOH B . 
O 8 HOH 45  645 569 HOH HOH B . 
O 8 HOH 46  646 21  HOH HOH B . 
O 8 HOH 47  647 332 HOH HOH B . 
O 8 HOH 48  648 247 HOH HOH B . 
O 8 HOH 49  649 409 HOH HOH B . 
O 8 HOH 50  650 227 HOH HOH B . 
O 8 HOH 51  651 294 HOH HOH B . 
O 8 HOH 52  652 169 HOH HOH B . 
O 8 HOH 53  653 30  HOH HOH B . 
O 8 HOH 54  654 70  HOH HOH B . 
O 8 HOH 55  655 323 HOH HOH B . 
O 8 HOH 56  656 80  HOH HOH B . 
O 8 HOH 57  657 110 HOH HOH B . 
O 8 HOH 58  658 212 HOH HOH B . 
O 8 HOH 59  659 168 HOH HOH B . 
O 8 HOH 60  660 414 HOH HOH B . 
O 8 HOH 61  661 135 HOH HOH B . 
O 8 HOH 62  662 538 HOH HOH B . 
O 8 HOH 63  663 442 HOH HOH B . 
O 8 HOH 64  664 254 HOH HOH B . 
O 8 HOH 65  665 69  HOH HOH B . 
O 8 HOH 66  666 183 HOH HOH B . 
O 8 HOH 67  667 405 HOH HOH B . 
O 8 HOH 68  668 208 HOH HOH B . 
O 8 HOH 69  669 352 HOH HOH B . 
O 8 HOH 70  670 619 HOH HOH B . 
O 8 HOH 71  671 99  HOH HOH B . 
O 8 HOH 72  672 228 HOH HOH B . 
O 8 HOH 73  673 32  HOH HOH B . 
O 8 HOH 74  674 241 HOH HOH B . 
O 8 HOH 75  675 604 HOH HOH B . 
O 8 HOH 76  676 291 HOH HOH B . 
O 8 HOH 77  677 317 HOH HOH B . 
O 8 HOH 78  678 147 HOH HOH B . 
O 8 HOH 79  679 214 HOH HOH B . 
O 8 HOH 80  680 86  HOH HOH B . 
O 8 HOH 81  681 177 HOH HOH B . 
O 8 HOH 82  682 478 HOH HOH B . 
O 8 HOH 83  683 415 HOH HOH B . 
O 8 HOH 84  684 293 HOH HOH B . 
O 8 HOH 85  685 11  HOH HOH B . 
O 8 HOH 86  686 96  HOH HOH B . 
O 8 HOH 87  687 22  HOH HOH B . 
O 8 HOH 88  688 649 HOH HOH B . 
O 8 HOH 89  689 55  HOH HOH B . 
O 8 HOH 90  690 28  HOH HOH B . 
O 8 HOH 91  691 83  HOH HOH B . 
O 8 HOH 92  692 37  HOH HOH B . 
O 8 HOH 93  693 404 HOH HOH B . 
O 8 HOH 94  694 561 HOH HOH B . 
O 8 HOH 95  695 47  HOH HOH B . 
O 8 HOH 96  696 223 HOH HOH B . 
O 8 HOH 97  697 35  HOH HOH B . 
O 8 HOH 98  698 340 HOH HOH B . 
O 8 HOH 99  699 191 HOH HOH B . 
O 8 HOH 100 700 178 HOH HOH B . 
O 8 HOH 101 701 8   HOH HOH B . 
O 8 HOH 102 702 398 HOH HOH B . 
O 8 HOH 103 703 73  HOH HOH B . 
O 8 HOH 104 704 74  HOH HOH B . 
O 8 HOH 105 705 394 HOH HOH B . 
O 8 HOH 106 706 211 HOH HOH B . 
O 8 HOH 107 707 226 HOH HOH B . 
O 8 HOH 108 708 126 HOH HOH B . 
O 8 HOH 109 709 366 HOH HOH B . 
O 8 HOH 110 710 265 HOH HOH B . 
O 8 HOH 111 711 640 HOH HOH B . 
O 8 HOH 112 712 200 HOH HOH B . 
O 8 HOH 113 713 262 HOH HOH B . 
O 8 HOH 114 714 108 HOH HOH B . 
O 8 HOH 115 715 145 HOH HOH B . 
O 8 HOH 116 716 473 HOH HOH B . 
O 8 HOH 117 717 230 HOH HOH B . 
O 8 HOH 118 718 193 HOH HOH B . 
O 8 HOH 119 719 10  HOH HOH B . 
O 8 HOH 120 720 466 HOH HOH B . 
O 8 HOH 121 721 259 HOH HOH B . 
O 8 HOH 122 722 160 HOH HOH B . 
O 8 HOH 123 723 66  HOH HOH B . 
O 8 HOH 124 724 593 HOH HOH B . 
O 8 HOH 125 725 144 HOH HOH B . 
O 8 HOH 126 726 567 HOH HOH B . 
O 8 HOH 127 727 304 HOH HOH B . 
O 8 HOH 128 728 161 HOH HOH B . 
O 8 HOH 129 729 235 HOH HOH B . 
O 8 HOH 130 730 100 HOH HOH B . 
O 8 HOH 131 731 481 HOH HOH B . 
O 8 HOH 132 732 113 HOH HOH B . 
O 8 HOH 133 733 615 HOH HOH B . 
O 8 HOH 134 734 6   HOH HOH B . 
O 8 HOH 135 735 128 HOH HOH B . 
O 8 HOH 136 736 16  HOH HOH B . 
O 8 HOH 137 737 220 HOH HOH B . 
O 8 HOH 138 738 163 HOH HOH B . 
O 8 HOH 139 739 209 HOH HOH B . 
O 8 HOH 140 740 276 HOH HOH B . 
O 8 HOH 141 741 94  HOH HOH B . 
O 8 HOH 142 742 185 HOH HOH B . 
O 8 HOH 143 743 261 HOH HOH B . 
O 8 HOH 144 744 329 HOH HOH B . 
O 8 HOH 145 745 258 HOH HOH B . 
O 8 HOH 146 746 143 HOH HOH B . 
O 8 HOH 147 747 316 HOH HOH B . 
O 8 HOH 148 748 107 HOH HOH B . 
O 8 HOH 149 749 249 HOH HOH B . 
O 8 HOH 150 750 114 HOH HOH B . 
O 8 HOH 151 751 238 HOH HOH B . 
O 8 HOH 152 752 378 HOH HOH B . 
O 8 HOH 153 753 50  HOH HOH B . 
O 8 HOH 154 754 314 HOH HOH B . 
O 8 HOH 155 755 231 HOH HOH B . 
O 8 HOH 156 756 189 HOH HOH B . 
O 8 HOH 157 757 641 HOH HOH B . 
O 8 HOH 158 758 586 HOH HOH B . 
O 8 HOH 159 759 92  HOH HOH B . 
O 8 HOH 160 760 140 HOH HOH B . 
O 8 HOH 161 761 116 HOH HOH B . 
O 8 HOH 162 762 385 HOH HOH B . 
O 8 HOH 163 763 491 HOH HOH B . 
O 8 HOH 164 764 129 HOH HOH B . 
O 8 HOH 165 765 137 HOH HOH B . 
O 8 HOH 166 766 581 HOH HOH B . 
O 8 HOH 167 767 224 HOH HOH B . 
O 8 HOH 168 768 271 HOH HOH B . 
O 8 HOH 169 769 49  HOH HOH B . 
O 8 HOH 170 770 583 HOH HOH B . 
O 8 HOH 171 771 139 HOH HOH B . 
O 8 HOH 172 772 51  HOH HOH B . 
O 8 HOH 173 773 613 HOH HOH B . 
O 8 HOH 174 774 269 HOH HOH B . 
O 8 HOH 175 775 264 HOH HOH B . 
O 8 HOH 176 776 120 HOH HOH B . 
O 8 HOH 177 777 456 HOH HOH B . 
O 8 HOH 178 778 497 HOH HOH B . 
O 8 HOH 179 779 408 HOH HOH B . 
O 8 HOH 180 780 54  HOH HOH B . 
O 8 HOH 181 781 351 HOH HOH B . 
O 8 HOH 182 782 243 HOH HOH B . 
O 8 HOH 183 783 482 HOH HOH B . 
O 8 HOH 184 784 564 HOH HOH B . 
O 8 HOH 185 785 42  HOH HOH B . 
O 8 HOH 186 786 325 HOH HOH B . 
O 8 HOH 187 787 206 HOH HOH B . 
O 8 HOH 188 788 122 HOH HOH B . 
O 8 HOH 189 789 301 HOH HOH B . 
O 8 HOH 190 790 620 HOH HOH B . 
O 8 HOH 191 791 495 HOH HOH B . 
O 8 HOH 192 792 464 HOH HOH B . 
O 8 HOH 193 793 580 HOH HOH B . 
O 8 HOH 194 794 85  HOH HOH B . 
O 8 HOH 195 795 57  HOH HOH B . 
O 8 HOH 196 796 242 HOH HOH B . 
O 8 HOH 197 797 255 HOH HOH B . 
O 8 HOH 198 798 609 HOH HOH B . 
O 8 HOH 199 799 557 HOH HOH B . 
O 8 HOH 200 800 97  HOH HOH B . 
O 8 HOH 201 801 202 HOH HOH B . 
O 8 HOH 202 802 155 HOH HOH B . 
O 8 HOH 203 803 136 HOH HOH B . 
O 8 HOH 204 804 443 HOH HOH B . 
O 8 HOH 205 805 563 HOH HOH B . 
O 8 HOH 206 806 59  HOH HOH B . 
O 8 HOH 207 807 606 HOH HOH B . 
O 8 HOH 208 808 292 HOH HOH B . 
O 8 HOH 209 809 467 HOH HOH B . 
O 8 HOH 210 810 639 HOH HOH B . 
O 8 HOH 211 811 246 HOH HOH B . 
O 8 HOH 212 812 310 HOH HOH B . 
O 8 HOH 213 813 574 HOH HOH B . 
O 8 HOH 214 814 321 HOH HOH B . 
O 8 HOH 215 815 449 HOH HOH B . 
O 8 HOH 216 816 123 HOH HOH B . 
O 8 HOH 217 817 494 HOH HOH B . 
O 8 HOH 218 818 222 HOH HOH B . 
O 8 HOH 219 819 489 HOH HOH B . 
O 8 HOH 220 820 584 HOH HOH B . 
O 8 HOH 221 821 336 HOH HOH B . 
O 8 HOH 222 822 578 HOH HOH B . 
O 8 HOH 223 823 484 HOH HOH B . 
O 8 HOH 224 824 573 HOH HOH B . 
O 8 HOH 225 825 469 HOH HOH B . 
O 8 HOH 226 826 430 HOH HOH B . 
O 8 HOH 227 827 369 HOH HOH B . 
O 8 HOH 228 828 383 HOH HOH B . 
O 8 HOH 229 829 556 HOH HOH B . 
O 8 HOH 230 830 462 HOH HOH B . 
O 8 HOH 231 831 266 HOH HOH B . 
O 8 HOH 232 832 420 HOH HOH B . 
O 8 HOH 233 833 44  HOH HOH B . 
O 8 HOH 234 834 572 HOH HOH B . 
O 8 HOH 235 835 251 HOH HOH B . 
O 8 HOH 236 836 562 HOH HOH B . 
O 8 HOH 237 837 342 HOH HOH B . 
O 8 HOH 238 838 219 HOH HOH B . 
O 8 HOH 239 839 381 HOH HOH B . 
O 8 HOH 240 840 216 HOH HOH B . 
O 8 HOH 241 841 618 HOH HOH B . 
O 8 HOH 242 842 338 HOH HOH B . 
O 8 HOH 243 843 589 HOH HOH B . 
O 8 HOH 244 844 588 HOH HOH B . 
O 8 HOH 245 845 90  HOH HOH B . 
O 8 HOH 246 846 359 HOH HOH B . 
O 8 HOH 247 847 582 HOH HOH B . 
O 8 HOH 248 848 389 HOH HOH B . 
O 8 HOH 249 849 570 HOH HOH B . 
O 8 HOH 250 850 488 HOH HOH B . 
O 8 HOH 251 851 650 HOH HOH B . 
O 8 HOH 252 852 585 HOH HOH B . 
O 8 HOH 253 853 348 HOH HOH B . 
O 8 HOH 254 854 429 HOH HOH B . 
O 8 HOH 255 855 418 HOH HOH B . 
O 8 HOH 256 856 322 HOH HOH B . 
O 8 HOH 257 857 295 HOH HOH B . 
O 8 HOH 258 858 422 HOH HOH B . 
O 8 HOH 259 859 451 HOH HOH B . 
O 8 HOH 260 860 171 HOH HOH B . 
O 8 HOH 261 861 438 HOH HOH B . 
O 8 HOH 262 862 164 HOH HOH B . 
O 8 HOH 263 863 591 HOH HOH B . 
O 8 HOH 264 864 319 HOH HOH B . 
O 8 HOH 265 865 448 HOH HOH B . 
O 8 HOH 266 866 349 HOH HOH B . 
O 8 HOH 267 867 421 HOH HOH B . 
O 8 HOH 268 868 571 HOH HOH B . 
O 8 HOH 269 869 565 HOH HOH B . 
O 8 HOH 270 870 327 HOH HOH B . 
O 8 HOH 271 871 312 HOH HOH B . 
O 8 HOH 272 872 109 HOH HOH B . 
O 8 HOH 273 873 299 HOH HOH B . 
O 8 HOH 274 874 499 HOH HOH B . 
O 8 HOH 275 875 560 HOH HOH B . 
O 8 HOH 276 876 614 HOH HOH B . 
O 8 HOH 277 877 315 HOH HOH B . 
O 8 HOH 278 878 399 HOH HOH B . 
O 8 HOH 279 879 458 HOH HOH B . 
O 8 HOH 280 880 592 HOH HOH B . 
O 8 HOH 281 881 354 HOH HOH B . 
O 8 HOH 282 882 376 HOH HOH B . 
O 8 HOH 283 883 445 HOH HOH B . 
O 8 HOH 284 884 240 HOH HOH B . 
O 8 HOH 285 885 423 HOH HOH B . 
O 8 HOH 286 886 472 HOH HOH B . 
O 8 HOH 287 887 566 HOH HOH B . 
O 8 HOH 288 888 590 HOH HOH B . 
O 8 HOH 289 889 498 HOH HOH B . 
O 8 HOH 290 890 287 HOH HOH B . 
O 8 HOH 291 891 463 HOH HOH B . 
O 8 HOH 292 892 229 HOH HOH B . 
O 8 HOH 293 893 309 HOH HOH B . 
O 8 HOH 294 894 118 HOH HOH B . 
O 8 HOH 295 895 396 HOH HOH B . 
O 8 HOH 296 896 651 HOH HOH B . 
O 8 HOH 297 897 401 HOH HOH B . 
O 8 HOH 298 898 539 HOH HOH B . 
O 8 HOH 299 899 628 HOH HOH B . 
O 8 HOH 300 900 610 HOH HOH B . 
O 8 HOH 301 901 487 HOH HOH B . 
O 8 HOH 302 902 95  HOH HOH B . 
O 8 HOH 303 903 268 HOH HOH B . 
O 8 HOH 304 904 305 HOH HOH B . 
O 8 HOH 305 905 402 HOH HOH B . 
O 8 HOH 306 906 461 HOH HOH B . 
O 8 HOH 307 907 483 HOH HOH B . 
# 
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 HIS 3 ? CG  ? A HIS 3 CG  
2  1 Y 1 A HIS 3 ? ND1 ? A HIS 3 ND1 
3  1 Y 1 A HIS 3 ? CD2 ? A HIS 3 CD2 
4  1 Y 1 A HIS 3 ? CE1 ? A HIS 3 CE1 
5  1 Y 1 A HIS 3 ? NE2 ? A HIS 3 NE2 
6  1 Y 1 B HIS 3 ? CG  ? B HIS 3 CG  
7  1 Y 1 B HIS 3 ? ND1 ? B HIS 3 ND1 
8  1 Y 1 B HIS 3 ? CD2 ? B HIS 3 CD2 
9  1 Y 1 B HIS 3 ? CE1 ? B HIS 3 CE1 
10 1 Y 1 B HIS 3 ? NE2 ? B HIS 3 NE2 
11 1 Y 1 B HIS 4 ? ND1 ? B HIS 4 ND1 
12 1 Y 1 B HIS 4 ? CD2 ? B HIS 4 CD2 
13 1 Y 1 B HIS 4 ? CE1 ? B HIS 4 CE1 
14 1 Y 1 B HIS 4 ? NE2 ? B HIS 4 NE2 
# 
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 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.210 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5LL4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.110 
_cell.length_a_esd                 ? 
_cell.length_b                     41.174 
_cell.length_b_esd                 ? 
_cell.length_c                     72.084 
_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                         5LL4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   5LL4 
_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            2.02 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.6 
_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              7 
_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: 0.1M sodium bicine (pH 9), 0.2M ammonium sulfate and 2M sodium malonate (pH 7)' 
_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_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-01-07 
# 
_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   0.826606 
_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 P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5LL4 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.1200 
_reflns.d_resolution_low                 41.174 
_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                       ? 
_reflns.number_obs                       144738 
_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             80.700 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.800 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.035 
_reflns.pdbx_netI_over_av_sigmaI         5.325 
_reflns.pdbx_netI_over_sigmaI            16.300 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_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_R_split 
1.120 1.180  ? 4.300  ? ? ? ? ? 49.300 ? ? ? ? 0.157 ? ? ? ? ? ? ? ? 3.600 ? ? ? ? ? ? ? 1  1 ? ? 
1.180 1.260  ? 5.500  ? ? ? ? ? 78.600 ? ? ? ? 0.133 ? ? ? ? ? ? ? ? 3.600 ? ? ? ? ? ? ? 2  1 ? ? 
1.260 1.340  ? 7.300  ? ? ? ? ? 85.500 ? ? ? ? 0.101 ? ? ? ? ? ? ? ? 3.900 ? ? ? ? ? ? ? 3  1 ? ? 
1.340 1.450  ? 10.400 ? ? ? ? ? 85.700 ? ? ? ? 0.071 ? ? ? ? ? ? ? ? 3.800 ? ? ? ? ? ? ? 4  1 ? ? 
1.450 1.590  ? 14.600 ? ? ? ? ? 86.400 ? ? ? ? 0.049 ? ? ? ? ? ? ? ? 3.900 ? ? ? ? ? ? ? 5  1 ? ? 
1.590 1.780  ? 18.900 ? ? ? ? ? 86.800 ? ? ? ? 0.037 ? ? ? ? ? ? ? ? 3.900 ? ? ? ? ? ? ? 6  1 ? ? 
1.780 2.050  ? 21.900 ? ? ? ? ? 90.100 ? ? ? ? 0.030 ? ? ? ? ? ? ? ? 3.900 ? ? ? ? ? ? ? 7  1 ? ? 
2.050 2.510  ? 24.000 ? ? ? ? ? 90.000 ? ? ? ? 0.027 ? ? ? ? ? ? ? ? 3.900 ? ? ? ? ? ? ? 8  1 ? ? 
2.510 3.550  ? 18.400 ? ? ? ? ? 90.900 ? ? ? ? 0.027 ? ? ? ? ? ? ? ? 3.900 ? ? ? ? ? ? ? 9  1 ? ? 
3.550 41.174 ? 10.600 ? ? ? ? ? 89.400 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 3.900 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.0100 
_refine.aniso_B[1][2]                            -0.0600 
_refine.aniso_B[1][3]                            0.0200 
_refine.aniso_B[2][2]                            0.1400 
_refine.aniso_B[2][3]                            0.0500 
_refine.aniso_B[3][3]                            -0.1300 
_refine.B_iso_max                                116.050 
_refine.B_iso_mean                               17.8370 
_refine.B_iso_min                                5.550 
_refine.correlation_coeff_Fo_to_Fc               0.9790 
_refine.correlation_coeff_Fo_to_Fc_free          0.9670 
_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                                 5LL4 
_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                            1.1200 
_refine.ls_d_res_low                             41.1700 
_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                     137528 
_refine.ls_number_reflns_R_free                  7204 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    80.7900 
_refine.ls_percent_reflns_R_free                 5.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1332 
_refine.ls_R_factor_R_free                       0.1713 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1312 
_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.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                      3HLJ 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0380 
_refine.pdbx_overall_ESU_R_Free                  0.0410 
_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             0.0384 
_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.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.1200 
_refine_hist.d_res_low                        41.1700 
_refine_hist.pdbx_number_atoms_ligand         97 
_refine_hist.number_atoms_solvent             652 
_refine_hist.number_atoms_total               4873 
_refine_hist.pdbx_number_residues_total       519 
_refine_hist.pdbx_B_iso_mean_ligand           24.77 
_refine_hist.pdbx_B_iso_mean_solvent          30.31 
_refine_hist.pdbx_number_atoms_protein        4124 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
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' ? 0.023  0.020  4677 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.247  1.970  6376 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.955  5.000  582  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 33.266 24.660 206  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.789 15.000 777  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 22.980 15.000 15   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.170  0.200  651  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  3667 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 8.904  3.000  4677 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 29.905 5.000  654  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 16.441 5.000  4524 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.1230 
_refine_ls_shell.d_res_low                        1.1520 
_refine_ls_shell.number_reflns_all                5291 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             239 
_refine_ls_shell.number_reflns_R_work             5052 
_refine_ls_shell.percent_reflns_obs               39.7600 
_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                  0.2170 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.1650 
_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_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                     5LL4 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme II with 4-(1H-benzimidazol-1-ylacetyl)benzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5LL4 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 6 ? 
M N N 7 ? 
N N N 8 ? 
O N N 8 ? 
# 
_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 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5LL4 A 1 ? 260 ? P00918 1 ? 260 ? 1 261 
2 1 5LL4 B 1 ? 260 ? P00918 1 ? 260 ? 1 261 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,N 
2 1 B,I,J,K,L,M,O   
# 
_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 ? VAL A 134 ? ASP A 130 VAL 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 
HELX_P HELX_P10 AB1 GLY B 12  ? ASP B 19  ? GLY B 12  ASP B 19  5 ? 8 
HELX_P HELX_P11 AB2 PHE B 20  ? GLY B 25  ? PHE B 20  GLY B 25  5 ? 6 
HELX_P HELX_P12 AB3 LYS B 126 ? GLY B 128 ? LYS B 127 GLY B 129 5 ? 3 
HELX_P HELX_P13 AB4 ASP B 129 ? VAL B 134 ? ASP B 130 VAL B 135 1 ? 6 
HELX_P HELX_P14 AB5 LYS B 153 ? GLY B 155 ? LYS B 154 GLY B 156 5 ? 3 
HELX_P HELX_P15 AB6 LEU B 156 ? LEU B 163 ? LEU B 157 LEU B 164 1 ? 8 
HELX_P HELX_P16 AB7 ASP B 164 ? LYS B 167 ? ASP B 165 LYS B 168 5 ? 4 
HELX_P HELX_P17 AB8 ASP B 179 ? LEU B 184 ? ASP B 180 LEU B 185 5 ? 6 
HELX_P HELX_P18 AB9 SER B 218 ? ARG B 226 ? SER B 219 ARG B 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 C ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 H 6YH . N10 ? ? A ZN  301 A 6YH 306 1_555 ? ? ? ? ? ? ? 1.924 ? ? 
metalc5 metalc ? ? B HIS 94  NE2 ? ? ? 1_555 I ZN  . ZN  ? ? B HIS 94  B ZN  301 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc6 metalc ? ? B HIS 96  NE2 ? ? ? 1_555 I ZN  . ZN  ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
metalc7 metalc ? ? B HIS 119 ND1 ? ? ? 1_555 I ZN  . ZN  ? ? B HIS 119 B ZN  301 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc8 metalc ? ? I ZN  .   ZN  ? ? ? 1_555 M 6YH . N10 ? ? B ZN  301 B 6YH 305 1_555 ? ? ? ? ? ? ? 1.939 ? ? 
# 
_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 ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.8 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.3 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.8  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 ? H 6YH .   ? A 6YH 306 ? 1_555 111.3 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 ? H 6YH .   ? A 6YH 306 ? 1_555 113.5 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 ? H 6YH .   ? A 6YH 306 ? 1_555 115.1 ? 
7  NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 103.8 ? 
8  NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 112.7 ? 
9  NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 98.7  ? 
10 NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N10 ? M 6YH .   ? B 6YH 305 ? 1_555 111.0 ? 
11 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N10 ? M 6YH .   ? B 6YH 305 ? 1_555 113.6 ? 
12 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N10 ? M 6YH .   ? B 6YH 305 ? 1_555 115.9 ? 
# 
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 0.03  
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 10.32 
3 SER 29  B . ? SER 29  B PRO 30  B ? PRO 30  B 1 -3.88 
4 PRO 200 B . ? PRO 201 B PRO 201 B ? PRO 202 B 1 8.86  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 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      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 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 
AA4 1  ASP B 32  ? ILE B 33  ? ASP B 32  ILE B 33  
AA4 2  THR B 108 ? VAL B 109 ? THR B 108 VAL B 109 
AA5 1  LYS B 39  ? TYR B 40  ? LYS B 39  TYR B 40  
AA5 2  LYS B 256 ? ALA B 257 ? LYS B 257 ALA B 258 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 191 GLY B 196 
AA5 4  VAL B 206 ? LEU B 211 ? VAL B 207 LEU B 212 
AA5 5  LEU B 140 ? VAL B 149 ? LEU B 141 VAL B 150 
AA5 6  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA5 7  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA5 8  PHE B 66  ? PHE B 70  ? PHE B 66  PHE B 70  
AA5 9  SER B 56  ? ASN B 61  ? SER B 56  ASN B 61  
AA5 10 SER B 172 ? ASP B 174 ? SER B 173 ASP B 175 
AA6 1  LEU B 47  ? SER B 50  ? LEU B 47  SER B 50  
AA6 2  VAL B 78  ? GLY B 81  ? VAL B 78  GLY B 81  
AA6 3  TYR B 88  ? TRP B 97  ? TYR B 88  TRP B 97  
AA6 4  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
AA6 5  LEU B 140 ? VAL B 149 ? LEU B 141 VAL B 150 
AA6 6  ILE B 215 ? VAL B 217 ? ILE B 216 VAL B 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 VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
AA4 1 2  N ILE B 33  ? N ILE B 33  O THR B 108 ? O THR B 108 
AA5 1 2  N LYS B 39  ? N LYS B 39  O ALA B 257 ? O ALA B 258 
AA5 2 3  O LYS B 256 ? O LYS B 257 N THR B 192 ? N THR B 193 
AA5 3 4  N GLY B 195 ? N GLY B 196 O VAL B 206 ? O VAL B 207 
AA5 4 5  O ILE B 209 ? O ILE B 210 N GLY B 144 ? N GLY B 145 
AA5 5 6  O ILE B 145 ? O ILE B 146 N LEU B 118 ? N LEU B 118 
AA5 6 7  O HIS B 119 ? O HIS B 119 N HIS B 94  ? N HIS B 94  
AA5 7 8  O PHE B 93  ? O PHE B 93  N VAL B 68  ? N VAL B 68  
AA5 8 9  O GLU B 69  ? O GLU B 69  N ARG B 58  ? N ARG B 58  
AA5 9 10 N ILE B 59  ? N ILE B 59  O ALA B 173 ? O ALA B 174 
AA6 1 2  N SER B 50  ? N SER B 50  O VAL B 78  ? O VAL B 78  
AA6 2 3  N LEU B 79  ? N LEU B 79  O TYR B 88  ? O TYR B 88  
AA6 3 4  N HIS B 94  ? N HIS B 94  O HIS B 119 ? O HIS B 119 
AA6 4 5  N LEU B 118 ? N LEU B 118 O ILE B 145 ? O ILE B 146 
AA6 5 6  N PHE B 146 ? N PHE B 147 O ILE B 215 ? O ILE B 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 ? 9  'binding site for residue BCN A 303' 
AC4 Software A PEG 304 ? 4  'binding site for residue PEG A 304' 
AC5 Software A MLA 305 ? 5  'binding site for residue MLA A 305' 
AC6 Software A 6YH 306 ? 13 'binding site for residue 6YH A 306' 
AC7 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC8 Software B DMS 302 ? 4  'binding site for residue DMS B 302' 
AC9 Software B BCN 303 ? 8  'binding site for residue BCN B 303' 
AD1 Software B MLA 304 ? 6  'binding site for residue MLA B 304' 
AD2 Software B 6YH 305 ? 13 'binding site for residue 6YH B 305' 
# 
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  6YH H .   ? 6YH A 306 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  HOH N .   ? HOH A 427 . ? 1_555 ? 
9  AC3 9  LYS A 148 ? LYS A 149 . ? 1_555 ? 
10 AC3 9  LYS A 212 ? LYS A 213 . ? 1_555 ? 
11 AC3 9  GLU A 213 ? GLU A 214 . ? 1_555 ? 
12 AC3 9  PRO A 214 ? PRO A 215 . ? 1_555 ? 
13 AC3 9  HOH N .   ? HOH A 435 . ? 1_555 ? 
14 AC3 9  HOH N .   ? HOH A 459 . ? 1_555 ? 
15 AC3 9  HOH N .   ? HOH A 488 . ? 1_555 ? 
16 AC3 9  HOH N .   ? HOH A 492 . ? 1_555 ? 
17 AC3 9  HOH N .   ? HOH A 672 . ? 1_555 ? 
18 AC4 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
19 AC4 4  PRO A 246 ? PRO A 247 . ? 1_555 ? 
20 AC4 4  HOH N .   ? HOH A 515 . ? 1_555 ? 
21 AC4 4  HOH N .   ? HOH A 590 . ? 1_555 ? 
22 AC5 5  ASN A 67  ? ASN A 67  . ? 1_555 ? 
23 AC5 5  GLN A 92  ? GLN A 92  . ? 1_555 ? 
24 AC5 5  PHE A 130 ? PHE A 131 . ? 1_555 ? 
25 AC5 5  6YH H .   ? 6YH A 306 . ? 1_555 ? 
26 AC5 5  HOH N .   ? HOH A 631 . ? 1_555 ? 
27 AC6 13 HIS A 94  ? HIS A 94  . ? 1_555 ? 
28 AC6 13 HIS A 96  ? HIS A 96  . ? 1_555 ? 
29 AC6 13 HIS A 119 ? HIS A 119 . ? 1_555 ? 
30 AC6 13 PHE A 130 ? PHE A 131 . ? 1_555 ? 
31 AC6 13 LEU A 197 ? LEU A 198 . ? 1_555 ? 
32 AC6 13 THR A 198 ? THR A 199 . ? 1_555 ? 
33 AC6 13 THR A 199 ? THR A 200 . ? 1_555 ? 
34 AC6 13 PRO A 201 ? PRO A 202 . ? 1_555 ? 
35 AC6 13 TRP A 208 ? TRP A 209 . ? 1_555 ? 
36 AC6 13 ZN  C .   ? ZN  A 301 . ? 1_555 ? 
37 AC6 13 MLA G .   ? MLA A 305 . ? 1_555 ? 
38 AC6 13 HOH N .   ? HOH A 483 . ? 1_555 ? 
39 AC6 13 HOH N .   ? HOH A 646 . ? 1_555 ? 
40 AC7 4  HIS B 94  ? HIS B 94  . ? 1_555 ? 
41 AC7 4  HIS B 96  ? HIS B 96  . ? 1_555 ? 
42 AC7 4  HIS B 119 ? HIS B 119 . ? 1_555 ? 
43 AC7 4  6YH M .   ? 6YH B 305 . ? 1_555 ? 
44 AC8 4  TYR B 7   ? TYR B 7   . ? 1_555 ? 
45 AC8 4  ASP B 242 ? ASP B 243 . ? 1_555 ? 
46 AC8 4  TRP B 244 ? TRP B 245 . ? 1_555 ? 
47 AC8 4  HOH O .   ? HOH B 854 . ? 1_555 ? 
48 AC9 8  LYS B 148 ? LYS B 149 . ? 1_555 ? 
49 AC9 8  LYS B 212 ? LYS B 213 . ? 1_555 ? 
50 AC9 8  GLU B 213 ? GLU B 214 . ? 1_555 ? 
51 AC9 8  PRO B 214 ? PRO B 215 . ? 1_555 ? 
52 AC9 8  HOH O .   ? HOH B 665 . ? 1_555 ? 
53 AC9 8  HOH O .   ? HOH B 669 . ? 1_555 ? 
54 AC9 8  HOH O .   ? HOH B 724 . ? 1_555 ? 
55 AC9 8  HOH O .   ? HOH B 779 . ? 1_555 ? 
56 AD1 6  ASN B 67  ? ASN B 67  . ? 1_555 ? 
57 AD1 6  ILE B 91  ? ILE B 91  . ? 1_555 ? 
58 AD1 6  GLN B 92  ? GLN B 92  . ? 1_555 ? 
59 AD1 6  PHE B 130 ? PHE B 131 . ? 1_555 ? 
60 AD1 6  6YH M .   ? 6YH B 305 . ? 1_555 ? 
61 AD1 6  HOH O .   ? HOH B 790 . ? 1_555 ? 
62 AD2 13 HIS B 94  ? HIS B 94  . ? 1_555 ? 
63 AD2 13 HIS B 96  ? HIS B 96  . ? 1_555 ? 
64 AD2 13 HIS B 119 ? HIS B 119 . ? 1_555 ? 
65 AD2 13 PHE B 130 ? PHE B 131 . ? 1_555 ? 
66 AD2 13 LEU B 197 ? LEU B 198 . ? 1_555 ? 
67 AD2 13 THR B 198 ? THR B 199 . ? 1_555 ? 
68 AD2 13 THR B 199 ? THR B 200 . ? 1_555 ? 
69 AD2 13 PRO B 201 ? PRO B 202 . ? 1_555 ? 
70 AD2 13 TRP B 208 ? TRP B 209 . ? 1_555 ? 
71 AD2 13 ZN  I .   ? ZN  B 301 . ? 1_555 ? 
72 AD2 13 MLA L .   ? MLA B 304 . ? 1_555 ? 
73 AD2 13 HOH O .   ? HOH B 635 . ? 1_555 ? 
74 AD2 13 HOH O .   ? HOH B 827 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 ND1 B HIS 10  ? A O B HOH 601 ? ? 1.97 
2  1 O   A LYS 76  ? ? O A HOH 401 ? ? 2.01 
3  1 O   A HOH 426 ? ? O A HOH 711 ? ? 2.02 
4  1 NE2 A HIS 4   ? ? O A HOH 402 ? ? 2.02 
5  1 OE1 A GLU 239 ? ? O A HOH 403 ? ? 2.03 
6  1 O   A HOH 405 ? ? O A HOH 598 ? ? 2.07 
7  1 ND1 B HIS 10  ? B O B HOH 601 ? ? 2.08 
8  1 O   B HOH 733 ? ? O B HOH 839 ? ? 2.11 
9  1 O   B HOH 604 ? ? O B HOH 666 ? ? 2.14 
10 1 O   A MET 1   ? ? O A HOH 404 ? ? 2.14 
11 1 O   B HOH 609 ? ? O B HOH 688 ? ? 2.15 
12 1 O   A HOH 413 ? ? O A HOH 616 ? ? 2.16 
13 1 NE2 B GLN 137 ? ? O B HOH 602 ? ? 2.16 
14 1 O   B HOH 814 ? ? O B HOH 829 ? ? 2.17 
15 1 OG  A SER 73  ? ? O A HOH 405 ? ? 2.17 
16 1 OE2 A GLU 26  ? ? O A HOH 406 ? ? 2.18 
17 1 O   A HOH 704 ? ? O A HOH 707 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 606 ? ? 1_555 O B HOH 641 ? ? 1_565 2.09 
2 1 O A HOH 627 ? ? 1_555 O B HOH 612 ? ? 1_566 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 36 ? ? CD2 A HIS 36 ? ? 1.415 1.354 0.061 0.009 N 
2 1 CG B HIS 36 ? A CD2 B HIS 36 ? A 1.411 1.354 0.057 0.009 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 SER A 2   ? ? -77.33  40.99   
2  1 HIS A 4   ? ? 88.89   -7.03   
3  1 ASN A 11  ? ? -140.90 14.01   
4  1 ARG A 27  ? ? -144.14 57.23   
5  1 GLU A 106 ? ? -91.44  -60.67  
6  1 LYS A 111 ? ? 75.15   -3.95   
7  1 ASN A 244 ? ? -94.06  44.41   
8  1 LYS A 252 ? ? 55.42   -138.16 
9  1 HIS B 3   ? ? -144.00 24.39   
10 1 ARG B 27  ? ? -144.09 53.73   
11 1 LEU B 57  ? ? -122.80 -52.08  
12 1 LYS B 76  ? ? -110.30 -87.76  
13 1 GLU B 106 ? ? -91.08  -61.60  
14 1 LYS B 111 ? ? 74.92   -2.97   
15 1 PHE B 176 ? ? -152.38 74.60   
16 1 ASN B 244 ? ? -93.59  46.76   
17 1 LYS B 252 ? ? 54.03   -134.74 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   HIS 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    3 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   HIS 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    4 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.26 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ALA 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              174 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.90 
# 
_phasing.method   MR 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     MET 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    MET 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
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 
6YH O12  O  N N 1   
6YH C11  C  N N 2   
6YH C4   C  Y N 3   
6YH C3   C  Y N 4   
6YH C2   C  Y N 5   
6YH C5   C  Y N 6   
6YH C6   C  Y N 7   
6YH C1   C  Y N 8   
6YH S7   S  N N 9   
6YH O9   O  N N 10  
6YH N10  N  N N 11  
6YH O8   O  N N 12  
6YH C13  C  N N 13  
6YH N14  N  Y N 14  
6YH C18  C  Y N 15  
6YH C20  C  Y N 16  
6YH C21  C  Y N 17  
6YH C22  C  Y N 18  
6YH C23  C  Y N 19  
6YH C19  C  Y N 20  
6YH N17  N  Y N 21  
6YH C16  C  Y N 22  
6YH H1   H  N N 23  
6YH H2   H  N N 24  
6YH H3   H  N N 25  
6YH H4   H  N N 26  
6YH H5   H  N N 27  
6YH H6   H  N N 28  
6YH H7   H  N N 29  
6YH H8   H  N N 30  
6YH H9   H  N N 31  
6YH H10  H  N N 32  
6YH H11  H  N N 33  
6YH H12  H  N N 34  
6YH H13  H  N N 35  
ALA N    N  N N 36  
ALA CA   C  N S 37  
ALA C    C  N N 38  
ALA O    O  N N 39  
ALA CB   C  N N 40  
ALA OXT  O  N N 41  
ALA H    H  N N 42  
ALA H2   H  N N 43  
ALA HA   H  N N 44  
ALA HB1  H  N N 45  
ALA HB2  H  N N 46  
ALA HB3  H  N N 47  
ALA HXT  H  N N 48  
ARG N    N  N N 49  
ARG CA   C  N S 50  
ARG C    C  N N 51  
ARG O    O  N N 52  
ARG CB   C  N N 53  
ARG CG   C  N N 54  
ARG CD   C  N N 55  
ARG NE   N  N N 56  
ARG CZ   C  N N 57  
ARG NH1  N  N N 58  
ARG NH2  N  N N 59  
ARG OXT  O  N N 60  
ARG H    H  N N 61  
ARG H2   H  N N 62  
ARG HA   H  N N 63  
ARG HB2  H  N N 64  
ARG HB3  H  N N 65  
ARG HG2  H  N N 66  
ARG HG3  H  N N 67  
ARG HD2  H  N N 68  
ARG HD3  H  N N 69  
ARG HE   H  N N 70  
ARG HH11 H  N N 71  
ARG HH12 H  N N 72  
ARG HH21 H  N N 73  
ARG HH22 H  N N 74  
ARG HXT  H  N N 75  
ASN N    N  N N 76  
ASN CA   C  N S 77  
ASN C    C  N N 78  
ASN O    O  N N 79  
ASN CB   C  N N 80  
ASN CG   C  N N 81  
ASN OD1  O  N N 82  
ASN ND2  N  N N 83  
ASN OXT  O  N N 84  
ASN H    H  N N 85  
ASN H2   H  N N 86  
ASN HA   H  N N 87  
ASN HB2  H  N N 88  
ASN HB3  H  N N 89  
ASN HD21 H  N N 90  
ASN HD22 H  N N 91  
ASN HXT  H  N N 92  
ASP N    N  N N 93  
ASP CA   C  N S 94  
ASP C    C  N N 95  
ASP O    O  N N 96  
ASP CB   C  N N 97  
ASP CG   C  N N 98  
ASP OD1  O  N N 99  
ASP OD2  O  N N 100 
ASP OXT  O  N N 101 
ASP H    H  N N 102 
ASP H2   H  N N 103 
ASP HA   H  N N 104 
ASP HB2  H  N N 105 
ASP HB3  H  N N 106 
ASP HD2  H  N N 107 
ASP HXT  H  N N 108 
BCN N1   N  N N 109 
BCN C1   C  N N 110 
BCN C2   C  N N 111 
BCN O21  O  N N 112 
BCN O22  O  N N 113 
BCN C3   C  N N 114 
BCN C4   C  N N 115 
BCN O4   O  N N 116 
BCN C5   C  N N 117 
BCN C6   C  N N 118 
BCN O6   O  N N 119 
BCN H11  H  N N 120 
BCN H12  H  N N 121 
BCN HO2  H  N N 122 
BCN H31  H  N N 123 
BCN H32  H  N N 124 
BCN H41  H  N N 125 
BCN H42  H  N N 126 
BCN HO4  H  N N 127 
BCN H51  H  N N 128 
BCN H52  H  N N 129 
BCN H61  H  N N 130 
BCN H62  H  N N 131 
BCN HO6  H  N N 132 
CYS N    N  N N 133 
CYS CA   C  N R 134 
CYS C    C  N N 135 
CYS O    O  N N 136 
CYS CB   C  N N 137 
CYS SG   S  N N 138 
CYS OXT  O  N N 139 
CYS H    H  N N 140 
CYS H2   H  N N 141 
CYS HA   H  N N 142 
CYS HB2  H  N N 143 
CYS HB3  H  N N 144 
CYS HG   H  N N 145 
CYS HXT  H  N N 146 
DMS S    S  N N 147 
DMS O    O  N N 148 
DMS C1   C  N N 149 
DMS C2   C  N N 150 
DMS H11  H  N N 151 
DMS H12  H  N N 152 
DMS H13  H  N N 153 
DMS H21  H  N N 154 
DMS H22  H  N N 155 
DMS H23  H  N N 156 
GLN N    N  N N 157 
GLN CA   C  N S 158 
GLN C    C  N N 159 
GLN O    O  N N 160 
GLN CB   C  N N 161 
GLN CG   C  N N 162 
GLN CD   C  N N 163 
GLN OE1  O  N N 164 
GLN NE2  N  N N 165 
GLN OXT  O  N N 166 
GLN H    H  N N 167 
GLN H2   H  N N 168 
GLN HA   H  N N 169 
GLN HB2  H  N N 170 
GLN HB3  H  N N 171 
GLN HG2  H  N N 172 
GLN HG3  H  N N 173 
GLN HE21 H  N N 174 
GLN HE22 H  N N 175 
GLN HXT  H  N N 176 
GLU N    N  N N 177 
GLU CA   C  N S 178 
GLU C    C  N N 179 
GLU O    O  N N 180 
GLU CB   C  N N 181 
GLU CG   C  N N 182 
GLU CD   C  N N 183 
GLU OE1  O  N N 184 
GLU OE2  O  N N 185 
GLU OXT  O  N N 186 
GLU H    H  N N 187 
GLU H2   H  N N 188 
GLU HA   H  N N 189 
GLU HB2  H  N N 190 
GLU HB3  H  N N 191 
GLU HG2  H  N N 192 
GLU HG3  H  N N 193 
GLU HE2  H  N N 194 
GLU HXT  H  N N 195 
GLY N    N  N N 196 
GLY CA   C  N N 197 
GLY C    C  N N 198 
GLY O    O  N N 199 
GLY OXT  O  N N 200 
GLY H    H  N N 201 
GLY H2   H  N N 202 
GLY HA2  H  N N 203 
GLY HA3  H  N N 204 
GLY HXT  H  N N 205 
HIS N    N  N N 206 
HIS CA   C  N S 207 
HIS C    C  N N 208 
HIS O    O  N N 209 
HIS CB   C  N N 210 
HIS CG   C  Y N 211 
HIS ND1  N  Y N 212 
HIS CD2  C  Y N 213 
HIS CE1  C  Y N 214 
HIS NE2  N  Y N 215 
HIS OXT  O  N N 216 
HIS H    H  N N 217 
HIS H2   H  N N 218 
HIS HA   H  N N 219 
HIS HB2  H  N N 220 
HIS HB3  H  N N 221 
HIS HD1  H  N N 222 
HIS HD2  H  N N 223 
HIS HE1  H  N N 224 
HIS HE2  H  N N 225 
HIS HXT  H  N N 226 
HOH O    O  N N 227 
HOH H1   H  N N 228 
HOH H2   H  N N 229 
ILE N    N  N N 230 
ILE CA   C  N S 231 
ILE C    C  N N 232 
ILE O    O  N N 233 
ILE CB   C  N S 234 
ILE CG1  C  N N 235 
ILE CG2  C  N N 236 
ILE CD1  C  N N 237 
ILE OXT  O  N N 238 
ILE H    H  N N 239 
ILE H2   H  N N 240 
ILE HA   H  N N 241 
ILE HB   H  N N 242 
ILE HG12 H  N N 243 
ILE HG13 H  N N 244 
ILE HG21 H  N N 245 
ILE HG22 H  N N 246 
ILE HG23 H  N N 247 
ILE HD11 H  N N 248 
ILE HD12 H  N N 249 
ILE HD13 H  N N 250 
ILE HXT  H  N N 251 
LEU N    N  N N 252 
LEU CA   C  N S 253 
LEU C    C  N N 254 
LEU O    O  N N 255 
LEU CB   C  N N 256 
LEU CG   C  N N 257 
LEU CD1  C  N N 258 
LEU CD2  C  N N 259 
LEU OXT  O  N N 260 
LEU H    H  N N 261 
LEU H2   H  N N 262 
LEU HA   H  N N 263 
LEU HB2  H  N N 264 
LEU HB3  H  N N 265 
LEU HG   H  N N 266 
LEU HD11 H  N N 267 
LEU HD12 H  N N 268 
LEU HD13 H  N N 269 
LEU HD21 H  N N 270 
LEU HD22 H  N N 271 
LEU HD23 H  N N 272 
LEU HXT  H  N N 273 
LYS N    N  N N 274 
LYS CA   C  N S 275 
LYS C    C  N N 276 
LYS O    O  N N 277 
LYS CB   C  N N 278 
LYS CG   C  N N 279 
LYS CD   C  N N 280 
LYS CE   C  N N 281 
LYS NZ   N  N N 282 
LYS OXT  O  N N 283 
LYS H    H  N N 284 
LYS H2   H  N N 285 
LYS HA   H  N N 286 
LYS HB2  H  N N 287 
LYS HB3  H  N N 288 
LYS HG2  H  N N 289 
LYS HG3  H  N N 290 
LYS HD2  H  N N 291 
LYS HD3  H  N N 292 
LYS HE2  H  N N 293 
LYS HE3  H  N N 294 
LYS HZ1  H  N N 295 
LYS HZ2  H  N N 296 
LYS HZ3  H  N N 297 
LYS HXT  H  N N 298 
MET N    N  N N 299 
MET CA   C  N S 300 
MET C    C  N N 301 
MET O    O  N N 302 
MET CB   C  N N 303 
MET CG   C  N N 304 
MET SD   S  N N 305 
MET CE   C  N N 306 
MET OXT  O  N N 307 
MET H    H  N N 308 
MET H2   H  N N 309 
MET HA   H  N N 310 
MET HB2  H  N N 311 
MET HB3  H  N N 312 
MET HG2  H  N N 313 
MET HG3  H  N N 314 
MET HE1  H  N N 315 
MET HE2  H  N N 316 
MET HE3  H  N N 317 
MET HXT  H  N N 318 
MLA C1   C  N N 319 
MLA O1A  O  N N 320 
MLA O1B  O  N N 321 
MLA C2   C  N N 322 
MLA C3   C  N N 323 
MLA O3A  O  N N 324 
MLA O3B  O  N N 325 
MLA H1A  H  N N 326 
MLA HC21 H  N N 327 
MLA HC22 H  N N 328 
MLA H3B  H  N N 329 
PEG C1   C  N N 330 
PEG O1   O  N N 331 
PEG C2   C  N N 332 
PEG O2   O  N N 333 
PEG C3   C  N N 334 
PEG C4   C  N N 335 
PEG O4   O  N N 336 
PEG H11  H  N N 337 
PEG H12  H  N N 338 
PEG HO1  H  N N 339 
PEG H21  H  N N 340 
PEG H22  H  N N 341 
PEG H31  H  N N 342 
PEG H32  H  N N 343 
PEG H41  H  N N 344 
PEG H42  H  N N 345 
PEG HO4  H  N N 346 
PHE N    N  N N 347 
PHE CA   C  N S 348 
PHE C    C  N N 349 
PHE O    O  N N 350 
PHE CB   C  N N 351 
PHE CG   C  Y N 352 
PHE CD1  C  Y N 353 
PHE CD2  C  Y N 354 
PHE CE1  C  Y N 355 
PHE CE2  C  Y N 356 
PHE CZ   C  Y N 357 
PHE OXT  O  N N 358 
PHE H    H  N N 359 
PHE H2   H  N N 360 
PHE HA   H  N N 361 
PHE HB2  H  N N 362 
PHE HB3  H  N N 363 
PHE HD1  H  N N 364 
PHE HD2  H  N N 365 
PHE HE1  H  N N 366 
PHE HE2  H  N N 367 
PHE HZ   H  N N 368 
PHE HXT  H  N N 369 
PRO N    N  N N 370 
PRO CA   C  N S 371 
PRO C    C  N N 372 
PRO O    O  N N 373 
PRO CB   C  N N 374 
PRO CG   C  N N 375 
PRO CD   C  N N 376 
PRO OXT  O  N N 377 
PRO H    H  N N 378 
PRO HA   H  N N 379 
PRO HB2  H  N N 380 
PRO HB3  H  N N 381 
PRO HG2  H  N N 382 
PRO HG3  H  N N 383 
PRO HD2  H  N N 384 
PRO HD3  H  N N 385 
PRO HXT  H  N N 386 
SER N    N  N N 387 
SER CA   C  N S 388 
SER C    C  N N 389 
SER O    O  N N 390 
SER CB   C  N N 391 
SER OG   O  N N 392 
SER OXT  O  N N 393 
SER H    H  N N 394 
SER H2   H  N N 395 
SER HA   H  N N 396 
SER HB2  H  N N 397 
SER HB3  H  N N 398 
SER HG   H  N N 399 
SER HXT  H  N N 400 
THR N    N  N N 401 
THR CA   C  N S 402 
THR C    C  N N 403 
THR O    O  N N 404 
THR CB   C  N R 405 
THR OG1  O  N N 406 
THR CG2  C  N N 407 
THR OXT  O  N N 408 
THR H    H  N N 409 
THR H2   H  N N 410 
THR HA   H  N N 411 
THR HB   H  N N 412 
THR HG1  H  N N 413 
THR HG21 H  N N 414 
THR HG22 H  N N 415 
THR HG23 H  N N 416 
THR HXT  H  N N 417 
TRP N    N  N N 418 
TRP CA   C  N S 419 
TRP C    C  N N 420 
TRP O    O  N N 421 
TRP CB   C  N N 422 
TRP CG   C  Y N 423 
TRP CD1  C  Y N 424 
TRP CD2  C  Y N 425 
TRP NE1  N  Y N 426 
TRP CE2  C  Y N 427 
TRP CE3  C  Y N 428 
TRP CZ2  C  Y N 429 
TRP CZ3  C  Y N 430 
TRP CH2  C  Y N 431 
TRP OXT  O  N N 432 
TRP H    H  N N 433 
TRP H2   H  N N 434 
TRP HA   H  N N 435 
TRP HB2  H  N N 436 
TRP HB3  H  N N 437 
TRP HD1  H  N N 438 
TRP HE1  H  N N 439 
TRP HE3  H  N N 440 
TRP HZ2  H  N N 441 
TRP HZ3  H  N N 442 
TRP HH2  H  N N 443 
TRP HXT  H  N N 444 
TYR N    N  N N 445 
TYR CA   C  N S 446 
TYR C    C  N N 447 
TYR O    O  N N 448 
TYR CB   C  N N 449 
TYR CG   C  Y N 450 
TYR CD1  C  Y N 451 
TYR CD2  C  Y N 452 
TYR CE1  C  Y N 453 
TYR CE2  C  Y N 454 
TYR CZ   C  Y N 455 
TYR OH   O  N N 456 
TYR OXT  O  N N 457 
TYR H    H  N N 458 
TYR H2   H  N N 459 
TYR HA   H  N N 460 
TYR HB2  H  N N 461 
TYR HB3  H  N N 462 
TYR HD1  H  N N 463 
TYR HD2  H  N N 464 
TYR HE1  H  N N 465 
TYR HE2  H  N N 466 
TYR HH   H  N N 467 
TYR HXT  H  N N 468 
VAL N    N  N N 469 
VAL CA   C  N S 470 
VAL C    C  N N 471 
VAL O    O  N N 472 
VAL CB   C  N N 473 
VAL CG1  C  N N 474 
VAL CG2  C  N N 475 
VAL OXT  O  N N 476 
VAL H    H  N N 477 
VAL H2   H  N N 478 
VAL HA   H  N N 479 
VAL HB   H  N N 480 
VAL HG11 H  N N 481 
VAL HG12 H  N N 482 
VAL HG13 H  N N 483 
VAL HG21 H  N N 484 
VAL HG22 H  N N 485 
VAL HG23 H  N N 486 
VAL HXT  H  N N 487 
ZN  ZN   ZN N N 488 
# 
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 
6YH N17 C16  doub Y N 1   
6YH N17 C19  sing Y N 2   
6YH C16 N14  sing Y N 3   
6YH C19 C23  doub Y N 4   
6YH C19 C18  sing Y N 5   
6YH N14 C18  sing Y N 6   
6YH N14 C13  sing N N 7   
6YH C23 C22  sing Y N 8   
6YH O12 C11  doub N N 9   
6YH C18 C20  doub Y N 10  
6YH C13 C11  sing N N 11  
6YH C11 C4   sing N N 12  
6YH C22 C21  doub Y N 13  
6YH C4  C3   doub Y N 14  
6YH C4  C5   sing Y N 15  
6YH C20 C21  sing Y N 16  
6YH C3  C2   sing Y N 17  
6YH C5  C6   doub Y N 18  
6YH C2  C1   doub Y N 19  
6YH C6  C1   sing Y N 20  
6YH C1  S7   sing N N 21  
6YH N10 S7   sing N N 22  
6YH O8  S7   doub N N 23  
6YH S7  O9   doub N N 24  
6YH C3  H1   sing N N 25  
6YH C2  H2   sing N N 26  
6YH C5  H3   sing N N 27  
6YH C6  H4   sing N N 28  
6YH N10 H5   sing N N 29  
6YH N10 H6   sing N N 30  
6YH C13 H7   sing N N 31  
6YH C13 H8   sing N N 32  
6YH C20 H9   sing N N 33  
6YH C21 H10  sing N N 34  
6YH C22 H11  sing N N 35  
6YH C23 H12  sing N N 36  
6YH C16 H13  sing N N 37  
ALA N   CA   sing N N 38  
ALA N   H    sing N N 39  
ALA N   H2   sing N N 40  
ALA CA  C    sing N N 41  
ALA CA  CB   sing N N 42  
ALA CA  HA   sing N N 43  
ALA C   O    doub N N 44  
ALA C   OXT  sing N N 45  
ALA CB  HB1  sing N N 46  
ALA CB  HB2  sing N N 47  
ALA CB  HB3  sing N N 48  
ALA OXT HXT  sing N N 49  
ARG N   CA   sing N N 50  
ARG N   H    sing N N 51  
ARG N   H2   sing N N 52  
ARG CA  C    sing N N 53  
ARG CA  CB   sing N N 54  
ARG CA  HA   sing N N 55  
ARG C   O    doub N N 56  
ARG C   OXT  sing N N 57  
ARG CB  CG   sing N N 58  
ARG CB  HB2  sing N N 59  
ARG CB  HB3  sing N N 60  
ARG CG  CD   sing N N 61  
ARG CG  HG2  sing N N 62  
ARG CG  HG3  sing N N 63  
ARG CD  NE   sing N N 64  
ARG CD  HD2  sing N N 65  
ARG CD  HD3  sing N N 66  
ARG NE  CZ   sing N N 67  
ARG NE  HE   sing N N 68  
ARG CZ  NH1  sing N N 69  
ARG CZ  NH2  doub N N 70  
ARG NH1 HH11 sing N N 71  
ARG NH1 HH12 sing N N 72  
ARG NH2 HH21 sing N N 73  
ARG NH2 HH22 sing N N 74  
ARG OXT HXT  sing N N 75  
ASN N   CA   sing N N 76  
ASN N   H    sing N N 77  
ASN N   H2   sing N N 78  
ASN CA  C    sing N N 79  
ASN CA  CB   sing N N 80  
ASN CA  HA   sing N N 81  
ASN C   O    doub N N 82  
ASN C   OXT  sing N N 83  
ASN CB  CG   sing N N 84  
ASN CB  HB2  sing N N 85  
ASN CB  HB3  sing N N 86  
ASN CG  OD1  doub N N 87  
ASN CG  ND2  sing N N 88  
ASN ND2 HD21 sing N N 89  
ASN ND2 HD22 sing N N 90  
ASN OXT HXT  sing N N 91  
ASP N   CA   sing N N 92  
ASP N   H    sing N N 93  
ASP N   H2   sing N N 94  
ASP CA  C    sing N N 95  
ASP CA  CB   sing N N 96  
ASP CA  HA   sing N N 97  
ASP C   O    doub N N 98  
ASP C   OXT  sing N N 99  
ASP CB  CG   sing N N 100 
ASP CB  HB2  sing N N 101 
ASP CB  HB3  sing N N 102 
ASP CG  OD1  doub N N 103 
ASP CG  OD2  sing N N 104 
ASP OD2 HD2  sing N N 105 
ASP OXT HXT  sing N N 106 
BCN N1  C1   sing N N 107 
BCN N1  C3   sing N N 108 
BCN N1  C5   sing N N 109 
BCN C1  C2   sing N N 110 
BCN C1  H11  sing N N 111 
BCN C1  H12  sing N N 112 
BCN C2  O21  doub N N 113 
BCN C2  O22  sing N N 114 
BCN O22 HO2  sing N N 115 
BCN C3  C4   sing N N 116 
BCN C3  H31  sing N N 117 
BCN C3  H32  sing N N 118 
BCN C4  O4   sing N N 119 
BCN C4  H41  sing N N 120 
BCN C4  H42  sing N N 121 
BCN O4  HO4  sing N N 122 
BCN C5  C6   sing N N 123 
BCN C5  H51  sing N N 124 
BCN C5  H52  sing N N 125 
BCN C6  O6   sing N N 126 
BCN C6  H61  sing N N 127 
BCN C6  H62  sing N N 128 
BCN O6  HO6  sing N N 129 
CYS N   CA   sing N N 130 
CYS N   H    sing N N 131 
CYS N   H2   sing N N 132 
CYS CA  C    sing N N 133 
CYS CA  CB   sing N N 134 
CYS CA  HA   sing N N 135 
CYS C   O    doub N N 136 
CYS C   OXT  sing N N 137 
CYS CB  SG   sing N N 138 
CYS CB  HB2  sing N N 139 
CYS CB  HB3  sing N N 140 
CYS SG  HG   sing N N 141 
CYS OXT HXT  sing N N 142 
DMS S   O    doub N N 143 
DMS S   C1   sing N N 144 
DMS S   C2   sing N N 145 
DMS C1  H11  sing N N 146 
DMS C1  H12  sing N N 147 
DMS C1  H13  sing N N 148 
DMS C2  H21  sing N N 149 
DMS C2  H22  sing N N 150 
DMS C2  H23  sing N N 151 
GLN N   CA   sing N N 152 
GLN N   H    sing N N 153 
GLN N   H2   sing N N 154 
GLN CA  C    sing N N 155 
GLN CA  CB   sing N N 156 
GLN CA  HA   sing N N 157 
GLN C   O    doub N N 158 
GLN C   OXT  sing N N 159 
GLN CB  CG   sing N N 160 
GLN CB  HB2  sing N N 161 
GLN CB  HB3  sing N N 162 
GLN CG  CD   sing N N 163 
GLN CG  HG2  sing N N 164 
GLN CG  HG3  sing N N 165 
GLN CD  OE1  doub N N 166 
GLN CD  NE2  sing N N 167 
GLN NE2 HE21 sing N N 168 
GLN NE2 HE22 sing N N 169 
GLN OXT HXT  sing N N 170 
GLU N   CA   sing N N 171 
GLU N   H    sing N N 172 
GLU N   H2   sing N N 173 
GLU CA  C    sing N N 174 
GLU CA  CB   sing N N 175 
GLU CA  HA   sing N N 176 
GLU C   O    doub N N 177 
GLU C   OXT  sing N N 178 
GLU CB  CG   sing N N 179 
GLU CB  HB2  sing N N 180 
GLU CB  HB3  sing N N 181 
GLU CG  CD   sing N N 182 
GLU CG  HG2  sing N N 183 
GLU CG  HG3  sing N N 184 
GLU CD  OE1  doub N N 185 
GLU CD  OE2  sing N N 186 
GLU OE2 HE2  sing N N 187 
GLU OXT HXT  sing N N 188 
GLY N   CA   sing N N 189 
GLY N   H    sing N N 190 
GLY N   H2   sing N N 191 
GLY CA  C    sing N N 192 
GLY CA  HA2  sing N N 193 
GLY CA  HA3  sing N N 194 
GLY C   O    doub N N 195 
GLY C   OXT  sing N N 196 
GLY OXT HXT  sing N N 197 
HIS N   CA   sing N N 198 
HIS N   H    sing N N 199 
HIS N   H2   sing N N 200 
HIS CA  C    sing N N 201 
HIS CA  CB   sing N N 202 
HIS CA  HA   sing N N 203 
HIS C   O    doub N N 204 
HIS C   OXT  sing N N 205 
HIS CB  CG   sing N N 206 
HIS CB  HB2  sing N N 207 
HIS CB  HB3  sing N N 208 
HIS CG  ND1  sing Y N 209 
HIS CG  CD2  doub Y N 210 
HIS ND1 CE1  doub Y N 211 
HIS ND1 HD1  sing N N 212 
HIS CD2 NE2  sing Y N 213 
HIS CD2 HD2  sing N N 214 
HIS CE1 NE2  sing Y N 215 
HIS CE1 HE1  sing N N 216 
HIS NE2 HE2  sing N N 217 
HIS OXT HXT  sing N N 218 
HOH O   H1   sing N N 219 
HOH O   H2   sing N N 220 
ILE N   CA   sing N N 221 
ILE N   H    sing N N 222 
ILE N   H2   sing N N 223 
ILE CA  C    sing N N 224 
ILE CA  CB   sing N N 225 
ILE CA  HA   sing N N 226 
ILE C   O    doub N N 227 
ILE C   OXT  sing N N 228 
ILE CB  CG1  sing N N 229 
ILE CB  CG2  sing N N 230 
ILE CB  HB   sing N N 231 
ILE CG1 CD1  sing N N 232 
ILE CG1 HG12 sing N N 233 
ILE CG1 HG13 sing N N 234 
ILE CG2 HG21 sing N N 235 
ILE CG2 HG22 sing N N 236 
ILE CG2 HG23 sing N N 237 
ILE CD1 HD11 sing N N 238 
ILE CD1 HD12 sing N N 239 
ILE CD1 HD13 sing N N 240 
ILE OXT HXT  sing N N 241 
LEU N   CA   sing N N 242 
LEU N   H    sing N N 243 
LEU N   H2   sing N N 244 
LEU CA  C    sing N N 245 
LEU CA  CB   sing N N 246 
LEU CA  HA   sing N N 247 
LEU C   O    doub N N 248 
LEU C   OXT  sing N N 249 
LEU CB  CG   sing N N 250 
LEU CB  HB2  sing N N 251 
LEU CB  HB3  sing N N 252 
LEU CG  CD1  sing N N 253 
LEU CG  CD2  sing N N 254 
LEU CG  HG   sing N N 255 
LEU CD1 HD11 sing N N 256 
LEU CD1 HD12 sing N N 257 
LEU CD1 HD13 sing N N 258 
LEU CD2 HD21 sing N N 259 
LEU CD2 HD22 sing N N 260 
LEU CD2 HD23 sing N N 261 
LEU OXT HXT  sing N N 262 
LYS N   CA   sing N N 263 
LYS N   H    sing N N 264 
LYS N   H2   sing N N 265 
LYS CA  C    sing N N 266 
LYS CA  CB   sing N N 267 
LYS CA  HA   sing N N 268 
LYS C   O    doub N N 269 
LYS C   OXT  sing N N 270 
LYS CB  CG   sing N N 271 
LYS CB  HB2  sing N N 272 
LYS CB  HB3  sing N N 273 
LYS CG  CD   sing N N 274 
LYS CG  HG2  sing N N 275 
LYS CG  HG3  sing N N 276 
LYS CD  CE   sing N N 277 
LYS CD  HD2  sing N N 278 
LYS CD  HD3  sing N N 279 
LYS CE  NZ   sing N N 280 
LYS CE  HE2  sing N N 281 
LYS CE  HE3  sing N N 282 
LYS NZ  HZ1  sing N N 283 
LYS NZ  HZ2  sing N N 284 
LYS NZ  HZ3  sing N N 285 
LYS OXT HXT  sing N N 286 
MET N   CA   sing N N 287 
MET N   H    sing N N 288 
MET N   H2   sing N N 289 
MET CA  C    sing N N 290 
MET CA  CB   sing N N 291 
MET CA  HA   sing N N 292 
MET C   O    doub N N 293 
MET C   OXT  sing N N 294 
MET CB  CG   sing N N 295 
MET CB  HB2  sing N N 296 
MET CB  HB3  sing N N 297 
MET CG  SD   sing N N 298 
MET CG  HG2  sing N N 299 
MET CG  HG3  sing N N 300 
MET SD  CE   sing N N 301 
MET CE  HE1  sing N N 302 
MET CE  HE2  sing N N 303 
MET CE  HE3  sing N N 304 
MET OXT HXT  sing N N 305 
MLA C1  O1A  sing N N 306 
MLA C1  O1B  doub N N 307 
MLA C1  C2   sing N N 308 
MLA O1A H1A  sing N N 309 
MLA C2  C3   sing N N 310 
MLA C2  HC21 sing N N 311 
MLA C2  HC22 sing N N 312 
MLA C3  O3A  doub N N 313 
MLA C3  O3B  sing N N 314 
MLA O3B H3B  sing N N 315 
PEG C1  O1   sing N N 316 
PEG C1  C2   sing N N 317 
PEG C1  H11  sing N N 318 
PEG C1  H12  sing N N 319 
PEG O1  HO1  sing N N 320 
PEG C2  O2   sing N N 321 
PEG C2  H21  sing N N 322 
PEG C2  H22  sing N N 323 
PEG O2  C3   sing N N 324 
PEG C3  C4   sing N N 325 
PEG C3  H31  sing N N 326 
PEG C3  H32  sing N N 327 
PEG C4  O4   sing N N 328 
PEG C4  H41  sing N N 329 
PEG C4  H42  sing N N 330 
PEG O4  HO4  sing N N 331 
PHE N   CA   sing N N 332 
PHE N   H    sing N N 333 
PHE N   H2   sing N N 334 
PHE CA  C    sing N N 335 
PHE CA  CB   sing N N 336 
PHE CA  HA   sing N N 337 
PHE C   O    doub N N 338 
PHE C   OXT  sing N N 339 
PHE CB  CG   sing N N 340 
PHE CB  HB2  sing N N 341 
PHE CB  HB3  sing N N 342 
PHE CG  CD1  doub Y N 343 
PHE CG  CD2  sing Y N 344 
PHE CD1 CE1  sing Y N 345 
PHE CD1 HD1  sing N N 346 
PHE CD2 CE2  doub Y N 347 
PHE CD2 HD2  sing N N 348 
PHE CE1 CZ   doub Y N 349 
PHE CE1 HE1  sing N N 350 
PHE CE2 CZ   sing Y N 351 
PHE CE2 HE2  sing N N 352 
PHE CZ  HZ   sing N N 353 
PHE OXT HXT  sing N N 354 
PRO N   CA   sing N N 355 
PRO N   CD   sing N N 356 
PRO N   H    sing N N 357 
PRO CA  C    sing N N 358 
PRO CA  CB   sing N N 359 
PRO CA  HA   sing N N 360 
PRO C   O    doub N N 361 
PRO C   OXT  sing N N 362 
PRO CB  CG   sing N N 363 
PRO CB  HB2  sing N N 364 
PRO CB  HB3  sing N N 365 
PRO CG  CD   sing N N 366 
PRO CG  HG2  sing N N 367 
PRO CG  HG3  sing N N 368 
PRO CD  HD2  sing N N 369 
PRO CD  HD3  sing N N 370 
PRO OXT HXT  sing N N 371 
SER N   CA   sing N N 372 
SER N   H    sing N N 373 
SER N   H2   sing N N 374 
SER CA  C    sing N N 375 
SER CA  CB   sing N N 376 
SER CA  HA   sing N N 377 
SER C   O    doub N N 378 
SER C   OXT  sing N N 379 
SER CB  OG   sing N N 380 
SER CB  HB2  sing N N 381 
SER CB  HB3  sing N N 382 
SER OG  HG   sing N N 383 
SER OXT HXT  sing N N 384 
THR N   CA   sing N N 385 
THR N   H    sing N N 386 
THR N   H2   sing N N 387 
THR CA  C    sing N N 388 
THR CA  CB   sing N N 389 
THR CA  HA   sing N N 390 
THR C   O    doub N N 391 
THR C   OXT  sing N N 392 
THR CB  OG1  sing N N 393 
THR CB  CG2  sing N N 394 
THR CB  HB   sing N N 395 
THR OG1 HG1  sing N N 396 
THR CG2 HG21 sing N N 397 
THR CG2 HG22 sing N N 398 
THR CG2 HG23 sing N N 399 
THR OXT HXT  sing N N 400 
TRP N   CA   sing N N 401 
TRP N   H    sing N N 402 
TRP N   H2   sing N N 403 
TRP CA  C    sing N N 404 
TRP CA  CB   sing N N 405 
TRP CA  HA   sing N N 406 
TRP C   O    doub N N 407 
TRP C   OXT  sing N N 408 
TRP CB  CG   sing N N 409 
TRP CB  HB2  sing N N 410 
TRP CB  HB3  sing N N 411 
TRP CG  CD1  doub Y N 412 
TRP CG  CD2  sing Y N 413 
TRP CD1 NE1  sing Y N 414 
TRP CD1 HD1  sing N N 415 
TRP CD2 CE2  doub Y N 416 
TRP CD2 CE3  sing Y N 417 
TRP NE1 CE2  sing Y N 418 
TRP NE1 HE1  sing N N 419 
TRP CE2 CZ2  sing Y N 420 
TRP CE3 CZ3  doub Y N 421 
TRP CE3 HE3  sing N N 422 
TRP CZ2 CH2  doub Y N 423 
TRP CZ2 HZ2  sing N N 424 
TRP CZ3 CH2  sing Y N 425 
TRP CZ3 HZ3  sing N N 426 
TRP CH2 HH2  sing N N 427 
TRP OXT HXT  sing N N 428 
TYR N   CA   sing N N 429 
TYR N   H    sing N N 430 
TYR N   H2   sing N N 431 
TYR CA  C    sing N N 432 
TYR CA  CB   sing N N 433 
TYR CA  HA   sing N N 434 
TYR C   O    doub N N 435 
TYR C   OXT  sing N N 436 
TYR CB  CG   sing N N 437 
TYR CB  HB2  sing N N 438 
TYR CB  HB3  sing N N 439 
TYR CG  CD1  doub Y N 440 
TYR CG  CD2  sing Y N 441 
TYR CD1 CE1  sing Y N 442 
TYR CD1 HD1  sing N N 443 
TYR CD2 CE2  doub Y N 444 
TYR CD2 HD2  sing N N 445 
TYR CE1 CZ   doub Y N 446 
TYR CE1 HE1  sing N N 447 
TYR CE2 CZ   sing Y N 448 
TYR CE2 HE2  sing N N 449 
TYR CZ  OH   sing N N 450 
TYR OH  HH   sing N N 451 
TYR OXT HXT  sing N N 452 
VAL N   CA   sing N N 453 
VAL N   H    sing N N 454 
VAL N   H2   sing N N 455 
VAL CA  C    sing N N 456 
VAL CA  CB   sing N N 457 
VAL CA  HA   sing N N 458 
VAL C   O    doub N N 459 
VAL C   OXT  sing N N 460 
VAL CB  CG1  sing N N 461 
VAL CB  CG2  sing N N 462 
VAL CB  HB   sing N N 463 
VAL CG1 HG11 sing N N 464 
VAL CG1 HG12 sing N N 465 
VAL CG1 HG13 sing N N 466 
VAL CG2 HG21 sing N N 467 
VAL CG2 HG22 sing N N 468 
VAL CG2 HG23 sing N N 469 
VAL OXT HXT  sing N N 470 
# 
_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   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    5LL4 
_atom_sites.fract_transf_matrix[1][1]   0.023747 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006015 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024287 
_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]   0.014311 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
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   . MET A 1 1   ? 18.906  9.073   -2.932  1.00 45.00  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 19.629  8.067   -3.764  1.00 35.35  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 18.679  7.031   -4.311  1.00 39.06  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 19.063  5.862   -4.414  1.00 36.58  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 20.611  7.362   -2.885  1.00 25.45  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 21.316  8.406   -2.081  1.00 31.54  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 20.527  8.683   -0.531  1.00 30.88  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 20.959  10.406  -0.233  1.00 29.51  ? 1   MET A CE  1 
ATOM   9    N  N   . SER A 1 2   ? 17.436  7.459   -4.584  1.00 51.71  ? 2   SER A N   1 
ATOM   10   C  CA  . SER A 1 2   ? 16.348  6.518   -4.849  1.00 41.68  ? 2   SER A CA  1 
ATOM   11   C  C   . SER A 1 2   ? 16.355  5.890   -6.254  1.00 43.73  ? 2   SER A C   1 
ATOM   12   O  O   . SER A 1 2   ? 15.308  5.724   -6.882  1.00 50.74  ? 2   SER A O   1 
ATOM   13   C  CB  . SER A 1 2   ? 14.954  7.019   -4.416  1.00 34.29  ? 2   SER A CB  1 
ATOM   14   O  OG  . SER A 1 2   ? 13.977  6.106   -4.869  1.00 34.65  ? 2   SER A OG  1 
ATOM   15   N  N   . HIS A 1 3   ? 17.562  5.543   -6.697  1.00 55.08  ? 3   HIS A N   1 
ATOM   16   C  CA  . HIS A 1 3   ? 17.826  4.528   -7.695  1.00 27.06  ? 3   HIS A CA  1 
ATOM   17   C  C   . HIS A 1 3   ? 19.076  3.856   -7.322  1.00 34.88  ? 3   HIS A C   1 
ATOM   18   O  O   . HIS A 1 3   ? 19.788  4.276   -6.407  1.00 55.27  ? 3   HIS A O   1 
ATOM   19   C  CB  . HIS A 1 3   ? 17.940  5.185   -9.074  1.00 37.06  ? 3   HIS A CB  1 
ATOM   20   N  N   . HIS A 1 4   ? 19.266  2.649   -7.822  1.00 31.18  ? 4   HIS A N   1 
ATOM   21   C  CA  . HIS A 1 4   ? 20.247  1.784   -7.209  1.00 23.24  ? 4   HIS A CA  1 
ATOM   22   C  C   . HIS A 1 4   ? 19.704  0.961   -6.119  1.00 20.37  ? 4   HIS A C   1 
ATOM   23   O  O   . HIS A 1 4   ? 20.431  0.080   -5.613  1.00 22.49  ? 4   HIS A O   1 
ATOM   24   C  CB  . HIS A 1 4   ? 21.284  2.574   -6.484  1.00 26.98  ? 4   HIS A CB  1 
ATOM   25   C  CG  . HIS A 1 4   ? 22.529  1.787   -6.153  1.00 47.53  ? 4   HIS A CG  1 
ATOM   26   N  ND1 . HIS A 1 4   ? 23.092  1.804   -4.931  1.00 49.28  ? 4   HIS A ND1 1 
ATOM   27   C  CD2 . HIS A 1 4   ? 23.316  0.945   -6.937  1.00 58.07  ? 4   HIS A CD2 1 
ATOM   28   C  CE1 . HIS A 1 4   ? 24.182  1.015   -4.929  1.00 78.24  ? 4   HIS A CE1 1 
ATOM   29   N  NE2 . HIS A 1 4   ? 24.318  0.489   -6.157  1.00 78.46  ? 4   HIS A NE2 1 
ATOM   30   N  N   . TRP A 1 5   ? 18.449  1.168   -5.698  1.00 19.50  ? 5   TRP A N   1 
ATOM   31   C  CA  . TRP A 1 5   ? 17.947  0.286   -4.623  1.00 15.36  ? 5   TRP A CA  1 
ATOM   32   C  C   . TRP A 1 5   ? 16.953  -0.526  -5.409  1.00 17.34  ? 5   TRP A C   1 
ATOM   33   O  O   . TRP A 1 5   ? 16.403  -0.036  -6.423  1.00 18.52  ? 5   TRP A O   1 
ATOM   34   C  CB  . TRP A 1 5   ? 17.363  0.980   -3.411  1.00 16.97  ? 5   TRP A CB  1 
ATOM   35   C  CG  . TRP A 1 5   ? 16.169  1.831   -3.751  1.00 14.93  ? 5   TRP A CG  1 
ATOM   36   C  CD1 . TRP A 1 5   ? 16.123  3.179   -4.043  1.00 16.36  ? 5   TRP A CD1 1 
ATOM   37   C  CD2 . TRP A 1 5   ? 14.778  1.368   -3.818  1.00 13.64  ? 5   TRP A CD2 1 
ATOM   38   N  NE1 . TRP A 1 5   ? 14.855  3.577   -4.304  1.00 16.10  ? 5   TRP A NE1 1 
ATOM   39   C  CE2 . TRP A 1 5   ? 13.986  2.517   -4.182  1.00 14.07  ? 5   TRP A CE2 1 
ATOM   40   C  CE3 . TRP A 1 5   ? 14.130  0.131   -3.591  1.00 13.90  ? 5   TRP A CE3 1 
ATOM   41   C  CZ2 . TRP A 1 5   ? 12.627  2.455   -4.304  1.00 14.88  ? 5   TRP A CZ2 1 
ATOM   42   C  CZ3 . TRP A 1 5   ? 12.741  0.090   -3.751  1.00 14.14  ? 5   TRP A CZ3 1 
ATOM   43   C  CH2 . TRP A 1 5   ? 12.001  1.239   -4.119  1.00 14.85  ? 5   TRP A CH2 1 
ATOM   44   N  N   . GLY A 1 6   ? 16.658  -1.716  -4.920  1.00 14.92  ? 6   GLY A N   1 
ATOM   45   C  CA  . GLY A 1 6   ? 15.582  -2.499  -5.548  1.00 15.67  ? 6   GLY A CA  1 
ATOM   46   C  C   . GLY A 1 6   ? 15.302  -3.646  -4.616  1.00 15.65  ? 6   GLY A C   1 
ATOM   47   O  O   . GLY A 1 6   ? 15.303  -3.502  -3.394  1.00 14.25  ? 6   GLY A O   1 
ATOM   48   N  N   A TYR A 1 7   ? 14.943  -4.798  -5.194  0.50 18.04  ? 7   TYR A N   1 
ATOM   49   N  N   B TYR A 1 7   ? 15.154  -4.840  -5.177  0.50 20.76  ? 7   TYR A N   1 
ATOM   50   C  CA  A TYR A 1 7   ? 14.467  -5.961  -4.419  0.50 18.45  ? 7   TYR A CA  1 
ATOM   51   C  CA  B TYR A 1 7   ? 14.742  -5.985  -4.367  0.50 21.92  ? 7   TYR A CA  1 
ATOM   52   C  C   A TYR A 1 7   ? 15.284  -7.204  -4.643  0.50 27.55  ? 7   TYR A C   1 
ATOM   53   C  C   B TYR A 1 7   ? 15.715  -7.220  -4.286  0.50 23.19  ? 7   TYR A C   1 
ATOM   54   O  O   A TYR A 1 7   ? 14.797  -8.336  -4.550  0.50 39.28  ? 7   TYR A O   1 
ATOM   55   O  O   B TYR A 1 7   ? 15.459  -8.264  -3.559  0.50 20.46  ? 7   TYR A O   1 
ATOM   56   C  CB  A TYR A 1 7   ? 12.964  -6.237  -4.702  0.50 17.20  ? 7   TYR A CB  1 
ATOM   57   C  CB  B TYR A 1 7   ? 13.203  -6.280  -4.682  0.50 20.29  ? 7   TYR A CB  1 
ATOM   58   C  CG  A TYR A 1 7   ? 12.091  -5.182  -4.082  0.50 12.12  ? 7   TYR A CG  1 
ATOM   59   C  CG  B TYR A 1 7   ? 12.248  -5.150  -4.179  0.50 12.77  ? 7   TYR A CG  1 
ATOM   60   C  CD1 A TYR A 1 7   ? 11.733  -5.264  -2.733  0.50 11.89  ? 7   TYR A CD1 1 
ATOM   61   C  CD1 B TYR A 1 7   ? 11.822  -5.144  -2.846  0.50 12.73  ? 7   TYR A CD1 1 
ATOM   62   C  CD2 A TYR A 1 7   ? 11.584  -4.152  -4.860  0.50 13.44  ? 7   TYR A CD2 1 
ATOM   63   C  CD2 B TYR A 1 7   ? 11.786  -4.139  -5.030  0.50 14.65  ? 7   TYR A CD2 1 
ATOM   64   C  CE1 A TYR A 1 7   ? 10.905  -4.290  -2.174  0.50 9.84   ? 7   TYR A CE1 1 
ATOM   65   C  CE1 B TYR A 1 7   ? 10.978  -4.137  -2.369  0.50 10.77  ? 7   TYR A CE1 1 
ATOM   66   C  CE2 A TYR A 1 7   ? 10.743  -3.191  -4.321  0.50 11.61  ? 7   TYR A CE2 1 
ATOM   67   C  CE2 B TYR A 1 7   ? 10.922  -3.150  -4.559  0.50 13.10  ? 7   TYR A CE2 1 
ATOM   68   C  CZ  A TYR A 1 7   ? 10.388  -3.281  -2.999  0.50 9.17   ? 7   TYR A CZ  1 
ATOM   69   C  CZ  B TYR A 1 7   ? 10.509  -3.169  -3.243  0.50 11.35  ? 7   TYR A CZ  1 
ATOM   70   O  OH  A TYR A 1 7   ? 9.548   -2.352  -2.501  0.50 9.95   ? 7   TYR A OH  1 
ATOM   71   O  OH  B TYR A 1 7   ? 9.664   -2.214  -2.768  0.50 12.90  ? 7   TYR A OH  1 
ATOM   72   N  N   A GLY A 1 8   ? 16.599  -7.033  -4.838  0.50 29.35  ? 8   GLY A N   1 
ATOM   73   N  N   B GLY A 1 8   ? 16.885  -7.138  -4.935  0.50 23.13  ? 8   GLY A N   1 
ATOM   74   C  CA  A GLY A 1 8   ? 17.516  -8.168  -5.024  0.50 20.62  ? 8   GLY A CA  1 
ATOM   75   C  CA  B GLY A 1 8   ? 17.840  -8.266  -5.000  0.50 18.42  ? 8   GLY A CA  1 
ATOM   76   C  C   A GLY A 1 8   ? 18.616  -8.454  -3.983  0.50 21.10  ? 8   GLY A C   1 
ATOM   77   C  C   B GLY A 1 8   ? 18.947  -8.538  -3.952  0.50 22.39  ? 8   GLY A C   1 
ATOM   78   O  O   A GLY A 1 8   ? 18.709  -7.757  -2.976  0.50 23.68  ? 8   GLY A O   1 
ATOM   79   O  O   B GLY A 1 8   ? 19.043  -7.820  -2.957  0.50 26.76  ? 8   GLY A O   1 
ATOM   80   N  N   A LYS A 1 9   ? 19.437  -9.489  -4.230  0.50 21.02  ? 9   LYS A N   1 
ATOM   81   N  N   B LYS A 1 9   ? 19.776  -9.579  -4.178  0.50 23.12  ? 9   LYS A N   1 
ATOM   82   C  CA  A LYS A 1 9   ? 20.530  -9.929  -3.362  0.50 31.02  ? 9   LYS A CA  1 
ATOM   83   C  CA  B LYS A 1 9   ? 20.880  -10.006 -3.280  0.50 27.55  ? 9   LYS A CA  1 
ATOM   84   C  C   A LYS A 1 9   ? 21.452  -8.769  -3.045  0.50 25.36  ? 9   LYS A C   1 
ATOM   85   C  C   B LYS A 1 9   ? 21.743  -8.839  -3.001  0.50 23.14  ? 9   LYS A C   1 
ATOM   86   O  O   A LYS A 1 9   ? 21.884  -8.587  -1.884  0.50 23.34  ? 9   LYS A O   1 
ATOM   87   O  O   B LYS A 1 9   ? 22.221  -8.671  -1.856  0.50 27.75  ? 9   LYS A O   1 
ATOM   88   C  CB  A LYS A 1 9   ? 21.302  -11.100 -4.029  0.50 33.48  ? 9   LYS A CB  1 
ATOM   89   C  CB  B LYS A 1 9   ? 21.759  -11.050 -3.976  0.50 29.67  ? 9   LYS A CB  1 
ATOM   90   C  CG  A LYS A 1 9   ? 20.557  -11.718 -5.207  0.50 38.50  ? 9   LYS A CG  1 
ATOM   91   C  CG  B LYS A 1 9   ? 21.355  -12.485 -3.739  0.50 41.54  ? 9   LYS A CG  1 
ATOM   92   C  CD  A LYS A 1 9   ? 21.162  -13.058 -5.592  0.50 53.77  ? 9   LYS A CD  1 
ATOM   93   C  CD  B LYS A 1 9   ? 22.173  -13.412 -4.644  0.50 56.81  ? 9   LYS A CD  1 
ATOM   94   C  CE  A LYS A 1 9   ? 20.078  -14.109 -5.801  0.50 58.65  ? 9   LYS A CE  1 
ATOM   95   C  CE  B LYS A 1 9   ? 21.508  -14.791 -4.643  0.50 64.08  ? 9   LYS A CE  1 
ATOM   96   N  NZ  A LYS A 1 9   ? 20.567  -15.501 -5.539  0.50 60.94  ? 9   LYS A NZ  1 
ATOM   97   N  NZ  B LYS A 1 9   ? 21.682  -15.485 -5.951  0.50 71.22  ? 9   LYS A NZ  1 
ATOM   98   N  N   A HIS A 1 10  ? 21.775  -7.986  -4.078  0.50 25.13  ? 10  HIS A N   1 
ATOM   99   N  N   B HIS A 1 10  ? 21.948  -8.029  -4.029  0.50 25.81  ? 10  HIS A N   1 
ATOM   100  C  CA  A HIS A 1 10  ? 22.764  -6.972  -3.895  0.50 27.96  ? 10  HIS A CA  1 
ATOM   101  C  CA  B HIS A 1 10  ? 22.852  -6.920  -3.927  0.50 25.89  ? 10  HIS A CA  1 
ATOM   102  C  C   A HIS A 1 10  ? 22.197  -5.624  -3.708  0.50 22.21  ? 10  HIS A C   1 
ATOM   103  C  C   B HIS A 1 10  ? 22.208  -5.541  -3.807  0.50 21.75  ? 10  HIS A C   1 
ATOM   104  O  O   A HIS A 1 10  ? 22.952  -4.773  -3.316  0.50 24.14  ? 10  HIS A O   1 
ATOM   105  O  O   B HIS A 1 10  ? 22.938  -4.561  -3.551  0.50 25.78  ? 10  HIS A O   1 
ATOM   106  C  CB  A HIS A 1 10  ? 23.772  -6.962  -5.006  0.50 26.99  ? 10  HIS A CB  1 
ATOM   107  C  CB  B HIS A 1 10  ? 23.906  -6.988  -5.047  0.50 28.70  ? 10  HIS A CB  1 
ATOM   108  C  CG  A HIS A 1 10  ? 24.450  -8.282  -5.157  0.50 16.91  ? 10  HIS A CG  1 
ATOM   109  C  CG  B HIS A 1 10  ? 24.648  -8.324  -5.136  0.50 20.96  ? 10  HIS A CG  1 
ATOM   110  N  ND1 A HIS A 1 10  ? 25.527  -8.700  -4.415  0.50 19.67  ? 10  HIS A ND1 1 
ATOM   111  N  ND1 B HIS A 1 10  ? 25.604  -8.690  -4.255  0.50 23.42  ? 10  HIS A ND1 1 
ATOM   112  C  CD2 A HIS A 1 10  ? 24.102  -9.321  -5.962  0.50 18.95  ? 10  HIS A CD2 1 
ATOM   113  C  CD2 B HIS A 1 10  ? 24.555  -9.367  -6.064  0.50 23.46  ? 10  HIS A CD2 1 
ATOM   114  C  CE1 A HIS A 1 10  ? 25.869  -9.968  -4.787  0.50 21.56  ? 10  HIS A CE1 1 
ATOM   115  C  CE1 B HIS A 1 10  ? 26.086  -9.904  -4.594  0.50 23.01  ? 10  HIS A CE1 1 
ATOM   116  N  NE2 A HIS A 1 10  ? 25.002  -10.350 -5.764  0.50 15.14  ? 10  HIS A NE2 1 
ATOM   117  N  NE2 B HIS A 1 10  ? 25.446  -10.319 -5.698  0.50 22.13  ? 10  HIS A NE2 1 
ATOM   118  N  N   . ASN A 1 11  ? 20.881  -5.395  -3.938  1.00 23.41  ? 11  ASN A N   1 
ATOM   119  C  CA  . ASN A 1 11  ? 20.337  -4.029  -3.774  1.00 19.98  ? 11  ASN A CA  1 
ATOM   120  C  C   . ASN A 1 11  ? 19.003  -4.054  -3.011  1.00 17.33  ? 11  ASN A C   1 
ATOM   121  O  O   . ASN A 1 11  ? 18.360  -3.024  -2.942  1.00 18.24  ? 11  ASN A O   1 
ATOM   122  C  CB  . ASN A 1 11  ? 20.129  -3.281  -5.087  1.00 18.90  ? 11  ASN A CB  1 
ATOM   123  C  CG  . ASN A 1 11  ? 19.068  -3.881  -5.981  1.00 18.82  ? 11  ASN A CG  1 
ATOM   124  O  OD1 . ASN A 1 11  ? 18.496  -4.924  -5.656  1.00 24.41  ? 11  ASN A OD1 1 
ATOM   125  N  ND2 . ASN A 1 11  ? 18.803  -3.272  -7.115  1.00 21.19  ? 11  ASN A ND2 1 
ATOM   126  N  N   . GLY A 1 12  ? 18.695  -5.160  -2.392  1.00 17.78  ? 12  GLY A N   1 
ATOM   127  C  CA  . GLY A 1 12  ? 17.370  -5.310  -1.760  1.00 16.49  ? 12  GLY A CA  1 
ATOM   128  C  C   . GLY A 1 12  ? 17.370  -4.786  -0.346  1.00 14.58  ? 12  GLY A C   1 
ATOM   129  O  O   . GLY A 1 12  ? 18.288  -4.096  0.131   1.00 15.48  ? 12  GLY A O   1 
ATOM   130  N  N   . PRO A 1 13  ? 16.297  -5.086  0.384   1.00 13.69  ? 13  PRO A N   1 
ATOM   131  C  CA  . PRO A 1 13  ? 16.047  -4.494  1.702   1.00 13.91  ? 13  PRO A CA  1 
ATOM   132  C  C   . PRO A 1 13  ? 17.182  -4.524  2.680   1.00 13.38  ? 13  PRO A C   1 
ATOM   133  O  O   . PRO A 1 13  ? 17.323  -3.570  3.469   1.00 13.80  ? 13  PRO A O   1 
ATOM   134  C  CB  . PRO A 1 13  ? 14.840  -5.301  2.193   1.00 13.86  ? 13  PRO A CB  1 
ATOM   135  C  CG  . PRO A 1 13  ? 14.034  -5.568  0.965   1.00 13.66  ? 13  PRO A CG  1 
ATOM   136  C  CD  . PRO A 1 13  ? 15.110  -5.832  -0.080  1.00 14.79  ? 13  PRO A CD  1 
ATOM   137  N  N   . GLU A 1 14  ? 18.027  -5.523  2.641   1.00 14.96  ? 14  GLU A N   1 
ATOM   138  C  CA  . GLU A 1 14  ? 19.114  -5.597  3.591   1.00 16.35  ? 14  GLU A CA  1 
ATOM   139  C  C   . GLU A 1 14  ? 20.221  -4.625  3.315   1.00 14.70  ? 14  GLU A C   1 
ATOM   140  O  O   . GLU A 1 14  ? 21.099  -4.399  4.167   1.00 16.83  ? 14  GLU A O   1 
ATOM   141  C  CB  . GLU A 1 14  ? 19.591  -7.088  3.557   1.00 21.04  ? 14  GLU A CB  1 
ATOM   142  C  CG  . GLU A 1 14  ? 20.212  -7.626  2.228   1.00 23.10  ? 14  GLU A CG  1 
ATOM   143  C  CD  . GLU A 1 14  ? 19.230  -8.212  1.191   1.00 26.17  ? 14  GLU A CD  1 
ATOM   144  O  OE1 . GLU A 1 14  ? 18.076  -7.763  1.028   1.00 22.60  ? 14  GLU A OE1 1 
ATOM   145  O  OE2 . GLU A 1 14  ? 19.660  -9.109  0.441   1.00 66.27  ? 14  GLU A OE2 1 
ATOM   146  N  N   . HIS A 1 15  ? 20.214  -4.029  2.121   1.00 14.07  ? 15  HIS A N   1 
ATOM   147  C  CA  . HIS A 1 15  ? 21.249  -3.043  1.747   1.00 14.27  ? 15  HIS A CA  1 
ATOM   148  C  C   . HIS A 1 15  ? 20.758  -1.605  1.903   1.00 13.95  ? 15  HIS A C   1 
ATOM   149  O  O   . HIS A 1 15  ? 21.586  -0.670  1.853   1.00 15.71  ? 15  HIS A O   1 
ATOM   150  C  CB  . HIS A 1 15  ? 21.574  -3.239  0.264   1.00 16.83  ? 15  HIS A CB  1 
ATOM   151  C  CG  . HIS A 1 15  ? 22.300  -4.504  0.005   1.00 16.62  ? 15  HIS A CG  1 
ATOM   152  N  ND1 . HIS A 1 15  ? 23.676  -4.610  0.121   1.00 19.01  ? 15  HIS A ND1 1 
ATOM   153  C  CD2 . HIS A 1 15  ? 21.820  -5.752  -0.359  1.00 17.64  ? 15  HIS A CD2 1 
ATOM   154  C  CE1 . HIS A 1 15  ? 23.989  -5.879  -0.118  1.00 22.70  ? 15  HIS A CE1 1 
ATOM   155  N  NE2 . HIS A 1 15  ? 22.884  -6.572  -0.422  1.00 23.99  ? 15  HIS A NE2 1 
ATOM   156  N  N   . TRP A 1 16  ? 19.435  -1.396  2.044   1.00 12.57  ? 16  TRP A N   1 
ATOM   157  C  CA  . TRP A 1 16  ? 18.897  -0.046  1.970   1.00 11.83  ? 16  TRP A CA  1 
ATOM   158  C  C   . TRP A 1 16  ? 19.457  0.920   2.981   1.00 11.80  ? 16  TRP A C   1 
ATOM   159  O  O   . TRP A 1 16  ? 19.574  2.140   2.732   1.00 13.30  ? 16  TRP A O   1 
ATOM   160  C  CB  . TRP A 1 16  ? 17.361  -0.057  2.094   1.00 12.10  ? 16  TRP A CB  1 
ATOM   161  C  CG  . TRP A 1 16  ? 16.689  -0.755  0.959   1.00 10.40  ? 16  TRP A CG  1 
ATOM   162  C  CD1 . TRP A 1 16  ? 17.220  -1.199  -0.247  1.00 12.39  ? 16  TRP A CD1 1 
ATOM   163  C  CD2 . TRP A 1 16  ? 15.280  -1.067  0.906   1.00 10.46  ? 16  TRP A CD2 1 
ATOM   164  N  NE1 . TRP A 1 16  ? 16.237  -1.782  -1.005  1.00 12.35  ? 16  TRP A NE1 1 
ATOM   165  C  CE2 . TRP A 1 16  ? 15.032  -1.701  -0.367  1.00 10.68  ? 16  TRP A CE2 1 
ATOM   166  C  CE3 . TRP A 1 16  ? 14.208  -0.895  1.792   1.00 10.46  ? 16  TRP A CE3 1 
ATOM   167  C  CZ2 . TRP A 1 16  ? 13.742  -2.147  -0.740  1.00 10.81  ? 16  TRP A CZ2 1 
ATOM   168  C  CZ3 . TRP A 1 16  ? 12.961  -1.330  1.420   1.00 10.80  ? 16  TRP A CZ3 1 
ATOM   169  C  CH2 . TRP A 1 16  ? 12.724  -1.933  0.178   1.00 10.53  ? 16  TRP A CH2 1 
ATOM   170  N  N   . HIS A 1 17  ? 19.852  0.399   4.122   1.00 12.49  ? 17  HIS A N   1 
ATOM   171  C  CA  . HIS A 1 17  ? 20.329  1.247   5.164   1.00 12.44  ? 17  HIS A CA  1 
ATOM   172  C  C   . HIS A 1 17  ? 21.600  2.019   4.839   1.00 14.10  ? 17  HIS A C   1 
ATOM   173  O  O   . HIS A 1 17  ? 21.870  3.095   5.461   1.00 14.75  ? 17  HIS A O   1 
ATOM   174  C  CB  . HIS A 1 17  ? 20.662  0.506   6.520   1.00 13.83  ? 17  HIS A CB  1 
ATOM   175  C  CG  . HIS A 1 17  ? 21.888  -0.377  6.444   1.00 15.32  ? 17  HIS A CG  1 
ATOM   176  N  ND1 . HIS A 1 17  ? 23.072  0.037   6.908   1.00 17.21  ? 17  HIS A ND1 1 
ATOM   177  C  CD2 . HIS A 1 17  ? 22.067  -1.578  5.846   1.00 17.05  ? 17  HIS A CD2 1 
ATOM   178  C  CE1 . HIS A 1 17  ? 23.945  -0.859  6.652   1.00 17.83  ? 17  HIS A CE1 1 
ATOM   179  N  NE2 . HIS A 1 17  ? 23.403  -1.875  6.015   1.00 16.24  ? 17  HIS A NE2 1 
ATOM   180  N  N   . LYS A 1 18  ? 22.371  1.571   3.843   1.00 14.95  ? 18  LYS A N   1 
ATOM   181  C  CA  . LYS A 1 18  ? 23.606  2.285   3.480   1.00 15.88  ? 18  LYS A CA  1 
ATOM   182  C  C   . LYS A 1 18  ? 23.310  3.643   2.814   1.00 16.04  ? 18  LYS A C   1 
ATOM   183  O  O   . LYS A 1 18  ? 23.981  4.583   3.080   1.00 22.41  ? 18  LYS A O   1 
ATOM   184  C  CB  . LYS A 1 18  ? 24.428  1.422   2.565   1.00 17.82  ? 18  LYS A CB  1 
ATOM   185  C  CG  . LYS A 1 18  ? 25.054  0.227   3.300   1.00 19.47  ? 18  LYS A CG  1 
ATOM   186  C  CD  . LYS A 1 18  ? 25.772  -0.752  2.378   1.00 18.07  ? 18  LYS A CD  1 
ATOM   187  C  CE  . LYS A 1 18  ? 24.828  -1.742  1.716   1.00 17.59  ? 18  LYS A CE  1 
ATOM   188  N  NZ  . LYS A 1 18  ? 25.451  -2.566  0.643   1.00 18.25  ? 18  LYS A NZ  1 
ATOM   189  N  N   . ASP A 1 19  ? 22.273  3.684   1.971   1.00 15.25  ? 19  ASP A N   1 
ATOM   190  C  CA  . ASP A 1 19  ? 21.838  4.953   1.355   1.00 15.79  ? 19  ASP A CA  1 
ATOM   191  C  C   . ASP A 1 19  ? 20.795  5.695   2.216   1.00 14.93  ? 19  ASP A C   1 
ATOM   192  O  O   . ASP A 1 19  ? 20.714  6.888   2.126   1.00 17.26  ? 19  ASP A O   1 
ATOM   193  C  CB  . ASP A 1 19  ? 21.328  4.697   -0.065  1.00 19.40  ? 19  ASP A CB  1 
ATOM   194  C  CG  . ASP A 1 19  ? 22.396  4.848   -1.150  1.00 23.99  ? 19  ASP A CG  1 
ATOM   195  O  OD1 . ASP A 1 19  ? 23.499  5.310   -0.854  1.00 28.12  ? 19  ASP A OD1 1 
ATOM   196  O  OD2 . ASP A 1 19  ? 22.093  4.449   -2.314  1.00 38.80  ? 19  ASP A OD2 1 
ATOM   197  N  N   . PHE A 1 20  ? 20.068  4.957   3.035   1.00 14.22  ? 20  PHE A N   1 
ATOM   198  C  CA  . PHE A 1 20  ? 18.949  5.464   3.782   1.00 14.81  ? 20  PHE A CA  1 
ATOM   199  C  C   . PHE A 1 20  ? 19.028  4.962   5.231   1.00 13.67  ? 20  PHE A C   1 
ATOM   200  O  O   . PHE A 1 20  ? 18.402  3.996   5.589   1.00 13.05  ? 20  PHE A O   1 
ATOM   201  C  CB  . PHE A 1 20  ? 17.588  5.025   3.139   1.00 14.07  ? 20  PHE A CB  1 
ATOM   202  C  CG  . PHE A 1 20  ? 17.511  5.406   1.693   1.00 14.68  ? 20  PHE A CG  1 
ATOM   203  C  CD1 . PHE A 1 20  ? 17.154  6.714   1.381   1.00 17.60  ? 20  PHE A CD1 1 
ATOM   204  C  CD2 . PHE A 1 20  ? 17.885  4.527   0.661   1.00 16.83  ? 20  PHE A CD2 1 
ATOM   205  C  CE1 . PHE A 1 20  ? 17.135  7.121   0.064   1.00 19.67  ? 20  PHE A CE1 1 
ATOM   206  C  CE2 . PHE A 1 20  ? 17.880  4.901   -0.653  1.00 19.65  ? 20  PHE A CE2 1 
ATOM   207  C  CZ  . PHE A 1 20  ? 17.498  6.213   -0.948  1.00 19.52  ? 20  PHE A CZ  1 
ATOM   208  N  N   . PRO A 1 21  ? 19.908  5.587   6.043   1.00 14.87  ? 21  PRO A N   1 
ATOM   209  C  CA  . PRO A 1 21  ? 20.144  5.073   7.357   1.00 14.05  ? 21  PRO A CA  1 
ATOM   210  C  C   . PRO A 1 21  ? 18.929  4.999   8.295   1.00 14.30  ? 21  PRO A C   1 
ATOM   211  O  O   . PRO A 1 21  ? 18.961  4.209   9.238   1.00 14.30  ? 21  PRO A O   1 
ATOM   212  C  CB  . PRO A 1 21  ? 21.212  5.991   7.973   1.00 19.72  ? 21  PRO A CB  1 
ATOM   213  C  CG  . PRO A 1 21  ? 21.469  7.065   6.983   1.00 26.56  ? 21  PRO A CG  1 
ATOM   214  C  CD  . PRO A 1 21  ? 20.904  6.607   5.673   1.00 17.22  ? 21  PRO A CD  1 
ATOM   215  N  N   A ILE A 1 22  ? 17.846  5.729   8.005   0.50 12.52  ? 22  ILE A N   1 
ATOM   216  N  N   B ILE A 1 22  ? 17.881  5.752   8.006   0.50 13.03  ? 22  ILE A N   1 
ATOM   217  C  CA  A ILE A 1 22  ? 16.601  5.632   8.766   0.50 12.80  ? 22  ILE A CA  1 
ATOM   218  C  CA  B ILE A 1 22  ? 16.667  5.650   8.766   0.50 12.94  ? 22  ILE A CA  1 
ATOM   219  C  C   A ILE A 1 22  ? 16.025  4.207   8.632   0.50 10.89  ? 22  ILE A C   1 
ATOM   220  C  C   B ILE A 1 22  ? 16.082  4.213   8.645   0.50 11.44  ? 22  ILE A C   1 
ATOM   221  O  O   A ILE A 1 22  ? 15.109  3.864   9.377   0.50 11.68  ? 22  ILE A O   1 
ATOM   222  O  O   B ILE A 1 22  ? 15.197  3.872   9.398   0.50 12.02  ? 22  ILE A O   1 
ATOM   223  C  CB  A ILE A 1 22  ? 15.592  6.695   8.307   0.50 12.16  ? 22  ILE A CB  1 
ATOM   224  C  CB  B ILE A 1 22  ? 15.671  6.707   8.290   0.50 13.00  ? 22  ILE A CB  1 
ATOM   225  C  CG1 A ILE A 1 22  ? 14.569  7.052   9.361   0.50 12.88  ? 22  ILE A CG1 1 
ATOM   226  C  CG1 B ILE A 1 22  ? 14.513  6.883   9.248   0.50 15.44  ? 22  ILE A CG1 1 
ATOM   227  C  CG2 A ILE A 1 22  ? 14.925  6.310   7.001   0.50 12.19  ? 22  ILE A CG2 1 
ATOM   228  C  CG2 B ILE A 1 22  ? 15.178  6.388   6.895   0.50 13.43  ? 22  ILE A CG2 1 
ATOM   229  C  CD1 A ILE A 1 22  ? 13.726  8.205   8.927   0.50 12.51  ? 22  ILE A CD1 1 
ATOM   230  C  CD1 B ILE A 1 22  ? 15.005  7.465   10.538  0.50 18.77  ? 22  ILE A CD1 1 
ATOM   231  N  N   . ALA A 1 23  ? 16.565  3.392   7.719   1.00 11.24  ? 23  ALA A N   1 
ATOM   232  C  CA  . ALA A 1 23  ? 16.110  2.002   7.605   1.00 11.36  ? 23  ALA A CA  1 
ATOM   233  C  C   . ALA A 1 23  ? 16.193  1.302   8.926   1.00 11.46  ? 23  ALA A C   1 
ATOM   234  O  O   . ALA A 1 23  ? 15.505  0.282   9.116   1.00 11.44  ? 23  ALA A O   1 
ATOM   235  C  CB  . ALA A 1 23  ? 16.897  1.201   6.594   1.00 12.66  ? 23  ALA A CB  1 
ATOM   236  N  N   . LYS A 1 24  ? 17.147  1.714   9.792   1.00 12.14  ? 24  LYS A N   1 
ATOM   237  C  CA  . LYS A 1 24  ? 17.313  1.079   11.099  1.00 13.37  ? 24  LYS A CA  1 
ATOM   238  C  C   . LYS A 1 24  ? 16.714  1.990   12.189  1.00 14.53  ? 24  LYS A C   1 
ATOM   239  O  O   . LYS A 1 24  ? 17.055  1.838   13.372  1.00 17.11  ? 24  LYS A O   1 
ATOM   240  C  CB  . LYS A 1 24  ? 18.800  0.790   11.433  1.00 14.71  ? 24  LYS A CB  1 
ATOM   241  C  CG  . LYS A 1 24  ? 19.445  -0.102  10.432  1.00 17.03  ? 24  LYS A CG  1 
ATOM   242  C  CD  . LYS A 1 24  ? 20.918  -0.296  10.827  1.00 23.33  ? 24  LYS A CD  1 
ATOM   243  C  CE  . LYS A 1 24  ? 21.578  -1.274  9.881   1.00 23.27  ? 24  LYS A CE  1 
ATOM   244  N  NZ  . LYS A 1 24  ? 21.290  -2.692  10.207  1.00 31.60  ? 24  LYS A NZ  1 
ATOM   245  N  N   . GLY A 1 25  ? 15.693  2.766   11.848  1.00 13.91  ? 25  GLY A N   1 
ATOM   246  C  CA  . GLY A 1 25  ? 15.115  3.770   12.794  1.00 14.69  ? 25  GLY A CA  1 
ATOM   247  C  C   . GLY A 1 25  ? 14.117  3.115   13.757  1.00 13.18  ? 25  GLY A C   1 
ATOM   248  O  O   . GLY A 1 25  ? 13.953  1.875   13.849  1.00 14.21  ? 25  GLY A O   1 
ATOM   249  N  N   . GLU A 1 26  ? 13.487  3.996   14.512  1.00 13.95  ? 26  GLU A N   1 
ATOM   250  C  CA  . GLU A 1 26  ? 12.616  3.610   15.572  1.00 14.71  ? 26  GLU A CA  1 
ATOM   251  C  C   . GLU A 1 26  ? 11.176  3.353   15.197  1.00 11.76  ? 26  GLU A C   1 
ATOM   252  O  O   . GLU A 1 26  ? 10.425  2.847   16.057  1.00 13.62  ? 26  GLU A O   1 
ATOM   253  C  CB  . GLU A 1 26  ? 12.632  4.714   16.708  1.00 18.09  ? 26  GLU A CB  1 
ATOM   254  C  CG  . GLU A 1 26  ? 14.061  4.890   17.295  1.00 20.22  ? 26  GLU A CG  1 
ATOM   255  C  CD  . GLU A 1 26  ? 14.588  3.615   18.003  1.00 26.80  ? 26  GLU A CD  1 
ATOM   256  O  OE1 . GLU A 1 26  ? 13.850  2.995   18.847  1.00 34.99  ? 26  GLU A OE1 1 
ATOM   257  O  OE2 . GLU A 1 26  ? 15.724  3.199   17.688  1.00 32.19  ? 26  GLU A OE2 1 
ATOM   258  N  N   . ARG A 1 27  ? 10.763  3.683   13.984  1.00 9.78   ? 27  ARG A N   1 
ATOM   259  C  CA  . ARG A 1 27  ? 9.364   3.458   13.620  1.00 9.10   ? 27  ARG A CA  1 
ATOM   260  C  C   . ARG A 1 27  ? 9.281   3.040   12.148  1.00 8.42   ? 27  ARG A C   1 
ATOM   261  O  O   . ARG A 1 27  ? 8.608   3.666   11.323  1.00 8.80   ? 27  ARG A O   1 
ATOM   262  C  CB  . ARG A 1 27  ? 8.527   4.695   13.941  1.00 12.28  ? 27  ARG A CB  1 
ATOM   263  C  CG  . ARG A 1 27  ? 8.792   5.996   13.305  1.00 16.65  ? 27  ARG A CG  1 
ATOM   264  C  CD  . ARG A 1 27  ? 7.750   7.084   13.575  1.00 21.13  ? 27  ARG A CD  1 
ATOM   265  N  NE  . ARG A 1 27  ? 6.627   7.043   12.643  1.00 15.07  ? 27  ARG A NE  1 
ATOM   266  C  CZ  . ARG A 1 27  ? 5.702   7.993   12.554  1.00 13.36  ? 27  ARG A CZ  1 
ATOM   267  N  NH1 . ARG A 1 27  ? 5.770   9.059   13.340  1.00 16.36  ? 27  ARG A NH1 1 
ATOM   268  N  NH2 . ARG A 1 27  ? 4.710   7.880   11.681  1.00 13.40  ? 27  ARG A NH2 1 
ATOM   269  N  N   . GLN A 1 28  ? 10.006  1.942   11.865  1.00 8.07   ? 28  GLN A N   1 
ATOM   270  C  CA  . GLN A 1 28  ? 10.034  1.394   10.501  1.00 7.59   ? 28  GLN A CA  1 
ATOM   271  C  C   . GLN A 1 28  ? 8.856   0.445   10.239  1.00 7.42   ? 28  GLN A C   1 
ATOM   272  O  O   . GLN A 1 28  ? 8.376   -0.246  11.134  1.00 8.48   ? 28  GLN A O   1 
ATOM   273  C  CB  . GLN A 1 28  ? 11.382  0.724   10.228  1.00 8.81   ? 28  GLN A CB  1 
ATOM   274  C  CG  . GLN A 1 28  ? 12.490  1.779   10.115  1.00 9.60   ? 28  GLN A CG  1 
ATOM   275  C  CD  . GLN A 1 28  ? 12.373  2.574   8.831   1.00 8.08   ? 28  GLN A CD  1 
ATOM   276  O  OE1 . GLN A 1 28  ? 12.548  2.048   7.743   1.00 8.73   ? 28  GLN A OE1 1 
ATOM   277  N  NE2 . GLN A 1 28  ? 12.060  3.865   8.964   1.00 9.02   ? 28  GLN A NE2 1 
ATOM   278  N  N   . SER A 1 29  ? 8.489   0.374   8.960   1.00 7.06   ? 29  SER A N   1 
ATOM   279  C  CA  . SER A 1 29  ? 7.435   -0.514  8.488   1.00 6.79   ? 29  SER A CA  1 
ATOM   280  C  C   . SER A 1 29  ? 7.943   -1.376  7.366   1.00 6.17   ? 29  SER A C   1 
ATOM   281  O  O   . SER A 1 29  ? 8.894   -1.029  6.671   1.00 7.18   ? 29  SER A O   1 
ATOM   282  C  CB  . SER A 1 29  ? 6.280   0.357   7.965   1.00 6.96   ? 29  SER A CB  1 
ATOM   283  O  OG  . SER A 1 29  ? 5.679   1.066   9.047   1.00 6.84   ? 29  SER A OG  1 
ATOM   284  N  N   . PRO A 1 30  ? 7.297   -2.536  7.120   1.00 6.49   ? 30  PRO A N   1 
ATOM   285  C  CA  . PRO A 1 30  ? 6.113   -3.064  7.853   1.00 6.73   ? 30  PRO A CA  1 
ATOM   286  C  C   . PRO A 1 30  ? 6.556   -3.738  9.160   1.00 6.20   ? 30  PRO A C   1 
ATOM   287  O  O   . PRO A 1 30  ? 7.748   -3.763  9.470   1.00 7.41   ? 30  PRO A O   1 
ATOM   288  C  CB  . PRO A 1 30  ? 5.600   -4.120  6.858   1.00 6.82   ? 30  PRO A CB  1 
ATOM   289  C  CG  . PRO A 1 30  ? 6.869   -4.680  6.222   1.00 7.36   ? 30  PRO A CG  1 
ATOM   290  C  CD  . PRO A 1 30  ? 7.736   -3.436  6.062   1.00 7.27   ? 30  PRO A CD  1 
ATOM   291  N  N   . VAL A 1 31  ? 5.562   -4.275  9.837   1.00 7.05   ? 31  VAL A N   1 
ATOM   292  C  CA  . VAL A 1 31  ? 5.727   -5.032  11.086  1.00 7.29   ? 31  VAL A CA  1 
ATOM   293  C  C   . VAL A 1 31  ? 4.885   -6.258  11.034  1.00 7.35   ? 31  VAL A C   1 
ATOM   294  O  O   . VAL A 1 31  ? 3.882   -6.316  10.284  1.00 8.24   ? 31  VAL A O   1 
ATOM   295  C  CB  . VAL A 1 31  ? 5.431   -4.182  12.324  1.00 8.40   ? 31  VAL A CB  1 
ATOM   296  C  CG1 . VAL A 1 31  ? 6.363   -2.996  12.437  1.00 9.20   ? 31  VAL A CG1 1 
ATOM   297  C  CG2 . VAL A 1 31  ? 3.934   -3.780  12.399  1.00 9.10   ? 31  VAL A CG2 1 
ATOM   298  N  N   . ASP A 1 32  ? 5.191   -7.242  11.888  1.00 7.41   ? 32  ASP A N   1 
ATOM   299  C  CA  . ASP A 1 32  ? 4.304   -8.320  12.180  1.00 7.65   ? 32  ASP A CA  1 
ATOM   300  C  C   . ASP A 1 32  ? 3.242   -7.803  13.158  1.00 8.09   ? 32  ASP A C   1 
ATOM   301  O  O   . ASP A 1 32  ? 3.545   -7.154  14.162  1.00 10.35  ? 32  ASP A O   1 
ATOM   302  C  CB  . ASP A 1 32  ? 5.046   -9.482  12.776  1.00 9.73   ? 32  ASP A CB  1 
ATOM   303  C  CG  . ASP A 1 32  ? 4.119   -10.632 13.061  1.00 9.20   ? 32  ASP A CG  1 
ATOM   304  O  OD1 . ASP A 1 32  ? 3.409   -11.116 12.148  1.00 9.34   ? 32  ASP A OD1 1 
ATOM   305  O  OD2 . ASP A 1 32  ? 4.077   -11.100 14.248  1.00 12.44  ? 32  ASP A OD2 1 
ATOM   306  N  N   . ILE A 1 33  ? 1.971   -8.101  12.877  1.00 8.17   ? 33  ILE A N   1 
ATOM   307  C  CA  . ILE A 1 33  ? 0.832   -7.732  13.747  1.00 8.45   ? 33  ILE A CA  1 
ATOM   308  C  C   . ILE A 1 33  ? 0.551   -8.967  14.606  1.00 8.78   ? 33  ILE A C   1 
ATOM   309  O  O   . ILE A 1 33  ? 0.031   -9.966  14.125  1.00 9.55   ? 33  ILE A O   1 
ATOM   310  C  CB  . ILE A 1 33  ? -0.373  -7.306  12.936  1.00 8.62   ? 33  ILE A CB  1 
ATOM   311  C  CG1 . ILE A 1 33  ? 0.019   -6.088  12.090  1.00 9.10   ? 33  ILE A CG1 1 
ATOM   312  C  CG2 . ILE A 1 33  ? -1.560  -7.055  13.868  1.00 11.14  ? 33  ILE A CG2 1 
ATOM   313  C  CD1 . ILE A 1 33  ? -1.022  -5.804  10.960  1.00 9.67   ? 33  ILE A CD1 1 
ATOM   314  N  N   A ASP A 1 34  ? 0.943   -8.894  15.869  0.50 10.53  ? 34  ASP A N   1 
ATOM   315  N  N   B ASP A 1 34  ? 0.979   -8.919  15.867  0.50 10.36  ? 34  ASP A N   1 
ATOM   316  C  CA  A ASP A 1 34  ? 0.656   -9.946  16.803  0.50 12.34  ? 34  ASP A CA  1 
ATOM   317  C  CA  B ASP A 1 34  ? 0.704   -9.959  16.840  0.50 11.83  ? 34  ASP A CA  1 
ATOM   318  C  C   A ASP A 1 34  ? -0.752  -9.682  17.334  0.50 12.76  ? 34  ASP A C   1 
ATOM   319  C  C   B ASP A 1 34  ? -0.728  -9.694  17.339  0.50 12.39  ? 34  ASP A C   1 
ATOM   320  O  O   A ASP A 1 34  ? -1.010  -8.722  18.097  0.50 14.29  ? 34  ASP A O   1 
ATOM   321  O  O   B ASP A 1 34  ? -0.973  -8.746  18.119  0.50 15.50  ? 34  ASP A O   1 
ATOM   322  C  CB  A ASP A 1 34  ? 1.719   -10.060 17.896  0.50 14.16  ? 34  ASP A CB  1 
ATOM   323  C  CB  B ASP A 1 34  ? 1.768   -9.917  17.954  0.50 13.74  ? 34  ASP A CB  1 
ATOM   324  C  CG  A ASP A 1 34  ? 1.492   -11.284 18.719  0.50 18.00  ? 34  ASP A CG  1 
ATOM   325  C  CG  B ASP A 1 34  ? 1.492   -10.934 19.029  0.50 16.34  ? 34  ASP A CG  1 
ATOM   326  O  OD1 A ASP A 1 34  ? 0.725   -11.199 19.685  0.50 18.14  ? 34  ASP A OD1 1 
ATOM   327  O  OD1 B ASP A 1 34  ? 0.328   -11.409 19.117  0.50 18.87  ? 34  ASP A OD1 1 
ATOM   328  O  OD2 A ASP A 1 34  ? 1.932   -12.372 18.306  0.50 21.22  ? 34  ASP A OD2 1 
ATOM   329  O  OD2 B ASP A 1 34  ? 2.432   -11.260 19.767  0.50 19.84  ? 34  ASP A OD2 1 
ATOM   330  N  N   . THR A 1 35  ? -1.698  -10.473 16.861  1.00 13.48  ? 35  THR A N   1 
ATOM   331  C  CA  . THR A 1 35  ? -3.128  -10.170 17.109  1.00 14.82  ? 35  THR A CA  1 
ATOM   332  C  C   . THR A 1 35  ? -3.513  -10.314 18.511  1.00 13.18  ? 35  THR A C   1 
ATOM   333  O  O   . THR A 1 35  ? -4.449  -9.619  18.964  1.00 17.19  ? 35  THR A O   1 
ATOM   334  C  CB  . THR A 1 35  ? -4.011  -11.023 16.248  1.00 14.79  ? 35  THR A CB  1 
ATOM   335  O  OG1 . THR A 1 35  ? -3.890  -12.379 16.732  1.00 15.67  ? 35  THR A OG1 1 
ATOM   336  C  CG2 . THR A 1 35  ? -3.717  -10.935 14.805  1.00 17.83  ? 35  THR A CG2 1 
ATOM   337  N  N   . HIS A 1 36  ? -2.812  -11.126 19.289  1.00 15.38  ? 36  HIS A N   1 
ATOM   338  C  CA  . HIS A 1 36  ? -3.066  -11.287 20.710  1.00 17.34  ? 36  HIS A CA  1 
ATOM   339  C  C   . HIS A 1 36  ? -2.598  -10.176 21.541  1.00 19.74  ? 36  HIS A C   1 
ATOM   340  O  O   . HIS A 1 36  ? -3.336  -9.837  22.522  1.00 22.23  ? 36  HIS A O   1 
ATOM   341  C  CB  . HIS A 1 36  ? -2.595  -12.670 21.115  1.00 21.11  ? 36  HIS A CB  1 
ATOM   342  C  CG  . HIS A 1 36  ? -3.553  -13.745 20.610  1.00 22.03  ? 36  HIS A CG  1 
ATOM   343  N  ND1 . HIS A 1 36  ? -3.241  -14.664 19.611  1.00 29.18  ? 36  HIS A ND1 1 
ATOM   344  C  CD2 . HIS A 1 36  ? -4.900  -13.972 20.980  1.00 24.35  ? 36  HIS A CD2 1 
ATOM   345  C  CE1 . HIS A 1 36  ? -4.341  -15.438 19.388  1.00 33.41  ? 36  HIS A CE1 1 
ATOM   346  N  NE2 . HIS A 1 36  ? -5.361  -15.019 20.223  1.00 30.94  ? 36  HIS A NE2 1 
ATOM   347  N  N   . THR A 1 37  ? -1.487  -9.498  21.142  1.00 18.47  ? 37  THR A N   1 
ATOM   348  C  CA  . THR A 1 37  ? -1.000  -8.355  21.897  1.00 19.18  ? 37  THR A CA  1 
ATOM   349  C  C   . THR A 1 37  ? -1.461  -6.980  21.407  1.00 16.24  ? 37  THR A C   1 
ATOM   350  O  O   . THR A 1 37  ? -1.365  -6.012  22.183  1.00 20.18  ? 37  THR A O   1 
ATOM   351  C  CB  . THR A 1 37  ? 0.483   -8.274  22.158  1.00 27.44  ? 37  THR A CB  1 
ATOM   352  O  OG1 . THR A 1 37  ? 1.174   -8.293  20.985  1.00 28.53  ? 37  THR A OG1 1 
ATOM   353  C  CG2 . THR A 1 37  ? 0.909   -9.522  22.765  1.00 27.80  ? 37  THR A CG2 1 
ATOM   354  N  N   . ALA A 1 38  ? -2.129  -6.918  20.256  1.00 14.99  ? 38  ALA A N   1 
ATOM   355  C  CA  . ALA A 1 38  ? -2.710  -5.669  19.810  1.00 14.98  ? 38  ALA A CA  1 
ATOM   356  C  C   . ALA A 1 38  ? -3.833  -5.328  20.761  1.00 17.75  ? 38  ALA A C   1 
ATOM   357  O  O   . ALA A 1 38  ? -4.579  -6.184  21.138  1.00 24.63  ? 38  ALA A O   1 
ATOM   358  C  CB  . ALA A 1 38  ? -3.227  -5.824  18.414  1.00 14.78  ? 38  ALA A CB  1 
ATOM   359  N  N   . LYS A 1 39  ? -3.886  -4.105  21.193  1.00 16.92  ? 39  LYS A N   1 
ATOM   360  C  CA  . LYS A 1 39  ? -4.874  -3.660  22.180  1.00 21.08  ? 39  LYS A CA  1 
ATOM   361  C  C   . LYS A 1 39  ? -6.154  -3.134  21.528  1.00 16.17  ? 39  LYS A C   1 
ATOM   362  O  O   . LYS A 1 39  ? -6.071  -2.159  20.790  1.00 14.99  ? 39  LYS A O   1 
ATOM   363  C  CB  . LYS A 1 39  ? -4.159  -2.517  22.945  1.00 26.51  ? 39  LYS A CB  1 
ATOM   364  C  CG  . LYS A 1 39  ? -4.914  -1.630  23.895  1.00 28.29  ? 39  LYS A CG  1 
ATOM   365  C  CD  . LYS A 1 39  ? -5.080  -2.352  25.229  1.00 32.00  ? 39  LYS A CD  1 
ATOM   366  C  CE  . LYS A 1 39  ? -5.780  -1.481  26.214  1.00 28.93  ? 39  LYS A CE  1 
ATOM   367  N  NZ  . LYS A 1 39  ? -6.199  -2.457  27.238  1.00 31.42  ? 39  LYS A NZ  1 
ATOM   368  N  N   . TYR A 1 40  ? -7.326  -3.673  21.885  1.00 18.18  ? 40  TYR A N   1 
ATOM   369  C  CA  . TYR A 1 40  ? -8.574  -3.048  21.465  1.00 15.89  ? 40  TYR A CA  1 
ATOM   370  C  C   . TYR A 1 40  ? -8.654  -1.663  22.092  1.00 14.44  ? 40  TYR A C   1 
ATOM   371  O  O   . TYR A 1 40  ? -8.482  -1.507  23.331  1.00 17.50  ? 40  TYR A O   1 
ATOM   372  C  CB  . TYR A 1 40  ? -9.818  -3.876  21.839  1.00 20.71  ? 40  TYR A CB  1 
ATOM   373  C  CG  . TYR A 1 40  ? -11.100 -3.122  21.703  1.00 23.41  ? 40  TYR A CG  1 
ATOM   374  C  CD1 . TYR A 1 40  ? -11.538 -2.619  20.459  1.00 21.04  ? 40  TYR A CD1 1 
ATOM   375  C  CD2 . TYR A 1 40  ? -11.892 -2.894  22.787  1.00 27.96  ? 40  TYR A CD2 1 
ATOM   376  C  CE1 . TYR A 1 40  ? -12.732 -1.905  20.337  1.00 25.72  ? 40  TYR A CE1 1 
ATOM   377  C  CE2 . TYR A 1 40  ? -13.089 -2.200  22.636  1.00 28.25  ? 40  TYR A CE2 1 
ATOM   378  C  CZ  . TYR A 1 40  ? -13.516 -1.706  21.424  1.00 27.64  ? 40  TYR A CZ  1 
ATOM   379  O  OH  . TYR A 1 40  ? -14.714 -1.004  21.276  1.00 36.47  ? 40  TYR A OH  1 
ATOM   380  N  N   . ASP A 1 41  ? -8.898  -0.650  21.266  1.00 13.70  ? 41  ASP A N   1 
ATOM   381  C  CA  . ASP A 1 41  ? -8.969  0.726   21.773  1.00 13.60  ? 41  ASP A CA  1 
ATOM   382  C  C   . ASP A 1 41  ? -10.380 1.247   21.499  1.00 15.86  ? 41  ASP A C   1 
ATOM   383  O  O   . ASP A 1 41  ? -10.733 1.605   20.333  1.00 16.24  ? 41  ASP A O   1 
ATOM   384  C  CB  . ASP A 1 41  ? -7.915  1.612   21.077  1.00 16.48  ? 41  ASP A CB  1 
ATOM   385  C  CG  . ASP A 1 41  ? -7.905  3.024   21.587  1.00 19.05  ? 41  ASP A CG  1 
ATOM   386  O  OD1 . ASP A 1 41  ? -8.845  3.427   22.360  1.00 20.34  ? 41  ASP A OD1 1 
ATOM   387  O  OD2 . ASP A 1 41  ? -6.930  3.733   21.203  1.00 22.06  ? 41  ASP A OD2 1 
ATOM   388  N  N   . PRO A 1 42  ? -11.205 1.298   22.544  1.00 20.21  ? 42  PRO A N   1 
ATOM   389  C  CA  . PRO A 1 42  ? -12.580 1.804   22.325  1.00 23.88  ? 42  PRO A CA  1 
ATOM   390  C  C   . PRO A 1 42  ? -12.697 3.315   21.893  1.00 23.17  ? 42  PRO A C   1 
ATOM   391  O  O   . PRO A 1 42  ? -13.765 3.799   21.462  1.00 31.87  ? 42  PRO A O   1 
ATOM   392  C  CB  . PRO A 1 42  ? -13.268 1.534   23.667  1.00 33.70  ? 42  PRO A CB  1 
ATOM   393  C  CG  . PRO A 1 42  ? -12.146 1.567   24.639  1.00 27.12  ? 42  PRO A CG  1 
ATOM   394  C  CD  . PRO A 1 42  ? -11.013 0.883   23.948  1.00 20.09  ? 42  PRO A CD  1 
ATOM   395  N  N   . SER A 1 43  ? -11.588 4.043   22.032  1.00 21.92  ? 43  SER A N   1 
ATOM   396  C  CA  . SER A 1 43  ? -11.520 5.475   21.638  1.00 23.32  ? 43  SER A CA  1 
ATOM   397  C  C   . SER A 1 43  ? -11.317 5.597   20.116  1.00 21.24  ? 43  SER A C   1 
ATOM   398  O  O   . SER A 1 43  ? -11.491 6.714   19.546  1.00 29.63  ? 43  SER A O   1 
ATOM   399  C  CB  . SER A 1 43  ? -10.413 6.256   22.382  1.00 25.34  ? 43  SER A CB  1 
ATOM   400  O  OG  . SER A 1 43  ? -9.123  5.940   21.954  1.00 27.07  ? 43  SER A OG  1 
ATOM   401  N  N   . LEU A 1 44  ? -10.959 4.499   19.425  1.00 22.40  ? 44  LEU A N   1 
ATOM   402  C  CA  . LEU A 1 44  ? -10.735 4.532   17.934  1.00 18.64  ? 44  LEU A CA  1 
ATOM   403  C  C   . LEU A 1 44  ? -12.084 4.679   17.271  1.00 20.72  ? 44  LEU A C   1 
ATOM   404  O  O   . LEU A 1 44  ? -13.100 4.236   17.786  1.00 26.11  ? 44  LEU A O   1 
ATOM   405  C  CB  . LEU A 1 44  ? -10.056 3.294   17.425  1.00 16.50  ? 44  LEU A CB  1 
ATOM   406  C  CG  . LEU A 1 44  ? -8.595  3.278   17.678  1.00 14.87  ? 44  LEU A CG  1 
ATOM   407  C  CD1 . LEU A 1 44  ? -8.111  1.894   17.236  1.00 16.68  ? 44  LEU A CD1 1 
ATOM   408  C  CD2 . LEU A 1 44  ? -7.821  4.386   16.933  1.00 17.08  ? 44  LEU A CD2 1 
ATOM   409  N  N   . LYS A 1 45  ? -12.165 5.433   16.173  1.00 19.82  ? 45  LYS A N   1 
ATOM   410  C  CA  . LYS A 1 45  ? -13.481 5.618   15.485  1.00 18.89  ? 45  LYS A CA  1 
ATOM   411  C  C   . LYS A 1 45  ? -13.486 4.772   14.274  1.00 18.39  ? 45  LYS A C   1 
ATOM   412  O  O   . LYS A 1 45  ? -12.447 4.262   13.838  1.00 18.32  ? 45  LYS A O   1 
ATOM   413  C  CB  . LYS A 1 45  ? -13.611 7.043   15.034  1.00 20.70  ? 45  LYS A CB  1 
ATOM   414  C  CG  . LYS A 1 45  ? -13.431 8.044   16.145  1.00 28.71  ? 45  LYS A CG  1 
ATOM   415  C  CD  . LYS A 1 45  ? -13.764 9.432   15.659  1.00 39.31  ? 45  LYS A CD  1 
ATOM   416  C  CE  . LYS A 1 45  ? -14.004 10.379  16.829  1.00 48.58  ? 45  LYS A CE  1 
ATOM   417  N  NZ  . LYS A 1 45  ? -12.743 11.070  17.237  1.00 56.99  ? 45  LYS A NZ  1 
ATOM   418  N  N   . PRO A 1 46  ? -14.741 4.587   13.743  1.00 17.91  ? 46  PRO A N   1 
ATOM   419  C  CA  . PRO A 1 46  ? -14.845 3.911   12.443  1.00 18.91  ? 46  PRO A CA  1 
ATOM   420  C  C   . PRO A 1 46  ? -13.990 4.646   11.450  1.00 13.81  ? 46  PRO A C   1 
ATOM   421  O  O   . PRO A 1 46  ? -13.933 5.875   11.497  1.00 14.99  ? 46  PRO A O   1 
ATOM   422  C  CB  . PRO A 1 46  ? -16.352 3.989   12.123  1.00 17.07  ? 46  PRO A CB  1 
ATOM   423  C  CG  . PRO A 1 46  ? -17.025 4.137   13.425  1.00 21.70  ? 46  PRO A CG  1 
ATOM   424  C  CD  . PRO A 1 46  ? -16.077 4.971   14.273  1.00 20.62  ? 46  PRO A CD  1 
ATOM   425  N  N   A LEU A 1 47  ? -13.438 3.877   10.508  0.50 15.24  ? 47  LEU A N   1 
ATOM   426  N  N   B LEU A 1 47  ? -13.445 3.898   10.510  0.50 15.29  ? 47  LEU A N   1 
ATOM   427  C  CA  A LEU A 1 47  ? -12.673 4.537   9.451   0.50 14.18  ? 47  LEU A CA  1 
ATOM   428  C  CA  B LEU A 1 47  ? -12.678 4.500   9.455   0.50 14.21  ? 47  LEU A CA  1 
ATOM   429  C  C   A LEU A 1 47  ? -13.704 5.141   8.469   0.50 16.71  ? 47  LEU A C   1 
ATOM   430  C  C   B LEU A 1 47  ? -13.697 5.121   8.451   0.50 16.75  ? 47  LEU A C   1 
ATOM   431  O  O   A LEU A 1 47  ? -14.664 4.459   8.143   0.50 20.04  ? 47  LEU A O   1 
ATOM   432  O  O   B LEU A 1 47  ? -14.667 4.453   8.108   0.50 20.08  ? 47  LEU A O   1 
ATOM   433  C  CB  A LEU A 1 47  ? -11.885 3.494   8.698   0.50 18.42  ? 47  LEU A CB  1 
ATOM   434  C  CB  B LEU A 1 47  ? -11.896 3.423   8.752   0.50 18.44  ? 47  LEU A CB  1 
ATOM   435  C  CG  A LEU A 1 47  ? -10.420 3.475   8.773   0.50 21.05  ? 47  LEU A CG  1 
ATOM   436  C  CG  B LEU A 1 47  ? -10.850 3.820   7.793   0.50 15.82  ? 47  LEU A CG  1 
ATOM   437  C  CD1 A LEU A 1 47  ? -9.898  2.738   7.535   0.50 22.41  ? 47  LEU A CD1 1 
ATOM   438  C  CD1 B LEU A 1 47  ? -9.733  4.656   8.453   0.50 16.99  ? 47  LEU A CD1 1 
ATOM   439  C  CD2 A LEU A 1 47  ? -9.899  4.917   8.846   0.50 20.97  ? 47  LEU A CD2 1 
ATOM   440  C  CD2 B LEU A 1 47  ? -10.344 2.529   7.138   0.50 18.57  ? 47  LEU A CD2 1 
ATOM   441  N  N   . SER A 1 48  ? -13.432 6.329   7.963   1.00 14.13  ? 48  SER A N   1 
ATOM   442  C  CA  . SER A 1 48  ? -14.288 6.968   6.964   1.00 13.67  ? 48  SER A CA  1 
ATOM   443  C  C   . SER A 1 48  ? -13.533 7.008   5.646   1.00 13.28  ? 48  SER A C   1 
ATOM   444  O  O   . SER A 1 48  ? -12.513 7.708   5.518   1.00 13.39  ? 48  SER A O   1 
ATOM   445  C  CB  . SER A 1 48  ? -14.645 8.385   7.426   1.00 16.66  ? 48  SER A CB  1 
ATOM   446  O  OG  . SER A 1 48  ? -15.252 9.116   6.398   1.00 18.53  ? 48  SER A OG  1 
ATOM   447  N  N   . VAL A 1 49  ? -13.957 6.246   4.699   1.00 15.04  ? 49  VAL A N   1 
ATOM   448  C  CA  . VAL A 1 49  ? -13.321 6.169   3.429   1.00 15.37  ? 49  VAL A CA  1 
ATOM   449  C  C   . VAL A 1 49  ? -14.317 6.723   2.443   1.00 18.13  ? 49  VAL A C   1 
ATOM   450  O  O   . VAL A 1 49  ? -15.332 6.117   2.221   1.00 22.16  ? 49  VAL A O   1 
ATOM   451  C  CB  . VAL A 1 49  ? -13.057 4.660   3.034   1.00 19.25  ? 49  VAL A CB  1 
ATOM   452  C  CG1 . VAL A 1 49  ? -12.252 4.576   1.722   1.00 23.98  ? 49  VAL A CG1 1 
ATOM   453  C  CG2 . VAL A 1 49  ? -12.265 4.002   4.153   1.00 20.08  ? 49  VAL A CG2 1 
ATOM   454  N  N   . SER A 1 50  ? -14.019 7.854   1.808   1.00 17.53  ? 50  SER A N   1 
ATOM   455  C  CA  . SER A 1 50  ? -14.949 8.555   0.945   1.00 21.40  ? 50  SER A CA  1 
ATOM   456  C  C   . SER A 1 50  ? -14.316 8.696   -0.408  1.00 18.22  ? 50  SER A C   1 
ATOM   457  O  O   . SER A 1 50  ? -13.654 9.695   -0.711  1.00 18.97  ? 50  SER A O   1 
ATOM   458  C  CB  . SER A 1 50  ? -15.317 9.925   1.509   1.00 25.05  ? 50  SER A CB  1 
ATOM   459  O  OG  . SER A 1 50  ? -15.984 9.763   2.750   1.00 27.75  ? 50  SER A OG  1 
ATOM   460  N  N   . TYR A 1 51  ? -14.589 7.710   -1.246  1.00 17.32  ? 51  TYR A N   1 
ATOM   461  C  CA  . TYR A 1 51  ? -13.976 7.585   -2.551  1.00 16.67  ? 51  TYR A CA  1 
ATOM   462  C  C   . TYR A 1 51  ? -14.923 7.843   -3.723  1.00 19.66  ? 51  TYR A C   1 
ATOM   463  O  O   . TYR A 1 51  ? -14.493 7.695   -4.879  1.00 19.66  ? 51  TYR A O   1 
ATOM   464  C  CB  . TYR A 1 51  ? -13.316 6.232   -2.731  1.00 15.48  ? 51  TYR A CB  1 
ATOM   465  C  CG  . TYR A 1 51  ? -12.045 5.943   -1.965  1.00 13.46  ? 51  TYR A CG  1 
ATOM   466  C  CD1 . TYR A 1 51  ? -11.309 6.949   -1.350  1.00 14.31  ? 51  TYR A CD1 1 
ATOM   467  C  CD2 . TYR A 1 51  ? -11.554 4.624   -1.884  1.00 13.14  ? 51  TYR A CD2 1 
ATOM   468  C  CE1 . TYR A 1 51  ? -10.127 6.660   -0.638  1.00 13.20  ? 51  TYR A CE1 1 
ATOM   469  C  CE2 . TYR A 1 51  ? -10.403 4.307   -1.190  1.00 12.35  ? 51  TYR A CE2 1 
ATOM   470  C  CZ  . TYR A 1 51  ? -9.657  5.323   -0.565  1.00 11.40  ? 51  TYR A CZ  1 
ATOM   471  O  OH  . TYR A 1 51  ? -8.518  4.968   0.091   1.00 12.08  ? 51  TYR A OH  1 
ATOM   472  N  N   . ASP A 1 52  ? -16.162 8.271   -3.441  1.00 21.23  ? 52  ASP A N   1 
ATOM   473  C  CA  . ASP A 1 52  ? -17.166 8.529   -4.490  1.00 24.86  ? 52  ASP A CA  1 
ATOM   474  C  C   . ASP A 1 52  ? -16.768 9.506   -5.600  1.00 24.84  ? 52  ASP A C   1 
ATOM   475  O  O   . ASP A 1 52  ? -17.180 9.325   -6.765  1.00 31.15  ? 52  ASP A O   1 
ATOM   476  C  CB  . ASP A 1 52  ? -18.531 8.848   -3.892  1.00 27.27  ? 52  ASP A CB  1 
ATOM   477  C  CG  . ASP A 1 52  ? -18.468 9.921   -2.776  1.00 38.47  ? 52  ASP A CG  1 
ATOM   478  O  OD1 . ASP A 1 52  ? -17.614 9.805   -1.831  1.00 37.69  ? 52  ASP A OD1 1 
ATOM   479  O  OD2 . ASP A 1 52  ? -19.251 10.909  -2.896  1.00 61.35  ? 52  ASP A OD2 1 
ATOM   480  N  N   . GLN A 1 53  ? -15.889 10.438  -5.286  1.00 22.46  ? 53  GLN A N   1 
ATOM   481  C  CA  . GLN A 1 53  ? -15.454 11.403  -6.323  1.00 23.29  ? 53  GLN A CA  1 
ATOM   482  C  C   . GLN A 1 53  ? -13.994 11.178  -6.777  1.00 18.63  ? 53  GLN A C   1 
ATOM   483  O  O   . GLN A 1 53  ? -13.406 11.992  -7.436  1.00 19.61  ? 53  GLN A O   1 
ATOM   484  C  CB  . GLN A 1 53  ? -15.671 12.850  -5.848  1.00 25.32  ? 53  GLN A CB  1 
ATOM   485  C  CG  . GLN A 1 53  ? -17.127 13.205  -5.621  1.00 32.87  ? 53  GLN A CG  1 
ATOM   486  C  CD  . GLN A 1 53  ? -17.863 13.120  -6.924  1.00 46.16  ? 53  GLN A CD  1 
ATOM   487  O  OE1 . GLN A 1 53  ? -17.288 13.427  -8.005  1.00 55.61  ? 53  GLN A OE1 1 
ATOM   488  N  NE2 . GLN A 1 53  ? -19.080 12.610  -6.867  1.00 50.65  ? 53  GLN A NE2 1 
ATOM   489  N  N   . ALA A 1 54  ? -13.445 10.012  -6.474  1.00 18.66  ? 54  ALA A N   1 
ATOM   490  C  CA  . ALA A 1 54  ? -12.040 9.796   -6.874  1.00 16.92  ? 54  ALA A CA  1 
ATOM   491  C  C   . ALA A 1 54  ? -11.833 9.892   -8.393  1.00 19.31  ? 54  ALA A C   1 
ATOM   492  O  O   . ALA A 1 54  ? -12.638 9.390   -9.189  1.00 23.35  ? 54  ALA A O   1 
ATOM   493  C  CB  . ALA A 1 54  ? -11.522 8.449   -6.353  1.00 19.62  ? 54  ALA A CB  1 
ATOM   494  N  N   . THR A 1 55  ? -10.771 10.559  -8.825  1.00 15.60  ? 55  THR A N   1 
ATOM   495  C  CA  . THR A 1 55  ? -10.533 10.721  -10.247 1.00 19.21  ? 55  THR A CA  1 
ATOM   496  C  C   . THR A 1 55  ? -9.155  10.168  -10.547 1.00 15.69  ? 55  THR A C   1 
ATOM   497  O  O   . THR A 1 55  ? -8.170  10.792  -10.264 1.00 14.93  ? 55  THR A O   1 
ATOM   498  C  CB  . THR A 1 55  ? -10.492 12.217  -10.649 1.00 26.81  ? 55  THR A CB  1 
ATOM   499  O  OG1 . THR A 1 55  ? -11.733 12.861  -10.327 1.00 34.28  ? 55  THR A OG1 1 
ATOM   500  C  CG2 . THR A 1 55  ? -10.208 12.255  -12.210 1.00 28.38  ? 55  THR A CG2 1 
ATOM   501  N  N   . SER A 1 56  ? -9.094  8.967   -11.032 1.00 19.22  ? 56  SER A N   1 
ATOM   502  C  CA  . SER A 1 56  ? -7.821  8.395   -11.388 1.00 18.32  ? 56  SER A CA  1 
ATOM   503  C  C   . SER A 1 56  ? -7.466  9.070   -12.667 1.00 18.02  ? 56  SER A C   1 
ATOM   504  O  O   . SER A 1 56  ? -8.233  9.528   -13.454 1.00 21.19  ? 56  SER A O   1 
ATOM   505  C  CB  . SER A 1 56  ? -7.826  6.867   -11.583 1.00 18.93  ? 56  SER A CB  1 
ATOM   506  O  OG  . SER A 1 56  ? -8.641  6.541   -12.726 1.00 20.12  ? 56  SER A OG  1 
ATOM   507  N  N   . LEU A 1 57  ? -6.200  9.098   -12.868 1.00 13.94  ? 57  LEU A N   1 
ATOM   508  C  CA  . LEU A 1 57  ? -5.649  9.735   -14.087 1.00 16.89  ? 57  LEU A CA  1 
ATOM   509  C  C   . LEU A 1 57  ? -4.766  8.794   -14.903 1.00 17.00  ? 57  LEU A C   1 
ATOM   510  O  O   . LEU A 1 57  ? -4.690  8.847   -16.147 1.00 20.37  ? 57  LEU A O   1 
ATOM   511  C  CB  . LEU A 1 57  ? -4.806  10.869  -13.634 1.00 21.20  ? 57  LEU A CB  1 
ATOM   512  C  CG  . LEU A 1 57  ? -5.534  12.108  -13.061 1.00 26.86  ? 57  LEU A CG  1 
ATOM   513  C  CD1 . LEU A 1 57  ? -4.429  13.066  -12.642 1.00 31.70  ? 57  LEU A CD1 1 
ATOM   514  C  CD2 . LEU A 1 57  ? -6.583  12.710  -14.026 1.00 85.37  ? 57  LEU A CD2 1 
ATOM   515  N  N   . ARG A 1 58  ? -3.968  8.042   -14.220 1.00 16.91  ? 58  ARG A N   1 
ATOM   516  C  CA  . ARG A 1 58  ? -2.912  7.373   -14.963 1.00 15.44  ? 58  ARG A CA  1 
ATOM   517  C  C   . ARG A 1 58  ? -2.339  6.175   -14.202 1.00 14.80  ? 58  ARG A C   1 
ATOM   518  O  O   . ARG A 1 58  ? -2.417  6.131   -12.991 1.00 17.24  ? 58  ARG A O   1 
ATOM   519  C  CB  . ARG A 1 58  ? -1.807  8.425   -15.139 1.00 16.43  ? 58  ARG A CB  1 
ATOM   520  C  CG  . ARG A 1 58  ? -0.738  8.037   -15.977 1.00 17.65  ? 58  ARG A CG  1 
ATOM   521  C  CD  . ARG A 1 58  ? 0.286   9.050   -16.288 1.00 20.73  ? 58  ARG A CD  1 
ATOM   522  N  NE  . ARG A 1 58  ? 1.181   9.034   -15.148 1.00 16.92  ? 58  ARG A NE  1 
ATOM   523  C  CZ  . ARG A 1 58  ? 2.496   9.180   -15.205 1.00 15.84  ? 58  ARG A CZ  1 
ATOM   524  N  NH1 . ARG A 1 58  ? 3.106   9.378   -16.366 1.00 21.24  ? 58  ARG A NH1 1 
ATOM   525  N  NH2 . ARG A 1 58  ? 3.198   9.115   -14.084 1.00 16.24  ? 58  ARG A NH2 1 
ATOM   526  N  N   . ILE A 1 59  ? -1.680  5.212   -14.890 1.00 16.58  ? 59  ILE A N   1 
ATOM   527  C  CA  . ILE A 1 59  ? -1.060  4.078   -14.210 1.00 15.22  ? 59  ILE A CA  1 
ATOM   528  C  C   . ILE A 1 59  ? 0.347   4.058   -14.764 1.00 13.35  ? 59  ILE A C   1 
ATOM   529  O  O   . ILE A 1 59  ? 0.697   4.262   -15.969 1.00 16.21  ? 59  ILE A O   1 
ATOM   530  C  CB  . ILE A 1 59  ? -1.741  2.760   -14.521 1.00 14.90  ? 59  ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 59  ? -1.142  1.638   -13.672 1.00 14.11  ? 59  ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 59  ? -1.726  2.349   -16.048 1.00 17.53  ? 59  ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 59  ? -1.955  0.380   -13.765 1.00 14.57  ? 59  ILE A CD1 1 
ATOM   534  N  N   . LEU A 1 60  ? 1.256   3.851   -13.878 1.00 13.52  ? 60  LEU A N   1 
ATOM   535  C  CA  . LEU A 1 60  ? 2.611   3.919   -14.106 1.00 12.70  ? 60  LEU A CA  1 
ATOM   536  C  C   . LEU A 1 60  ? 3.511   2.731   -13.566 1.00 13.69  ? 60  LEU A C   1 
ATOM   537  O  O   . LEU A 1 60  ? 3.367   2.368   -12.433 1.00 13.52  ? 60  LEU A O   1 
ATOM   538  C  CB  . LEU A 1 60  ? 3.160   5.235   -13.432 1.00 15.12  ? 60  LEU A CB  1 
ATOM   539  C  CG  . LEU A 1 60  ? 4.675   5.346   -13.482 1.00 15.21  ? 60  LEU A CG  1 
ATOM   540  C  CD1 . LEU A 1 60  ? 5.217   5.691   -14.879 1.00 16.46  ? 60  LEU A CD1 1 
ATOM   541  C  CD2 . LEU A 1 60  ? 5.193   6.461   -12.494 1.00 18.03  ? 60  LEU A CD2 1 
ATOM   542  N  N   . ASN A 1 61  ? 4.360   2.164   -14.398 1.00 14.23  ? 61  ASN A N   1 
ATOM   543  C  CA  . ASN A 1 61  ? 5.389   1.247   -13.943 1.00 14.91  ? 61  ASN A CA  1 
ATOM   544  C  C   . ASN A 1 61  ? 6.639   1.996   -13.566 1.00 14.34  ? 61  ASN A C   1 
ATOM   545  O  O   . ASN A 1 61  ? 7.355   2.535   -14.410 1.00 17.84  ? 61  ASN A O   1 
ATOM   546  C  CB  . ASN A 1 61  ? 5.659   0.159   -15.031 1.00 17.25  ? 61  ASN A CB  1 
ATOM   547  C  CG  . ASN A 1 61  ? 6.740   -0.857  -14.644 1.00 14.76  ? 61  ASN A CG  1 
ATOM   548  O  OD1 . ASN A 1 61  ? 7.639   -0.635  -13.761 1.00 15.81  ? 61  ASN A OD1 1 
ATOM   549  N  ND2 . ASN A 1 61  ? 6.653   -2.056  -15.247 1.00 15.96  ? 61  ASN A ND2 1 
ATOM   550  N  N   . ASN A 1 62  ? 6.880   2.081   -12.268 1.00 16.05  ? 62  ASN A N   1 
ATOM   551  C  CA  . ASN A 1 62  ? 7.849   2.960   -11.765 1.00 14.95  ? 62  ASN A CA  1 
ATOM   552  C  C   . ASN A 1 62  ? 9.082   2.175   -11.611 1.00 13.04  ? 62  ASN A C   1 
ATOM   553  O  O   . ASN A 1 62  ? 10.125  2.565   -11.046 1.00 18.37  ? 62  ASN A O   1 
ATOM   554  C  CB  . ASN A 1 62  ? 7.547   3.725   -10.458 1.00 17.80  ? 62  ASN A CB  1 
ATOM   555  C  CG  . ASN A 1 62  ? 7.528   2.773   -9.287  1.00 16.30  ? 62  ASN A CG  1 
ATOM   556  O  OD1 . ASN A 1 62  ? 7.759   1.557   -9.360  1.00 16.10  ? 62  ASN A OD1 1 
ATOM   557  N  ND2 . ASN A 1 62  ? 7.324   3.342   -8.161  1.00 20.87  ? 62  ASN A ND2 1 
ATOM   558  N  N   . GLY A 1 63  ? 9.038   0.898   -12.007 1.00 15.64  ? 63  GLY A N   1 
ATOM   559  C  CA  . GLY A 1 63  ? 10.212  0.014   -11.864 1.00 12.44  ? 63  GLY A CA  1 
ATOM   560  C  C   . GLY A 1 63  ? 10.412  -0.775  -10.555 1.00 15.27  ? 63  GLY A C   1 
ATOM   561  O  O   . GLY A 1 63  ? 11.344  -1.599  -10.380 1.00 18.05  ? 63  GLY A O   1 
ATOM   562  N  N   . HIS A 1 64  ? 9.532   -0.532  -9.647  1.00 13.97  ? 64  HIS A N   1 
ATOM   563  C  CA  . HIS A 1 64  ? 9.450   -1.248  -8.321  1.00 14.70  ? 64  HIS A CA  1 
ATOM   564  C  C   . HIS A 1 64  ? 8.097   -1.851  -8.192  1.00 13.76  ? 64  HIS A C   1 
ATOM   565  O  O   . HIS A 1 64  ? 8.014   -2.997  -7.674  1.00 19.06  ? 64  HIS A O   1 
ATOM   566  C  CB  . HIS A 1 64  ? 9.707   -0.243  -7.184  1.00 14.49  ? 64  HIS A CB  1 
ATOM   567  C  CG  . HIS A 1 64  ? 10.991  0.548   -7.339  1.00 17.25  ? 64  HIS A CG  1 
ATOM   568  N  ND1 . HIS A 1 64  ? 12.236  -0.061  -7.260  1.00 18.96  ? 64  HIS A ND1 1 
ATOM   569  C  CD2 . HIS A 1 64  ? 11.214  1.877   -7.567  1.00 17.49  ? 64  HIS A CD2 1 
ATOM   570  C  CE1 . HIS A 1 64  ? 13.193  0.871   -7.360  1.00 20.43  ? 64  HIS A CE1 1 
ATOM   571  N  NE2 . HIS A 1 64  ? 12.585  2.066   -7.586  1.00 22.11  ? 64  HIS A NE2 1 
ATOM   572  N  N   . ALA A 1 65  ? 7.064   -1.197  -8.674  1.00 13.03  ? 65  ALA A N   1 
ATOM   573  C  CA  . ALA A 1 65  ? 5.675   -1.636  -8.633  1.00 12.22  ? 65  ALA A CA  1 
ATOM   574  C  C   . ALA A 1 65  ? 4.994   -0.882  -9.753  1.00 12.60  ? 65  ALA A C   1 
ATOM   575  O  O   . ALA A 1 65  ? 5.662   -0.232  -10.589 1.00 14.64  ? 65  ALA A O   1 
ATOM   576  C  CB  . ALA A 1 65  ? 5.038   -1.414  -7.219  1.00 13.94  ? 65  ALA A CB  1 
ATOM   577  N  N   . PHE A 1 66  ? 3.681   -0.929  -9.757  1.00 12.11  ? 66  PHE A N   1 
ATOM   578  C  CA  . PHE A 1 66  ? 2.924   0.034   -10.558 1.00 11.89  ? 66  PHE A CA  1 
ATOM   579  C  C   . PHE A 1 66  ? 2.062   0.887   -9.680  1.00 11.76  ? 66  PHE A C   1 
ATOM   580  O  O   . PHE A 1 66  ? 1.440   0.436   -8.712  1.00 12.16  ? 66  PHE A O   1 
ATOM   581  C  CB  . PHE A 1 66  ? 2.080   -0.658  -11.664 1.00 14.12  ? 66  PHE A CB  1 
ATOM   582  C  CG  . PHE A 1 66  ? 1.020   -1.578  -11.151 1.00 13.54  ? 66  PHE A CG  1 
ATOM   583  C  CD1 . PHE A 1 66  ? -0.217  -1.073  -10.799 1.00 13.34  ? 66  PHE A CD1 1 
ATOM   584  C  CD2 . PHE A 1 66  ? 1.236   -2.951  -11.034 1.00 12.64  ? 66  PHE A CD2 1 
ATOM   585  C  CE1 . PHE A 1 66  ? -1.190  -1.905  -10.288 1.00 13.49  ? 66  PHE A CE1 1 
ATOM   586  C  CE2 . PHE A 1 66  ? 0.247   -3.800  -10.507 1.00 13.63  ? 66  PHE A CE2 1 
ATOM   587  C  CZ  . PHE A 1 66  ? -0.995  -3.282  -10.140 1.00 13.85  ? 66  PHE A CZ  1 
ATOM   588  N  N   . ASN A 1 67  ? 1.985   2.172   -10.026 1.00 11.65  ? 67  ASN A N   1 
ATOM   589  C  CA  . ASN A 1 67  ? 1.131   3.126   -9.252  1.00 12.41  ? 67  ASN A CA  1 
ATOM   590  C  C   . ASN A 1 67  ? -0.169  3.533   -10.052 1.00 10.87  ? 67  ASN A C   1 
ATOM   591  O  O   . ASN A 1 67  ? 0.016   3.968   -11.225 1.00 14.98  ? 67  ASN A O   1 
ATOM   592  C  CB  . ASN A 1 67  ? 1.890   4.402   -8.893  1.00 14.88  ? 67  ASN A CB  1 
ATOM   593  C  CG  . ASN A 1 67  ? 3.016   4.195   -7.967  1.00 15.64  ? 67  ASN A CG  1 
ATOM   594  O  OD1 . ASN A 1 67  ? 3.146   3.139   -7.296  1.00 17.44  ? 67  ASN A OD1 1 
ATOM   595  N  ND2 . ASN A 1 67  ? 3.826   5.204   -7.877  1.00 20.60  ? 67  ASN A ND2 1 
ATOM   596  N  N   . VAL A 1 68  ? -1.352  3.501   -9.479  1.00 12.23  ? 68  VAL A N   1 
ATOM   597  C  CA  . VAL A 1 68  ? -2.553  4.071   -10.083 1.00 12.52  ? 68  VAL A CA  1 
ATOM   598  C  C   . VAL A 1 68  ? -2.584  5.491   -9.382  1.00 14.58  ? 68  VAL A C   1 
ATOM   599  O  O   . VAL A 1 68  ? -2.648  5.567   -8.152  1.00 12.45  ? 68  VAL A O   1 
ATOM   600  C  CB  . VAL A 1 68  ? -3.774  3.213   -9.849  1.00 14.39  ? 68  VAL A CB  1 
ATOM   601  C  CG1 . VAL A 1 68  ? -4.972  4.059   -10.314 1.00 16.07  ? 68  VAL A CG1 1 
ATOM   602  C  CG2 . VAL A 1 68  ? -3.606  1.962   -10.668 1.00 14.48  ? 68  VAL A CG2 1 
ATOM   603  N  N   . GLU A 1 69  ? -2.484  6.560   -10.158 1.00 15.69  ? 69  GLU A N   1 
ATOM   604  C  CA  . GLU A 1 69  ? -2.463  7.928   -9.663  1.00 13.56  ? 69  GLU A CA  1 
ATOM   605  C  C   . GLU A 1 69  ? -3.772  8.638   -9.737  1.00 16.09  ? 69  GLU A C   1 
ATOM   606  O  O   . GLU A 1 69  ? -4.640  8.397   -10.699 1.00 16.47  ? 69  GLU A O   1 
ATOM   607  C  CB  . GLU A 1 69  ? -1.608  8.647   -10.625 1.00 15.73  ? 69  GLU A CB  1 
ATOM   608  C  CG  . GLU A 1 69  ? -0.259  8.160   -10.528 1.00 14.83  ? 69  GLU A CG  1 
ATOM   609  C  CD  . GLU A 1 69  ? 0.588   8.548   -11.695 1.00 16.38  ? 69  GLU A CD  1 
ATOM   610  O  OE1 . GLU A 1 69  ? 0.096   9.272   -12.642 1.00 18.21  ? 69  GLU A OE1 1 
ATOM   611  O  OE2 . GLU A 1 69  ? 1.791   8.228   -11.765 1.00 18.27  ? 69  GLU A OE2 1 
ATOM   612  N  N   . PHE A 1 70  ? -3.962  9.517   -8.789  1.00 13.36  ? 70  PHE A N   1 
ATOM   613  C  CA  . PHE A 1 70  ? -5.220  10.225  -8.713  1.00 12.64  ? 70  PHE A CA  1 
ATOM   614  C  C   . PHE A 1 70  ? -4.968  11.716  -8.784  1.00 13.95  ? 70  PHE A C   1 
ATOM   615  O  O   . PHE A 1 70  ? -3.909  12.222  -8.403  1.00 14.14  ? 70  PHE A O   1 
ATOM   616  C  CB  . PHE A 1 70  ? -5.944  9.891   -7.438  1.00 12.94  ? 70  PHE A CB  1 
ATOM   617  C  CG  . PHE A 1 70  ? -6.477  8.480   -7.470  1.00 13.44  ? 70  PHE A CG  1 
ATOM   618  C  CD1 . PHE A 1 70  ? -5.633  7.393   -7.241  1.00 13.02  ? 70  PHE A CD1 1 
ATOM   619  C  CD2 . PHE A 1 70  ? -7.779  8.265   -7.800  1.00 13.54  ? 70  PHE A CD2 1 
ATOM   620  C  CE1 . PHE A 1 70  ? -6.150  6.114   -7.382  1.00 13.39  ? 70  PHE A CE1 1 
ATOM   621  C  CE2 . PHE A 1 70  ? -8.302  6.978   -7.909  1.00 13.35  ? 70  PHE A CE2 1 
ATOM   622  C  CZ  . PHE A 1 70  ? -7.466  5.884   -7.714  1.00 14.25  ? 70  PHE A CZ  1 
ATOM   623  N  N   . ASP A 1 71  ? -5.921  12.450  -9.294  1.00 16.15  ? 71  ASP A N   1 
ATOM   624  C  CA  . ASP A 1 71  ? -5.858  13.896  -9.184  1.00 16.56  ? 71  ASP A CA  1 
ATOM   625  C  C   . ASP A 1 71  ? -6.233  14.257  -7.787  1.00 17.20  ? 71  ASP A C   1 
ATOM   626  O  O   . ASP A 1 71  ? -7.385  14.063  -7.371  1.00 21.28  ? 71  ASP A O   1 
ATOM   627  C  CB  . ASP A 1 71  ? -6.923  14.435  -10.169 1.00 24.53  ? 71  ASP A CB  1 
ATOM   628  C  CG  . ASP A 1 71  ? -7.098  15.931  -10.080 1.00 31.31  ? 71  ASP A CG  1 
ATOM   629  O  OD1 . ASP A 1 71  ? -6.350  16.598  -9.371  1.00 23.35  ? 71  ASP A OD1 1 
ATOM   630  O  OD2 . ASP A 1 71  ? -8.025  16.491  -10.730 1.00 99.84  ? 71  ASP A OD2 1 
ATOM   631  N  N   . ASP A 1 72  ? -5.229  14.762  -7.093  1.00 13.04  ? 72  ASP A N   1 
ATOM   632  C  CA  . ASP A 1 72  ? -5.404  15.162  -5.684  1.00 14.76  ? 72  ASP A CA  1 
ATOM   633  C  C   . ASP A 1 72  ? -5.379  16.684  -5.551  1.00 15.04  ? 72  ASP A C   1 
ATOM   634  O  O   . ASP A 1 72  ? -5.063  17.217  -4.512  1.00 17.45  ? 72  ASP A O   1 
ATOM   635  C  CB  . ASP A 1 72  ? -4.321  14.559  -4.788  1.00 14.38  ? 72  ASP A CB  1 
ATOM   636  C  CG  . ASP A 1 72  ? -2.985  15.020  -5.165  1.00 13.38  ? 72  ASP A CG  1 
ATOM   637  O  OD1 . ASP A 1 72  ? -2.789  15.716  -6.226  1.00 16.22  ? 72  ASP A OD1 1 
ATOM   638  O  OD2 . ASP A 1 72  ? -2.017  14.800  -4.373  1.00 14.34  ? 72  ASP A OD2 1 
ATOM   639  N  N   . SER A 1 73  ? -5.763  17.398  -6.607  1.00 17.10  ? 73  SER A N   1 
ATOM   640  C  CA  . SER A 1 73  ? -5.771  18.912  -6.603  1.00 17.49  ? 73  SER A CA  1 
ATOM   641  C  C   . SER A 1 73  ? -7.092  19.467  -5.991  1.00 16.59  ? 73  SER A C   1 
ATOM   642  O  O   . SER A 1 73  ? -7.206  20.679  -5.844  1.00 16.83  ? 73  SER A O   1 
ATOM   643  C  CB  . SER A 1 73  ? -5.522  19.392  -8.013  1.00 23.74  ? 73  SER A CB  1 
ATOM   644  O  OG  . SER A 1 73  ? -6.665  19.219  -8.801  1.00 22.31  ? 73  SER A OG  1 
ATOM   645  N  N   . GLN A 1 74  ? -8.081  18.637  -5.686  1.00 19.90  ? 74  GLN A N   1 
ATOM   646  C  CA  . GLN A 1 74  ? -9.350  19.067  -5.043  1.00 21.38  ? 74  GLN A CA  1 
ATOM   647  C  C   . GLN A 1 74  ? -9.667  18.100  -3.979  1.00 17.92  ? 74  GLN A C   1 
ATOM   648  O  O   . GLN A 1 74  ? -9.097  16.959  -3.914  1.00 15.36  ? 74  GLN A O   1 
ATOM   649  C  CB  . GLN A 1 74  ? -10.548 19.124  -6.017  1.00 23.59  ? 74  GLN A CB  1 
ATOM   650  C  CG  . GLN A 1 74  ? -10.250 20.208  -6.978  1.00 27.42  ? 74  GLN A CG  1 
ATOM   651  C  CD  . GLN A 1 74  ? -10.657 19.866  -8.388  1.00 44.43  ? 74  GLN A CD  1 
ATOM   652  O  OE1 . GLN A 1 74  ? -11.843 19.841  -8.663  1.00 37.25  ? 74  GLN A OE1 1 
ATOM   653  N  NE2 . GLN A 1 74  ? -9.645  19.625  -9.313  1.00 39.88  ? 74  GLN A NE2 1 
ATOM   654  N  N   . ASP A 1 75  ? -10.668 18.505  -3.210  1.00 20.49  ? 75  ASP A N   1 
ATOM   655  C  CA  . ASP A 1 75  ? -11.107 17.779  -2.058  1.00 16.85  ? 75  ASP A CA  1 
ATOM   656  C  C   . ASP A 1 75  ? -12.015 16.613  -2.531  1.00 19.25  ? 75  ASP A C   1 
ATOM   657  O  O   . ASP A 1 75  ? -13.228 16.792  -2.575  1.00 24.33  ? 75  ASP A O   1 
ATOM   658  C  CB  . ASP A 1 75  ? -11.843 18.778  -1.142  1.00 19.78  ? 75  ASP A CB  1 
ATOM   659  C  CG  . ASP A 1 75  ? -12.443 18.127  0.086   1.00 27.38  ? 75  ASP A CG  1 
ATOM   660  O  OD1 . ASP A 1 75  ? -12.095 16.985  0.375   1.00 26.00  ? 75  ASP A OD1 1 
ATOM   661  O  OD2 . ASP A 1 75  ? -13.268 18.777  0.786   1.00 42.49  ? 75  ASP A OD2 1 
ATOM   662  N  N   . LYS A 1 76  ? -11.412 15.514  -2.913  1.00 16.62  ? 76  LYS A N   1 
ATOM   663  C  CA  . LYS A 1 76  ? -12.208 14.424  -3.507  1.00 18.58  ? 76  LYS A CA  1 
ATOM   664  C  C   . LYS A 1 76  ? -12.284 13.057  -2.806  1.00 40.83  ? 76  LYS A C   1 
ATOM   665  O  O   . LYS A 1 76  ? -13.352 12.646  -2.336  1.00 66.98  ? 76  LYS A O   1 
ATOM   666  C  CB  . LYS A 1 76  ? -11.770 14.189  -4.944  1.00 19.24  ? 76  LYS A CB  1 
ATOM   667  C  CG  . LYS A 1 76  ? -12.122 15.336  -5.879  1.00 31.04  ? 76  LYS A CG  1 
ATOM   668  C  CD  . LYS A 1 76  ? -11.433 15.146  -7.239  1.00 35.70  ? 76  LYS A CD  1 
ATOM   669  C  CE  . LYS A 1 76  ? -11.944 16.064  -8.362  1.00 36.19  ? 76  LYS A CE  1 
ATOM   670  N  NZ  . LYS A 1 76  ? -11.045 16.145  -9.550  1.00 46.86  ? 76  LYS A NZ  1 
ATOM   671  N  N   . ALA A 1 77  ? -11.168 12.349  -2.783  1.00 24.24  ? 77  ALA A N   1 
ATOM   672  C  CA  . ALA A 1 77  ? -11.141 10.991  -2.256  1.00 17.56  ? 77  ALA A CA  1 
ATOM   673  C  C   . ALA A 1 77  ? -10.393 11.018  -0.959  1.00 13.20  ? 77  ALA A C   1 
ATOM   674  O  O   . ALA A 1 77  ? -9.168  11.079  -0.934  1.00 20.08  ? 77  ALA A O   1 
ATOM   675  C  CB  . ALA A 1 77  ? -10.457 10.065  -3.244  1.00 16.67  ? 77  ALA A CB  1 
ATOM   676  N  N   . VAL A 1 78  ? -11.112 10.990  0.127   1.00 13.69  ? 78  VAL A N   1 
ATOM   677  C  CA  . VAL A 1 78  ? -10.569 11.328  1.451   1.00 13.50  ? 78  VAL A CA  1 
ATOM   678  C  C   . VAL A 1 78  ? -10.728 10.203  2.438   1.00 11.66  ? 78  VAL A C   1 
ATOM   679  O  O   . VAL A 1 78  ? -11.749 9.514   2.500   1.00 14.16  ? 78  VAL A O   1 
ATOM   680  C  CB  . VAL A 1 78  ? -11.403 12.568  1.985   1.00 19.89  ? 78  VAL A CB  1 
ATOM   681  C  CG1 . VAL A 1 78  ? -11.356 12.767  3.512   1.00 21.94  ? 78  VAL A CG1 1 
ATOM   682  C  CG2 . VAL A 1 78  ? -10.966 13.832  1.237   1.00 23.83  ? 78  VAL A CG2 1 
ATOM   683  N  N   . LEU A 1 79  ? -9.661  10.032  3.234   1.00 10.83  ? 79  LEU A N   1 
ATOM   684  C  CA  . LEU A 1 79  ? -9.672  9.119   4.402   1.00 11.10  ? 79  LEU A CA  1 
ATOM   685  C  C   . LEU A 1 79  ? -9.685  10.002  5.624   1.00 10.74  ? 79  LEU A C   1 
ATOM   686  O  O   . LEU A 1 79  ? -8.832  10.934  5.730   1.00 12.52  ? 79  LEU A O   1 
ATOM   687  C  CB  . LEU A 1 79  ? -8.402  8.243   4.331   1.00 12.97  ? 79  LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 79  ? -8.260  7.198   5.322   1.00 11.78  ? 79  LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 79  ? -9.308  6.119   5.092   1.00 16.90  ? 79  LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 79  ? -6.874  6.560   5.254   1.00 11.05  ? 79  LEU A CD2 1 
ATOM   691  N  N   . LYS A 1 80  ? -10.529 9.670   6.577   1.00 12.43  ? 80  LYS A N   1 
ATOM   692  C  CA  . LYS A 1 80  ? -10.587 10.391  7.865   1.00 12.48  ? 80  LYS A CA  1 
ATOM   693  C  C   . LYS A 1 80  ? -11.121 9.445   8.907   1.00 12.64  ? 80  LYS A C   1 
ATOM   694  O  O   . LYS A 1 80  ? -11.390 8.284   8.625   1.00 13.08  ? 80  LYS A O   1 
ATOM   695  C  CB  . LYS A 1 80  ? -11.330 11.710  7.783   1.00 15.75  ? 80  LYS A CB  1 
ATOM   696  C  CG  . LYS A 1 80  ? -12.685 11.468  7.495   1.00 16.58  ? 80  LYS A CG  1 
ATOM   697  C  CD  . LYS A 1 80  ? -13.201 12.859  7.189   1.00 31.13  ? 80  LYS A CD  1 
ATOM   698  C  CE  . LYS A 1 80  ? -14.418 13.232  7.995   1.00 49.21  ? 80  LYS A CE  1 
ATOM   699  N  NZ  . LYS A 1 80  ? -15.503 12.219  7.884   1.00 56.91  ? 80  LYS A NZ  1 
ATOM   700  N  N   . GLY A 1 81  ? -11.260 9.926   10.125  1.00 14.15  ? 81  GLY A N   1 
ATOM   701  C  CA  . GLY A 1 81  ? -11.763 9.081   11.177  1.00 15.09  ? 81  GLY A CA  1 
ATOM   702  C  C   . GLY A 1 81  ? -10.737 8.048   11.496  1.00 14.14  ? 81  GLY A C   1 
ATOM   703  O  O   . GLY A 1 81  ? -9.541  8.257   11.349  1.00 13.40  ? 81  GLY A O   1 
ATOM   704  N  N   . GLY A 1 82  ? -11.201 6.934   12.050  1.00 18.39  ? 82  GLY A N   1 
ATOM   705  C  CA  . GLY A 1 82  ? -10.244 5.909   12.418  1.00 19.85  ? 82  GLY A CA  1 
ATOM   706  C  C   . GLY A 1 82  ? -9.384  6.492   13.534  1.00 17.29  ? 82  GLY A C   1 
ATOM   707  O  O   . GLY A 1 82  ? -9.879  7.184   14.435  1.00 23.57  ? 82  GLY A O   1 
ATOM   708  N  N   . PRO A 1 83  ? -8.047  6.351   13.404  1.00 14.83  ? 83  PRO A N   1 
ATOM   709  C  CA  . PRO A 1 83  ? -7.154  6.930   14.354  1.00 14.88  ? 83  PRO A CA  1 
ATOM   710  C  C   . PRO A 1 83  ? -6.717  8.361   13.962  1.00 15.57  ? 83  PRO A C   1 
ATOM   711  O  O   . PRO A 1 83  ? -5.898  8.935   14.695  1.00 17.31  ? 83  PRO A O   1 
ATOM   712  C  CB  . PRO A 1 83  ? -5.856  6.031   14.234  1.00 15.64  ? 83  PRO A CB  1 
ATOM   713  C  CG  . PRO A 1 83  ? -5.891  5.707   12.762  1.00 13.35  ? 83  PRO A CG  1 
ATOM   714  C  CD  . PRO A 1 83  ? -7.336  5.544   12.399  1.00 13.70  ? 83  PRO A CD  1 
ATOM   715  N  N   . LEU A 1 84  ? -7.217  8.884   12.881  1.00 12.28  ? 84  LEU A N   1 
ATOM   716  C  CA  . LEU A 1 84  ? -6.664  10.091  12.269  1.00 12.49  ? 84  LEU A CA  1 
ATOM   717  C  C   . LEU A 1 84  ? -7.281  11.352  12.857  1.00 13.93  ? 84  LEU A C   1 
ATOM   718  O  O   . LEU A 1 84  ? -8.461  11.367  13.163  1.00 16.19  ? 84  LEU A O   1 
ATOM   719  C  CB  . LEU A 1 84  ? -6.919  10.095  10.790  1.00 10.59  ? 84  LEU A CB  1 
ATOM   720  C  CG  . LEU A 1 84  ? -6.329  8.827   10.072  1.00 10.25  ? 84  LEU A CG  1 
ATOM   721  C  CD1 . LEU A 1 84  ? -6.805  8.789   8.622   1.00 11.49  ? 84  LEU A CD1 1 
ATOM   722  C  CD2 . LEU A 1 84  ? -4.766  8.835   10.174  1.00 10.50  ? 84  LEU A CD2 1 
ATOM   723  N  N   . ASP A 1 85  ? -6.516  12.429  12.919  1.00 15.36  ? 85  ASP A N   1 
ATOM   724  C  CA  . ASP A 1 85  ? -7.001  13.774  13.196  1.00 18.63  ? 85  ASP A CA  1 
ATOM   725  C  C   . ASP A 1 85  ? -7.045  14.448  11.788  1.00 16.93  ? 85  ASP A C   1 
ATOM   726  O  O   . ASP A 1 85  ? -6.044  14.398  11.044  1.00 22.97  ? 85  ASP A O   1 
ATOM   727  C  CB  . ASP A 1 85  ? -6.038  14.462  14.140  1.00 21.69  ? 85  ASP A CB  1 
ATOM   728  C  CG  . ASP A 1 85  ? -6.187  14.017  15.581  1.00 35.56  ? 85  ASP A CG  1 
ATOM   729  O  OD1 . ASP A 1 85  ? -7.233  13.459  15.971  1.00 36.93  ? 85  ASP A OD1 1 
ATOM   730  O  OD2 . ASP A 1 85  ? -5.229  14.249  16.338  1.00 50.10  ? 85  ASP A OD2 1 
ATOM   731  N  N   . GLY A 1 86  ? -8.078  15.174  11.446  1.00 24.53  ? 86  GLY A N   1 
ATOM   732  C  CA  . GLY A 1 86  ? -8.048  15.786  10.163  1.00 21.92  ? 86  GLY A CA  1 
ATOM   733  C  C   . GLY A 1 86  ? -8.341  14.840  8.965   1.00 18.28  ? 86  GLY A C   1 
ATOM   734  O  O   . GLY A 1 86  ? -8.861  13.709  9.087   1.00 26.49  ? 86  GLY A O   1 
ATOM   735  N  N   A THR A 1 87  ? -7.971  15.304  7.780   0.50 13.70  ? 87  THR A N   1 
ATOM   736  N  N   B THR A 1 87  ? -7.964  15.316  7.782   0.50 13.83  ? 87  THR A N   1 
ATOM   737  C  CA  A THR A 1 87  ? -8.365  14.637  6.528   0.50 13.44  ? 87  THR A CA  1 
ATOM   738  C  CA  B THR A 1 87  ? -8.389  14.717  6.497   0.50 14.37  ? 87  THR A CA  1 
ATOM   739  C  C   A THR A 1 87  ? -7.136  14.401  5.669   0.50 10.89  ? 87  THR A C   1 
ATOM   740  C  C   B THR A 1 87  ? -7.160  14.426  5.644   0.50 11.56  ? 87  THR A C   1 
ATOM   741  O  O   A THR A 1 87  ? -6.237  15.247  5.564   0.50 11.67  ? 87  THR A O   1 
ATOM   742  O  O   B THR A 1 87  ? -6.268  15.267  5.530   0.50 11.94  ? 87  THR A O   1 
ATOM   743  C  CB  A THR A 1 87  ? -9.383  15.535  5.806   0.50 13.79  ? 87  THR A CB  1 
ATOM   744  C  CB  B THR A 1 87  ? -9.319  15.707  5.738   0.50 18.48  ? 87  THR A CB  1 
ATOM   745  O  OG1 A THR A 1 87  ? -8.790  16.814  5.653   0.50 12.75  ? 87  THR A OG1 1 
ATOM   746  O  OG1 B THR A 1 87  ? -10.501 15.995  6.511   0.50 21.47  ? 87  THR A OG1 1 
ATOM   747  C  CG2 A THR A 1 87  ? -10.594 15.759  6.666   0.50 18.84  ? 87  THR A CG2 1 
ATOM   748  C  CG2 B THR A 1 87  ? -9.695  15.161  4.368   0.50 22.94  ? 87  THR A CG2 1 
ATOM   749  N  N   . TYR A 1 88  ? -7.178  13.262  5.021   1.00 9.56   ? 88  TYR A N   1 
ATOM   750  C  CA  . TYR A 1 88  ? -6.053  12.801  4.199   1.00 9.39   ? 88  TYR A CA  1 
ATOM   751  C  C   . TYR A 1 88  ? -6.592  12.502  2.826   1.00 9.58   ? 88  TYR A C   1 
ATOM   752  O  O   . TYR A 1 88  ? -7.586  11.789  2.655   1.00 13.34  ? 88  TYR A O   1 
ATOM   753  C  CB  . TYR A 1 88  ? -5.413  11.552  4.812   1.00 9.17   ? 88  TYR A CB  1 
ATOM   754  C  CG  . TYR A 1 88  ? -4.672  11.794  6.135   1.00 8.02   ? 88  TYR A CG  1 
ATOM   755  C  CD1 . TYR A 1 88  ? -5.320  12.104  7.311   1.00 9.47   ? 88  TYR A CD1 1 
ATOM   756  C  CD2 . TYR A 1 88  ? -3.273  11.650  6.149   1.00 7.94   ? 88  TYR A CD2 1 
ATOM   757  C  CE1 . TYR A 1 88  ? -4.633  12.317  8.493   1.00 9.75   ? 88  TYR A CE1 1 
ATOM   758  C  CE2 . TYR A 1 88  ? -2.582  11.797  7.352   1.00 7.57   ? 88  TYR A CE2 1 
ATOM   759  C  CZ  . TYR A 1 88  ? -3.267  12.099  8.517   1.00 8.36   ? 88  TYR A CZ  1 
ATOM   760  O  OH  . TYR A 1 88  ? -2.580  12.193  9.691   1.00 9.13   ? 88  TYR A OH  1 
ATOM   761  N  N   . ARG A 1 89  ? -5.912  13.017  1.820   1.00 8.54   ? 89  ARG A N   1 
ATOM   762  C  CA  . ARG A 1 89  ? -6.351  12.881  0.412   1.00 9.08   ? 89  ARG A CA  1 
ATOM   763  C  C   . ARG A 1 89  ? -5.566  11.812  -0.332  1.00 7.30   ? 89  ARG A C   1 
ATOM   764  O  O   . ARG A 1 89  ? -4.333  11.723  -0.250  1.00 8.02   ? 89  ARG A O   1 
ATOM   765  C  CB  . ARG A 1 89  ? -6.109  14.218  -0.254  1.00 11.68  ? 89  ARG A CB  1 
ATOM   766  C  CG  . ARG A 1 89  ? -6.830  14.344  -1.535  1.00 12.99  ? 89  ARG A CG  1 
ATOM   767  C  CD  . ARG A 1 89  ? -6.743  15.740  -2.092  1.00 13.13  ? 89  ARG A CD  1 
ATOM   768  N  NE  . ARG A 1 89  ? -7.381  16.766  -1.268  1.00 14.02  ? 89  ARG A NE  1 
ATOM   769  C  CZ  . ARG A 1 89  ? -7.232  18.079  -1.450  1.00 13.77  ? 89  ARG A CZ  1 
ATOM   770  N  NH1 . ARG A 1 89  ? -6.459  18.543  -2.428  1.00 15.79  ? 89  ARG A NH1 1 
ATOM   771  N  NH2 . ARG A 1 89  ? -7.859  18.927  -0.647  1.00 15.05  ? 89  ARG A NH2 1 
ATOM   772  N  N   . LEU A 1 90  ? -6.312  10.977  -1.070  1.00 8.37   ? 90  LEU A N   1 
ATOM   773  C  CA  . LEU A 1 90  ? -5.745  9.885   -1.845  1.00 8.72   ? 90  LEU A CA  1 
ATOM   774  C  C   . LEU A 1 90  ? -4.882  10.457  -2.995  1.00 8.76   ? 90  LEU A C   1 
ATOM   775  O  O   . LEU A 1 90  ? -5.358  11.296  -3.796  1.00 10.37  ? 90  LEU A O   1 
ATOM   776  C  CB  . LEU A 1 90  ? -6.830  9.053   -2.431  1.00 9.78   ? 90  LEU A CB  1 
ATOM   777  C  CG  . LEU A 1 90  ? -6.402  7.860   -3.321  1.00 10.46  ? 90  LEU A CG  1 
ATOM   778  C  CD1 . LEU A 1 90  ? -5.642  6.803   -2.514  1.00 11.47  ? 90  LEU A CD1 1 
ATOM   779  C  CD2 . LEU A 1 90  ? -7.640  7.207   -3.965  1.00 12.97  ? 90  LEU A CD2 1 
ATOM   780  N  N   . ILE A 1 91  ? -3.643  9.981   -3.103  1.00 8.88   ? 91  ILE A N   1 
ATOM   781  C  CA  . ILE A 1 91  ? -2.747  10.367  -4.178  1.00 8.68   ? 91  ILE A CA  1 
ATOM   782  C  C   . ILE A 1 91  ? -2.453  9.200   -5.122  1.00 8.43   ? 91  ILE A C   1 
ATOM   783  O  O   . ILE A 1 91  ? -2.344  9.374   -6.333  1.00 9.30   ? 91  ILE A O   1 
ATOM   784  C  CB  . ILE A 1 91  ? -1.479  11.063  -3.692  1.00 9.65   ? 91  ILE A CB  1 
ATOM   785  C  CG1 . ILE A 1 91  ? -0.590  11.487  -4.864  1.00 13.09  ? 91  ILE A CG1 1 
ATOM   786  C  CG2 . ILE A 1 91  ? -0.674  10.225  -2.673  1.00 9.85   ? 91  ILE A CG2 1 
ATOM   787  C  CD1 . ILE A 1 91  ? 0.490   12.487  -4.425  1.00 14.59  ? 91  ILE A CD1 1 
ATOM   788  N  N   . GLN A 1 92  ? -2.307  7.966   -4.599  1.00 7.78   ? 92  GLN A N   1 
ATOM   789  C  CA  . GLN A 1 92  ? -1.978  6.827   -5.442  1.00 8.69   ? 92  GLN A CA  1 
ATOM   790  C  C   . GLN A 1 92  ? -2.259  5.548   -4.679  1.00 8.19   ? 92  GLN A C   1 
ATOM   791  O  O   . GLN A 1 92  ? -2.330  5.564   -3.452  1.00 8.07   ? 92  GLN A O   1 
ATOM   792  C  CB  . GLN A 1 92  ? -0.519  6.804   -5.940  1.00 10.82  ? 92  GLN A CB  1 
ATOM   793  C  CG  . GLN A 1 92  ? 0.545   6.917   -4.838  1.00 10.41  ? 92  GLN A CG  1 
ATOM   794  C  CD  . GLN A 1 92  ? 1.244   5.604   -4.594  1.00 10.50  ? 92  GLN A CD  1 
ATOM   795  O  OE1 . GLN A 1 92  ? 0.666   4.520   -4.616  1.00 11.03  ? 92  GLN A OE1 1 
ATOM   796  N  NE2 . GLN A 1 92  ? 2.499   5.708   -4.267  1.00 13.16  ? 92  GLN A NE2 1 
ATOM   797  N  N   . PHE A 1 93  ? -2.429  4.460   -5.429  1.00 8.32   ? 93  PHE A N   1 
ATOM   798  C  CA  . PHE A 1 93  ? -2.308  3.145   -4.849  1.00 7.45   ? 93  PHE A CA  1 
ATOM   799  C  C   . PHE A 1 93  ? -1.349  2.301   -5.626  1.00 7.55   ? 93  PHE A C   1 
ATOM   800  O  O   . PHE A 1 93  ? -1.106  2.519   -6.808  1.00 9.49   ? 93  PHE A O   1 
ATOM   801  C  CB  . PHE A 1 93  ? -3.671  2.458   -4.607  1.00 9.15   ? 93  PHE A CB  1 
ATOM   802  C  CG  . PHE A 1 93  ? -4.402  2.002   -5.849  1.00 9.14   ? 93  PHE A CG  1 
ATOM   803  C  CD1 . PHE A 1 93  ? -4.056  0.816   -6.531  1.00 10.44  ? 93  PHE A CD1 1 
ATOM   804  C  CD2 . PHE A 1 93  ? -5.530  2.685   -6.273  1.00 10.76  ? 93  PHE A CD2 1 
ATOM   805  C  CE1 . PHE A 1 93  ? -4.740  0.408   -7.649  1.00 11.56  ? 93  PHE A CE1 1 
ATOM   806  C  CE2 . PHE A 1 93  ? -6.223  2.248   -7.392  1.00 12.31  ? 93  PHE A CE2 1 
ATOM   807  C  CZ  . PHE A 1 93  ? -5.829  1.123   -8.093  1.00 13.13  ? 93  PHE A CZ  1 
ATOM   808  N  N   . HIS A 1 94  ? -0.844  1.254   -4.951  1.00 7.91   ? 94  HIS A N   1 
ATOM   809  C  CA  . HIS A 1 94  ? 0.042   0.272   -5.545  1.00 7.49   ? 94  HIS A CA  1 
ATOM   810  C  C   . HIS A 1 94  ? -0.051  -1.003  -4.719  1.00 6.51   ? 94  HIS A C   1 
ATOM   811  O  O   . HIS A 1 94  ? -0.667  -1.022  -3.680  1.00 7.03   ? 94  HIS A O   1 
ATOM   812  C  CB  . HIS A 1 94  ? 1.493   0.766   -5.598  1.00 8.43   ? 94  HIS A CB  1 
ATOM   813  C  CG  . HIS A 1 94  ? 2.029   1.072   -4.227  1.00 7.85   ? 94  HIS A CG  1 
ATOM   814  N  ND1 . HIS A 1 94  ? 1.810   2.251   -3.590  1.00 7.76   ? 94  HIS A ND1 1 
ATOM   815  C  CD2 . HIS A 1 94  ? 2.630   0.240   -3.325  1.00 7.88   ? 94  HIS A CD2 1 
ATOM   816  C  CE1 . HIS A 1 94  ? 2.291   2.129   -2.335  1.00 7.27   ? 94  HIS A CE1 1 
ATOM   817  N  NE2 . HIS A 1 94  ? 2.797   0.894   -2.151  1.00 6.71   ? 94  HIS A NE2 1 
ATOM   818  N  N   . PHE A 1 95  ? 0.636   -2.034  -5.200  1.00 7.66   ? 95  PHE A N   1 
ATOM   819  C  CA  . PHE A 1 95  ? 0.666   -3.327  -4.523  1.00 7.32   ? 95  PHE A CA  1 
ATOM   820  C  C   . PHE A 1 95  ? 2.126   -3.757  -4.309  1.00 7.59   ? 95  PHE A C   1 
ATOM   821  O  O   . PHE A 1 95  ? 3.033   -3.298  -4.997  1.00 7.79   ? 95  PHE A O   1 
ATOM   822  C  CB  . PHE A 1 95  ? -0.051  -4.403  -5.371  1.00 8.16   ? 95  PHE A CB  1 
ATOM   823  C  CG  . PHE A 1 95  ? -1.497  -4.127  -5.688  1.00 7.48   ? 95  PHE A CG  1 
ATOM   824  C  CD1 . PHE A 1 95  ? -1.831  -3.237  -6.740  1.00 9.12   ? 95  PHE A CD1 1 
ATOM   825  C  CD2 . PHE A 1 95  ? -2.514  -4.753  -5.000  1.00 8.17   ? 95  PHE A CD2 1 
ATOM   826  C  CE1 . PHE A 1 95  ? -3.137  -3.039  -7.092  1.00 9.68   ? 95  PHE A CE1 1 
ATOM   827  C  CE2 . PHE A 1 95  ? -3.851  -4.567  -5.364  1.00 9.07   ? 95  PHE A CE2 1 
ATOM   828  C  CZ  . PHE A 1 95  ? -4.141  -3.691  -6.404  1.00 10.13  ? 95  PHE A CZ  1 
ATOM   829  N  N   . HIS A 1 96  ? 2.255   -4.734  -3.411  1.00 7.00   ? 96  HIS A N   1 
ATOM   830  C  CA  . HIS A 1 96  ? 3.443   -5.543  -3.233  1.00 7.13   ? 96  HIS A CA  1 
ATOM   831  C  C   . HIS A 1 96  ? 3.026   -6.993  -3.355  1.00 6.97   ? 96  HIS A C   1 
ATOM   832  O  O   . HIS A 1 96  ? 1.943   -7.349  -2.857  1.00 7.12   ? 96  HIS A O   1 
ATOM   833  C  CB  . HIS A 1 96  ? 4.092   -5.317  -1.857  1.00 7.82   ? 96  HIS A CB  1 
ATOM   834  C  CG  . HIS A 1 96  ? 4.404   -3.860  -1.577  1.00 7.28   ? 96  HIS A CG  1 
ATOM   835  N  ND1 . HIS A 1 96  ? 5.630   -3.330  -1.725  1.00 8.33   ? 96  HIS A ND1 1 
ATOM   836  C  CD2 . HIS A 1 96  ? 3.588   -2.841  -1.168  1.00 6.89   ? 96  HIS A CD2 1 
ATOM   837  C  CE1 . HIS A 1 96  ? 5.561   -1.997  -1.402  1.00 8.09   ? 96  HIS A CE1 1 
ATOM   838  N  NE2 . HIS A 1 96  ? 4.309   -1.695  -1.073  1.00 7.21   ? 96  HIS A NE2 1 
ATOM   839  N  N   . TRP A 1 97  ? 3.805   -7.839  -4.019  1.00 6.95   ? 97  TRP A N   1 
ATOM   840  C  CA  . TRP A 1 97  ? 3.393   -9.224  -4.236  1.00 7.60   ? 97  TRP A CA  1 
ATOM   841  C  C   . TRP A 1 97  ? 4.577   -10.126 -4.384  1.00 7.07   ? 97  TRP A C   1 
ATOM   842  O  O   . TRP A 1 97  ? 5.749   -9.702  -4.467  1.00 7.93   ? 97  TRP A O   1 
ATOM   843  C  CB  . TRP A 1 97  ? 2.463   -9.315  -5.503  1.00 8.42   ? 97  TRP A CB  1 
ATOM   844  C  CG  . TRP A 1 97  ? 3.143   -8.931  -6.793  1.00 7.83   ? 97  TRP A CG  1 
ATOM   845  C  CD1 . TRP A 1 97  ? 3.826   -9.767  -7.623  1.00 9.98   ? 97  TRP A CD1 1 
ATOM   846  C  CD2 . TRP A 1 97  ? 3.201   -7.639  -7.349  1.00 9.12   ? 97  TRP A CD2 1 
ATOM   847  N  NE1 . TRP A 1 97  ? 4.236   -9.041  -8.740  1.00 10.44  ? 97  TRP A NE1 1 
ATOM   848  C  CE2 . TRP A 1 97  ? 3.937   -7.733  -8.570  1.00 10.09  ? 97  TRP A CE2 1 
ATOM   849  C  CE3 . TRP A 1 97  ? 2.717   -6.363  -6.943  1.00 8.53   ? 97  TRP A CE3 1 
ATOM   850  C  CZ2 . TRP A 1 97  ? 4.093   -6.626  -9.423  1.00 10.94  ? 97  TRP A CZ2 1 
ATOM   851  C  CZ3 . TRP A 1 97  ? 2.918   -5.256  -7.783  1.00 9.82   ? 97  TRP A CZ3 1 
ATOM   852  C  CH2 . TRP A 1 97  ? 3.594   -5.412  -8.992  1.00 11.16  ? 97  TRP A CH2 1 
ATOM   853  N  N   . GLY A 1 98  ? 4.283   -11.434 -4.362  1.00 7.87   ? 98  GLY A N   1 
ATOM   854  C  CA  . GLY A 1 98  ? 5.321   -12.467 -4.331  1.00 8.24   ? 98  GLY A CA  1 
ATOM   855  C  C   . GLY A 1 98  ? 5.530   -13.126 -5.659  1.00 9.30   ? 98  GLY A C   1 
ATOM   856  O  O   . GLY A 1 98  ? 4.800   -12.996 -6.632  1.00 10.17  ? 98  GLY A O   1 
ATOM   857  N  N   . SER A 1 99  ? 6.582   -13.979 -5.660  1.00 9.59   ? 99  SER A N   1 
ATOM   858  C  CA  . SER A 1 99  ? 6.793   -14.934 -6.761  1.00 11.26  ? 99  SER A CA  1 
ATOM   859  C  C   . SER A 1 99  ? 5.885   -16.173 -6.664  1.00 11.31  ? 99  SER A C   1 
ATOM   860  O  O   . SER A 1 99  ? 5.781   -16.893 -7.668  1.00 13.14  ? 99  SER A O   1 
ATOM   861  C  CB  . SER A 1 99  ? 8.290   -15.295 -6.822  1.00 12.85  ? 99  SER A CB  1 
ATOM   862  O  OG  . SER A 1 99  ? 8.688   -15.805 -5.569  1.00 12.26  ? 99  SER A OG  1 
ATOM   863  N  N   . LEU A 1 100 ? 5.312   -16.392 -5.487  1.00 10.79  ? 100 LEU A N   1 
ATOM   864  C  CA  . LEU A 1 100 ? 4.498   -17.538 -5.147  1.00 12.49  ? 100 LEU A CA  1 
ATOM   865  C  C   . LEU A 1 100 ? 3.396   -17.084 -4.300  1.00 10.59  ? 100 LEU A C   1 
ATOM   866  O  O   . LEU A 1 100 ? 3.567   -16.053 -3.630  1.00 10.50  ? 100 LEU A O   1 
ATOM   867  C  CB  . LEU A 1 100 ? 5.355   -18.562 -4.272  1.00 19.59  ? 100 LEU A CB  1 
ATOM   868  C  CG  . LEU A 1 100 ? 6.717   -18.901 -4.857  1.00 20.09  ? 100 LEU A CG  1 
ATOM   869  C  CD1 . LEU A 1 100 ? 7.696   -19.416 -3.804  1.00 32.06  ? 100 LEU A CD1 1 
ATOM   870  C  CD2 . LEU A 1 100 ? 6.394   -19.975 -5.874  1.00 28.40  ? 100 LEU A CD2 1 
ATOM   871  N  N   . ASP A 1 101 ? 2.279   -17.829 -4.246  1.00 10.37  ? 101 ASP A N   1 
ATOM   872  C  CA  . ASP A 1 101 ? 1.124   -17.351 -3.461  1.00 10.57  ? 101 ASP A CA  1 
ATOM   873  C  C   . ASP A 1 101 ? 1.414   -17.266 -1.969  1.00 9.87   ? 101 ASP A C   1 
ATOM   874  O  O   . ASP A 1 101 ? 0.753   -16.547 -1.267  1.00 11.71  ? 101 ASP A O   1 
ATOM   875  C  CB  . ASP A 1 101 ? -0.085  -18.244 -3.694  1.00 11.79  ? 101 ASP A CB  1 
ATOM   876  C  CG  . ASP A 1 101 ? -0.578  -18.301 -5.128  1.00 12.49  ? 101 ASP A CG  1 
ATOM   877  O  OD1 . ASP A 1 101 ? -0.273  -17.427 -5.956  1.00 13.69  ? 101 ASP A OD1 1 
ATOM   878  O  OD2 . ASP A 1 101 ? -1.427  -19.152 -5.353  1.00 17.09  ? 101 ASP A OD2 1 
ATOM   879  N  N   . GLY A 1 102 ? 2.421   -18.038 -1.512  1.00 11.10  ? 102 GLY A N   1 
ATOM   880  C  CA  . GLY A 1 102 ? 2.737   -18.023 -0.063  1.00 10.63  ? 102 GLY A CA  1 
ATOM   881  C  C   . GLY A 1 102 ? 3.538   -16.869 0.477   1.00 9.74   ? 102 GLY A C   1 
ATOM   882  O  O   . GLY A 1 102 ? 3.854   -16.876 1.656   1.00 10.70  ? 102 GLY A O   1 
ATOM   883  N  N   . GLN A 1 103 ? 3.827   -15.872 -0.315  1.00 8.93   ? 103 GLN A N   1 
ATOM   884  C  CA  . GLN A 1 103 ? 4.487   -14.695 0.175   1.00 8.63   ? 103 GLN A CA  1 
ATOM   885  C  C   . GLN A 1 103 ? 4.130   -13.536 -0.696  1.00 7.85   ? 103 GLN A C   1 
ATOM   886  O  O   . GLN A 1 103 ? 3.593   -13.735 -1.787  1.00 8.42   ? 103 GLN A O   1 
ATOM   887  C  CB  . GLN A 1 103 ? 6.038   -14.900 0.198   1.00 10.07  ? 103 GLN A CB  1 
ATOM   888  C  CG  . GLN A 1 103 ? 6.594   -15.091 -1.196  1.00 11.34  ? 103 GLN A CG  1 
ATOM   889  C  CD  . GLN A 1 103 ? 8.015   -15.660 -1.135  1.00 13.19  ? 103 GLN A CD  1 
ATOM   890  O  OE1 . GLN A 1 103 ? 8.260   -16.559 -0.330  1.00 23.73  ? 103 GLN A OE1 1 
ATOM   891  N  NE2 . GLN A 1 103 ? 8.921   -15.211 -1.963  1.00 14.42  ? 103 GLN A NE2 1 
ATOM   892  N  N   . GLY A 1 104 ? 4.418   -12.314 -0.242  1.00 7.22   ? 104 GLY A N   1 
ATOM   893  C  CA  . GLY A 1 104 ? 4.114   -11.132 -1.016  1.00 7.05   ? 104 GLY A CA  1 
ATOM   894  C  C   . GLY A 1 104 ? 3.706   -9.953  -0.180  1.00 7.46   ? 104 GLY A C   1 
ATOM   895  O  O   . GLY A 1 104 ? 3.963   -8.809  -0.538  1.00 7.86   ? 104 GLY A O   1 
ATOM   896  N  N   . SER A 1 105 ? 2.967   -10.209 0.923   1.00 6.81   ? 105 SER A N   1 
ATOM   897  C  CA  . SER A 1 105 ? 2.591   -9.085  1.797   1.00 6.85   ? 105 SER A CA  1 
ATOM   898  C  C   . SER A 1 105 ? 3.781   -8.527  2.531   1.00 6.42   ? 105 SER A C   1 
ATOM   899  O  O   . SER A 1 105 ? 4.819   -9.202  2.752   1.00 7.54   ? 105 SER A O   1 
ATOM   900  C  CB  . SER A 1 105 ? 1.447   -9.450  2.730   1.00 6.96   ? 105 SER A CB  1 
ATOM   901  O  OG  . SER A 1 105 ? 1.798   -10.387 3.703   1.00 7.22   ? 105 SER A OG  1 
ATOM   902  N  N   . GLU A 1 106 ? 3.659   -7.260  2.933   1.00 6.48   ? 106 GLU A N   1 
ATOM   903  C  CA  . GLU A 1 106 ? 4.660   -6.578  3.755   1.00 6.56   ? 106 GLU A CA  1 
ATOM   904  C  C   . GLU A 1 106 ? 4.301   -6.761  5.228   1.00 6.88   ? 106 GLU A C   1 
ATOM   905  O  O   . GLU A 1 106 ? 5.114   -7.320  6.012   1.00 7.21   ? 106 GLU A O   1 
ATOM   906  C  CB  . GLU A 1 106 ? 4.729   -5.087  3.333   1.00 6.95   ? 106 GLU A CB  1 
ATOM   907  C  CG  . GLU A 1 106 ? 5.182   -4.975  1.898   1.00 9.16   ? 106 GLU A CG  1 
ATOM   908  C  CD  . GLU A 1 106 ? 5.868   -3.711  1.615   1.00 7.38   ? 106 GLU A CD  1 
ATOM   909  O  OE1 . GLU A 1 106 ? 5.274   -2.626  1.887   1.00 7.40   ? 106 GLU A OE1 1 
ATOM   910  O  OE2 . GLU A 1 106 ? 7.037   -3.754  1.147   1.00 8.69   ? 106 GLU A OE2 1 
ATOM   911  N  N   . HIS A 1 107 ? 3.134   -6.290  5.663   1.00 6.41   ? 107 HIS A N   1 
ATOM   912  C  CA  . HIS A 1 107 ? 2.670   -6.692  6.970   1.00 6.40   ? 107 HIS A CA  1 
ATOM   913  C  C   . HIS A 1 107 ? 2.371   -8.175  6.999   1.00 6.29   ? 107 HIS A C   1 
ATOM   914  O  O   . HIS A 1 107 ? 2.040   -8.780  5.967   1.00 6.70   ? 107 HIS A O   1 
ATOM   915  C  CB  . HIS A 1 107 ? 1.415   -5.888  7.357   1.00 6.70   ? 107 HIS A CB  1 
ATOM   916  C  CG  . HIS A 1 107 ? 1.731   -4.409  7.512   1.00 6.15   ? 107 HIS A CG  1 
ATOM   917  N  ND1 . HIS A 1 107 ? 1.693   -3.530  6.458   1.00 6.64   ? 107 HIS A ND1 1 
ATOM   918  C  CD2 . HIS A 1 107 ? 2.234   -3.716  8.590   1.00 6.49   ? 107 HIS A CD2 1 
ATOM   919  C  CE1 . HIS A 1 107 ? 2.135   -2.344  6.898   1.00 6.80   ? 107 HIS A CE1 1 
ATOM   920  N  NE2 . HIS A 1 107 ? 2.461   -2.406  8.186   1.00 7.01   ? 107 HIS A NE2 1 
ATOM   921  N  N   . THR A 1 108 ? 2.512   -8.746  8.190   1.00 6.96   ? 108 THR A N   1 
ATOM   922  C  CA  . THR A 1 108 ? 2.152   -10.112 8.460   1.00 7.27   ? 108 THR A CA  1 
ATOM   923  C  C   . THR A 1 108 ? 1.206   -10.132 9.665   1.00 7.14   ? 108 THR A C   1 
ATOM   924  O  O   . THR A 1 108 ? 1.204   -9.155  10.448  1.00 7.35   ? 108 THR A O   1 
ATOM   925  C  CB  . THR A 1 108 ? 3.376   -11.038 8.627   1.00 8.35   ? 108 THR A CB  1 
ATOM   926  O  OG1 . THR A 1 108 ? 4.233   -10.551 9.675   1.00 8.55   ? 108 THR A OG1 1 
ATOM   927  C  CG2 . THR A 1 108 ? 4.148   -11.075 7.356   1.00 8.21   ? 108 THR A CG2 1 
ATOM   928  N  N   . VAL A 1 109 ? 0.433   -11.214 9.809   1.00 7.68   ? 109 VAL A N   1 
ATOM   929  C  CA  . VAL A 1 109 ? -0.566  -11.292 10.894  1.00 7.93   ? 109 VAL A CA  1 
ATOM   930  C  C   . VAL A 1 109 ? -0.229  -12.582 11.641  1.00 7.96   ? 109 VAL A C   1 
ATOM   931  O  O   . VAL A 1 109 ? -0.388  -13.686 11.089  1.00 8.41   ? 109 VAL A O   1 
ATOM   932  C  CB  . VAL A 1 109 ? -2.011  -11.313 10.341  1.00 8.29   ? 109 VAL A CB  1 
ATOM   933  C  CG1 . VAL A 1 109 ? -2.995  -11.414 11.495  1.00 10.36  ? 109 VAL A CG1 1 
ATOM   934  C  CG2 . VAL A 1 109 ? -2.270  -10.063 9.499   1.00 9.77   ? 109 VAL A CG2 1 
ATOM   935  N  N   . ASP A 1 110 ? 0.316   -12.470 12.860  1.00 9.34   ? 110 ASP A N   1 
ATOM   936  C  CA  . ASP A 1 110 ? 0.787   -13.694 13.571  1.00 9.57   ? 110 ASP A CA  1 
ATOM   937  C  C   . ASP A 1 110 ? 1.717   -14.501 12.677  1.00 9.61   ? 110 ASP A C   1 
ATOM   938  O  O   . ASP A 1 110 ? 1.636   -15.719 12.610  1.00 10.25  ? 110 ASP A O   1 
ATOM   939  C  CB  . ASP A 1 110 ? -0.403  -14.519 14.067  1.00 12.30  ? 110 ASP A CB  1 
ATOM   940  C  CG  . ASP A 1 110 ? -1.229  -13.743 15.091  1.00 13.96  ? 110 ASP A CG  1 
ATOM   941  O  OD1 . ASP A 1 110 ? -0.649  -12.885 15.818  1.00 15.17  ? 110 ASP A OD1 1 
ATOM   942  O  OD2 . ASP A 1 110 ? -2.391  -14.011 15.220  1.00 15.63  ? 110 ASP A OD2 1 
ATOM   943  N  N   . LYS A 1 111 ? 2.597   -13.778 11.949  1.00 8.99   ? 111 LYS A N   1 
ATOM   944  C  CA  . LYS A 1 111 ? 3.596   -14.314 11.046  1.00 9.30   ? 111 LYS A CA  1 
ATOM   945  C  C   . LYS A 1 111 ? 3.022   -14.826 9.701   1.00 8.80   ? 111 LYS A C   1 
ATOM   946  O  O   . LYS A 1 111 ? 3.817   -15.228 8.837   1.00 10.33  ? 111 LYS A O   1 
ATOM   947  C  CB  . LYS A 1 111 ? 4.536   -15.372 11.667  1.00 11.91  ? 111 LYS A CB  1 
ATOM   948  C  CG  . LYS A 1 111 ? 5.256   -14.830 12.924  1.00 15.26  ? 111 LYS A CG  1 
ATOM   949  C  CD  . LYS A 1 111 ? 6.181   -13.609 12.602  1.00 18.03  ? 111 LYS A CD  1 
ATOM   950  C  CE  . LYS A 1 111 ? 6.987   -12.982 13.775  1.00 22.41  ? 111 LYS A CE  1 
ATOM   951  N  NZ  . LYS A 1 111 ? 8.106   -13.867 13.998  1.00 23.16  ? 111 LYS A NZ  1 
ATOM   952  N  N   . LYS A 1 112 ? 1.698   -14.807 9.529   1.00 8.47   ? 112 LYS A N   1 
ATOM   953  C  CA  . LYS A 1 112 ? 1.123   -15.196 8.239   1.00 8.87   ? 112 LYS A CA  1 
ATOM   954  C  C   . LYS A 1 112 ? 1.457   -14.150 7.184   1.00 7.86   ? 112 LYS A C   1 
ATOM   955  O  O   . LYS A 1 112 ? 1.229   -12.940 7.385   1.00 8.06   ? 112 LYS A O   1 
ATOM   956  C  CB  . LYS A 1 112 ? -0.424  -15.278 8.336   1.00 9.99   ? 112 LYS A CB  1 
ATOM   957  C  CG  . LYS A 1 112 ? -1.118  -15.638 7.030   1.00 10.58  ? 112 LYS A CG  1 
ATOM   958  C  CD  . LYS A 1 112 ? -2.592  -15.551 7.116   1.00 12.61  ? 112 LYS A CD  1 
ATOM   959  C  CE  . LYS A 1 112 ? -3.238  -15.767 5.791   1.00 12.82  ? 112 LYS A CE  1 
ATOM   960  N  NZ  . LYS A 1 112 ? -3.087  -17.084 5.349   1.00 13.15  ? 112 LYS A NZ  1 
ATOM   961  N  N   A LYS A 1 113 ? 1.961   -14.631 6.038   0.50 7.75   ? 113 LYS A N   1 
ATOM   962  N  N   B LYS A 1 113 ? 1.972   -14.639 6.049   0.50 7.85   ? 113 LYS A N   1 
ATOM   963  C  CA  A LYS A 1 113 ? 2.167   -13.833 4.846   0.50 7.77   ? 113 LYS A CA  1 
ATOM   964  C  CA  B LYS A 1 113 ? 2.178   -13.851 4.851   0.50 7.75   ? 113 LYS A CA  1 
ATOM   965  C  C   A LYS A 1 113 ? 1.032   -14.072 3.882   0.50 7.50   ? 113 LYS A C   1 
ATOM   966  C  C   B LYS A 1 113 ? 1.048   -14.073 3.871   0.50 7.49   ? 113 LYS A C   1 
ATOM   967  O  O   A LYS A 1 113 ? 0.657   -15.221 3.594   0.50 9.79   ? 113 LYS A O   1 
ATOM   968  O  O   B LYS A 1 113 ? 0.694   -15.220 3.561   0.50 9.90   ? 113 LYS A O   1 
ATOM   969  C  CB  A LYS A 1 113 ? 3.483   -14.227 4.166   0.50 8.34   ? 113 LYS A CB  1 
ATOM   970  C  CB  B LYS A 1 113 ? 3.488   -14.259 4.168   0.50 8.52   ? 113 LYS A CB  1 
ATOM   971  C  CG  A LYS A 1 113 ? 4.746   -13.927 4.953   0.50 9.71   ? 113 LYS A CG  1 
ATOM   972  C  CG  B LYS A 1 113 ? 4.746   -13.938 4.944   0.50 9.66   ? 113 LYS A CG  1 
ATOM   973  C  CD  A LYS A 1 113 ? 5.942   -14.532 4.251   0.50 11.51  ? 113 LYS A CD  1 
ATOM   974  C  CD  B LYS A 1 113 ? 5.979   -14.466 4.251   0.50 11.55  ? 113 LYS A CD  1 
ATOM   975  C  CE  A LYS A 1 113 ? 7.261   -14.023 4.834   0.50 13.60  ? 113 LYS A CE  1 
ATOM   976  C  CE  B LYS A 1 113 ? 7.206   -13.952 5.014   0.50 14.45  ? 113 LYS A CE  1 
ATOM   977  N  NZ  A LYS A 1 113 ? 7.598   -14.774 6.048   0.50 14.60  ? 113 LYS A NZ  1 
ATOM   978  N  NZ  B LYS A 1 113 ? 8.450   -14.727 4.840   0.50 17.63  ? 113 LYS A NZ  1 
ATOM   979  N  N   . TYR A 1 114 ? 0.476   -12.966 3.376   1.00 7.04   ? 114 TYR A N   1 
ATOM   980  C  CA  . TYR A 1 114 ? -0.519  -13.023 2.326   1.00 7.81   ? 114 TYR A CA  1 
ATOM   981  C  C   . TYR A 1 114 ? 0.179   -12.977 0.955   1.00 7.13   ? 114 TYR A C   1 
ATOM   982  O  O   . TYR A 1 114 ? 1.375   -12.700 0.838   1.00 7.77   ? 114 TYR A O   1 
ATOM   983  C  CB  . TYR A 1 114 ? -1.544  -11.903 2.486   1.00 7.57   ? 114 TYR A CB  1 
ATOM   984  C  CG  . TYR A 1 114 ? -2.491  -12.131 3.635   1.00 7.37   ? 114 TYR A CG  1 
ATOM   985  C  CD1 . TYR A 1 114 ? -2.205  -11.705 4.952   1.00 9.03   ? 114 TYR A CD1 1 
ATOM   986  C  CD2 . TYR A 1 114 ? -3.705  -12.742 3.384   1.00 8.67   ? 114 TYR A CD2 1 
ATOM   987  C  CE1 . TYR A 1 114 ? -3.139  -11.894 5.981   1.00 10.77  ? 114 TYR A CE1 1 
ATOM   988  C  CE2 . TYR A 1 114 ? -4.701  -12.895 4.366   1.00 10.79  ? 114 TYR A CE2 1 
ATOM   989  C  CZ  . TYR A 1 114 ? -4.385  -12.458 5.667   1.00 11.35  ? 114 TYR A CZ  1 
ATOM   990  O  OH  . TYR A 1 114 ? -5.265  -12.631 6.738   1.00 15.76  ? 114 TYR A OH  1 
ATOM   991  N  N   . ALA A 1 115 ? -0.594  -13.292 -0.097  1.00 7.34   ? 115 ALA A N   1 
ATOM   992  C  CA  . ALA A 1 115 ? -0.056  -13.317 -1.451  1.00 7.40   ? 115 ALA A CA  1 
ATOM   993  C  C   . ALA A 1 115 ? 0.332   -11.920 -1.943  1.00 7.63   ? 115 ALA A C   1 
ATOM   994  O  O   . ALA A 1 115 ? 1.163   -11.782 -2.817  1.00 8.09   ? 115 ALA A O   1 
ATOM   995  C  CB  . ALA A 1 115 ? -1.096  -13.932 -2.400  1.00 9.30   ? 115 ALA A CB  1 
ATOM   996  N  N   . ALA A 1 116 ? -0.326  -10.867 -1.412  1.00 6.87   ? 116 ALA A N   1 
ATOM   997  C  CA  . ALA A 1 116 ? -0.023  -9.515  -1.852  1.00 6.81   ? 116 ALA A CA  1 
ATOM   998  C  C   . ALA A 1 116 ? -0.626  -8.572  -0.832  1.00 6.75   ? 116 ALA A C   1 
ATOM   999  O  O   . ALA A 1 116 ? -1.370  -8.967  0.066   1.00 6.80   ? 116 ALA A O   1 
ATOM   1000 C  CB  . ALA A 1 116 ? -0.545  -9.261  -3.286  1.00 8.09   ? 116 ALA A CB  1 
ATOM   1001 N  N   . GLU A 1 117 ? -0.316  -7.281  -1.026  1.00 6.74   ? 117 GLU A N   1 
ATOM   1002 C  CA  . GLU A 1 117 ? -0.822  -6.229  -0.145  1.00 6.21   ? 117 GLU A CA  1 
ATOM   1003 C  C   . GLU A 1 117 ? -0.991  -4.965  -0.979  1.00 6.95   ? 117 GLU A C   1 
ATOM   1004 O  O   . GLU A 1 117 ? -0.089  -4.572  -1.719  1.00 8.00   ? 117 GLU A O   1 
ATOM   1005 C  CB  . GLU A 1 117 ? 0.150   -6.007  1.028   1.00 7.05   ? 117 GLU A CB  1 
ATOM   1006 C  CG  . GLU A 1 117 ? -0.377  -5.052  2.115   1.00 7.44   ? 117 GLU A CG  1 
ATOM   1007 C  CD  . GLU A 1 117 ? 0.540   -4.992  3.322   1.00 6.53   ? 117 GLU A CD  1 
ATOM   1008 O  OE1 . GLU A 1 117 ? 1.200   -6.008  3.612   1.00 7.55   ? 117 GLU A OE1 1 
ATOM   1009 O  OE2 . GLU A 1 117 ? 0.567   -3.916  3.988   1.00 7.53   ? 117 GLU A OE2 1 
ATOM   1010 N  N   . LEU A 1 118 ? -2.200  -4.385  -0.876  1.00 6.43   ? 118 LEU A N   1 
ATOM   1011 C  CA  . LEU A 1 118 ? -2.551  -3.139  -1.529  1.00 6.61   ? 118 LEU A CA  1 
ATOM   1012 C  C   . LEU A 1 118 ? -2.347  -1.994  -0.525  1.00 6.56   ? 118 LEU A C   1 
ATOM   1013 O  O   . LEU A 1 118 ? -2.742  -2.072  0.619   1.00 6.06   ? 118 LEU A O   1 
ATOM   1014 C  CB  . LEU A 1 118 ? -4.041  -3.241  -1.882  1.00 7.83   ? 118 LEU A CB  1 
ATOM   1015 C  CG  . LEU A 1 118 ? -4.787  -1.940  -2.240  1.00 7.96   ? 118 LEU A CG  1 
ATOM   1016 C  CD1 . LEU A 1 118 ? -4.182  -1.262  -3.478  1.00 8.63   ? 118 LEU A CD1 1 
ATOM   1017 C  CD2 . LEU A 1 118 ? -6.252  -2.288  -2.514  1.00 9.50   ? 118 LEU A CD2 1 
ATOM   1018 N  N   . HIS A 1 119 ? -1.701  -0.919  -1.023  1.00 6.47   ? 119 HIS A N   1 
ATOM   1019 C  CA  . HIS A 1 119 ? -1.474  0.305   -0.245  1.00 5.94   ? 119 HIS A CA  1 
ATOM   1020 C  C   . HIS A 1 119 ? -2.142  1.461   -0.932  1.00 5.92   ? 119 HIS A C   1 
ATOM   1021 O  O   . HIS A 1 119 ? -1.767  1.826   -2.048  1.00 6.99   ? 119 HIS A O   1 
ATOM   1022 C  CB  . HIS A 1 119 ? 0.029   0.568   -0.142  1.00 6.53   ? 119 HIS A CB  1 
ATOM   1023 C  CG  . HIS A 1 119 ? 0.719   -0.421  0.746   1.00 5.93   ? 119 HIS A CG  1 
ATOM   1024 N  ND1 . HIS A 1 119 ? 2.087   -0.636  0.737   1.00 6.03   ? 119 HIS A ND1 1 
ATOM   1025 C  CD2 . HIS A 1 119 ? 0.187   -1.233  1.711   1.00 6.49   ? 119 HIS A CD2 1 
ATOM   1026 C  CE1 . HIS A 1 119 ? 2.341   -1.586  1.665   1.00 6.91   ? 119 HIS A CE1 1 
ATOM   1027 N  NE2 . HIS A 1 119 ? 1.219   -1.940  2.273   1.00 6.54   ? 119 HIS A NE2 1 
ATOM   1028 N  N   . LEU A 1 120 ? -3.140  2.037   -0.245  1.00 6.07   ? 120 LEU A N   1 
ATOM   1029 C  CA  . LEU A 1 120 ? -3.800  3.303   -0.704  1.00 6.92   ? 120 LEU A CA  1 
ATOM   1030 C  C   . LEU A 1 120 ? -3.166  4.423   0.098   1.00 5.75   ? 120 LEU A C   1 
ATOM   1031 O  O   . LEU A 1 120 ? -3.269  4.456   1.306   1.00 6.32   ? 120 LEU A O   1 
ATOM   1032 C  CB  . LEU A 1 120 ? -5.312  3.183   -0.489  1.00 7.32   ? 120 LEU A CB  1 
ATOM   1033 C  CG  . LEU A 1 120 ? -5.979  2.123   -1.391  1.00 8.89   ? 120 LEU A CG  1 
ATOM   1034 C  CD1 . LEU A 1 120 ? -6.887  1.225   -0.576  1.00 12.35  ? 120 LEU A CD1 1 
ATOM   1035 C  CD2 . LEU A 1 120 ? -6.808  2.810   -2.485  1.00 10.75  ? 120 LEU A CD2 1 
ATOM   1036 N  N   . VAL A 1 121 ? -2.451  5.297   -0.619  1.00 6.33   ? 121 VAL A N   1 
ATOM   1037 C  CA  . VAL A 1 121 ? -1.597  6.304   0.019   1.00 6.72   ? 121 VAL A CA  1 
ATOM   1038 C  C   . VAL A 1 121 ? -2.296  7.666   0.043   1.00 6.32   ? 121 VAL A C   1 
ATOM   1039 O  O   . VAL A 1 121 ? -2.716  8.141   -1.011  1.00 7.17   ? 121 VAL A O   1 
ATOM   1040 C  CB  . VAL A 1 121 ? -0.272  6.411   -0.783  1.00 7.17   ? 121 VAL A CB  1 
ATOM   1041 C  CG1 . VAL A 1 121 ? 0.668   7.440   -0.160  1.00 8.63   ? 121 VAL A CG1 1 
ATOM   1042 C  CG2 . VAL A 1 121 ? 0.373   5.022   -0.940  1.00 8.05   ? 121 VAL A CG2 1 
ATOM   1043 N  N   . HIS A 1 122 ? -2.378  8.255   1.216   1.00 6.48   ? 122 HIS A N   1 
ATOM   1044 C  CA  . HIS A 1 122 ? -3.078  9.523   1.407   1.00 6.87   ? 122 HIS A CA  1 
ATOM   1045 C  C   . HIS A 1 122 ? -2.192  10.513  2.170   1.00 7.12   ? 122 HIS A C   1 
ATOM   1046 O  O   . HIS A 1 122 ? -1.440  10.107  3.063   1.00 7.83   ? 122 HIS A O   1 
ATOM   1047 C  CB  . HIS A 1 122 ? -4.339  9.338   2.252   1.00 7.52   ? 122 HIS A CB  1 
ATOM   1048 C  CG  . HIS A 1 122 ? -5.223  8.201   1.829   1.00 6.76   ? 122 HIS A CG  1 
ATOM   1049 N  ND1 . HIS A 1 122 ? -4.911  6.886   2.079   1.00 7.32   ? 122 HIS A ND1 1 
ATOM   1050 C  CD2 . HIS A 1 122 ? -6.439  8.147   1.193   1.00 8.07   ? 122 HIS A CD2 1 
ATOM   1051 C  CE1 . HIS A 1 122 ? -5.894  6.118   1.628   1.00 8.33   ? 122 HIS A CE1 1 
ATOM   1052 N  NE2 . HIS A 1 122 ? -6.844  6.855   1.082   1.00 8.57   ? 122 HIS A NE2 1 
ATOM   1053 N  N   . TRP A 1 123 ? -2.286  11.814  1.852   1.00 7.11   ? 123 TRP A N   1 
ATOM   1054 C  CA  . TRP A 1 123 ? -1.511  12.806  2.546   1.00 7.34   ? 123 TRP A CA  1 
ATOM   1055 C  C   . TRP A 1 123 ? -2.404  13.768  3.303   1.00 6.95   ? 123 TRP A C   1 
ATOM   1056 O  O   . TRP A 1 123 ? -3.513  14.113  2.897   1.00 7.78   ? 123 TRP A O   1 
ATOM   1057 C  CB  . TRP A 1 123 ? -0.560  13.575  1.579   1.00 9.11   ? 123 TRP A CB  1 
ATOM   1058 C  CG  . TRP A 1 123 ? -1.254  14.217  0.394   1.00 8.67   ? 123 TRP A CG  1 
ATOM   1059 C  CD1 . TRP A 1 123 ? -1.473  13.609  -0.828  1.00 9.30   ? 123 TRP A CD1 1 
ATOM   1060 C  CD2 . TRP A 1 123 ? -1.754  15.552  0.287   1.00 9.52   ? 123 TRP A CD2 1 
ATOM   1061 N  NE1 . TRP A 1 123 ? -2.092  14.460  -1.677  1.00 10.71  ? 123 TRP A NE1 1 
ATOM   1062 C  CE2 . TRP A 1 123 ? -2.298  15.677  -1.037  1.00 10.34  ? 123 TRP A CE2 1 
ATOM   1063 C  CE3 . TRP A 1 123 ? -1.840  16.644  1.160   1.00 9.75   ? 123 TRP A CE3 1 
ATOM   1064 C  CZ2 . TRP A 1 123 ? -2.887  16.822  -1.498  1.00 12.04  ? 123 TRP A CZ2 1 
ATOM   1065 C  CZ3 . TRP A 1 123 ? -2.432  17.823  0.666   1.00 12.32  ? 123 TRP A CZ3 1 
ATOM   1066 C  CH2 . TRP A 1 123 ? -2.930  17.895  -0.642  1.00 12.77  ? 123 TRP A CH2 1 
ATOM   1067 N  N   . ASN A 1 124 ? -1.880  14.234  4.446   1.00 7.51   ? 124 ASN A N   1 
ATOM   1068 C  CA  . ASN A 1 124 ? -2.632  15.109  5.355   1.00 8.16   ? 124 ASN A CA  1 
ATOM   1069 C  C   . ASN A 1 124 ? -2.762  16.511  4.766   1.00 7.92   ? 124 ASN A C   1 
ATOM   1070 O  O   . ASN A 1 124 ? -1.758  17.184  4.484   1.00 8.56   ? 124 ASN A O   1 
ATOM   1071 C  CB  . ASN A 1 124 ? -1.833  15.190  6.650   1.00 8.48   ? 124 ASN A CB  1 
ATOM   1072 C  CG  . ASN A 1 124 ? -2.617  15.776  7.769   1.00 8.43   ? 124 ASN A CG  1 
ATOM   1073 O  OD1 . ASN A 1 124 ? -3.449  16.657  7.570   1.00 9.50   ? 124 ASN A OD1 1 
ATOM   1074 N  ND2 . ASN A 1 124 ? -2.325  15.335  8.982   1.00 10.55  ? 124 ASN A ND2 1 
ATOM   1075 N  N   . THR A 1 125 ? -4.026  16.919  4.555   1.00 8.74   ? 125 THR A N   1 
ATOM   1076 C  CA  . THR A 1 125 ? -4.275  18.209  3.859   1.00 9.70   ? 125 THR A CA  1 
ATOM   1077 C  C   . THR A 1 125 ? -3.748  19.404  4.605   1.00 10.29  ? 125 THR A C   1 
ATOM   1078 O  O   . THR A 1 125 ? -3.585  20.462  4.023   1.00 11.39  ? 125 THR A O   1 
ATOM   1079 C  CB  . THR A 1 125 ? -5.785  18.321  3.511   1.00 12.02  ? 125 THR A CB  1 
ATOM   1080 O  OG1 . THR A 1 125 ? -6.541  18.294  4.734   1.00 17.02  ? 125 THR A OG1 1 
ATOM   1081 C  CG2 . THR A 1 125 ? -6.199  17.229  2.536   1.00 14.71  ? 125 THR A CG2 1 
ATOM   1082 N  N   . LYS A 1 126 ? -3.400  19.225  5.937   1.00 9.85   ? 127 LYS A N   1 
ATOM   1083 C  CA  . LYS A 1 126 ? -2.897  20.363  6.687   1.00 11.20  ? 127 LYS A CA  1 
ATOM   1084 C  C   . LYS A 1 126 ? -1.492  20.754  6.193   1.00 10.28  ? 127 LYS A C   1 
ATOM   1085 O  O   . LYS A 1 126 ? -1.002  21.841  6.556   1.00 12.30  ? 127 LYS A O   1 
ATOM   1086 C  CB  . LYS A 1 126 ? -2.975  20.100  8.170   1.00 13.53  ? 127 LYS A CB  1 
ATOM   1087 C  CG  . LYS A 1 126 ? -1.846  19.288  8.710   1.00 13.36  ? 127 LYS A CG  1 
ATOM   1088 C  CD  . LYS A 1 126 ? -2.022  18.777  10.199  1.00 18.42  ? 127 LYS A CD  1 
ATOM   1089 C  CE  . LYS A 1 126 ? -1.462  19.855  11.131  1.00 25.40  ? 127 LYS A CE  1 
ATOM   1090 N  NZ  . LYS A 1 126 ? -1.227  19.165  12.433  1.00 40.50  ? 127 LYS A NZ  1 
ATOM   1091 N  N   . TYR A 1 127 ? -0.832  19.911  5.373   1.00 9.62   ? 128 TYR A N   1 
ATOM   1092 C  CA  . TYR A 1 127 ? 0.515   20.178  4.886   1.00 9.35   ? 128 TYR A CA  1 
ATOM   1093 C  C   . TYR A 1 127 ? 0.523   20.592  3.405   1.00 10.02  ? 128 TYR A C   1 
ATOM   1094 O  O   . TYR A 1 127 ? 1.602   20.826  2.836   1.00 10.47  ? 128 TYR A O   1 
ATOM   1095 C  CB  . TYR A 1 127 ? 1.480   19.051  5.158   1.00 10.46  ? 128 TYR A CB  1 
ATOM   1096 C  CG  . TYR A 1 127 ? 1.607   18.725  6.615   1.00 9.82   ? 128 TYR A CG  1 
ATOM   1097 C  CD1 . TYR A 1 127 ? 1.966   19.739  7.533   1.00 10.31  ? 128 TYR A CD1 1 
ATOM   1098 C  CD2 . TYR A 1 127 ? 1.265   17.469  7.140   1.00 8.98   ? 128 TYR A CD2 1 
ATOM   1099 C  CE1 . TYR A 1 127 ? 2.045   19.446  8.869   1.00 11.34  ? 128 TYR A CE1 1 
ATOM   1100 C  CE2 . TYR A 1 127 ? 1.385   17.184  8.462   1.00 9.54   ? 128 TYR A CE2 1 
ATOM   1101 C  CZ  . TYR A 1 127 ? 1.719   18.203  9.340   1.00 10.69  ? 128 TYR A CZ  1 
ATOM   1102 O  OH  . TYR A 1 127 ? 1.832   17.972  10.672  1.00 12.43  ? 128 TYR A OH  1 
ATOM   1103 N  N   . GLY A 1 128 ? -0.648  20.687  2.756   1.00 9.91   ? 129 GLY A N   1 
ATOM   1104 C  CA  . GLY A 1 128 ? -0.739  21.348  1.479   1.00 11.08  ? 129 GLY A CA  1 
ATOM   1105 C  C   . GLY A 1 128 ? -0.407  20.492  0.254   1.00 10.85  ? 129 GLY A C   1 
ATOM   1106 O  O   . GLY A 1 128 ? -1.063  20.637  -0.768  1.00 12.53  ? 129 GLY A O   1 
ATOM   1107 N  N   . ASP A 1 129 ? 0.619   19.632  0.329   1.00 11.11  ? 130 ASP A N   1 
ATOM   1108 C  CA  . ASP A 1 129 ? 0.848   18.701  -0.767  1.00 11.84  ? 130 ASP A CA  1 
ATOM   1109 C  C   . ASP A 1 129 ? 1.592   17.513  -0.207  1.00 10.66  ? 130 ASP A C   1 
ATOM   1110 O  O   . ASP A 1 129 ? 2.070   17.509  0.951   1.00 12.29  ? 130 ASP A O   1 
ATOM   1111 C  CB  . ASP A 1 129 ? 1.427   19.319  -1.988  1.00 15.60  ? 130 ASP A CB  1 
ATOM   1112 C  CG  . ASP A 1 129 ? 2.839   19.776  -1.788  1.00 13.70  ? 130 ASP A CG  1 
ATOM   1113 O  OD1 . ASP A 1 129 ? 3.422   19.523  -0.729  1.00 19.40  ? 130 ASP A OD1 1 
ATOM   1114 O  OD2 . ASP A 1 129 ? 3.362   20.433  -2.689  1.00 19.53  ? 130 ASP A OD2 1 
ATOM   1115 N  N   . PHE A 1 130 ? 1.779   16.484  -1.055  1.00 10.97  ? 131 PHE A N   1 
ATOM   1116 C  CA  . PHE A 1 130 ? 2.463   15.279  -0.631  1.00 10.01  ? 131 PHE A CA  1 
ATOM   1117 C  C   . PHE A 1 130 ? 3.919   15.515  -0.261  1.00 10.48  ? 131 PHE A C   1 
ATOM   1118 O  O   . PHE A 1 130 ? 4.405   14.951  0.724   1.00 10.27  ? 131 PHE A O   1 
ATOM   1119 C  CB  . PHE A 1 130 ? 2.363   14.253  -1.804  1.00 10.39  ? 131 PHE A CB  1 
ATOM   1120 C  CG  . PHE A 1 130 ? 3.079   12.966  -1.525  1.00 9.54   ? 131 PHE A CG  1 
ATOM   1121 C  CD1 . PHE A 1 130 ? 2.411   11.956  -0.883  1.00 10.43  ? 131 PHE A CD1 1 
ATOM   1122 C  CD2 . PHE A 1 130 ? 4.391   12.764  -1.866  1.00 12.05  ? 131 PHE A CD2 1 
ATOM   1123 C  CE1 . PHE A 1 130 ? 3.008   10.737  -0.656  1.00 12.23  ? 131 PHE A CE1 1 
ATOM   1124 C  CE2 . PHE A 1 130 ? 4.987   11.541  -1.651  1.00 13.88  ? 131 PHE A CE2 1 
ATOM   1125 C  CZ  . PHE A 1 130 ? 4.300   10.551  -0.982  1.00 13.62  ? 131 PHE A CZ  1 
ATOM   1126 N  N   . GLY A 1 131 ? 4.635   16.307  -1.082  1.00 12.68  ? 132 GLY A N   1 
ATOM   1127 C  CA  . GLY A 1 131 ? 6.060   16.467  -0.806  1.00 12.83  ? 132 GLY A CA  1 
ATOM   1128 C  C   . GLY A 1 131 ? 6.366   17.121  0.551   1.00 12.60  ? 132 GLY A C   1 
ATOM   1129 O  O   . GLY A 1 131 ? 7.404   16.826  1.173   1.00 13.52  ? 132 GLY A O   1 
ATOM   1130 N  N   A LYS A 1 132 ? 5.524   18.031  1.010   0.50 11.73  ? 133 LYS A N   1 
ATOM   1131 N  N   B LYS A 1 132 ? 5.524   18.029  1.009   0.50 11.71  ? 133 LYS A N   1 
ATOM   1132 C  CA  A LYS A 1 132 ? 5.683   18.594  2.350   0.50 11.46  ? 133 LYS A CA  1 
ATOM   1133 C  CA  B LYS A 1 132 ? 5.680   18.595  2.348   0.50 11.56  ? 133 LYS A CA  1 
ATOM   1134 C  C   A LYS A 1 132 ? 5.150   17.630  3.413   0.50 9.57   ? 133 LYS A C   1 
ATOM   1135 C  C   B LYS A 1 132 ? 5.149   17.631  3.413   0.50 9.66   ? 133 LYS A C   1 
ATOM   1136 O  O   A LYS A 1 132 ? 5.725   17.557  4.496   0.50 10.17  ? 133 LYS A O   1 
ATOM   1137 O  O   B LYS A 1 132 ? 5.726   17.558  4.496   0.50 10.41  ? 133 LYS A O   1 
ATOM   1138 C  CB  A LYS A 1 132 ? 4.941   19.928  2.464   0.50 12.47  ? 133 LYS A CB  1 
ATOM   1139 C  CB  B LYS A 1 132 ? 4.939   19.930  2.450   0.50 11.80  ? 133 LYS A CB  1 
ATOM   1140 C  CG  A LYS A 1 132 ? 5.581   21.014  1.609   0.50 14.33  ? 133 LYS A CG  1 
ATOM   1141 C  CG  B LYS A 1 132 ? 5.671   21.040  1.691   0.50 17.16  ? 133 LYS A CG  1 
ATOM   1142 C  CD  A LYS A 1 132 ? 6.974   21.359  2.035   0.50 21.10  ? 133 LYS A CD  1 
ATOM   1143 C  CD  B LYS A 1 132 ? 6.955   21.396  2.431   0.50 22.98  ? 133 LYS A CD  1 
ATOM   1144 C  CE  A LYS A 1 132 ? 7.010   22.347  3.151   0.50 30.34  ? 133 LYS A CE  1 
ATOM   1145 C  CE  B LYS A 1 132 ? 7.554   22.710  1.951   0.50 27.15  ? 133 LYS A CE  1 
ATOM   1146 N  NZ  A LYS A 1 132 ? 8.332   23.035  3.099   0.50 32.19  ? 133 LYS A NZ  1 
ATOM   1147 N  NZ  B LYS A 1 132 ? 8.815   23.048  2.687   0.50 34.50  ? 133 LYS A NZ  1 
ATOM   1148 N  N   . ALA A 1 133 ? 4.055   16.933  3.098   1.00 9.60   ? 134 ALA A N   1 
ATOM   1149 C  CA  . ALA A 1 133 ? 3.502   15.981  4.076   1.00 9.80   ? 134 ALA A CA  1 
ATOM   1150 C  C   . ALA A 1 133 ? 4.507   14.916  4.512   1.00 9.17   ? 134 ALA A C   1 
ATOM   1151 O  O   . ALA A 1 133 ? 4.555   14.510  5.656   1.00 9.02   ? 134 ALA A O   1 
ATOM   1152 C  CB  . ALA A 1 133 ? 2.256   15.352  3.510   1.00 9.89   ? 134 ALA A CB  1 
ATOM   1153 N  N   . VAL A 1 134 ? 5.317   14.395  3.569   1.00 9.41   ? 135 VAL A N   1 
ATOM   1154 C  CA  . VAL A 1 134 ? 6.236   13.270  3.931   1.00 9.99   ? 135 VAL A CA  1 
ATOM   1155 C  C   . VAL A 1 134 ? 7.319   13.701  4.876   1.00 10.34  ? 135 VAL A C   1 
ATOM   1156 O  O   . VAL A 1 134 ? 8.045   12.828  5.388   1.00 11.33  ? 135 VAL A O   1 
ATOM   1157 C  CB  . VAL A 1 134 ? 6.898   12.619  2.714   1.00 11.76  ? 135 VAL A CB  1 
ATOM   1158 C  CG1 . VAL A 1 134 ? 5.892   11.889  1.900   1.00 14.50  ? 135 VAL A CG1 1 
ATOM   1159 C  CG2 . VAL A 1 134 ? 7.746   13.536  1.892   1.00 12.26  ? 135 VAL A CG2 1 
ATOM   1160 N  N   . GLN A 1 135 ? 7.481   15.023  5.065   1.00 10.06  ? 136 GLN A N   1 
ATOM   1161 C  CA  . GLN A 1 135 ? 8.474   15.499  6.004   1.00 11.13  ? 136 GLN A CA  1 
ATOM   1162 C  C   . GLN A 1 135 ? 7.950   15.639  7.407   1.00 10.47  ? 136 GLN A C   1 
ATOM   1163 O  O   . GLN A 1 135 ? 8.644   16.179  8.316   1.00 13.79  ? 136 GLN A O   1 
ATOM   1164 C  CB  . GLN A 1 135 ? 9.040   16.844  5.489   1.00 12.48  ? 136 GLN A CB  1 
ATOM   1165 C  CG  . GLN A 1 135 ? 9.603   16.750  4.120   1.00 15.46  ? 136 GLN A CG  1 
ATOM   1166 C  CD  . GLN A 1 135 ? 10.122  18.078  3.632   1.00 18.11  ? 136 GLN A CD  1 
ATOM   1167 O  OE1 . GLN A 1 135 ? 10.991  18.733  4.281   1.00 24.59  ? 136 GLN A OE1 1 
ATOM   1168 N  NE2 . GLN A 1 135 ? 9.586   18.558  2.489   1.00 21.19  ? 136 GLN A NE2 1 
ATOM   1169 N  N   . GLN A 1 136 ? 6.722   15.171  7.636   1.00 10.02  ? 137 GLN A N   1 
ATOM   1170 C  CA  . GLN A 1 136 ? 6.053   15.342  8.927   1.00 10.00  ? 137 GLN A CA  1 
ATOM   1171 C  C   . GLN A 1 136 ? 5.704   13.996  9.536   1.00 9.11   ? 137 GLN A C   1 
ATOM   1172 O  O   . GLN A 1 136 ? 5.320   13.071  8.807   1.00 9.31   ? 137 GLN A O   1 
ATOM   1173 C  CB  . GLN A 1 136 ? 4.735   16.130  8.774   1.00 10.63  ? 137 GLN A CB  1 
ATOM   1174 C  CG  . GLN A 1 136 ? 4.950   17.418  8.000   1.00 14.85  ? 137 GLN A CG  1 
ATOM   1175 C  CD  . GLN A 1 136 ? 5.861   18.371  8.640   1.00 17.81  ? 137 GLN A CD  1 
ATOM   1176 O  OE1 . GLN A 1 136 ? 6.041   18.361  9.824   1.00 20.38  ? 137 GLN A OE1 1 
ATOM   1177 N  NE2 . GLN A 1 136 ? 6.450   19.233  7.844   1.00 31.11  ? 137 GLN A NE2 1 
ATOM   1178 N  N   . PRO A 1 137 ? 5.675   13.883  10.885  1.00 9.60   ? 138 PRO A N   1 
ATOM   1179 C  CA  . PRO A 1 137 ? 5.421   12.558  11.497  1.00 10.79  ? 138 PRO A CA  1 
ATOM   1180 C  C   . PRO A 1 137 ? 4.009   12.066  11.324  1.00 10.33  ? 138 PRO A C   1 
ATOM   1181 O  O   . PRO A 1 137 ? 3.766   10.864  11.396  1.00 13.06  ? 138 PRO A O   1 
ATOM   1182 C  CB  . PRO A 1 137 ? 5.721   12.731  12.983  1.00 13.74  ? 138 PRO A CB  1 
ATOM   1183 C  CG  . PRO A 1 137 ? 5.843   14.165  13.137  1.00 19.40  ? 138 PRO A CG  1 
ATOM   1184 C  CD  . PRO A 1 137 ? 6.222   14.835  11.853  1.00 12.77  ? 138 PRO A CD  1 
ATOM   1185 N  N   . ASP A 1 138 ? 3.048   13.007  11.068  1.00 9.31   ? 139 ASP A N   1 
ATOM   1186 C  CA  . ASP A 1 138 ? 1.648   12.715  10.788  1.00 9.08   ? 139 ASP A CA  1 
ATOM   1187 C  C   . ASP A 1 138 ? 1.306   13.119  9.370   1.00 7.94   ? 139 ASP A C   1 
ATOM   1188 O  O   . ASP A 1 138 ? 0.144   13.497  9.102   1.00 9.18   ? 139 ASP A O   1 
ATOM   1189 C  CB  . ASP A 1 138 ? 0.693   13.315  11.789  1.00 11.20  ? 139 ASP A CB  1 
ATOM   1190 C  CG  . ASP A 1 138 ? 0.783   14.814  11.846  1.00 11.74  ? 139 ASP A CG  1 
ATOM   1191 O  OD1 . ASP A 1 138 ? 1.719   15.411  11.252  1.00 11.09  ? 139 ASP A OD1 1 
ATOM   1192 O  OD2 . ASP A 1 138 ? -0.095  15.393  12.513  1.00 14.86  ? 139 ASP A OD2 1 
ATOM   1193 N  N   . GLY A 1 139 ? 2.244   12.981  8.431   1.00 7.77   ? 140 GLY A N   1 
ATOM   1194 C  CA  . GLY A 1 139 ? 2.005   13.464  7.090   1.00 8.04   ? 140 GLY A CA  1 
ATOM   1195 C  C   . GLY A 1 139 ? 1.180   12.569  6.204   1.00 6.94   ? 140 GLY A C   1 
ATOM   1196 O  O   . GLY A 1 139 ? 0.469   13.070  5.330   1.00 7.91   ? 140 GLY A O   1 
ATOM   1197 N  N   . LEU A 1 140 ? 1.289   11.226  6.370   1.00 6.76   ? 141 LEU A N   1 
ATOM   1198 C  CA  . LEU A 1 140 ? 0.630   10.274  5.523   1.00 6.70   ? 141 LEU A CA  1 
ATOM   1199 C  C   . LEU A 1 140 ? -0.190  9.342   6.306   1.00 6.45   ? 141 LEU A C   1 
ATOM   1200 O  O   . LEU A 1 140 ? 0.049   9.043   7.459   1.00 6.71   ? 141 LEU A O   1 
ATOM   1201 C  CB  . LEU A 1 140 ? 1.604   9.427   4.675   1.00 7.40   ? 141 LEU A CB  1 
ATOM   1202 C  CG  . LEU A 1 140 ? 2.478   10.117  3.674   1.00 9.60   ? 141 LEU A CG  1 
ATOM   1203 C  CD1 . LEU A 1 140 ? 3.260   9.063   2.849   1.00 9.57   ? 141 LEU A CD1 1 
ATOM   1204 C  CD2 . LEU A 1 140 ? 1.891   11.184  2.799   1.00 12.94  ? 141 LEU A CD2 1 
ATOM   1205 N  N   . ALA A 1 141 ? -1.260  8.830   5.624   1.00 6.62   ? 142 ALA A N   1 
ATOM   1206 C  CA  . ALA A 1 141 ? -2.044  7.672   6.150   1.00 6.80   ? 142 ALA A CA  1 
ATOM   1207 C  C   . ALA A 1 141 ? -2.084  6.708   5.011   1.00 6.55   ? 142 ALA A C   1 
ATOM   1208 O  O   . ALA A 1 141 ? -2.486  7.044   3.883   1.00 7.11   ? 142 ALA A O   1 
ATOM   1209 C  CB  . ALA A 1 141 ? -3.442  8.107   6.549   1.00 8.58   ? 142 ALA A CB  1 
ATOM   1210 N  N   . VAL A 1 142 ? -1.599  5.465   5.272   1.00 6.12   ? 143 VAL A N   1 
ATOM   1211 C  CA  . VAL A 1 142 ? -1.618  4.415   4.256   1.00 6.25   ? 143 VAL A CA  1 
ATOM   1212 C  C   . VAL A 1 142 ? -2.578  3.353   4.741   1.00 5.92   ? 143 VAL A C   1 
ATOM   1213 O  O   . VAL A 1 142 ? -2.449  2.841   5.863   1.00 6.50   ? 143 VAL A O   1 
ATOM   1214 C  CB  . VAL A 1 142 ? -0.238  3.840   3.881   1.00 6.58   ? 143 VAL A CB  1 
ATOM   1215 C  CG1 . VAL A 1 142 ? -0.407  2.807   2.758   1.00 7.52   ? 143 VAL A CG1 1 
ATOM   1216 C  CG2 . VAL A 1 142 ? 0.718   4.947   3.451   1.00 8.19   ? 143 VAL A CG2 1 
ATOM   1217 N  N   . LEU A 1 143 ? -3.575  3.088   3.893   1.00 6.18   ? 144 LEU A N   1 
ATOM   1218 C  CA  . LEU A 1 143 ? -4.546  2.047   4.145   1.00 6.23   ? 144 LEU A CA  1 
ATOM   1219 C  C   . LEU A 1 143 ? -4.040  0.772   3.430   1.00 6.38   ? 144 LEU A C   1 
ATOM   1220 O  O   . LEU A 1 143 ? -3.886  0.748   2.219   1.00 7.10   ? 144 LEU A O   1 
ATOM   1221 C  CB  . LEU A 1 143 ? -5.918  2.488   3.587   1.00 8.16   ? 144 LEU A CB  1 
ATOM   1222 C  CG  . LEU A 1 143 ? -7.058  1.495   3.716   1.00 9.40   ? 144 LEU A CG  1 
ATOM   1223 C  CD1 . LEU A 1 143 ? -7.310  1.163   5.176   1.00 10.60  ? 144 LEU A CD1 1 
ATOM   1224 C  CD2 . LEU A 1 143 ? -8.294  2.091   3.086   1.00 10.81  ? 144 LEU A CD2 1 
ATOM   1225 N  N   . GLY A 1 144 ? -3.763  -0.256  4.254   1.00 6.02   ? 145 GLY A N   1 
ATOM   1226 C  CA  . GLY A 1 144 ? -3.217  -1.519  3.732   1.00 6.29   ? 145 GLY A CA  1 
ATOM   1227 C  C   . GLY A 1 144 ? -4.309  -2.592  3.790   1.00 6.06   ? 145 GLY A C   1 
ATOM   1228 O  O   . GLY A 1 144 ? -5.025  -2.726  4.751   1.00 7.09   ? 145 GLY A O   1 
ATOM   1229 N  N   . ILE A 1 145 ? -4.336  -3.331  2.660   1.00 6.09   ? 146 ILE A N   1 
ATOM   1230 C  CA  . ILE A 1 145 ? -5.386  -4.350  2.476   1.00 6.08   ? 146 ILE A CA  1 
ATOM   1231 C  C   . ILE A 1 145 ? -4.693  -5.595  1.943   1.00 6.57   ? 146 ILE A C   1 
ATOM   1232 O  O   . ILE A 1 145 ? -3.957  -5.557  0.950   1.00 6.84   ? 146 ILE A O   1 
ATOM   1233 C  CB  . ILE A 1 145 ? -6.496  -3.883  1.482   1.00 7.63   ? 146 ILE A CB  1 
ATOM   1234 C  CG1 . ILE A 1 145 ? -7.053  -2.540  1.990   1.00 9.25   ? 146 ILE A CG1 1 
ATOM   1235 C  CG2 . ILE A 1 145 ? -7.499  -4.974  1.303   1.00 9.46   ? 146 ILE A CG2 1 
ATOM   1236 C  CD1 . ILE A 1 145 ? -8.167  -1.979  1.122   1.00 9.44   ? 146 ILE A CD1 1 
ATOM   1237 N  N   . PHE A 1 146 ? -4.848  -6.704  2.650   1.00 5.90   ? 147 PHE A N   1 
ATOM   1238 C  CA  . PHE A 1 146 ? -4.230  -7.993  2.220   1.00 6.31   ? 147 PHE A CA  1 
ATOM   1239 C  C   . PHE A 1 146 ? -5.007  -8.572  1.054   1.00 6.83   ? 147 PHE A C   1 
ATOM   1240 O  O   . PHE A 1 146 ? -6.231  -8.456  0.979   1.00 7.62   ? 147 PHE A O   1 
ATOM   1241 C  CB  . PHE A 1 146 ? -4.256  -8.934  3.403   1.00 6.67   ? 147 PHE A CB  1 
ATOM   1242 C  CG  . PHE A 1 146 ? -3.385  -8.487  4.555   1.00 5.99   ? 147 PHE A CG  1 
ATOM   1243 C  CD1 . PHE A 1 146 ? -2.021  -8.313  4.376   1.00 6.59   ? 147 PHE A CD1 1 
ATOM   1244 C  CD2 . PHE A 1 146 ? -3.928  -8.263  5.788   1.00 7.33   ? 147 PHE A CD2 1 
ATOM   1245 C  CE1 . PHE A 1 146 ? -1.220  -7.941  5.461   1.00 7.50   ? 147 PHE A CE1 1 
ATOM   1246 C  CE2 . PHE A 1 146 ? -3.135  -7.883  6.874   1.00 7.19   ? 147 PHE A CE2 1 
ATOM   1247 C  CZ  . PHE A 1 146 ? -1.769  -7.759  6.707   1.00 7.09   ? 147 PHE A CZ  1 
ATOM   1248 N  N   . LEU A 1 147 ? -4.280  -9.316  0.209   1.00 6.71   ? 148 LEU A N   1 
ATOM   1249 C  CA  . LEU A 1 147 ? -4.861  -10.101 -0.889  1.00 7.14   ? 148 LEU A CA  1 
ATOM   1250 C  C   . LEU A 1 147 ? -4.525  -11.575 -0.664  1.00 6.82   ? 148 LEU A C   1 
ATOM   1251 O  O   . LEU A 1 147 ? -3.345  -11.911 -0.427  1.00 7.35   ? 148 LEU A O   1 
ATOM   1252 C  CB  . LEU A 1 147 ? -4.254  -9.701  -2.221  1.00 8.11   ? 148 LEU A CB  1 
ATOM   1253 C  CG  . LEU A 1 147 ? -4.776  -8.427  -2.900  1.00 8.73   ? 148 LEU A CG  1 
ATOM   1254 C  CD1 . LEU A 1 147 ? -4.543  -7.193  -2.065  1.00 9.62   ? 148 LEU A CD1 1 
ATOM   1255 C  CD2 . LEU A 1 147 ? -4.185  -8.264  -4.261  1.00 9.67   ? 148 LEU A CD2 1 
ATOM   1256 N  N   . LYS A 1 148 ? -5.539  -12.407 -0.759  1.00 7.90   ? 149 LYS A N   1 
ATOM   1257 C  CA  . LYS A 1 148 ? -5.383  -13.858 -0.811  1.00 8.20   ? 149 LYS A CA  1 
ATOM   1258 C  C   . LYS A 1 148 ? -5.861  -14.327 -2.161  1.00 8.71   ? 149 LYS A C   1 
ATOM   1259 O  O   . LYS A 1 148 ? -6.700  -13.680 -2.833  1.00 10.02  ? 149 LYS A O   1 
ATOM   1260 C  CB  . LYS A 1 148 ? -6.113  -14.523 0.341   1.00 9.64   ? 149 LYS A CB  1 
ATOM   1261 C  CG  . LYS A 1 148 ? -7.634  -14.424 0.271   1.00 11.37  ? 149 LYS A CG  1 
ATOM   1262 C  CD  . LYS A 1 148 ? -8.176  -15.101 1.494   1.00 17.46  ? 149 LYS A CD  1 
ATOM   1263 C  CE  . LYS A 1 148 ? -9.646  -15.343 1.314   1.00 26.88  ? 149 LYS A CE  1 
ATOM   1264 N  NZ  . LYS A 1 148 ? -10.104 -16.418 2.279   1.00 41.33  ? 149 LYS A NZ  1 
ATOM   1265 N  N   . VAL A 1 149 ? -5.365  -15.493 -2.592  1.00 9.06   ? 150 VAL A N   1 
ATOM   1266 C  CA  . VAL A 1 149 ? -5.762  -16.093 -3.893  1.00 9.74   ? 150 VAL A CA  1 
ATOM   1267 C  C   . VAL A 1 149 ? -6.968  -16.998 -3.689  1.00 9.89   ? 150 VAL A C   1 
ATOM   1268 O  O   . VAL A 1 149 ? -6.940  -17.958 -2.925  1.00 11.25  ? 150 VAL A O   1 
ATOM   1269 C  CB  . VAL A 1 149 ? -4.538  -16.822 -4.476  1.00 9.94   ? 150 VAL A CB  1 
ATOM   1270 C  CG1 . VAL A 1 149 ? -4.939  -17.597 -5.727  1.00 12.05  ? 150 VAL A CG1 1 
ATOM   1271 C  CG2 . VAL A 1 149 ? -3.509  -15.803 -4.782  1.00 12.63  ? 150 VAL A CG2 1 
ATOM   1272 N  N   . GLY A 1 150 ? -8.014  -16.711 -4.441  1.00 10.19  ? 151 GLY A N   1 
ATOM   1273 C  CA  . GLY A 1 150 ? -9.225  -17.517 -4.420  1.00 11.51  ? 151 GLY A CA  1 
ATOM   1274 C  C   . GLY A 1 150 ? -10.110 -17.034 -5.534  1.00 11.35  ? 151 GLY A C   1 
ATOM   1275 O  O   . GLY A 1 150 ? -9.750  -17.138 -6.708  1.00 12.63  ? 151 GLY A O   1 
ATOM   1276 N  N   . SER A 1 151 ? -11.295 -16.545 -5.180  1.00 12.69  ? 152 SER A N   1 
ATOM   1277 C  CA  . SER A 1 151 ? -12.230 -15.938 -6.143  1.00 13.81  ? 152 SER A CA  1 
ATOM   1278 C  C   . SER A 1 151 ? -11.595 -14.679 -6.771  1.00 11.68  ? 152 SER A C   1 
ATOM   1279 O  O   . SER A 1 151 ? -10.815 -13.976 -6.111  1.00 12.31  ? 152 SER A O   1 
ATOM   1280 C  CB  . SER A 1 151 ? -13.518 -15.494 -5.416  1.00 18.80  ? 152 SER A CB  1 
ATOM   1281 O  OG  . SER A 1 151 ? -14.096 -16.650 -4.944  1.00 27.35  ? 152 SER A OG  1 
ATOM   1282 N  N   . ALA A 1 152 ? -11.885 -14.361 -8.046  1.00 11.63  ? 153 ALA A N   1 
ATOM   1283 C  CA  . ALA A 1 152 ? -11.486 -13.118 -8.614  1.00 11.70  ? 153 ALA A CA  1 
ATOM   1284 C  C   . ALA A 1 152 ? -12.134 -11.920 -7.930  1.00 11.51  ? 153 ALA A C   1 
ATOM   1285 O  O   . ALA A 1 152 ? -13.218 -11.971 -7.408  1.00 14.18  ? 153 ALA A O   1 
ATOM   1286 C  CB  . ALA A 1 152 ? -11.825 -13.105 -10.088 1.00 14.53  ? 153 ALA A CB  1 
ATOM   1287 N  N   . LYS A 1 153 ? -11.417 -10.786 -8.019  1.00 12.33  ? 154 LYS A N   1 
ATOM   1288 C  CA  . LYS A 1 153 ? -11.923 -9.510  -7.499  1.00 13.50  ? 154 LYS A CA  1 
ATOM   1289 C  C   . LYS A 1 153 ? -12.345 -8.706  -8.794  1.00 11.98  ? 154 LYS A C   1 
ATOM   1290 O  O   . LYS A 1 153 ? -11.499 -8.226  -9.552  1.00 12.43  ? 154 LYS A O   1 
ATOM   1291 C  CB  . LYS A 1 153 ? -10.892 -8.726  -6.758  1.00 13.86  ? 154 LYS A CB  1 
ATOM   1292 C  CG  . LYS A 1 153 ? -11.318 -7.470  -6.055  1.00 17.97  ? 154 LYS A CG  1 
ATOM   1293 C  CD  . LYS A 1 153 ? -12.186 -7.832  -4.856  1.00 18.43  ? 154 LYS A CD  1 
ATOM   1294 C  CE  . LYS A 1 153 ? -12.179 -6.646  -3.923  1.00 18.26  ? 154 LYS A CE  1 
ATOM   1295 N  NZ  . LYS A 1 153 ? -13.195 -6.933  -2.892  1.00 17.09  ? 154 LYS A NZ  1 
ATOM   1296 N  N   . PRO A 1 154 ? -13.648 -8.605  -9.053  1.00 14.11  ? 155 PRO A N   1 
ATOM   1297 C  CA  . PRO A 1 154 ? -14.067 -8.001  -10.333 1.00 14.94  ? 155 PRO A CA  1 
ATOM   1298 C  C   . PRO A 1 154 ? -13.574 -6.584  -10.481 1.00 15.11  ? 155 PRO A C   1 
ATOM   1299 O  O   . PRO A 1 154 ? -13.172 -6.234  -11.593 1.00 17.09  ? 155 PRO A O   1 
ATOM   1300 C  CB  . PRO A 1 154 ? -15.598 -8.101  -10.271 1.00 17.63  ? 155 PRO A CB  1 
ATOM   1301 C  CG  . PRO A 1 154 ? -15.831 -9.302  -9.358  1.00 18.40  ? 155 PRO A CG  1 
ATOM   1302 C  CD  . PRO A 1 154 ? -14.808 -9.115  -8.283  1.00 16.99  ? 155 PRO A CD  1 
ATOM   1303 N  N   . GLY A 1 155 ? -13.470 -5.845  -9.365  1.00 14.99  ? 156 GLY A N   1 
ATOM   1304 C  CA  . GLY A 1 155 ? -13.102 -4.464  -9.406  1.00 16.33  ? 156 GLY A CA  1 
ATOM   1305 C  C   . GLY A 1 155 ? -11.631 -4.281  -9.661  1.00 15.32  ? 156 GLY A C   1 
ATOM   1306 O  O   . GLY A 1 155 ? -11.145 -3.155  -9.895  1.00 18.23  ? 156 GLY A O   1 
ATOM   1307 N  N   . LEU A 1 156 ? -10.891 -5.359  -9.605  1.00 13.94  ? 157 LEU A N   1 
ATOM   1308 C  CA  . LEU A 1 156 ? -9.478  -5.345  -9.976  1.00 13.83  ? 157 LEU A CA  1 
ATOM   1309 C  C   . LEU A 1 156 ? -9.148  -5.549  -11.436 1.00 14.86  ? 157 LEU A C   1 
ATOM   1310 O  O   . LEU A 1 156 ? -8.051  -5.239  -11.921 1.00 14.66  ? 157 LEU A O   1 
ATOM   1311 C  CB  . LEU A 1 156 ? -8.695  -6.379  -9.123  1.00 13.83  ? 157 LEU A CB  1 
ATOM   1312 C  CG  . LEU A 1 156 ? -7.172  -6.509  -9.274  1.00 14.06  ? 157 LEU A CG  1 
ATOM   1313 C  CD1 . LEU A 1 156 ? -6.449  -5.218  -8.915  1.00 14.91  ? 157 LEU A CD1 1 
ATOM   1314 C  CD2 . LEU A 1 156 ? -6.599  -7.660  -8.443  1.00 13.97  ? 157 LEU A CD2 1 
ATOM   1315 N  N   . GLN A 1 157 ? -10.115 -6.111  -12.193 1.00 14.17  ? 158 GLN A N   1 
ATOM   1316 C  CA  . GLN A 1 157 ? -9.761  -6.569  -13.539 1.00 16.19  ? 158 GLN A CA  1 
ATOM   1317 C  C   . GLN A 1 157 ? -9.347  -5.414  -14.445 1.00 15.53  ? 158 GLN A C   1 
ATOM   1318 O  O   . GLN A 1 157 ? -8.515  -5.629  -15.298 1.00 15.46  ? 158 GLN A O   1 
ATOM   1319 C  CB  . GLN A 1 157 ? -10.912 -7.364  -14.116 1.00 17.03  ? 158 GLN A CB  1 
ATOM   1320 C  CG  . GLN A 1 157 ? -10.558 -8.135  -15.386 1.00 18.73  ? 158 GLN A CG  1 
ATOM   1321 C  CD  . GLN A 1 157 ? -9.439  -9.144  -15.159 1.00 19.54  ? 158 GLN A CD  1 
ATOM   1322 O  OE1 . GLN A 1 157 ? -9.249  -9.706  -14.044 1.00 19.42  ? 158 GLN A OE1 1 
ATOM   1323 N  NE2 . GLN A 1 157 ? -8.644  -9.380  -16.215 1.00 21.29  ? 158 GLN A NE2 1 
ATOM   1324 N  N   A LYS A 1 158 ? -9.912  -4.208  -14.308 0.50 15.78  ? 159 LYS A N   1 
ATOM   1325 N  N   B LYS A 1 158 ? -9.919  -4.217  -14.290 0.50 15.94  ? 159 LYS A N   1 
ATOM   1326 C  CA  A LYS A 1 158 ? -9.491  -3.096  -15.190 0.50 16.76  ? 159 LYS A CA  1 
ATOM   1327 C  CA  B LYS A 1 158 ? -9.510  -3.091  -15.134 0.50 16.99  ? 159 LYS A CA  1 
ATOM   1328 C  C   A LYS A 1 158 ? -7.985  -2.782  -14.999 0.50 15.47  ? 159 LYS A C   1 
ATOM   1329 C  C   B LYS A 1 158 ? -8.002  -2.806  -14.988 0.50 15.50  ? 159 LYS A C   1 
ATOM   1330 O  O   A LYS A 1 158 ? -7.287  -2.445  -15.964 0.50 16.55  ? 159 LYS A O   1 
ATOM   1331 O  O   B LYS A 1 158 ? -7.329  -2.470  -15.957 0.50 16.52  ? 159 LYS A O   1 
ATOM   1332 C  CB  A LYS A 1 158 ? -10.439 -1.882  -15.066 0.50 17.04  ? 159 LYS A CB  1 
ATOM   1333 C  CB  B LYS A 1 158 ? -10.333 -1.848  -14.825 0.50 19.26  ? 159 LYS A CB  1 
ATOM   1334 C  CG  A LYS A 1 158 ? -11.802 -2.192  -15.688 0.50 20.43  ? 159 LYS A CG  1 
ATOM   1335 C  CG  B LYS A 1 158 ? -9.941  -0.739  -15.737 0.50 20.71  ? 159 LYS A CG  1 
ATOM   1336 C  CD  A LYS A 1 158 ? -12.574 -0.909  -15.875 0.50 25.66  ? 159 LYS A CD  1 
ATOM   1337 C  CD  B LYS A 1 158 ? -10.823 0.475   -15.479 0.50 22.46  ? 159 LYS A CD  1 
ATOM   1338 C  CE  A LYS A 1 158 ? -14.012 -1.165  -16.322 0.50 35.47  ? 159 LYS A CE  1 
ATOM   1339 C  CE  B LYS A 1 158 ? -10.170 1.775   -15.878 0.50 24.25  ? 159 LYS A CE  1 
ATOM   1340 N  NZ  A LYS A 1 158 ? -14.977 -0.074  -15.992 0.50 30.97  ? 159 LYS A NZ  1 
ATOM   1341 N  NZ  B LYS A 1 158 ? -11.169 2.731   -15.389 0.50 26.21  ? 159 LYS A NZ  1 
ATOM   1342 N  N   . VAL A 1 159 ? -7.500  -2.932  -13.766 1.00 15.04  ? 160 VAL A N   1 
ATOM   1343 C  CA  . VAL A 1 159 ? -6.068  -2.768  -13.506 1.00 14.41  ? 160 VAL A CA  1 
ATOM   1344 C  C   . VAL A 1 159 ? -5.255  -3.871  -14.233 1.00 14.12  ? 160 VAL A C   1 
ATOM   1345 O  O   . VAL A 1 159 ? -4.241  -3.648  -14.968 1.00 15.84  ? 160 VAL A O   1 
ATOM   1346 C  CB  . VAL A 1 159 ? -5.752  -2.743  -12.008 1.00 15.24  ? 160 VAL A CB  1 
ATOM   1347 C  CG1 . VAL A 1 159 ? -4.253  -2.809  -11.740 1.00 16.22  ? 160 VAL A CG1 1 
ATOM   1348 C  CG2 . VAL A 1 159 ? -6.435  -1.584  -11.333 1.00 16.35  ? 160 VAL A CG2 1 
ATOM   1349 N  N   . VAL A 1 160 ? -5.686  -5.102  -13.985 1.00 13.87  ? 161 VAL A N   1 
ATOM   1350 C  CA  . VAL A 1 160 ? -4.931  -6.249  -14.564 1.00 14.82  ? 161 VAL A CA  1 
ATOM   1351 C  C   . VAL A 1 160 ? -4.833  -6.175  -16.062 1.00 15.67  ? 161 VAL A C   1 
ATOM   1352 O  O   . VAL A 1 160 ? -3.819  -6.465  -16.655 1.00 17.56  ? 161 VAL A O   1 
ATOM   1353 C  CB  . VAL A 1 160 ? -5.661  -7.629  -14.172 1.00 18.68  ? 161 VAL A CB  1 
ATOM   1354 C  CG1 . VAL A 1 160 ? -5.237  -8.783  -15.064 1.00 21.36  ? 161 VAL A CG1 1 
ATOM   1355 C  CG2 . VAL A 1 160 ? -5.457  -7.797  -12.676 1.00 19.25  ? 161 VAL A CG2 1 
ATOM   1356 N  N   . ASP A 1 161 ? -5.906  -5.729  -16.687 1.00 17.86  ? 162 ASP A N   1 
ATOM   1357 C  CA  . ASP A 1 161 ? -5.943  -5.742  -18.148 1.00 21.52  ? 162 ASP A CA  1 
ATOM   1358 C  C   . ASP A 1 161 ? -5.099  -4.688  -18.801 1.00 19.68  ? 162 ASP A C   1 
ATOM   1359 O  O   . ASP A 1 161 ? -4.802  -4.789  -19.998 1.00 27.20  ? 162 ASP A O   1 
ATOM   1360 C  CB  . ASP A 1 161 ? -7.380  -5.675  -18.583 1.00 23.77  ? 162 ASP A CB  1 
ATOM   1361 C  CG  . ASP A 1 161 ? -8.044  -7.053  -18.529 1.00 22.39  ? 162 ASP A CG  1 
ATOM   1362 O  OD1 . ASP A 1 161 ? -7.380  -8.110  -18.599 1.00 25.02  ? 162 ASP A OD1 1 
ATOM   1363 O  OD2 . ASP A 1 161 ? -9.259  -7.055  -18.402 1.00 29.42  ? 162 ASP A OD2 1 
ATOM   1364 N  N   . VAL A 1 162 ? -4.650  -3.665  -18.078 1.00 19.95  ? 163 VAL A N   1 
ATOM   1365 C  CA  . VAL A 1 162 ? -3.849  -2.579  -18.620 1.00 21.73  ? 163 VAL A CA  1 
ATOM   1366 C  C   . VAL A 1 162 ? -2.348  -2.903  -18.453 1.00 18.39  ? 163 VAL A C   1 
ATOM   1367 O  O   . VAL A 1 162 ? -1.458  -2.213  -18.999 1.00 20.60  ? 163 VAL A O   1 
ATOM   1368 C  CB  . VAL A 1 162 ? -4.315  -1.198  -18.019 1.00 23.41  ? 163 VAL A CB  1 
ATOM   1369 C  CG1 . VAL A 1 162 ? -3.649  -0.968  -16.690 1.00 23.02  ? 163 VAL A CG1 1 
ATOM   1370 C  CG2 . VAL A 1 162 ? -4.107  0.024   -18.914 1.00 21.33  ? 163 VAL A CG2 1 
ATOM   1371 N  N   . LEU A 1 163 ? -2.030  -3.899  -17.632 1.00 19.82  ? 164 LEU A N   1 
ATOM   1372 C  CA  . LEU A 1 163 ? -0.637  -4.144  -17.277 1.00 17.48  ? 164 LEU A CA  1 
ATOM   1373 C  C   . LEU A 1 163 ? 0.258   -4.501  -18.441 1.00 18.89  ? 164 LEU A C   1 
ATOM   1374 O  O   . LEU A 1 163 ? 1.468   -4.177  -18.447 1.00 19.71  ? 164 LEU A O   1 
ATOM   1375 C  CB  . LEU A 1 163 ? -0.473  -5.213  -16.184 1.00 16.10  ? 164 LEU A CB  1 
ATOM   1376 C  CG  . LEU A 1 163 ? -1.099  -4.851  -14.836 1.00 13.55  ? 164 LEU A CG  1 
ATOM   1377 C  CD1 . LEU A 1 163 ? -0.911  -5.974  -13.832 1.00 16.66  ? 164 LEU A CD1 1 
ATOM   1378 C  CD2 . LEU A 1 163 ? -0.535  -3.555  -14.280 1.00 15.09  ? 164 LEU A CD2 1 
ATOM   1379 N  N   . ASP A 1 164 ? -0.313  -5.203  -19.441 1.00 22.08  ? 165 ASP A N   1 
ATOM   1380 C  CA  . ASP A 1 164 ? 0.526   -5.498  -20.578 1.00 25.07  ? 165 ASP A CA  1 
ATOM   1381 C  C   . ASP A 1 164 ? 1.016   -4.197  -21.299 1.00 27.97  ? 165 ASP A C   1 
ATOM   1382 O  O   . ASP A 1 164 ? 1.987   -4.314  -22.061 1.00 30.78  ? 165 ASP A O   1 
ATOM   1383 C  CB  . ASP A 1 164 ? -0.189  -6.370  -21.586 1.00 33.82  ? 165 ASP A CB  1 
ATOM   1384 C  CG  . ASP A 1 164 ? -1.226  -5.606  -22.369 1.00 48.42  ? 165 ASP A CG  1 
ATOM   1385 O  OD1 . ASP A 1 164 ? -1.948  -4.741  -21.800 1.00 61.79  ? 165 ASP A OD1 1 
ATOM   1386 O  OD2 . ASP A 1 164 ? -1.360  -5.903  -23.579 1.00 116.05 ? 165 ASP A OD2 1 
ATOM   1387 N  N   . SER A 1 165 ? 0.349   -3.049  -21.105 1.00 21.98  ? 166 SER A N   1 
ATOM   1388 C  CA  . SER A 1 165 ? 0.753   -1.802  -21.738 1.00 24.89  ? 166 SER A CA  1 
ATOM   1389 C  C   . SER A 1 165 ? 1.806   -1.076  -20.966 1.00 22.24  ? 166 SER A C   1 
ATOM   1390 O  O   . SER A 1 165 ? 2.365   -0.069  -21.444 1.00 22.67  ? 166 SER A O   1 
ATOM   1391 C  CB  . SER A 1 165 ? -0.440  -0.916  -21.965 1.00 28.34  ? 166 SER A CB  1 
ATOM   1392 O  OG  . SER A 1 165 ? -0.786  -0.321  -20.772 1.00 28.16  ? 166 SER A OG  1 
ATOM   1393 N  N   . ILE A 1 166 ? 2.069   -1.552  -19.737 1.00 19.05  ? 167 ILE A N   1 
ATOM   1394 C  CA  . ILE A 1 166 ? 3.066   -0.864  -18.932 1.00 16.72  ? 167 ILE A CA  1 
ATOM   1395 C  C   . ILE A 1 166 ? 3.997   -1.933  -18.419 1.00 13.42  ? 167 ILE A C   1 
ATOM   1396 O  O   . ILE A 1 166 ? 4.468   -1.966  -17.245 1.00 17.70  ? 167 ILE A O   1 
ATOM   1397 C  CB  . ILE A 1 166 ? 2.480   -0.055  -17.760 1.00 16.99  ? 167 ILE A CB  1 
ATOM   1398 C  CG1 . ILE A 1 166 ? 1.580   -0.883  -16.847 1.00 17.15  ? 167 ILE A CG1 1 
ATOM   1399 C  CG2 . ILE A 1 166 ? 1.771   1.169   -18.330 1.00 18.25  ? 167 ILE A CG2 1 
ATOM   1400 C  CD1 . ILE A 1 166 ? 1.639   -0.303  -15.444 1.00 16.42  ? 167 ILE A CD1 1 
ATOM   1401 N  N   . LYS A 1 167 ? 4.400   -2.854  -19.321 1.00 18.55  ? 168 LYS A N   1 
ATOM   1402 C  CA  . LYS A 1 167 ? 5.142   -4.013  -18.869 1.00 17.75  ? 168 LYS A CA  1 
ATOM   1403 C  C   . LYS A 1 167 ? 6.401   -3.628  -18.234 1.00 15.77  ? 168 LYS A C   1 
ATOM   1404 O  O   . LYS A 1 167 ? 6.904   -4.264  -17.263 1.00 15.71  ? 168 LYS A O   1 
ATOM   1405 C  CB  . LYS A 1 167 ? 5.574   -4.937  -20.038 1.00 19.14  ? 168 LYS A CB  1 
ATOM   1406 C  CG  . LYS A 1 167 ? 6.372   -6.179  -19.578 1.00 19.11  ? 168 LYS A CG  1 
ATOM   1407 C  CD  . LYS A 1 167 ? 6.708   -7.111  -20.800 1.00 31.97  ? 168 LYS A CD  1 
ATOM   1408 C  CE  . LYS A 1 167 ? 7.213   -8.490  -20.415 1.00 36.75  ? 168 LYS A CE  1 
ATOM   1409 N  NZ  . LYS A 1 167 ? 7.576   -9.302  -21.641 1.00 38.64  ? 168 LYS A NZ  1 
ATOM   1410 N  N   . THR A 1 168 ? 7.019   -2.613  -18.823 1.00 15.39  ? 169 THR A N   1 
ATOM   1411 C  CA  . THR A 1 168 ? 8.369   -2.258  -18.432 1.00 13.57  ? 169 THR A CA  1 
ATOM   1412 C  C   . THR A 1 168 ? 8.494   -0.906  -17.739 1.00 15.10  ? 169 THR A C   1 
ATOM   1413 O  O   . THR A 1 168 ? 7.643   -0.027  -17.882 1.00 17.50  ? 169 THR A O   1 
ATOM   1414 C  CB  . THR A 1 168 ? 9.327   -2.335  -19.633 1.00 16.33  ? 169 THR A CB  1 
ATOM   1415 O  OG1 . THR A 1 168 ? 8.802   -1.553  -20.714 1.00 20.74  ? 169 THR A OG1 1 
ATOM   1416 C  CG2 . THR A 1 168 ? 9.468   -3.780  -20.089 1.00 20.29  ? 169 THR A CG2 1 
ATOM   1417 N  N   A LYS A 1 169 ? 9.572   -0.770  -16.981 0.50 17.53  ? 170 LYS A N   1 
ATOM   1418 N  N   B LYS A 1 169 ? 9.591   -0.760  -17.000 0.50 17.77  ? 170 LYS A N   1 
ATOM   1419 C  CA  A LYS A 1 169 ? 9.866   0.467   -16.209 0.50 16.19  ? 170 LYS A CA  1 
ATOM   1420 C  CA  B LYS A 1 169 ? 9.897   0.466   -16.204 0.50 17.00  ? 170 LYS A CA  1 
ATOM   1421 C  C   A LYS A 1 169 ? 9.842   1.738   -16.981 0.50 17.32  ? 170 LYS A C   1 
ATOM   1422 C  C   B LYS A 1 169 ? 9.834   1.742   -16.991 0.50 17.36  ? 170 LYS A C   1 
ATOM   1423 O  O   A LYS A 1 169 ? 10.483  1.871   -18.023 0.50 22.14  ? 170 LYS A O   1 
ATOM   1424 O  O   B LYS A 1 169 ? 10.407  1.837   -18.091 0.50 21.82  ? 170 LYS A O   1 
ATOM   1425 C  CB  A LYS A 1 169 ? 11.230  0.283   -15.599 0.50 15.20  ? 170 LYS A CB  1 
ATOM   1426 C  CB  B LYS A 1 169 ? 11.299  0.308   -15.634 0.50 16.05  ? 170 LYS A CB  1 
ATOM   1427 C  CG  A LYS A 1 169 ? 11.711  1.546   -14.923 0.50 19.01  ? 170 LYS A CG  1 
ATOM   1428 C  CG  B LYS A 1 169 ? 11.702  1.472   -14.733 0.50 19.79  ? 170 LYS A CG  1 
ATOM   1429 C  CD  A LYS A 1 169 ? 12.976  1.239   -14.175 0.50 14.01  ? 170 LYS A CD  1 
ATOM   1430 C  CD  B LYS A 1 169 ? 13.182  1.745   -14.684 0.50 24.37  ? 170 LYS A CD  1 
ATOM   1431 C  CE  A LYS A 1 169 ? 14.011  0.697   -15.160 0.50 22.19  ? 170 LYS A CE  1 
ATOM   1432 C  CE  B LYS A 1 169 ? 13.935  1.107   -13.526 0.50 26.48  ? 170 LYS A CE  1 
ATOM   1433 N  NZ  A LYS A 1 169 ? 15.401  0.510   -14.661 0.50 24.95  ? 170 LYS A NZ  1 
ATOM   1434 N  NZ  B LYS A 1 169 ? 15.124  1.894   -13.081 0.50 38.10  ? 170 LYS A NZ  1 
ATOM   1435 N  N   . GLY A 1 170 ? 9.057   2.686   -16.468 1.00 18.53  ? 171 GLY A N   1 
ATOM   1436 C  CA  . GLY A 1 170 ? 8.901   3.923   -17.194 1.00 17.87  ? 171 GLY A CA  1 
ATOM   1437 C  C   . GLY A 1 170 ? 7.686   4.036   -18.081 1.00 18.99  ? 171 GLY A C   1 
ATOM   1438 O  O   . GLY A 1 170 ? 7.472   5.153   -18.546 1.00 25.56  ? 171 GLY A O   1 
ATOM   1439 N  N   . LYS A 1 171 ? 7.022   2.934   -18.476 1.00 15.51  ? 172 LYS A N   1 
ATOM   1440 C  CA  . LYS A 1 171 ? 5.686   2.998   -19.171 1.00 18.56  ? 172 LYS A CA  1 
ATOM   1441 C  C   . LYS A 1 171 ? 4.467   3.506   -18.359 1.00 15.32  ? 172 LYS A C   1 
ATOM   1442 O  O   . LYS A 1 171 ? 4.352   3.089   -17.183 1.00 16.34  ? 172 LYS A O   1 
ATOM   1443 C  CB  . LYS A 1 171 ? 5.526   1.665   -19.846 1.00 18.60  ? 172 LYS A CB  1 
ATOM   1444 C  CG  . LYS A 1 171 ? 6.649   1.209   -20.765 1.00 21.54  ? 172 LYS A CG  1 
ATOM   1445 C  CD  . LYS A 1 171 ? 6.208   0.107   -21.777 1.00 32.49  ? 172 LYS A CD  1 
ATOM   1446 C  CE  . LYS A 1 171 ? 5.186   0.562   -22.820 1.00 45.44  ? 172 LYS A CE  1 
ATOM   1447 N  NZ  . LYS A 1 171 ? 4.655   -0.510  -23.746 1.00 47.35  ? 172 LYS A NZ  1 
ATOM   1448 N  N   . SER A 1 172 ? 3.595   4.335   -18.855 1.00 16.19  ? 173 SER A N   1 
ATOM   1449 C  CA  . SER A 1 172 ? 2.408   4.862   -18.327 1.00 16.23  ? 173 SER A CA  1 
ATOM   1450 C  C   . SER A 1 172 ? 1.233   4.705   -19.231 1.00 12.06  ? 173 SER A C   1 
ATOM   1451 O  O   . SER A 1 172 ? 1.481   4.581   -20.425 1.00 19.82  ? 173 SER A O   1 
ATOM   1452 C  CB  . SER A 1 172 ? 2.670   6.218   -17.782 1.00 20.88  ? 173 SER A CB  1 
ATOM   1453 O  OG  . SER A 1 172 ? 3.383   7.118   -18.679 1.00 30.45  ? 173 SER A OG  1 
ATOM   1454 N  N   . ALA A 1 173 ? -0.016  4.736   -18.836 1.00 19.04  ? 174 ALA A N   1 
ATOM   1455 C  CA  . ALA A 1 173 ? -1.209  4.742   -19.618 1.00 20.37  ? 174 ALA A CA  1 
ATOM   1456 C  C   . ALA A 1 173 ? -2.333  5.471   -18.943 1.00 19.11  ? 174 ALA A C   1 
ATOM   1457 O  O   . ALA A 1 173 ? -2.255  5.543   -17.694 1.00 18.26  ? 174 ALA A O   1 
ATOM   1458 C  CB  . ALA A 1 173 ? -1.503  3.282   -19.861 1.00 25.28  ? 174 ALA A CB  1 
ATOM   1459 N  N   . ASP A 1 174 ? -3.047  6.285   -19.727 1.00 19.51  ? 175 ASP A N   1 
ATOM   1460 C  CA  . ASP A 1 174 ? -4.295  6.865   -19.275 1.00 18.47  ? 175 ASP A CA  1 
ATOM   1461 C  C   . ASP A 1 174 ? -4.975  5.832   -18.560 1.00 21.95  ? 175 ASP A C   1 
ATOM   1462 O  O   . ASP A 1 174 ? -4.949  4.663   -18.977 1.00 27.74  ? 175 ASP A O   1 
ATOM   1463 C  CB  . ASP A 1 174 ? -5.106  7.377   -20.464 1.00 27.27  ? 175 ASP A CB  1 
ATOM   1464 C  CG  . ASP A 1 174 ? -4.353  8.464   -21.179 1.00 36.13  ? 175 ASP A CG  1 
ATOM   1465 O  OD1 . ASP A 1 174 ? -3.642  9.219   -20.493 1.00 49.47  ? 175 ASP A OD1 1 
ATOM   1466 O  OD2 . ASP A 1 174 ? -4.334  8.524   -22.412 1.00 32.39  ? 175 ASP A OD2 1 
ATOM   1467 N  N   . PHE A 1 175 ? -5.427  6.226   -17.395 1.00 20.78  ? 176 PHE A N   1 
ATOM   1468 C  CA  . PHE A 1 175 ? -6.165  5.264   -16.618 1.00 20.37  ? 176 PHE A CA  1 
ATOM   1469 C  C   . PHE A 1 175 ? -7.127  6.101   -15.864 1.00 19.41  ? 176 PHE A C   1 
ATOM   1470 O  O   . PHE A 1 175 ? -6.897  6.410   -14.712 1.00 22.41  ? 176 PHE A O   1 
ATOM   1471 C  CB  . PHE A 1 175 ? -5.251  4.457   -15.734 1.00 20.65  ? 176 PHE A CB  1 
ATOM   1472 C  CG  . PHE A 1 175 ? -5.878  3.249   -15.196 1.00 18.76  ? 176 PHE A CG  1 
ATOM   1473 C  CD1 . PHE A 1 175 ? -6.215  2.176   -16.029 1.00 20.14  ? 176 PHE A CD1 1 
ATOM   1474 C  CD2 . PHE A 1 175 ? -6.098  3.118   -13.861 1.00 19.66  ? 176 PHE A CD2 1 
ATOM   1475 C  CE1 . PHE A 1 175 ? -6.722  1.043   -15.527 1.00 21.09  ? 176 PHE A CE1 1 
ATOM   1476 C  CE2 . PHE A 1 175 ? -6.631  1.962   -13.344 1.00 19.93  ? 176 PHE A CE2 1 
ATOM   1477 C  CZ  . PHE A 1 175 ? -6.954  0.917   -14.192 1.00 23.17  ? 176 PHE A CZ  1 
ATOM   1478 N  N   . THR A 1 176 ? -8.175  6.502   -16.559 1.00 18.07  ? 177 THR A N   1 
ATOM   1479 C  CA  . THR A 1 176 ? -9.203  7.339   -15.985 1.00 20.02  ? 177 THR A CA  1 
ATOM   1480 C  C   . THR A 1 176 ? -10.393 6.520   -15.570 1.00 15.99  ? 177 THR A C   1 
ATOM   1481 O  O   . THR A 1 176 ? -10.553 5.359   -16.020 1.00 18.08  ? 177 THR A O   1 
ATOM   1482 C  CB  . THR A 1 176 ? -9.657  8.389   -17.018 1.00 21.66  ? 177 THR A CB  1 
ATOM   1483 O  OG1 . THR A 1 176 ? -9.984  7.734   -18.269 1.00 26.08  ? 177 THR A OG1 1 
ATOM   1484 C  CG2 . THR A 1 176 ? -8.582  9.478   -17.148 1.00 26.25  ? 177 THR A CG2 1 
ATOM   1485 N  N   . ASN A 1 177 ? -11.213 7.065   -14.664 1.00 18.81  ? 178 ASN A N   1 
ATOM   1486 C  CA  . ASN A 1 177 ? -12.475 6.497   -14.239 1.00 19.25  ? 178 ASN A CA  1 
ATOM   1487 C  C   . ASN A 1 177 ? -12.309 5.202   -13.500 1.00 19.59  ? 178 ASN A C   1 
ATOM   1488 O  O   . ASN A 1 177 ? -13.209 4.408   -13.529 1.00 24.51  ? 178 ASN A O   1 
ATOM   1489 C  CB  . ASN A 1 177 ? -13.436 6.390   -15.430 1.00 20.55  ? 178 ASN A CB  1 
ATOM   1490 C  CG  . ASN A 1 177 ? -13.715 7.768   -16.022 1.00 18.37  ? 178 ASN A CG  1 
ATOM   1491 O  OD1 . ASN A 1 177 ? -14.317 8.617   -15.379 1.00 22.40  ? 178 ASN A OD1 1 
ATOM   1492 N  ND2 . ASN A 1 177 ? -13.144 8.036   -17.180 1.00 19.79  ? 178 ASN A ND2 1 
ATOM   1493 N  N   . PHE A 1 178 ? -11.139 4.944   -12.868 1.00 17.21  ? 179 PHE A N   1 
ATOM   1494 C  CA  . PHE A 1 178 ? -11.054 3.737   -12.070 1.00 17.54  ? 179 PHE A CA  1 
ATOM   1495 C  C   . PHE A 1 178 ? -11.584 4.020   -10.687 1.00 14.63  ? 179 PHE A C   1 
ATOM   1496 O  O   . PHE A 1 178 ? -11.191 4.990   -10.076 1.00 16.05  ? 179 PHE A O   1 
ATOM   1497 C  CB  . PHE A 1 178 ? -9.644  3.261   -11.968 1.00 16.78  ? 179 PHE A CB  1 
ATOM   1498 C  CG  . PHE A 1 178 ? -9.532  2.039   -11.152 1.00 16.11  ? 179 PHE A CG  1 
ATOM   1499 C  CD1 . PHE A 1 178 ? -9.867  0.761   -11.713 1.00 17.62  ? 179 PHE A CD1 1 
ATOM   1500 C  CD2 . PHE A 1 178 ? -9.170  2.116   -9.813  1.00 13.96  ? 179 PHE A CD2 1 
ATOM   1501 C  CE1 . PHE A 1 178 ? -9.839  -0.357  -10.955 1.00 19.64  ? 179 PHE A CE1 1 
ATOM   1502 C  CE2 . PHE A 1 178 ? -9.168  0.873   -9.056  1.00 12.90  ? 179 PHE A CE2 1 
ATOM   1503 C  CZ  . PHE A 1 178 ? -9.517  -0.274  -9.620  1.00 14.51  ? 179 PHE A CZ  1 
ATOM   1504 N  N   . ASP A 1 179 ? -12.486 3.153   -10.201 1.00 15.13  ? 180 ASP A N   1 
ATOM   1505 C  CA  . ASP A 1 179 ? -13.126 3.374   -8.917  1.00 15.66  ? 180 ASP A CA  1 
ATOM   1506 C  C   . ASP A 1 179 ? -12.462 2.486   -7.850  1.00 13.57  ? 180 ASP A C   1 
ATOM   1507 O  O   . ASP A 1 179 ? -12.634 1.272   -7.825  1.00 14.05  ? 180 ASP A O   1 
ATOM   1508 C  CB  . ASP A 1 179 ? -14.624 2.936   -9.035  1.00 17.42  ? 180 ASP A CB  1 
ATOM   1509 C  CG  . ASP A 1 179 ? -15.425 3.339   -7.806  1.00 17.82  ? 180 ASP A CG  1 
ATOM   1510 O  OD1 . ASP A 1 179 ? -14.796 3.610   -6.734  1.00 17.19  ? 180 ASP A OD1 1 
ATOM   1511 O  OD2 . ASP A 1 179 ? -16.634 3.478   -7.938  1.00 29.06  ? 180 ASP A OD2 1 
ATOM   1512 N  N   . PRO A 1 180 ? -11.689 3.078   -6.904  1.00 11.97  ? 181 PRO A N   1 
ATOM   1513 C  CA  . PRO A 1 180 ? -10.966 2.220   -5.927  1.00 11.72  ? 181 PRO A CA  1 
ATOM   1514 C  C   . PRO A 1 180 ? -11.915 1.615   -4.861  1.00 11.97  ? 181 PRO A C   1 
ATOM   1515 O  O   . PRO A 1 180 ? -11.473 0.728   -4.137  1.00 11.82  ? 181 PRO A O   1 
ATOM   1516 C  CB  . PRO A 1 180 ? -9.922  3.193   -5.347  1.00 12.74  ? 181 PRO A CB  1 
ATOM   1517 C  CG  . PRO A 1 180 ? -10.592 4.553   -5.480  1.00 13.76  ? 181 PRO A CG  1 
ATOM   1518 C  CD  . PRO A 1 180 ? -11.341 4.494   -6.811  1.00 12.84  ? 181 PRO A CD  1 
ATOM   1519 N  N   . ARG A 1 181 ? -13.204 2.006   -4.849  1.00 11.69  ? 182 ARG A N   1 
ATOM   1520 C  CA  . ARG A 1 181 ? -14.166 1.337   -3.932  1.00 12.38  ? 182 ARG A CA  1 
ATOM   1521 C  C   . ARG A 1 181 ? -14.231 -0.133  -4.277  1.00 13.10  ? 182 ARG A C   1 
ATOM   1522 O  O   . ARG A 1 181 ? -14.591 -0.936  -3.405  1.00 14.32  ? 182 ARG A O   1 
ATOM   1523 C  CB  . ARG A 1 181 ? -15.539 1.972   -4.025  1.00 13.52  ? 182 ARG A CB  1 
ATOM   1524 C  CG  . ARG A 1 181 ? -15.524 3.400   -3.445  1.00 15.17  ? 182 ARG A CG  1 
ATOM   1525 C  CD  . ARG A 1 181 ? -16.893 4.091   -3.538  1.00 17.91  ? 182 ARG A CD  1 
ATOM   1526 N  NE  . ARG A 1 181 ? -17.193 4.356   -4.922  1.00 19.19  ? 182 ARG A NE  1 
ATOM   1527 C  CZ  . ARG A 1 181 ? -18.284 5.015   -5.302  1.00 22.11  ? 182 ARG A CZ  1 
ATOM   1528 N  NH1 . ARG A 1 181 ? -19.163 5.461   -4.411  1.00 25.00  ? 182 ARG A NH1 1 
ATOM   1529 N  NH2 . ARG A 1 181 ? -18.509 5.202   -6.589  1.00 22.59  ? 182 ARG A NH2 1 
ATOM   1530 N  N   . GLY A 1 182 ? -13.967 -0.490  -5.523  1.00 13.35  ? 183 GLY A N   1 
ATOM   1531 C  CA  . GLY A 1 182 ? -14.071 -1.893  -5.898  1.00 15.53  ? 183 GLY A CA  1 
ATOM   1532 C  C   . GLY A 1 182 ? -12.944 -2.749  -5.400  1.00 15.11  ? 183 GLY A C   1 
ATOM   1533 O  O   . GLY A 1 182 ? -12.989 -3.939  -5.680  1.00 17.37  ? 183 GLY A O   1 
ATOM   1534 N  N   . LEU A 1 183 ? -11.975 -2.199  -4.643  1.00 13.01  ? 184 LEU A N   1 
ATOM   1535 C  CA  . LEU A 1 183 ? -10.854 -2.934  -4.100  1.00 12.84  ? 184 LEU A CA  1 
ATOM   1536 C  C   . LEU A 1 183 ? -11.021 -3.133  -2.600  1.00 12.20  ? 184 LEU A C   1 
ATOM   1537 O  O   . LEU A 1 183 ? -10.095 -3.725  -1.982  1.00 13.33  ? 184 LEU A O   1 
ATOM   1538 C  CB  . LEU A 1 183 ? -9.548  -2.245  -4.410  1.00 12.91  ? 184 LEU A CB  1 
ATOM   1539 C  CG  . LEU A 1 183 ? -9.208  -2.145  -5.890  1.00 15.23  ? 184 LEU A CG  1 
ATOM   1540 C  CD1 . LEU A 1 183 ? -7.958  -1.295  -6.022  1.00 18.00  ? 184 LEU A CD1 1 
ATOM   1541 C  CD2 . LEU A 1 183 ? -9.138  -3.427  -6.673  1.00 16.94  ? 184 LEU A CD2 1 
ATOM   1542 N  N   . LEU A 1 184 ? -12.128 -2.673  -1.993  1.00 12.57  ? 185 LEU A N   1 
ATOM   1543 C  CA  . LEU A 1 184 ? -12.265 -2.710  -0.542  1.00 12.02  ? 185 LEU A CA  1 
ATOM   1544 C  C   . LEU A 1 184 ? -13.064 -3.948  -0.037  1.00 13.92  ? 185 LEU A C   1 
ATOM   1545 O  O   . LEU A 1 184 ? -14.115 -4.345  -0.573  1.00 19.66  ? 185 LEU A O   1 
ATOM   1546 C  CB  . LEU A 1 184 ? -13.054 -1.480  -0.009  1.00 11.08  ? 185 LEU A CB  1 
ATOM   1547 C  CG  . LEU A 1 184 ? -12.450 -0.135  -0.422  1.00 10.56  ? 185 LEU A CG  1 
ATOM   1548 C  CD1 . LEU A 1 184 ? -13.285 1.019   0.078   1.00 12.46  ? 185 LEU A CD1 1 
ATOM   1549 C  CD2 . LEU A 1 184 ? -11.022 0.034   0.101   1.00 13.78  ? 185 LEU A CD2 1 
ATOM   1550 N  N   . PRO A 1 185 ? -12.650 -4.537  1.060   1.00 11.01  ? 186 PRO A N   1 
ATOM   1551 C  CA  . PRO A 1 185 ? -13.367 -5.665  1.602   1.00 12.31  ? 186 PRO A CA  1 
ATOM   1552 C  C   . PRO A 1 185 ? -14.657 -5.120  2.238   1.00 12.40  ? 186 PRO A C   1 
ATOM   1553 O  O   . PRO A 1 185 ? -14.851 -3.930  2.342   1.00 16.16  ? 186 PRO A O   1 
ATOM   1554 C  CB  . PRO A 1 185 ? -12.377 -6.273  2.631   1.00 11.67  ? 186 PRO A CB  1 
ATOM   1555 C  CG  . PRO A 1 185 ? -11.693 -5.034  3.113   1.00 9.79   ? 186 PRO A CG  1 
ATOM   1556 C  CD  . PRO A 1 185 ? -11.500 -4.151  1.875   1.00 9.53   ? 186 PRO A CD  1 
ATOM   1557 N  N   A GLU A 1 186 ? -15.459 -6.041  2.736   0.50 13.69  ? 187 GLU A N   1 
ATOM   1558 N  N   B GLU A 1 186 ? -15.482 -6.037  2.744   0.50 13.72  ? 187 GLU A N   1 
ATOM   1559 C  CA  A GLU A 1 186 ? -16.713 -5.673  3.300   0.50 15.13  ? 187 GLU A CA  1 
ATOM   1560 C  CA  B GLU A 1 186 ? -16.736 -5.662  3.377   0.50 15.33  ? 187 GLU A CA  1 
ATOM   1561 C  C   A GLU A 1 186 ? -16.540 -4.926  4.619   0.50 13.02  ? 187 GLU A C   1 
ATOM   1562 C  C   B GLU A 1 186 ? -16.518 -4.891  4.632   0.50 13.33  ? 187 GLU A C   1 
ATOM   1563 O  O   A GLU A 1 186 ? -17.133 -3.853  4.859   0.50 17.25  ? 187 GLU A O   1 
ATOM   1564 O  O   B GLU A 1 186 ? -17.106 -3.832  4.879   0.50 16.90  ? 187 GLU A O   1 
ATOM   1565 C  CB  A GLU A 1 186 ? -17.480 -6.971  3.458   0.50 20.12  ? 187 GLU A CB  1 
ATOM   1566 C  CB  B GLU A 1 186 ? -17.480 -6.925  3.773   0.50 22.31  ? 187 GLU A CB  1 
ATOM   1567 C  CG  A GLU A 1 186 ? -18.611 -6.892  4.423   0.50 25.61  ? 187 GLU A CG  1 
ATOM   1568 C  CG  B GLU A 1 186 ? -18.392 -7.462  2.710   0.50 23.41  ? 187 GLU A CG  1 
ATOM   1569 C  CD  A GLU A 1 186 ? -19.331 -8.209  4.588   0.50 31.67  ? 187 GLU A CD  1 
ATOM   1570 C  CD  B GLU A 1 186 ? -19.048 -8.756  3.115   0.50 33.92  ? 187 GLU A CD  1 
ATOM   1571 O  OE1 A GLU A 1 186 ? -19.232 -9.091  3.691   0.50 33.39  ? 187 GLU A OE1 1 
ATOM   1572 O  OE1 B GLU A 1 186 ? -19.093 -9.102  4.325   0.50 28.43  ? 187 GLU A OE1 1 
ATOM   1573 O  OE2 A GLU A 1 186 ? -19.936 -8.356  5.668   0.50 48.79  ? 187 GLU A OE2 1 
ATOM   1574 O  OE2 B GLU A 1 186 ? -19.543 -9.438  2.193   0.50 35.60  ? 187 GLU A OE2 1 
ATOM   1575 N  N   . SER A 1 187 ? -15.640 -5.424  5.479   1.00 12.38  ? 188 SER A N   1 
ATOM   1576 C  CA  . SER A 1 187 ? -15.423 -4.809  6.787   1.00 13.22  ? 188 SER A CA  1 
ATOM   1577 C  C   . SER A 1 187 ? -14.286 -3.815  6.770   1.00 11.85  ? 188 SER A C   1 
ATOM   1578 O  O   . SER A 1 187 ? -13.255 -4.085  6.169   1.00 12.77  ? 188 SER A O   1 
ATOM   1579 C  CB  . SER A 1 187 ? -15.011 -5.894  7.775   1.00 14.01  ? 188 SER A CB  1 
ATOM   1580 O  OG  . SER A 1 187 ? -14.790 -5.389  9.069   1.00 14.38  ? 188 SER A OG  1 
ATOM   1581 N  N   . LEU A 1 188 ? -14.452 -2.741  7.482   1.00 12.34  ? 189 LEU A N   1 
ATOM   1582 C  CA  . LEU A 1 188 ? -13.406 -1.766  7.727   1.00 12.13  ? 189 LEU A CA  1 
ATOM   1583 C  C   . LEU A 1 188 ? -12.760 -1.896  9.117   1.00 11.61  ? 189 LEU A C   1 
ATOM   1584 O  O   . LEU A 1 188 ? -12.067 -0.989  9.588   1.00 13.17  ? 189 LEU A O   1 
ATOM   1585 C  CB  . LEU A 1 188 ? -13.911 -0.315  7.472   1.00 13.99  ? 189 LEU A CB  1 
ATOM   1586 C  CG  . LEU A 1 188 ? -14.304 0.018   6.038   1.00 15.58  ? 189 LEU A CG  1 
ATOM   1587 C  CD1 . LEU A 1 188 ? -14.761 1.440   5.930   1.00 18.93  ? 189 LEU A CD1 1 
ATOM   1588 C  CD2 . LEU A 1 188 ? -13.175 -0.203  5.041   1.00 17.41  ? 189 LEU A CD2 1 
ATOM   1589 N  N   . ASP A 1 189 ? -12.924 -3.054  9.798   1.00 11.53  ? 190 ASP A N   1 
ATOM   1590 C  CA  . ASP A 1 189 ? -12.161 -3.282  11.012  1.00 12.45  ? 190 ASP A CA  1 
ATOM   1591 C  C   . ASP A 1 189 ? -10.647 -3.266  10.725  1.00 9.57   ? 190 ASP A C   1 
ATOM   1592 O  O   . ASP A 1 189 ? -10.202 -3.781  9.697   1.00 9.21   ? 190 ASP A O   1 
ATOM   1593 C  CB  . ASP A 1 189 ? -12.497 -4.624  11.622  1.00 14.21  ? 190 ASP A CB  1 
ATOM   1594 C  CG  . ASP A 1 189 ? -13.871 -4.668  12.266  1.00 20.93  ? 190 ASP A CG  1 
ATOM   1595 O  OD1 . ASP A 1 189 ? -14.507 -3.636  12.513  1.00 25.09  ? 190 ASP A OD1 1 
ATOM   1596 O  OD2 . ASP A 1 189 ? -14.337 -5.783  12.536  1.00 26.28  ? 190 ASP A OD2 1 
ATOM   1597 N  N   . TYR A 1 190 ? -9.884  -2.671  11.626  1.00 9.53   ? 191 TYR A N   1 
ATOM   1598 C  CA  . TYR A 1 190 ? -8.446  -2.427  11.330  1.00 8.83   ? 191 TYR A CA  1 
ATOM   1599 C  C   . TYR A 1 190 ? -7.584  -2.467  12.575  1.00 8.64   ? 191 TYR A C   1 
ATOM   1600 O  O   . TYR A 1 190 ? -7.991  -2.353  13.709  1.00 9.34   ? 191 TYR A O   1 
ATOM   1601 C  CB  . TYR A 1 190 ? -8.310  -1.039  10.642  1.00 8.97   ? 191 TYR A CB  1 
ATOM   1602 C  CG  . TYR A 1 190 ? -8.695  0.115   11.532  1.00 8.96   ? 191 TYR A CG  1 
ATOM   1603 C  CD1 . TYR A 1 190 ? -7.785  0.731   12.400  1.00 9.39   ? 191 TYR A CD1 1 
ATOM   1604 C  CD2 . TYR A 1 190 ? -9.996  0.647   11.480  1.00 10.44  ? 191 TYR A CD2 1 
ATOM   1605 C  CE1 . TYR A 1 190 ? -8.167  1.798   13.240  1.00 10.60  ? 191 TYR A CE1 1 
ATOM   1606 C  CE2 . TYR A 1 190 ? -10.394 1.721   12.318  1.00 11.22  ? 191 TYR A CE2 1 
ATOM   1607 C  CZ  . TYR A 1 190 ? -9.504  2.255   13.176  1.00 10.10  ? 191 TYR A CZ  1 
ATOM   1608 O  OH  . TYR A 1 190 ? -9.853  3.282   14.006  1.00 12.34  ? 191 TYR A OH  1 
ATOM   1609 N  N   . TRP A 1 191 ? -6.271  -2.606  12.248  1.00 7.34   ? 192 TRP A N   1 
ATOM   1610 C  CA  . TRP A 1 191 ? -5.205  -2.364  13.205  1.00 7.81   ? 192 TRP A CA  1 
ATOM   1611 C  C   . TRP A 1 191 ? -4.498  -1.069  12.780  1.00 6.95   ? 192 TRP A C   1 
ATOM   1612 O  O   . TRP A 1 191 ? -4.456  -0.721  11.616  1.00 8.19   ? 192 TRP A O   1 
ATOM   1613 C  CB  . TRP A 1 191 ? -4.151  -3.475  13.193  1.00 7.96   ? 192 TRP A CB  1 
ATOM   1614 C  CG  . TRP A 1 191 ? -4.676  -4.800  13.604  1.00 8.20   ? 192 TRP A CG  1 
ATOM   1615 C  CD1 . TRP A 1 191 ? -4.888  -5.226  14.900  1.00 10.58  ? 192 TRP A CD1 1 
ATOM   1616 C  CD2 . TRP A 1 191 ? -4.967  -5.941  12.751  1.00 8.01   ? 192 TRP A CD2 1 
ATOM   1617 N  NE1 . TRP A 1 191 ? -5.281  -6.553  14.898  1.00 10.54  ? 192 TRP A NE1 1 
ATOM   1618 C  CE2 . TRP A 1 191 ? -5.361  -7.003  13.596  1.00 10.32  ? 192 TRP A CE2 1 
ATOM   1619 C  CE3 . TRP A 1 191 ? -4.876  -6.159  11.379  1.00 9.07   ? 192 TRP A CE3 1 
ATOM   1620 C  CZ2 . TRP A 1 191 ? -5.671  -8.270  13.049  1.00 10.30  ? 192 TRP A CZ2 1 
ATOM   1621 C  CZ3 . TRP A 1 191 ? -5.148  -7.386  10.878  1.00 10.34  ? 192 TRP A CZ3 1 
ATOM   1622 C  CH2 . TRP A 1 191 ? -5.522  -8.435  11.685  1.00 11.30  ? 192 TRP A CH2 1 
ATOM   1623 N  N   . THR A 1 192 ? -3.891  -0.369  13.759  1.00 7.29   ? 193 THR A N   1 
ATOM   1624 C  CA  . THR A 1 192 ? -3.180  0.872   13.441  1.00 7.23   ? 193 THR A CA  1 
ATOM   1625 C  C   . THR A 1 192 ? -1.963  1.025   14.294  1.00 7.55   ? 193 THR A C   1 
ATOM   1626 O  O   . THR A 1 192 ? -1.933  0.643   15.454  1.00 8.47   ? 193 THR A O   1 
ATOM   1627 C  CB  . THR A 1 192 ? -4.133  2.083   13.539  1.00 7.90   ? 193 THR A CB  1 
ATOM   1628 O  OG1 . THR A 1 192 ? -3.422  3.273   13.149  1.00 8.12   ? 193 THR A OG1 1 
ATOM   1629 C  CG2 . THR A 1 192 ? -4.650  2.288   14.942  1.00 9.27   ? 193 THR A CG2 1 
ATOM   1630 N  N   . TYR A 1 193 ? -0.907  1.631   13.721  1.00 7.00   ? 194 TYR A N   1 
ATOM   1631 C  CA  . TYR A 1 193 ? 0.331   1.900   14.422  1.00 7.48   ? 194 TYR A CA  1 
ATOM   1632 C  C   . TYR A 1 193 ? 1.095   2.991   13.658  1.00 7.00   ? 194 TYR A C   1 
ATOM   1633 O  O   . TYR A 1 193 ? 0.885   3.166   12.461  1.00 7.44   ? 194 TYR A O   1 
ATOM   1634 C  CB  . TYR A 1 193 ? 1.180   0.625   14.618  1.00 7.69   ? 194 TYR A CB  1 
ATOM   1635 C  CG  . TYR A 1 193 ? 1.867   0.149   13.374  1.00 7.49   ? 194 TYR A CG  1 
ATOM   1636 C  CD1 . TYR A 1 193 ? 1.190   -0.569  12.379  1.00 7.11   ? 194 TYR A CD1 1 
ATOM   1637 C  CD2 . TYR A 1 193 ? 3.185   0.489   13.127  1.00 7.86   ? 194 TYR A CD2 1 
ATOM   1638 C  CE1 . TYR A 1 193 ? 1.805   -0.903  11.192  1.00 6.86   ? 194 TYR A CE1 1 
ATOM   1639 C  CE2 . TYR A 1 193 ? 3.829   0.161   11.952  1.00 7.45   ? 194 TYR A CE2 1 
ATOM   1640 C  CZ  . TYR A 1 193 ? 3.156   -0.512  10.963  1.00 6.46   ? 194 TYR A CZ  1 
ATOM   1641 O  OH  . TYR A 1 193 ? 3.788   -0.823  9.801   1.00 7.04   ? 194 TYR A OH  1 
ATOM   1642 N  N   . PRO A 1 194 ? 2.059   3.660   14.316  1.00 7.12   ? 195 PRO A N   1 
ATOM   1643 C  CA  . PRO A 1 194 ? 2.892   4.690   13.641  1.00 7.78   ? 195 PRO A CA  1 
ATOM   1644 C  C   . PRO A 1 194 ? 4.073   4.011   12.962  1.00 6.41   ? 195 PRO A C   1 
ATOM   1645 O  O   . PRO A 1 194 ? 4.811   3.249   13.625  1.00 8.48   ? 195 PRO A O   1 
ATOM   1646 C  CB  . PRO A 1 194 ? 3.344   5.580   14.802  1.00 9.36   ? 195 PRO A CB  1 
ATOM   1647 C  CG  . PRO A 1 194 ? 3.347   4.645   16.016  1.00 9.92   ? 195 PRO A CG  1 
ATOM   1648 C  CD  . PRO A 1 194 ? 2.220   3.692   15.811  1.00 10.28  ? 195 PRO A CD  1 
ATOM   1649 N  N   . GLY A 1 195 ? 4.326   4.338   11.718  1.00 7.02   ? 196 GLY A N   1 
ATOM   1650 C  CA  . GLY A 1 195 ? 5.425   3.715   10.980  1.00 7.19   ? 196 GLY A CA  1 
ATOM   1651 C  C   . GLY A 1 195 ? 5.960   4.582   9.873   1.00 6.15   ? 196 GLY A C   1 
ATOM   1652 O  O   . GLY A 1 195 ? 6.076   5.833   10.033  1.00 7.00   ? 196 GLY A O   1 
ATOM   1653 N  N   . SER A 1 196 ? 6.381   3.926   8.838   1.00 6.16   ? 197 SER A N   1 
ATOM   1654 C  CA  . SER A 1 196 ? 7.176   4.559   7.803   1.00 6.89   ? 197 SER A CA  1 
ATOM   1655 C  C   . SER A 1 196 ? 6.773   4.168   6.409   1.00 6.10   ? 197 SER A C   1 
ATOM   1656 O  O   . SER A 1 196 ? 6.007   3.189   6.224   1.00 6.74   ? 197 SER A O   1 
ATOM   1657 C  CB  . SER A 1 196 ? 8.703   4.165   7.957   1.00 7.12   ? 197 SER A CB  1 
ATOM   1658 O  OG  . SER A 1 196 ? 8.939   2.826   7.528   1.00 7.42   ? 197 SER A OG  1 
ATOM   1659 N  N   . LEU A 1 197 ? 7.291   4.851   5.401   1.00 6.33   ? 198 LEU A N   1 
ATOM   1660 C  CA  . LEU A 1 197 ? 7.281   4.291   4.058   1.00 6.63   ? 198 LEU A CA  1 
ATOM   1661 C  C   . LEU A 1 197 ? 8.011   2.980   4.059   1.00 6.68   ? 198 LEU A C   1 
ATOM   1662 O  O   . LEU A 1 197 ? 9.050   2.831   4.748   1.00 7.74   ? 198 LEU A O   1 
ATOM   1663 C  CB  . LEU A 1 197 ? 7.996   5.249   3.097   1.00 7.91   ? 198 LEU A CB  1 
ATOM   1664 C  CG  . LEU A 1 197 ? 7.455   6.671   3.009   1.00 8.31   ? 198 LEU A CG  1 
ATOM   1665 C  CD1 . LEU A 1 197 ? 8.300   7.487   2.021   1.00 10.81  ? 198 LEU A CD1 1 
ATOM   1666 C  CD2 . LEU A 1 197 ? 6.012   6.664   2.531   1.00 9.87   ? 198 LEU A CD2 1 
ATOM   1667 N  N   . THR A 1 198 ? 7.578   2.017   3.233   1.00 6.59   ? 199 THR A N   1 
ATOM   1668 C  CA  . THR A 1 198 ? 8.228   0.717   3.174   1.00 7.44   ? 199 THR A CA  1 
ATOM   1669 C  C   . THR A 1 198 ? 9.235   0.612   2.049   1.00 7.25   ? 199 THR A C   1 
ATOM   1670 O  O   . THR A 1 198 ? 9.845   -0.468  1.870   1.00 8.20   ? 199 THR A O   1 
ATOM   1671 C  CB  . THR A 1 198 ? 7.233   -0.425  3.091   1.00 7.28   ? 199 THR A CB  1 
ATOM   1672 O  OG1 . THR A 1 198 ? 6.661   -0.402  1.804   1.00 7.05   ? 199 THR A OG1 1 
ATOM   1673 C  CG2 . THR A 1 198 ? 6.171   -0.410  4.202   1.00 7.76   ? 199 THR A CG2 1 
ATOM   1674 N  N   . THR A 1 199 ? 9.425   1.688   1.266   1.00 8.21   ? 200 THR A N   1 
ATOM   1675 C  CA  . THR A 1 199 ? 10.509  1.776   0.272   1.00 8.75   ? 200 THR A CA  1 
ATOM   1676 C  C   . THR A 1 199 ? 11.299  3.016   0.586   1.00 8.86   ? 200 THR A C   1 
ATOM   1677 O  O   . THR A 1 199 ? 10.810  3.935   1.220   1.00 8.53   ? 200 THR A O   1 
ATOM   1678 C  CB  . THR A 1 199 ? 10.026  1.857   -1.198  1.00 9.04   ? 200 THR A CB  1 
ATOM   1679 O  OG1 . THR A 1 199 ? 9.431   3.129   -1.420  1.00 13.21  ? 200 THR A OG1 1 
ATOM   1680 C  CG2 . THR A 1 199 ? 9.048   0.807   -1.534  1.00 11.70  ? 200 THR A CG2 1 
ATOM   1681 N  N   . PRO A 1 200 ? 12.571  3.052   0.125   1.00 9.66   ? 201 PRO A N   1 
ATOM   1682 C  CA  . PRO A 1 200 ? 13.280  4.338   0.170   1.00 10.07  ? 201 PRO A CA  1 
ATOM   1683 C  C   . PRO A 1 200 ? 12.391  5.467   -0.342  1.00 10.94  ? 201 PRO A C   1 
ATOM   1684 O  O   . PRO A 1 200 ? 11.663  5.276   -1.346  1.00 11.65  ? 201 PRO A O   1 
ATOM   1685 C  CB  . PRO A 1 200 ? 14.512  4.052   -0.737  1.00 12.31  ? 201 PRO A CB  1 
ATOM   1686 C  CG  . PRO A 1 200 ? 14.788  2.594   -0.495  1.00 11.30  ? 201 PRO A CG  1 
ATOM   1687 C  CD  . PRO A 1 200 ? 13.379  1.969   -0.479  1.00 11.46  ? 201 PRO A CD  1 
ATOM   1688 N  N   . PRO A 1 201 ? 12.412  6.623   0.298   1.00 10.34  ? 202 PRO A N   1 
ATOM   1689 C  CA  . PRO A 1 201 ? 13.363  7.047   1.355   1.00 10.61  ? 202 PRO A CA  1 
ATOM   1690 C  C   . PRO A 1 201 ? 13.018  6.608   2.772   1.00 10.21  ? 202 PRO A C   1 
ATOM   1691 O  O   . PRO A 1 201 ? 13.674  7.026   3.722   1.00 10.45  ? 202 PRO A O   1 
ATOM   1692 C  CB  . PRO A 1 201 ? 13.357  8.590   1.222   1.00 12.95  ? 202 PRO A CB  1 
ATOM   1693 C  CG  . PRO A 1 201 ? 11.948  8.879   0.759   1.00 12.86  ? 202 PRO A CG  1 
ATOM   1694 C  CD  . PRO A 1 201 ? 11.604  7.769   -0.220  1.00 11.24  ? 202 PRO A CD  1 
ATOM   1695 N  N   . LEU A 1 202 ? 12.013  5.720   2.969   1.00 8.89   ? 203 LEU A N   1 
ATOM   1696 C  CA  . LEU A 1 202 ? 11.812  5.075   4.303   1.00 8.68   ? 203 LEU A CA  1 
ATOM   1697 C  C   . LEU A 1 202 ? 11.435  6.083   5.417   1.00 7.96   ? 203 LEU A C   1 
ATOM   1698 O  O   . LEU A 1 202 ? 11.587  5.832   6.572   1.00 8.12   ? 203 LEU A O   1 
ATOM   1699 C  CB  . LEU A 1 202 ? 13.025  4.241   4.740   1.00 9.09   ? 203 LEU A CB  1 
ATOM   1700 C  CG  . LEU A 1 202 ? 13.305  3.060   3.763   1.00 9.41   ? 203 LEU A CG  1 
ATOM   1701 C  CD1 . LEU A 1 202 ? 14.627  2.437   4.193   1.00 11.25  ? 203 LEU A CD1 1 
ATOM   1702 C  CD2 . LEU A 1 202 ? 12.217  2.022   3.729   1.00 9.84   ? 203 LEU A CD2 1 
ATOM   1703 N  N   . LEU A 1 203 ? 10.838  7.235   4.990   1.00 8.09   ? 204 LEU A N   1 
ATOM   1704 C  CA  . LEU A 1 203 ? 10.549  8.327   5.931   1.00 8.49   ? 204 LEU A CA  1 
ATOM   1705 C  C   . LEU A 1 203 ? 9.512   7.894   6.959   1.00 8.04   ? 204 LEU A C   1 
ATOM   1706 O  O   . LEU A 1 203 ? 8.550   7.171   6.646   1.00 8.14   ? 204 LEU A O   1 
ATOM   1707 C  CB  . LEU A 1 203 ? 10.053  9.529   5.167   1.00 9.34   ? 204 LEU A CB  1 
ATOM   1708 C  CG  . LEU A 1 203 ? 11.074  10.173  4.220   1.00 11.12  ? 204 LEU A CG  1 
ATOM   1709 C  CD1 . LEU A 1 203 ? 10.443  11.182  3.265   1.00 13.59  ? 204 LEU A CD1 1 
ATOM   1710 C  CD2 . LEU A 1 203 ? 12.302  10.721  5.018   1.00 15.43  ? 204 LEU A CD2 1 
ATOM   1711 N  N   . GLU A 1 204 ? 9.683   8.348   8.194   1.00 8.82   ? 205 GLU A N   1 
ATOM   1712 C  CA  . GLU A 1 204 ? 8.864   7.965   9.316   1.00 8.82   ? 205 GLU A CA  1 
ATOM   1713 C  C   . GLU A 1 204 ? 7.676   8.956   9.459   1.00 8.90   ? 205 GLU A C   1 
ATOM   1714 O  O   . GLU A 1 204 ? 7.583   9.742   10.407  1.00 10.59  ? 205 GLU A O   1 
ATOM   1715 C  CB  . GLU A 1 204 ? 9.739   7.821   10.575  1.00 9.93   ? 205 GLU A CB  1 
ATOM   1716 C  CG  . GLU A 1 204 ? 10.613  6.601   10.440  1.00 10.66  ? 205 GLU A CG  1 
ATOM   1717 C  CD  . GLU A 1 204 ? 11.555  6.333   11.600  1.00 10.87  ? 205 GLU A CD  1 
ATOM   1718 O  OE1 . GLU A 1 204 ? 11.886  7.272   12.385  1.00 13.95  ? 205 GLU A OE1 1 
ATOM   1719 O  OE2 . GLU A 1 204 ? 11.961  5.152   11.761  1.00 11.15  ? 205 GLU A OE2 1 
ATOM   1720 N  N   . CYS A 1 205 ? 6.797   8.871   8.504   1.00 7.66   ? 206 CYS A N   1 
ATOM   1721 C  CA  . CYS A 1 205 ? 5.735   9.871   8.297   1.00 7.91   ? 206 CYS A CA  1 
ATOM   1722 C  C   . CYS A 1 205 ? 4.385   9.244   8.167   1.00 6.91   ? 206 CYS A C   1 
ATOM   1723 O  O   . CYS A 1 205 ? 3.441   9.950   7.807   1.00 8.85   ? 206 CYS A O   1 
ATOM   1724 C  CB  . CYS A 1 205 ? 6.030   10.712  7.050   1.00 8.24   ? 206 CYS A CB  1 
ATOM   1725 S  SG  . CYS A 1 205 ? 6.075   9.730   5.502   1.00 9.29   ? 206 CYS A SG  1 
ATOM   1726 N  N   . VAL A 1 206 ? 4.232   7.943   8.472   1.00 6.93   ? 207 VAL A N   1 
ATOM   1727 C  CA  . VAL A 1 206 ? 2.999   7.252   8.128   1.00 6.71   ? 207 VAL A CA  1 
ATOM   1728 C  C   . VAL A 1 206 ? 2.238   6.781   9.345   1.00 6.76   ? 207 VAL A C   1 
ATOM   1729 O  O   . VAL A 1 206 ? 2.776   6.112   10.214  1.00 8.26   ? 207 VAL A O   1 
ATOM   1730 C  CB  . VAL A 1 206 ? 3.288   5.965   7.270   1.00 7.24   ? 207 VAL A CB  1 
ATOM   1731 C  CG1 . VAL A 1 206 ? 1.975   5.257   6.900   1.00 7.90   ? 207 VAL A CG1 1 
ATOM   1732 C  CG2 . VAL A 1 206 ? 4.026   6.359   5.993   1.00 8.47   ? 207 VAL A CG2 1 
ATOM   1733 N  N   . THR A 1 207 ? 0.913   7.091   9.385   1.00 6.30   ? 208 THR A N   1 
ATOM   1734 C  CA  . THR A 1 207 ? -0.014  6.364   10.247  1.00 7.24   ? 208 THR A CA  1 
ATOM   1735 C  C   . THR A 1 207 ? -0.556  5.187   9.414   1.00 6.25   ? 208 THR A C   1 
ATOM   1736 O  O   . THR A 1 207 ? -1.223  5.396   8.386   1.00 6.63   ? 208 THR A O   1 
ATOM   1737 C  CB  . THR A 1 207 ? -1.199  7.226   10.701  1.00 7.27   ? 208 THR A CB  1 
ATOM   1738 O  OG1 . THR A 1 207 ? -0.706  8.347   11.428  1.00 8.71   ? 208 THR A OG1 1 
ATOM   1739 C  CG2 . THR A 1 207 ? -2.142  6.408   11.583  1.00 9.69   ? 208 THR A CG2 1 
ATOM   1740 N  N   . TRP A 1 208 ? -0.199  3.957   9.813   1.00 5.86   ? 209 TRP A N   1 
ATOM   1741 C  CA  . TRP A 1 208 ? -0.620  2.774   9.098   1.00 5.99   ? 209 TRP A CA  1 
ATOM   1742 C  C   . TRP A 1 208 ? -2.015  2.352   9.614   1.00 5.69   ? 209 TRP A C   1 
ATOM   1743 O  O   . TRP A 1 208 ? -2.237  2.305   10.827  1.00 6.63   ? 209 TRP A O   1 
ATOM   1744 C  CB  . TRP A 1 208 ? 0.383   1.616   9.302   1.00 6.40   ? 209 TRP A CB  1 
ATOM   1745 C  CG  . TRP A 1 208 ? 1.493   1.730   8.339   1.00 5.95   ? 209 TRP A CG  1 
ATOM   1746 C  CD1 . TRP A 1 208 ? 2.746   2.308   8.505   1.00 6.59   ? 209 TRP A CD1 1 
ATOM   1747 C  CD2 . TRP A 1 208 ? 1.426   1.315   6.956   1.00 6.11   ? 209 TRP A CD2 1 
ATOM   1748 N  NE1 . TRP A 1 208 ? 3.416   2.293   7.343   1.00 6.89   ? 209 TRP A NE1 1 
ATOM   1749 C  CE2 . TRP A 1 208 ? 2.682   1.700   6.366   1.00 6.36   ? 209 TRP A CE2 1 
ATOM   1750 C  CE3 . TRP A 1 208 ? 0.468   0.688   6.179   1.00 5.76   ? 209 TRP A CE3 1 
ATOM   1751 C  CZ2 . TRP A 1 208 ? 2.937   1.462   5.031   1.00 7.20   ? 209 TRP A CZ2 1 
ATOM   1752 C  CZ3 . TRP A 1 208 ? 0.727   0.414   4.885   1.00 7.00   ? 209 TRP A CZ3 1 
ATOM   1753 C  CH2 . TRP A 1 208 ? 1.933   0.805   4.295   1.00 7.50   ? 209 TRP A CH2 1 
ATOM   1754 N  N   . ILE A 1 209 ? -2.876  2.000   8.693   1.00 5.74   ? 210 ILE A N   1 
ATOM   1755 C  CA  . ILE A 1 209 ? -4.224  1.483   8.991   1.00 6.10   ? 210 ILE A CA  1 
ATOM   1756 C  C   . ILE A 1 209 ? -4.325  0.213   8.134   1.00 5.55   ? 210 ILE A C   1 
ATOM   1757 O  O   . ILE A 1 209 ? -4.387  0.295   6.916   1.00 6.91   ? 210 ILE A O   1 
ATOM   1758 C  CB  . ILE A 1 209 ? -5.294  2.506   8.632   1.00 7.05   ? 210 ILE A CB  1 
ATOM   1759 C  CG1 . ILE A 1 209 ? -5.107  3.763   9.470   1.00 8.82   ? 210 ILE A CG1 1 
ATOM   1760 C  CG2 . ILE A 1 209 ? -6.687  1.882   8.869   1.00 8.57   ? 210 ILE A CG2 1 
ATOM   1761 C  CD1 . ILE A 1 209 ? -5.913  4.958   8.941   1.00 10.89  ? 210 ILE A CD1 1 
ATOM   1762 N  N   . VAL A 1 210 ? -4.283  -0.962  8.792   1.00 6.23   ? 211 VAL A N   1 
ATOM   1763 C  CA  . VAL A 1 210 ? -4.226  -2.244  8.086   1.00 6.07   ? 211 VAL A CA  1 
ATOM   1764 C  C   . VAL A 1 210 ? -5.556  -2.951  8.348   1.00 6.20   ? 211 VAL A C   1 
ATOM   1765 O  O   . VAL A 1 210 ? -5.887  -3.234  9.481   1.00 7.13   ? 211 VAL A O   1 
ATOM   1766 C  CB  . VAL A 1 210 ? -3.032  -3.115  8.544   1.00 7.00   ? 211 VAL A CB  1 
ATOM   1767 C  CG1 . VAL A 1 210 ? -3.046  -4.462  7.821   1.00 8.02   ? 211 VAL A CG1 1 
ATOM   1768 C  CG2 . VAL A 1 210 ? -1.728  -2.343  8.227   1.00 7.96   ? 211 VAL A CG2 1 
ATOM   1769 N  N   . LEU A 1 211 ? -6.318  -3.214  7.276   1.00 7.00   ? 212 LEU A N   1 
ATOM   1770 C  CA  . LEU A 1 211 ? -7.626  -3.872  7.462   1.00 7.48   ? 212 LEU A CA  1 
ATOM   1771 C  C   . LEU A 1 211 ? -7.415  -5.349  7.802   1.00 7.08   ? 212 LEU A C   1 
ATOM   1772 O  O   . LEU A 1 211 ? -6.555  -6.054  7.264   1.00 7.74   ? 212 LEU A O   1 
ATOM   1773 C  CB  . LEU A 1 211 ? -8.451  -3.754  6.164   1.00 8.02   ? 212 LEU A CB  1 
ATOM   1774 C  CG  . LEU A 1 211 ? -8.813  -2.318  5.741   1.00 8.59   ? 212 LEU A CG  1 
ATOM   1775 C  CD1 . LEU A 1 211 ? -9.807  -2.386  4.582   1.00 11.09  ? 212 LEU A CD1 1 
ATOM   1776 C  CD2 . LEU A 1 211 ? -9.327  -1.476  6.885   1.00 9.97   ? 212 LEU A CD2 1 
ATOM   1777 N  N   A LYS A 1 212 ? -8.308  -5.829  8.680   0.50 7.84   ? 213 LYS A N   1 
ATOM   1778 N  N   B LYS A 1 212 ? -8.281  -5.831  8.703   0.50 7.94   ? 213 LYS A N   1 
ATOM   1779 C  CA  A LYS A 1 212 ? -8.233  -7.226  9.051   0.50 8.43   ? 213 LYS A CA  1 
ATOM   1780 C  CA  B LYS A 1 212 ? -8.241  -7.240  9.074   0.50 8.52   ? 213 LYS A CA  1 
ATOM   1781 C  C   A LYS A 1 212 ? -8.711  -8.138  7.959   0.50 7.97   ? 213 LYS A C   1 
ATOM   1782 C  C   B LYS A 1 212 ? -8.725  -8.148  7.962   0.50 8.20   ? 213 LYS A C   1 
ATOM   1783 O  O   A LYS A 1 212 ? -8.190  -9.271  7.817   0.50 9.64   ? 213 LYS A O   1 
ATOM   1784 O  O   B LYS A 1 212 ? -8.211  -9.266  7.785   0.50 9.75   ? 213 LYS A O   1 
ATOM   1785 C  CB  A LYS A 1 212 ? -8.993  -7.455  10.348  0.50 11.16  ? 213 LYS A CB  1 
ATOM   1786 C  CB  B LYS A 1 212 ? -9.030  -7.438  10.368  0.50 11.58  ? 213 LYS A CB  1 
ATOM   1787 C  CG  A LYS A 1 212 ? -9.089  -8.922  10.754  0.50 13.44  ? 213 LYS A CG  1 
ATOM   1788 C  CG  B LYS A 1 212 ? -9.174  -8.896  10.771  0.50 15.10  ? 213 LYS A CG  1 
ATOM   1789 C  CD  A LYS A 1 212 ? -9.689  -9.086  12.150  0.50 20.27  ? 213 LYS A CD  1 
ATOM   1790 C  CD  B LYS A 1 212 ? -10.149 -9.126  11.913  0.50 21.83  ? 213 LYS A CD  1 
ATOM   1791 C  CE  A LYS A 1 212 ? -10.087 -10.523 12.489  0.50 21.53  ? 213 LYS A CE  1 
ATOM   1792 C  CE  B LYS A 1 212 ? -11.390 -8.243  11.853  0.50 27.22  ? 213 LYS A CE  1 
ATOM   1793 N  NZ  A LYS A 1 212 ? -10.885 -10.595 13.741  0.50 28.68  ? 213 LYS A NZ  1 
ATOM   1794 N  NZ  B LYS A 1 212 ? -12.563 -8.912  12.517  0.50 43.12  ? 213 LYS A NZ  1 
ATOM   1795 N  N   . GLU A 1 213 ? -9.773  -7.776  7.216   1.00 8.09   ? 214 GLU A N   1 
ATOM   1796 C  CA  . GLU A 1 213 ? -10.369 -8.638  6.213   1.00 8.60   ? 214 GLU A CA  1 
ATOM   1797 C  C   . GLU A 1 213 ? -9.605  -8.521  4.929   1.00 7.72   ? 214 GLU A C   1 
ATOM   1798 O  O   . GLU A 1 213 ? -9.531  -7.431  4.361   1.00 7.96   ? 214 GLU A O   1 
ATOM   1799 C  CB  . GLU A 1 213 ? -11.828 -8.308  5.988   1.00 9.77   ? 214 GLU A CB  1 
ATOM   1800 C  CG  . GLU A 1 213 ? -12.499 -9.239  5.043   1.00 11.46  ? 214 GLU A CG  1 
ATOM   1801 C  CD  . GLU A 1 213 ? -13.943 -8.984  4.876   1.00 15.55  ? 214 GLU A CD  1 
ATOM   1802 O  OE1 . GLU A 1 213 ? -14.588 -8.138  5.456   1.00 16.30  ? 214 GLU A OE1 1 
ATOM   1803 O  OE2 . GLU A 1 213 ? -14.522 -9.761  4.089   1.00 30.64  ? 214 GLU A OE2 1 
ATOM   1804 N  N   A PRO A 1 214 ? -9.075  -9.641  4.405   0.50 7.73   ? 215 PRO A N   1 
ATOM   1805 N  N   B PRO A 1 214 ? -8.985  -9.636  4.421   0.50 8.48   ? 215 PRO A N   1 
ATOM   1806 C  CA  A PRO A 1 214 ? -8.441  -9.574  3.096   0.50 7.75   ? 215 PRO A CA  1 
ATOM   1807 C  CA  B PRO A 1 214 ? -8.349  -9.574  3.094   0.50 8.12   ? 215 PRO A CA  1 
ATOM   1808 C  C   A PRO A 1 214 ? -9.453  -9.531  1.974   0.50 8.40   ? 215 PRO A C   1 
ATOM   1809 C  C   B PRO A 1 214 ? -9.380  -9.539  1.976   0.50 8.62   ? 215 PRO A C   1 
ATOM   1810 O  O   A PRO A 1 214 ? -10.641 -9.916  2.172   0.50 10.18  ? 215 PRO A O   1 
ATOM   1811 O  O   B PRO A 1 214 ? -10.541 -9.920  2.178   0.50 10.51  ? 215 PRO A O   1 
ATOM   1812 C  CB  A PRO A 1 214 ? -7.676  -10.893 3.005   0.50 8.43   ? 215 PRO A CB  1 
ATOM   1813 C  CB  B PRO A 1 214 ? -7.571  -10.884 3.011   0.50 9.49   ? 215 PRO A CB  1 
ATOM   1814 C  CG  A PRO A 1 214 ? -8.468  -11.861 3.878   0.50 8.10   ? 215 PRO A CG  1 
ATOM   1815 C  CG  B PRO A 1 214 ? -7.384  -11.278 4.465   0.50 14.30  ? 215 PRO A CG  1 
ATOM   1816 C  CD  A PRO A 1 214 ? -9.106  -11.005 4.953   0.50 6.85   ? 215 PRO A CD  1 
ATOM   1817 C  CD  B PRO A 1 214 ? -8.640  -10.877 5.159   0.50 12.51  ? 215 PRO A CD  1 
ATOM   1818 N  N   . ILE A 1 215 ? -9.018  -9.096  0.805   1.00 8.30   ? 216 ILE A N   1 
ATOM   1819 C  CA  . ILE A 1 215 ? -9.789  -9.299  -0.400  1.00 8.74   ? 216 ILE A CA  1 
ATOM   1820 C  C   . ILE A 1 215 ? -9.267  -10.549 -1.105  1.00 8.66   ? 216 ILE A C   1 
ATOM   1821 O  O   . ILE A 1 215 ? -8.082  -10.923 -0.933  1.00 9.79   ? 216 ILE A O   1 
ATOM   1822 C  CB  . ILE A 1 215 ? -9.778  -8.093  -1.346  1.00 9.62   ? 216 ILE A CB  1 
ATOM   1823 C  CG1 . ILE A 1 215 ? -8.379  -7.714  -1.838  1.00 10.49  ? 216 ILE A CG1 1 
ATOM   1824 C  CG2 . ILE A 1 215 ? -10.486 -6.879  -0.676  1.00 11.71  ? 216 ILE A CG2 1 
ATOM   1825 C  CD1 . ILE A 1 215 ? -8.345  -6.711  -3.026  1.00 12.53  ? 216 ILE A CD1 1 
ATOM   1826 N  N   A SER A 1 216 ? -10.123 -11.210 -1.869  0.50 9.72   ? 217 SER A N   1 
ATOM   1827 N  N   B SER A 1 216 ? -10.125 -11.227 -1.844  0.50 9.74   ? 217 SER A N   1 
ATOM   1828 C  CA  A SER A 1 216 ? -9.733  -12.352 -2.699  0.50 9.25   ? 217 SER A CA  1 
ATOM   1829 C  CA  B SER A 1 216 ? -9.741  -12.363 -2.663  0.50 9.52   ? 217 SER A CA  1 
ATOM   1830 C  C   A SER A 1 216 ? -9.505  -11.898 -4.100  0.50 9.07   ? 217 SER A C   1 
ATOM   1831 C  C   B SER A 1 216 ? -9.515  -11.914 -4.094  0.50 9.08   ? 217 SER A C   1 
ATOM   1832 O  O   A SER A 1 216 ? -10.349 -11.148 -4.641  0.50 10.94  ? 217 SER A O   1 
ATOM   1833 O  O   B SER A 1 216 ? -10.356 -11.153 -4.640  0.50 10.93  ? 217 SER A O   1 
ATOM   1834 C  CB  A SER A 1 216 ? -10.841 -13.422 -2.707  0.50 11.88  ? 217 SER A CB  1 
ATOM   1835 C  CB  B SER A 1 216 ? -10.846 -13.422 -2.593  0.50 14.18  ? 217 SER A CB  1 
ATOM   1836 O  OG  A SER A 1 216 ? -10.882 -14.081 -1.465  0.50 11.30  ? 217 SER A OG  1 
ATOM   1837 O  OG  B SER A 1 216 ? -10.411 -14.514 -3.331  0.50 19.22  ? 217 SER A OG  1 
ATOM   1838 N  N   . VAL A 1 217 ? -8.409  -12.363 -4.703  1.00 9.39   ? 218 VAL A N   1 
ATOM   1839 C  CA  . VAL A 1 217 ? -8.142  -12.166 -6.099  1.00 10.05  ? 218 VAL A CA  1 
ATOM   1840 C  C   . VAL A 1 217 ? -7.895  -13.526 -6.733  1.00 9.29   ? 218 VAL A C   1 
ATOM   1841 O  O   . VAL A 1 217 ? -7.540  -14.484 -6.024  1.00 9.84   ? 218 VAL A O   1 
ATOM   1842 C  CB  . VAL A 1 217 ? -6.926  -11.227 -6.371  1.00 10.65  ? 218 VAL A CB  1 
ATOM   1843 C  CG1 . VAL A 1 217 ? -7.153  -9.906  -5.643  1.00 11.06  ? 218 VAL A CG1 1 
ATOM   1844 C  CG2 . VAL A 1 217 ? -5.663  -11.857 -5.840  1.00 11.94  ? 218 VAL A CG2 1 
ATOM   1845 N  N   . SER A 1 218 ? -8.010  -13.670 -8.037  1.00 9.92   ? 219 SER A N   1 
ATOM   1846 C  CA  . SER A 1 218 ? -7.832  -15.002 -8.601  1.00 10.62  ? 219 SER A CA  1 
ATOM   1847 C  C   . SER A 1 218 ? -6.367  -15.268 -8.885  1.00 10.29  ? 219 SER A C   1 
ATOM   1848 O  O   . SER A 1 218 ? -5.554  -14.345 -9.031  1.00 10.91  ? 219 SER A O   1 
ATOM   1849 C  CB  . SER A 1 218 ? -8.650  -15.186 -9.875  1.00 10.55  ? 219 SER A CB  1 
ATOM   1850 O  OG  . SER A 1 218 ? -8.168  -14.293 -10.859 1.00 12.32  ? 219 SER A OG  1 
ATOM   1851 N  N   A SER A 1 219 ? -6.050  -16.551 -9.041  0.50 10.56  ? 220 SER A N   1 
ATOM   1852 N  N   B SER A 1 219 ? -6.029  -16.535 -9.012  0.50 10.98  ? 220 SER A N   1 
ATOM   1853 C  CA  A SER A 1 219 ? -4.707  -16.933 -9.454  0.50 11.82  ? 220 SER A CA  1 
ATOM   1854 C  CA  B SER A 1 219 ? -4.695  -16.882 -9.431  0.50 12.60  ? 220 SER A CA  1 
ATOM   1855 C  C   A SER A 1 219 ? -4.335  -16.230 -10.730 0.50 13.19  ? 220 SER A C   1 
ATOM   1856 C  C   B SER A 1 219 ? -4.319  -16.227 -10.745 0.50 13.45  ? 220 SER A C   1 
ATOM   1857 O  O   A SER A 1 219 ? -3.256  -15.737 -10.858 0.50 14.34  ? 220 SER A O   1 
ATOM   1858 O  O   B SER A 1 219 ? -3.209  -15.787 -10.924 0.50 14.96  ? 220 SER A O   1 
ATOM   1859 C  CB  A SER A 1 219 ? -4.571  -18.473 -9.541  0.50 14.60  ? 220 SER A CB  1 
ATOM   1860 C  CB  B SER A 1 219 ? -4.611  -18.401 -9.489  0.50 13.83  ? 220 SER A CB  1 
ATOM   1861 O  OG  A SER A 1 219 ? -5.531  -19.015 -10.432 0.50 13.29  ? 220 SER A OG  1 
ATOM   1862 O  OG  B SER A 1 219 ? -3.294  -18.799 -9.690  0.50 14.18  ? 220 SER A OG  1 
ATOM   1863 N  N   . GLU A 1 220 ? -5.279  -16.133 -11.670 1.00 11.96  ? 221 GLU A N   1 
ATOM   1864 C  CA  . GLU A 1 220 ? -5.006  -15.513 -12.954 1.00 13.96  ? 221 GLU A CA  1 
ATOM   1865 C  C   . GLU A 1 220 ? -4.681  -14.012 -12.789 1.00 13.60  ? 221 GLU A C   1 
ATOM   1866 O  O   . GLU A 1 220 ? -3.833  -13.463 -13.520 1.00 14.14  ? 221 GLU A O   1 
ATOM   1867 C  CB  . GLU A 1 220 ? -6.152  -15.633 -13.929 1.00 18.05  ? 221 GLU A CB  1 
ATOM   1868 C  CG  . GLU A 1 220 ? -6.331  -17.103 -14.357 1.00 23.33  ? 221 GLU A CG  1 
ATOM   1869 C  CD  . GLU A 1 220 ? -7.335  -17.878 -13.480 1.00 26.05  ? 221 GLU A CD  1 
ATOM   1870 O  OE1 . GLU A 1 220 ? -7.766  -17.438 -12.410 1.00 20.97  ? 221 GLU A OE1 1 
ATOM   1871 O  OE2 . GLU A 1 220 ? -7.667  -19.024 -13.865 1.00 66.19  ? 221 GLU A OE2 1 
ATOM   1872 N  N   . GLN A 1 221 ? -5.348  -13.318 -11.872 1.00 11.71  ? 222 GLN A N   1 
ATOM   1873 C  CA  . GLN A 1 221 ? -5.108  -11.879 -11.667 1.00 11.47  ? 222 GLN A CA  1 
ATOM   1874 C  C   . GLN A 1 221 ? -3.689  -11.704 -11.091 1.00 10.95  ? 222 GLN A C   1 
ATOM   1875 O  O   . GLN A 1 221 ? -2.926  -10.845 -11.588 1.00 12.53  ? 222 GLN A O   1 
ATOM   1876 C  CB  . GLN A 1 221 ? -6.127  -11.322 -10.716 1.00 11.58  ? 222 GLN A CB  1 
ATOM   1877 C  CG  . GLN A 1 221 ? -7.511  -11.204 -11.406 1.00 11.33  ? 222 GLN A CG  1 
ATOM   1878 C  CD  . GLN A 1 221 ? -8.626  -10.674 -10.540 1.00 11.06  ? 222 GLN A CD  1 
ATOM   1879 O  OE1 . GLN A 1 221 ? -8.783  -11.031 -9.351  1.00 11.13  ? 222 GLN A OE1 1 
ATOM   1880 N  NE2 . GLN A 1 221 ? -9.454  -9.809  -11.144 1.00 12.21  ? 222 GLN A NE2 1 
ATOM   1881 N  N   . VAL A 1 222 ? -3.297  -12.488 -10.096 1.00 11.83  ? 223 VAL A N   1 
ATOM   1882 C  CA  . VAL A 1 222 ? -1.957  -12.282 -9.541  1.00 12.86  ? 223 VAL A CA  1 
ATOM   1883 C  C   . VAL A 1 222 ? -0.854  -12.743 -10.495 1.00 12.53  ? 223 VAL A C   1 
ATOM   1884 O  O   . VAL A 1 222 ? 0.205   -12.149 -10.546 1.00 13.08  ? 223 VAL A O   1 
ATOM   1885 C  CB  . VAL A 1 222 ? -1.832  -12.874 -8.117  1.00 13.25  ? 223 VAL A CB  1 
ATOM   1886 C  CG1 . VAL A 1 222 ? -1.872  -14.362 -8.146  1.00 14.07  ? 223 VAL A CG1 1 
ATOM   1887 C  CG2 . VAL A 1 222 ? -0.578  -12.382 -7.404  1.00 14.95  ? 223 VAL A CG2 1 
ATOM   1888 N  N   . LEU A 1 223 ? -1.148  -13.741 -11.321 1.00 13.21  ? 224 LEU A N   1 
ATOM   1889 C  CA  . LEU A 1 223 ? -0.202  -14.179 -12.322 1.00 14.94  ? 224 LEU A CA  1 
ATOM   1890 C  C   . LEU A 1 223 ? 0.119   -13.025 -13.298 1.00 15.70  ? 224 LEU A C   1 
ATOM   1891 O  O   . LEU A 1 223 ? 1.255   -12.874 -13.735 1.00 16.45  ? 224 LEU A O   1 
ATOM   1892 C  CB  . LEU A 1 223 ? -0.671  -15.429 -13.040 1.00 18.49  ? 224 LEU A CB  1 
ATOM   1893 C  CG  . LEU A 1 223 ? -0.499  -16.684 -12.188 1.00 20.60  ? 224 LEU A CG  1 
ATOM   1894 C  CD1 . LEU A 1 223 ? -1.343  -17.821 -12.713 1.00 24.69  ? 224 LEU A CD1 1 
ATOM   1895 C  CD2 . LEU A 1 223 ? 0.982   -17.049 -12.091 1.00 24.08  ? 224 LEU A CD2 1 
ATOM   1896 N  N   . LYS A 1 224 ? -0.875  -12.154 -13.584 1.00 14.46  ? 225 LYS A N   1 
ATOM   1897 C  CA  . LYS A 1 224 ? -0.647  -11.044 -14.485 1.00 15.51  ? 225 LYS A CA  1 
ATOM   1898 C  C   . LYS A 1 224 ? 0.257   -9.988  -13.791 1.00 14.84  ? 225 LYS A C   1 
ATOM   1899 O  O   . LYS A 1 224 ? 1.093   -9.380  -14.434 1.00 13.92  ? 225 LYS A O   1 
ATOM   1900 C  CB  . LYS A 1 224 ? -1.954  -10.519 -15.079 1.00 18.30  ? 225 LYS A CB  1 
ATOM   1901 C  CG  . LYS A 1 224 ? -2.462  -11.587 -16.094 1.00 24.35  ? 225 LYS A CG  1 
ATOM   1902 C  CD  . LYS A 1 224 ? -3.779  -11.278 -16.770 1.00 26.63  ? 225 LYS A CD  1 
ATOM   1903 C  CE  . LYS A 1 224 ? -4.268  -12.376 -17.725 1.00 37.17  ? 225 LYS A CE  1 
ATOM   1904 N  NZ  . LYS A 1 224 ? -5.625  -12.123 -18.319 1.00 34.74  ? 225 LYS A NZ  1 
ATOM   1905 N  N   . PHE A 1 225 ? 0.168   -9.791  -12.466 1.00 12.97  ? 226 PHE A N   1 
ATOM   1906 C  CA  . PHE A 1 225 ? 1.068   -8.913  -11.763 1.00 12.53  ? 226 PHE A CA  1 
ATOM   1907 C  C   . PHE A 1 225 ? 2.535   -9.436  -11.996 1.00 12.27  ? 226 PHE A C   1 
ATOM   1908 O  O   . PHE A 1 225 ? 3.468   -8.673  -12.204 1.00 12.80  ? 226 PHE A O   1 
ATOM   1909 C  CB  . PHE A 1 225 ? 0.891   -8.907  -10.260 1.00 12.25  ? 226 PHE A CB  1 
ATOM   1910 C  CG  . PHE A 1 225 ? -0.305  -8.143  -9.719  1.00 12.60  ? 226 PHE A CG  1 
ATOM   1911 C  CD1 . PHE A 1 225 ? -1.330  -7.650  -10.512 1.00 16.49  ? 226 PHE A CD1 1 
ATOM   1912 C  CD2 . PHE A 1 225 ? -0.396  -7.963  -8.341  1.00 14.99  ? 226 PHE A CD2 1 
ATOM   1913 C  CE1 . PHE A 1 225 ? -2.410  -6.978  -9.929  1.00 18.15  ? 226 PHE A CE1 1 
ATOM   1914 C  CE2 . PHE A 1 225 ? -1.468  -7.297  -7.763  1.00 16.29  ? 226 PHE A CE2 1 
ATOM   1915 C  CZ  . PHE A 1 225 ? -2.475  -6.804  -8.552  1.00 15.89  ? 226 PHE A CZ  1 
ATOM   1916 N  N   . ARG A 1 226 ? 2.684   -10.766 -11.923 1.00 11.56  ? 227 ARG A N   1 
ATOM   1917 C  CA  . ARG A 1 226 ? 3.983   -11.352 -11.973 1.00 12.29  ? 227 ARG A CA  1 
ATOM   1918 C  C   . ARG A 1 226 ? 4.608   -11.383 -13.383 1.00 13.43  ? 227 ARG A C   1 
ATOM   1919 O  O   . ARG A 1 226 ? 5.769   -11.782 -13.515 1.00 15.35  ? 227 ARG A O   1 
ATOM   1920 C  CB  . ARG A 1 226 ? 3.938   -12.822 -11.448 1.00 12.91  ? 227 ARG A CB  1 
ATOM   1921 C  CG  . ARG A 1 226 ? 3.521   -12.928 -9.993  1.00 13.24  ? 227 ARG A CG  1 
ATOM   1922 C  CD  . ARG A 1 226 ? 3.562   -14.398 -9.540  1.00 14.83  ? 227 ARG A CD  1 
ATOM   1923 N  NE  . ARG A 1 226 ? 2.995   -14.528 -8.194  1.00 11.81  ? 227 ARG A NE  1 
ATOM   1924 C  CZ  . ARG A 1 226 ? 2.075   -15.414 -7.806  1.00 12.23  ? 227 ARG A CZ  1 
ATOM   1925 N  NH1 . ARG A 1 226 ? 1.605   -16.337 -8.651  1.00 17.07  ? 227 ARG A NH1 1 
ATOM   1926 N  NH2 . ARG A 1 226 ? 1.546   -15.350 -6.642  1.00 13.40  ? 227 ARG A NH2 1 
ATOM   1927 N  N   . LYS A 1 227 ? 3.877   -10.919 -14.412 1.00 12.56  ? 228 LYS A N   1 
ATOM   1928 C  CA  . LYS A 1 227 ? 4.414   -10.784 -15.766 1.00 14.56  ? 228 LYS A CA  1 
ATOM   1929 C  C   . LYS A 1 227 ? 5.022   -9.397  -15.989 1.00 15.86  ? 228 LYS A C   1 
ATOM   1930 O  O   . LYS A 1 227 ? 5.680   -9.180  -17.033 1.00 16.57  ? 228 LYS A O   1 
ATOM   1931 C  CB  . LYS A 1 227 ? 3.281   -10.993 -16.771 1.00 17.20  ? 228 LYS A CB  1 
ATOM   1932 C  CG  . LYS A 1 227 ? 2.848   -12.422 -16.912 1.00 19.72  ? 228 LYS A CG  1 
ATOM   1933 C  CD  . LYS A 1 227 ? 1.702   -12.631 -17.931 1.00 30.32  ? 228 LYS A CD  1 
ATOM   1934 C  CE  . LYS A 1 227 ? 1.968   -12.281 -19.403 1.00 35.93  ? 228 LYS A CE  1 
ATOM   1935 N  NZ  . LYS A 1 227 ? 0.827   -12.633 -20.331 1.00 61.56  ? 228 LYS A NZ  1 
ATOM   1936 N  N   . LEU A 1 228 ? 4.754   -8.452  -15.078 1.00 14.27  ? 229 LEU A N   1 
ATOM   1937 C  CA  . LEU A 1 228 ? 5.412   -7.184  -15.155 1.00 15.26  ? 229 LEU A CA  1 
ATOM   1938 C  C   . LEU A 1 228 ? 6.911   -7.358  -15.045 1.00 15.34  ? 229 LEU A C   1 
ATOM   1939 O  O   . LEU A 1 228 ? 7.468   -8.410  -14.607 1.00 14.20  ? 229 LEU A O   1 
ATOM   1940 C  CB  . LEU A 1 228 ? 4.921   -6.248  -14.071 1.00 14.97  ? 229 LEU A CB  1 
ATOM   1941 C  CG  . LEU A 1 228 ? 3.460   -5.803  -14.288 1.00 15.05  ? 229 LEU A CG  1 
ATOM   1942 C  CD1 . LEU A 1 228 ? 3.015   -5.148  -12.997 1.00 15.90  ? 229 LEU A CD1 1 
ATOM   1943 C  CD2 . LEU A 1 228 ? 3.469   -4.766  -15.413 1.00 18.05  ? 229 LEU A CD2 1 
ATOM   1944 N  N   . ASN A 1 229 ? 7.592   -6.308  -15.434 1.00 15.59  ? 230 ASN A N   1 
ATOM   1945 C  CA  . ASN A 1 229 ? 9.027   -6.351  -15.418 1.00 14.43  ? 230 ASN A CA  1 
ATOM   1946 C  C   . ASN A 1 229 ? 9.650   -5.194  -14.591 1.00 18.37  ? 230 ASN A C   1 
ATOM   1947 O  O   . ASN A 1 229 ? 9.193   -4.046  -14.626 1.00 17.54  ? 230 ASN A O   1 
ATOM   1948 C  CB  . ASN A 1 229 ? 9.696   -6.127  -16.854 1.00 16.37  ? 230 ASN A CB  1 
ATOM   1949 C  CG  . ASN A 1 229 ? 9.715   -7.344  -17.752 1.00 18.66  ? 230 ASN A CG  1 
ATOM   1950 O  OD1 . ASN A 1 229 ? 10.283  -7.216  -18.833 1.00 24.14  ? 230 ASN A OD1 1 
ATOM   1951 N  ND2 . ASN A 1 229 ? 9.093   -8.470  -17.393 1.00 18.85  ? 230 ASN A ND2 1 
ATOM   1952 N  N   . PHE A 1 230 ? 10.714  -5.502  -13.831 1.00 16.69  ? 231 PHE A N   1 
ATOM   1953 C  CA  . PHE A 1 230 ? 11.464  -4.441  -13.161 1.00 16.88  ? 231 PHE A CA  1 
ATOM   1954 C  C   . PHE A 1 230 ? 12.420  -3.657  -14.095 1.00 19.85  ? 231 PHE A C   1 
ATOM   1955 O  O   . PHE A 1 230 ? 12.683  -2.500  -13.815 1.00 20.30  ? 231 PHE A O   1 
ATOM   1956 C  CB  . PHE A 1 230 ? 12.436  -5.004  -12.145 1.00 18.45  ? 231 PHE A CB  1 
ATOM   1957 C  CG  . PHE A 1 230 ? 11.818  -5.563  -10.859 1.00 15.64  ? 231 PHE A CG  1 
ATOM   1958 C  CD1 . PHE A 1 230 ? 11.057  -4.790  -9.978  1.00 16.19  ? 231 PHE A CD1 1 
ATOM   1959 C  CD2 . PHE A 1 230 ? 12.198  -6.821  -10.439 1.00 14.73  ? 231 PHE A CD2 1 
ATOM   1960 C  CE1 . PHE A 1 230 ? 10.597  -5.314  -8.785  1.00 16.86  ? 231 PHE A CE1 1 
ATOM   1961 C  CE2 . PHE A 1 230 ? 11.758  -7.381  -9.259  1.00 14.73  ? 231 PHE A CE2 1 
ATOM   1962 C  CZ  . PHE A 1 230 ? 10.993  -6.600  -8.383  1.00 14.30  ? 231 PHE A CZ  1 
ATOM   1963 N  N   . ASN A 1 231 ? 12.920  -4.314  -15.118 1.00 19.66  ? 232 ASN A N   1 
ATOM   1964 C  CA  . ASN A 1 231 ? 13.706  -3.621  -16.194 1.00 19.81  ? 232 ASN A CA  1 
ATOM   1965 C  C   . ASN A 1 231 ? 12.830  -2.728  -17.152 1.00 15.92  ? 232 ASN A C   1 
ATOM   1966 O  O   . ASN A 1 231 ? 11.657  -2.843  -17.289 1.00 19.10  ? 232 ASN A O   1 
ATOM   1967 C  CB  . ASN A 1 231 ? 14.359  -4.784  -16.956 1.00 21.25  ? 232 ASN A CB  1 
ATOM   1968 C  CG  . ASN A 1 231 ? 13.362  -5.727  -17.536 1.00 22.42  ? 232 ASN A CG  1 
ATOM   1969 O  OD1 . ASN A 1 231 ? 12.864  -6.603  -16.821 1.00 23.94  ? 232 ASN A OD1 1 
ATOM   1970 N  ND2 . ASN A 1 231 ? 13.071  -5.614  -18.828 1.00 23.74  ? 232 ASN A ND2 1 
ATOM   1971 N  N   . GLY A 1 232 ? 13.602  -1.841  -17.899 1.00 18.93  ? 233 GLY A N   1 
ATOM   1972 C  CA  . GLY A 1 232 ? 13.003  -1.011  -18.997 1.00 18.98  ? 233 GLY A CA  1 
ATOM   1973 C  C   . GLY A 1 232 ? 13.047  -1.770  -20.284 1.00 16.15  ? 233 GLY A C   1 
ATOM   1974 O  O   . GLY A 1 232 ? 13.705  -2.844  -20.305 1.00 22.76  ? 233 GLY A O   1 
ATOM   1975 N  N   . GLU A 1 233 ? 12.190  -1.298  -21.220 1.00 16.71  ? 234 GLU A N   1 
ATOM   1976 C  CA  . GLU A 1 233 ? 12.182  -1.810  -22.586 1.00 17.93  ? 234 GLU A CA  1 
ATOM   1977 C  C   . GLU A 1 233 ? 13.566  -1.988  -23.189 1.00 21.04  ? 234 GLU A C   1 
ATOM   1978 O  O   . GLU A 1 233 ? 14.417  -1.125  -23.036 1.00 22.38  ? 234 GLU A O   1 
ATOM   1979 C  CB  . GLU A 1 233 ? 11.253  -0.992  -23.463 1.00 19.29  ? 234 GLU A CB  1 
ATOM   1980 C  CG  . GLU A 1 233 ? 11.021  -1.570  -24.858 1.00 21.88  ? 234 GLU A CG  1 
ATOM   1981 C  CD  . GLU A 1 233 ? 10.162  -0.619  -25.678 1.00 37.96  ? 234 GLU A CD  1 
ATOM   1982 O  OE1 . GLU A 1 233 ? 9.982   0.568   -25.210 1.00 34.29  ? 234 GLU A OE1 1 
ATOM   1983 O  OE2 . GLU A 1 233 ? 9.695   -1.024  -26.786 1.00 44.30  ? 234 GLU A OE2 1 
ATOM   1984 N  N   . GLY A 1 234 ? 13.813  -3.155  -23.787 1.00 27.61  ? 235 GLY A N   1 
ATOM   1985 C  CA  . GLY A 1 234 ? 15.084  -3.393  -24.476 1.00 26.31  ? 235 GLY A CA  1 
ATOM   1986 C  C   . GLY A 1 234 ? 16.228  -3.778  -23.553 1.00 26.36  ? 235 GLY A C   1 
ATOM   1987 O  O   . GLY A 1 234 ? 17.425  -3.901  -23.943 1.00 37.22  ? 235 GLY A O   1 
ATOM   1988 N  N   . GLU A 1 235 ? 15.835  -4.002  -22.296 1.00 23.80  ? 236 GLU A N   1 
ATOM   1989 C  CA  . GLU A 1 235 ? 16.775  -4.642  -21.362 1.00 19.67  ? 236 GLU A CA  1 
ATOM   1990 C  C   . GLU A 1 235 ? 16.359  -6.103  -21.033 1.00 32.42  ? 236 GLU A C   1 
ATOM   1991 O  O   . GLU A 1 235 ? 15.195  -6.541  -21.221 1.00 31.89  ? 236 GLU A O   1 
ATOM   1992 C  CB  . GLU A 1 235 ? 16.747  -3.897  -20.030 1.00 21.84  ? 236 GLU A CB  1 
ATOM   1993 C  CG  . GLU A 1 235 ? 17.440  -2.536  -20.078 1.00 27.90  ? 236 GLU A CG  1 
ATOM   1994 C  CD  . GLU A 1 235 ? 17.071  -1.616  -18.919 1.00 37.13  ? 236 GLU A CD  1 
ATOM   1995 O  OE1 . GLU A 1 235 ? 16.524  -2.083  -17.860 1.00 34.85  ? 236 GLU A OE1 1 
ATOM   1996 O  OE2 . GLU A 1 235 ? 17.352  -0.410  -19.087 1.00 40.68  ? 236 GLU A OE2 1 
ATOM   1997 N  N   . PRO A 1 236 ? 17.272  -6.848  -20.411 1.00 23.66  ? 237 PRO A N   1 
ATOM   1998 C  CA  . PRO A 1 236 ? 17.094  -8.307  -20.091 1.00 33.64  ? 237 PRO A CA  1 
ATOM   1999 C  C   . PRO A 1 236 ? 16.008  -8.474  -19.000 1.00 27.68  ? 237 PRO A C   1 
ATOM   2000 O  O   . PRO A 1 236 ? 15.968  -7.700  -18.031 1.00 26.99  ? 237 PRO A O   1 
ATOM   2001 C  CB  . PRO A 1 236 ? 18.406  -8.710  -19.443 1.00 35.49  ? 237 PRO A CB  1 
ATOM   2002 C  CG  . PRO A 1 236 ? 19.412  -7.660  -19.768 1.00 36.93  ? 237 PRO A CG  1 
ATOM   2003 C  CD  . PRO A 1 236 ? 18.643  -6.394  -20.048 1.00 29.90  ? 237 PRO A CD  1 
ATOM   2004 N  N   . GLU A 1 237 ? 15.180  -9.486  -19.141 1.00 25.21  ? 238 GLU A N   1 
ATOM   2005 C  CA  . GLU A 1 237 ? 13.977  -9.540  -18.415 1.00 22.43  ? 238 GLU A CA  1 
ATOM   2006 C  C   . GLU A 1 237 ? 14.223  -9.953  -16.975 1.00 21.77  ? 238 GLU A C   1 
ATOM   2007 O  O   . GLU A 1 237 ? 14.803  -10.970 -16.724 1.00 20.31  ? 238 GLU A O   1 
ATOM   2008 C  CB  . GLU A 1 237 ? 13.007  -10.524 -19.031 1.00 21.65  ? 238 GLU A CB  1 
ATOM   2009 C  CG  . GLU A 1 237 ? 11.659  -10.480 -18.294 1.00 22.60  ? 238 GLU A CG  1 
ATOM   2010 C  CD  . GLU A 1 237 ? 10.565  -11.165 -19.084 1.00 20.56  ? 238 GLU A CD  1 
ATOM   2011 O  OE1 . GLU A 1 237 ? 10.919  -12.192 -19.713 1.00 34.96  ? 238 GLU A OE1 1 
ATOM   2012 O  OE2 . GLU A 1 237 ? 9.399   -10.682 -19.151 1.00 22.45  ? 238 GLU A OE2 1 
ATOM   2013 N  N   . GLU A 1 238 ? 13.730  -9.145  -16.045 1.00 20.07  ? 239 GLU A N   1 
ATOM   2014 C  CA  . GLU A 1 238 ? 13.708  -9.458  -14.594 1.00 20.95  ? 239 GLU A CA  1 
ATOM   2015 C  C   . GLU A 1 238 ? 12.276  -9.335  -14.168 1.00 16.80  ? 239 GLU A C   1 
ATOM   2016 O  O   . GLU A 1 238 ? 11.792  -8.219  -14.089 1.00 20.02  ? 239 GLU A O   1 
ATOM   2017 C  CB  . GLU A 1 238 ? 14.534  -8.465  -13.793 1.00 27.45  ? 239 GLU A CB  1 
ATOM   2018 C  CG  . GLU A 1 238 ? 15.811  -8.000  -14.411 1.00 27.53  ? 239 GLU A CG  1 
ATOM   2019 C  CD  . GLU A 1 238 ? 16.582  -7.049  -13.512 1.00 45.81  ? 239 GLU A CD  1 
ATOM   2020 O  OE1 . GLU A 1 238 ? 16.067  -5.934  -13.284 1.00 51.71  ? 239 GLU A OE1 1 
ATOM   2021 O  OE2 . GLU A 1 238 ? 17.692  -7.420  -13.027 1.00 77.37  ? 239 GLU A OE2 1 
ATOM   2022 N  N   . LEU A 1 239 ? 11.602  -10.448 -13.884 1.00 15.07  ? 240 LEU A N   1 
ATOM   2023 C  CA  . LEU A 1 239 ? 10.197  -10.353 -13.556 1.00 12.97  ? 240 LEU A CA  1 
ATOM   2024 C  C   . LEU A 1 239 ? 10.006  -9.543  -12.264 1.00 13.85  ? 240 LEU A C   1 
ATOM   2025 O  O   . LEU A 1 239 ? 10.755  -9.707  -11.279 1.00 14.37  ? 240 LEU A O   1 
ATOM   2026 C  CB  . LEU A 1 239 ? 9.597   -11.759 -13.355 1.00 12.39  ? 240 LEU A CB  1 
ATOM   2027 C  CG  . LEU A 1 239 ? 9.590   -12.636 -14.612 1.00 13.37  ? 240 LEU A CG  1 
ATOM   2028 C  CD1 . LEU A 1 239 ? 8.988   -13.954 -14.234 1.00 19.64  ? 240 LEU A CD1 1 
ATOM   2029 C  CD2 . LEU A 1 239 ? 8.783   -11.920 -15.666 1.00 15.74  ? 240 LEU A CD2 1 
ATOM   2030 N  N   . MET A 1 240 ? 8.961   -8.729  -12.255 1.00 13.27  ? 241 MET A N   1 
ATOM   2031 C  CA  . MET A 1 240 ? 8.572   -7.893  -11.088 1.00 13.81  ? 241 MET A CA  1 
ATOM   2032 C  C   . MET A 1 240 ? 7.800   -8.829  -10.166 1.00 11.70  ? 241 MET A C   1 
ATOM   2033 O  O   . MET A 1 240 ? 6.624   -8.980  -10.239 1.00 12.03  ? 241 MET A O   1 
ATOM   2034 C  CB  . MET A 1 240 ? 7.724   -6.724  -11.581 1.00 14.16  ? 241 MET A CB  1 
ATOM   2035 C  CG  . MET A 1 240 ? 7.419   -5.765  -10.412 1.00 13.60  ? 241 MET A CG  1 
ATOM   2036 S  SD  . MET A 1 240 ? 6.447   -4.361  -10.920 1.00 15.53  ? 241 MET A SD  1 
ATOM   2037 C  CE  . MET A 1 240 ? 7.710   -3.275  -11.592 1.00 16.40  ? 241 MET A CE  1 
ATOM   2038 N  N   . VAL A 1 241 ? 8.589   -9.406  -9.218  1.00 11.33  ? 242 VAL A N   1 
ATOM   2039 C  CA  . VAL A 1 241 ? 8.072   -10.301 -8.173  1.00 10.54  ? 242 VAL A CA  1 
ATOM   2040 C  C   . VAL A 1 241 ? 8.850   -10.109 -6.906  1.00 10.62  ? 242 VAL A C   1 
ATOM   2041 O  O   . VAL A 1 241 ? 9.997   -9.672  -6.972  1.00 11.47  ? 242 VAL A O   1 
ATOM   2042 C  CB  . VAL A 1 241 ? 8.114   -11.801 -8.605  1.00 11.64  ? 242 VAL A CB  1 
ATOM   2043 C  CG1 . VAL A 1 241 ? 7.154   -12.132 -9.772  1.00 12.72  ? 242 VAL A CG1 1 
ATOM   2044 C  CG2 . VAL A 1 241 ? 9.535   -12.282 -8.819  1.00 14.18  ? 242 VAL A CG2 1 
ATOM   2045 N  N   . ASP A 1 242 ? 8.238   -10.389 -5.765  1.00 9.29   ? 243 ASP A N   1 
ATOM   2046 C  CA  . ASP A 1 242 ? 8.880   -10.254 -4.493  1.00 9.42   ? 243 ASP A CA  1 
ATOM   2047 C  C   . ASP A 1 242 ? 9.359   -8.828  -4.242  1.00 9.48   ? 243 ASP A C   1 
ATOM   2048 O  O   . ASP A 1 242 ? 10.492  -8.576  -3.769  1.00 11.36  ? 243 ASP A O   1 
ATOM   2049 C  CB  . ASP A 1 242 ? 9.990   -11.295 -4.272  1.00 10.20  ? 243 ASP A CB  1 
ATOM   2050 C  CG  . ASP A 1 242 ? 9.412   -12.722 -4.156  1.00 10.25  ? 243 ASP A CG  1 
ATOM   2051 O  OD1 . ASP A 1 242 ? 8.353   -12.866 -3.522  1.00 9.48   ? 243 ASP A OD1 1 
ATOM   2052 O  OD2 . ASP A 1 242 ? 10.040  -13.622 -4.757  1.00 12.61  ? 243 ASP A OD2 1 
ATOM   2053 N  N   . ASN A 1 243 ? 8.487   -7.880  -4.507  1.00 9.04   ? 244 ASN A N   1 
ATOM   2054 C  CA  . ASN A 1 243 ? 8.721   -6.441  -4.314  1.00 8.75   ? 244 ASN A CA  1 
ATOM   2055 C  C   . ASN A 1 243 ? 8.195   -6.012  -2.936  1.00 7.93   ? 244 ASN A C   1 
ATOM   2056 O  O   . ASN A 1 243 ? 7.513   -4.972  -2.847  1.00 9.25   ? 244 ASN A O   1 
ATOM   2057 C  CB  . ASN A 1 243 ? 8.210   -5.600  -5.460  1.00 10.31  ? 244 ASN A CB  1 
ATOM   2058 C  CG  . ASN A 1 243 ? 6.755   -5.802  -5.711  1.00 9.62   ? 244 ASN A CG  1 
ATOM   2059 O  OD1 . ASN A 1 243 ? 6.088   -6.640  -5.116  1.00 10.00  ? 244 ASN A OD1 1 
ATOM   2060 N  ND2 . ASN A 1 243 ? 6.217   -5.056  -6.701  1.00 15.93  ? 244 ASN A ND2 1 
ATOM   2061 N  N   . TRP A 1 244 ? 8.468   -6.786  -1.889  1.00 7.66   ? 245 TRP A N   1 
ATOM   2062 C  CA  . TRP A 1 244 ? 8.065   -6.533  -0.525  1.00 7.56   ? 245 TRP A CA  1 
ATOM   2063 C  C   . TRP A 1 244 ? 9.259   -6.451  0.383   1.00 7.64   ? 245 TRP A C   1 
ATOM   2064 O  O   . TRP A 1 244 ? 10.260  -7.161  0.248   1.00 9.32   ? 245 TRP A O   1 
ATOM   2065 C  CB  . TRP A 1 244 ? 7.084   -7.616  -0.021  1.00 7.81   ? 245 TRP A CB  1 
ATOM   2066 C  CG  . TRP A 1 244 ? 7.551   -9.032  -0.200  1.00 7.92   ? 245 TRP A CG  1 
ATOM   2067 C  CD1 . TRP A 1 244 ? 7.489   -9.785  -1.325  1.00 8.18   ? 245 TRP A CD1 1 
ATOM   2068 C  CD2 . TRP A 1 244 ? 8.165   -9.877  0.775   1.00 7.75   ? 245 TRP A CD2 1 
ATOM   2069 N  NE1 . TRP A 1 244 ? 7.990   -11.064 -1.138  1.00 8.38   ? 245 TRP A NE1 1 
ATOM   2070 C  CE2 . TRP A 1 244 ? 8.401   -11.153 0.134   1.00 8.71   ? 245 TRP A CE2 1 
ATOM   2071 C  CE3 . TRP A 1 244 ? 8.446   -9.748  2.120   1.00 8.41   ? 245 TRP A CE3 1 
ATOM   2072 C  CZ2 . TRP A 1 244 ? 8.971   -12.226 0.835   1.00 9.33   ? 245 TRP A CZ2 1 
ATOM   2073 C  CZ3 . TRP A 1 244 ? 8.994   -10.831 2.805   1.00 9.94   ? 245 TRP A CZ3 1 
ATOM   2074 C  CH2 . TRP A 1 244 ? 9.266   -12.036 2.157   1.00 10.28  ? 245 TRP A CH2 1 
ATOM   2075 N  N   . ARG A 1 245 ? 9.131   -5.564  1.378   1.00 7.79   ? 246 ARG A N   1 
ATOM   2076 C  CA  . ARG A 1 245 ? 10.071  -5.456  2.491   1.00 8.04   ? 246 ARG A CA  1 
ATOM   2077 C  C   . ARG A 1 245 ? 9.650   -6.350  3.615   1.00 7.32   ? 246 ARG A C   1 
ATOM   2078 O  O   . ARG A 1 245 ? 8.431   -6.352  3.942   1.00 8.40   ? 246 ARG A O   1 
ATOM   2079 C  CB  . ARG A 1 245 ? 10.165  -3.970  2.984   1.00 7.86   ? 246 ARG A CB  1 
ATOM   2080 C  CG  . ARG A 1 245 ? 11.277  -3.759  3.982   1.00 7.79   ? 246 ARG A CG  1 
ATOM   2081 C  CD  . ARG A 1 245 ? 11.185  -2.376  4.640   1.00 8.95   ? 246 ARG A CD  1 
ATOM   2082 N  NE  . ARG A 1 245 ? 12.424  -2.068  5.327   1.00 8.75   ? 246 ARG A NE  1 
ATOM   2083 C  CZ  . ARG A 1 245 ? 12.609  -1.020  6.122   1.00 8.19   ? 246 ARG A CZ  1 
ATOM   2084 N  NH1 . ARG A 1 245 ? 11.612  -0.242  6.514   1.00 9.58   ? 246 ARG A NH1 1 
ATOM   2085 N  NH2 . ARG A 1 245 ? 13.852  -0.786  6.574   1.00 11.07  ? 246 ARG A NH2 1 
ATOM   2086 N  N   . PRO A 1 246 ? 10.524  -7.141  4.212   1.00 8.31   ? 247 PRO A N   1 
ATOM   2087 C  CA  . PRO A 1 246 ? 10.113  -7.965  5.359   1.00 9.42   ? 247 PRO A CA  1 
ATOM   2088 C  C   . PRO A 1 246 ? 9.741   -7.160  6.598   1.00 8.55   ? 247 PRO A C   1 
ATOM   2089 O  O   . PRO A 1 246 ? 10.099  -5.960  6.741   1.00 8.80   ? 247 PRO A O   1 
ATOM   2090 C  CB  . PRO A 1 246 ? 11.331  -8.833  5.656   1.00 13.22  ? 247 PRO A CB  1 
ATOM   2091 C  CG  . PRO A 1 246 ? 12.214  -8.680  4.491   1.00 18.79  ? 247 PRO A CG  1 
ATOM   2092 C  CD  . PRO A 1 246 ? 11.941  -7.344  3.907   1.00 11.08  ? 247 PRO A CD  1 
ATOM   2093 N  N   . ALA A 1 247 ? 9.096   -7.822  7.556   1.00 8.87   ? 248 ALA A N   1 
ATOM   2094 C  CA  . ALA A 1 247 ? 8.756   -7.163  8.837   1.00 8.89   ? 248 ALA A CA  1 
ATOM   2095 C  C   . ALA A 1 247 ? 9.983   -6.661  9.582   1.00 9.14   ? 248 ALA A C   1 
ATOM   2096 O  O   . ALA A 1 247 ? 11.033  -7.325  9.595   1.00 10.38  ? 248 ALA A O   1 
ATOM   2097 C  CB  . ALA A 1 247 ? 8.011   -8.171  9.710   1.00 11.59  ? 248 ALA A CB  1 
ATOM   2098 N  N   . GLN A 1 248 ? 9.870   -5.451  10.147  1.00 8.41   ? 249 GLN A N   1 
ATOM   2099 C  CA  . GLN A 1 248 ? 10.916  -4.735  10.868  1.00 9.15   ? 249 GLN A CA  1 
ATOM   2100 C  C   . GLN A 1 248 ? 10.628  -4.761  12.337  1.00 8.97   ? 249 GLN A C   1 
ATOM   2101 O  O   . GLN A 1 248 ? 9.499   -4.968  12.780  1.00 10.11  ? 249 GLN A O   1 
ATOM   2102 C  CB  . GLN A 1 248 ? 10.953  -3.302  10.330  1.00 10.05  ? 249 GLN A CB  1 
ATOM   2103 C  CG  . GLN A 1 248 ? 11.274  -3.241  8.836   1.00 10.20  ? 249 GLN A CG  1 
ATOM   2104 C  CD  . GLN A 1 248 ? 12.609  -3.890  8.507   1.00 10.71  ? 249 GLN A CD  1 
ATOM   2105 O  OE1 . GLN A 1 248 ? 13.632  -3.546  9.043   1.00 13.91  ? 249 GLN A OE1 1 
ATOM   2106 N  NE2 . GLN A 1 248 ? 12.603  -4.861  7.552   1.00 12.80  ? 249 GLN A NE2 1 
ATOM   2107 N  N   . PRO A 1 249 ? 11.630  -4.443  13.167  1.00 11.49  ? 250 PRO A N   1 
ATOM   2108 C  CA  . PRO A 1 249 ? 11.423  -4.467  14.613  1.00 13.29  ? 250 PRO A CA  1 
ATOM   2109 C  C   . PRO A 1 249 ? 10.349  -3.488  15.084  1.00 10.94  ? 250 PRO A C   1 
ATOM   2110 O  O   . PRO A 1 249 ? 10.385  -2.316  14.727  1.00 10.89  ? 250 PRO A O   1 
ATOM   2111 C  CB  . PRO A 1 249 ? 12.849  -4.060  15.161  1.00 15.92  ? 250 PRO A CB  1 
ATOM   2112 C  CG  . PRO A 1 249 ? 13.781  -4.565  14.113  1.00 18.03  ? 250 PRO A CG  1 
ATOM   2113 C  CD  . PRO A 1 249 ? 13.043  -4.211  12.799  1.00 14.87  ? 250 PRO A CD  1 
ATOM   2114 N  N   . LEU A 1 250 ? 9.477   -3.975  15.965  1.00 11.65  ? 251 LEU A N   1 
ATOM   2115 C  CA  . LEU A 1 250 ? 8.413   -3.119  16.470  1.00 10.58  ? 251 LEU A CA  1 
ATOM   2116 C  C   . LEU A 1 250 ? 8.929   -2.032  17.396  1.00 11.41  ? 251 LEU A C   1 
ATOM   2117 O  O   . LEU A 1 250 ? 8.358   -0.944  17.483  1.00 11.42  ? 251 LEU A O   1 
ATOM   2118 C  CB  . LEU A 1 250 ? 7.394   -3.957  17.218  1.00 13.09  ? 251 LEU A CB  1 
ATOM   2119 C  CG  . LEU A 1 250 ? 6.093   -3.264  17.649  1.00 12.81  ? 251 LEU A CG  1 
ATOM   2120 C  CD1 . LEU A 1 250 ? 5.304   -2.718  16.438  1.00 13.21  ? 251 LEU A CD1 1 
ATOM   2121 C  CD2 . LEU A 1 250 ? 5.132   -4.204  18.398  1.00 17.55  ? 251 LEU A CD2 1 
ATOM   2122 N  N   . LYS A 1 251 ? 10.002  -2.301  18.151  1.00 12.41  ? 252 LYS A N   1 
ATOM   2123 C  CA  . LYS A 1 251 ? 10.687  -1.293  19.023  1.00 13.64  ? 252 LYS A CA  1 
ATOM   2124 C  C   . LYS A 1 251 ? 9.611   -0.721  19.961  1.00 14.45  ? 252 LYS A C   1 
ATOM   2125 O  O   . LYS A 1 251 ? 8.824   -1.532  20.507  1.00 16.80  ? 252 LYS A O   1 
ATOM   2126 C  CB  . LYS A 1 251 ? 11.476  -0.250  18.230  1.00 15.68  ? 252 LYS A CB  1 
ATOM   2127 C  CG  . LYS A 1 251 ? 12.486  -0.961  17.400  1.00 19.29  ? 252 LYS A CG  1 
ATOM   2128 C  CD  . LYS A 1 251 ? 13.444  0.006   16.808  1.00 21.94  ? 252 LYS A CD  1 
ATOM   2129 C  CE  . LYS A 1 251 ? 14.597  -0.744  16.240  1.00 28.07  ? 252 LYS A CE  1 
ATOM   2130 N  NZ  . LYS A 1 251 ? 15.577  0.150   15.565  1.00 28.43  ? 252 LYS A NZ  1 
ATOM   2131 N  N   . ASN A 1 252 ? 9.585   0.550   20.207  1.00 14.36  ? 253 ASN A N   1 
ATOM   2132 C  CA  . ASN A 1 252 ? 8.768   1.038   21.214  1.00 22.38  ? 253 ASN A CA  1 
ATOM   2133 C  C   . ASN A 1 252 ? 7.436   1.438   20.620  1.00 23.32  ? 253 ASN A C   1 
ATOM   2134 O  O   . ASN A 1 252 ? 7.235   2.727   20.592  1.00 26.06  ? 253 ASN A O   1 
ATOM   2135 C  CB  . ASN A 1 252 ? 9.533   2.262   21.850  1.00 28.78  ? 253 ASN A CB  1 
ATOM   2136 C  CG  . ASN A 1 252 ? 8.959   2.715   23.180  1.00 30.81  ? 253 ASN A CG  1 
ATOM   2137 O  OD1 . ASN A 1 252 ? 8.768   1.916   24.100  1.00 60.24  ? 253 ASN A OD1 1 
ATOM   2138 N  ND2 . ASN A 1 252 ? 8.690   4.013   23.291  1.00 42.58  ? 253 ASN A ND2 1 
ATOM   2139 N  N   . ARG A 1 253 ? 6.616   0.441   20.053  1.00 15.57  ? 254 ARG A N   1 
ATOM   2140 C  CA  . ARG A 1 253 ? 5.345   0.775   19.537  1.00 11.06  ? 254 ARG A CA  1 
ATOM   2141 C  C   . ARG A 1 253 ? 4.252   -0.138  19.986  1.00 12.28  ? 254 ARG A C   1 
ATOM   2142 O  O   . ARG A 1 253 ? 4.487   -1.330  20.196  1.00 18.52  ? 254 ARG A O   1 
ATOM   2143 C  CB  . ARG A 1 253 ? 5.414   0.825   18.026  1.00 10.98  ? 254 ARG A CB  1 
ATOM   2144 C  CG  . ARG A 1 253 ? 6.272   1.962   17.509  1.00 11.19  ? 254 ARG A CG  1 
ATOM   2145 C  CD  . ARG A 1 253 ? 6.422   1.970   15.987  1.00 9.84   ? 254 ARG A CD  1 
ATOM   2146 N  NE  . ARG A 1 253 ? 7.250   0.819   15.536  1.00 9.02   ? 254 ARG A NE  1 
ATOM   2147 C  CZ  . ARG A 1 253 ? 7.490   0.547   14.268  1.00 8.34   ? 254 ARG A CZ  1 
ATOM   2148 N  NH1 . ARG A 1 253 ? 6.899   1.230   13.290  1.00 7.91   ? 254 ARG A NH1 1 
ATOM   2149 N  NH2 . ARG A 1 253 ? 8.313   -0.432  13.918  1.00 8.44   ? 254 ARG A NH2 1 
ATOM   2150 N  N   . GLN A 1 254 ? 3.034   0.377   20.059  1.00 12.16  ? 255 GLN A N   1 
ATOM   2151 C  CA  . GLN A 1 254 ? 1.833   -0.400  20.331  1.00 13.24  ? 255 GLN A CA  1 
ATOM   2152 C  C   . GLN A 1 254 ? 0.955   -0.392  19.081  1.00 11.90  ? 255 GLN A C   1 
ATOM   2153 O  O   . GLN A 1 254 ? 0.708   0.653   18.445  1.00 15.05  ? 255 GLN A O   1 
ATOM   2154 C  CB  . GLN A 1 254 ? 1.011   0.135   21.501  1.00 17.73  ? 255 GLN A CB  1 
ATOM   2155 C  CG  . GLN A 1 254 ? 1.673   -0.201  22.880  1.00 24.18  ? 255 GLN A CG  1 
ATOM   2156 C  CD  . GLN A 1 254 ? 0.901   0.427   24.038  1.00 30.34  ? 255 GLN A CD  1 
ATOM   2157 O  OE1 . GLN A 1 254 ? -0.258  0.870   23.841  1.00 41.23  ? 255 GLN A OE1 1 
ATOM   2158 N  NE2 . GLN A 1 254 ? 1.513   0.488   25.266  1.00 38.39  ? 255 GLN A NE2 1 
ATOM   2159 N  N   . ILE A 1 255 ? 0.520   -1.583  18.699  1.00 10.35  ? 256 ILE A N   1 
ATOM   2160 C  CA  . ILE A 1 255 ? -0.499  -1.746  17.655  1.00 10.00  ? 256 ILE A CA  1 
ATOM   2161 C  C   . ILE A 1 255 ? -1.882  -1.757  18.314  1.00 10.00  ? 256 ILE A C   1 
ATOM   2162 O  O   . ILE A 1 255 ? -2.063  -2.501  19.294  1.00 12.24  ? 256 ILE A O   1 
ATOM   2163 C  CB  . ILE A 1 255 ? -0.245  -2.971  16.831  1.00 10.58  ? 256 ILE A CB  1 
ATOM   2164 C  CG1 . ILE A 1 255 ? 1.230   -2.975  16.284  1.00 10.71  ? 256 ILE A CG1 1 
ATOM   2165 C  CG2 . ILE A 1 255 ? -1.268  -3.138  15.739  1.00 10.64  ? 256 ILE A CG2 1 
ATOM   2166 C  CD1 . ILE A 1 255 ? 1.577   -4.188  15.461  1.00 12.67  ? 256 ILE A CD1 1 
ATOM   2167 N  N   . LYS A 1 256 ? -2.797  -0.936  17.830  1.00 9.70   ? 257 LYS A N   1 
ATOM   2168 C  CA  . LYS A 1 256 ? -4.130  -0.854  18.374  1.00 9.87   ? 257 LYS A CA  1 
ATOM   2169 C  C   . LYS A 1 256 ? -5.102  -1.492  17.404  1.00 9.77   ? 257 LYS A C   1 
ATOM   2170 O  O   . LYS A 1 256 ? -4.929  -1.352  16.214  1.00 12.17  ? 257 LYS A O   1 
ATOM   2171 C  CB  . LYS A 1 256 ? -4.485  0.655   18.663  1.00 12.30  ? 257 LYS A CB  1 
ATOM   2172 C  CG  . LYS A 1 256 ? -3.522  1.217   19.700  1.00 17.09  ? 257 LYS A CG  1 
ATOM   2173 C  CD  . LYS A 1 256 ? -3.688  2.598   20.052  1.00 20.17  ? 257 LYS A CD  1 
ATOM   2174 C  CE  . LYS A 1 256 ? -2.491  2.987   20.895  1.00 28.25  ? 257 LYS A CE  1 
ATOM   2175 N  NZ  . LYS A 1 256 ? -2.584  4.482   21.126  1.00 35.23  ? 257 LYS A NZ  1 
ATOM   2176 N  N   . ALA A 1 257 ? -6.146  -2.098  17.933  1.00 10.71  ? 258 ALA A N   1 
ATOM   2177 C  CA  . ALA A 1 257 ? -7.222  -2.707  17.153  1.00 11.05  ? 258 ALA A CA  1 
ATOM   2178 C  C   . ALA A 1 257 ? -8.502  -1.914  17.325  1.00 10.83  ? 258 ALA A C   1 
ATOM   2179 O  O   . ALA A 1 257 ? -8.837  -1.465  18.450  1.00 12.18  ? 258 ALA A O   1 
ATOM   2180 C  CB  . ALA A 1 257 ? -7.510  -4.167  17.586  1.00 12.35  ? 258 ALA A CB  1 
ATOM   2181 N  N   . SER A 1 258 ? -9.233  -1.759  16.212  1.00 10.76  ? 259 SER A N   1 
ATOM   2182 C  CA  . SER A 1 258 ? -10.522 -1.027  16.224  1.00 12.11  ? 259 SER A CA  1 
ATOM   2183 C  C   . SER A 1 258 ? -11.650 -1.916  16.674  1.00 13.43  ? 259 SER A C   1 
ATOM   2184 O  O   . SER A 1 258 ? -12.772 -1.436  16.823  1.00 18.15  ? 259 SER A O   1 
ATOM   2185 C  CB  . SER A 1 258 ? -10.830 -0.463  14.864  1.00 12.48  ? 259 SER A CB  1 
ATOM   2186 O  OG  . SER A 1 258 ? -11.212 -1.540  13.960  1.00 11.71  ? 259 SER A OG  1 
ATOM   2187 N  N   . PHE A 1 259 ? -11.385 -3.210  16.904  1.00 14.33  ? 260 PHE A N   1 
ATOM   2188 C  CA  . PHE A 1 259 ? -12.410 -4.255  17.052  1.00 16.40  ? 260 PHE A CA  1 
ATOM   2189 C  C   . PHE A 1 259 ? -12.010 -5.174  18.178  1.00 18.44  ? 260 PHE A C   1 
ATOM   2190 O  O   . PHE A 1 259 ? -10.820 -5.343  18.483  1.00 20.54  ? 260 PHE A O   1 
ATOM   2191 C  CB  . PHE A 1 259 ? -12.614 -5.061  15.752  1.00 16.31  ? 260 PHE A CB  1 
ATOM   2192 C  CG  . PHE A 1 259 ? -11.341 -5.773  15.354  1.00 14.59  ? 260 PHE A CG  1 
ATOM   2193 C  CD1 . PHE A 1 259 ? -10.327 -5.067  14.642  1.00 13.30  ? 260 PHE A CD1 1 
ATOM   2194 C  CD2 . PHE A 1 259 ? -11.074 -7.060  15.800  1.00 18.66  ? 260 PHE A CD2 1 
ATOM   2195 C  CE1 . PHE A 1 259 ? -9.103  -5.692  14.375  1.00 15.71  ? 260 PHE A CE1 1 
ATOM   2196 C  CE2 . PHE A 1 259 ? -9.845  -7.659  15.499  1.00 20.24  ? 260 PHE A CE2 1 
ATOM   2197 C  CZ  . PHE A 1 259 ? -8.886  -7.007  14.789  1.00 18.54  ? 260 PHE A CZ  1 
ATOM   2198 N  N   . LYS A 1 260 ? -13.044 -5.796  18.746  1.00 30.73  ? 261 LYS A N   1 
ATOM   2199 C  CA  . LYS A 1 260 ? -13.035 -6.947  19.691  1.00 35.55  ? 261 LYS A CA  1 
ATOM   2200 C  C   . LYS A 1 260 ? -12.360 -6.877  21.058  1.00 44.65  ? 261 LYS A C   1 
ATOM   2201 O  O   . LYS A 1 260 ? -11.145 -7.004  21.215  0.01 37.58  ? 261 LYS A O   1 
ATOM   2202 C  CB  . LYS A 1 260 ? -12.800 -8.306  18.980  1.00 45.72  ? 261 LYS A CB  1 
ATOM   2203 C  CG  . LYS A 1 260 ? -13.800 -8.552  17.856  1.00 52.23  ? 261 LYS A CG  1 
ATOM   2204 C  CD  . LYS A 1 260 ? -13.645 -9.954  17.261  1.00 56.66  ? 261 LYS A CD  1 
ATOM   2205 C  CE  . LYS A 1 260 ? -12.203 -10.227 16.790  1.00 49.00  ? 261 LYS A CE  1 
ATOM   2206 N  NZ  . LYS A 1 260 ? -11.916 -11.582 16.216  1.00 58.80  ? 261 LYS A NZ  1 
ATOM   2207 O  OXT . LYS A 1 260 ? -13.095 -6.680  22.043  1.00 63.45  ? 261 LYS A OXT 1 
ATOM   2208 N  N   . SER B 1 2   ? 2.726   -13.316 -27.220 1.00 57.25  ? 2   SER B N   1 
ATOM   2209 C  CA  . SER B 1 2   ? 3.808   -14.242 -26.761 1.00 41.67  ? 2   SER B CA  1 
ATOM   2210 C  C   . SER B 1 2   ? 3.649   -14.490 -25.265 1.00 43.30  ? 2   SER B C   1 
ATOM   2211 O  O   . SER B 1 2   ? 4.622   -14.318 -24.505 1.00 59.49  ? 2   SER B O   1 
ATOM   2212 C  CB  . SER B 1 2   ? 5.223   -13.708 -27.148 1.00 29.86  ? 2   SER B CB  1 
ATOM   2213 O  OG  . SER B 1 2   ? 6.322   -14.561 -26.784 1.00 35.31  ? 2   SER B OG  1 
ATOM   2214 N  N   . HIS B 1 3   ? 2.426   -14.848 -24.842 1.00 46.94  ? 3   HIS B N   1 
ATOM   2215 C  CA  . HIS B 1 3   ? 2.275   -15.447 -23.524 1.00 46.80  ? 3   HIS B CA  1 
ATOM   2216 C  C   . HIS B 1 3   ? 1.225   -16.523 -23.415 1.00 51.19  ? 3   HIS B C   1 
ATOM   2217 O  O   . HIS B 1 3   ? 0.713   -16.780 -22.308 1.00 53.37  ? 3   HIS B O   1 
ATOM   2218 C  CB  . HIS B 1 3   ? 2.149   -14.380 -22.399 1.00 52.32  ? 3   HIS B CB  1 
ATOM   2219 N  N   . HIS B 1 4   ? 0.881   -17.187 -24.515 1.00 48.58  ? 4   HIS B N   1 
ATOM   2220 C  CA  . HIS B 1 4   ? 0.477   -18.578 -24.344 1.00 36.31  ? 4   HIS B CA  1 
ATOM   2221 C  C   . HIS B 1 4   ? 1.023   -19.636 -25.286 1.00 23.97  ? 4   HIS B C   1 
ATOM   2222 O  O   . HIS B 1 4   ? 0.756   -20.843 -25.114 1.00 24.71  ? 4   HIS B O   1 
ATOM   2223 C  CB  . HIS B 1 4   ? -0.945  -18.872 -23.927 1.00 39.89  ? 4   HIS B CB  1 
ATOM   2224 C  CG  . HIS B 1 4   ? -1.023  -19.860 -22.782 1.00 71.81  ? 4   HIS B CG  1 
ATOM   2225 N  N   . TRP B 1 5   ? 1.896   -19.267 -26.176 1.00 19.86  ? 5   TRP B N   1 
ATOM   2226 C  CA  . TRP B 1 5   ? 2.511   -20.277 -27.065 1.00 17.76  ? 5   TRP B CA  1 
ATOM   2227 C  C   . TRP B 1 5   ? 3.526   -21.071 -26.271 1.00 18.13  ? 5   TRP B C   1 
ATOM   2228 O  O   . TRP B 1 5   ? 4.042   -20.573 -25.244 1.00 19.23  ? 5   TRP B O   1 
ATOM   2229 C  CB  . TRP B 1 5   ? 3.125   -19.551 -28.255 1.00 16.95  ? 5   TRP B CB  1 
ATOM   2230 C  CG  . TRP B 1 5   ? 4.319   -18.736 -27.899 1.00 14.03  ? 5   TRP B CG  1 
ATOM   2231 C  CD1 . TRP B 1 5   ? 4.363   -17.379 -27.594 1.00 16.44  ? 5   TRP B CD1 1 
ATOM   2232 C  CD2 . TRP B 1 5   ? 5.701   -19.194 -27.835 1.00 14.11  ? 5   TRP B CD2 1 
ATOM   2233 N  NE1 . TRP B 1 5   ? 5.640   -16.978 -27.336 1.00 17.12  ? 5   TRP B NE1 1 
ATOM   2234 C  CE2 . TRP B 1 5   ? 6.489   -18.019 -27.474 1.00 14.75  ? 5   TRP B CE2 1 
ATOM   2235 C  CE3 . TRP B 1 5   ? 6.358   -20.425 -28.085 1.00 14.30  ? 5   TRP B CE3 1 
ATOM   2236 C  CZ2 . TRP B 1 5   ? 7.834   -18.076 -27.346 1.00 15.04  ? 5   TRP B CZ2 1 
ATOM   2237 C  CZ3 . TRP B 1 5   ? 7.733   -20.464 -27.944 1.00 13.98  ? 5   TRP B CZ3 1 
ATOM   2238 C  CH2 . TRP B 1 5   ? 8.476   -19.299 -27.580 1.00 13.80  ? 5   TRP B CH2 1 
ATOM   2239 N  N   . GLY B 1 6   ? 3.814   -22.273 -26.749 1.00 16.49  ? 6   GLY B N   1 
ATOM   2240 C  CA  . GLY B 1 6   ? 4.885   -23.081 -26.160 1.00 18.49  ? 6   GLY B CA  1 
ATOM   2241 C  C   . GLY B 1 6   ? 5.176   -24.213 -27.086 1.00 16.40  ? 6   GLY B C   1 
ATOM   2242 O  O   . GLY B 1 6   ? 5.189   -24.045 -28.278 1.00 15.13  ? 6   GLY B O   1 
ATOM   2243 N  N   A TYR B 1 7   ? 5.373   -25.384 -26.506 0.50 19.84  ? 7   TYR B N   1 
ATOM   2244 N  N   B TYR B 1 7   ? 5.526   -25.356 -26.520 0.50 18.86  ? 7   TYR B N   1 
ATOM   2245 C  CA  A TYR B 1 7   ? 5.766   -26.566 -27.284 0.50 22.00  ? 7   TYR B CA  1 
ATOM   2246 C  CA  B TYR B 1 7   ? 5.992   -26.521 -27.323 0.50 21.35  ? 7   TYR B CA  1 
ATOM   2247 C  C   A TYR B 1 7   ? 4.806   -27.789 -27.188 0.50 25.51  ? 7   TYR B C   1 
ATOM   2248 C  C   B TYR B 1 7   ? 5.113   -27.763 -27.310 0.50 27.84  ? 7   TYR B C   1 
ATOM   2249 O  O   A TYR B 1 7   ? 5.129   -28.886 -27.702 0.50 38.29  ? 7   TYR B O   1 
ATOM   2250 O  O   B TYR B 1 7   ? 5.374   -28.745 -28.036 0.50 37.48  ? 7   TYR B O   1 
ATOM   2251 C  CB  A TYR B 1 7   ? 7.267   -26.846 -27.047 0.50 19.07  ? 7   TYR B CB  1 
ATOM   2252 C  CB  B TYR B 1 7   ? 7.457   -26.807 -27.007 0.50 18.33  ? 7   TYR B CB  1 
ATOM   2253 C  CG  A TYR B 1 7   ? 8.214   -25.752 -27.652 0.50 13.09  ? 7   TYR B CG  1 
ATOM   2254 C  CG  B TYR B 1 7   ? 8.359   -25.701 -27.531 0.50 13.29  ? 7   TYR B CG  1 
ATOM   2255 C  CD1 A TYR B 1 7   ? 8.616   -25.817 -28.990 0.50 12.55  ? 7   TYR B CD1 1 
ATOM   2256 C  CD1 B TYR B 1 7   ? 8.783   -25.703 -28.861 0.50 14.54  ? 7   TYR B CD1 1 
ATOM   2257 C  CD2 A TYR B 1 7   ? 8.749   -24.715 -26.851 0.50 15.10  ? 7   TYR B CD2 1 
ATOM   2258 C  CD2 B TYR B 1 7   ? 8.837   -24.697 -26.675 0.50 13.79  ? 7   TYR B CD2 1 
ATOM   2259 C  CE1 A TYR B 1 7   ? 9.510   -24.832 -29.505 0.50 10.09  ? 7   TYR B CE1 1 
ATOM   2260 C  CE1 B TYR B 1 7   ? 9.625   -24.690 -29.324 0.50 11.00  ? 7   TYR B CE1 1 
ATOM   2261 C  CE2 A TYR B 1 7   ? 9.598   -23.742 -27.368 0.50 13.16  ? 7   TYR B CE2 1 
ATOM   2262 C  CE2 B TYR B 1 7   ? 9.657   -23.693 -27.144 0.50 14.49  ? 7   TYR B CE2 1 
ATOM   2263 C  CZ  A TYR B 1 7   ? 10.012  -23.837 -28.670 0.50 10.24  ? 7   TYR B CZ  1 
ATOM   2264 C  CZ  B TYR B 1 7   ? 10.082  -23.731 -28.457 0.50 11.45  ? 7   TYR B CZ  1 
ATOM   2265 O  OH  A TYR B 1 7   ? 10.855  -22.920 -29.167 0.50 10.97  ? 7   TYR B OH  1 
ATOM   2266 O  OH  B TYR B 1 7   ? 10.915  -22.787 -28.926 0.50 13.15  ? 7   TYR B OH  1 
ATOM   2267 N  N   A GLY B 1 8   ? 3.571   -27.615 -26.698 0.50 26.62  ? 8   GLY B N   1 
ATOM   2268 N  N   B GLY B 1 8   ? 3.973   -27.705 -26.619 0.50 28.11  ? 8   GLY B N   1 
ATOM   2269 C  CA  A GLY B 1 8   ? 2.604   -28.727 -26.610 0.50 24.18  ? 8   GLY B CA  1 
ATOM   2270 C  CA  B GLY B 1 8   ? 3.032   -28.828 -26.584 0.50 24.51  ? 8   GLY B CA  1 
ATOM   2271 C  C   A GLY B 1 8   ? 1.557   -29.012 -27.711 0.50 28.30  ? 8   GLY B C   1 
ATOM   2272 C  C   B GLY B 1 8   ? 1.987   -29.014 -27.695 0.50 23.48  ? 8   GLY B C   1 
ATOM   2273 O  O   A GLY B 1 8   ? 1.527   -28.321 -28.730 0.50 28.47  ? 8   GLY B O   1 
ATOM   2274 O  O   B GLY B 1 8   ? 1.978   -28.285 -28.688 0.50 37.22  ? 8   GLY B O   1 
ATOM   2275 N  N   A LYS B 1 9   ? 0.703   -30.032 -27.499 0.50 21.70  ? 9   LYS B N   1 
ATOM   2276 N  N   B LYS B 1 9   ? 1.109   -30.008 -27.507 0.50 20.36  ? 9   LYS B N   1 
ATOM   2277 C  CA  A LYS B 1 9   ? -0.339  -30.452 -28.430 0.50 26.02  ? 9   LYS B CA  1 
ATOM   2278 C  CA  B LYS B 1 9   ? 0.035   -30.400 -28.440 0.50 28.04  ? 9   LYS B CA  1 
ATOM   2279 C  C   A LYS B 1 9   ? -1.205  -29.299 -28.694 0.50 20.68  ? 9   LYS B C   1 
ATOM   2280 C  C   B LYS B 1 9   ? -0.937  -29.289 -28.675 0.50 20.89  ? 9   LYS B C   1 
ATOM   2281 O  O   A LYS B 1 9   ? -1.607  -29.084 -29.863 0.50 25.88  ? 9   LYS B O   1 
ATOM   2282 O  O   B LYS B 1 9   ? -1.496  -29.165 -29.795 0.50 26.54  ? 9   LYS B O   1 
ATOM   2283 C  CB  A LYS B 1 9   ? -1.207  -31.572 -27.867 0.50 23.72  ? 9   LYS B CB  1 
ATOM   2284 C  CB  B LYS B 1 9   ? -0.754  -31.594 -27.892 0.50 26.80  ? 9   LYS B CB  1 
ATOM   2285 C  CG  A LYS B 1 9   ? -2.352  -31.993 -28.766 0.50 29.10  ? 9   LYS B CG  1 
ATOM   2286 C  CG  B LYS B 1 9   ? -2.036  -31.928 -28.627 0.50 29.65  ? 9   LYS B CG  1 
ATOM   2287 C  CD  A LYS B 1 9   ? -2.999  -33.272 -28.235 0.50 35.87  ? 9   LYS B CD  1 
ATOM   2288 C  CD  B LYS B 1 9   ? -2.665  -33.182 -28.019 0.50 31.94  ? 9   LYS B CD  1 
ATOM   2289 C  CE  A LYS B 1 9   ? -4.252  -33.630 -29.031 0.50 38.46  ? 9   LYS B CE  1 
ATOM   2290 C  CE  B LYS B 1 9   ? -4.016  -33.515 -28.651 0.50 41.18  ? 9   LYS B CE  1 
ATOM   2291 N  NZ  A LYS B 1 9   ? -5.240  -34.451 -28.265 0.50 46.67  ? 9   LYS B NZ  1 
ATOM   2292 N  NZ  B LYS B 1 9   ? -4.876  -34.376 -27.783 0.50 45.24  ? 9   LYS B NZ  1 
ATOM   2293 N  N   A HIS B 1 10  ? -1.564  -28.606 -27.609 0.50 30.17  ? 10  HIS B N   1 
ATOM   2294 N  N   B HIS B 1 10  ? -1.190  -28.527 -27.611 0.50 30.24  ? 10  HIS B N   1 
ATOM   2295 C  CA  A HIS B 1 10  ? -2.464  -27.500 -27.778 0.50 26.30  ? 10  HIS B CA  1 
ATOM   2296 C  CA  B HIS B 1 10  ? -2.254  -27.561 -27.686 0.50 29.89  ? 10  HIS B CA  1 
ATOM   2297 C  C   A HIS B 1 10  ? -1.771  -26.163 -27.955 0.50 23.49  ? 10  HIS B C   1 
ATOM   2298 C  C   B HIS B 1 10  ? -1.751  -26.194 -27.861 0.50 23.66  ? 10  HIS B C   1 
ATOM   2299 O  O   A HIS B 1 10  ? -2.459  -25.249 -28.339 0.50 26.28  ? 10  HIS B O   1 
ATOM   2300 O  O   B HIS B 1 10  ? -2.549  -25.301 -28.056 0.50 27.45  ? 10  HIS B O   1 
ATOM   2301 C  CB  A HIS B 1 10  ? -3.560  -27.474 -26.743 0.50 28.36  ? 10  HIS B CB  1 
ATOM   2302 C  CB  B HIS B 1 10  ? -3.124  -27.618 -26.475 0.50 25.88  ? 10  HIS B CB  1 
ATOM   2303 C  CG  A HIS B 1 10  ? -4.146  -28.831 -26.522 0.50 21.03  ? 10  HIS B CG  1 
ATOM   2304 C  CG  B HIS B 1 10  ? -3.953  -28.859 -26.439 0.50 22.20  ? 10  HIS B CG  1 
ATOM   2305 N  ND1 A HIS B 1 10  ? -5.289  -29.297 -27.142 0.50 26.32  ? 10  HIS B ND1 1 
ATOM   2306 N  ND1 B HIS B 1 10  ? -4.924  -29.140 -27.361 0.50 25.86  ? 10  HIS B ND1 1 
ATOM   2307 C  CD2 A HIS B 1 10  ? -3.656  -29.839 -25.787 0.50 16.87  ? 10  HIS B CD2 1 
ATOM   2308 C  CD2 B HIS B 1 10  ? -3.917  -29.901 -25.560 0.50 24.12  ? 10  HIS B CD2 1 
ATOM   2309 C  CE1 A HIS B 1 10  ? -5.526  -30.560 -26.746 0.50 20.01  ? 10  HIS B CE1 1 
ATOM   2310 C  CE1 B HIS B 1 10  ? -5.462  -30.340 -27.065 0.50 26.34  ? 10  HIS B CE1 1 
ATOM   2311 N  NE2 A HIS B 1 10  ? -4.494  -30.901 -25.918 0.50 16.61  ? 10  HIS B NE2 1 
ATOM   2312 N  NE2 B HIS B 1 10  ? -4.813  -30.814 -25.972 0.50 19.81  ? 10  HIS B NE2 1 
ATOM   2313 N  N   . ASN B 1 11  ? -0.430  -25.992 -27.757 1.00 24.74  ? 11  ASN B N   1 
ATOM   2314 C  CA  . ASN B 1 11  ? 0.152   -24.658 -27.889 1.00 20.29  ? 11  ASN B CA  1 
ATOM   2315 C  C   . ASN B 1 11  ? 1.461   -24.652 -28.668 1.00 18.75  ? 11  ASN B C   1 
ATOM   2316 O  O   . ASN B 1 11  ? 2.089   -23.598 -28.779 1.00 18.74  ? 11  ASN B O   1 
ATOM   2317 C  CB  . ASN B 1 11  ? 0.346   -23.882 -26.568 1.00 21.79  ? 11  ASN B CB  1 
ATOM   2318 C  CG  . ASN B 1 11  ? 1.412   -24.470 -25.672 1.00 22.09  ? 11  ASN B CG  1 
ATOM   2319 O  OD1 . ASN B 1 11  ? 1.988   -25.502 -25.990 1.00 24.42  ? 11  ASN B OD1 1 
ATOM   2320 N  ND2 . ASN B 1 11  ? 1.719   -23.798 -24.578 1.00 21.53  ? 11  ASN B ND2 1 
ATOM   2321 N  N   . GLY B 1 12  ? 1.809   -25.760 -29.286 1.00 18.27  ? 12  GLY B N   1 
ATOM   2322 C  CA  . GLY B 1 12  ? 3.112   -25.888 -29.948 1.00 17.99  ? 12  GLY B CA  1 
ATOM   2323 C  C   . GLY B 1 12  ? 3.092   -25.355 -31.344 1.00 14.61  ? 12  GLY B C   1 
ATOM   2324 O  O   . GLY B 1 12  ? 2.153   -24.680 -31.766 1.00 15.99  ? 12  GLY B O   1 
ATOM   2325 N  N   . PRO B 1 13  ? 4.170   -25.620 -32.074 1.00 14.65  ? 13  PRO B N   1 
ATOM   2326 C  CA  . PRO B 1 13  ? 4.451   -25.038 -33.360 1.00 14.58  ? 13  PRO B CA  1 
ATOM   2327 C  C   . PRO B 1 13  ? 3.302   -25.098 -34.329 1.00 13.21  ? 13  PRO B C   1 
ATOM   2328 O  O   . PRO B 1 13  ? 3.147   -24.120 -35.117 1.00 14.73  ? 13  PRO B O   1 
ATOM   2329 C  CB  . PRO B 1 13  ? 5.640   -25.848 -33.878 1.00 14.14  ? 13  PRO B CB  1 
ATOM   2330 C  CG  . PRO B 1 13  ? 6.440   -26.141 -32.653 1.00 15.63  ? 13  PRO B CG  1 
ATOM   2331 C  CD  . PRO B 1 13  ? 5.338   -26.395 -31.625 1.00 15.35  ? 13  PRO B CD  1 
ATOM   2332 N  N   . GLU B 1 14  ? 2.507   -26.140 -34.339 1.00 15.60  ? 14  GLU B N   1 
ATOM   2333 C  CA  . GLU B 1 14  ? 1.401   -26.232 -35.265 1.00 18.95  ? 14  GLU B CA  1 
ATOM   2334 C  C   . GLU B 1 14  ? 0.254   -25.231 -34.991 1.00 18.16  ? 14  GLU B C   1 
ATOM   2335 O  O   . GLU B 1 14  ? -0.625  -25.015 -35.832 1.00 18.90  ? 14  GLU B O   1 
ATOM   2336 C  CB  . GLU B 1 14  ? 0.982   -27.696 -35.265 1.00 21.11  ? 14  GLU B CB  1 
ATOM   2337 C  CG  . GLU B 1 14  ? 0.368   -28.270 -33.976 1.00 21.18  ? 14  GLU B CG  1 
ATOM   2338 C  CD  . GLU B 1 14  ? 1.211   -28.755 -32.769 1.00 23.18  ? 14  GLU B CD  1 
ATOM   2339 O  OE1 . GLU B 1 14  ? 2.365   -28.302 -32.621 1.00 20.60  ? 14  GLU B OE1 1 
ATOM   2340 O  OE2 . GLU B 1 14  ? 0.699   -29.582 -31.987 1.00 26.53  ? 14  GLU B OE2 1 
ATOM   2341 N  N   . HIS B 1 15  ? 0.277   -24.632 -33.804 1.00 15.25  ? 15  HIS B N   1 
ATOM   2342 C  CA  . HIS B 1 15  ? -0.737  -23.632 -33.382 1.00 16.62  ? 15  HIS B CA  1 
ATOM   2343 C  C   . HIS B 1 15  ? -0.291  -22.189 -33.555 1.00 15.15  ? 15  HIS B C   1 
ATOM   2344 O  O   . HIS B 1 15  ? -1.150  -21.275 -33.542 1.00 16.77  ? 15  HIS B O   1 
ATOM   2345 C  CB  . HIS B 1 15  ? -1.097  -23.812 -31.927 1.00 16.76  ? 15  HIS B CB  1 
ATOM   2346 C  CG  . HIS B 1 15  ? -1.809  -25.077 -31.700 1.00 17.14  ? 15  HIS B CG  1 
ATOM   2347 N  ND1 . HIS B 1 15  ? -3.194  -25.184 -31.824 1.00 19.53  ? 15  HIS B ND1 1 
ATOM   2348 C  CD2 . HIS B 1 15  ? -1.344  -26.352 -31.377 1.00 19.96  ? 15  HIS B CD2 1 
ATOM   2349 C  CE1 . HIS B 1 15  ? -3.545  -26.447 -31.549 1.00 26.62  ? 15  HIS B CE1 1 
ATOM   2350 N  NE2 . HIS B 1 15  ? -2.433  -27.162 -31.264 1.00 25.13  ? 15  HIS B NE2 1 
ATOM   2351 N  N   . TRP B 1 16  ? 1.016   -21.969 -33.722 1.00 13.30  ? 16  TRP B N   1 
ATOM   2352 C  CA  . TRP B 1 16  ? 1.537   -20.620 -33.673 1.00 12.62  ? 16  TRP B CA  1 
ATOM   2353 C  C   . TRP B 1 16  ? 0.978   -19.636 -34.669 1.00 11.92  ? 16  TRP B C   1 
ATOM   2354 O  O   . TRP B 1 16  ? 0.880   -18.427 -34.405 1.00 12.98  ? 16  TRP B O   1 
ATOM   2355 C  CB  . TRP B 1 16  ? 3.076   -20.650 -33.762 1.00 12.03  ? 16  TRP B CB  1 
ATOM   2356 C  CG  . TRP B 1 16  ? 3.775   -21.328 -32.609 1.00 10.94  ? 16  TRP B CG  1 
ATOM   2357 C  CD1 . TRP B 1 16  ? 3.263   -21.777 -31.421 1.00 12.68  ? 16  TRP B CD1 1 
ATOM   2358 C  CD2 . TRP B 1 16  ? 5.167   -21.633 -32.576 1.00 11.04  ? 16  TRP B CD2 1 
ATOM   2359 N  NE1 . TRP B 1 16  ? 4.230   -22.366 -30.684 1.00 13.07  ? 16  TRP B NE1 1 
ATOM   2360 C  CE2 . TRP B 1 16  ? 5.434   -22.275 -31.314 1.00 11.77  ? 16  TRP B CE2 1 
ATOM   2361 C  CE3 . TRP B 1 16  ? 6.225   -21.464 -33.486 1.00 11.31  ? 16  TRP B CE3 1 
ATOM   2362 C  CZ2 . TRP B 1 16  ? 6.722   -22.718 -30.949 1.00 10.98  ? 16  TRP B CZ2 1 
ATOM   2363 C  CZ3 . TRP B 1 16  ? 7.502   -21.896 -33.099 1.00 11.35  ? 16  TRP B CZ3 1 
ATOM   2364 C  CH2 . TRP B 1 16  ? 7.734   -22.504 -31.857 1.00 11.85  ? 16  TRP B CH2 1 
ATOM   2365 N  N   . HIS B 1 17  ? 0.604   -20.157 -35.847 1.00 12.72  ? 17  HIS B N   1 
ATOM   2366 C  CA  . HIS B 1 17  ? 0.109   -19.294 -36.900 1.00 13.93  ? 17  HIS B CA  1 
ATOM   2367 C  C   . HIS B 1 17  ? -1.156  -18.520 -36.524 1.00 14.44  ? 17  HIS B C   1 
ATOM   2368 O  O   . HIS B 1 17  ? -1.454  -17.472 -37.137 1.00 15.20  ? 17  HIS B O   1 
ATOM   2369 C  CB  . HIS B 1 17  ? -0.200  -20.059 -38.215 1.00 15.15  ? 17  HIS B CB  1 
ATOM   2370 C  CG  . HIS B 1 17  ? -1.423  -20.924 -38.125 1.00 15.96  ? 17  HIS B CG  1 
ATOM   2371 N  ND1 . HIS B 1 17  ? -2.640  -20.532 -38.584 1.00 19.05  ? 17  HIS B ND1 1 
ATOM   2372 C  CD2 . HIS B 1 17  ? -1.592  -22.148 -37.549 1.00 17.38  ? 17  HIS B CD2 1 
ATOM   2373 C  CE1 . HIS B 1 17  ? -3.518  -21.450 -38.347 1.00 19.27  ? 17  HIS B CE1 1 
ATOM   2374 N  NE2 . HIS B 1 17  ? -2.939  -22.461 -37.719 1.00 18.43  ? 17  HIS B NE2 1 
ATOM   2375 N  N   . LYS B 1 18  ? -1.932  -18.979 -35.540 1.00 15.99  ? 18  LYS B N   1 
ATOM   2376 C  CA  . LYS B 1 18  ? -3.173  -18.260 -35.146 1.00 16.21  ? 18  LYS B CA  1 
ATOM   2377 C  C   . LYS B 1 18  ? -2.845  -16.925 -34.449 1.00 17.82  ? 18  LYS B C   1 
ATOM   2378 O  O   . LYS B 1 18  ? -3.481  -15.919 -34.727 1.00 23.79  ? 18  LYS B O   1 
ATOM   2379 C  CB  . LYS B 1 18  ? -3.969  -19.159 -34.244 1.00 17.26  ? 18  LYS B CB  1 
ATOM   2380 C  CG  . LYS B 1 18  ? -4.567  -20.376 -34.983 1.00 18.74  ? 18  LYS B CG  1 
ATOM   2381 C  CD  . LYS B 1 18  ? -5.301  -21.345 -34.056 1.00 18.37  ? 18  LYS B CD  1 
ATOM   2382 C  CE  . LYS B 1 18  ? -4.320  -22.294 -33.415 1.00 17.18  ? 18  LYS B CE  1 
ATOM   2383 N  NZ  . LYS B 1 18  ? -5.020  -23.136 -32.420 1.00 17.10  ? 18  LYS B NZ  1 
ATOM   2384 N  N   . ASP B 1 19  ? -1.818  -16.896 -33.612 1.00 15.97  ? 19  ASP B N   1 
ATOM   2385 C  CA  . ASP B 1 19  ? -1.366  -15.612 -33.012 1.00 17.79  ? 19  ASP B CA  1 
ATOM   2386 C  C   . ASP B 1 19  ? -0.381  -14.871 -33.910 1.00 16.13  ? 19  ASP B C   1 
ATOM   2387 O  O   . ASP B 1 19  ? -0.239  -13.683 -33.809 1.00 18.43  ? 19  ASP B O   1 
ATOM   2388 C  CB  . ASP B 1 19  ? -0.810  -15.800 -31.576 1.00 22.93  ? 19  ASP B CB  1 
ATOM   2389 C  CG  . ASP B 1 19  ? -1.886  -15.848 -30.497 1.00 25.35  ? 19  ASP B CG  1 
ATOM   2390 O  OD1 . ASP B 1 19  ? -2.957  -15.303 -30.702 1.00 28.70  ? 19  ASP B OD1 1 
ATOM   2391 O  OD2 . ASP B 1 19  ? -1.654  -16.456 -29.426 1.00 44.82  ? 19  ASP B OD2 1 
ATOM   2392 N  N   . PHE B 1 20  ? 0.364   -15.639 -34.705 1.00 14.57  ? 20  PHE B N   1 
ATOM   2393 C  CA  . PHE B 1 20  ? 1.487   -15.094 -35.461 1.00 14.44  ? 20  PHE B CA  1 
ATOM   2394 C  C   . PHE B 1 20  ? 1.373   -15.588 -36.893 1.00 14.10  ? 20  PHE B C   1 
ATOM   2395 O  O   . PHE B 1 20  ? 2.054   -16.559 -37.261 1.00 13.40  ? 20  PHE B O   1 
ATOM   2396 C  CB  . PHE B 1 20  ? 2.843   -15.533 -34.811 1.00 13.92  ? 20  PHE B CB  1 
ATOM   2397 C  CG  . PHE B 1 20  ? 2.937   -15.150 -33.367 1.00 14.94  ? 20  PHE B CG  1 
ATOM   2398 C  CD1 . PHE B 1 20  ? 3.336   -13.835 -33.047 1.00 18.11  ? 20  PHE B CD1 1 
ATOM   2399 C  CD2 . PHE B 1 20  ? 2.577   -16.051 -32.328 1.00 17.17  ? 20  PHE B CD2 1 
ATOM   2400 C  CE1 . PHE B 1 20  ? 3.326   -13.426 -31.723 1.00 18.29  ? 20  PHE B CE1 1 
ATOM   2401 C  CE2 . PHE B 1 20  ? 2.550   -15.625 -31.007 1.00 18.54  ? 20  PHE B CE2 1 
ATOM   2402 C  CZ  . PHE B 1 20  ? 2.979   -14.335 -30.715 1.00 18.45  ? 20  PHE B CZ  1 
ATOM   2403 N  N   . PRO B 1 21  ? 0.509   -14.964 -37.712 1.00 15.44  ? 21  PRO B N   1 
ATOM   2404 C  CA  . PRO B 1 21  ? 0.288   -15.498 -39.054 1.00 14.75  ? 21  PRO B CA  1 
ATOM   2405 C  C   . PRO B 1 21  ? 1.504   -15.568 -39.967 1.00 14.98  ? 21  PRO B C   1 
ATOM   2406 O  O   . PRO B 1 21  ? 1.493   -16.319 -40.923 1.00 15.33  ? 21  PRO B O   1 
ATOM   2407 C  CB  . PRO B 1 21  ? -0.799  -14.534 -39.681 1.00 20.12  ? 21  PRO B CB  1 
ATOM   2408 C  CG  . PRO B 1 21  ? -1.030  -13.478 -38.659 1.00 26.19  ? 21  PRO B CG  1 
ATOM   2409 C  CD  . PRO B 1 21  ? -0.457  -13.904 -37.339 1.00 17.57  ? 21  PRO B CD  1 
ATOM   2410 N  N   A ILE B 1 22  ? 2.561   -14.820 -39.678 0.50 13.99  ? 22  ILE B N   1 
ATOM   2411 N  N   B ILE B 1 22  ? 2.553   -14.810 -39.679 0.50 14.11  ? 22  ILE B N   1 
ATOM   2412 C  CA  A ILE B 1 22  ? 3.802   -14.940 -40.432 0.50 13.37  ? 22  ILE B CA  1 
ATOM   2413 C  CA  B ILE B 1 22  ? 3.795   -14.928 -40.422 0.50 13.40  ? 22  ILE B CA  1 
ATOM   2414 C  C   A ILE B 1 22  ? 4.396   -16.365 -40.307 0.50 11.73  ? 22  ILE B C   1 
ATOM   2415 C  C   B ILE B 1 22  ? 4.384   -16.359 -40.310 0.50 11.80  ? 22  ILE B C   1 
ATOM   2416 O  O   A ILE B 1 22  ? 5.310   -16.717 -41.084 0.50 12.43  ? 22  ILE B O   1 
ATOM   2417 O  O   B ILE B 1 22  ? 5.282   -16.708 -41.098 0.50 12.46  ? 22  ILE B O   1 
ATOM   2418 C  CB  A ILE B 1 22  ? 4.814   -13.879 -39.974 0.50 12.81  ? 22  ILE B CB  1 
ATOM   2419 C  CB  B ILE B 1 22  ? 4.808   -13.869 -39.945 0.50 13.41  ? 22  ILE B CB  1 
ATOM   2420 C  CG1 A ILE B 1 22  ? 5.939   -13.633 -40.978 0.50 13.69  ? 22  ILE B CG1 1 
ATOM   2421 C  CG1 B ILE B 1 22  ? 5.853   -13.509 -40.998 0.50 14.95  ? 22  ILE B CG1 1 
ATOM   2422 C  CG2 A ILE B 1 22  ? 5.398   -14.173 -38.577 0.50 13.88  ? 22  ILE B CG2 1 
ATOM   2423 C  CG2 B ILE B 1 22  ? 5.484   -14.244 -38.610 0.50 14.71  ? 22  ILE B CG2 1 
ATOM   2424 C  CD1 A ILE B 1 22  ? 6.761   -12.444 -40.618 0.50 12.59  ? 22  ILE B CD1 1 
ATOM   2425 C  CD1 B ILE B 1 22  ? 5.232   -13.100 -42.303 0.50 17.70  ? 22  ILE B CD1 1 
ATOM   2426 N  N   . ALA B 1 23  ? 3.903   -17.182 -39.381 1.00 12.04  ? 23  ALA B N   1 
ATOM   2427 C  CA  . ALA B 1 23  ? 4.342   -18.593 -39.278 1.00 12.17  ? 23  ALA B CA  1 
ATOM   2428 C  C   . ALA B 1 23  ? 4.251   -19.287 -40.582 1.00 12.47  ? 23  ALA B C   1 
ATOM   2429 O  O   . ALA B 1 23  ? 4.963   -20.292 -40.800 1.00 12.15  ? 23  ALA B O   1 
ATOM   2430 C  CB  . ALA B 1 23  ? 3.549   -19.349 -38.279 1.00 12.89  ? 23  ALA B CB  1 
ATOM   2431 N  N   . LYS B 1 24  ? 3.315   -18.864 -41.471 1.00 12.91  ? 24  LYS B N   1 
ATOM   2432 C  CA  . LYS B 1 24  ? 3.142   -19.504 -42.801 1.00 13.93  ? 24  LYS B CA  1 
ATOM   2433 C  C   . LYS B 1 24  ? 3.755   -18.605 -43.901 1.00 15.80  ? 24  LYS B C   1 
ATOM   2434 O  O   . LYS B 1 24  ? 3.400   -18.758 -45.061 1.00 18.34  ? 24  LYS B O   1 
ATOM   2435 C  CB  . LYS B 1 24  ? 1.642   -19.798 -43.132 1.00 15.45  ? 24  LYS B CB  1 
ATOM   2436 C  CG  . LYS B 1 24  ? 1.019   -20.734 -42.101 1.00 17.74  ? 24  LYS B CG  1 
ATOM   2437 C  CD  . LYS B 1 24  ? -0.429  -20.914 -42.539 1.00 22.10  ? 24  LYS B CD  1 
ATOM   2438 C  CE  . LYS B 1 24  ? -1.255  -21.789 -41.632 1.00 26.38  ? 24  LYS B CE  1 
ATOM   2439 N  NZ  . LYS B 1 24  ? -0.796  -23.181 -41.745 1.00 29.15  ? 24  LYS B NZ  1 
ATOM   2440 N  N   . GLY B 1 25  ? 4.778   -17.802 -43.547 1.00 14.00  ? 25  GLY B N   1 
ATOM   2441 C  CA  . GLY B 1 25  ? 5.361   -16.831 -44.481 1.00 14.79  ? 25  GLY B CA  1 
ATOM   2442 C  C   . GLY B 1 25  ? 6.306   -17.479 -45.463 1.00 13.61  ? 25  GLY B C   1 
ATOM   2443 O  O   . GLY B 1 25  ? 6.534   -18.700 -45.535 1.00 14.86  ? 25  GLY B O   1 
ATOM   2444 N  N   . GLU B 1 26  ? 6.980   -16.566 -46.165 1.00 15.40  ? 26  GLU B N   1 
ATOM   2445 C  CA  . GLU B 1 26  ? 7.846   -16.969 -47.252 1.00 15.47  ? 26  GLU B CA  1 
ATOM   2446 C  C   . GLU B 1 26  ? 9.279   -17.247 -46.864 1.00 13.26  ? 26  GLU B C   1 
ATOM   2447 O  O   . GLU B 1 26  ? 10.038  -17.711 -47.735 1.00 14.73  ? 26  GLU B O   1 
ATOM   2448 C  CB  . GLU B 1 26  ? 7.827   -15.863 -48.335 1.00 19.19  ? 26  GLU B CB  1 
ATOM   2449 C  CG  . GLU B 1 26  ? 6.388   -15.688 -48.961 1.00 20.24  ? 26  GLU B CG  1 
ATOM   2450 C  CD  . GLU B 1 26  ? 5.742   -16.961 -49.569 1.00 29.86  ? 26  GLU B CD  1 
ATOM   2451 O  OE1 . GLU B 1 26  ? 6.341   -17.624 -50.455 1.00 41.14  ? 26  GLU B OE1 1 
ATOM   2452 O  OE2 . GLU B 1 26  ? 4.593   -17.286 -49.182 1.00 42.64  ? 26  GLU B OE2 1 
ATOM   2453 N  N   . ARG B 1 27  ? 9.682   -16.920 -45.632 1.00 11.13  ? 27  ARG B N   1 
ATOM   2454 C  CA  . ARG B 1 27  ? 11.080  -17.101 -45.292 1.00 9.67   ? 27  ARG B CA  1 
ATOM   2455 C  C   . ARG B 1 27  ? 11.190  -17.548 -43.830 1.00 8.69   ? 27  ARG B C   1 
ATOM   2456 O  O   . ARG B 1 27  ? 11.911  -16.948 -43.003 1.00 9.46   ? 27  ARG B O   1 
ATOM   2457 C  CB  . ARG B 1 27  ? 11.953  -15.891 -45.641 1.00 12.63  ? 27  ARG B CB  1 
ATOM   2458 C  CG  . ARG B 1 27  ? 11.591  -14.567 -45.050 1.00 16.04  ? 27  ARG B CG  1 
ATOM   2459 C  CD  . ARG B 1 27  ? 12.661  -13.492 -45.267 1.00 22.10  ? 27  ARG B CD  1 
ATOM   2460 N  NE  . ARG B 1 27  ? 13.805  -13.541 -44.350 1.00 15.18  ? 27  ARG B NE  1 
ATOM   2461 C  CZ  . ARG B 1 27  ? 14.733  -12.578 -44.254 1.00 12.67  ? 27  ARG B CZ  1 
ATOM   2462 N  NH1 . ARG B 1 27  ? 14.650  -11.488 -45.016 1.00 16.68  ? 27  ARG B NH1 1 
ATOM   2463 N  NH2 . ARG B 1 27  ? 15.745  -12.688 -43.393 1.00 13.79  ? 27  ARG B NH2 1 
ATOM   2464 N  N   . GLN B 1 28  ? 10.453  -18.632 -43.531 1.00 8.68   ? 28  GLN B N   1 
ATOM   2465 C  CA  . GLN B 1 28  ? 10.425  -19.175 -42.185 1.00 8.15   ? 28  GLN B CA  1 
ATOM   2466 C  C   . GLN B 1 28  ? 11.605  -20.115 -41.918 1.00 8.19   ? 28  GLN B C   1 
ATOM   2467 O  O   . GLN B 1 28  ? 12.069  -20.840 -42.813 1.00 8.82   ? 28  GLN B O   1 
ATOM   2468 C  CB  . GLN B 1 28  ? 9.082   -19.827 -41.904 1.00 9.91   ? 28  GLN B CB  1 
ATOM   2469 C  CG  . GLN B 1 28  ? 7.948   -18.780 -41.796 1.00 10.21  ? 28  GLN B CG  1 
ATOM   2470 C  CD  . GLN B 1 28  ? 8.070   -17.974 -40.511 1.00 8.94   ? 28  GLN B CD  1 
ATOM   2471 O  OE1 . GLN B 1 28  ? 7.901   -18.522 -39.429 1.00 9.52   ? 28  GLN B OE1 1 
ATOM   2472 N  NE2 . GLN B 1 28  ? 8.402   -16.697 -40.629 1.00 9.67   ? 28  GLN B NE2 1 
ATOM   2473 N  N   . SER B 1 29  ? 11.972  -20.201 -40.633 1.00 7.92   ? 29  SER B N   1 
ATOM   2474 C  CA  . SER B 1 29  ? 13.039  -21.080 -40.160 1.00 7.56   ? 29  SER B CA  1 
ATOM   2475 C  C   . SER B 1 29  ? 12.517  -21.968 -39.062 1.00 7.22   ? 29  SER B C   1 
ATOM   2476 O  O   . SER B 1 29  ? 11.547  -21.597 -38.352 1.00 7.83   ? 29  SER B O   1 
ATOM   2477 C  CB  . SER B 1 29  ? 14.171  -20.209 -39.635 1.00 7.82   ? 29  SER B CB  1 
ATOM   2478 O  OG  . SER B 1 29  ? 14.796  -19.491 -40.714 1.00 7.76   ? 29  SER B OG  1 
ATOM   2479 N  N   . PRO B 1 30  ? 13.166  -23.097 -38.786 1.00 7.05   ? 30  PRO B N   1 
ATOM   2480 C  CA  . PRO B 1 30  ? 14.336  -23.630 -39.514 1.00 7.44   ? 30  PRO B CA  1 
ATOM   2481 C  C   . PRO B 1 30  ? 13.924  -24.312 -40.816 1.00 7.02   ? 30  PRO B C   1 
ATOM   2482 O  O   . PRO B 1 30  ? 12.739  -24.324 -41.145 1.00 7.88   ? 30  PRO B O   1 
ATOM   2483 C  CB  . PRO B 1 30  ? 14.891  -24.685 -38.519 1.00 7.69   ? 30  PRO B CB  1 
ATOM   2484 C  CG  . PRO B 1 30  ? 13.573  -25.258 -37.903 1.00 8.34   ? 30  PRO B CG  1 
ATOM   2485 C  CD  . PRO B 1 30  ? 12.679  -24.011 -37.748 1.00 8.17   ? 30  PRO B CD  1 
ATOM   2486 N  N   . VAL B 1 31  ? 14.903  -24.842 -41.520 1.00 7.56   ? 31  VAL B N   1 
ATOM   2487 C  CA  . VAL B 1 31  ? 14.722  -25.620 -42.750 1.00 7.54   ? 31  VAL B CA  1 
ATOM   2488 C  C   . VAL B 1 31  ? 15.582  -26.834 -42.702 1.00 7.90   ? 31  VAL B C   1 
ATOM   2489 O  O   . VAL B 1 31  ? 16.597  -26.884 -41.963 1.00 8.85   ? 31  VAL B O   1 
ATOM   2490 C  CB  . VAL B 1 31  ? 15.033  -24.760 -44.010 1.00 9.09   ? 31  VAL B CB  1 
ATOM   2491 C  CG1 . VAL B 1 31  ? 14.112  -23.580 -44.100 1.00 9.63   ? 31  VAL B CG1 1 
ATOM   2492 C  CG2 . VAL B 1 31  ? 16.539  -24.352 -44.057 1.00 9.95   ? 31  VAL B CG2 1 
ATOM   2493 N  N   . ASP B 1 32  ? 15.274  -27.798 -43.578 1.00 8.19   ? 32  ASP B N   1 
ATOM   2494 C  CA  . ASP B 1 32  ? 16.178  -28.897 -43.871 1.00 8.74   ? 32  ASP B CA  1 
ATOM   2495 C  C   . ASP B 1 32  ? 17.212  -28.384 -44.851 1.00 8.12   ? 32  ASP B C   1 
ATOM   2496 O  O   . ASP B 1 32  ? 16.919  -27.729 -45.859 1.00 10.55  ? 32  ASP B O   1 
ATOM   2497 C  CB  . ASP B 1 32  ? 15.443  -30.081 -44.460 1.00 10.07  ? 32  ASP B CB  1 
ATOM   2498 C  CG  . ASP B 1 32  ? 16.359  -31.242 -44.750 1.00 10.57  ? 32  ASP B CG  1 
ATOM   2499 O  OD1 . ASP B 1 32  ? 17.056  -31.673 -43.818 1.00 9.97   ? 32  ASP B OD1 1 
ATOM   2500 O  OD2 . ASP B 1 32  ? 16.399  -31.691 -45.938 1.00 13.38  ? 32  ASP B OD2 1 
ATOM   2501 N  N   A ILE B 1 33  ? 18.451  -28.669 -44.544 0.50 8.60   ? 33  ILE B N   1 
ATOM   2502 N  N   B ILE B 1 33  ? 18.488  -28.660 -44.552 0.50 8.85   ? 33  ILE B N   1 
ATOM   2503 C  CA  A ILE B 1 33  ? 19.554  -28.299 -45.432 0.50 9.01   ? 33  ILE B CA  1 
ATOM   2504 C  CA  B ILE B 1 33  ? 19.639  -28.304 -45.438 0.50 9.19   ? 33  ILE B CA  1 
ATOM   2505 C  C   A ILE B 1 33  ? 19.825  -29.537 -46.289 0.50 9.72   ? 33  ILE B C   1 
ATOM   2506 C  C   B ILE B 1 33  ? 19.923  -29.540 -46.297 0.50 10.02  ? 33  ILE B C   1 
ATOM   2507 O  O   A ILE B 1 33  ? 20.353  -30.539 -45.811 0.50 10.15  ? 33  ILE B O   1 
ATOM   2508 O  O   B ILE B 1 33  ? 20.462  -30.536 -45.813 0.50 10.63  ? 33  ILE B O   1 
ATOM   2509 C  CB  A ILE B 1 33  ? 20.749  -27.897 -44.614 0.50 8.83   ? 33  ILE B CB  1 
ATOM   2510 C  CB  B ILE B 1 33  ? 20.851  -27.910 -44.617 0.50 9.73   ? 33  ILE B CB  1 
ATOM   2511 C  CG1 A ILE B 1 33  ? 20.406  -26.633 -43.787 0.50 8.12   ? 33  ILE B CG1 1 
ATOM   2512 C  CG1 B ILE B 1 33  ? 20.467  -26.734 -43.714 0.50 11.11  ? 33  ILE B CG1 1 
ATOM   2513 C  CG2 A ILE B 1 33  ? 21.965  -27.642 -45.540 0.50 10.26  ? 33  ILE B CG2 1 
ATOM   2514 C  CG2 B ILE B 1 33  ? 22.039  -27.557 -45.548 0.50 10.91  ? 33  ILE B CG2 1 
ATOM   2515 C  CD1 A ILE B 1 33  ? 21.447  -26.380 -42.640 0.50 7.29   ? 33  ILE B CD1 1 
ATOM   2516 C  CD1 B ILE B 1 33  ? 20.349  -25.481 -44.450 0.50 16.98  ? 33  ILE B CD1 1 
ATOM   2517 N  N   A ASP B 1 34  ? 19.439  -29.488 -47.555 0.50 10.75  ? 34  ASP B N   1 
ATOM   2518 N  N   B ASP B 1 34  ? 19.529  -29.495 -47.564 0.50 11.10  ? 34  ASP B N   1 
ATOM   2519 C  CA  A ASP B 1 34  ? 19.762  -30.541 -48.492 0.50 11.68  ? 34  ASP B CA  1 
ATOM   2520 C  CA  B ASP B 1 34  ? 19.814  -30.548 -48.529 0.50 11.85  ? 34  ASP B CA  1 
ATOM   2521 C  C   A ASP B 1 34  ? 21.217  -30.288 -49.008 0.50 12.21  ? 34  ASP B C   1 
ATOM   2522 C  C   B ASP B 1 34  ? 21.255  -30.281 -49.026 0.50 12.65  ? 34  ASP B C   1 
ATOM   2523 O  O   A ASP B 1 34  ? 21.454  -29.339 -49.774 0.50 15.73  ? 34  ASP B O   1 
ATOM   2524 O  O   B ASP B 1 34  ? 21.528  -29.328 -49.775 0.50 16.09  ? 34  ASP B O   1 
ATOM   2525 C  CB  A ASP B 1 34  ? 18.723  -30.570 -49.610 0.50 13.30  ? 34  ASP B CB  1 
ATOM   2526 C  CB  B ASP B 1 34  ? 18.761  -30.531 -49.651 0.50 14.22  ? 34  ASP B CB  1 
ATOM   2527 C  CG  A ASP B 1 34  ? 18.917  -31.782 -50.481 0.50 19.83  ? 34  ASP B CG  1 
ATOM   2528 C  CG  B ASP B 1 34  ? 19.063  -31.551 -50.751 0.50 22.13  ? 34  ASP B CG  1 
ATOM   2529 O  OD1 A ASP B 1 34  ? 19.883  -31.844 -51.253 0.50 22.53  ? 34  ASP B OD1 1 
ATOM   2530 O  OD1 B ASP B 1 34  ? 20.177  -32.149 -50.753 0.50 28.60  ? 34  ASP B OD1 1 
ATOM   2531 O  OD2 A ASP B 1 34  ? 18.181  -32.742 -50.298 0.50 29.62  ? 34  ASP B OD2 1 
ATOM   2532 O  OD2 B ASP B 1 34  ? 18.164  -31.752 -51.596 0.50 26.55  ? 34  ASP B OD2 1 
ATOM   2533 N  N   . THR B 1 35  ? 22.195  -31.061 -48.538 1.00 14.25  ? 35  THR B N   1 
ATOM   2534 C  CA  . THR B 1 35  ? 23.618  -30.735 -48.786 1.00 14.79  ? 35  THR B CA  1 
ATOM   2535 C  C   . THR B 1 35  ? 23.991  -30.886 -50.216 1.00 13.93  ? 35  THR B C   1 
ATOM   2536 O  O   . THR B 1 35  ? 24.925  -30.197 -50.692 1.00 17.89  ? 35  THR B O   1 
ATOM   2537 C  CB  . THR B 1 35  ? 24.477  -31.625 -47.946 1.00 15.43  ? 35  THR B CB  1 
ATOM   2538 O  OG1 . THR B 1 35  ? 24.362  -32.971 -48.427 1.00 17.28  ? 35  THR B OG1 1 
ATOM   2539 C  CG2 . THR B 1 35  ? 24.141  -31.504 -46.487 1.00 17.58  ? 35  THR B CG2 1 
ATOM   2540 N  N   A HIS B 1 36  ? 23.248  -31.719 -50.949 0.50 16.88  ? 36  HIS B N   1 
ATOM   2541 N  N   B HIS B 1 36  ? 23.296  -31.742 -50.959 0.50 16.87  ? 36  HIS B N   1 
ATOM   2542 C  CA  A HIS B 1 36  ? 23.506  -31.929 -52.367 0.50 18.70  ? 36  HIS B CA  1 
ATOM   2543 C  CA  B HIS B 1 36  ? 23.559  -31.894 -52.386 0.50 18.83  ? 36  HIS B CA  1 
ATOM   2544 C  C   A HIS B 1 36  ? 23.018  -30.825 -53.259 0.50 20.01  ? 36  HIS B C   1 
ATOM   2545 C  C   B HIS B 1 36  ? 23.073  -30.770 -53.234 0.50 19.52  ? 36  HIS B C   1 
ATOM   2546 O  O   A HIS B 1 36  ? 23.657  -30.564 -54.292 0.50 23.56  ? 36  HIS B O   1 
ATOM   2547 O  O   B HIS B 1 36  ? 23.744  -30.470 -54.240 0.50 21.92  ? 36  HIS B O   1 
ATOM   2548 C  CB  A HIS B 1 36  ? 23.054  -33.357 -52.753 0.50 20.31  ? 36  HIS B CB  1 
ATOM   2549 C  CB  B HIS B 1 36  ? 22.993  -33.233 -52.840 0.50 21.16  ? 36  HIS B CB  1 
ATOM   2550 C  CG  A HIS B 1 36  ? 24.073  -34.414 -52.353 0.50 18.66  ? 36  HIS B CG  1 
ATOM   2551 C  CG  B HIS B 1 36  ? 23.475  -34.378 -52.009 0.50 25.71  ? 36  HIS B CG  1 
ATOM   2552 N  ND1 A HIS B 1 36  ? 23.858  -35.336 -51.370 0.50 23.00  ? 36  HIS B ND1 1 
ATOM   2553 N  ND1 B HIS B 1 36  ? 24.743  -34.824 -52.073 0.50 34.05  ? 36  HIS B ND1 1 
ATOM   2554 C  CD2 A HIS B 1 36  ? 25.424  -34.559 -52.734 0.50 21.10  ? 36  HIS B CD2 1 
ATOM   2555 C  CD2 B HIS B 1 36  ? 22.833  -35.141 -51.034 0.50 28.92  ? 36  HIS B CD2 1 
ATOM   2556 C  CE1 A HIS B 1 36  ? 24.981  -36.059 -51.186 0.50 23.58  ? 36  HIS B CE1 1 
ATOM   2557 C  CE1 B HIS B 1 36  ? 24.904  -35.823 -51.188 0.50 32.01  ? 36  HIS B CE1 1 
ATOM   2558 N  NE2 A HIS B 1 36  ? 25.938  -35.588 -52.025 0.50 23.93  ? 36  HIS B NE2 1 
ATOM   2559 N  NE2 B HIS B 1 36  ? 23.731  -36.025 -50.570 0.50 30.12  ? 36  HIS B NE2 1 
ATOM   2560 N  N   . THR B 1 37  ? 21.973  -30.094 -52.834 1.00 19.42  ? 37  THR B N   1 
ATOM   2561 C  CA  . THR B 1 37  ? 21.447  -28.954 -53.590 1.00 19.16  ? 37  THR B CA  1 
ATOM   2562 C  C   . THR B 1 37  ? 21.969  -27.585 -53.104 1.00 17.07  ? 37  THR B C   1 
ATOM   2563 O  O   . THR B 1 37  ? 21.865  -26.615 -53.858 1.00 22.01  ? 37  THR B O   1 
ATOM   2564 C  CB  . THR B 1 37  ? 19.921  -28.885 -53.758 1.00 27.33  ? 37  THR B CB  1 
ATOM   2565 O  OG1 . THR B 1 37  ? 19.278  -28.895 -52.529 1.00 36.49  ? 37  THR B OG1 1 
ATOM   2566 C  CG2 . THR B 1 37  ? 19.419  -30.083 -54.287 1.00 27.96  ? 37  THR B CG2 1 
ATOM   2567 N  N   . ALA B 1 38  ? 22.564  -27.533 -51.927 1.00 16.24  ? 38  ALA B N   1 
ATOM   2568 C  CA  . ALA B 1 38  ? 23.224  -26.270 -51.514 1.00 15.65  ? 38  ALA B CA  1 
ATOM   2569 C  C   . ALA B 1 38  ? 24.357  -25.920 -52.442 1.00 17.07  ? 38  ALA B C   1 
ATOM   2570 O  O   . ALA B 1 38  ? 25.071  -26.759 -52.882 1.00 24.68  ? 38  ALA B O   1 
ATOM   2571 C  CB  . ALA B 1 38  ? 23.750  -26.402 -50.092 1.00 15.35  ? 38  ALA B CB  1 
ATOM   2572 N  N   . LYS B 1 39  ? 24.372  -24.700 -52.892 1.00 16.23  ? 39  LYS B N   1 
ATOM   2573 C  CA  . LYS B 1 39  ? 25.325  -24.231 -53.861 1.00 21.01  ? 39  LYS B CA  1 
ATOM   2574 C  C   . LYS B 1 39  ? 26.609  -23.721 -53.208 1.00 14.38  ? 39  LYS B C   1 
ATOM   2575 O  O   . LYS B 1 39  ? 26.527  -22.760 -52.458 1.00 14.27  ? 39  LYS B O   1 
ATOM   2576 C  CB  . LYS B 1 39  ? 24.587  -23.064 -54.586 1.00 25.13  ? 39  LYS B CB  1 
ATOM   2577 C  CG  . LYS B 1 39  ? 25.262  -22.204 -55.611 1.00 24.43  ? 39  LYS B CG  1 
ATOM   2578 C  CD  . LYS B 1 39  ? 25.557  -22.984 -56.878 1.00 29.62  ? 39  LYS B CD  1 
ATOM   2579 C  CE  . LYS B 1 39  ? 26.254  -22.057 -57.829 1.00 26.56  ? 39  LYS B CE  1 
ATOM   2580 N  NZ  . LYS B 1 39  ? 26.636  -22.815 -59.019 1.00 35.37  ? 39  LYS B NZ  1 
ATOM   2581 N  N   . TYR B 1 40  ? 27.764  -24.239 -53.606 1.00 18.39  ? 40  TYR B N   1 
ATOM   2582 C  CA  . TYR B 1 40  ? 29.026  -23.632 -53.190 1.00 16.35  ? 40  TYR B CA  1 
ATOM   2583 C  C   . TYR B 1 40  ? 29.094  -22.255 -53.811 1.00 14.34  ? 40  TYR B C   1 
ATOM   2584 O  O   . TYR B 1 40  ? 28.933  -22.067 -55.037 1.00 16.67  ? 40  TYR B O   1 
ATOM   2585 C  CB  . TYR B 1 40  ? 30.256  -24.451 -53.592 1.00 19.78  ? 40  TYR B CB  1 
ATOM   2586 C  CG  . TYR B 1 40  ? 31.565  -23.700 -53.431 1.00 22.82  ? 40  TYR B CG  1 
ATOM   2587 C  CD1 . TYR B 1 40  ? 31.982  -23.205 -52.167 1.00 20.18  ? 40  TYR B CD1 1 
ATOM   2588 C  CD2 . TYR B 1 40  ? 32.406  -23.480 -54.528 1.00 23.90  ? 40  TYR B CD2 1 
ATOM   2589 C  CE1 . TYR B 1 40  ? 33.185  -22.538 -52.010 1.00 25.13  ? 40  TYR B CE1 1 
ATOM   2590 C  CE2 . TYR B 1 40  ? 33.632  -22.832 -54.343 1.00 26.81  ? 40  TYR B CE2 1 
ATOM   2591 C  CZ  . TYR B 1 40  ? 33.987  -22.343 -53.119 1.00 27.36  ? 40  TYR B CZ  1 
ATOM   2592 O  OH  . TYR B 1 40  ? 35.180  -21.673 -53.004 1.00 35.73  ? 40  TYR B OH  1 
ATOM   2593 N  N   . ASP B 1 41  ? 29.316  -21.257 -52.976 1.00 13.94  ? 41  ASP B N   1 
ATOM   2594 C  CA  . ASP B 1 41  ? 29.427  -19.836 -53.457 1.00 14.34  ? 41  ASP B CA  1 
ATOM   2595 C  C   . ASP B 1 41  ? 30.826  -19.359 -53.178 1.00 15.73  ? 41  ASP B C   1 
ATOM   2596 O  O   . ASP B 1 41  ? 31.176  -19.028 -52.002 1.00 15.34  ? 41  ASP B O   1 
ATOM   2597 C  CB  . ASP B 1 41  ? 28.382  -18.970 -52.748 1.00 16.29  ? 41  ASP B CB  1 
ATOM   2598 C  CG  . ASP B 1 41  ? 28.353  -17.592 -53.226 1.00 18.62  ? 41  ASP B CG  1 
ATOM   2599 O  OD1 . ASP B 1 41  ? 29.310  -17.198 -53.999 1.00 20.21  ? 41  ASP B OD1 1 
ATOM   2600 O  OD2 . ASP B 1 41  ? 27.401  -16.838 -52.872 1.00 21.92  ? 41  ASP B OD2 1 
ATOM   2601 N  N   . PRO B 1 42  ? 31.674  -19.314 -54.207 1.00 18.86  ? 42  PRO B N   1 
ATOM   2602 C  CA  . PRO B 1 42  ? 33.026  -18.848 -53.971 1.00 22.72  ? 42  PRO B CA  1 
ATOM   2603 C  C   . PRO B 1 42  ? 33.146  -17.351 -53.562 1.00 23.52  ? 42  PRO B C   1 
ATOM   2604 O  O   . PRO B 1 42  ? 34.219  -16.889 -53.135 1.00 29.69  ? 42  PRO B O   1 
ATOM   2605 C  CB  . PRO B 1 42  ? 33.704  -19.069 -55.326 1.00 27.76  ? 42  PRO B CB  1 
ATOM   2606 C  CG  . PRO B 1 42  ? 32.590  -19.003 -56.349 1.00 27.78  ? 42  PRO B CG  1 
ATOM   2607 C  CD  . PRO B 1 42  ? 31.449  -19.705 -55.626 1.00 23.79  ? 42  PRO B CD  1 
ATOM   2608 N  N   . SER B 1 43  ? 32.065  -16.584 -53.720 1.00 19.90  ? 43  SER B N   1 
ATOM   2609 C  CA  . SER B 1 43  ? 32.027  -15.164 -53.282 1.00 22.52  ? 43  SER B CA  1 
ATOM   2610 C  C   . SER B 1 43  ? 31.785  -14.995 -51.766 1.00 20.79  ? 43  SER B C   1 
ATOM   2611 O  O   . SER B 1 43  ? 31.931  -13.899 -51.202 1.00 27.77  ? 43  SER B O   1 
ATOM   2612 C  CB  . SER B 1 43  ? 30.940  -14.395 -54.057 1.00 24.02  ? 43  SER B CB  1 
ATOM   2613 O  OG  . SER B 1 43  ? 29.641  -14.630 -53.591 1.00 24.93  ? 43  SER B OG  1 
ATOM   2614 N  N   . LEU B 1 44  ? 31.389  -16.081 -51.100 1.00 21.61  ? 44  LEU B N   1 
ATOM   2615 C  CA  . LEU B 1 44  ? 31.218  -16.067 -49.611 1.00 20.14  ? 44  LEU B CA  1 
ATOM   2616 C  C   . LEU B 1 44  ? 32.574  -15.934 -48.934 1.00 19.29  ? 44  LEU B C   1 
ATOM   2617 O  O   . LEU B 1 44  ? 33.578  -16.403 -49.419 1.00 26.57  ? 44  LEU B O   1 
ATOM   2618 C  CB  . LEU B 1 44  ? 30.506  -17.307 -49.131 1.00 17.33  ? 44  LEU B CB  1 
ATOM   2619 C  CG  . LEU B 1 44  ? 29.019  -17.326 -49.369 1.00 14.36  ? 44  LEU B CG  1 
ATOM   2620 C  CD1 . LEU B 1 44  ? 28.569  -18.725 -48.952 1.00 18.39  ? 44  LEU B CD1 1 
ATOM   2621 C  CD2 . LEU B 1 44  ? 28.302  -16.259 -48.607 1.00 18.83  ? 44  LEU B CD2 1 
ATOM   2622 N  N   . LYS B 1 45  ? 32.621  -15.152 -47.864 1.00 19.05  ? 45  LYS B N   1 
ATOM   2623 C  CA  . LYS B 1 45  ? 33.926  -14.929 -47.167 1.00 18.15  ? 45  LYS B CA  1 
ATOM   2624 C  C   . LYS B 1 45  ? 34.000  -15.823 -45.951 1.00 16.44  ? 45  LYS B C   1 
ATOM   2625 O  O   . LYS B 1 45  ? 32.941  -16.316 -45.493 1.00 17.74  ? 45  LYS B O   1 
ATOM   2626 C  CB  . LYS B 1 45  ? 34.036  -13.513 -46.729 1.00 19.16  ? 45  LYS B CB  1 
ATOM   2627 C  CG  . LYS B 1 45  ? 33.797  -12.455 -47.780 1.00 25.56  ? 45  LYS B CG  1 
ATOM   2628 C  CD  . LYS B 1 45  ? 33.812  -11.059 -47.189 1.00 32.02  ? 45  LYS B CD  1 
ATOM   2629 C  CE  . LYS B 1 45  ? 35.196  -10.650 -46.703 1.00 48.35  ? 45  LYS B CE  1 
ATOM   2630 N  NZ  . LYS B 1 45  ? 35.312  -9.200  -46.376 1.00 56.19  ? 45  LYS B NZ  1 
ATOM   2631 N  N   . PRO B 1 46  ? 35.223  -16.011 -45.417 1.00 17.69  ? 46  PRO B N   1 
ATOM   2632 C  CA  . PRO B 1 46  ? 35.317  -16.707 -44.117 1.00 18.64  ? 46  PRO B CA  1 
ATOM   2633 C  C   . PRO B 1 46  ? 34.465  -15.950 -43.103 1.00 13.98  ? 46  PRO B C   1 
ATOM   2634 O  O   . PRO B 1 46  ? 34.390  -14.703 -43.185 1.00 15.04  ? 46  PRO B O   1 
ATOM   2635 C  CB  . PRO B 1 46  ? 36.819  -16.608 -43.794 1.00 19.19  ? 46  PRO B CB  1 
ATOM   2636 C  CG  . PRO B 1 46  ? 37.533  -16.359 -45.111 1.00 23.32  ? 46  PRO B CG  1 
ATOM   2637 C  CD  . PRO B 1 46  ? 36.529  -15.636 -45.958 1.00 19.91  ? 46  PRO B CD  1 
ATOM   2638 N  N   . LEU B 1 47  ? 33.937  -16.692 -42.146 1.00 15.37  ? 47  LEU B N   1 
ATOM   2639 C  CA  . LEU B 1 47  ? 33.131  -16.039 -41.110 1.00 13.91  ? 47  LEU B CA  1 
ATOM   2640 C  C   . LEU B 1 47  ? 34.143  -15.457 -40.142 1.00 16.79  ? 47  LEU B C   1 
ATOM   2641 O  O   . LEU B 1 47  ? 35.123  -16.140 -39.834 1.00 21.00  ? 47  LEU B O   1 
ATOM   2642 C  CB  . LEU B 1 47  ? 32.289  -17.127 -40.433 1.00 19.81  ? 47  LEU B CB  1 
ATOM   2643 C  CG  . LEU B 1 47  ? 31.260  -16.712 -39.467 1.00 18.54  ? 47  LEU B CG  1 
ATOM   2644 C  CD1 . LEU B 1 47  ? 30.222  -15.758 -40.165 1.00 20.67  ? 47  LEU B CD1 1 
ATOM   2645 C  CD2 . LEU B 1 47  ? 30.631  -17.952 -38.836 1.00 20.69  ? 47  LEU B CD2 1 
ATOM   2646 N  N   . SER B 1 48  ? 33.913  -14.238 -39.632 1.00 14.53  ? 48  SER B N   1 
ATOM   2647 C  CA  . SER B 1 48  ? 34.743  -13.633 -38.631 1.00 14.69  ? 48  SER B CA  1 
ATOM   2648 C  C   . SER B 1 48  ? 33.988  -13.589 -37.324 1.00 14.38  ? 48  SER B C   1 
ATOM   2649 O  O   . SER B 1 48  ? 32.974  -12.868 -37.206 1.00 13.80  ? 48  SER B O   1 
ATOM   2650 C  CB  . SER B 1 48  ? 35.089  -12.180 -39.088 1.00 16.85  ? 48  SER B CB  1 
ATOM   2651 O  OG  . SER B 1 48  ? 35.738  -11.461 -38.085 1.00 21.22  ? 48  SER B OG  1 
ATOM   2652 N  N   . VAL B 1 49  ? 34.432  -14.347 -36.361 1.00 15.00  ? 49  VAL B N   1 
ATOM   2653 C  CA  . VAL B 1 49  ? 33.821  -14.413 -35.073 1.00 16.66  ? 49  VAL B CA  1 
ATOM   2654 C  C   . VAL B 1 49  ? 34.825  -13.788 -34.077 1.00 19.16  ? 49  VAL B C   1 
ATOM   2655 O  O   . VAL B 1 49  ? 35.875  -14.373 -33.869 1.00 22.21  ? 49  VAL B O   1 
ATOM   2656 C  CB  . VAL B 1 49  ? 33.561  -15.893 -34.645 1.00 19.03  ? 49  VAL B CB  1 
ATOM   2657 C  CG1 . VAL B 1 49  ? 32.851  -15.906 -33.274 1.00 23.82  ? 49  VAL B CG1 1 
ATOM   2658 C  CG2 . VAL B 1 49  ? 32.770  -16.625 -35.732 1.00 21.53  ? 49  VAL B CG2 1 
ATOM   2659 N  N   . SER B 1 50  ? 34.506  -12.637 -33.466 1.00 17.16  ? 50  SER B N   1 
ATOM   2660 C  CA  . SER B 1 50  ? 35.441  -11.891 -32.588 1.00 19.94  ? 50  SER B CA  1 
ATOM   2661 C  C   . SER B 1 50  ? 34.842  -11.804 -31.241 1.00 20.34  ? 50  SER B C   1 
ATOM   2662 O  O   . SER B 1 50  ? 34.134  -10.859 -30.943 1.00 20.23  ? 50  SER B O   1 
ATOM   2663 C  CB  . SER B 1 50  ? 35.772  -10.510 -33.171 1.00 25.96  ? 50  SER B CB  1 
ATOM   2664 O  OG  . SER B 1 50  ? 36.454  -10.738 -34.403 1.00 27.77  ? 50  SER B OG  1 
ATOM   2665 N  N   . TYR B 1 51  ? 35.076  -12.819 -30.419 1.00 18.57  ? 51  TYR B N   1 
ATOM   2666 C  CA  . TYR B 1 51  ? 34.424  -12.909 -29.138 1.00 17.38  ? 51  TYR B CA  1 
ATOM   2667 C  C   . TYR B 1 51  ? 35.362  -12.656 -27.955 1.00 21.07  ? 51  TYR B C   1 
ATOM   2668 O  O   . TYR B 1 51  ? 34.960  -12.852 -26.800 1.00 20.97  ? 51  TYR B O   1 
ATOM   2669 C  CB  . TYR B 1 51  ? 33.787  -14.312 -28.965 1.00 15.28  ? 51  TYR B CB  1 
ATOM   2670 C  CG  . TYR B 1 51  ? 32.516  -14.610 -29.731 1.00 13.90  ? 51  TYR B CG  1 
ATOM   2671 C  CD1 . TYR B 1 51  ? 31.800  -13.610 -30.387 1.00 15.32  ? 51  TYR B CD1 1 
ATOM   2672 C  CD2 . TYR B 1 51  ? 32.009  -15.918 -29.807 1.00 13.67  ? 51  TYR B CD2 1 
ATOM   2673 C  CE1 . TYR B 1 51  ? 30.614  -13.924 -31.088 1.00 13.05  ? 51  TYR B CE1 1 
ATOM   2674 C  CE2 . TYR B 1 51  ? 30.837  -16.257 -30.479 1.00 12.44  ? 51  TYR B CE2 1 
ATOM   2675 C  CZ  . TYR B 1 51  ? 30.127  -15.240 -31.138 1.00 11.90  ? 51  TYR B CZ  1 
ATOM   2676 O  OH  . TYR B 1 51  ? 28.970  -15.576 -31.770 1.00 12.22  ? 51  TYR B OH  1 
ATOM   2677 N  N   . ASP B 1 52  ? 36.569  -12.175 -28.212 1.00 22.60  ? 52  ASP B N   1 
ATOM   2678 C  CA  . ASP B 1 52  ? 37.577  -12.050 -27.152 1.00 22.65  ? 52  ASP B CA  1 
ATOM   2679 C  C   . ASP B 1 52  ? 37.204  -11.030 -26.061 1.00 25.08  ? 52  ASP B C   1 
ATOM   2680 O  O   . ASP B 1 52  ? 37.640  -11.188 -24.911 1.00 29.35  ? 52  ASP B O   1 
ATOM   2681 C  CB  . ASP B 1 52  ? 38.944  -11.711 -27.711 1.00 25.58  ? 52  ASP B CB  1 
ATOM   2682 C  CG  . ASP B 1 52  ? 38.920  -10.561 -28.702 1.00 40.71  ? 52  ASP B CG  1 
ATOM   2683 O  OD1 . ASP B 1 52  ? 38.260  -10.682 -29.791 1.00 42.19  ? 52  ASP B OD1 1 
ATOM   2684 O  OD2 . ASP B 1 52  ? 39.591  -9.545  -28.385 1.00 71.22  ? 52  ASP B OD2 1 
ATOM   2685 N  N   . GLN B 1 53  ? 36.339  -10.083 -26.391 1.00 24.04  ? 53  GLN B N   1 
ATOM   2686 C  CA  . GLN B 1 53  ? 35.980  -9.109  -25.360 1.00 23.90  ? 53  GLN B CA  1 
ATOM   2687 C  C   . GLN B 1 53  ? 34.549  -9.349  -24.885 1.00 17.87  ? 53  GLN B C   1 
ATOM   2688 O  O   . GLN B 1 53  ? 33.955  -8.497  -24.257 1.00 20.12  ? 53  GLN B O   1 
ATOM   2689 C  CB  . GLN B 1 53  ? 36.196  -7.660  -25.870 1.00 30.26  ? 53  GLN B CB  1 
ATOM   2690 C  CG  . GLN B 1 53  ? 37.656  -7.301  -26.078 1.00 35.08  ? 53  GLN B CG  1 
ATOM   2691 C  CD  . GLN B 1 53  ? 38.478  -7.599  -24.856 1.00 34.74  ? 53  GLN B CD  1 
ATOM   2692 O  OE1 . GLN B 1 53  ? 37.979  -7.459  -23.721 1.00 53.54  ? 53  GLN B OE1 1 
ATOM   2693 N  NE2 . GLN B 1 53  ? 39.731  -7.987  -25.052 1.00 48.01  ? 53  GLN B NE2 1 
ATOM   2694 N  N   . ALA B 1 54  ? 33.975  -10.498 -25.213 1.00 17.54  ? 54  ALA B N   1 
ATOM   2695 C  CA  . ALA B 1 54  ? 32.576  -10.764 -24.816 1.00 16.80  ? 54  ALA B CA  1 
ATOM   2696 C  C   . ALA B 1 54  ? 32.352  -10.652 -23.286 1.00 19.85  ? 54  ALA B C   1 
ATOM   2697 O  O   . ALA B 1 54  ? 33.161  -11.120 -22.486 1.00 24.87  ? 54  ALA B O   1 
ATOM   2698 C  CB  . ALA B 1 54  ? 32.097  -12.140 -25.300 1.00 20.09  ? 54  ALA B CB  1 
ATOM   2699 N  N   . THR B 1 55  ? 31.268  -10.016 -22.876 1.00 15.40  ? 55  THR B N   1 
ATOM   2700 C  CA  . THR B 1 55  ? 30.945  -9.825  -21.471 1.00 17.30  ? 55  THR B CA  1 
ATOM   2701 C  C   . THR B 1 55  ? 29.585  -10.375 -21.147 1.00 14.05  ? 55  THR B C   1 
ATOM   2702 O  O   . THR B 1 55  ? 28.566  -9.745  -21.422 1.00 14.66  ? 55  THR B O   1 
ATOM   2703 C  CB  . THR B 1 55  ? 30.941  -8.316  -21.054 1.00 23.07  ? 55  THR B CB  1 
ATOM   2704 O  OG1 . THR B 1 55  ? 32.201  -7.679  -21.274 1.00 28.48  ? 55  THR B OG1 1 
ATOM   2705 C  CG2 . THR B 1 55  ? 30.539  -8.261  -19.538 1.00 25.36  ? 55  THR B CG2 1 
ATOM   2706 N  N   . SER B 1 56  ? 29.560  -11.604 -20.679 1.00 16.39  ? 56  SER B N   1 
ATOM   2707 C  CA  . SER B 1 56  ? 28.306  -12.182 -20.290 1.00 15.59  ? 56  SER B CA  1 
ATOM   2708 C  C   . SER B 1 56  ? 27.894  -11.512 -19.004 1.00 17.63  ? 56  SER B C   1 
ATOM   2709 O  O   . SER B 1 56  ? 28.674  -11.034 -18.200 1.00 20.31  ? 56  SER B O   1 
ATOM   2710 C  CB  . SER B 1 56  ? 28.335  -13.715 -20.120 1.00 18.15  ? 56  SER B CB  1 
ATOM   2711 O  OG  . SER B 1 56  ? 29.181  -14.041 -18.979 1.00 19.11  ? 56  SER B OG  1 
ATOM   2712 N  N   . LEU B 1 57  ? 26.624  -11.474 -18.803 1.00 14.43  ? 57  LEU B N   1 
ATOM   2713 C  CA  . LEU B 1 57  ? 26.076  -10.866 -17.614 1.00 18.16  ? 57  LEU B CA  1 
ATOM   2714 C  C   . LEU B 1 57  ? 25.193  -11.799 -16.775 1.00 17.51  ? 57  LEU B C   1 
ATOM   2715 O  O   . LEU B 1 57  ? 25.216  -11.751 -15.541 1.00 17.84  ? 57  LEU B O   1 
ATOM   2716 C  CB  . LEU B 1 57  ? 25.222  -9.714  -18.035 1.00 20.74  ? 57  LEU B CB  1 
ATOM   2717 C  CG  . LEU B 1 57  ? 26.004  -8.502  -18.619 1.00 24.22  ? 57  LEU B CG  1 
ATOM   2718 C  CD1 . LEU B 1 57  ? 24.976  -7.498  -19.088 1.00 27.83  ? 57  LEU B CD1 1 
ATOM   2719 C  CD2 . LEU B 1 57  ? 27.143  -7.887  -17.762 1.00 31.79  ? 57  LEU B CD2 1 
ATOM   2720 N  N   A ARG B 1 58  ? 24.383  -12.567 -17.454 0.50 17.89  ? 58  ARG B N   1 
ATOM   2721 N  N   B ARG B 1 58  ? 24.209  -12.431 -17.404 0.50 18.61  ? 58  ARG B N   1 
ATOM   2722 C  CA  A ARG B 1 58  ? 23.383  -13.278 -16.720 0.50 15.35  ? 58  ARG B CA  1 
ATOM   2723 C  CA  B ARG B 1 58  ? 23.140  -13.148 -16.631 0.50 16.08  ? 58  ARG B CA  1 
ATOM   2724 C  C   A ARG B 1 58  ? 22.829  -14.422 -17.502 0.50 14.21  ? 58  ARG B C   1 
ATOM   2725 C  C   B ARG B 1 58  ? 22.797  -14.385 -17.453 0.50 14.52  ? 58  ARG B C   1 
ATOM   2726 O  O   A ARG B 1 58  ? 22.829  -14.418 -18.722 0.50 17.02  ? 58  ARG B O   1 
ATOM   2727 O  O   B ARG B 1 58  ? 22.890  -14.400 -18.664 0.50 17.08  ? 58  ARG B O   1 
ATOM   2728 C  CB  A ARG B 1 58  ? 22.291  -12.232 -16.494 0.50 14.50  ? 58  ARG B CB  1 
ATOM   2729 C  CB  B ARG B 1 58  ? 21.769  -12.310 -16.328 0.50 17.75  ? 58  ARG B CB  1 
ATOM   2730 C  CG  A ARG B 1 58  ? 21.190  -12.638 -15.626 0.50 14.68  ? 58  ARG B CG  1 
ATOM   2731 C  CG  B ARG B 1 58  ? 21.655  -11.024 -15.392 0.50 19.11  ? 58  ARG B CG  1 
ATOM   2732 C  CD  A ARG B 1 58  ? 20.151  -11.608 -15.353 0.50 15.21  ? 58  ARG B CD  1 
ATOM   2733 C  CD  B ARG B 1 58  ? 20.431  -10.704 -14.536 0.50 22.42  ? 58  ARG B CD  1 
ATOM   2734 N  NE  A ARG B 1 58  ? 19.270  -11.603 -16.497 0.50 11.34  ? 58  ARG B NE  1 
ATOM   2735 N  NE  B ARG B 1 58  ? 20.894  -10.560 -13.155 0.50 31.12  ? 58  ARG B NE  1 
ATOM   2736 C  CZ  A ARG B 1 58  ? 17.966  -11.386 -16.464 0.50 13.12  ? 58  ARG B CZ  1 
ATOM   2737 C  CZ  B ARG B 1 58  ? 20.373  -11.197 -12.116 0.50 23.32  ? 58  ARG B CZ  1 
ATOM   2738 N  NH1 A ARG B 1 58  ? 17.331  -11.126 -15.326 0.50 14.27  ? 58  ARG B NH1 1 
ATOM   2739 N  NH1 B ARG B 1 58  ? 19.327  -11.993 -12.294 0.50 20.79  ? 58  ARG B NH1 1 
ATOM   2740 N  NH2 A ARG B 1 58  ? 17.302  -11.441 -17.601 0.50 10.77  ? 58  ARG B NH2 1 
ATOM   2741 N  NH2 B ARG B 1 58  ? 20.866  -10.997 -10.892 0.50 35.02  ? 58  ARG B NH2 1 
ATOM   2742 N  N   . ILE B 1 59  ? 22.253  -15.389 -16.785 1.00 14.06  ? 59  ILE B N   1 
ATOM   2743 C  CA  . ILE B 1 59  ? 21.652  -16.492 -17.423 1.00 12.63  ? 59  ILE B CA  1 
ATOM   2744 C  C   . ILE B 1 59  ? 20.174  -16.519 -16.928 1.00 12.21  ? 59  ILE B C   1 
ATOM   2745 O  O   . ILE B 1 59  ? 19.835  -16.290 -15.700 1.00 16.97  ? 59  ILE B O   1 
ATOM   2746 C  CB  . ILE B 1 59  ? 22.265  -17.802 -17.163 1.00 14.05  ? 59  ILE B CB  1 
ATOM   2747 C  CG1 . ILE B 1 59  ? 21.643  -18.916 -18.020 1.00 13.18  ? 59  ILE B CG1 1 
ATOM   2748 C  CG2 . ILE B 1 59  ? 22.155  -18.211 -15.654 1.00 15.73  ? 59  ILE B CG2 1 
ATOM   2749 C  CD1 . ILE B 1 59  ? 22.419  -20.197 -17.950 1.00 14.94  ? 59  ILE B CD1 1 
ATOM   2750 N  N   . LEU B 1 60  ? 19.240  -16.733 -17.810 1.00 13.31  ? 60  LEU B N   1 
ATOM   2751 C  CA  . LEU B 1 60  ? 17.851  -16.668 -17.569 1.00 12.83  ? 60  LEU B CA  1 
ATOM   2752 C  C   . LEU B 1 60  ? 16.951  -17.832 -18.089 1.00 12.59  ? 60  LEU B C   1 
ATOM   2753 O  O   . LEU B 1 60  ? 17.136  -18.184 -19.250 1.00 12.41  ? 60  LEU B O   1 
ATOM   2754 C  CB  . LEU B 1 60  ? 17.293  -15.324 -18.160 1.00 14.24  ? 60  LEU B CB  1 
ATOM   2755 C  CG  . LEU B 1 60  ? 15.766  -15.231 -18.203 1.00 14.24  ? 60  LEU B CG  1 
ATOM   2756 C  CD1 . LEU B 1 60  ? 15.196  -14.914 -16.790 1.00 16.10  ? 60  LEU B CD1 1 
ATOM   2757 C  CD2 . LEU B 1 60  ? 15.192  -14.117 -19.182 1.00 17.85  ? 60  LEU B CD2 1 
ATOM   2758 N  N   . ASN B 1 61  ? 16.064  -18.436 -17.274 1.00 14.56  ? 61  ASN B N   1 
ATOM   2759 C  CA  . ASN B 1 61  ? 15.051  -19.398 -17.735 1.00 15.39  ? 61  ASN B CA  1 
ATOM   2760 C  C   . ASN B 1 61  ? 13.789  -18.615 -18.128 1.00 14.45  ? 61  ASN B C   1 
ATOM   2761 O  O   . ASN B 1 61  ? 13.092  -18.072 -17.276 1.00 16.91  ? 61  ASN B O   1 
ATOM   2762 C  CB  . ASN B 1 61  ? 14.757  -20.442 -16.647 1.00 16.08  ? 61  ASN B CB  1 
ATOM   2763 C  CG  . ASN B 1 61  ? 13.710  -21.468 -17.054 1.00 14.35  ? 61  ASN B CG  1 
ATOM   2764 O  OD1 . ASN B 1 61  ? 12.819  -21.214 -17.917 1.00 15.20  ? 61  ASN B OD1 1 
ATOM   2765 N  ND2 . ASN B 1 61  ? 13.760  -22.663 -16.455 1.00 15.43  ? 61  ASN B ND2 1 
ATOM   2766 N  N   . ASN B 1 62  ? 13.536  -18.526 -19.424 1.00 15.66  ? 62  ASN B N   1 
ATOM   2767 C  CA  . ASN B 1 62  ? 12.504  -17.674 -19.915 1.00 16.04  ? 62  ASN B CA  1 
ATOM   2768 C  C   . ASN B 1 62  ? 11.196  -18.487 -20.117 1.00 16.45  ? 62  ASN B C   1 
ATOM   2769 O  O   . ASN B 1 62  ? 10.120  -18.048 -20.701 1.00 21.25  ? 62  ASN B O   1 
ATOM   2770 C  CB  . ASN B 1 62  ? 12.825  -16.874 -21.210 1.00 20.46  ? 62  ASN B CB  1 
ATOM   2771 C  CG  . ASN B 1 62  ? 12.958  -17.806 -22.383 1.00 16.13  ? 62  ASN B CG  1 
ATOM   2772 O  OD1 . ASN B 1 62  ? 12.693  -19.004 -22.336 1.00 15.63  ? 62  ASN B OD1 1 
ATOM   2773 N  ND2 . ASN B 1 62  ? 13.159  -17.220 -23.502 1.00 22.49  ? 62  ASN B ND2 1 
ATOM   2774 N  N   . GLY B 1 63  ? 11.181  -19.748 -19.628 1.00 16.07  ? 63  GLY B N   1 
ATOM   2775 C  CA  . GLY B 1 63  ? 10.013  -20.567 -19.844 1.00 16.12  ? 63  GLY B CA  1 
ATOM   2776 C  C   . GLY B 1 63  ? 9.911   -21.389 -21.146 1.00 16.11  ? 63  GLY B C   1 
ATOM   2777 O  O   . GLY B 1 63  ? 9.060   -22.249 -21.348 1.00 18.31  ? 63  GLY B O   1 
ATOM   2778 N  N   . HIS B 1 64  ? 10.828  -21.114 -22.018 1.00 14.12  ? 64  HIS B N   1 
ATOM   2779 C  CA  . HIS B 1 64  ? 11.004  -21.817 -23.365 1.00 14.98  ? 64  HIS B CA  1 
ATOM   2780 C  C   . HIS B 1 64  ? 12.345  -22.437 -23.504 1.00 13.47  ? 64  HIS B C   1 
ATOM   2781 O  O   . HIS B 1 64  ? 12.443  -23.559 -24.076 1.00 21.24  ? 64  HIS B O   1 
ATOM   2782 C  CB  . HIS B 1 64  ? 10.747  -20.785 -24.514 1.00 15.12  ? 64  HIS B CB  1 
ATOM   2783 C  CG  . HIS B 1 64  ? 9.481   -20.026 -24.366 1.00 16.71  ? 64  HIS B CG  1 
ATOM   2784 N  ND1 . HIS B 1 64  ? 8.250   -20.642 -24.383 1.00 18.75  ? 64  HIS B ND1 1 
ATOM   2785 C  CD2 . HIS B 1 64  ? 9.260   -18.683 -24.152 1.00 18.42  ? 64  HIS B CD2 1 
ATOM   2786 C  CE1 . HIS B 1 64  ? 7.270   -19.715 -24.304 1.00 20.47  ? 64  HIS B CE1 1 
ATOM   2787 N  NE2 . HIS B 1 64  ? 7.881   -18.495 -24.090 1.00 23.12  ? 64  HIS B NE2 1 
ATOM   2788 N  N   . ALA B 1 65  ? 13.363  -21.768 -23.030 1.00 12.25  ? 65  ALA B N   1 
ATOM   2789 C  CA  . ALA B 1 65  ? 14.753  -22.205 -23.057 1.00 11.23  ? 65  ALA B CA  1 
ATOM   2790 C  C   . ALA B 1 65  ? 15.429  -21.447 -21.917 1.00 11.52  ? 65  ALA B C   1 
ATOM   2791 O  O   . ALA B 1 65  ? 14.799  -20.819 -21.098 1.00 13.60  ? 65  ALA B O   1 
ATOM   2792 C  CB  . ALA B 1 65  ? 15.398  -22.018 -24.423 1.00 13.69  ? 65  ALA B CB  1 
ATOM   2793 N  N   . PHE B 1 66  ? 16.746  -21.493 -21.919 1.00 11.64  ? 66  PHE B N   1 
ATOM   2794 C  CA  . PHE B 1 66  ? 17.555  -20.528 -21.103 1.00 12.38  ? 66  PHE B CA  1 
ATOM   2795 C  C   . PHE B 1 66  ? 18.384  -19.671 -22.009 1.00 10.66  ? 66  PHE B C   1 
ATOM   2796 O  O   . PHE B 1 66  ? 19.009  -20.147 -22.967 1.00 12.54  ? 66  PHE B O   1 
ATOM   2797 C  CB  . PHE B 1 66  ? 18.394  -21.249 -20.008 1.00 13.87  ? 66  PHE B CB  1 
ATOM   2798 C  CG  . PHE B 1 66  ? 19.453  -22.153 -20.525 1.00 12.54  ? 66  PHE B CG  1 
ATOM   2799 C  CD1 . PHE B 1 66  ? 20.731  -21.664 -20.867 1.00 13.53  ? 66  PHE B CD1 1 
ATOM   2800 C  CD2 . PHE B 1 66  ? 19.208  -23.509 -20.684 1.00 13.45  ? 66  PHE B CD2 1 
ATOM   2801 C  CE1 . PHE B 1 66  ? 21.673  -22.520 -21.423 1.00 12.83  ? 66  PHE B CE1 1 
ATOM   2802 C  CE2 . PHE B 1 66  ? 20.191  -24.404 -21.194 1.00 12.80  ? 66  PHE B CE2 1 
ATOM   2803 C  CZ  . PHE B 1 66  ? 21.424  -23.897 -21.555 1.00 12.75  ? 66  PHE B CZ  1 
ATOM   2804 N  N   . ASN B 1 67  ? 18.457  -18.398 -21.646 1.00 11.75  ? 67  ASN B N   1 
ATOM   2805 C  CA  . ASN B 1 67  ? 19.330  -17.432 -22.416 1.00 11.94  ? 67  ASN B CA  1 
ATOM   2806 C  C   . ASN B 1 67  ? 20.612  -17.033 -21.639 1.00 11.60  ? 67  ASN B C   1 
ATOM   2807 O  O   . ASN B 1 67  ? 20.436  -16.590 -20.458 1.00 14.13  ? 67  ASN B O   1 
ATOM   2808 C  CB  . ASN B 1 67  ? 18.579  -16.172 -22.774 1.00 13.39  ? 67  ASN B CB  1 
ATOM   2809 C  CG  . ASN B 1 67  ? 17.464  -16.402 -23.701 1.00 15.94  ? 67  ASN B CG  1 
ATOM   2810 O  OD1 . ASN B 1 67  ? 17.312  -17.455 -24.385 1.00 16.69  ? 67  ASN B OD1 1 
ATOM   2811 N  ND2 . ASN B 1 67  ? 16.681  -15.335 -23.816 1.00 19.48  ? 67  ASN B ND2 1 
ATOM   2812 N  N   . VAL B 1 68  ? 21.812  -17.065 -22.203 1.00 12.16  ? 68  VAL B N   1 
ATOM   2813 C  CA  . VAL B 1 68  ? 23.010  -16.487 -21.617 1.00 13.32  ? 68  VAL B CA  1 
ATOM   2814 C  C   . VAL B 1 68  ? 23.085  -15.093 -22.298 1.00 14.14  ? 68  VAL B C   1 
ATOM   2815 O  O   . VAL B 1 68  ? 23.136  -15.002 -23.531 1.00 13.36  ? 68  VAL B O   1 
ATOM   2816 C  CB  . VAL B 1 68  ? 24.241  -17.344 -21.810 1.00 14.15  ? 68  VAL B CB  1 
ATOM   2817 C  CG1 . VAL B 1 68  ? 25.489  -16.543 -21.362 1.00 16.24  ? 68  VAL B CG1 1 
ATOM   2818 C  CG2 . VAL B 1 68  ? 24.033  -18.656 -21.059 1.00 15.31  ? 68  VAL B CG2 1 
ATOM   2819 N  N   . GLU B 1 69  ? 23.051  -14.034 -21.509 1.00 15.83  ? 69  GLU B N   1 
ATOM   2820 C  CA  . GLU B 1 69  ? 22.980  -12.652 -21.992 1.00 13.43  ? 69  GLU B CA  1 
ATOM   2821 C  C   . GLU B 1 69  ? 24.295  -11.956 -21.950 1.00 16.46  ? 69  GLU B C   1 
ATOM   2822 O  O   . GLU B 1 69  ? 25.165  -12.202 -21.110 1.00 15.08  ? 69  GLU B O   1 
ATOM   2823 C  CB  . GLU B 1 69  ? 22.036  -11.938 -21.081 1.00 14.66  ? 69  GLU B CB  1 
ATOM   2824 C  CG  . GLU B 1 69  ? 20.663  -12.483 -21.139 1.00 15.18  ? 69  GLU B CG  1 
ATOM   2825 C  CD  . GLU B 1 69  ? 19.809  -12.070 -19.983 1.00 15.39  ? 69  GLU B CD  1 
ATOM   2826 O  OE1 . GLU B 1 69  ? 20.307  -11.300 -19.090 1.00 18.74  ? 69  GLU B OE1 1 
ATOM   2827 O  OE2 . GLU B 1 69  ? 18.593  -12.393 -19.890 1.00 19.30  ? 69  GLU B OE2 1 
ATOM   2828 N  N   . PHE B 1 70  ? 24.465  -11.046 -22.900 1.00 13.25  ? 70  PHE B N   1 
ATOM   2829 C  CA  . PHE B 1 70  ? 25.684  -10.308 -22.965 1.00 12.74  ? 70  PHE B CA  1 
ATOM   2830 C  C   . PHE B 1 70  ? 25.432  -8.841  -22.897 1.00 13.56  ? 70  PHE B C   1 
ATOM   2831 O  O   . PHE B 1 70  ? 24.356  -8.327  -23.289 1.00 14.89  ? 70  PHE B O   1 
ATOM   2832 C  CB  . PHE B 1 70  ? 26.409  -10.691 -24.246 1.00 12.46  ? 70  PHE B CB  1 
ATOM   2833 C  CG  . PHE B 1 70  ? 26.925  -12.096 -24.231 1.00 12.99  ? 70  PHE B CG  1 
ATOM   2834 C  CD1 . PHE B 1 70  ? 26.087  -13.196 -24.434 1.00 12.86  ? 70  PHE B CD1 1 
ATOM   2835 C  CD2 . PHE B 1 70  ? 28.274  -12.308 -23.894 1.00 13.63  ? 70  PHE B CD2 1 
ATOM   2836 C  CE1 . PHE B 1 70  ? 26.555  -14.481 -24.294 1.00 14.31  ? 70  PHE B CE1 1 
ATOM   2837 C  CE2 . PHE B 1 70  ? 28.738  -13.610 -23.762 1.00 14.23  ? 70  PHE B CE2 1 
ATOM   2838 C  CZ  . PHE B 1 70  ? 27.903  -14.690 -23.992 1.00 14.10  ? 70  PHE B CZ  1 
ATOM   2839 N  N   . ASP B 1 71  ? 26.411  -8.109  -22.401 1.00 15.63  ? 71  ASP B N   1 
ATOM   2840 C  CA  . ASP B 1 71  ? 26.349  -6.676  -22.468 1.00 15.69  ? 71  ASP B CA  1 
ATOM   2841 C  C   . ASP B 1 71  ? 26.710  -6.322  -23.894 1.00 15.98  ? 71  ASP B C   1 
ATOM   2842 O  O   . ASP B 1 71  ? 27.831  -6.490  -24.329 1.00 21.43  ? 71  ASP B O   1 
ATOM   2843 C  CB  . ASP B 1 71  ? 27.373  -6.146  -21.507 1.00 22.10  ? 71  ASP B CB  1 
ATOM   2844 C  CG  . ASP B 1 71  ? 27.586  -4.657  -21.631 1.00 25.82  ? 71  ASP B CG  1 
ATOM   2845 O  OD1 . ASP B 1 71  ? 26.808  -3.955  -22.362 1.00 24.72  ? 71  ASP B OD1 1 
ATOM   2846 O  OD2 . ASP B 1 71  ? 28.516  -4.114  -21.008 1.00 40.02  ? 71  ASP B OD2 1 
ATOM   2847 N  N   . ASP B 1 72  ? 25.703  -5.830  -24.601 1.00 12.67  ? 72  ASP B N   1 
ATOM   2848 C  CA  . ASP B 1 72  ? 25.850  -5.419  -25.985 1.00 13.92  ? 72  ASP B CA  1 
ATOM   2849 C  C   . ASP B 1 72  ? 25.848  -3.907  -26.108 1.00 18.29  ? 72  ASP B C   1 
ATOM   2850 O  O   . ASP B 1 72  ? 25.463  -3.377  -27.154 1.00 18.11  ? 72  ASP B O   1 
ATOM   2851 C  CB  . ASP B 1 72  ? 24.751  -6.018  -26.870 1.00 14.30  ? 72  ASP B CB  1 
ATOM   2852 C  CG  . ASP B 1 72  ? 23.383  -5.549  -26.521 1.00 13.65  ? 72  ASP B CG  1 
ATOM   2853 O  OD1 . ASP B 1 72  ? 23.168  -4.844  -25.457 1.00 16.84  ? 72  ASP B OD1 1 
ATOM   2854 O  OD2 . ASP B 1 72  ? 22.431  -5.813  -27.309 1.00 15.85  ? 72  ASP B OD2 1 
ATOM   2855 N  N   . SER B 1 73  ? 26.230  -3.172  -25.066 1.00 17.82  ? 73  SER B N   1 
ATOM   2856 C  CA  . SER B 1 73  ? 26.221  -1.667  -25.117 1.00 18.76  ? 73  SER B CA  1 
ATOM   2857 C  C   . SER B 1 73  ? 27.582  -1.110  -25.652 1.00 18.58  ? 73  SER B C   1 
ATOM   2858 O  O   . SER B 1 73  ? 27.658  0.077   -25.843 1.00 18.74  ? 73  SER B O   1 
ATOM   2859 C  CB  . SER B 1 73  ? 25.909  -1.158  -23.756 1.00 26.30  ? 73  SER B CB  1 
ATOM   2860 O  OG  . SER B 1 73  ? 27.042  -1.353  -22.967 1.00 22.52  ? 73  SER B OG  1 
ATOM   2861 N  N   . GLN B 1 74  ? 28.558  -1.955  -25.931 1.00 21.62  ? 74  GLN B N   1 
ATOM   2862 C  CA  . GLN B 1 74  ? 29.774  -1.519  -26.584 1.00 23.92  ? 74  GLN B CA  1 
ATOM   2863 C  C   . GLN B 1 74  ? 30.061  -2.457  -27.698 1.00 19.94  ? 74  GLN B C   1 
ATOM   2864 O  O   . GLN B 1 74  ? 29.496  -3.598  -27.785 1.00 16.00  ? 74  GLN B O   1 
ATOM   2865 C  CB  . GLN B 1 74  ? 31.007  -1.491  -25.632 1.00 26.31  ? 74  GLN B CB  1 
ATOM   2866 C  CG  . GLN B 1 74  ? 30.943  -0.373  -24.633 1.00 32.74  ? 74  GLN B CG  1 
ATOM   2867 C  CD  . GLN B 1 74  ? 32.074  -0.471  -23.609 1.00 45.34  ? 74  GLN B CD  1 
ATOM   2868 O  OE1 . GLN B 1 74  ? 33.239  -0.533  -23.965 1.00 59.28  ? 74  GLN B OE1 1 
ATOM   2869 N  NE2 . GLN B 1 74  ? 31.711  -0.517  -22.327 1.00 54.21  ? 74  GLN B NE2 1 
ATOM   2870 N  N   . ASP B 1 75  ? 31.018  -2.008  -28.518 1.00 22.14  ? 75  ASP B N   1 
ATOM   2871 C  CA  . ASP B 1 75  ? 31.476  -2.860  -29.573 1.00 18.09  ? 75  ASP B CA  1 
ATOM   2872 C  C   . ASP B 1 75  ? 32.437  -4.035  -29.151 1.00 21.53  ? 75  ASP B C   1 
ATOM   2873 O  O   . ASP B 1 75  ? 33.662  -3.921  -29.187 1.00 31.96  ? 75  ASP B O   1 
ATOM   2874 C  CB  . ASP B 1 75  ? 31.963  -2.148  -30.770 1.00 33.08  ? 75  ASP B CB  1 
ATOM   2875 C  CG  . ASP B 1 75  ? 31.692  -2.941  -32.019 1.00 49.72  ? 75  ASP B CG  1 
ATOM   2876 O  OD1 . ASP B 1 75  ? 30.496  -3.066  -32.360 1.00 44.63  ? 75  ASP B OD1 1 
ATOM   2877 O  OD2 . ASP B 1 75  ? 32.642  -3.491  -32.613 1.00 39.61  ? 75  ASP B OD2 1 
ATOM   2878 N  N   . LYS B 1 76  ? 31.844  -5.150  -28.729 1.00 18.30  ? 76  LYS B N   1 
ATOM   2879 C  CA  . LYS B 1 76  ? 32.642  -6.241  -28.151 1.00 23.67  ? 76  LYS B CA  1 
ATOM   2880 C  C   . LYS B 1 76  ? 32.772  -7.513  -28.952 1.00 38.39  ? 76  LYS B C   1 
ATOM   2881 O  O   . LYS B 1 76  ? 33.731  -7.710  -29.706 1.00 57.68  ? 76  LYS B O   1 
ATOM   2882 C  CB  . LYS B 1 76  ? 32.265  -6.424  -26.668 1.00 21.77  ? 76  LYS B CB  1 
ATOM   2883 C  CG  . LYS B 1 76  ? 32.592  -5.234  -25.783 1.00 33.49  ? 76  LYS B CG  1 
ATOM   2884 C  CD  . LYS B 1 76  ? 32.172  -5.467  -24.327 1.00 42.96  ? 76  LYS B CD  1 
ATOM   2885 C  CE  . LYS B 1 76  ? 32.448  -4.322  -23.359 1.00 48.87  ? 76  LYS B CE  1 
ATOM   2886 N  NZ  . LYS B 1 76  ? 32.089  -4.731  -21.969 1.00 36.07  ? 76  LYS B NZ  1 
ATOM   2887 N  N   . ALA B 1 77  ? 31.819  -8.367  -28.736 1.00 24.96  ? 77  ALA B N   1 
ATOM   2888 C  CA  . ALA B 1 77  ? 31.573  -9.683  -29.323 1.00 16.42  ? 77  ALA B CA  1 
ATOM   2889 C  C   . ALA B 1 77  ? 30.843  -9.543  -30.676 1.00 14.65  ? 77  ALA B C   1 
ATOM   2890 O  O   . ALA B 1 77  ? 29.645  -9.373  -30.714 1.00 20.86  ? 77  ALA B O   1 
ATOM   2891 C  CB  . ALA B 1 77  ? 30.703  -10.379 -28.296 1.00 17.13  ? 77  ALA B CB  1 
ATOM   2892 N  N   . VAL B 1 78  ? 31.529  -9.615  -31.764 1.00 14.45  ? 78  VAL B N   1 
ATOM   2893 C  CA  . VAL B 1 78  ? 30.926  -9.271  -33.059 1.00 13.72  ? 78  VAL B CA  1 
ATOM   2894 C  C   . VAL B 1 78  ? 31.144  -10.378 -34.077 1.00 12.77  ? 78  VAL B C   1 
ATOM   2895 O  O   . VAL B 1 78  ? 32.179  -11.072 -34.110 1.00 15.39  ? 78  VAL B O   1 
ATOM   2896 C  CB  . VAL B 1 78  ? 31.369  -7.929  -33.597 1.00 20.92  ? 78  VAL B CB  1 
ATOM   2897 C  CG1 . VAL B 1 78  ? 31.115  -6.795  -32.645 1.00 25.59  ? 78  VAL B CG1 1 
ATOM   2898 C  CG2 . VAL B 1 78  ? 32.788  -7.964  -33.929 1.00 23.66  ? 78  VAL B CG2 1 
ATOM   2899 N  N   . LEU B 1 79  ? 30.112  -10.544 -34.896 1.00 11.60  ? 79  LEU B N   1 
ATOM   2900 C  CA  . LEU B 1 79  ? 30.137  -11.440 -36.044 1.00 11.29  ? 79  LEU B CA  1 
ATOM   2901 C  C   . LEU B 1 79  ? 30.140  -10.572 -37.273 1.00 12.54  ? 79  LEU B C   1 
ATOM   2902 O  O   . LEU B 1 79  ? 29.338  -9.626  -37.383 1.00 13.66  ? 79  LEU B O   1 
ATOM   2903 C  CB  . LEU B 1 79  ? 28.887  -12.322 -36.004 1.00 13.33  ? 79  LEU B CB  1 
ATOM   2904 C  CG  . LEU B 1 79  ? 28.721  -13.414 -37.014 1.00 12.83  ? 79  LEU B CG  1 
ATOM   2905 C  CD1 . LEU B 1 79  ? 29.733  -14.500 -36.733 1.00 19.19  ? 79  LEU B CD1 1 
ATOM   2906 C  CD2 . LEU B 1 79  ? 27.330  -14.006 -36.938 1.00 12.50  ? 79  LEU B CD2 1 
ATOM   2907 N  N   . LYS B 1 80  ? 30.992  -10.907 -38.244 1.00 13.24  ? 80  LYS B N   1 
ATOM   2908 C  CA  . LYS B 1 80  ? 31.054  -10.191 -39.525 1.00 13.60  ? 80  LYS B CA  1 
ATOM   2909 C  C   . LYS B 1 80  ? 31.592  -11.140 -40.559 1.00 13.41  ? 80  LYS B C   1 
ATOM   2910 O  O   . LYS B 1 80  ? 31.866  -12.308 -40.259 1.00 13.49  ? 80  LYS B O   1 
ATOM   2911 C  CB  . LYS B 1 80  ? 31.805  -8.905  -39.377 1.00 16.75  ? 80  LYS B CB  1 
ATOM   2912 C  CG  . LYS B 1 80  ? 33.238  -9.126  -39.232 1.00 17.12  ? 80  LYS B CG  1 
ATOM   2913 C  CD  . LYS B 1 80  ? 33.883  -7.763  -39.100 1.00 22.57  ? 80  LYS B CD  1 
ATOM   2914 C  CE  . LYS B 1 80  ? 33.414  -7.103  -37.835 1.00 34.64  ? 80  LYS B CE  1 
ATOM   2915 N  NZ  . LYS B 1 80  ? 34.307  -5.963  -37.467 1.00 72.90  ? 80  LYS B NZ  1 
ATOM   2916 N  N   . GLY B 1 81  ? 31.690  -10.659 -41.795 1.00 14.64  ? 81  GLY B N   1 
ATOM   2917 C  CA  . GLY B 1 81  ? 32.201  -11.498 -42.847 1.00 15.74  ? 81  GLY B CA  1 
ATOM   2918 C  C   . GLY B 1 81  ? 31.205  -12.548 -43.185 1.00 14.85  ? 81  GLY B C   1 
ATOM   2919 O  O   . GLY B 1 81  ? 30.007  -12.340 -43.027 1.00 13.66  ? 81  GLY B O   1 
ATOM   2920 N  N   . GLY B 1 82  ? 31.666  -13.687 -43.672 1.00 17.90  ? 82  GLY B N   1 
ATOM   2921 C  CA  . GLY B 1 82  ? 30.693  -14.668 -44.028 1.00 18.40  ? 82  GLY B CA  1 
ATOM   2922 C  C   . GLY B 1 82  ? 29.864  -14.064 -45.149 1.00 16.41  ? 82  GLY B C   1 
ATOM   2923 O  O   . GLY B 1 82  ? 30.370  -13.368 -46.043 1.00 22.46  ? 82  GLY B O   1 
ATOM   2924 N  N   . PRO B 1 83  ? 28.514  -14.238 -45.074 1.00 14.38  ? 83  PRO B N   1 
ATOM   2925 C  CA  . PRO B 1 83  ? 27.601  -13.666 -46.034 1.00 14.58  ? 83  PRO B CA  1 
ATOM   2926 C  C   . PRO B 1 83  ? 27.163  -12.224 -45.646 1.00 15.90  ? 83  PRO B C   1 
ATOM   2927 O  O   . PRO B 1 83  ? 26.363  -11.649 -46.344 1.00 16.72  ? 83  PRO B O   1 
ATOM   2928 C  CB  . PRO B 1 83  ? 26.326  -14.559 -45.914 1.00 16.49  ? 83  PRO B CB  1 
ATOM   2929 C  CG  . PRO B 1 83  ? 26.300  -14.893 -44.439 1.00 13.23  ? 83  PRO B CG  1 
ATOM   2930 C  CD  . PRO B 1 83  ? 27.781  -15.054 -44.068 1.00 14.22  ? 83  PRO B CD  1 
ATOM   2931 N  N   . LEU B 1 84  ? 27.674  -11.701 -44.550 1.00 13.03  ? 84  LEU B N   1 
ATOM   2932 C  CA  . LEU B 1 84  ? 27.117  -10.484 -43.948 1.00 11.94  ? 84  LEU B CA  1 
ATOM   2933 C  C   . LEU B 1 84  ? 27.733  -9.232  -44.502 1.00 14.11  ? 84  LEU B C   1 
ATOM   2934 O  O   . LEU B 1 84  ? 28.922  -9.208  -44.813 1.00 17.15  ? 84  LEU B O   1 
ATOM   2935 C  CB  . LEU B 1 84  ? 27.341  -10.512 -42.463 1.00 11.98  ? 84  LEU B CB  1 
ATOM   2936 C  CG  . LEU B 1 84  ? 26.768  -11.722 -41.730 1.00 10.48  ? 84  LEU B CG  1 
ATOM   2937 C  CD1 . LEU B 1 84  ? 27.238  -11.782 -40.276 1.00 13.28  ? 84  LEU B CD1 1 
ATOM   2938 C  CD2 . LEU B 1 84  ? 25.247  -11.739 -41.819 1.00 11.11  ? 84  LEU B CD2 1 
ATOM   2939 N  N   A ASP B 1 85  ? 26.955  -8.160  -44.564 0.50 15.95  ? 85  ASP B N   1 
ATOM   2940 N  N   B ASP B 1 85  ? 26.992  -8.142  -44.581 0.50 15.77  ? 85  ASP B N   1 
ATOM   2941 C  CA  A ASP B 1 85  ? 27.381  -6.874  -45.105 0.50 19.64  ? 85  ASP B CA  1 
ATOM   2942 C  CA  B ASP B 1 85  ? 27.554  -6.797  -44.717 0.50 17.53  ? 85  ASP B CA  1 
ATOM   2943 C  C   A ASP B 1 85  ? 27.736  -5.902  -44.054 0.50 23.60  ? 85  ASP B C   1 
ATOM   2944 C  C   B ASP B 1 85  ? 27.513  -6.138  -43.349 0.50 16.45  ? 85  ASP B C   1 
ATOM   2945 O  O   A ASP B 1 85  ? 27.932  -4.734  -44.371 0.50 22.13  ? 85  ASP B O   1 
ATOM   2946 O  O   B ASP B 1 85  ? 26.513  -6.140  -42.644 0.50 17.93  ? 85  ASP B O   1 
ATOM   2947 C  CB  A ASP B 1 85  ? 26.268  -6.248  -45.950 0.50 23.67  ? 85  ASP B CB  1 
ATOM   2948 C  CB  B ASP B 1 85  ? 26.771  -5.968  -45.728 0.50 22.93  ? 85  ASP B CB  1 
ATOM   2949 C  CG  A ASP B 1 85  ? 26.430  -6.554  -47.420 0.50 32.94  ? 85  ASP B CG  1 
ATOM   2950 C  CG  B ASP B 1 85  ? 26.756  -6.584  -47.112 0.50 36.73  ? 85  ASP B CG  1 
ATOM   2951 O  OD1 A ASP B 1 85  ? 25.405  -6.637  -48.151 0.50 39.19  ? 85  ASP B OD1 1 
ATOM   2952 O  OD1 B ASP B 1 85  ? 27.761  -7.234  -47.541 0.50 40.01  ? 85  ASP B OD1 1 
ATOM   2953 O  OD2 A ASP B 1 85  ? 27.605  -6.704  -47.852 0.50 49.70  ? 85  ASP B OD2 1 
ATOM   2954 O  OD2 B ASP B 1 85  ? 25.713  -6.386  -47.793 0.50 46.60  ? 85  ASP B OD2 1 
ATOM   2955 N  N   A GLY B 1 86  ? 27.738  -6.298  -42.800 0.50 23.54  ? 86  GLY B N   1 
ATOM   2956 N  N   B GLY B 1 86  ? 28.595  -5.433  -43.038 0.50 18.98  ? 86  GLY B N   1 
ATOM   2957 C  CA  A GLY B 1 86  ? 28.010  -5.285  -41.810 0.50 24.86  ? 86  GLY B CA  1 
ATOM   2958 C  CA  B GLY B 1 86  ? 28.704  -4.730  -41.796 0.50 18.26  ? 86  GLY B CA  1 
ATOM   2959 C  C   A GLY B 1 86  ? 28.520  -5.940  -40.562 0.50 19.74  ? 86  GLY B C   1 
ATOM   2960 C  C   B GLY B 1 86  ? 28.856  -5.669  -40.608 0.50 19.26  ? 86  GLY B C   1 
ATOM   2961 O  O   A GLY B 1 86  ? 29.037  -7.057  -40.600 0.50 26.18  ? 86  GLY B O   1 
ATOM   2962 O  O   B GLY B 1 86  ? 29.401  -6.767  -40.726 0.50 26.95  ? 86  GLY B O   1 
ATOM   2963 N  N   A THR B 1 87  ? 28.396  -5.269  -39.429 0.50 14.04  ? 87  THR B N   1 
ATOM   2964 N  N   B THR B 1 87  ? 28.397  -5.234  -39.435 0.50 14.28  ? 87  THR B N   1 
ATOM   2965 C  CA  A THR B 1 87  ? 28.825  -5.932  -38.191 0.50 13.71  ? 87  THR B CA  1 
ATOM   2966 C  CA  B THR B 1 87  ? 28.835  -5.842  -38.159 0.50 15.35  ? 87  THR B CA  1 
ATOM   2967 C  C   A THR B 1 87  ? 27.611  -6.133  -37.310 0.50 11.58  ? 87  THR B C   1 
ATOM   2968 C  C   B THR B 1 87  ? 27.618  -6.111  -37.291 0.50 11.87  ? 87  THR B C   1 
ATOM   2969 O  O   A THR B 1 87  ? 26.696  -5.316  -37.208 0.50 12.77  ? 87  THR B O   1 
ATOM   2970 O  O   B THR B 1 87  ? 26.699  -5.304  -37.185 0.50 12.80  ? 87  THR B O   1 
ATOM   2971 C  CB  A THR B 1 87  ? 29.818  -5.054  -37.480 0.50 13.84  ? 87  THR B CB  1 
ATOM   2972 C  CB  B THR B 1 87  ? 29.728  -4.842  -37.417 0.50 20.22  ? 87  THR B CB  1 
ATOM   2973 O  OG1 A THR B 1 87  ? 29.230  -3.765  -37.374 0.50 13.57  ? 87  THR B OG1 1 
ATOM   2974 O  OG1 B THR B 1 87  ? 30.980  -4.665  -38.111 0.50 24.21  ? 87  THR B OG1 1 
ATOM   2975 C  CG2 A THR B 1 87  ? 31.022  -4.834  -38.349 0.50 17.42  ? 87  THR B CG2 1 
ATOM   2976 C  CG2 B THR B 1 87  ? 30.003  -5.286  -36.014 0.50 21.21  ? 87  THR B CG2 1 
ATOM   2977 N  N   . TYR B 1 88  ? 27.623  -7.288  -36.681 1.00 10.15  ? 88  TYR B N   1 
ATOM   2978 C  CA  . TYR B 1 88  ? 26.502  -7.763  -35.878 1.00 10.03  ? 88  TYR B CA  1 
ATOM   2979 C  C   . TYR B 1 88  ? 27.039  -8.089  -34.504 1.00 10.29  ? 88  TYR B C   1 
ATOM   2980 O  O   . TYR B 1 88  ? 28.002  -8.790  -34.306 1.00 14.33  ? 88  TYR B O   1 
ATOM   2981 C  CB  . TYR B 1 88  ? 25.864  -9.011  -36.485 1.00 9.98   ? 88  TYR B CB  1 
ATOM   2982 C  CG  . TYR B 1 88  ? 25.136  -8.794  -37.792 1.00 9.18   ? 88  TYR B CG  1 
ATOM   2983 C  CD1 . TYR B 1 88  ? 25.802  -8.420  -38.976 1.00 11.28  ? 88  TYR B CD1 1 
ATOM   2984 C  CD2 . TYR B 1 88  ? 23.747  -8.915  -37.826 1.00 8.74   ? 88  TYR B CD2 1 
ATOM   2985 C  CE1 . TYR B 1 88  ? 25.071  -8.240  -40.167 1.00 10.11  ? 88  TYR B CE1 1 
ATOM   2986 C  CE2 . TYR B 1 88  ? 23.064  -8.810  -39.046 1.00 8.72   ? 88  TYR B CE2 1 
ATOM   2987 C  CZ  . TYR B 1 88  ? 23.722  -8.493  -40.181 1.00 8.79   ? 88  TYR B CZ  1 
ATOM   2988 O  OH  . TYR B 1 88  ? 23.019  -8.386  -41.350 1.00 9.81   ? 88  TYR B OH  1 
ATOM   2989 N  N   . ARG B 1 89  ? 26.367  -7.576  -33.492 1.00 9.16   ? 89  ARG B N   1 
ATOM   2990 C  CA  . ARG B 1 89  ? 26.780  -7.689  -32.092 1.00 9.38   ? 89  ARG B CA  1 
ATOM   2991 C  C   . ARG B 1 89  ? 26.053  -8.780  -31.355 1.00 7.83   ? 89  ARG B C   1 
ATOM   2992 O  O   . ARG B 1 89  ? 24.795  -8.869  -31.428 1.00 8.10   ? 89  ARG B O   1 
ATOM   2993 C  CB  . ARG B 1 89  ? 26.480  -6.363  -31.387 1.00 12.71  ? 89  ARG B CB  1 
ATOM   2994 C  CG  . ARG B 1 89  ? 27.302  -6.248  -30.162 1.00 15.33  ? 89  ARG B CG  1 
ATOM   2995 C  CD  . ARG B 1 89  ? 27.133  -4.819  -29.610 1.00 15.62  ? 89  ARG B CD  1 
ATOM   2996 N  NE  . ARG B 1 89  ? 27.794  -3.792  -30.420 1.00 16.25  ? 89  ARG B NE  1 
ATOM   2997 C  CZ  . ARG B 1 89  ? 27.660  -2.476  -30.250 1.00 14.73  ? 89  ARG B CZ  1 
ATOM   2998 N  NH1 . ARG B 1 89  ? 26.881  -1.987  -29.293 1.00 18.59  ? 89  ARG B NH1 1 
ATOM   2999 N  NH2 . ARG B 1 89  ? 28.312  -1.642  -31.048 1.00 17.04  ? 89  ARG B NH2 1 
ATOM   3000 N  N   . LEU B 1 90  ? 26.770  -9.617  -30.599 1.00 8.50   ? 90  LEU B N   1 
ATOM   3001 C  CA  . LEU B 1 90  ? 26.175  -10.700 -29.821 1.00 8.74   ? 90  LEU B CA  1 
ATOM   3002 C  C   . LEU B 1 90  ? 25.336  -10.123 -28.673 1.00 8.80   ? 90  LEU B C   1 
ATOM   3003 O  O   . LEU B 1 90  ? 25.811  -9.299  -27.878 1.00 10.56  ? 90  LEU B O   1 
ATOM   3004 C  CB  . LEU B 1 90  ? 27.265  -11.557 -29.251 1.00 9.57   ? 90  LEU B CB  1 
ATOM   3005 C  CG  . LEU B 1 90  ? 26.845  -12.735 -28.380 1.00 9.99   ? 90  LEU B CG  1 
ATOM   3006 C  CD1 . LEU B 1 90  ? 26.141  -13.817 -29.171 1.00 11.45  ? 90  LEU B CD1 1 
ATOM   3007 C  CD2 . LEU B 1 90  ? 28.095  -13.360 -27.701 1.00 13.70  ? 90  LEU B CD2 1 
ATOM   3008 N  N   . ILE B 1 91  ? 24.098  -10.582 -28.581 1.00 8.80   ? 91  ILE B N   1 
ATOM   3009 C  CA  . ILE B 1 91  ? 23.206  -10.221 -27.491 1.00 8.85   ? 91  ILE B CA  1 
ATOM   3010 C  C   . ILE B 1 91  ? 22.902  -11.385 -26.558 1.00 8.86   ? 91  ILE B C   1 
ATOM   3011 O  O   . ILE B 1 91  ? 22.787  -11.191 -25.354 1.00 9.15   ? 91  ILE B O   1 
ATOM   3012 C  CB  . ILE B 1 91  ? 21.900  -9.528  -27.985 1.00 9.55   ? 91  ILE B CB  1 
ATOM   3013 C  CG1 . ILE B 1 91  ? 20.988  -9.128  -26.824 1.00 13.02  ? 91  ILE B CG1 1 
ATOM   3014 C  CG2 . ILE B 1 91  ? 21.149  -10.333 -29.016 1.00 10.71  ? 91  ILE B CG2 1 
ATOM   3015 C  CD1 . ILE B 1 91  ? 19.908  -8.144  -27.236 1.00 14.97  ? 91  ILE B CD1 1 
ATOM   3016 N  N   . GLN B 1 92  ? 22.735  -12.606 -27.089 1.00 8.32   ? 92  GLN B N   1 
ATOM   3017 C  CA  . GLN B 1 92  ? 22.447  -13.755 -26.216 1.00 9.04   ? 92  GLN B CA  1 
ATOM   3018 C  C   . GLN B 1 92  ? 22.681  -15.022 -27.008 1.00 8.35   ? 92  GLN B C   1 
ATOM   3019 O  O   . GLN B 1 92  ? 22.765  -15.020 -28.235 1.00 8.74   ? 92  GLN B O   1 
ATOM   3020 C  CB  . GLN B 1 92  ? 20.965  -13.752 -25.739 1.00 10.69  ? 92  GLN B CB  1 
ATOM   3021 C  CG  . GLN B 1 92  ? 19.925  -13.660 -26.856 1.00 11.21  ? 92  GLN B CG  1 
ATOM   3022 C  CD  . GLN B 1 92  ? 19.197  -14.961 -27.108 1.00 10.89  ? 92  GLN B CD  1 
ATOM   3023 O  OE1 . GLN B 1 92  ? 19.779  -16.059 -27.070 1.00 11.25  ? 92  GLN B OE1 1 
ATOM   3024 N  NE2 . GLN B 1 92  ? 17.903  -14.880 -27.453 1.00 13.93  ? 92  GLN B NE2 1 
ATOM   3025 N  N   . PHE B 1 93  ? 22.881  -16.120 -26.251 1.00 8.47   ? 93  PHE B N   1 
ATOM   3026 C  CA  . PHE B 1 93  ? 22.770  -17.425 -26.848 1.00 8.54   ? 93  PHE B CA  1 
ATOM   3027 C  C   . PHE B 1 93  ? 21.791  -18.273 -26.054 1.00 7.99   ? 93  PHE B C   1 
ATOM   3028 O  O   . PHE B 1 93  ? 21.553  -18.052 -24.860 1.00 10.45  ? 93  PHE B O   1 
ATOM   3029 C  CB  . PHE B 1 93  ? 24.121  -18.112 -27.091 1.00 8.99   ? 93  PHE B CB  1 
ATOM   3030 C  CG  . PHE B 1 93  ? 24.866  -18.593 -25.838 1.00 9.12   ? 93  PHE B CG  1 
ATOM   3031 C  CD1 . PHE B 1 93  ? 24.500  -19.755 -25.181 1.00 11.06  ? 93  PHE B CD1 1 
ATOM   3032 C  CD2 . PHE B 1 93  ? 25.989  -17.884 -25.434 1.00 11.29  ? 93  PHE B CD2 1 
ATOM   3033 C  CE1 . PHE B 1 93  ? 25.194  -20.148 -24.044 1.00 11.35  ? 93  PHE B CE1 1 
ATOM   3034 C  CE2 . PHE B 1 93  ? 26.680  -18.310 -24.259 1.00 13.35  ? 93  PHE B CE2 1 
ATOM   3035 C  CZ  . PHE B 1 93  ? 26.288  -19.454 -23.602 1.00 13.11  ? 93  PHE B CZ  1 
ATOM   3036 N  N   . HIS B 1 94  ? 21.307  -19.309 -26.733 1.00 8.13   ? 94  HIS B N   1 
ATOM   3037 C  CA  . HIS B 1 94  ? 20.404  -20.306 -26.141 1.00 7.91   ? 94  HIS B CA  1 
ATOM   3038 C  C   . HIS B 1 94  ? 20.502  -21.565 -26.966 1.00 6.92   ? 94  HIS B C   1 
ATOM   3039 O  O   . HIS B 1 94  ? 21.124  -21.593 -28.016 1.00 8.08   ? 94  HIS B O   1 
ATOM   3040 C  CB  . HIS B 1 94  ? 18.977  -19.792 -26.104 1.00 8.22   ? 94  HIS B CB  1 
ATOM   3041 C  CG  . HIS B 1 94  ? 18.466  -19.520 -27.475 1.00 8.22   ? 94  HIS B CG  1 
ATOM   3042 N  ND1 . HIS B 1 94  ? 18.634  -18.318 -28.111 1.00 8.31   ? 94  HIS B ND1 1 
ATOM   3043 C  CD2 . HIS B 1 94  ? 17.826  -20.362 -28.338 1.00 7.35   ? 94  HIS B CD2 1 
ATOM   3044 C  CE1 . HIS B 1 94  ? 18.140  -18.458 -29.352 1.00 7.78   ? 94  HIS B CE1 1 
ATOM   3045 N  NE2 . HIS B 1 94  ? 17.654  -19.685 -29.519 1.00 7.41   ? 94  HIS B NE2 1 
ATOM   3046 N  N   . PHE B 1 95  ? 19.830  -22.610 -26.480 1.00 8.07   ? 95  PHE B N   1 
ATOM   3047 C  CA  . PHE B 1 95  ? 19.788  -23.897 -27.161 1.00 7.31   ? 95  PHE B CA  1 
ATOM   3048 C  C   . PHE B 1 95  ? 18.346  -24.334 -27.374 1.00 7.49   ? 95  PHE B C   1 
ATOM   3049 O  O   . PHE B 1 95  ? 17.409  -23.877 -26.699 1.00 8.42   ? 95  PHE B O   1 
ATOM   3050 C  CB  . PHE B 1 95  ? 20.530  -24.984 -26.318 1.00 8.30   ? 95  PHE B CB  1 
ATOM   3051 C  CG  . PHE B 1 95  ? 21.970  -24.704 -25.993 1.00 8.20   ? 95  PHE B CG  1 
ATOM   3052 C  CD1 . PHE B 1 95  ? 22.287  -23.809 -24.955 1.00 9.08   ? 95  PHE B CD1 1 
ATOM   3053 C  CD2 . PHE B 1 95  ? 22.985  -25.342 -26.688 1.00 9.10   ? 95  PHE B CD2 1 
ATOM   3054 C  CE1 . PHE B 1 95  ? 23.611  -23.628 -24.594 1.00 9.14   ? 95  PHE B CE1 1 
ATOM   3055 C  CE2 . PHE B 1 95  ? 24.318  -25.133 -26.334 1.00 9.50   ? 95  PHE B CE2 1 
ATOM   3056 C  CZ  . PHE B 1 95  ? 24.614  -24.256 -25.290 1.00 9.36   ? 95  PHE B CZ  1 
ATOM   3057 N  N   . HIS B 1 96  ? 18.210  -25.307 -28.263 1.00 7.56   ? 96  HIS B N   1 
ATOM   3058 C  CA  . HIS B 1 96  ? 17.010  -26.125 -28.445 1.00 7.43   ? 96  HIS B CA  1 
ATOM   3059 C  C   . HIS B 1 96  ? 17.460  -27.565 -28.333 1.00 7.21   ? 96  HIS B C   1 
ATOM   3060 O  O   . HIS B 1 96  ? 18.539  -27.922 -28.833 1.00 7.54   ? 96  HIS B O   1 
ATOM   3061 C  CB  . HIS B 1 96  ? 16.366  -25.912 -29.832 1.00 7.88   ? 96  HIS B CB  1 
ATOM   3062 C  CG  . HIS B 1 96  ? 16.065  -24.450 -30.107 1.00 8.34   ? 96  HIS B CG  1 
ATOM   3063 N  ND1 . HIS B 1 96  ? 14.831  -23.888 -29.945 1.00 8.54   ? 96  HIS B ND1 1 
ATOM   3064 C  CD2 . HIS B 1 96  ? 16.883  -23.422 -30.498 1.00 7.37   ? 96  HIS B CD2 1 
ATOM   3065 C  CE1 . HIS B 1 96  ? 14.898  -22.589 -30.261 1.00 8.64   ? 96  HIS B CE1 1 
ATOM   3066 N  NE2 . HIS B 1 96  ? 16.146  -22.266 -30.580 1.00 7.69   ? 96  HIS B NE2 1 
ATOM   3067 N  N   . TRP B 1 97  ? 16.673  -28.417 -27.673 1.00 6.94   ? 97  TRP B N   1 
ATOM   3068 C  CA  . TRP B 1 97  ? 17.064  -29.795 -27.460 1.00 7.84   ? 97  TRP B CA  1 
ATOM   3069 C  C   . TRP B 1 97  ? 15.880  -30.709 -27.309 1.00 7.64   ? 97  TRP B C   1 
ATOM   3070 O  O   . TRP B 1 97  ? 14.706  -30.277 -27.228 1.00 8.37   ? 97  TRP B O   1 
ATOM   3071 C  CB  . TRP B 1 97  ? 17.972  -29.905 -26.171 1.00 8.19   ? 97  TRP B CB  1 
ATOM   3072 C  CG  . TRP B 1 97  ? 17.318  -29.490 -24.912 1.00 7.91   ? 97  TRP B CG  1 
ATOM   3073 C  CD1 . TRP B 1 97  ? 16.653  -30.332 -24.049 1.00 9.43   ? 97  TRP B CD1 1 
ATOM   3074 C  CD2 . TRP B 1 97  ? 17.292  -28.206 -24.326 1.00 8.62   ? 97  TRP B CD2 1 
ATOM   3075 N  NE1 . TRP B 1 97  ? 16.228  -29.633 -22.956 1.00 10.04  ? 97  TRP B NE1 1 
ATOM   3076 C  CE2 . TRP B 1 97  ? 16.563  -28.310 -23.107 1.00 9.12   ? 97  TRP B CE2 1 
ATOM   3077 C  CE3 . TRP B 1 97  ? 17.745  -26.921 -24.749 1.00 8.60   ? 97  TRP B CE3 1 
ATOM   3078 C  CZ2 . TRP B 1 97  ? 16.416  -27.213 -22.269 1.00 10.41  ? 97  TRP B CZ2 1 
ATOM   3079 C  CZ3 . TRP B 1 97  ? 17.512  -25.838 -23.938 1.00 9.71   ? 97  TRP B CZ3 1 
ATOM   3080 C  CH2 . TRP B 1 97  ? 16.854  -25.976 -22.707 1.00 10.25  ? 97  TRP B CH2 1 
ATOM   3081 N  N   . GLY B 1 98  ? 16.167  -32.015 -27.319 1.00 8.12   ? 98  GLY B N   1 
ATOM   3082 C  CA  . GLY B 1 98  ? 15.153  -33.029 -27.370 1.00 8.67   ? 98  GLY B CA  1 
ATOM   3083 C  C   . GLY B 1 98  ? 14.931  -33.701 -26.030 1.00 9.53   ? 98  GLY B C   1 
ATOM   3084 O  O   . GLY B 1 98  ? 15.688  -33.568 -25.071 1.00 9.80   ? 98  GLY B O   1 
ATOM   3085 N  N   . SER B 1 99  ? 13.888  -34.563 -26.058 1.00 10.64  ? 99  SER B N   1 
ATOM   3086 C  CA  . SER B 1 99  ? 13.669  -35.538 -24.957 1.00 11.42  ? 99  SER B CA  1 
ATOM   3087 C  C   . SER B 1 99  ? 14.574  -36.738 -25.054 1.00 11.89  ? 99  SER B C   1 
ATOM   3088 O  O   . SER B 1 99  ? 14.738  -37.491 -24.046 1.00 14.16  ? 99  SER B O   1 
ATOM   3089 C  CB  . SER B 1 99  ? 12.229  -35.880 -24.907 1.00 13.55  ? 99  SER B CB  1 
ATOM   3090 O  OG  . SER B 1 99  ? 11.775  -36.398 -26.142 1.00 13.08  ? 99  SER B OG  1 
ATOM   3091 N  N   . LEU B 1 100 ? 15.150  -36.982 -26.219 1.00 11.45  ? 100 LEU B N   1 
ATOM   3092 C  CA  . LEU B 1 100 ? 16.005  -38.129 -26.540 1.00 11.75  ? 100 LEU B CA  1 
ATOM   3093 C  C   . LEU B 1 100 ? 17.102  -37.644 -27.376 1.00 11.06  ? 100 LEU B C   1 
ATOM   3094 O  O   . LEU B 1 100 ? 16.956  -36.586 -28.017 1.00 11.27  ? 100 LEU B O   1 
ATOM   3095 C  CB  . LEU B 1 100 ? 15.170  -39.133 -27.421 1.00 19.89  ? 100 LEU B CB  1 
ATOM   3096 C  CG  . LEU B 1 100 ? 13.808  -39.475 -26.822 1.00 21.21  ? 100 LEU B CG  1 
ATOM   3097 C  CD1 . LEU B 1 100 ? 12.787  -39.940 -27.857 1.00 30.03  ? 100 LEU B CD1 1 
ATOM   3098 C  CD2 . LEU B 1 100 ? 14.089  -40.566 -25.811 1.00 28.26  ? 100 LEU B CD2 1 
ATOM   3099 N  N   . ASP B 1 101 ? 18.210  -38.370 -27.411 1.00 11.54  ? 101 ASP B N   1 
ATOM   3100 C  CA  . ASP B 1 101 ? 19.359  -37.934 -28.249 1.00 11.84  ? 101 ASP B CA  1 
ATOM   3101 C  C   . ASP B 1 101 ? 19.076  -37.853 -29.748 1.00 10.53  ? 101 ASP B C   1 
ATOM   3102 O  O   . ASP B 1 101 ? 19.749  -37.147 -30.444 1.00 12.69  ? 101 ASP B O   1 
ATOM   3103 C  CB  . ASP B 1 101 ? 20.557  -38.822 -28.021 1.00 12.79  ? 101 ASP B CB  1 
ATOM   3104 C  CG  . ASP B 1 101 ? 21.012  -38.826 -26.575 1.00 13.06  ? 101 ASP B CG  1 
ATOM   3105 O  OD1 . ASP B 1 101 ? 20.571  -37.945 -25.808 1.00 13.85  ? 101 ASP B OD1 1 
ATOM   3106 O  OD2 . ASP B 1 101 ? 21.813  -39.711 -26.206 1.00 17.36  ? 101 ASP B OD2 1 
ATOM   3107 N  N   . GLY B 1 102 ? 18.057  -38.613 -30.196 1.00 12.08  ? 102 GLY B N   1 
ATOM   3108 C  CA  . GLY B 1 102 ? 17.746  -38.638 -31.642 1.00 11.54  ? 102 GLY B CA  1 
ATOM   3109 C  C   . GLY B 1 102 ? 16.938  -37.449 -32.189 1.00 10.82  ? 102 GLY B C   1 
ATOM   3110 O  O   . GLY B 1 102 ? 16.626  -37.445 -33.362 1.00 11.65  ? 102 GLY B O   1 
ATOM   3111 N  N   . GLN B 1 103 ? 16.656  -36.449 -31.372 1.00 9.47   ? 103 GLN B N   1 
ATOM   3112 C  CA  . GLN B 1 103 ? 15.985  -35.286 -31.862 1.00 8.93   ? 103 GLN B CA  1 
ATOM   3113 C  C   . GLN B 1 103 ? 16.368  -34.108 -30.973 1.00 8.42   ? 103 GLN B C   1 
ATOM   3114 O  O   . GLN B 1 103 ? 16.890  -34.307 -29.899 1.00 9.17   ? 103 GLN B O   1 
ATOM   3115 C  CB  . GLN B 1 103 ? 14.444  -35.463 -31.867 1.00 11.48  ? 103 GLN B CB  1 
ATOM   3116 C  CG  . GLN B 1 103 ? 13.871  -35.673 -30.483 1.00 11.70  ? 103 GLN B CG  1 
ATOM   3117 C  CD  . GLN B 1 103 ? 12.485  -36.248 -30.518 1.00 14.01  ? 103 GLN B CD  1 
ATOM   3118 O  OE1 . GLN B 1 103 ? 12.228  -37.108 -31.335 1.00 26.25  ? 103 GLN B OE1 1 
ATOM   3119 N  NE2 . GLN B 1 103 ? 11.584  -35.769 -29.742 1.00 14.55  ? 103 GLN B NE2 1 
ATOM   3120 N  N   . GLY B 1 104 ? 16.070  -32.884 -31.446 1.00 7.71   ? 104 GLY B N   1 
ATOM   3121 C  CA  . GLY B 1 104 ? 16.315  -31.698 -30.663 1.00 7.93   ? 104 GLY B CA  1 
ATOM   3122 C  C   . GLY B 1 104 ? 16.767  -30.533 -31.508 1.00 7.67   ? 104 GLY B C   1 
ATOM   3123 O  O   . GLY B 1 104 ? 16.508  -29.383 -31.156 1.00 8.44   ? 104 GLY B O   1 
ATOM   3124 N  N   . SER B 1 105 ? 17.483  -30.790 -32.614 1.00 7.40   ? 105 SER B N   1 
ATOM   3125 C  CA  . SER B 1 105 ? 17.901  -29.670 -33.454 1.00 7.36   ? 105 SER B CA  1 
ATOM   3126 C  C   . SER B 1 105 ? 16.681  -29.094 -34.221 1.00 6.82   ? 105 SER B C   1 
ATOM   3127 O  O   . SER B 1 105 ? 15.656  -29.765 -34.428 1.00 8.19   ? 105 SER B O   1 
ATOM   3128 C  CB  . SER B 1 105 ? 19.005  -30.016 -34.390 1.00 6.88   ? 105 SER B CB  1 
ATOM   3129 O  OG  . SER B 1 105 ? 18.663  -30.961 -35.378 1.00 7.70   ? 105 SER B OG  1 
ATOM   3130 N  N   . GLU B 1 106 ? 16.824  -27.857 -34.614 1.00 7.13   ? 106 GLU B N   1 
ATOM   3131 C  CA  . GLU B 1 106 ? 15.802  -27.141 -35.448 1.00 7.45   ? 106 GLU B CA  1 
ATOM   3132 C  C   . GLU B 1 106 ? 16.138  -27.339 -36.919 1.00 7.37   ? 106 GLU B C   1 
ATOM   3133 O  O   . GLU B 1 106 ? 15.354  -27.904 -37.687 1.00 8.17   ? 106 GLU B O   1 
ATOM   3134 C  CB  . GLU B 1 106 ? 15.769  -25.667 -35.002 1.00 6.94   ? 106 GLU B CB  1 
ATOM   3135 C  CG  . GLU B 1 106 ? 15.321  -25.545 -33.573 1.00 9.25   ? 106 GLU B CG  1 
ATOM   3136 C  CD  . GLU B 1 106 ? 14.607  -24.300 -33.289 1.00 7.85   ? 106 GLU B CD  1 
ATOM   3137 O  OE1 . GLU B 1 106 ? 15.175  -23.204 -33.565 1.00 7.81   ? 106 GLU B OE1 1 
ATOM   3138 O  OE2 . GLU B 1 106 ? 13.431  -24.328 -32.821 1.00 9.04   ? 106 GLU B OE2 1 
ATOM   3139 N  N   . HIS B 1 107 ? 17.312  -26.868 -37.355 1.00 6.94   ? 107 HIS B N   1 
ATOM   3140 C  CA  . HIS B 1 107 ? 17.771  -27.256 -38.643 1.00 6.74   ? 107 HIS B CA  1 
ATOM   3141 C  C   . HIS B 1 107 ? 18.087  -28.736 -38.660 1.00 6.78   ? 107 HIS B C   1 
ATOM   3142 O  O   . HIS B 1 107 ? 18.433  -29.358 -37.648 1.00 7.57   ? 107 HIS B O   1 
ATOM   3143 C  CB  . HIS B 1 107 ? 19.024  -26.456 -39.037 1.00 7.21   ? 107 HIS B CB  1 
ATOM   3144 C  CG  . HIS B 1 107 ? 18.735  -25.007 -39.183 1.00 6.83   ? 107 HIS B CG  1 
ATOM   3145 N  ND1 . HIS B 1 107 ? 18.755  -24.114 -38.138 1.00 7.15   ? 107 HIS B ND1 1 
ATOM   3146 C  CD2 . HIS B 1 107 ? 18.230  -24.302 -40.270 1.00 6.59   ? 107 HIS B CD2 1 
ATOM   3147 C  CE1 . HIS B 1 107 ? 18.324  -22.912 -38.574 1.00 7.40   ? 107 HIS B CE1 1 
ATOM   3148 N  NE2 . HIS B 1 107 ? 18.012  -22.994 -39.874 1.00 7.21   ? 107 HIS B NE2 1 
ATOM   3149 N  N   . THR B 1 108 ? 17.954  -29.326 -39.855 1.00 7.58   ? 108 THR B N   1 
ATOM   3150 C  CA  . THR B 1 108 ? 18.292  -30.698 -40.117 1.00 7.73   ? 108 THR B CA  1 
ATOM   3151 C  C   . THR B 1 108 ? 19.238  -30.710 -41.335 1.00 7.19   ? 108 THR B C   1 
ATOM   3152 O  O   . THR B 1 108 ? 19.260  -29.734 -42.112 1.00 8.23   ? 108 THR B O   1 
ATOM   3153 C  CB  . THR B 1 108 ? 17.099  -31.615 -40.328 1.00 9.06   ? 108 THR B CB  1 
ATOM   3154 O  OG1 . THR B 1 108 ? 16.231  -31.118 -41.368 1.00 9.36   ? 108 THR B OG1 1 
ATOM   3155 C  CG2 . THR B 1 108 ? 16.308  -31.648 -39.046 1.00 10.15  ? 108 THR B CG2 1 
ATOM   3156 N  N   . VAL B 1 109 ? 19.996  -31.788 -41.491 1.00 8.45   ? 109 VAL B N   1 
ATOM   3157 C  CA  . VAL B 1 109 ? 21.026  -31.886 -42.552 1.00 9.27   ? 109 VAL B CA  1 
ATOM   3158 C  C   . VAL B 1 109 ? 20.689  -33.180 -43.340 1.00 8.73   ? 109 VAL B C   1 
ATOM   3159 O  O   . VAL B 1 109 ? 20.823  -34.276 -42.767 1.00 8.92   ? 109 VAL B O   1 
ATOM   3160 C  CB  . VAL B 1 109 ? 22.458  -31.907 -42.009 1.00 9.52   ? 109 VAL B CB  1 
ATOM   3161 C  CG1 . VAL B 1 109 ? 23.449  -32.048 -43.174 1.00 10.69  ? 109 VAL B CG1 1 
ATOM   3162 C  CG2 . VAL B 1 109 ? 22.710  -30.653 -41.205 1.00 10.26  ? 109 VAL B CG2 1 
ATOM   3163 N  N   . ASP B 1 110 ? 20.134  -33.067 -44.552 1.00 9.64   ? 110 ASP B N   1 
ATOM   3164 C  CA  . ASP B 1 110 ? 19.690  -34.282 -45.251 1.00 10.46  ? 110 ASP B CA  1 
ATOM   3165 C  C   . ASP B 1 110 ? 18.725  -35.091 -44.355 1.00 10.12  ? 110 ASP B C   1 
ATOM   3166 O  O   . ASP B 1 110 ? 18.796  -36.302 -44.293 1.00 11.01  ? 110 ASP B O   1 
ATOM   3167 C  CB  . ASP B 1 110 ? 20.861  -35.125 -45.746 1.00 13.41  ? 110 ASP B CB  1 
ATOM   3168 C  CG  . ASP B 1 110 ? 21.692  -34.335 -46.775 1.00 13.30  ? 110 ASP B CG  1 
ATOM   3169 O  OD1 . ASP B 1 110 ? 21.111  -33.460 -47.470 1.00 15.40  ? 110 ASP B OD1 1 
ATOM   3170 O  OD2 . ASP B 1 110 ? 22.862  -34.605 -46.921 1.00 17.25  ? 110 ASP B OD2 1 
ATOM   3171 N  N   . LYS B 1 111 ? 17.850  -34.342 -43.632 1.00 9.77   ? 111 LYS B N   1 
ATOM   3172 C  CA  . LYS B 1 111 ? 16.811  -34.880 -42.726 1.00 10.01  ? 111 LYS B CA  1 
ATOM   3173 C  C   . LYS B 1 111 ? 17.423  -35.410 -41.382 1.00 9.37   ? 111 LYS B C   1 
ATOM   3174 O  O   . LYS B 1 111 ? 16.627  -35.803 -40.525 1.00 11.17  ? 111 LYS B O   1 
ATOM   3175 C  CB  . LYS B 1 111 ? 15.932  -35.941 -43.364 1.00 12.76  ? 111 LYS B CB  1 
ATOM   3176 C  CG  . LYS B 1 111 ? 15.214  -35.355 -44.640 1.00 16.58  ? 111 LYS B CG  1 
ATOM   3177 C  CD  . LYS B 1 111 ? 14.260  -34.171 -44.306 1.00 20.01  ? 111 LYS B CD  1 
ATOM   3178 C  CE  . LYS B 1 111 ? 13.432  -33.563 -45.455 1.00 21.03  ? 111 LYS B CE  1 
ATOM   3179 N  NZ  . LYS B 1 111 ? 12.251  -34.376 -45.691 1.00 24.03  ? 111 LYS B NZ  1 
ATOM   3180 N  N   . LYS B 1 112 ? 18.743  -35.389 -41.211 1.00 9.21   ? 112 LYS B N   1 
ATOM   3181 C  CA  . LYS B 1 112 ? 19.321  -35.784 -39.924 1.00 9.82   ? 112 LYS B CA  1 
ATOM   3182 C  C   . LYS B 1 112 ? 18.964  -34.743 -38.868 1.00 8.60   ? 112 LYS B C   1 
ATOM   3183 O  O   . LYS B 1 112 ? 19.235  -33.543 -39.064 1.00 8.66   ? 112 LYS B O   1 
ATOM   3184 C  CB  . LYS B 1 112 ? 20.850  -35.871 -40.035 1.00 10.79  ? 112 LYS B CB  1 
ATOM   3185 C  CG  . LYS B 1 112 ? 21.533  -36.226 -38.698 1.00 11.63  ? 112 LYS B CG  1 
ATOM   3186 C  CD  . LYS B 1 112 ? 23.011  -36.185 -38.799 1.00 13.79  ? 112 LYS B CD  1 
ATOM   3187 C  CE  . LYS B 1 112 ? 23.681  -36.342 -37.473 1.00 15.72  ? 112 LYS B CE  1 
ATOM   3188 N  NZ  . LYS B 1 112 ? 23.583  -37.691 -37.014 1.00 14.91  ? 112 LYS B NZ  1 
ATOM   3189 N  N   A LYS B 1 113 ? 18.464  -35.230 -37.731 0.50 8.62   ? 113 LYS B N   1 
ATOM   3190 N  N   B LYS B 1 113 ? 18.460  -35.237 -37.736 0.50 8.71   ? 113 LYS B N   1 
ATOM   3191 C  CA  A LYS B 1 113 ? 18.272  -34.406 -36.558 0.50 8.81   ? 113 LYS B CA  1 
ATOM   3192 C  CA  B LYS B 1 113 ? 18.266  -34.429 -36.544 0.50 8.69   ? 113 LYS B CA  1 
ATOM   3193 C  C   A LYS B 1 113 ? 19.408  -34.652 -35.586 0.50 8.28   ? 113 LYS B C   1 
ATOM   3194 C  C   B LYS B 1 113 ? 19.405  -34.658 -35.572 0.50 8.36   ? 113 LYS B C   1 
ATOM   3195 O  O   A LYS B 1 113 ? 19.759  -35.799 -35.292 0.50 10.61  ? 113 LYS B O   1 
ATOM   3196 O  O   B LYS B 1 113 ? 19.756  -35.799 -35.259 0.50 10.55  ? 113 LYS B O   1 
ATOM   3197 C  CB  A LYS B 1 113 ? 16.961  -34.805 -35.844 0.50 9.68   ? 113 LYS B CB  1 
ATOM   3198 C  CB  B LYS B 1 113 ? 16.945  -34.829 -35.837 0.50 9.48   ? 113 LYS B CB  1 
ATOM   3199 C  CG  A LYS B 1 113 ? 15.696  -34.503 -36.617 0.50 10.25  ? 113 LYS B CG  1 
ATOM   3200 C  CG  B LYS B 1 113 ? 15.723  -34.520 -36.671 0.50 10.54  ? 113 LYS B CG  1 
ATOM   3201 C  CD  A LYS B 1 113 ? 14.546  -35.157 -35.901 0.50 12.74  ? 113 LYS B CD  1 
ATOM   3202 C  CD  B LYS B 1 113 ? 14.456  -35.024 -36.047 0.50 11.66  ? 113 LYS B CD  1 
ATOM   3203 C  CE  A LYS B 1 113 ? 13.206  -34.618 -36.405 0.50 14.85  ? 113 LYS B CE  1 
ATOM   3204 C  CE  B LYS B 1 113 ? 13.282  -34.448 -36.831 0.50 15.89  ? 113 LYS B CE  1 
ATOM   3205 N  NZ  A LYS B 1 113 ? 12.828  -35.205 -37.718 0.50 13.54  ? 113 LYS B NZ  1 
ATOM   3206 N  NZ  B LYS B 1 113 ? 12.049  -35.195 -36.527 0.50 16.57  ? 113 LYS B NZ  1 
ATOM   3207 N  N   . TYR B 1 114 ? 19.988  -33.551 -35.060 1.00 8.17   ? 114 TYR B N   1 
ATOM   3208 C  CA  . TYR B 1 114 ? 20.978  -33.593 -34.025 1.00 8.27   ? 114 TYR B CA  1 
ATOM   3209 C  C   . TYR B 1 114 ? 20.295  -33.562 -32.652 1.00 7.32   ? 114 TYR B C   1 
ATOM   3210 O  O   . TYR B 1 114 ? 19.110  -33.281 -32.537 1.00 8.20   ? 114 TYR B O   1 
ATOM   3211 C  CB  . TYR B 1 114 ? 22.018  -32.507 -34.182 1.00 8.14   ? 114 TYR B CB  1 
ATOM   3212 C  CG  . TYR B 1 114 ? 22.966  -32.722 -35.337 1.00 8.22   ? 114 TYR B CG  1 
ATOM   3213 C  CD1 . TYR B 1 114 ? 22.677  -32.282 -36.635 1.00 9.64   ? 114 TYR B CD1 1 
ATOM   3214 C  CD2 . TYR B 1 114 ? 24.195  -33.331 -35.076 1.00 9.37   ? 114 TYR B CD2 1 
ATOM   3215 C  CE1 . TYR B 1 114 ? 23.582  -32.458 -37.663 1.00 10.85  ? 114 TYR B CE1 1 
ATOM   3216 C  CE2 . TYR B 1 114 ? 25.168  -33.480 -36.060 1.00 11.60  ? 114 TYR B CE2 1 
ATOM   3217 C  CZ  . TYR B 1 114 ? 24.815  -33.059 -37.354 1.00 12.17  ? 114 TYR B CZ  1 
ATOM   3218 O  OH  . TYR B 1 114 ? 25.754  -33.182 -38.409 1.00 16.22  ? 114 TYR B OH  1 
ATOM   3219 N  N   . ALA B 1 115 ? 21.070  -33.858 -31.610 1.00 7.80   ? 115 ALA B N   1 
ATOM   3220 C  CA  . ALA B 1 115 ? 20.506  -33.903 -30.241 1.00 8.16   ? 115 ALA B CA  1 
ATOM   3221 C  C   . ALA B 1 115 ? 20.130  -32.500 -29.760 1.00 7.66   ? 115 ALA B C   1 
ATOM   3222 O  O   . ALA B 1 115 ? 19.298  -32.358 -28.880 1.00 8.28   ? 115 ALA B O   1 
ATOM   3223 C  CB  . ALA B 1 115 ? 21.578  -34.498 -29.289 1.00 10.03  ? 115 ALA B CB  1 
ATOM   3224 N  N   . ALA B 1 116 ? 20.786  -31.449 -30.272 1.00 7.22   ? 116 ALA B N   1 
ATOM   3225 C  CA  . ALA B 1 116 ? 20.499  -30.101 -29.822 1.00 7.32   ? 116 ALA B CA  1 
ATOM   3226 C  C   . ALA B 1 116 ? 21.108  -29.144 -30.853 1.00 6.74   ? 116 ALA B C   1 
ATOM   3227 O  O   . ALA B 1 116 ? 21.814  -29.550 -31.753 1.00 7.25   ? 116 ALA B O   1 
ATOM   3228 C  CB  . ALA B 1 116 ? 21.030  -29.824 -28.404 1.00 8.68   ? 116 ALA B CB  1 
ATOM   3229 N  N   . GLU B 1 117 ? 20.760  -27.856 -30.670 1.00 7.22   ? 117 GLU B N   1 
ATOM   3230 C  CA  . GLU B 1 117 ? 21.292  -26.828 -31.549 1.00 6.72   ? 117 GLU B CA  1 
ATOM   3231 C  C   . GLU B 1 117 ? 21.450  -25.547 -30.703 1.00 6.86   ? 117 GLU B C   1 
ATOM   3232 O  O   . GLU B 1 117 ? 20.548  -25.145 -29.967 1.00 8.14   ? 117 GLU B O   1 
ATOM   3233 C  CB  . GLU B 1 117 ? 20.321  -26.599 -32.739 1.00 7.65   ? 117 GLU B CB  1 
ATOM   3234 C  CG  . GLU B 1 117 ? 20.829  -25.621 -33.765 1.00 8.18   ? 117 GLU B CG  1 
ATOM   3235 C  CD  . GLU B 1 117 ? 19.935  -25.560 -35.018 1.00 6.88   ? 117 GLU B CD  1 
ATOM   3236 O  OE1 . GLU B 1 117 ? 19.276  -26.587 -35.297 1.00 8.19   ? 117 GLU B OE1 1 
ATOM   3237 O  OE2 . GLU B 1 117 ? 19.901  -24.486 -35.671 1.00 7.72   ? 117 GLU B OE2 1 
ATOM   3238 N  N   . LEU B 1 118 ? 22.651  -24.964 -30.814 1.00 6.71   ? 118 LEU B N   1 
ATOM   3239 C  CA  . LEU B 1 118 ? 23.017  -23.729 -30.157 1.00 6.73   ? 118 LEU B CA  1 
ATOM   3240 C  C   . LEU B 1 118 ? 22.807  -22.574 -31.146 1.00 6.77   ? 118 LEU B C   1 
ATOM   3241 O  O   . LEU B 1 118 ? 23.227  -22.653 -32.303 1.00 6.57   ? 118 LEU B O   1 
ATOM   3242 C  CB  . LEU B 1 118 ? 24.517  -23.807 -29.804 1.00 7.89   ? 118 LEU B CB  1 
ATOM   3243 C  CG  . LEU B 1 118 ? 25.257  -22.542 -29.425 1.00 8.13   ? 118 LEU B CG  1 
ATOM   3244 C  CD1 . LEU B 1 118 ? 24.666  -21.840 -28.210 1.00 9.56   ? 118 LEU B CD1 1 
ATOM   3245 C  CD2 . LEU B 1 118 ? 26.712  -22.836 -29.143 1.00 10.29  ? 118 LEU B CD2 1 
ATOM   3246 N  N   . HIS B 1 119 ? 22.174  -21.505 -30.653 1.00 6.63   ? 119 HIS B N   1 
ATOM   3247 C  CA  . HIS B 1 119 ? 21.935  -20.298 -31.417 1.00 6.64   ? 119 HIS B CA  1 
ATOM   3248 C  C   . HIS B 1 119 ? 22.600  -19.114 -30.756 1.00 6.57   ? 119 HIS B C   1 
ATOM   3249 O  O   . HIS B 1 119 ? 22.218  -18.759 -29.627 1.00 7.59   ? 119 HIS B O   1 
ATOM   3250 C  CB  . HIS B 1 119 ? 20.413  -20.007 -31.541 1.00 7.14   ? 119 HIS B CB  1 
ATOM   3251 C  CG  . HIS B 1 119 ? 19.728  -21.000 -32.425 1.00 6.48   ? 119 HIS B CG  1 
ATOM   3252 N  ND1 . HIS B 1 119 ? 18.366  -21.228 -32.414 1.00 6.60   ? 119 HIS B ND1 1 
ATOM   3253 C  CD2 . HIS B 1 119 ? 20.297  -21.828 -33.395 1.00 6.95   ? 119 HIS B CD2 1 
ATOM   3254 C  CE1 . HIS B 1 119 ? 18.105  -22.163 -33.319 1.00 7.00   ? 119 HIS B CE1 1 
ATOM   3255 N  NE2 . HIS B 1 119 ? 19.247  -22.515 -33.947 1.00 6.94   ? 119 HIS B NE2 1 
ATOM   3256 N  N   . LEU B 1 120 ? 23.606  -18.524 -31.432 1.00 6.25   ? 120 LEU B N   1 
ATOM   3257 C  CA  . LEU B 1 120 ? 24.236  -17.269 -30.981 1.00 7.07   ? 120 LEU B CA  1 
ATOM   3258 C  C   . LEU B 1 120 ? 23.618  -16.151 -31.783 1.00 6.10   ? 120 LEU B C   1 
ATOM   3259 O  O   . LEU B 1 120 ? 23.730  -16.123 -33.004 1.00 6.95   ? 120 LEU B O   1 
ATOM   3260 C  CB  . LEU B 1 120 ? 25.748  -17.367 -31.195 1.00 7.76   ? 120 LEU B CB  1 
ATOM   3261 C  CG  . LEU B 1 120 ? 26.429  -18.464 -30.319 1.00 9.47   ? 120 LEU B CG  1 
ATOM   3262 C  CD1 . LEU B 1 120 ? 27.302  -19.344 -31.133 1.00 12.64  ? 120 LEU B CD1 1 
ATOM   3263 C  CD2 . LEU B 1 120 ? 27.257  -17.788 -29.225 1.00 11.91  ? 120 LEU B CD2 1 
ATOM   3264 N  N   . VAL B 1 121 ? 22.909  -15.277 -31.076 1.00 6.74   ? 121 VAL B N   1 
ATOM   3265 C  CA  . VAL B 1 121 ? 22.047  -14.259 -31.708 1.00 7.39   ? 121 VAL B CA  1 
ATOM   3266 C  C   . VAL B 1 121 ? 22.755  -12.921 -31.726 1.00 7.23   ? 121 VAL B C   1 
ATOM   3267 O  O   . VAL B 1 121 ? 23.155  -12.435 -30.648 1.00 8.03   ? 121 VAL B O   1 
ATOM   3268 C  CB  . VAL B 1 121 ? 20.725  -14.170 -30.886 1.00 7.44   ? 121 VAL B CB  1 
ATOM   3269 C  CG1 . VAL B 1 121 ? 19.785  -13.138 -31.512 1.00 8.99   ? 121 VAL B CG1 1 
ATOM   3270 C  CG2 . VAL B 1 121 ? 20.049  -15.541 -30.735 1.00 8.38   ? 121 VAL B CG2 1 
ATOM   3271 N  N   . HIS B 1 122 ? 22.814  -12.302 -32.890 1.00 6.85   ? 122 HIS B N   1 
ATOM   3272 C  CA  . HIS B 1 122 ? 23.495  -11.068 -33.089 1.00 7.24   ? 122 HIS B CA  1 
ATOM   3273 C  C   . HIS B 1 122 ? 22.620  -10.070 -33.833 1.00 7.07   ? 122 HIS B C   1 
ATOM   3274 O  O   . HIS B 1 122 ? 21.887  -10.473 -34.729 1.00 8.28   ? 122 HIS B O   1 
ATOM   3275 C  CB  . HIS B 1 122 ? 24.789  -11.249 -33.921 1.00 8.19   ? 122 HIS B CB  1 
ATOM   3276 C  CG  . HIS B 1 122 ? 25.658  -12.384 -33.516 1.00 7.24   ? 122 HIS B CG  1 
ATOM   3277 N  ND1 . HIS B 1 122 ? 25.354  -13.696 -33.777 1.00 7.64   ? 122 HIS B ND1 1 
ATOM   3278 C  CD2 . HIS B 1 122 ? 26.886  -12.419 -32.894 1.00 8.62   ? 122 HIS B CD2 1 
ATOM   3279 C  CE1 . HIS B 1 122 ? 26.353  -14.469 -33.327 1.00 8.55   ? 122 HIS B CE1 1 
ATOM   3280 N  NE2 . HIS B 1 122 ? 27.280  -13.731 -32.788 1.00 8.80   ? 122 HIS B NE2 1 
ATOM   3281 N  N   . TRP B 1 123 ? 22.743  -8.780  -33.518 1.00 7.45   ? 123 TRP B N   1 
ATOM   3282 C  CA  . TRP B 1 123 ? 21.935  -7.770  -34.234 1.00 7.88   ? 123 TRP B CA  1 
ATOM   3283 C  C   . TRP B 1 123 ? 22.859  -6.785  -34.970 1.00 7.64   ? 123 TRP B C   1 
ATOM   3284 O  O   . TRP B 1 123 ? 23.973  -6.472  -34.569 1.00 8.52   ? 123 TRP B O   1 
ATOM   3285 C  CB  . TRP B 1 123 ? 21.005  -7.014  -33.272 1.00 9.88   ? 123 TRP B CB  1 
ATOM   3286 C  CG  . TRP B 1 123 ? 21.670  -6.371  -32.087 1.00 9.66   ? 123 TRP B CG  1 
ATOM   3287 C  CD1 . TRP B 1 123 ? 21.909  -6.977  -30.862 1.00 10.35  ? 123 TRP B CD1 1 
ATOM   3288 C  CD2 . TRP B 1 123 ? 22.192  -5.046  -31.978 1.00 10.60  ? 123 TRP B CD2 1 
ATOM   3289 N  NE1 . TRP B 1 123 ? 22.512  -6.125  -30.006 1.00 10.95  ? 123 TRP B NE1 1 
ATOM   3290 C  CE2 . TRP B 1 123 ? 22.776  -4.926  -30.637 1.00 11.51  ? 123 TRP B CE2 1 
ATOM   3291 C  CE3 . TRP B 1 123 ? 22.251  -3.934  -32.817 1.00 10.88  ? 123 TRP B CE3 1 
ATOM   3292 C  CZ2 . TRP B 1 123 ? 23.318  -3.743  -30.148 1.00 13.78  ? 123 TRP B CZ2 1 
ATOM   3293 C  CZ3 . TRP B 1 123 ? 22.839  -2.741  -32.338 1.00 13.10  ? 123 TRP B CZ3 1 
ATOM   3294 C  CH2 . TRP B 1 123 ? 23.368  -2.678  -31.033 1.00 14.22  ? 123 TRP B CH2 1 
ATOM   3295 N  N   . ASN B 1 124 ? 22.318  -6.357  -36.127 1.00 8.37   ? 124 ASN B N   1 
ATOM   3296 C  CA  . ASN B 1 124 ? 23.069  -5.458  -37.011 1.00 8.68   ? 124 ASN B CA  1 
ATOM   3297 C  C   . ASN B 1 124 ? 23.223  -4.080  -36.438 1.00 8.71   ? 124 ASN B C   1 
ATOM   3298 O  O   . ASN B 1 124 ? 22.210  -3.374  -36.163 1.00 9.16   ? 124 ASN B O   1 
ATOM   3299 C  CB  . ASN B 1 124 ? 22.257  -5.381  -38.314 1.00 9.26   ? 124 ASN B CB  1 
ATOM   3300 C  CG  . ASN B 1 124 ? 23.047  -4.798  -39.432 1.00 9.70   ? 124 ASN B CG  1 
ATOM   3301 O  OD1 . ASN B 1 124 ? 23.884  -3.909  -39.243 1.00 10.98  ? 124 ASN B OD1 1 
ATOM   3302 N  ND2 . ASN B 1 124 ? 22.752  -5.251  -40.655 1.00 11.61  ? 124 ASN B ND2 1 
ATOM   3303 N  N   . THR B 1 125 ? 24.479  -3.662  -36.216 1.00 9.64   ? 125 THR B N   1 
ATOM   3304 C  CA  . THR B 1 125 ? 24.720  -2.379  -35.534 1.00 11.04  ? 125 THR B CA  1 
ATOM   3305 C  C   . THR B 1 125 ? 24.198  -1.182  -36.286 1.00 10.72  ? 125 THR B C   1 
ATOM   3306 O  O   . THR B 1 125 ? 24.027  -0.135  -35.684 1.00 11.95  ? 125 THR B O   1 
ATOM   3307 C  CB  . THR B 1 125 ? 26.216  -2.234  -35.183 1.00 14.01  ? 125 THR B CB  1 
ATOM   3308 O  OG1 . THR B 1 125 ? 26.984  -2.276  -36.386 1.00 18.81  ? 125 THR B OG1 1 
ATOM   3309 C  CG2 . THR B 1 125 ? 26.626  -3.339  -34.229 1.00 16.20  ? 125 THR B CG2 1 
ATOM   3310 N  N   . LYS B 1 126 ? 23.874  -1.347  -37.625 1.00 10.80  ? 127 LYS B N   1 
ATOM   3311 C  CA  . LYS B 1 126 ? 23.343  -0.200  -38.344 1.00 12.09  ? 127 LYS B CA  1 
ATOM   3312 C  C   . LYS B 1 126 ? 21.926  0.171   -37.852 1.00 12.12  ? 127 LYS B C   1 
ATOM   3313 O  O   . LYS B 1 126 ? 21.419  1.261   -38.216 1.00 13.77  ? 127 LYS B O   1 
ATOM   3314 C  CB  . LYS B 1 126 ? 23.466  -0.431  -39.812 1.00 14.28  ? 127 LYS B CB  1 
ATOM   3315 C  CG  . LYS B 1 126 ? 22.377  -1.252  -40.395 1.00 13.93  ? 127 LYS B CG  1 
ATOM   3316 C  CD  . LYS B 1 126 ? 22.844  -1.673  -41.801 1.00 20.09  ? 127 LYS B CD  1 
ATOM   3317 C  CE  . LYS B 1 126 ? 21.841  -2.337  -42.648 1.00 26.71  ? 127 LYS B CE  1 
ATOM   3318 N  NZ  . LYS B 1 126 ? 21.078  -1.268  -43.328 1.00 47.71  ? 127 LYS B NZ  1 
ATOM   3319 N  N   . TYR B 1 127 ? 21.282  -0.670  -37.060 1.00 10.56  ? 128 TYR B N   1 
ATOM   3320 C  CA  . TYR B 1 127 ? 19.922  -0.361  -36.569 1.00 10.11  ? 128 TYR B CA  1 
ATOM   3321 C  C   . TYR B 1 127 ? 19.934  0.012   -35.106 1.00 11.10  ? 128 TYR B C   1 
ATOM   3322 O  O   . TYR B 1 127 ? 18.839  0.249   -34.549 1.00 11.63  ? 128 TYR B O   1 
ATOM   3323 C  CB  . TYR B 1 127 ? 18.963  -1.507  -36.842 1.00 12.02  ? 128 TYR B CB  1 
ATOM   3324 C  CG  . TYR B 1 127 ? 18.812  -1.847  -38.292 1.00 10.23  ? 128 TYR B CG  1 
ATOM   3325 C  CD1 . TYR B 1 127 ? 18.496  -0.846  -39.225 1.00 12.27  ? 128 TYR B CD1 1 
ATOM   3326 C  CD2 . TYR B 1 127 ? 19.178  -3.097  -38.788 1.00 10.45  ? 128 TYR B CD2 1 
ATOM   3327 C  CE1 . TYR B 1 127 ? 18.413  -1.134  -40.562 1.00 12.57  ? 128 TYR B CE1 1 
ATOM   3328 C  CE2 . TYR B 1 127 ? 19.058  -3.407  -40.119 1.00 9.93   ? 128 TYR B CE2 1 
ATOM   3329 C  CZ  . TYR B 1 127 ? 18.729  -2.405  -41.038 1.00 11.71  ? 128 TYR B CZ  1 
ATOM   3330 O  OH  . TYR B 1 127 ? 18.628  -2.639  -42.352 1.00 13.79  ? 128 TYR B OH  1 
ATOM   3331 N  N   . GLY B 1 128 ? 21.091  0.111   -34.456 1.00 10.60  ? 129 GLY B N   1 
ATOM   3332 C  CA  . GLY B 1 128 ? 21.241  0.769   -33.161 1.00 12.11  ? 129 GLY B CA  1 
ATOM   3333 C  C   . GLY B 1 128 ? 20.846  -0.062  -31.937 1.00 11.38  ? 129 GLY B C   1 
ATOM   3334 O  O   . GLY B 1 128 ? 21.514  0.065   -30.899 1.00 13.23  ? 129 GLY B O   1 
ATOM   3335 N  N   . ASP B 1 129 ? 19.824  -0.917  -32.016 1.00 11.49  ? 130 ASP B N   1 
ATOM   3336 C  CA  . ASP B 1 129 ? 19.579  -1.840  -30.910 1.00 13.50  ? 130 ASP B CA  1 
ATOM   3337 C  C   . ASP B 1 129 ? 18.814  -3.050  -31.456 1.00 12.68  ? 130 ASP B C   1 
ATOM   3338 O  O   . ASP B 1 129 ? 18.330  -3.060  -32.619 1.00 13.63  ? 130 ASP B O   1 
ATOM   3339 C  CB  . ASP B 1 129 ? 18.997  -1.240  -29.695 1.00 16.12  ? 130 ASP B CB  1 
ATOM   3340 C  CG  . ASP B 1 129 ? 17.582  -0.781  -29.905 1.00 14.39  ? 130 ASP B CG  1 
ATOM   3341 O  OD1 . ASP B 1 129 ? 16.970  -1.059  -30.945 1.00 22.27  ? 130 ASP B OD1 1 
ATOM   3342 O  OD2 . ASP B 1 129 ? 17.086  -0.128  -28.987 1.00 21.07  ? 130 ASP B OD2 1 
ATOM   3343 N  N   . PHE B 1 130 ? 18.676  -4.081  -30.634 1.00 12.13  ? 131 PHE B N   1 
ATOM   3344 C  CA  . PHE B 1 130 ? 18.018  -5.322  -31.045 1.00 10.50  ? 131 PHE B CA  1 
ATOM   3345 C  C   . PHE B 1 130 ? 16.544  -5.037  -31.418 1.00 10.96  ? 131 PHE B C   1 
ATOM   3346 O  O   . PHE B 1 130 ? 16.022  -5.612  -32.404 1.00 11.12  ? 131 PHE B O   1 
ATOM   3347 C  CB  . PHE B 1 130 ? 18.072  -6.315  -29.876 1.00 11.26  ? 131 PHE B CB  1 
ATOM   3348 C  CG  . PHE B 1 130 ? 17.395  -7.606  -30.156 1.00 10.50  ? 131 PHE B CG  1 
ATOM   3349 C  CD1 . PHE B 1 130 ? 18.043  -8.637  -30.784 1.00 10.90  ? 131 PHE B CD1 1 
ATOM   3350 C  CD2 . PHE B 1 130 ? 16.046  -7.793  -29.787 1.00 12.85  ? 131 PHE B CD2 1 
ATOM   3351 C  CE1 . PHE B 1 130 ? 17.448  -9.849  -31.038 1.00 12.83  ? 131 PHE B CE1 1 
ATOM   3352 C  CE2 . PHE B 1 130 ? 15.419  -9.016  -30.043 1.00 14.30  ? 131 PHE B CE2 1 
ATOM   3353 C  CZ  . PHE B 1 130 ? 16.135  -10.048 -30.699 1.00 14.28  ? 131 PHE B CZ  1 
ATOM   3354 N  N   . GLY B 1 131 ? 15.807  -4.246  -30.609 1.00 13.47  ? 132 GLY B N   1 
ATOM   3355 C  CA  . GLY B 1 131 ? 14.371  -4.102  -30.877 1.00 14.32  ? 132 GLY B CA  1 
ATOM   3356 C  C   . GLY B 1 131 ? 14.096  -3.418  -32.209 1.00 14.52  ? 132 GLY B C   1 
ATOM   3357 O  O   . GLY B 1 131 ? 13.100  -3.723  -32.845 1.00 14.58  ? 132 GLY B O   1 
ATOM   3358 N  N   . LYS B 1 132 ? 14.962  -2.533  -32.679 1.00 13.50  ? 133 LYS B N   1 
ATOM   3359 C  CA  . LYS B 1 132 ? 14.800  -1.969  -34.023 1.00 12.57  ? 133 LYS B CA  1 
ATOM   3360 C  C   . LYS B 1 132 ? 15.313  -2.940  -35.077 1.00 11.06  ? 133 LYS B C   1 
ATOM   3361 O  O   . LYS B 1 132 ? 14.711  -3.048  -36.170 1.00 11.62  ? 133 LYS B O   1 
ATOM   3362 C  CB  . LYS B 1 132 ? 15.551  -0.651  -34.125 1.00 13.75  ? 133 LYS B CB  1 
ATOM   3363 C  CG  . LYS B 1 132 ? 14.852  0.468   -33.394 1.00 17.91  ? 133 LYS B CG  1 
ATOM   3364 C  CD  . LYS B 1 132 ? 13.585  0.826   -34.127 1.00 24.05  ? 133 LYS B CD  1 
ATOM   3365 C  CE  . LYS B 1 132 ? 13.295  2.312   -33.999 1.00 33.85  ? 133 LYS B CE  1 
ATOM   3366 N  NZ  . LYS B 1 132 ? 12.167  2.824   -34.814 1.00 40.13  ? 133 LYS B NZ  1 
ATOM   3367 N  N   . ALA B 1 133 ? 16.415  -3.659  -34.781 1.00 10.49  ? 134 ALA B N   1 
ATOM   3368 C  CA  . ALA B 1 133 ? 16.960  -4.591  -35.752 1.00 10.02  ? 134 ALA B CA  1 
ATOM   3369 C  C   . ALA B 1 133 ? 15.917  -5.668  -36.177 1.00 10.16  ? 134 ALA B C   1 
ATOM   3370 O  O   . ALA B 1 133 ? 15.890  -6.068  -37.326 1.00 9.97   ? 134 ALA B O   1 
ATOM   3371 C  CB  . ALA B 1 133 ? 18.211  -5.236  -35.202 1.00 10.32  ? 134 ALA B CB  1 
ATOM   3372 N  N   . VAL B 1 134 ? 15.142  -6.160  -35.237 1.00 10.30  ? 135 VAL B N   1 
ATOM   3373 C  CA  . VAL B 1 134 ? 14.229  -7.294  -35.597 1.00 11.80  ? 135 VAL B CA  1 
ATOM   3374 C  C   . VAL B 1 134 ? 13.125  -6.876  -36.518 1.00 11.12  ? 135 VAL B C   1 
ATOM   3375 O  O   . VAL B 1 134 ? 12.397  -7.746  -37.073 1.00 12.36  ? 135 VAL B O   1 
ATOM   3376 C  CB  . VAL B 1 134 ? 13.581  -7.937  -34.390 1.00 14.28  ? 135 VAL B CB  1 
ATOM   3377 C  CG1 . VAL B 1 134 ? 14.591  -8.640  -33.553 1.00 14.93  ? 135 VAL B CG1 1 
ATOM   3378 C  CG2 . VAL B 1 134 ? 12.770  -6.997  -33.525 1.00 13.39  ? 135 VAL B CG2 1 
ATOM   3379 N  N   . GLN B 1 135 ? 12.984  -5.539  -36.727 1.00 10.98  ? 136 GLN B N   1 
ATOM   3380 C  CA  . GLN B 1 135 ? 11.966  -5.057  -37.686 1.00 11.92  ? 136 GLN B CA  1 
ATOM   3381 C  C   . GLN B 1 135 ? 12.533  -4.949  -39.090 1.00 11.92  ? 136 GLN B C   1 
ATOM   3382 O  O   . GLN B 1 135 ? 11.850  -4.398  -40.011 1.00 14.82  ? 136 GLN B O   1 
ATOM   3383 C  CB  . GLN B 1 135 ? 11.448  -3.696  -37.180 1.00 13.67  ? 136 GLN B CB  1 
ATOM   3384 C  CG  . GLN B 1 135 ? 10.780  -3.803  -35.842 1.00 16.87  ? 136 GLN B CG  1 
ATOM   3385 C  CD  . GLN B 1 135 ? 10.313  -2.432  -35.352 1.00 19.92  ? 136 GLN B CD  1 
ATOM   3386 O  OE1 . GLN B 1 135 ? 9.508   -1.761  -36.027 1.00 29.04  ? 136 GLN B OE1 1 
ATOM   3387 N  NE2 . GLN B 1 135 ? 10.836  -1.988  -34.180 1.00 20.67  ? 136 GLN B NE2 1 
ATOM   3388 N  N   . GLN B 1 136 ? 13.767  -5.429  -39.297 1.00 10.51  ? 137 GLN B N   1 
ATOM   3389 C  CA  . GLN B 1 136 ? 14.449  -5.235  -40.604 1.00 11.00  ? 137 GLN B CA  1 
ATOM   3390 C  C   . GLN B 1 136 ? 14.743  -6.590  -41.213 1.00 10.61  ? 137 GLN B C   1 
ATOM   3391 O  O   . GLN B 1 136 ? 15.127  -7.498  -40.498 1.00 10.32  ? 137 GLN B O   1 
ATOM   3392 C  CB  . GLN B 1 136 ? 15.702  -4.418  -40.456 1.00 10.94  ? 137 GLN B CB  1 
ATOM   3393 C  CG  . GLN B 1 136 ? 15.603  -3.176  -39.637 1.00 15.23  ? 137 GLN B CG  1 
ATOM   3394 C  CD  . GLN B 1 136 ? 14.633  -2.210  -40.199 1.00 19.93  ? 137 GLN B CD  1 
ATOM   3395 O  OE1 . GLN B 1 136 ? 14.405  -2.145  -41.384 1.00 22.05  ? 137 GLN B OE1 1 
ATOM   3396 N  NE2 . GLN B 1 136 ? 13.993  -1.439  -39.343 1.00 31.45  ? 137 GLN B NE2 1 
ATOM   3397 N  N   . PRO B 1 137 ? 14.759  -6.707  -42.563 1.00 9.77   ? 138 PRO B N   1 
ATOM   3398 C  CA  . PRO B 1 137 ? 15.043  -8.023  -43.177 1.00 11.00  ? 138 PRO B CA  1 
ATOM   3399 C  C   . PRO B 1 137 ? 16.455  -8.490  -42.996 1.00 11.08  ? 138 PRO B C   1 
ATOM   3400 O  O   . PRO B 1 137 ? 16.655  -9.690  -43.107 1.00 14.34  ? 138 PRO B O   1 
ATOM   3401 C  CB  . PRO B 1 137 ? 14.707  -7.849  -44.665 1.00 14.61  ? 138 PRO B CB  1 
ATOM   3402 C  CG  . PRO B 1 137 ? 14.509  -6.451  -44.819 1.00 21.54  ? 138 PRO B CG  1 
ATOM   3403 C  CD  . PRO B 1 137 ? 14.257  -5.728  -43.525 1.00 13.93  ? 138 PRO B CD  1 
ATOM   3404 N  N   . ASP B 1 138 ? 17.386  -7.569  -42.727 1.00 9.97   ? 139 ASP B N   1 
ATOM   3405 C  CA  . ASP B 1 138 ? 18.785  -7.901  -42.444 1.00 9.95   ? 139 ASP B CA  1 
ATOM   3406 C  C   . ASP B 1 138 ? 19.132  -7.464  -41.037 1.00 8.77   ? 139 ASP B C   1 
ATOM   3407 O  O   . ASP B 1 138 ? 20.287  -7.072  -40.769 1.00 10.22  ? 139 ASP B O   1 
ATOM   3408 C  CB  . ASP B 1 138 ? 19.759  -7.286  -43.454 1.00 11.57  ? 139 ASP B CB  1 
ATOM   3409 C  CG  . ASP B 1 138 ? 19.648  -5.792  -43.535 1.00 12.11  ? 139 ASP B CG  1 
ATOM   3410 O  OD1 . ASP B 1 138 ? 18.718  -5.203  -42.917 1.00 12.44  ? 139 ASP B OD1 1 
ATOM   3411 O  OD2 . ASP B 1 138 ? 20.524  -5.211  -44.205 1.00 15.40  ? 139 ASP B OD2 1 
ATOM   3412 N  N   . GLY B 1 139 ? 18.199  -7.576  -40.104 1.00 8.47   ? 140 GLY B N   1 
ATOM   3413 C  CA  . GLY B 1 139 ? 18.455  -7.093  -38.771 1.00 8.52   ? 140 GLY B CA  1 
ATOM   3414 C  C   . GLY B 1 139 ? 19.274  -8.009  -37.883 1.00 7.38   ? 140 GLY B C   1 
ATOM   3415 O  O   . GLY B 1 139 ? 19.989  -7.509  -37.001 1.00 8.32   ? 140 GLY B O   1 
ATOM   3416 N  N   . LEU B 1 140 ? 19.142  -9.340  -38.060 1.00 7.81   ? 141 LEU B N   1 
ATOM   3417 C  CA  . LEU B 1 140 ? 19.834  -10.284 -37.171 1.00 7.40   ? 141 LEU B CA  1 
ATOM   3418 C  C   . LEU B 1 140 ? 20.644  -11.227 -37.975 1.00 7.24   ? 141 LEU B C   1 
ATOM   3419 O  O   . LEU B 1 140 ? 20.390  -11.528 -39.124 1.00 7.66   ? 141 LEU B O   1 
ATOM   3420 C  CB  . LEU B 1 140 ? 18.826  -11.150 -36.379 1.00 7.98   ? 141 LEU B CB  1 
ATOM   3421 C  CG  . LEU B 1 140 ? 17.897  -10.468 -35.361 1.00 10.30  ? 141 LEU B CG  1 
ATOM   3422 C  CD1 . LEU B 1 140 ? 17.216  -11.511 -34.485 1.00 9.95   ? 141 LEU B CD1 1 
ATOM   3423 C  CD2 . LEU B 1 140 ? 18.574  -9.395  -34.510 1.00 14.10  ? 141 LEU B CD2 1 
ATOM   3424 N  N   . ALA B 1 141 ? 21.706  -11.749 -37.314 1.00 7.02   ? 142 ALA B N   1 
ATOM   3425 C  CA  . ALA B 1 141 ? 22.504  -12.919 -37.832 1.00 7.16   ? 142 ALA B CA  1 
ATOM   3426 C  C   . ALA B 1 141 ? 22.527  -13.893 -36.684 1.00 7.01   ? 142 ALA B C   1 
ATOM   3427 O  O   . ALA B 1 141 ? 22.919  -13.539 -35.564 1.00 7.88   ? 142 ALA B O   1 
ATOM   3428 C  CB  . ALA B 1 141 ? 23.897  -12.483 -38.231 1.00 8.82   ? 142 ALA B CB  1 
ATOM   3429 N  N   . VAL B 1 142 ? 22.041  -15.123 -36.940 1.00 6.54   ? 143 VAL B N   1 
ATOM   3430 C  CA  . VAL B 1 142 ? 22.069  -16.160 -35.947 1.00 6.76   ? 143 VAL B CA  1 
ATOM   3431 C  C   . VAL B 1 142 ? 23.034  -17.206 -36.427 1.00 6.30   ? 143 VAL B C   1 
ATOM   3432 O  O   . VAL B 1 142 ? 22.914  -17.750 -37.540 1.00 7.13   ? 143 VAL B O   1 
ATOM   3433 C  CB  . VAL B 1 142 ? 20.689  -16.745 -35.552 1.00 7.10   ? 143 VAL B CB  1 
ATOM   3434 C  CG1 . VAL B 1 142 ? 20.849  -17.770 -34.449 1.00 8.05   ? 143 VAL B CG1 1 
ATOM   3435 C  CG2 . VAL B 1 142 ? 19.767  -15.622 -35.110 1.00 8.64   ? 143 VAL B CG2 1 
ATOM   3436 N  N   . LEU B 1 143 ? 24.018  -17.493 -35.564 1.00 6.96   ? 144 LEU B N   1 
ATOM   3437 C  CA  . LEU B 1 143 ? 25.005  -18.556 -35.817 1.00 6.77   ? 144 LEU B CA  1 
ATOM   3438 C  C   . LEU B 1 143 ? 24.491  -19.807 -35.125 1.00 6.59   ? 144 LEU B C   1 
ATOM   3439 O  O   . LEU B 1 143 ? 24.356  -19.830 -33.905 1.00 7.90   ? 144 LEU B O   1 
ATOM   3440 C  CB  . LEU B 1 143 ? 26.351  -18.086 -35.250 1.00 8.61   ? 144 LEU B CB  1 
ATOM   3441 C  CG  . LEU B 1 143 ? 27.506  -19.082 -35.404 1.00 9.43   ? 144 LEU B CG  1 
ATOM   3442 C  CD1 . LEU B 1 143 ? 27.766  -19.426 -36.859 1.00 11.29  ? 144 LEU B CD1 1 
ATOM   3443 C  CD2 . LEU B 1 143 ? 28.771  -18.514 -34.742 1.00 11.11  ? 144 LEU B CD2 1 
ATOM   3444 N  N   . GLY B 1 144 ? 24.223  -20.836 -35.933 1.00 6.63   ? 145 GLY B N   1 
ATOM   3445 C  CA  . GLY B 1 144 ? 23.676  -22.092 -35.427 1.00 7.06   ? 145 GLY B CA  1 
ATOM   3446 C  C   . GLY B 1 144 ? 24.752  -23.171 -35.471 1.00 6.23   ? 145 GLY B C   1 
ATOM   3447 O  O   . GLY B 1 144 ? 25.470  -23.316 -36.437 1.00 7.48   ? 145 GLY B O   1 
ATOM   3448 N  N   . ILE B 1 145 ? 24.811  -23.904 -34.360 1.00 6.62   ? 146 ILE B N   1 
ATOM   3449 C  CA  . ILE B 1 145 ? 25.842  -24.941 -34.162 1.00 6.62   ? 146 ILE B CA  1 
ATOM   3450 C  C   . ILE B 1 145 ? 25.140  -26.192 -33.635 1.00 6.72   ? 146 ILE B C   1 
ATOM   3451 O  O   . ILE B 1 145 ? 24.434  -26.141 -32.638 1.00 7.52   ? 146 ILE B O   1 
ATOM   3452 C  CB  . ILE B 1 145 ? 26.948  -24.447 -33.203 1.00 7.78   ? 146 ILE B CB  1 
ATOM   3453 C  CG1 . ILE B 1 145 ? 27.519  -23.116 -33.693 1.00 9.94   ? 146 ILE B CG1 1 
ATOM   3454 C  CG2 . ILE B 1 145 ? 27.992  -25.545 -32.991 1.00 9.92   ? 146 ILE B CG2 1 
ATOM   3455 C  CD1 . ILE B 1 145 ? 28.624  -22.560 -32.795 1.00 9.54   ? 146 ILE B CD1 1 
ATOM   3456 N  N   . PHE B 1 146 ? 25.309  -27.298 -34.357 1.00 6.89   ? 147 PHE B N   1 
ATOM   3457 C  CA  . PHE B 1 146 ? 24.710  -28.558 -33.915 1.00 7.01   ? 147 PHE B CA  1 
ATOM   3458 C  C   . PHE B 1 146 ? 25.476  -29.155 -32.763 1.00 7.05   ? 147 PHE B C   1 
ATOM   3459 O  O   . PHE B 1 146 ? 26.710  -29.033 -32.680 1.00 8.22   ? 147 PHE B O   1 
ATOM   3460 C  CB  . PHE B 1 146 ? 24.703  -29.525 -35.103 1.00 7.73   ? 147 PHE B CB  1 
ATOM   3461 C  CG  . PHE B 1 146 ? 23.847  -29.068 -36.239 1.00 6.71   ? 147 PHE B CG  1 
ATOM   3462 C  CD1 . PHE B 1 146 ? 22.478  -28.877 -36.063 1.00 7.36   ? 147 PHE B CD1 1 
ATOM   3463 C  CD2 . PHE B 1 146 ? 24.374  -28.847 -37.488 1.00 8.08   ? 147 PHE B CD2 1 
ATOM   3464 C  CE1 . PHE B 1 146 ? 21.651  -28.506 -37.132 1.00 7.92   ? 147 PHE B CE1 1 
ATOM   3465 C  CE2 . PHE B 1 146 ? 23.581  -28.469 -38.557 1.00 7.84   ? 147 PHE B CE2 1 
ATOM   3466 C  CZ  . PHE B 1 146 ? 22.220  -28.317 -38.400 1.00 7.36   ? 147 PHE B CZ  1 
ATOM   3467 N  N   . LEU B 1 147 ? 24.750  -29.896 -31.914 1.00 7.32   ? 148 LEU B N   1 
ATOM   3468 C  CA  . LEU B 1 147 ? 25.333  -30.673 -30.816 1.00 7.87   ? 148 LEU B CA  1 
ATOM   3469 C  C   . LEU B 1 147 ? 24.999  -32.150 -31.030 1.00 7.76   ? 148 LEU B C   1 
ATOM   3470 O  O   . LEU B 1 147 ? 23.831  -32.476 -31.268 1.00 7.81   ? 148 LEU B O   1 
ATOM   3471 C  CB  . LEU B 1 147 ? 24.733  -30.278 -29.473 1.00 8.57   ? 148 LEU B CB  1 
ATOM   3472 C  CG  . LEU B 1 147 ? 25.266  -29.017 -28.787 1.00 8.87   ? 148 LEU B CG  1 
ATOM   3473 C  CD1 . LEU B 1 147 ? 25.039  -27.754 -29.636 1.00 10.31  ? 148 LEU B CD1 1 
ATOM   3474 C  CD2 . LEU B 1 147 ? 24.683  -28.827 -27.415 1.00 10.36  ? 148 LEU B CD2 1 
ATOM   3475 N  N   . LYS B 1 148 ? 26.035  -32.979 -30.949 1.00 8.51   ? 149 LYS B N   1 
ATOM   3476 C  CA  . LYS B 1 148 ? 25.885  -34.443 -30.904 1.00 8.82   ? 149 LYS B CA  1 
ATOM   3477 C  C   . LYS B 1 148 ? 26.337  -34.915 -29.559 1.00 9.51   ? 149 LYS B C   1 
ATOM   3478 O  O   . LYS B 1 148 ? 27.179  -34.276 -28.901 1.00 10.95  ? 149 LYS B O   1 
ATOM   3479 C  CB  . LYS B 1 148 ? 26.615  -35.126 -32.039 1.00 10.65  ? 149 LYS B CB  1 
ATOM   3480 C  CG  . LYS B 1 148 ? 28.131  -34.991 -31.981 1.00 11.87  ? 149 LYS B CG  1 
ATOM   3481 C  CD  . LYS B 1 148 ? 28.736  -35.715 -33.151 1.00 18.53  ? 149 LYS B CD  1 
ATOM   3482 C  CE  . LYS B 1 148 ? 30.238  -35.759 -33.101 1.00 26.85  ? 149 LYS B CE  1 
ATOM   3483 N  NZ  . LYS B 1 148 ? 30.740  -36.719 -34.088 1.00 38.29  ? 149 LYS B NZ  1 
ATOM   3484 N  N   . VAL B 1 149 ? 25.843  -36.083 -29.118 1.00 10.05  ? 150 VAL B N   1 
ATOM   3485 C  CA  . VAL B 1 149 ? 26.229  -36.663 -27.837 1.00 10.33  ? 150 VAL B CA  1 
ATOM   3486 C  C   . VAL B 1 149 ? 27.438  -37.566 -28.048 1.00 10.97  ? 150 VAL B C   1 
ATOM   3487 O  O   . VAL B 1 149 ? 27.411  -38.526 -28.824 1.00 12.50  ? 150 VAL B O   1 
ATOM   3488 C  CB  . VAL B 1 149 ? 24.984  -37.403 -27.246 1.00 10.38  ? 150 VAL B CB  1 
ATOM   3489 C  CG1 . VAL B 1 149 ? 25.361  -38.182 -25.990 1.00 12.92  ? 150 VAL B CG1 1 
ATOM   3490 C  CG2 . VAL B 1 149 ? 23.927  -36.384 -26.891 1.00 13.79  ? 150 VAL B CG2 1 
ATOM   3491 N  N   . GLY B 1 150 ? 28.481  -37.312 -27.275 1.00 11.15  ? 151 GLY B N   1 
ATOM   3492 C  CA  . GLY B 1 150 ? 29.714  -38.116 -27.311 1.00 12.60  ? 151 GLY B CA  1 
ATOM   3493 C  C   . GLY B 1 150 ? 30.577  -37.638 -26.162 1.00 11.61  ? 151 GLY B C   1 
ATOM   3494 O  O   . GLY B 1 150 ? 30.224  -37.713 -25.018 1.00 12.79  ? 151 GLY B O   1 
ATOM   3495 N  N   A SER B 1 151 ? 31.758  -37.123 -26.506 0.50 12.50  ? 152 SER B N   1 
ATOM   3496 N  N   B SER B 1 151 ? 31.784  -37.149 -26.499 0.50 12.96  ? 152 SER B N   1 
ATOM   3497 C  CA  A SER B 1 151 ? 32.639  -36.511 -25.526 0.50 13.14  ? 152 SER B CA  1 
ATOM   3498 C  CA  B SER B 1 151 ? 32.691  -36.547 -25.521 0.50 14.04  ? 152 SER B CA  1 
ATOM   3499 C  C   A SER B 1 151 ? 32.026  -35.267 -24.927 0.50 11.91  ? 152 SER B C   1 
ATOM   3500 C  C   B SER B 1 151 ? 32.094  -35.265 -24.943 0.50 11.95  ? 152 SER B C   1 
ATOM   3501 O  O   A SER B 1 151 ? 31.264  -34.551 -25.598 0.50 12.90  ? 152 SER B O   1 
ATOM   3502 O  O   B SER B 1 151 ? 31.366  -34.542 -25.625 0.50 13.29  ? 152 SER B O   1 
ATOM   3503 C  CB  A SER B 1 151 ? 33.957  -36.119 -26.160 0.50 18.51  ? 152 SER B CB  1 
ATOM   3504 C  CB  B SER B 1 151 ? 34.045  -36.241 -26.150 0.50 20.43  ? 152 SER B CB  1 
ATOM   3505 O  OG  A SER B 1 151 ? 34.565  -37.255 -26.702 0.50 21.88  ? 152 SER B OG  1 
ATOM   3506 O  OG  B SER B 1 151 ? 33.927  -35.192 -27.079 0.50 25.71  ? 152 SER B OG  1 
ATOM   3507 N  N   . ALA B 1 152 ? 32.366  -34.960 -23.680 1.00 12.43  ? 153 ALA B N   1 
ATOM   3508 C  CA  . ALA B 1 152 ? 31.974  -33.697 -23.114 1.00 12.76  ? 153 ALA B CA  1 
ATOM   3509 C  C   . ALA B 1 152 ? 32.629  -32.499 -23.767 1.00 12.35  ? 153 ALA B C   1 
ATOM   3510 O  O   . ALA B 1 152 ? 33.729  -32.551 -24.293 1.00 14.52  ? 153 ALA B O   1 
ATOM   3511 C  CB  . ALA B 1 152 ? 32.294  -33.665 -21.567 1.00 14.05  ? 153 ALA B CB  1 
ATOM   3512 N  N   . LYS B 1 153 ? 31.904  -31.344 -23.687 1.00 13.05  ? 154 LYS B N   1 
ATOM   3513 C  CA  . LYS B 1 153 ? 32.395  -30.079 -24.191 1.00 13.00  ? 154 LYS B CA  1 
ATOM   3514 C  C   . LYS B 1 153 ? 32.821  -29.297 -22.902 1.00 13.13  ? 154 LYS B C   1 
ATOM   3515 O  O   . LYS B 1 153 ? 31.970  -28.838 -22.147 1.00 13.43  ? 154 LYS B O   1 
ATOM   3516 C  CB  . LYS B 1 153 ? 31.376  -29.302 -24.986 1.00 13.70  ? 154 LYS B CB  1 
ATOM   3517 C  CG  . LYS B 1 153 ? 31.966  -28.101 -25.687 1.00 17.33  ? 154 LYS B CG  1 
ATOM   3518 C  CD  . LYS B 1 153 ? 32.771  -28.491 -26.931 1.00 18.18  ? 154 LYS B CD  1 
ATOM   3519 C  CE  . LYS B 1 153 ? 32.850  -27.308 -27.858 1.00 21.35  ? 154 LYS B CE  1 
ATOM   3520 N  NZ  . LYS B 1 153 ? 33.733  -27.710 -28.977 1.00 21.65  ? 154 LYS B NZ  1 
ATOM   3521 N  N   . PRO B 1 154 ? 34.140  -29.216 -22.676 1.00 14.90  ? 155 PRO B N   1 
ATOM   3522 C  CA  . PRO B 1 154 ? 34.536  -28.632 -21.385 1.00 15.88  ? 155 PRO B CA  1 
ATOM   3523 C  C   . PRO B 1 154 ? 34.072  -27.183 -21.231 1.00 14.81  ? 155 PRO B C   1 
ATOM   3524 O  O   . PRO B 1 154 ? 33.657  -26.808 -20.130 1.00 17.41  ? 155 PRO B O   1 
ATOM   3525 C  CB  . PRO B 1 154 ? 36.063  -28.697 -21.423 1.00 17.58  ? 155 PRO B CB  1 
ATOM   3526 C  CG  . PRO B 1 154 ? 36.290  -29.870 -22.339 1.00 19.04  ? 155 PRO B CG  1 
ATOM   3527 C  CD  . PRO B 1 154 ? 35.284  -29.762 -23.432 1.00 16.60  ? 155 PRO B CD  1 
ATOM   3528 N  N   . GLY B 1 155 ? 33.973  -26.434 -22.328 1.00 14.11  ? 156 GLY B N   1 
ATOM   3529 C  CA  . GLY B 1 155 ? 33.568  -25.071 -22.237 1.00 15.88  ? 156 GLY B CA  1 
ATOM   3530 C  C   . GLY B 1 155 ? 32.073  -24.851 -22.039 1.00 16.20  ? 156 GLY B C   1 
ATOM   3531 O  O   . GLY B 1 155 ? 31.626  -23.737 -21.822 1.00 19.46  ? 156 GLY B O   1 
ATOM   3532 N  N   . LEU B 1 156 ? 31.326  -25.914 -22.053 1.00 13.90  ? 157 LEU B N   1 
ATOM   3533 C  CA  . LEU B 1 156 ? 29.897  -25.932 -21.758 1.00 13.15  ? 157 LEU B CA  1 
ATOM   3534 C  C   . LEU B 1 156 ? 29.596  -26.118 -20.272 1.00 13.84  ? 157 LEU B C   1 
ATOM   3535 O  O   . LEU B 1 156 ? 28.492  -25.827 -19.762 1.00 13.98  ? 157 LEU B O   1 
ATOM   3536 C  CB  . LEU B 1 156 ? 29.120  -26.968 -22.588 1.00 13.52  ? 157 LEU B CB  1 
ATOM   3537 C  CG  . LEU B 1 156 ? 27.573  -27.076 -22.427 1.00 13.71  ? 157 LEU B CG  1 
ATOM   3538 C  CD1 . LEU B 1 156 ? 26.879  -25.760 -22.787 1.00 15.80  ? 157 LEU B CD1 1 
ATOM   3539 C  CD2 . LEU B 1 156 ? 27.025  -28.186 -23.270 1.00 13.89  ? 157 LEU B CD2 1 
ATOM   3540 N  N   . GLN B 1 157 ? 30.573  -26.695 -19.521 1.00 14.75  ? 158 GLN B N   1 
ATOM   3541 C  CA  . GLN B 1 157 ? 30.255  -27.175 -18.159 1.00 15.93  ? 158 GLN B CA  1 
ATOM   3542 C  C   . GLN B 1 157 ? 29.818  -26.018 -17.273 1.00 15.76  ? 158 GLN B C   1 
ATOM   3543 O  O   . GLN B 1 157 ? 28.994  -26.226 -16.420 1.00 15.48  ? 158 GLN B O   1 
ATOM   3544 C  CB  . GLN B 1 157 ? 31.438  -27.975 -17.597 1.00 18.05  ? 158 GLN B CB  1 
ATOM   3545 C  CG  . GLN B 1 157 ? 31.036  -28.720 -16.330 1.00 18.27  ? 158 GLN B CG  1 
ATOM   3546 C  CD  . GLN B 1 157 ? 29.922  -29.706 -16.577 1.00 17.83  ? 158 GLN B CD  1 
ATOM   3547 O  OE1 . GLN B 1 157 ? 29.786  -30.270 -17.673 1.00 17.28  ? 158 GLN B OE1 1 
ATOM   3548 N  NE2 . GLN B 1 157 ? 29.130  -29.961 -15.509 1.00 18.97  ? 158 GLN B NE2 1 
ATOM   3549 N  N   . LYS B 1 158 ? 30.363  -24.796 -17.388 1.00 16.39  ? 159 LYS B N   1 
ATOM   3550 C  CA  . LYS B 1 158 ? 29.961  -23.681 -16.517 1.00 15.02  ? 159 LYS B CA  1 
ATOM   3551 C  C   . LYS B 1 158 ? 28.468  -23.388 -16.693 1.00 14.41  ? 159 LYS B C   1 
ATOM   3552 O  O   . LYS B 1 158 ? 27.798  -23.029 -15.738 1.00 18.24  ? 159 LYS B O   1 
ATOM   3553 C  CB  . LYS B 1 158 ? 30.845  -22.479 -16.768 1.00 19.64  ? 159 LYS B CB  1 
ATOM   3554 C  CG  . LYS B 1 158 ? 32.179  -22.708 -16.033 1.00 27.38  ? 159 LYS B CG  1 
ATOM   3555 C  CD  . LYS B 1 158 ? 33.028  -21.449 -16.021 1.00 50.58  ? 159 LYS B CD  1 
ATOM   3556 C  CE  . LYS B 1 158 ? 34.476  -21.681 -15.547 1.00 45.21  ? 159 LYS B CE  1 
ATOM   3557 N  NZ  . LYS B 1 158 ? 35.381  -20.488 -15.713 1.00 39.33  ? 159 LYS B NZ  1 
ATOM   3558 N  N   . VAL B 1 159 ? 28.000  -23.534 -17.919 1.00 15.81  ? 160 VAL B N   1 
ATOM   3559 C  CA  . VAL B 1 159 ? 26.571  -23.320 -18.173 1.00 14.41  ? 160 VAL B CA  1 
ATOM   3560 C  C   . VAL B 1 159 ? 25.758  -24.463 -17.506 1.00 14.41  ? 160 VAL B C   1 
ATOM   3561 O  O   . VAL B 1 159 ? 24.817  -24.228 -16.757 1.00 15.02  ? 160 VAL B O   1 
ATOM   3562 C  CB  . VAL B 1 159 ? 26.243  -23.329 -19.669 1.00 14.82  ? 160 VAL B CB  1 
ATOM   3563 C  CG1 . VAL B 1 159 ? 24.706  -23.374 -19.930 1.00 16.96  ? 160 VAL B CG1 1 
ATOM   3564 C  CG2 . VAL B 1 159 ? 26.868  -22.146 -20.324 1.00 18.34  ? 160 VAL B CG2 1 
ATOM   3565 N  N   . VAL B 1 160 ? 26.165  -25.726 -17.721 1.00 13.86  ? 161 VAL B N   1 
ATOM   3566 C  CA  . VAL B 1 160 ? 25.438  -26.850 -17.143 1.00 15.54  ? 161 VAL B CA  1 
ATOM   3567 C  C   . VAL B 1 160 ? 25.391  -26.742 -15.646 1.00 15.33  ? 161 VAL B C   1 
ATOM   3568 O  O   . VAL B 1 160 ? 24.344  -27.011 -15.057 1.00 17.16  ? 161 VAL B O   1 
ATOM   3569 C  CB  . VAL B 1 160 ? 26.189  -28.208 -17.546 1.00 19.53  ? 161 VAL B CB  1 
ATOM   3570 C  CG1 . VAL B 1 160 ? 25.772  -29.404 -16.675 1.00 20.01  ? 161 VAL B CG1 1 
ATOM   3571 C  CG2 . VAL B 1 160 ? 25.958  -28.390 -19.042 1.00 18.50  ? 161 VAL B CG2 1 
ATOM   3572 N  N   . ASP B 1 161 ? 26.463  -26.310 -14.994 1.00 17.74  ? 162 ASP B N   1 
ATOM   3573 C  CA  . ASP B 1 161 ? 26.478  -26.303 -13.519 1.00 20.62  ? 162 ASP B CA  1 
ATOM   3574 C  C   . ASP B 1 161 ? 25.560  -25.238 -12.888 1.00 16.72  ? 162 ASP B C   1 
ATOM   3575 O  O   . ASP B 1 161 ? 25.194  -25.388 -11.718 1.00 26.51  ? 162 ASP B O   1 
ATOM   3576 C  CB  . ASP B 1 161 ? 27.887  -26.210 -13.069 1.00 22.63  ? 162 ASP B CB  1 
ATOM   3577 C  CG  . ASP B 1 161 ? 28.589  -27.586 -13.134 1.00 22.04  ? 162 ASP B CG  1 
ATOM   3578 O  OD1 . ASP B 1 161 ? 27.894  -28.666 -13.120 1.00 26.25  ? 162 ASP B OD1 1 
ATOM   3579 O  OD2 . ASP B 1 161 ? 29.820  -27.568 -13.254 1.00 33.63  ? 162 ASP B OD2 1 
ATOM   3580 N  N   . VAL B 1 162 ? 25.138  -24.211 -13.634 1.00 17.70  ? 163 VAL B N   1 
ATOM   3581 C  CA  . VAL B 1 162 ? 24.338  -23.161 -13.072 1.00 20.29  ? 163 VAL B CA  1 
ATOM   3582 C  C   . VAL B 1 162 ? 22.845  -23.474 -13.274 1.00 17.91  ? 163 VAL B C   1 
ATOM   3583 O  O   . VAL B 1 162 ? 21.960  -22.812 -12.707 1.00 19.45  ? 163 VAL B O   1 
ATOM   3584 C  CB  . VAL B 1 162 ? 24.773  -21.770 -13.660 1.00 21.95  ? 163 VAL B CB  1 
ATOM   3585 C  CG1 . VAL B 1 162 ? 24.130  -21.532 -15.017 1.00 20.44  ? 163 VAL B CG1 1 
ATOM   3586 C  CG2 . VAL B 1 162 ? 24.421  -20.598 -12.798 1.00 22.58  ? 163 VAL B CG2 1 
ATOM   3587 N  N   . LEU B 1 163 ? 22.554  -24.482 -14.086 1.00 19.63  ? 164 LEU B N   1 
ATOM   3588 C  CA  . LEU B 1 163 ? 21.165  -24.735 -14.426 1.00 17.21  ? 164 LEU B CA  1 
ATOM   3589 C  C   . LEU B 1 163 ? 20.277  -25.102 -13.247 1.00 19.59  ? 164 LEU B C   1 
ATOM   3590 O  O   . LEU B 1 163 ? 19.100  -24.798 -13.213 1.00 18.08  ? 164 LEU B O   1 
ATOM   3591 C  CB  . LEU B 1 163 ? 20.995  -25.794 -15.551 1.00 16.02  ? 164 LEU B CB  1 
ATOM   3592 C  CG  . LEU B 1 163 ? 21.616  -25.421 -16.878 1.00 14.58  ? 164 LEU B CG  1 
ATOM   3593 C  CD1 . LEU B 1 163 ? 21.396  -26.588 -17.869 1.00 16.17  ? 164 LEU B CD1 1 
ATOM   3594 C  CD2 . LEU B 1 163 ? 21.075  -24.127 -17.435 1.00 15.34  ? 164 LEU B CD2 1 
ATOM   3595 N  N   . ASP B 1 164 ? 20.834  -25.795 -12.259 1.00 20.84  ? 165 ASP B N   1 
ATOM   3596 C  CA  . ASP B 1 164 ? 20.004  -26.101 -11.076 1.00 23.74  ? 165 ASP B CA  1 
ATOM   3597 C  C   . ASP B 1 164 ? 19.507  -24.811 -10.346 1.00 26.53  ? 165 ASP B C   1 
ATOM   3598 O  O   . ASP B 1 164 ? 18.504  -24.882 -9.585  1.00 32.16  ? 165 ASP B O   1 
ATOM   3599 C  CB  . ASP B 1 164 ? 20.776  -26.986 -10.098 1.00 30.85  ? 165 ASP B CB  1 
ATOM   3600 C  CG  . ASP B 1 164 ? 21.778  -26.185 -9.323  1.00 40.20  ? 165 ASP B CG  1 
ATOM   3601 O  OD1 . ASP B 1 164 ? 22.432  -25.291 -9.916  1.00 47.01  ? 165 ASP B OD1 1 
ATOM   3602 O  OD2 . ASP B 1 164 ? 21.885  -26.415 -8.106  1.00 84.28  ? 165 ASP B OD2 1 
ATOM   3603 N  N   . SER B 1 165 ? 20.188  -23.656 -10.550 1.00 21.26  ? 166 SER B N   1 
ATOM   3604 C  CA  . SER B 1 165 ? 19.779  -22.387 -9.923  1.00 21.93  ? 166 SER B CA  1 
ATOM   3605 C  C   . SER B 1 165 ? 18.768  -21.651 -10.727 1.00 18.33  ? 166 SER B C   1 
ATOM   3606 O  O   . SER B 1 165 ? 18.225  -20.650 -10.219 1.00 22.64  ? 166 SER B O   1 
ATOM   3607 C  CB  . SER B 1 165 ? 20.996  -21.520 -9.639  1.00 27.47  ? 166 SER B CB  1 
ATOM   3608 O  OG  . SER B 1 165 ? 21.419  -20.924 -10.835 1.00 28.47  ? 166 SER B OG  1 
ATOM   3609 N  N   . ILE B 1 166 ? 18.466  -22.138 -11.950 1.00 18.52  ? 167 ILE B N   1 
ATOM   3610 C  CA  . ILE B 1 166 ? 17.446  -21.467 -12.761 1.00 17.17  ? 167 ILE B CA  1 
ATOM   3611 C  C   . ILE B 1 166 ? 16.444  -22.514 -13.278 1.00 14.53  ? 167 ILE B C   1 
ATOM   3612 O  O   . ILE B 1 166 ? 16.007  -22.540 -14.446 1.00 16.11  ? 167 ILE B O   1 
ATOM   3613 C  CB  . ILE B 1 166 ? 18.017  -20.625 -13.928 1.00 16.36  ? 167 ILE B CB  1 
ATOM   3614 C  CG1 . ILE B 1 166 ? 18.929  -21.478 -14.835 1.00 15.87  ? 167 ILE B CG1 1 
ATOM   3615 C  CG2 . ILE B 1 166 ? 18.704  -19.395 -13.367 1.00 19.19  ? 167 ILE B CG2 1 
ATOM   3616 C  CD1 . ILE B 1 166 ? 18.881  -20.887 -16.236 1.00 14.75  ? 167 ILE B CD1 1 
ATOM   3617 N  N   . LYS B 1 167 ? 16.033  -23.393 -12.388 1.00 16.97  ? 168 LYS B N   1 
ATOM   3618 C  CA  . LYS B 1 167 ? 15.339  -24.594 -12.814 1.00 16.29  ? 168 LYS B CA  1 
ATOM   3619 C  C   . LYS B 1 167 ? 14.003  -24.214 -13.476 1.00 14.75  ? 168 LYS B C   1 
ATOM   3620 O  O   . LYS B 1 167 ? 13.502  -24.852 -14.434 1.00 15.18  ? 168 LYS B O   1 
ATOM   3621 C  CB  . LYS B 1 167 ? 14.965  -25.506 -11.630 1.00 17.14  ? 168 LYS B CB  1 
ATOM   3622 C  CG  . LYS B 1 167 ? 14.183  -26.786 -12.061 1.00 17.22  ? 168 LYS B CG  1 
ATOM   3623 C  CD  . LYS B 1 167 ? 13.918  -27.710 -10.833 1.00 25.77  ? 168 LYS B CD  1 
ATOM   3624 C  CE  . LYS B 1 167 ? 13.269  -29.043 -11.216 1.00 30.14  ? 168 LYS B CE  1 
ATOM   3625 N  NZ  . LYS B 1 167 ? 13.146  -29.931 -10.008 1.00 31.28  ? 168 LYS B NZ  1 
ATOM   3626 N  N   . THR B 1 168 ? 13.385  -23.178 -12.948 1.00 16.24  ? 169 THR B N   1 
ATOM   3627 C  CA  . THR B 1 168 ? 11.978  -22.921 -13.315 1.00 16.64  ? 169 THR B CA  1 
ATOM   3628 C  C   . THR B 1 168 ? 11.859  -21.492 -13.981 1.00 16.42  ? 169 THR B C   1 
ATOM   3629 O  O   . THR B 1 168 ? 12.701  -20.613 -13.864 1.00 17.80  ? 169 THR B O   1 
ATOM   3630 C  CB  . THR B 1 168 ? 10.993  -22.925 -12.049 1.00 17.75  ? 169 THR B CB  1 
ATOM   3631 O  OG1 . THR B 1 168 ? 11.610  -22.146 -11.033 1.00 20.78  ? 169 THR B OG1 1 
ATOM   3632 C  CG2 . THR B 1 168 ? 10.816  -24.371 -11.621 1.00 20.08  ? 169 THR B CG2 1 
ATOM   3633 N  N   A LYS B 1 169 ? 10.773  -21.376 -14.708 0.50 19.20  ? 170 LYS B N   1 
ATOM   3634 N  N   B LYS B 1 169 ? 10.807  -21.384 -14.751 0.50 19.49  ? 170 LYS B N   1 
ATOM   3635 C  CA  A LYS B 1 169 ? 10.487  -20.174 -15.487 0.50 19.21  ? 170 LYS B CA  1 
ATOM   3636 C  CA  B LYS B 1 169 ? 10.572  -20.170 -15.519 0.50 17.43  ? 170 LYS B CA  1 
ATOM   3637 C  C   A LYS B 1 169 ? 10.527  -18.879 -14.710 0.50 17.60  ? 170 LYS B C   1 
ATOM   3638 C  C   B LYS B 1 169 ? 10.618  -18.913 -14.692 0.50 18.43  ? 170 LYS B C   1 
ATOM   3639 O  O   A LYS B 1 169 ? 9.904   -18.756 -13.642 0.50 23.08  ? 170 LYS B O   1 
ATOM   3640 O  O   B LYS B 1 169 ? 10.105  -18.842 -13.578 0.50 20.61  ? 170 LYS B O   1 
ATOM   3641 C  CB  A LYS B 1 169 ? 9.111   -20.318 -16.017 0.50 16.73  ? 170 LYS B CB  1 
ATOM   3642 C  CB  B LYS B 1 169 ? 9.204   -20.260 -16.109 0.50 16.62  ? 170 LYS B CB  1 
ATOM   3643 C  CG  A LYS B 1 169 ? 8.641   -19.052 -16.700 0.50 17.15  ? 170 LYS B CG  1 
ATOM   3644 C  CG  B LYS B 1 169 ? 8.796   -19.032 -16.960 0.50 22.27  ? 170 LYS B CG  1 
ATOM   3645 C  CD  A LYS B 1 169 ? 7.378   -19.293 -17.448 0.50 16.87  ? 170 LYS B CD  1 
ATOM   3646 C  CD  B LYS B 1 169 ? 7.468   -19.207 -17.683 0.50 22.16  ? 170 LYS B CD  1 
ATOM   3647 C  CE  A LYS B 1 169 ? 6.273   -19.503 -16.457 0.50 21.42  ? 170 LYS B CE  1 
ATOM   3648 C  CE  B LYS B 1 169 ? 6.976   -17.979 -18.464 0.50 28.62  ? 170 LYS B CE  1 
ATOM   3649 N  NZ  A LYS B 1 169 ? 5.152   -20.073 -17.194 0.50 24.15  ? 170 LYS B NZ  1 
ATOM   3650 N  NZ  B LYS B 1 169 ? 5.656   -18.350 -19.047 0.50 34.19  ? 170 LYS B NZ  1 
ATOM   3651 N  N   . GLY B 1 170 ? 11.307  -17.926 -15.241 1.00 19.28  ? 171 GLY B N   1 
ATOM   3652 C  CA  . GLY B 1 170 ? 11.574  -16.667 -14.503 1.00 16.78  ? 171 GLY B CA  1 
ATOM   3653 C  C   . GLY B 1 170 ? 12.720  -16.561 -13.584 1.00 19.49  ? 171 GLY B C   1 
ATOM   3654 O  O   . GLY B 1 170 ? 12.974  -15.419 -13.166 1.00 24.48  ? 171 GLY B O   1 
ATOM   3655 N  N   . LYS B 1 171 ? 13.321  -17.675 -13.235 1.00 19.06  ? 172 LYS B N   1 
ATOM   3656 C  CA  . LYS B 1 171 ? 14.584  -17.602 -12.482 1.00 19.40  ? 172 LYS B CA  1 
ATOM   3657 C  C   . LYS B 1 171 ? 15.748  -17.129 -13.382 1.00 18.43  ? 172 LYS B C   1 
ATOM   3658 O  O   . LYS B 1 171 ? 15.914  -17.521 -14.514 1.00 17.38  ? 172 LYS B O   1 
ATOM   3659 C  CB  . LYS B 1 171 ? 14.834  -18.940 -11.854 1.00 19.30  ? 172 LYS B CB  1 
ATOM   3660 C  CG  . LYS B 1 171 ? 13.739  -19.391 -10.906 1.00 22.41  ? 172 LYS B CG  1 
ATOM   3661 C  CD  . LYS B 1 171 ? 14.247  -20.442 -9.861  1.00 30.81  ? 172 LYS B CD  1 
ATOM   3662 C  CE  . LYS B 1 171 ? 13.572  -20.403 -8.485  1.00 37.21  ? 172 LYS B CE  1 
ATOM   3663 N  NZ  . LYS B 1 171 ? 13.657  -19.102 -7.756  1.00 40.54  ? 172 LYS B NZ  1 
ATOM   3664 N  N   . SER B 1 172 ? 16.560  -16.284 -12.808 1.00 19.48  ? 173 SER B N   1 
ATOM   3665 C  CA  . SER B 1 172 ? 17.795  -15.821 -13.395 1.00 20.38  ? 173 SER B CA  1 
ATOM   3666 C  C   . SER B 1 172 ? 18.989  -15.912 -12.416 1.00 17.58  ? 173 SER B C   1 
ATOM   3667 O  O   . SER B 1 172 ? 18.748  -15.980 -11.211 1.00 23.19  ? 173 SER B O   1 
ATOM   3668 C  CB  . SER B 1 172 ? 17.587  -14.422 -13.926 1.00 23.74  ? 173 SER B CB  1 
ATOM   3669 O  OG  . SER B 1 172 ? 17.219  -13.489 -12.925 1.00 27.36  ? 173 SER B OG  1 
ATOM   3670 N  N   . ALA B 1 173 ? 20.241  -15.844 -12.852 1.00 20.26  ? 174 ALA B N   1 
ATOM   3671 C  CA  . ALA B 1 173 ? 21.422  -15.862 -12.038 1.00 22.83  ? 174 ALA B CA  1 
ATOM   3672 C  C   . ALA B 1 173 ? 22.586  -15.058 -12.679 1.00 17.86  ? 174 ALA B C   1 
ATOM   3673 O  O   . ALA B 1 173 ? 22.740  -15.057 -13.943 1.00 16.53  ? 174 ALA B O   1 
ATOM   3674 C  CB  . ALA B 1 173 ? 21.826  -17.329 -11.815 1.00 27.78  ? 174 ALA B CB  1 
ATOM   3675 N  N   . ASP B 1 174 ? 23.308  -14.323 -11.889 1.00 24.14  ? 175 ASP B N   1 
ATOM   3676 C  CA  . ASP B 1 174 ? 24.562  -13.706 -12.454 1.00 22.83  ? 175 ASP B CA  1 
ATOM   3677 C  C   . ASP B 1 174 ? 25.348  -14.765 -13.154 1.00 19.38  ? 175 ASP B C   1 
ATOM   3678 O  O   . ASP B 1 174 ? 25.402  -15.909 -12.708 1.00 27.06  ? 175 ASP B O   1 
ATOM   3679 C  CB  . ASP B 1 174 ? 25.463  -13.089 -11.358 1.00 28.56  ? 175 ASP B CB  1 
ATOM   3680 C  CG  . ASP B 1 174 ? 24.720  -12.120 -10.531 1.00 33.14  ? 175 ASP B CG  1 
ATOM   3681 O  OD1 . ASP B 1 174 ? 24.079  -11.193 -11.077 1.00 40.52  ? 175 ASP B OD1 1 
ATOM   3682 O  OD2 . ASP B 1 174 ? 24.705  -12.319 -9.285  1.00 35.55  ? 175 ASP B OD2 1 
ATOM   3683 N  N   . PHE B 1 175 ? 25.897  -14.353 -14.291 1.00 18.79  ? 176 PHE B N   1 
ATOM   3684 C  CA  . PHE B 1 175 ? 26.644  -15.303 -15.097 1.00 18.79  ? 176 PHE B CA  1 
ATOM   3685 C  C   . PHE B 1 175 ? 27.654  -14.489 -15.853 1.00 18.47  ? 176 PHE B C   1 
ATOM   3686 O  O   . PHE B 1 175 ? 27.478  -14.227 -17.025 1.00 21.82  ? 176 PHE B O   1 
ATOM   3687 C  CB  . PHE B 1 175 ? 25.680  -16.120 -15.959 1.00 20.63  ? 176 PHE B CB  1 
ATOM   3688 C  CG  . PHE B 1 175 ? 26.289  -17.327 -16.494 1.00 19.20  ? 176 PHE B CG  1 
ATOM   3689 C  CD1 . PHE B 1 175 ? 26.622  -18.382 -15.673 1.00 20.03  ? 176 PHE B CD1 1 
ATOM   3690 C  CD2 . PHE B 1 175 ? 26.551  -17.468 -17.828 1.00 20.86  ? 176 PHE B CD2 1 
ATOM   3691 C  CE1 . PHE B 1 175 ? 27.206  -19.536 -16.149 1.00 22.70  ? 176 PHE B CE1 1 
ATOM   3692 C  CE2 . PHE B 1 175 ? 27.096  -18.647 -18.329 1.00 19.62  ? 176 PHE B CE2 1 
ATOM   3693 C  CZ  . PHE B 1 175 ? 27.454  -19.665 -17.486 1.00 20.59  ? 176 PHE B CZ  1 
ATOM   3694 N  N   . THR B 1 176 ? 28.658  -14.065 -15.151 1.00 17.75  ? 177 THR B N   1 
ATOM   3695 C  CA  . THR B 1 176 ? 29.723  -13.258 -15.738 1.00 17.81  ? 177 THR B CA  1 
ATOM   3696 C  C   . THR B 1 176 ? 30.922  -14.082 -16.139 1.00 15.88  ? 177 THR B C   1 
ATOM   3697 O  O   . THR B 1 176 ? 31.085  -15.259 -15.662 1.00 18.25  ? 177 THR B O   1 
ATOM   3698 C  CB  . THR B 1 176 ? 30.156  -12.197 -14.683 1.00 18.77  ? 177 THR B CB  1 
ATOM   3699 O  OG1 . THR B 1 176 ? 30.463  -12.824 -13.422 1.00 23.07  ? 177 THR B OG1 1 
ATOM   3700 C  CG2 . THR B 1 176 ? 29.014  -11.178 -14.528 1.00 25.69  ? 177 THR B CG2 1 
ATOM   3701 N  N   . ASN B 1 177 ? 31.737  -13.543 -17.042 1.00 16.78  ? 178 ASN B N   1 
ATOM   3702 C  CA  . ASN B 1 177 ? 32.983  -14.133 -17.468 1.00 18.38  ? 178 ASN B CA  1 
ATOM   3703 C  C   . ASN B 1 177 ? 32.856  -15.406 -18.203 1.00 17.75  ? 178 ASN B C   1 
ATOM   3704 O  O   . ASN B 1 177 ? 33.761  -16.183 -18.209 1.00 25.68  ? 178 ASN B O   1 
ATOM   3705 C  CB  . ASN B 1 177 ? 33.940  -14.199 -16.270 1.00 18.37  ? 178 ASN B CB  1 
ATOM   3706 C  CG  . ASN B 1 177 ? 34.209  -12.815 -15.689 1.00 18.02  ? 178 ASN B CG  1 
ATOM   3707 O  OD1 . ASN B 1 177 ? 34.842  -11.979 -16.323 1.00 23.32  ? 178 ASN B OD1 1 
ATOM   3708 N  ND2 . ASN B 1 177 ? 33.616  -12.537 -14.538 1.00 17.41  ? 178 ASN B ND2 1 
ATOM   3709 N  N   . PHE B 1 178 ? 31.683  -15.651 -18.817 1.00 16.28  ? 179 PHE B N   1 
ATOM   3710 C  CA  . PHE B 1 178 ? 31.520  -16.842 -19.620 1.00 17.24  ? 179 PHE B CA  1 
ATOM   3711 C  C   . PHE B 1 178 ? 32.058  -16.580 -20.991 1.00 13.02  ? 179 PHE B C   1 
ATOM   3712 O  O   . PHE B 1 178 ? 31.633  -15.599 -21.615 1.00 15.50  ? 179 PHE B O   1 
ATOM   3713 C  CB  . PHE B 1 178 ? 30.096  -17.317 -19.693 1.00 17.77  ? 179 PHE B CB  1 
ATOM   3714 C  CG  . PHE B 1 178 ? 29.982  -18.555 -20.526 1.00 14.87  ? 179 PHE B CG  1 
ATOM   3715 C  CD1 . PHE B 1 178 ? 30.309  -19.820 -19.968 1.00 17.05  ? 179 PHE B CD1 1 
ATOM   3716 C  CD2 . PHE B 1 178 ? 29.658  -18.497 -21.872 1.00 15.14  ? 179 PHE B CD2 1 
ATOM   3717 C  CE1 . PHE B 1 178 ? 30.298  -20.952 -20.717 1.00 19.63  ? 179 PHE B CE1 1 
ATOM   3718 C  CE2 . PHE B 1 178 ? 29.678  -19.685 -22.642 1.00 13.50  ? 179 PHE B CE2 1 
ATOM   3719 C  CZ  . PHE B 1 178 ? 29.967  -20.904 -22.094 1.00 16.00  ? 179 PHE B CZ  1 
ATOM   3720 N  N   . ASP B 1 179 ? 32.945  -17.438 -21.502 1.00 14.76  ? 180 ASP B N   1 
ATOM   3721 C  CA  . ASP B 1 179 ? 33.574  -17.230 -22.805 1.00 16.09  ? 180 ASP B CA  1 
ATOM   3722 C  C   . ASP B 1 179 ? 32.901  -18.112 -23.843 1.00 13.50  ? 180 ASP B C   1 
ATOM   3723 O  O   . ASP B 1 179 ? 33.125  -19.322 -23.887 1.00 13.72  ? 180 ASP B O   1 
ATOM   3724 C  CB  . ASP B 1 179 ? 35.070  -17.610 -22.691 1.00 17.64  ? 180 ASP B CB  1 
ATOM   3725 C  CG  . ASP B 1 179 ? 35.866  -17.212 -23.899 1.00 18.99  ? 180 ASP B CG  1 
ATOM   3726 O  OD1 . ASP B 1 179 ? 35.296  -16.962 -24.983 1.00 17.20  ? 180 ASP B OD1 1 
ATOM   3727 O  OD2 . ASP B 1 179 ? 37.064  -16.990 -23.760 1.00 26.87  ? 180 ASP B OD2 1 
ATOM   3728 N  N   . PRO B 1 180 ? 32.133  -17.497 -24.784 1.00 12.20  ? 181 PRO B N   1 
ATOM   3729 C  CA  . PRO B 1 180 ? 31.419  -18.362 -25.762 1.00 12.26  ? 181 PRO B CA  1 
ATOM   3730 C  C   . PRO B 1 180 ? 32.377  -18.967 -26.804 1.00 11.60  ? 181 PRO B C   1 
ATOM   3731 O  O   . PRO B 1 180 ? 31.930  -19.849 -27.554 1.00 11.69  ? 181 PRO B O   1 
ATOM   3732 C  CB  . PRO B 1 180 ? 30.434  -17.356 -26.401 1.00 13.56  ? 181 PRO B CB  1 
ATOM   3733 C  CG  . PRO B 1 180 ? 31.096  -16.007 -26.216 1.00 13.51  ? 181 PRO B CG  1 
ATOM   3734 C  CD  . PRO B 1 180 ? 31.749  -16.084 -24.841 1.00 13.42  ? 181 PRO B CD  1 
ATOM   3735 N  N   . ARG B 1 181 ? 33.677  -18.547 -26.847 1.00 11.93  ? 182 ARG B N   1 
ATOM   3736 C  CA  . ARG B 1 181 ? 34.611  -19.204 -27.757 1.00 12.56  ? 182 ARG B CA  1 
ATOM   3737 C  C   . ARG B 1 181 ? 34.684  -20.703 -27.426 1.00 14.17  ? 182 ARG B C   1 
ATOM   3738 O  O   . ARG B 1 181 ? 35.038  -21.533 -28.291 1.00 14.41  ? 182 ARG B O   1 
ATOM   3739 C  CB  . ARG B 1 181 ? 36.007  -18.580 -27.698 1.00 14.02  ? 182 ARG B CB  1 
ATOM   3740 C  CG  . ARG B 1 181 ? 35.953  -17.129 -28.224 1.00 15.58  ? 182 ARG B CG  1 
ATOM   3741 C  CD  . ARG B 1 181 ? 37.274  -16.449 -28.133 1.00 18.93  ? 182 ARG B CD  1 
ATOM   3742 N  NE  . ARG B 1 181 ? 37.684  -16.223 -26.746 1.00 20.09  ? 182 ARG B NE  1 
ATOM   3743 C  CZ  . ARG B 1 181 ? 38.769  -15.514 -26.420 1.00 23.80  ? 182 ARG B CZ  1 
ATOM   3744 N  NH1 . ARG B 1 181 ? 39.555  -14.997 -27.346 1.00 28.02  ? 182 ARG B NH1 1 
ATOM   3745 N  NH2 . ARG B 1 181 ? 39.078  -15.354 -25.150 1.00 28.42  ? 182 ARG B NH2 1 
ATOM   3746 N  N   . GLY B 1 182 ? 34.460  -21.066 -26.152 1.00 14.32  ? 183 GLY B N   1 
ATOM   3747 C  CA  . GLY B 1 182 ? 34.489  -22.492 -25.774 1.00 15.95  ? 183 GLY B CA  1 
ATOM   3748 C  C   . GLY B 1 182 ? 33.369  -23.332 -26.286 1.00 15.53  ? 183 GLY B C   1 
ATOM   3749 O  O   . GLY B 1 182 ? 33.384  -24.526 -25.999 1.00 18.77  ? 183 GLY B O   1 
ATOM   3750 N  N   . LEU B 1 183 ? 32.430  -22.749 -27.051 1.00 13.16  ? 184 LEU B N   1 
ATOM   3751 C  CA  . LEU B 1 183 ? 31.297  -23.489 -27.595 1.00 12.74  ? 184 LEU B CA  1 
ATOM   3752 C  C   . LEU B 1 183 ? 31.461  -23.711 -29.111 1.00 12.44  ? 184 LEU B C   1 
ATOM   3753 O  O   . LEU B 1 183 ? 30.539  -24.300 -29.734 1.00 13.29  ? 184 LEU B O   1 
ATOM   3754 C  CB  . LEU B 1 183 ? 29.977  -22.794 -27.329 1.00 12.97  ? 184 LEU B CB  1 
ATOM   3755 C  CG  . LEU B 1 183 ? 29.670  -22.663 -25.801 1.00 15.27  ? 184 LEU B CG  1 
ATOM   3756 C  CD1 . LEU B 1 183 ? 28.396  -21.849 -25.658 1.00 18.79  ? 184 LEU B CD1 1 
ATOM   3757 C  CD2 . LEU B 1 183 ? 29.572  -23.970 -25.043 1.00 18.79  ? 184 LEU B CD2 1 
ATOM   3758 N  N   . LEU B 1 184 ? 32.575  -23.253 -29.708 1.00 13.34  ? 185 LEU B N   1 
ATOM   3759 C  CA  . LEU B 1 184 ? 32.731  -23.310 -31.143 1.00 11.71  ? 185 LEU B CA  1 
ATOM   3760 C  C   . LEU B 1 184 ? 33.513  -24.554 -31.607 1.00 14.53  ? 185 LEU B C   1 
ATOM   3761 O  O   . LEU B 1 184 ? 34.497  -24.958 -30.993 1.00 22.48  ? 185 LEU B O   1 
ATOM   3762 C  CB  . LEU B 1 184 ? 33.512  -22.065 -31.679 1.00 11.42  ? 185 LEU B CB  1 
ATOM   3763 C  CG  . LEU B 1 184 ? 32.891  -20.728 -31.254 1.00 11.04  ? 185 LEU B CG  1 
ATOM   3764 C  CD1 . LEU B 1 184 ? 33.747  -19.618 -31.738 1.00 13.49  ? 185 LEU B CD1 1 
ATOM   3765 C  CD2 . LEU B 1 184 ? 31.492  -20.572 -31.859 1.00 12.81  ? 185 LEU B CD2 1 
ATOM   3766 N  N   . PRO B 1 185 ? 33.113  -25.133 -32.738 1.00 11.52  ? 186 PRO B N   1 
ATOM   3767 C  CA  . PRO B 1 185 ? 33.864  -26.271 -33.290 1.00 12.73  ? 186 PRO B CA  1 
ATOM   3768 C  C   . PRO B 1 185 ? 35.127  -25.721 -33.959 1.00 12.78  ? 186 PRO B C   1 
ATOM   3769 O  O   . PRO B 1 185 ? 35.314  -24.514 -34.077 1.00 16.22  ? 186 PRO B O   1 
ATOM   3770 C  CB  . PRO B 1 185 ? 32.897  -26.872 -34.345 1.00 12.23  ? 186 PRO B CB  1 
ATOM   3771 C  CG  . PRO B 1 185 ? 32.134  -25.649 -34.817 1.00 11.00  ? 186 PRO B CG  1 
ATOM   3772 C  CD  . PRO B 1 185 ? 31.958  -24.757 -33.575 1.00 9.94   ? 186 PRO B CD  1 
ATOM   3773 N  N   A GLU B 1 186 ? 35.914  -26.660 -34.443 0.50 14.18  ? 187 GLU B N   1 
ATOM   3774 N  N   B GLU B 1 186 ? 35.993  -26.637 -34.409 0.50 14.32  ? 187 GLU B N   1 
ATOM   3775 C  CA  A GLU B 1 186 ? 37.191  -26.303 -34.996 0.50 14.22  ? 187 GLU B CA  1 
ATOM   3776 C  CA  B GLU B 1 186 ? 37.236  -26.244 -35.121 0.50 15.22  ? 187 GLU B CA  1 
ATOM   3777 C  C   A GLU B 1 186 ? 37.049  -25.571 -36.360 0.50 14.36  ? 187 GLU B C   1 
ATOM   3778 C  C   B GLU B 1 186 ? 36.947  -25.428 -36.363 0.50 14.06  ? 187 GLU B C   1 
ATOM   3779 O  O   A GLU B 1 186 ? 37.794  -24.628 -36.638 0.50 21.75  ? 187 GLU B O   1 
ATOM   3780 O  O   B GLU B 1 186 ? 37.540  -24.355 -36.621 0.50 14.30  ? 187 GLU B O   1 
ATOM   3781 C  CB  A GLU B 1 186 ? 38.055  -27.532 -35.051 0.50 17.62  ? 187 GLU B CB  1 
ATOM   3782 C  CB  B GLU B 1 186 ? 38.014  -27.472 -35.590 0.50 18.90  ? 187 GLU B CB  1 
ATOM   3783 C  CG  A GLU B 1 186 ? 39.199  -27.380 -36.005 0.50 20.91  ? 187 GLU B CG  1 
ATOM   3784 C  CG  B GLU B 1 186 ? 38.932  -28.076 -34.570 0.50 17.48  ? 187 GLU B CG  1 
ATOM   3785 C  CD  A GLU B 1 186 ? 39.806  -28.707 -36.344 0.50 24.93  ? 187 GLU B CD  1 
ATOM   3786 C  CD  B GLU B 1 186 ? 39.514  -29.383 -35.044 0.50 19.81  ? 187 GLU B CD  1 
ATOM   3787 O  OE1 A GLU B 1 186 ? 39.664  -29.639 -35.504 0.50 23.81  ? 187 GLU B OE1 1 
ATOM   3788 O  OE1 B GLU B 1 186 ? 39.498  -29.646 -36.280 0.50 22.39  ? 187 GLU B OE1 1 
ATOM   3789 O  OE2 A GLU B 1 186 ? 40.392  -28.787 -37.450 0.50 27.75  ? 187 GLU B OE2 1 
ATOM   3790 O  OE2 B GLU B 1 186 ? 40.017  -30.118 -34.178 0.50 25.41  ? 187 GLU B OE2 1 
ATOM   3791 N  N   . SER B 1 187 ? 36.118  -25.995 -37.226 1.00 13.36  ? 188 SER B N   1 
ATOM   3792 C  CA  . SER B 1 187 ? 35.900  -25.399 -38.505 1.00 13.68  ? 188 SER B CA  1 
ATOM   3793 C  C   . SER B 1 187 ? 34.765  -24.391 -38.479 1.00 12.49  ? 188 SER B C   1 
ATOM   3794 O  O   . SER B 1 187 ? 33.728  -24.636 -37.847 1.00 13.51  ? 188 SER B O   1 
ATOM   3795 C  CB  . SER B 1 187 ? 35.453  -26.456 -39.494 1.00 15.44  ? 188 SER B CB  1 
ATOM   3796 O  OG  . SER B 1 187 ? 35.234  -25.898 -40.803 1.00 14.71  ? 188 SER B OG  1 
ATOM   3797 N  N   . LEU B 1 188 ? 34.945  -23.299 -39.201 1.00 12.37  ? 189 LEU B N   1 
ATOM   3798 C  CA  . LEU B 1 188 ? 33.874  -22.325 -39.414 1.00 12.87  ? 189 LEU B CA  1 
ATOM   3799 C  C   . LEU B 1 188 ? 33.211  -22.478 -40.802 1.00 11.48  ? 189 LEU B C   1 
ATOM   3800 O  O   . LEU B 1 188 ? 32.533  -21.582 -41.273 1.00 12.90  ? 189 LEU B O   1 
ATOM   3801 C  CB  . LEU B 1 188 ? 34.372  -20.909 -39.144 1.00 13.74  ? 189 LEU B CB  1 
ATOM   3802 C  CG  . LEU B 1 188 ? 34.774  -20.553 -37.713 1.00 16.34  ? 189 LEU B CG  1 
ATOM   3803 C  CD1 . LEU B 1 188 ? 35.292  -19.129 -37.590 1.00 19.52  ? 189 LEU B CD1 1 
ATOM   3804 C  CD2 . LEU B 1 188 ? 33.602  -20.810 -36.770 1.00 17.11  ? 189 LEU B CD2 1 
ATOM   3805 N  N   . ASP B 1 189 ? 33.382  -23.630 -41.484 1.00 11.68  ? 190 ASP B N   1 
ATOM   3806 C  CA  . ASP B 1 189 ? 32.617  -23.860 -42.708 1.00 11.78  ? 190 ASP B CA  1 
ATOM   3807 C  C   . ASP B 1 189 ? 31.097  -23.821 -42.424 1.00 10.06  ? 190 ASP B C   1 
ATOM   3808 O  O   . ASP B 1 189 ? 30.663  -24.356 -41.409 1.00 9.82   ? 190 ASP B O   1 
ATOM   3809 C  CB  . ASP B 1 189 ? 32.969  -25.173 -43.325 1.00 15.23  ? 190 ASP B CB  1 
ATOM   3810 C  CG  . ASP B 1 189 ? 34.339  -25.217 -43.952 1.00 20.96  ? 190 ASP B CG  1 
ATOM   3811 O  OD1 . ASP B 1 189 ? 35.008  -24.183 -44.154 1.00 24.87  ? 190 ASP B OD1 1 
ATOM   3812 O  OD2 . ASP B 1 189 ? 34.804  -26.350 -44.243 1.00 29.23  ? 190 ASP B OD2 1 
ATOM   3813 N  N   . TYR B 1 190 ? 30.322  -23.223 -43.332 1.00 9.97   ? 191 TYR B N   1 
ATOM   3814 C  CA  . TYR B 1 190 ? 28.902  -22.985 -43.009 1.00 9.22   ? 191 TYR B CA  1 
ATOM   3815 C  C   . TYR B 1 190 ? 28.042  -23.048 -44.266 1.00 8.67   ? 191 TYR B C   1 
ATOM   3816 O  O   . TYR B 1 190 ? 28.465  -22.927 -45.396 1.00 9.60   ? 191 TYR B O   1 
ATOM   3817 C  CB  . TYR B 1 190 ? 28.804  -21.599 -42.324 1.00 9.29   ? 191 TYR B CB  1 
ATOM   3818 C  CG  . TYR B 1 190 ? 29.152  -20.452 -43.217 1.00 9.58   ? 191 TYR B CG  1 
ATOM   3819 C  CD1 . TYR B 1 190 ? 28.221  -19.838 -44.102 1.00 10.28  ? 191 TYR B CD1 1 
ATOM   3820 C  CD2 . TYR B 1 190 ? 30.453  -19.919 -43.174 1.00 10.52  ? 191 TYR B CD2 1 
ATOM   3821 C  CE1 . TYR B 1 190 ? 28.636  -18.768 -44.910 1.00 11.20  ? 191 TYR B CE1 1 
ATOM   3822 C  CE2 . TYR B 1 190 ? 30.845  -18.837 -43.975 1.00 11.93  ? 191 TYR B CE2 1 
ATOM   3823 C  CZ  . TYR B 1 190 ? 29.977  -18.320 -44.858 1.00 10.81  ? 191 TYR B CZ  1 
ATOM   3824 O  OH  . TYR B 1 190 ? 30.316  -17.275 -45.695 1.00 13.04  ? 191 TYR B OH  1 
ATOM   3825 N  N   . TRP B 1 191 ? 26.739  -23.177 -43.952 1.00 8.19   ? 192 TRP B N   1 
ATOM   3826 C  CA  . TRP B 1 191 ? 25.653  -22.932 -44.890 1.00 8.14   ? 192 TRP B CA  1 
ATOM   3827 C  C   . TRP B 1 191 ? 24.951  -21.652 -44.465 1.00 7.64   ? 192 TRP B C   1 
ATOM   3828 O  O   . TRP B 1 191 ? 24.902  -21.287 -43.293 1.00 8.92   ? 192 TRP B O   1 
ATOM   3829 C  CB  . TRP B 1 191 ? 24.616  -24.048 -44.888 1.00 8.42   ? 192 TRP B CB  1 
ATOM   3830 C  CG  . TRP B 1 191 ? 25.127  -25.400 -45.302 1.00 9.02   ? 192 TRP B CG  1 
ATOM   3831 C  CD1 . TRP B 1 191 ? 25.363  -25.832 -46.571 1.00 9.92   ? 192 TRP B CD1 1 
ATOM   3832 C  CD2 . TRP B 1 191 ? 25.402  -26.530 -44.441 1.00 9.14   ? 192 TRP B CD2 1 
ATOM   3833 N  NE1 . TRP B 1 191 ? 25.756  -27.165 -46.560 1.00 11.63  ? 192 TRP B NE1 1 
ATOM   3834 C  CE2 . TRP B 1 191 ? 25.827  -27.607 -45.277 1.00 10.72  ? 192 TRP B CE2 1 
ATOM   3835 C  CE3 . TRP B 1 191 ? 25.331  -26.720 -43.056 1.00 9.57   ? 192 TRP B CE3 1 
ATOM   3836 C  CZ2 . TRP B 1 191 ? 26.126  -28.867 -44.736 1.00 10.99  ? 192 TRP B CZ2 1 
ATOM   3837 C  CZ3 . TRP B 1 191 ? 25.605  -27.977 -42.553 1.00 10.36  ? 192 TRP B CZ3 1 
ATOM   3838 C  CH2 . TRP B 1 191 ? 25.996  -29.020 -43.374 1.00 11.47  ? 192 TRP B CH2 1 
ATOM   3839 N  N   . THR B 1 192 ? 24.367  -20.930 -45.426 1.00 7.56   ? 193 THR B N   1 
ATOM   3840 C  CA  . THR B 1 192 ? 23.659  -19.716 -45.108 1.00 8.08   ? 193 THR B CA  1 
ATOM   3841 C  C   . THR B 1 192 ? 22.407  -19.556 -45.973 1.00 7.92   ? 193 THR B C   1 
ATOM   3842 O  O   . THR B 1 192 ? 22.406  -19.950 -47.142 1.00 8.73   ? 193 THR B O   1 
ATOM   3843 C  CB  . THR B 1 192 ? 24.596  -18.497 -45.225 1.00 8.42   ? 193 THR B CB  1 
ATOM   3844 O  OG1 . THR B 1 192 ? 23.878  -17.289 -44.823 1.00 8.31   ? 193 THR B OG1 1 
ATOM   3845 C  CG2 . THR B 1 192 ? 25.145  -18.270 -46.626 1.00 9.32   ? 193 THR B CG2 1 
ATOM   3846 N  N   . TYR B 1 193 ? 21.360  -18.932 -45.393 1.00 7.30   ? 194 TYR B N   1 
ATOM   3847 C  CA  . TYR B 1 193 ? 20.120  -18.660 -46.115 1.00 8.05   ? 194 TYR B CA  1 
ATOM   3848 C  C   . TYR B 1 193 ? 19.360  -17.595 -45.333 1.00 7.33   ? 194 TYR B C   1 
ATOM   3849 O  O   . TYR B 1 193 ? 19.575  -17.412 -44.152 1.00 7.73   ? 194 TYR B O   1 
ATOM   3850 C  CB  . TYR B 1 193 ? 19.304  -19.967 -46.290 1.00 8.49   ? 194 TYR B CB  1 
ATOM   3851 C  CG  . TYR B 1 193 ? 18.620  -20.442 -45.032 1.00 7.64   ? 194 TYR B CG  1 
ATOM   3852 C  CD1 . TYR B 1 193 ? 19.271  -21.157 -44.078 1.00 7.74   ? 194 TYR B CD1 1 
ATOM   3853 C  CD2 . TYR B 1 193 ? 17.285  -20.092 -44.806 1.00 8.17   ? 194 TYR B CD2 1 
ATOM   3854 C  CE1 . TYR B 1 193 ? 18.638  -21.496 -42.877 1.00 7.50   ? 194 TYR B CE1 1 
ATOM   3855 C  CE2 . TYR B 1 193 ? 16.629  -20.409 -43.616 1.00 8.24   ? 194 TYR B CE2 1 
ATOM   3856 C  CZ  . TYR B 1 193 ? 17.310  -21.106 -42.657 1.00 7.04   ? 194 TYR B CZ  1 
ATOM   3857 O  OH  . TYR B 1 193 ? 16.672  -21.405 -41.489 1.00 7.66   ? 194 TYR B OH  1 
ATOM   3858 N  N   . PRO B 1 194 ? 18.411  -16.915 -46.004 1.00 7.60   ? 195 PRO B N   1 
ATOM   3859 C  CA  . PRO B 1 194 ? 17.579  -15.892 -45.322 1.00 8.28   ? 195 PRO B CA  1 
ATOM   3860 C  C   . PRO B 1 194 ? 16.371  -16.562 -44.630 1.00 7.08   ? 195 PRO B C   1 
ATOM   3861 O  O   . PRO B 1 194 ? 15.639  -17.330 -45.292 1.00 8.98   ? 195 PRO B O   1 
ATOM   3862 C  CB  . PRO B 1 194 ? 17.091  -15.003 -46.489 1.00 10.04  ? 195 PRO B CB  1 
ATOM   3863 C  CG  . PRO B 1 194 ? 17.084  -15.930 -47.692 1.00 10.74  ? 195 PRO B CG  1 
ATOM   3864 C  CD  . PRO B 1 194 ? 18.196  -16.908 -47.471 1.00 10.37  ? 195 PRO B CD  1 
ATOM   3865 N  N   . GLY B 1 195 ? 16.142  -16.259 -43.378 1.00 7.12   ? 196 GLY B N   1 
ATOM   3866 C  CA  . GLY B 1 195 ? 15.017  -16.848 -42.657 1.00 7.74   ? 196 GLY B CA  1 
ATOM   3867 C  C   . GLY B 1 195 ? 14.488  -15.987 -41.555 1.00 7.14   ? 196 GLY B C   1 
ATOM   3868 O  O   . GLY B 1 195 ? 14.375  -14.741 -41.702 1.00 7.72   ? 196 GLY B O   1 
ATOM   3869 N  N   . SER B 1 196 ? 14.071  -16.651 -40.498 1.00 6.89   ? 197 SER B N   1 
ATOM   3870 C  CA  . SER B 1 196 ? 13.256  -15.998 -39.471 1.00 7.51   ? 197 SER B CA  1 
ATOM   3871 C  C   . SER B 1 196 ? 13.705  -16.398 -38.076 1.00 7.04   ? 197 SER B C   1 
ATOM   3872 O  O   . SER B 1 196 ? 14.452  -17.371 -37.894 1.00 7.34   ? 197 SER B O   1 
ATOM   3873 C  CB  . SER B 1 196 ? 11.749  -16.405 -39.617 1.00 8.11   ? 197 SER B CB  1 
ATOM   3874 O  OG  . SER B 1 196 ? 11.517  -17.749 -39.186 1.00 7.75   ? 197 SER B OG  1 
ATOM   3875 N  N   . LEU B 1 197 ? 13.171  -15.717 -37.064 1.00 7.12   ? 198 LEU B N   1 
ATOM   3876 C  CA  . LEU B 1 197 ? 13.186  -16.278 -35.732 1.00 7.23   ? 198 LEU B CA  1 
ATOM   3877 C  C   . LEU B 1 197 ? 12.460  -17.600 -35.747 1.00 7.25   ? 198 LEU B C   1 
ATOM   3878 O  O   . LEU B 1 197 ? 11.407  -17.730 -36.436 1.00 8.25   ? 198 LEU B O   1 
ATOM   3879 C  CB  . LEU B 1 197 ? 12.469  -15.315 -34.755 1.00 8.36   ? 198 LEU B CB  1 
ATOM   3880 C  CG  . LEU B 1 197 ? 12.999  -13.897 -34.690 1.00 8.71   ? 198 LEU B CG  1 
ATOM   3881 C  CD1 . LEU B 1 197 ? 12.139  -13.083 -33.728 1.00 10.79  ? 198 LEU B CD1 1 
ATOM   3882 C  CD2 . LEU B 1 197 ? 14.430  -13.881 -34.222 1.00 11.58  ? 198 LEU B CD2 1 
ATOM   3883 N  N   . THR B 1 198 ? 12.870  -18.558 -34.928 1.00 7.18   ? 199 THR B N   1 
ATOM   3884 C  CA  . THR B 1 198 ? 12.198  -19.847 -34.840 1.00 8.49   ? 199 THR B CA  1 
ATOM   3885 C  C   . THR B 1 198 ? 11.203  -19.941 -33.711 1.00 8.12   ? 199 THR B C   1 
ATOM   3886 O  O   . THR B 1 198 ? 10.613  -21.056 -33.535 1.00 8.45   ? 199 THR B O   1 
ATOM   3887 C  CB  . THR B 1 198 ? 13.200  -21.004 -34.757 1.00 7.92   ? 199 THR B CB  1 
ATOM   3888 O  OG1 . THR B 1 198 ? 13.807  -20.968 -33.466 1.00 7.78   ? 199 THR B OG1 1 
ATOM   3889 C  CG2 . THR B 1 198 ? 14.268  -20.964 -35.874 1.00 8.77   ? 199 THR B CG2 1 
ATOM   3890 N  N   . THR B 1 199 ? 11.038  -18.872 -32.943 1.00 9.33   ? 200 THR B N   1 
ATOM   3891 C  CA  . THR B 1 199 ? 9.954   -18.807 -31.963 1.00 9.10   ? 200 THR B CA  1 
ATOM   3892 C  C   . THR B 1 199 ? 9.175   -17.555 -32.244 1.00 9.57   ? 200 THR B C   1 
ATOM   3893 O  O   . THR B 1 199 ? 9.662   -16.634 -32.883 1.00 9.66   ? 200 THR B O   1 
ATOM   3894 C  CB  . THR B 1 199 ? 10.438  -18.714 -30.500 1.00 9.60   ? 200 THR B CB  1 
ATOM   3895 O  OG1 . THR B 1 199 ? 11.057  -17.457 -30.250 1.00 14.29  ? 200 THR B OG1 1 
ATOM   3896 C  CG2 . THR B 1 199 ? 11.408  -19.806 -30.159 1.00 12.73  ? 200 THR B CG2 1 
ATOM   3897 N  N   . PRO B 1 200 ? 7.884   -17.506 -31.795 1.00 10.29  ? 201 PRO B N   1 
ATOM   3898 C  CA  . PRO B 1 200 ? 7.169   -16.252 -31.849 1.00 10.72  ? 201 PRO B CA  1 
ATOM   3899 C  C   . PRO B 1 200 ? 8.059   -15.113 -31.333 1.00 11.69  ? 201 PRO B C   1 
ATOM   3900 O  O   . PRO B 1 200 ? 8.778   -15.289 -30.321 1.00 12.48  ? 201 PRO B O   1 
ATOM   3901 C  CB  . PRO B 1 200 ? 5.948   -16.552 -30.915 1.00 12.98  ? 201 PRO B CB  1 
ATOM   3902 C  CG  . PRO B 1 200 ? 5.705   -17.980 -31.175 1.00 11.66  ? 201 PRO B CG  1 
ATOM   3903 C  CD  . PRO B 1 200 ? 7.068   -18.608 -31.188 1.00 10.99  ? 201 PRO B CD  1 
ATOM   3904 N  N   . PRO B 1 201 ? 8.012   -13.944 -31.977 1.00 10.81  ? 202 PRO B N   1 
ATOM   3905 C  CA  . PRO B 1 201 ? 7.080   -13.528 -33.030 1.00 11.09  ? 202 PRO B CA  1 
ATOM   3906 C  C   . PRO B 1 201 ? 7.426   -13.972 -34.455 1.00 10.04  ? 202 PRO B C   1 
ATOM   3907 O  O   . PRO B 1 201 ? 6.766   -13.515 -35.377 1.00 10.99  ? 202 PRO B O   1 
ATOM   3908 C  CB  . PRO B 1 201 ? 7.122   -11.999 -32.867 1.00 13.19  ? 202 PRO B CB  1 
ATOM   3909 C  CG  . PRO B 1 201 ? 8.510   -11.691 -32.450 1.00 12.91  ? 202 PRO B CG  1 
ATOM   3910 C  CD  . PRO B 1 201 ? 8.849   -12.806 -31.454 1.00 11.09  ? 202 PRO B CD  1 
ATOM   3911 N  N   . LEU B 1 202 ? 8.436   -14.820 -34.645 1.00 8.65   ? 203 LEU B N   1 
ATOM   3912 C  CA  . LEU B 1 202 ? 8.636   -15.460 -35.966 1.00 8.81   ? 203 LEU B CA  1 
ATOM   3913 C  C   . LEU B 1 202 ? 9.044   -14.482 -37.073 1.00 8.52   ? 203 LEU B C   1 
ATOM   3914 O  O   . LEU B 1 202 ? 8.864   -14.727 -38.244 1.00 8.67   ? 203 LEU B O   1 
ATOM   3915 C  CB  . LEU B 1 202 ? 7.443   -16.350 -36.415 1.00 10.01  ? 203 LEU B CB  1 
ATOM   3916 C  CG  . LEU B 1 202 ? 7.150   -17.508 -35.418 1.00 9.45   ? 203 LEU B CG  1 
ATOM   3917 C  CD1 . LEU B 1 202 ? 5.847   -18.152 -35.844 1.00 12.65  ? 203 LEU B CD1 1 
ATOM   3918 C  CD2 . LEU B 1 202 ? 8.257   -18.563 -35.414 1.00 10.06  ? 203 LEU B CD2 1 
ATOM   3919 N  N   . LEU B 1 203 ? 9.629   -13.337 -36.644 1.00 9.31   ? 204 LEU B N   1 
ATOM   3920 C  CA  . LEU B 1 203 ? 9.910   -12.247 -37.586 1.00 8.76   ? 204 LEU B CA  1 
ATOM   3921 C  C   . LEU B 1 203 ? 10.934  -12.680 -38.603 1.00 8.50   ? 204 LEU B C   1 
ATOM   3922 O  O   . LEU B 1 203 ? 11.908  -13.396 -38.296 1.00 8.85   ? 204 LEU B O   1 
ATOM   3923 C  CB  . LEU B 1 203 ? 10.420  -11.044 -36.829 1.00 10.04  ? 204 LEU B CB  1 
ATOM   3924 C  CG  . LEU B 1 203 ? 9.378   -10.397 -35.898 1.00 11.53  ? 204 LEU B CG  1 
ATOM   3925 C  CD1 . LEU B 1 203 ? 10.019  -9.349  -34.995 1.00 13.33  ? 204 LEU B CD1 1 
ATOM   3926 C  CD2 . LEU B 1 203 ? 8.149   -9.835  -36.708 1.00 15.39  ? 204 LEU B CD2 1 
ATOM   3927 N  N   . GLU B 1 204 ? 10.765  -12.227 -39.837 1.00 9.57   ? 205 GLU B N   1 
ATOM   3928 C  CA  . GLU B 1 204 ? 11.589  -12.583 -40.978 1.00 9.13   ? 205 GLU B CA  1 
ATOM   3929 C  C   . GLU B 1 204 ? 12.760  -11.609 -41.107 1.00 8.93   ? 205 GLU B C   1 
ATOM   3930 O  O   . GLU B 1 204 ? 12.873  -10.841 -42.056 1.00 11.32  ? 205 GLU B O   1 
ATOM   3931 C  CB  . GLU B 1 204 ? 10.701  -12.743 -42.239 1.00 10.94  ? 205 GLU B CB  1 
ATOM   3932 C  CG  . GLU B 1 204 ? 9.804   -13.971 -42.077 1.00 10.63  ? 205 GLU B CG  1 
ATOM   3933 C  CD  . GLU B 1 204 ? 8.886   -14.228 -43.246 1.00 11.23  ? 205 GLU B CD  1 
ATOM   3934 O  OE1 . GLU B 1 204 ? 8.575   -13.305 -44.043 1.00 14.29  ? 205 GLU B OE1 1 
ATOM   3935 O  OE2 . GLU B 1 204 ? 8.473   -15.402 -43.419 1.00 11.73  ? 205 GLU B OE2 1 
ATOM   3936 N  N   . CYS B 1 205 ? 13.676  -11.710 -40.161 1.00 8.43   ? 206 CYS B N   1 
ATOM   3937 C  CA  . CYS B 1 205 ? 14.716  -10.695 -39.959 1.00 8.61   ? 206 CYS B CA  1 
ATOM   3938 C  C   . CYS B 1 205 ? 16.092  -11.331 -39.849 1.00 7.71   ? 206 CYS B C   1 
ATOM   3939 O  O   . CYS B 1 205 ? 17.014  -10.625 -39.490 1.00 9.81   ? 206 CYS B O   1 
ATOM   3940 C  CB  . CYS B 1 205 ? 14.417  -9.878  -38.709 1.00 8.99   ? 206 CYS B CB  1 
ATOM   3941 S  SG  . CYS B 1 205 ? 14.379  -10.832 -37.180 1.00 10.09  ? 206 CYS B SG  1 
ATOM   3942 N  N   . VAL B 1 206 ? 16.225  -12.636 -40.143 1.00 7.77   ? 207 VAL B N   1 
ATOM   3943 C  CA  . VAL B 1 206 ? 17.481  -13.318 -39.779 1.00 7.22   ? 207 VAL B CA  1 
ATOM   3944 C  C   . VAL B 1 206 ? 18.227  -13.777 -41.002 1.00 7.44   ? 207 VAL B C   1 
ATOM   3945 O  O   . VAL B 1 206 ? 17.684  -14.444 -41.898 1.00 8.62   ? 207 VAL B O   1 
ATOM   3946 C  CB  . VAL B 1 206 ? 17.153  -14.606 -38.923 1.00 7.85   ? 207 VAL B CB  1 
ATOM   3947 C  CG1 . VAL B 1 206 ? 18.508  -15.284 -38.572 1.00 7.77   ? 207 VAL B CG1 1 
ATOM   3948 C  CG2 . VAL B 1 206 ? 16.434  -14.214 -37.622 1.00 8.99   ? 207 VAL B CG2 1 
ATOM   3949 N  N   . THR B 1 207 ? 19.565  -13.479 -41.066 1.00 7.11   ? 208 THR B N   1 
ATOM   3950 C  CA  . THR B 1 207 ? 20.462  -14.210 -41.912 1.00 7.47   ? 208 THR B CA  1 
ATOM   3951 C  C   . THR B 1 207 ? 21.001  -15.383 -41.089 1.00 6.79   ? 208 THR B C   1 
ATOM   3952 O  O   . THR B 1 207 ? 21.673  -15.195 -40.056 1.00 7.60   ? 208 THR B O   1 
ATOM   3953 C  CB  . THR B 1 207 ? 21.654  -13.360 -42.371 1.00 7.97   ? 208 THR B CB  1 
ATOM   3954 O  OG1 . THR B 1 207 ? 21.145  -12.219 -43.109 1.00 8.91   ? 208 THR B OG1 1 
ATOM   3955 C  CG2 . THR B 1 207 ? 22.587  -14.153 -43.258 1.00 9.85   ? 208 THR B CG2 1 
ATOM   3956 N  N   . TRP B 1 208 ? 20.639  -16.608 -41.496 1.00 6.58   ? 209 TRP B N   1 
ATOM   3957 C  CA  . TRP B 1 208 ? 21.072  -17.799 -40.775 1.00 6.53   ? 209 TRP B CA  1 
ATOM   3958 C  C   . TRP B 1 208 ? 22.450  -18.212 -41.280 1.00 6.60   ? 209 TRP B C   1 
ATOM   3959 O  O   . TRP B 1 208 ? 22.689  -18.283 -42.507 1.00 7.40   ? 209 TRP B O   1 
ATOM   3960 C  CB  . TRP B 1 208 ? 20.074  -18.944 -40.984 1.00 6.91   ? 209 TRP B CB  1 
ATOM   3961 C  CG  . TRP B 1 208 ? 18.955  -18.838 -40.019 1.00 6.49   ? 209 TRP B CG  1 
ATOM   3962 C  CD1 . TRP B 1 208 ? 17.702  -18.264 -40.196 1.00 7.27   ? 209 TRP B CD1 1 
ATOM   3963 C  CD2 . TRP B 1 208 ? 19.025  -19.263 -38.650 1.00 6.85   ? 209 TRP B CD2 1 
ATOM   3964 N  NE1 . TRP B 1 208 ? 17.046  -18.266 -39.017 1.00 7.43   ? 209 TRP B NE1 1 
ATOM   3965 C  CE2 . TRP B 1 208 ? 17.778  -18.870 -38.057 1.00 6.53   ? 209 TRP B CE2 1 
ATOM   3966 C  CE3 . TRP B 1 208 ? 19.982  -19.878 -37.861 1.00 6.31   ? 209 TRP B CE3 1 
ATOM   3967 C  CZ2 . TRP B 1 208 ? 17.496  -19.102 -36.725 1.00 7.94   ? 209 TRP B CZ2 1 
ATOM   3968 C  CZ3 . TRP B 1 208 ? 19.706  -20.163 -36.571 1.00 7.77   ? 209 TRP B CZ3 1 
ATOM   3969 C  CH2 . TRP B 1 208 ? 18.502  -19.781 -35.982 1.00 8.03   ? 209 TRP B CH2 1 
ATOM   3970 N  N   . ILE B 1 209 ? 23.327  -18.595 -40.368 1.00 6.32   ? 210 ILE B N   1 
ATOM   3971 C  CA  . ILE B 1 209 ? 24.667  -19.107 -40.674 1.00 6.50   ? 210 ILE B CA  1 
ATOM   3972 C  C   . ILE B 1 209 ? 24.772  -20.386 -39.838 1.00 6.37   ? 210 ILE B C   1 
ATOM   3973 O  O   . ILE B 1 209 ? 24.840  -20.277 -38.597 1.00 8.00   ? 210 ILE B O   1 
ATOM   3974 C  CB  . ILE B 1 209 ? 25.727  -18.089 -40.312 1.00 7.77   ? 210 ILE B CB  1 
ATOM   3975 C  CG1 . ILE B 1 209 ? 25.532  -16.803 -41.112 1.00 9.65   ? 210 ILE B CG1 1 
ATOM   3976 C  CG2 . ILE B 1 209 ? 27.135  -18.676 -40.544 1.00 9.67   ? 210 ILE B CG2 1 
ATOM   3977 C  CD1 . ILE B 1 209 ? 26.367  -15.654 -40.655 1.00 10.55  ? 210 ILE B CD1 1 
ATOM   3978 N  N   . VAL B 1 210 ? 24.732  -21.541 -40.475 1.00 6.53   ? 211 VAL B N   1 
ATOM   3979 C  CA  . VAL B 1 210 ? 24.695  -22.830 -39.783 1.00 6.32   ? 211 VAL B CA  1 
ATOM   3980 C  C   . VAL B 1 210 ? 26.024  -23.511 -40.022 1.00 6.94   ? 211 VAL B C   1 
ATOM   3981 O  O   . VAL B 1 210 ? 26.364  -23.817 -41.169 1.00 7.92   ? 211 VAL B O   1 
ATOM   3982 C  CB  . VAL B 1 210 ? 23.478  -23.668 -40.230 1.00 8.12   ? 211 VAL B CB  1 
ATOM   3983 C  CG1 . VAL B 1 210 ? 23.513  -25.033 -39.509 1.00 8.76   ? 211 VAL B CG1 1 
ATOM   3984 C  CG2 . VAL B 1 210 ? 22.165  -22.931 -39.935 1.00 9.01   ? 211 VAL B CG2 1 
ATOM   3985 N  N   . LEU B 1 211 ? 26.790  -23.799 -38.951 1.00 7.56   ? 212 LEU B N   1 
ATOM   3986 C  CA  . LEU B 1 211 ? 28.082  -24.474 -39.143 1.00 8.16   ? 212 LEU B CA  1 
ATOM   3987 C  C   . LEU B 1 211 ? 27.894  -25.919 -39.513 1.00 8.00   ? 212 LEU B C   1 
ATOM   3988 O  O   . LEU B 1 211 ? 27.019  -26.641 -38.964 1.00 8.67   ? 212 LEU B O   1 
ATOM   3989 C  CB  . LEU B 1 211 ? 28.922  -24.351 -37.868 1.00 8.56   ? 212 LEU B CB  1 
ATOM   3990 C  CG  . LEU B 1 211 ? 29.275  -22.914 -37.456 1.00 9.25   ? 212 LEU B CG  1 
ATOM   3991 C  CD1 . LEU B 1 211 ? 30.288  -22.992 -36.292 1.00 10.99  ? 212 LEU B CD1 1 
ATOM   3992 C  CD2 . LEU B 1 211 ? 29.785  -22.075 -38.584 1.00 10.37  ? 212 LEU B CD2 1 
ATOM   3993 N  N   . LYS B 1 212 ? 28.773  -26.414 -40.399 1.00 8.65   ? 213 LYS B N   1 
ATOM   3994 C  CA  . LYS B 1 212 ? 28.716  -27.809 -40.777 1.00 9.16   ? 213 LYS B CA  1 
ATOM   3995 C  C   . LYS B 1 212 ? 29.189  -28.706 -39.667 1.00 8.70   ? 213 LYS B C   1 
ATOM   3996 O  O   . LYS B 1 212 ? 28.678  -29.837 -39.522 1.00 10.68  ? 213 LYS B O   1 
ATOM   3997 C  CB  . LYS B 1 212 ? 29.498  -28.016 -42.062 1.00 11.68  ? 213 LYS B CB  1 
ATOM   3998 C  CG  . LYS B 1 212 ? 29.563  -29.501 -42.458 1.00 15.47  ? 213 LYS B CG  1 
ATOM   3999 C  CD  . LYS B 1 212 ? 30.368  -29.716 -43.742 1.00 22.88  ? 213 LYS B CD  1 
ATOM   4000 C  CE  . LYS B 1 212 ? 30.434  -31.151 -44.207 1.00 30.45  ? 213 LYS B CE  1 
ATOM   4001 N  NZ  . LYS B 1 212 ? 31.365  -31.245 -45.375 1.00 43.83  ? 213 LYS B NZ  1 
ATOM   4002 N  N   . GLU B 1 213 ? 30.230  -28.328 -38.916 1.00 8.63   ? 214 GLU B N   1 
ATOM   4003 C  CA  . GLU B 1 213 ? 30.831  -29.217 -37.908 1.00 9.30   ? 214 GLU B CA  1 
ATOM   4004 C  C   . GLU B 1 213 ? 30.057  -29.094 -36.644 1.00 8.37   ? 214 GLU B C   1 
ATOM   4005 O  O   . GLU B 1 213 ? 29.985  -28.017 -36.069 1.00 8.41   ? 214 GLU B O   1 
ATOM   4006 C  CB  . GLU B 1 213 ? 32.311  -28.850 -37.717 1.00 10.32  ? 214 GLU B CB  1 
ATOM   4007 C  CG  . GLU B 1 213 ? 32.942  -29.789 -36.740 1.00 12.58  ? 214 GLU B CG  1 
ATOM   4008 C  CD  . GLU B 1 213 ? 34.443  -29.563 -36.553 1.00 15.41  ? 214 GLU B CD  1 
ATOM   4009 O  OE1 . GLU B 1 213 ? 35.035  -28.661 -37.184 1.00 15.87  ? 214 GLU B OE1 1 
ATOM   4010 O  OE2 . GLU B 1 213 ? 35.035  -30.350 -35.784 1.00 30.56  ? 214 GLU B OE2 1 
ATOM   4011 N  N   A PRO B 1 214 ? 29.467  -30.225 -36.115 0.50 8.20   ? 215 PRO B N   1 
ATOM   4012 N  N   B PRO B 1 214 ? 29.548  -30.224 -36.110 0.50 8.84   ? 215 PRO B N   1 
ATOM   4013 C  CA  A PRO B 1 214 ? 28.830  -30.168 -34.800 0.50 8.89   ? 215 PRO B CA  1 
ATOM   4014 C  CA  B PRO B 1 214 ? 28.927  -30.172 -34.803 0.50 9.15   ? 215 PRO B CA  1 
ATOM   4015 C  C   A PRO B 1 214 ? 29.849  -30.109 -33.677 0.50 8.87   ? 215 PRO B C   1 
ATOM   4016 C  C   B PRO B 1 214 ? 29.919  -30.102 -33.673 0.50 9.32   ? 215 PRO B C   1 
ATOM   4017 O  O   A PRO B 1 214 ? 31.023  -30.483 -33.890 0.50 11.01  ? 215 PRO B O   1 
ATOM   4018 O  O   B PRO B 1 214 ? 31.115  -30.476 -33.876 0.50 11.38  ? 215 PRO B O   1 
ATOM   4019 C  CB  A PRO B 1 214 ? 28.073  -31.495 -34.722 0.50 8.74   ? 215 PRO B CB  1 
ATOM   4020 C  CB  B PRO B 1 214 ? 28.141  -31.487 -34.727 0.50 10.07  ? 215 PRO B CB  1 
ATOM   4021 C  CG  A PRO B 1 214 ? 28.986  -32.454 -35.504 0.50 9.00   ? 215 PRO B CG  1 
ATOM   4022 C  CG  B PRO B 1 214 ? 27.995  -31.943 -36.167 0.50 14.94  ? 215 PRO B CG  1 
ATOM   4023 C  CD  A PRO B 1 214 ? 29.556  -31.615 -36.630 0.50 8.17   ? 215 PRO B CD  1 
ATOM   4024 C  CD  B PRO B 1 214 ? 29.245  -31.468 -36.841 0.50 12.95  ? 215 PRO B CD  1 
ATOM   4025 N  N   . ILE B 1 215 ? 29.454  -29.664 -32.515 1.00 9.02   ? 216 ILE B N   1 
ATOM   4026 C  CA  . ILE B 1 215 ? 30.243  -29.890 -31.294 1.00 9.64   ? 216 ILE B CA  1 
ATOM   4027 C  C   . ILE B 1 215 ? 29.733  -31.131 -30.617 1.00 9.25   ? 216 ILE B C   1 
ATOM   4028 O  O   . ILE B 1 215 ? 28.566  -31.515 -30.785 1.00 10.29  ? 216 ILE B O   1 
ATOM   4029 C  CB  . ILE B 1 215 ? 30.232  -28.689 -30.357 1.00 9.86   ? 216 ILE B CB  1 
ATOM   4030 C  CG1 . ILE B 1 215 ? 28.850  -28.308 -29.847 1.00 10.90  ? 216 ILE B CG1 1 
ATOM   4031 C  CG2 . ILE B 1 215 ? 30.969  -27.462 -31.033 1.00 11.65  ? 216 ILE B CG2 1 
ATOM   4032 C  CD1 . ILE B 1 215 ? 28.837  -27.310 -28.682 1.00 13.47  ? 216 ILE B CD1 1 
ATOM   4033 N  N   A SER B 1 216 ? 30.574  -31.785 -29.842 0.50 10.12  ? 217 SER B N   1 
ATOM   4034 N  N   B SER B 1 216 ? 30.633  -31.776 -29.859 0.50 10.48  ? 217 SER B N   1 
ATOM   4035 C  CA  A SER B 1 216 ? 30.157  -32.938 -29.027 0.50 10.12  ? 217 SER B CA  1 
ATOM   4036 C  CA  B SER B 1 216 ? 30.251  -32.934 -29.034 0.50 10.85  ? 217 SER B CA  1 
ATOM   4037 C  C   A SER B 1 216 ? 29.969  -32.473 -27.618 0.50 10.16  ? 217 SER B C   1 
ATOM   4038 C  C   B SER B 1 216 ? 30.030  -32.487 -27.608 0.50 10.59  ? 217 SER B C   1 
ATOM   4039 O  O   A SER B 1 216 ? 30.807  -31.731 -27.074 0.50 11.59  ? 217 SER B O   1 
ATOM   4040 O  O   B SER B 1 216 ? 30.894  -31.740 -27.067 0.50 11.82  ? 217 SER B O   1 
ATOM   4041 C  CB  A SER B 1 216 ? 31.274  -34.005 -29.035 0.50 13.75  ? 217 SER B CB  1 
ATOM   4042 C  CB  B SER B 1 216 ? 31.397  -33.963 -29.077 0.50 15.82  ? 217 SER B CB  1 
ATOM   4043 O  OG  A SER B 1 216 ? 31.309  -34.673 -30.266 0.50 13.49  ? 217 SER B OG  1 
ATOM   4044 O  OG  B SER B 1 216 ? 31.042  -35.045 -28.290 0.50 22.13  ? 217 SER B OG  1 
ATOM   4045 N  N   . VAL B 1 217 ? 28.905  -32.945 -27.001 1.00 10.26  ? 218 VAL B N   1 
ATOM   4046 C  CA  . VAL B 1 217 ? 28.627  -32.752 -25.581 1.00 10.27  ? 218 VAL B CA  1 
ATOM   4047 C  C   . VAL B 1 217 ? 28.353  -34.101 -24.991 1.00 10.39  ? 218 VAL B C   1 
ATOM   4048 O  O   . VAL B 1 217 ? 27.995  -35.070 -25.688 1.00 10.56  ? 218 VAL B O   1 
ATOM   4049 C  CB  . VAL B 1 217 ? 27.433  -31.805 -25.348 1.00 11.03  ? 218 VAL B CB  1 
ATOM   4050 C  CG1 . VAL B 1 217 ? 27.658  -30.479 -26.042 1.00 11.72  ? 218 VAL B CG1 1 
ATOM   4051 C  CG2 . VAL B 1 217 ? 26.137  -32.440 -25.851 1.00 12.32  ? 218 VAL B CG2 1 
ATOM   4052 N  N   . SER B 1 218 ? 28.504  -34.262 -23.676 1.00 10.14  ? 219 SER B N   1 
ATOM   4053 C  CA  . SER B 1 218 ? 28.331  -35.581 -23.116 1.00 10.96  ? 219 SER B CA  1 
ATOM   4054 C  C   . SER B 1 218 ? 26.829  -35.840 -22.816 1.00 10.66  ? 219 SER B C   1 
ATOM   4055 O  O   . SER B 1 218 ? 26.020  -34.922 -22.672 1.00 10.81  ? 219 SER B O   1 
ATOM   4056 C  CB  . SER B 1 218 ? 29.128  -35.746 -21.831 1.00 10.98  ? 219 SER B CB  1 
ATOM   4057 O  OG  . SER B 1 218 ? 28.649  -34.871 -20.831 1.00 12.24  ? 219 SER B OG  1 
ATOM   4058 N  N   A SER B 1 219 ? 26.480  -37.116 -22.689 0.50 10.74  ? 220 SER B N   1 
ATOM   4059 N  N   B SER B 1 219 ? 26.524  -37.120 -22.679 0.50 10.87  ? 220 SER B N   1 
ATOM   4060 C  CA  A SER B 1 219 ? 25.154  -37.474 -22.263 0.50 12.86  ? 220 SER B CA  1 
ATOM   4061 C  CA  B SER B 1 219 ? 25.201  -37.478 -22.274 0.50 13.06  ? 220 SER B CA  1 
ATOM   4062 C  C   A SER B 1 219 ? 24.787  -36.803 -20.947 0.50 12.47  ? 220 SER B C   1 
ATOM   4063 C  C   B SER B 1 219 ? 24.821  -36.797 -20.965 0.50 12.45  ? 220 SER B C   1 
ATOM   4064 O  O   A SER B 1 219 ? 23.655  -36.341 -20.769 0.50 14.38  ? 220 SER B O   1 
ATOM   4065 O  O   B SER B 1 219 ? 23.710  -36.322 -20.802 0.50 14.58  ? 220 SER B O   1 
ATOM   4066 C  CB  A SER B 1 219 ? 25.071  -38.984 -22.215 0.50 15.90  ? 220 SER B CB  1 
ATOM   4067 C  CB  B SER B 1 219 ? 25.116  -38.980 -22.200 0.50 15.28  ? 220 SER B CB  1 
ATOM   4068 O  OG  A SER B 1 219 ? 25.989  -39.586 -21.301 0.50 16.09  ? 220 SER B OG  1 
ATOM   4069 O  OG  B SER B 1 219 ? 23.759  -39.410 -22.015 0.50 18.08  ? 220 SER B OG  1 
ATOM   4070 N  N   . GLU B 1 220 ? 25.746  -36.709 -20.037 1.00 12.29  ? 221 GLU B N   1 
ATOM   4071 C  CA  . GLU B 1 220 ? 25.466  -36.085 -18.745 1.00 13.93  ? 221 GLU B CA  1 
ATOM   4072 C  C   . GLU B 1 220 ? 25.176  -34.590 -18.916 1.00 12.31  ? 221 GLU B C   1 
ATOM   4073 O  O   . GLU B 1 220 ? 24.302  -34.058 -18.206 1.00 14.17  ? 221 GLU B O   1 
ATOM   4074 C  CB  . GLU B 1 220 ? 26.606  -36.241 -17.783 1.00 17.77  ? 221 GLU B CB  1 
ATOM   4075 C  CG  . GLU B 1 220 ? 26.749  -37.699 -17.348 1.00 21.54  ? 221 GLU B CG  1 
ATOM   4076 C  CD  . GLU B 1 220 ? 27.806  -38.453 -18.164 1.00 24.21  ? 221 GLU B CD  1 
ATOM   4077 O  OE1 . GLU B 1 220 ? 28.205  -38.035 -19.298 1.00 20.06  ? 221 GLU B OE1 1 
ATOM   4078 O  OE2 . GLU B 1 220 ? 28.268  -39.489 -17.674 1.00 40.22  ? 221 GLU B OE2 1 
ATOM   4079 N  N   . GLN B 1 221 ? 25.853  -33.904 -19.838 1.00 11.67  ? 222 GLN B N   1 
ATOM   4080 C  CA  . GLN B 1 221 ? 25.590  -32.498 -20.051 1.00 11.84  ? 222 GLN B CA  1 
ATOM   4081 C  C   . GLN B 1 221 ? 24.157  -32.293 -20.619 1.00 10.97  ? 222 GLN B C   1 
ATOM   4082 O  O   . GLN B 1 221 ? 23.418  -31.442 -20.101 1.00 12.22  ? 222 GLN B O   1 
ATOM   4083 C  CB  . GLN B 1 221 ? 26.658  -31.903 -20.976 1.00 11.70  ? 222 GLN B CB  1 
ATOM   4084 C  CG  . GLN B 1 221 ? 27.994  -31.776 -20.290 1.00 11.43  ? 222 GLN B CG  1 
ATOM   4085 C  CD  . GLN B 1 221 ? 29.092  -31.240 -21.164 1.00 11.40  ? 222 GLN B CD  1 
ATOM   4086 O  OE1 . GLN B 1 221 ? 29.225  -31.610 -22.332 1.00 11.25  ? 222 GLN B OE1 1 
ATOM   4087 N  NE2 . GLN B 1 221 ? 29.914  -30.357 -20.560 1.00 12.54  ? 222 GLN B NE2 1 
ATOM   4088 N  N   . VAL B 1 222 ? 23.779  -33.054 -21.624 1.00 11.46  ? 223 VAL B N   1 
ATOM   4089 C  CA  . VAL B 1 222 ? 22.468  -32.856 -22.185 1.00 12.33  ? 223 VAL B CA  1 
ATOM   4090 C  C   . VAL B 1 222 ? 21.365  -33.333 -21.209 1.00 12.92  ? 223 VAL B C   1 
ATOM   4091 O  O   . VAL B 1 222 ? 20.258  -32.748 -21.154 1.00 12.54  ? 223 VAL B O   1 
ATOM   4092 C  CB  . VAL B 1 222 ? 22.348  -33.436 -23.611 1.00 14.88  ? 223 VAL B CB  1 
ATOM   4093 C  CG1 . VAL B 1 222 ? 22.315  -34.938 -23.586 1.00 16.74  ? 223 VAL B CG1 1 
ATOM   4094 C  CG2 . VAL B 1 222 ? 21.110  -32.882 -24.321 1.00 17.11  ? 223 VAL B CG2 1 
ATOM   4095 N  N   . LEU B 1 223 ? 21.671  -34.325 -20.368 1.00 13.66  ? 224 LEU B N   1 
ATOM   4096 C  CA  . LEU B 1 223 ? 20.739  -34.725 -19.351 1.00 14.40  ? 224 LEU B CA  1 
ATOM   4097 C  C   . LEU B 1 223 ? 20.408  -33.595 -18.410 1.00 15.22  ? 224 LEU B C   1 
ATOM   4098 O  O   . LEU B 1 223 ? 19.241  -33.472 -17.982 1.00 16.32  ? 224 LEU B O   1 
ATOM   4099 C  CB  . LEU B 1 223 ? 21.205  -35.988 -18.634 1.00 17.80  ? 224 LEU B CB  1 
ATOM   4100 C  CG  . LEU B 1 223 ? 21.017  -37.260 -19.495 1.00 20.20  ? 224 LEU B CG  1 
ATOM   4101 C  CD1 . LEU B 1 223 ? 21.909  -38.386 -19.030 1.00 22.74  ? 224 LEU B CD1 1 
ATOM   4102 C  CD2 . LEU B 1 223 ? 19.558  -37.754 -19.540 1.00 25.98  ? 224 LEU B CD2 1 
ATOM   4103 N  N   . LYS B 1 224 ? 21.384  -32.748 -18.106 1.00 14.01  ? 225 LYS B N   1 
ATOM   4104 C  CA  . LYS B 1 224 ? 21.104  -31.613 -17.224 1.00 15.16  ? 225 LYS B CA  1 
ATOM   4105 C  C   . LYS B 1 224 ? 20.219  -30.564 -17.914 1.00 14.22  ? 225 LYS B C   1 
ATOM   4106 O  O   . LYS B 1 224 ? 19.403  -29.957 -17.251 1.00 13.98  ? 225 LYS B O   1 
ATOM   4107 C  CB  . LYS B 1 224 ? 22.389  -31.109 -16.617 1.00 17.36  ? 225 LYS B CB  1 
ATOM   4108 C  CG  . LYS B 1 224 ? 22.907  -32.178 -15.584 1.00 22.64  ? 225 LYS B CG  1 
ATOM   4109 C  CD  . LYS B 1 224 ? 24.215  -31.868 -14.957 1.00 24.33  ? 225 LYS B CD  1 
ATOM   4110 C  CE  . LYS B 1 224 ? 24.766  -33.022 -14.105 1.00 34.39  ? 225 LYS B CE  1 
ATOM   4111 N  NZ  . LYS B 1 224 ? 26.048  -32.673 -13.442 1.00 35.14  ? 225 LYS B NZ  1 
ATOM   4112 N  N   . PHE B 1 225 ? 20.315  -30.391 -19.238 1.00 12.75  ? 226 PHE B N   1 
ATOM   4113 C  CA  . PHE B 1 225 ? 19.420  -29.502 -19.950 1.00 11.60  ? 226 PHE B CA  1 
ATOM   4114 C  C   . PHE B 1 225 ? 17.970  -30.021 -19.719 1.00 12.28  ? 226 PHE B C   1 
ATOM   4115 O  O   . PHE B 1 225 ? 17.024  -29.262 -19.502 1.00 12.92  ? 226 PHE B O   1 
ATOM   4116 C  CB  . PHE B 1 225 ? 19.593  -29.494 -21.452 1.00 11.72  ? 226 PHE B CB  1 
ATOM   4117 C  CG  . PHE B 1 225 ? 20.797  -28.741 -21.981 1.00 12.09  ? 226 PHE B CG  1 
ATOM   4118 C  CD1 . PHE B 1 225 ? 21.840  -28.317 -21.172 1.00 15.61  ? 226 PHE B CD1 1 
ATOM   4119 C  CD2 . PHE B 1 225 ? 20.879  -28.493 -23.343 1.00 15.02  ? 226 PHE B CD2 1 
ATOM   4120 C  CE1 . PHE B 1 225 ? 22.929  -27.645 -21.724 1.00 17.49  ? 226 PHE B CE1 1 
ATOM   4121 C  CE2 . PHE B 1 225 ? 21.956  -27.829 -23.898 1.00 15.83  ? 226 PHE B CE2 1 
ATOM   4122 C  CZ  . PHE B 1 225 ? 22.986  -27.402 -23.087 1.00 15.22  ? 226 PHE B CZ  1 
ATOM   4123 N  N   . ARG B 1 226 ? 17.773  -31.353 -19.797 1.00 11.18  ? 227 ARG B N   1 
ATOM   4124 C  CA  . ARG B 1 226 ? 16.471  -31.960 -19.731 1.00 12.40  ? 227 ARG B CA  1 
ATOM   4125 C  C   . ARG B 1 226 ? 15.847  -31.997 -18.318 1.00 13.49  ? 227 ARG B C   1 
ATOM   4126 O  O   . ARG B 1 226 ? 14.699  -32.412 -18.153 1.00 15.01  ? 227 ARG B O   1 
ATOM   4127 C  CB  . ARG B 1 226 ? 16.531  -33.402 -20.257 1.00 12.58  ? 227 ARG B CB  1 
ATOM   4128 C  CG  . ARG B 1 226 ? 17.031  -33.499 -21.692 1.00 12.14  ? 227 ARG B CG  1 
ATOM   4129 C  CD  . ARG B 1 226 ? 16.896  -34.940 -22.188 1.00 14.95  ? 227 ARG B CD  1 
ATOM   4130 N  NE  . ARG B 1 226 ? 17.507  -35.059 -23.508 1.00 11.74  ? 227 ARG B NE  1 
ATOM   4131 C  CZ  . ARG B 1 226 ? 18.415  -35.967 -23.866 1.00 12.15  ? 227 ARG B CZ  1 
ATOM   4132 N  NH1 . ARG B 1 226 ? 18.839  -36.879 -23.000 1.00 17.19  ? 227 ARG B NH1 1 
ATOM   4133 N  NH2 . ARG B 1 226 ? 18.889  -35.967 -25.111 1.00 14.32  ? 227 ARG B NH2 1 
ATOM   4134 N  N   . LYS B 1 227 ? 16.582  -31.507 -17.325 1.00 12.25  ? 228 LYS B N   1 
ATOM   4135 C  CA  . LYS B 1 227 ? 16.067  -31.377 -15.928 1.00 14.73  ? 228 LYS B CA  1 
ATOM   4136 C  C   . LYS B 1 227 ? 15.446  -30.000 -15.699 1.00 14.06  ? 228 LYS B C   1 
ATOM   4137 O  O   . LYS B 1 227 ? 14.816  -29.789 -14.675 1.00 17.14  ? 228 LYS B O   1 
ATOM   4138 C  CB  . LYS B 1 227 ? 17.215  -31.557 -14.898 1.00 17.02  ? 228 LYS B CB  1 
ATOM   4139 C  CG  . LYS B 1 227 ? 17.656  -32.992 -14.827 1.00 20.83  ? 228 LYS B CG  1 
ATOM   4140 C  CD  . LYS B 1 227 ? 18.772  -33.263 -13.804 1.00 29.55  ? 228 LYS B CD  1 
ATOM   4141 C  CE  . LYS B 1 227 ? 18.564  -32.710 -12.395 1.00 40.38  ? 228 LYS B CE  1 
ATOM   4142 N  NZ  . LYS B 1 227 ? 19.840  -32.552 -11.589 1.00 73.72  ? 228 LYS B NZ  1 
ATOM   4143 N  N   . LEU B 1 228 ? 15.664  -29.044 -16.616 1.00 14.13  ? 229 LEU B N   1 
ATOM   4144 C  CA  . LEU B 1 228 ? 15.019  -27.758 -16.527 1.00 14.51  ? 229 LEU B CA  1 
ATOM   4145 C  C   . LEU B 1 228 ? 13.496  -27.957 -16.650 1.00 14.18  ? 229 LEU B C   1 
ATOM   4146 O  O   . LEU B 1 228 ? 12.949  -29.022 -17.099 1.00 13.52  ? 229 LEU B O   1 
ATOM   4147 C  CB  . LEU B 1 228 ? 15.543  -26.838 -17.627 1.00 14.56  ? 229 LEU B CB  1 
ATOM   4148 C  CG  . LEU B 1 228 ? 17.001  -26.362 -17.405 1.00 14.44  ? 229 LEU B CG  1 
ATOM   4149 C  CD1 . LEU B 1 228 ? 17.499  -25.750 -18.682 1.00 15.78  ? 229 LEU B CD1 1 
ATOM   4150 C  CD2 . LEU B 1 228 ? 17.015  -25.305 -16.297 1.00 18.33  ? 229 LEU B CD2 1 
ATOM   4151 N  N   . ASN B 1 229 ? 12.778  -26.923 -16.281 1.00 14.56  ? 230 ASN B N   1 
ATOM   4152 C  CA  . ASN B 1 229 ? 11.331  -26.954 -16.299 1.00 14.67  ? 230 ASN B CA  1 
ATOM   4153 C  C   . ASN B 1 229 ? 10.768  -25.797 -17.123 1.00 16.76  ? 230 ASN B C   1 
ATOM   4154 O  O   . ASN B 1 229 ? 11.248  -24.606 -17.072 1.00 16.10  ? 230 ASN B O   1 
ATOM   4155 C  CB  . ASN B 1 229 ? 10.726  -26.739 -14.869 1.00 15.94  ? 230 ASN B CB  1 
ATOM   4156 C  CG  . ASN B 1 229 ? 10.798  -27.935 -13.945 1.00 18.62  ? 230 ASN B CG  1 
ATOM   4157 O  OD1 . ASN B 1 229 ? 10.185  -27.806 -12.868 1.00 23.44  ? 230 ASN B OD1 1 
ATOM   4158 N  ND2 . ASN B 1 229 ? 11.454  -29.035 -14.294 1.00 18.00  ? 230 ASN B ND2 1 
ATOM   4159 N  N   . PHE B 1 230 ? 9.706   -26.110 -17.905 1.00 16.60  ? 231 PHE B N   1 
ATOM   4160 C  CA  . PHE B 1 230 ? 8.931   -25.034 -18.548 1.00 15.50  ? 231 PHE B CA  1 
ATOM   4161 C  C   . PHE B 1 230 ? 8.041   -24.264 -17.603 1.00 20.00  ? 231 PHE B C   1 
ATOM   4162 O  O   . PHE B 1 230 ? 7.752   -23.103 -17.853 1.00 18.92  ? 231 PHE B O   1 
ATOM   4163 C  CB  . PHE B 1 230 ? 7.972   -25.628 -19.572 1.00 18.22  ? 231 PHE B CB  1 
ATOM   4164 C  CG  . PHE B 1 230 ? 8.596   -26.193 -20.823 1.00 15.32  ? 231 PHE B CG  1 
ATOM   4165 C  CD1 . PHE B 1 230 ? 9.331   -25.398 -21.696 1.00 16.25  ? 231 PHE B CD1 1 
ATOM   4166 C  CD2 . PHE B 1 230 ? 8.235   -27.449 -21.268 1.00 16.49  ? 231 PHE B CD2 1 
ATOM   4167 C  CE1 . PHE B 1 230 ? 9.804   -25.906 -22.890 1.00 15.90  ? 231 PHE B CE1 1 
ATOM   4168 C  CE2 . PHE B 1 230 ? 8.678   -27.967 -22.426 1.00 15.15  ? 231 PHE B CE2 1 
ATOM   4169 C  CZ  . PHE B 1 230 ? 9.443   -27.181 -23.292 1.00 14.85  ? 231 PHE B CZ  1 
ATOM   4170 N  N   . ASN B 1 231 ? 7.545   -24.945 -16.592 1.00 18.52  ? 232 ASN B N   1 
ATOM   4171 C  CA  . ASN B 1 231 ? 6.692   -24.305 -15.558 1.00 18.17  ? 232 ASN B CA  1 
ATOM   4172 C  C   . ASN B 1 231 ? 7.506   -23.381 -14.590 1.00 17.46  ? 232 ASN B C   1 
ATOM   4173 O  O   . ASN B 1 231 ? 8.698   -23.456 -14.478 1.00 19.55  ? 232 ASN B O   1 
ATOM   4174 C  CB  . ASN B 1 231 ? 6.026   -25.403 -14.751 1.00 21.56  ? 232 ASN B CB  1 
ATOM   4175 C  CG  . ASN B 1 231 ? 7.039   -26.349 -14.187 1.00 19.81  ? 232 ASN B CG  1 
ATOM   4176 O  OD1 . ASN B 1 231 ? 7.518   -27.237 -14.893 1.00 23.12  ? 232 ASN B OD1 1 
ATOM   4177 N  ND2 . ASN B 1 231 ? 7.367   -26.184 -12.884 1.00 24.03  ? 232 ASN B ND2 1 
ATOM   4178 N  N   . GLY B 1 232 ? 6.732   -22.484 -13.889 1.00 21.39  ? 233 GLY B N   1 
ATOM   4179 C  CA  . GLY B 1 232 ? 7.327   -21.659 -12.781 1.00 20.84  ? 233 GLY B CA  1 
ATOM   4180 C  C   . GLY B 1 232 ? 7.355   -22.409 -11.450 1.00 18.55  ? 233 GLY B C   1 
ATOM   4181 O  O   . GLY B 1 232 ? 6.709   -23.470 -11.417 1.00 25.32  ? 233 GLY B O   1 
ATOM   4182 N  N   . GLU B 1 233 ? 8.185   -21.924 -10.488 1.00 17.86  ? 234 GLU B N   1 
ATOM   4183 C  CA  . GLU B 1 233 ? 8.241   -22.499 -9.130  1.00 17.03  ? 234 GLU B CA  1 
ATOM   4184 C  C   . GLU B 1 233 ? 6.829   -22.627 -8.547  1.00 19.13  ? 234 GLU B C   1 
ATOM   4185 O  O   . GLU B 1 233 ? 5.974   -21.729 -8.655  1.00 23.16  ? 234 GLU B O   1 
ATOM   4186 C  CB  . GLU B 1 233 ? 9.127   -21.665 -8.220  1.00 19.41  ? 234 GLU B CB  1 
ATOM   4187 C  CG  . GLU B 1 233 ? 9.356   -22.219 -6.852  1.00 21.49  ? 234 GLU B CG  1 
ATOM   4188 C  CD  . GLU B 1 233 ? 10.133  -21.247 -6.016  1.00 34.17  ? 234 GLU B CD  1 
ATOM   4189 O  OE1 . GLU B 1 233 ? 10.426  -20.085 -6.504  1.00 30.96  ? 234 GLU B OE1 1 
ATOM   4190 O  OE2 . GLU B 1 233 ? 10.393  -21.657 -4.857  1.00 32.36  ? 234 GLU B OE2 1 
ATOM   4191 N  N   . GLY B 1 234 ? 6.536   -23.785 -7.989  1.00 25.09  ? 235 GLY B N   1 
ATOM   4192 C  CA  . GLY B 1 234 ? 5.249   -24.006 -7.324  1.00 25.08  ? 235 GLY B CA  1 
ATOM   4193 C  C   . GLY B 1 234 ? 4.175   -24.464 -8.254  1.00 30.86  ? 235 GLY B C   1 
ATOM   4194 O  O   . GLY B 1 234 ? 2.987   -24.545 -7.894  1.00 38.88  ? 235 GLY B O   1 
ATOM   4195 N  N   . GLU B 1 235 ? 4.589   -24.750 -9.487  1.00 27.17  ? 236 GLU B N   1 
ATOM   4196 C  CA  . GLU B 1 235 ? 3.586   -25.311 -10.443 1.00 20.70  ? 236 GLU B CA  1 
ATOM   4197 C  C   . GLU B 1 235 ? 3.935   -26.762 -10.809 1.00 31.02  ? 236 GLU B C   1 
ATOM   4198 O  O   . GLU B 1 235 ? 5.090   -27.178 -10.596 1.00 35.45  ? 236 GLU B O   1 
ATOM   4199 C  CB  . GLU B 1 235 ? 3.609   -24.503 -11.758 1.00 24.03  ? 236 GLU B CB  1 
ATOM   4200 C  CG  . GLU B 1 235 ? 3.076   -23.071 -11.595 1.00 28.96  ? 236 GLU B CG  1 
ATOM   4201 C  CD  . GLU B 1 235 ? 3.289   -22.176 -12.827 1.00 43.35  ? 236 GLU B CD  1 
ATOM   4202 O  OE1 . GLU B 1 235 ? 4.041   -22.572 -13.768 1.00 36.41  ? 236 GLU B OE1 1 
ATOM   4203 O  OE2 . GLU B 1 235 ? 2.684   -21.076 -12.863 1.00 46.09  ? 236 GLU B OE2 1 
ATOM   4204 N  N   . PRO B 1 236 ? 2.980   -27.519 -11.408 1.00 28.14  ? 237 PRO B N   1 
ATOM   4205 C  CA  . PRO B 1 236 ? 3.188   -28.943 -11.736 1.00 34.02  ? 237 PRO B CA  1 
ATOM   4206 C  C   . PRO B 1 236 ? 4.371   -29.061 -12.736 1.00 28.22  ? 237 PRO B C   1 
ATOM   4207 O  O   . PRO B 1 236 ? 4.436   -28.311 -13.725 1.00 26.25  ? 237 PRO B O   1 
ATOM   4208 C  CB  . PRO B 1 236 ? 1.912   -29.321 -12.469 1.00 40.03  ? 237 PRO B CB  1 
ATOM   4209 C  CG  . PRO B 1 236 ? 0.848   -28.389 -11.908 1.00 41.77  ? 237 PRO B CG  1 
ATOM   4210 C  CD  . PRO B 1 236 ? 1.577   -27.090 -11.662 1.00 35.90  ? 237 PRO B CD  1 
ATOM   4211 N  N   . GLU B 1 237 ? 5.276   -30.021 -12.498 1.00 23.15  ? 238 GLU B N   1 
ATOM   4212 C  CA  . GLU B 1 237 ? 6.495   -30.120 -13.284 1.00 22.98  ? 238 GLU B CA  1 
ATOM   4213 C  C   . GLU B 1 237 ? 6.260   -30.535 -14.713 1.00 22.15  ? 238 GLU B C   1 
ATOM   4214 O  O   . GLU B 1 237 ? 5.656   -31.557 -14.971 1.00 19.50  ? 238 GLU B O   1 
ATOM   4215 C  CB  . GLU B 1 237 ? 7.476   -31.115 -12.661 1.00 21.05  ? 238 GLU B CB  1 
ATOM   4216 C  CG  . GLU B 1 237 ? 8.828   -31.094 -13.383 1.00 22.80  ? 238 GLU B CG  1 
ATOM   4217 C  CD  . GLU B 1 237 ? 9.954   -31.797 -12.615 1.00 18.97  ? 238 GLU B CD  1 
ATOM   4218 O  OE1 . GLU B 1 237 ? 9.628   -32.877 -12.048 1.00 29.66  ? 238 GLU B OE1 1 
ATOM   4219 O  OE2 . GLU B 1 237 ? 11.133  -31.265 -12.523 1.00 22.73  ? 238 GLU B OE2 1 
ATOM   4220 N  N   . GLU B 1 238 ? 6.802   -29.740 -15.619 1.00 21.13  ? 239 GLU B N   1 
ATOM   4221 C  CA  . GLU B 1 238 ? 6.791   -29.980 -17.019 1.00 20.27  ? 239 GLU B CA  1 
ATOM   4222 C  C   . GLU B 1 238 ? 8.234   -29.838 -17.508 1.00 13.88  ? 239 GLU B C   1 
ATOM   4223 O  O   . GLU B 1 238 ? 8.728   -28.751 -17.600 1.00 18.44  ? 239 GLU B O   1 
ATOM   4224 C  CB  . GLU B 1 238 ? 6.001   -28.937 -17.756 1.00 21.25  ? 239 GLU B CB  1 
ATOM   4225 C  CG  . GLU B 1 238 ? 5.040   -29.600 -18.749 1.00 32.39  ? 239 GLU B CG  1 
ATOM   4226 C  CD  . GLU B 1 238 ? 3.765   -28.848 -19.118 1.00 54.59  ? 239 GLU B CD  1 
ATOM   4227 O  OE1 . GLU B 1 238 ? 3.617   -27.659 -18.770 1.00 58.28  ? 239 GLU B OE1 1 
ATOM   4228 O  OE2 . GLU B 1 238 ? 2.906   -29.466 -19.786 1.00 32.33  ? 239 GLU B OE2 1 
ATOM   4229 N  N   . LEU B 1 239 ? 8.885   -30.995 -17.780 1.00 14.19  ? 240 LEU B N   1 
ATOM   4230 C  CA  . LEU B 1 239 ? 10.255  -30.929 -18.106 1.00 12.85  ? 240 LEU B CA  1 
ATOM   4231 C  C   . LEU B 1 239 ? 10.440  -30.125 -19.421 1.00 13.20  ? 240 LEU B C   1 
ATOM   4232 O  O   . LEU B 1 239 ? 9.711   -30.317 -20.406 1.00 13.56  ? 240 LEU B O   1 
ATOM   4233 C  CB  . LEU B 1 239 ? 10.841  -32.328 -18.304 1.00 11.78  ? 240 LEU B CB  1 
ATOM   4234 C  CG  . LEU B 1 239 ? 10.898  -33.241 -17.113 1.00 12.70  ? 240 LEU B CG  1 
ATOM   4235 C  CD1 . LEU B 1 239 ? 11.487  -34.550 -17.552 1.00 18.51  ? 240 LEU B CD1 1 
ATOM   4236 C  CD2 . LEU B 1 239 ? 11.668  -32.494 -16.023 1.00 14.84  ? 240 LEU B CD2 1 
ATOM   4237 N  N   . MET B 1 240 ? 11.501  -29.315 -19.414 1.00 12.48  ? 241 MET B N   1 
ATOM   4238 C  CA  . MET B 1 240 ? 11.887  -28.487 -20.608 1.00 14.22  ? 241 MET B CA  1 
ATOM   4239 C  C   . MET B 1 240 ? 12.678  -29.413 -21.522 1.00 11.63  ? 241 MET B C   1 
ATOM   4240 O  O   . MET B 1 240 ? 13.861  -29.564 -21.444 1.00 12.15  ? 241 MET B O   1 
ATOM   4241 C  CB  . MET B 1 240 ? 12.754  -27.325 -20.111 1.00 14.29  ? 241 MET B CB  1 
ATOM   4242 C  CG  . MET B 1 240 ? 13.097  -26.329 -21.285 1.00 13.15  ? 241 MET B CG  1 
ATOM   4243 S  SD  . MET B 1 240 ? 14.025  -24.931 -20.760 1.00 15.17  ? 241 MET B SD  1 
ATOM   4244 C  CE  . MET B 1 240 ? 12.685  -23.879 -20.149 1.00 16.36  ? 241 MET B CE  1 
ATOM   4245 N  N   . VAL B 1 241 ? 11.905  -30.001 -22.473 1.00 11.39  ? 242 VAL B N   1 
ATOM   4246 C  CA  . VAL B 1 241 ? 12.416  -30.888 -23.525 1.00 10.34  ? 242 VAL B CA  1 
ATOM   4247 C  C   . VAL B 1 241 ? 11.617  -30.665 -24.782 1.00 10.87  ? 242 VAL B C   1 
ATOM   4248 O  O   . VAL B 1 241 ? 10.452  -30.236 -24.722 1.00 11.66  ? 242 VAL B O   1 
ATOM   4249 C  CB  . VAL B 1 241 ? 12.364  -32.382 -23.098 1.00 10.92  ? 242 VAL B CB  1 
ATOM   4250 C  CG1 . VAL B 1 241 ? 13.274  -32.678 -21.930 1.00 12.72  ? 242 VAL B CG1 1 
ATOM   4251 C  CG2 . VAL B 1 241 ? 10.917  -32.854 -22.918 1.00 13.75  ? 242 VAL B CG2 1 
ATOM   4252 N  N   . ASP B 1 242 ? 12.220  -30.965 -25.923 1.00 9.98   ? 243 ASP B N   1 
ATOM   4253 C  CA  . ASP B 1 242 ? 11.584  -30.832 -27.198 1.00 9.71   ? 243 ASP B CA  1 
ATOM   4254 C  C   . ASP B 1 242 ? 11.097  -29.359 -27.461 1.00 9.48   ? 243 ASP B C   1 
ATOM   4255 O  O   . ASP B 1 242 ? 9.973   -29.148 -27.938 1.00 11.73  ? 243 ASP B O   1 
ATOM   4256 C  CB  . ASP B 1 242 ? 10.473  -31.867 -27.412 1.00 10.27  ? 243 ASP B CB  1 
ATOM   4257 C  CG  . ASP B 1 242 ? 11.050  -33.276 -27.545 1.00 10.53  ? 243 ASP B CG  1 
ATOM   4258 O  OD1 . ASP B 1 242 ? 12.115  -33.448 -28.168 1.00 9.76   ? 243 ASP B OD1 1 
ATOM   4259 O  OD2 . ASP B 1 242 ? 10.466  -34.206 -26.919 1.00 12.93  ? 243 ASP B OD2 1 
ATOM   4260 N  N   . ASN B 1 243 ? 11.989  -28.434 -27.169 1.00 9.10   ? 244 ASN B N   1 
ATOM   4261 C  CA  . ASN B 1 243 ? 11.725  -27.024 -27.381 1.00 9.05   ? 244 ASN B CA  1 
ATOM   4262 C  C   . ASN B 1 243 ? 12.254  -26.584 -28.770 1.00 8.33   ? 244 ASN B C   1 
ATOM   4263 O  O   . ASN B 1 243 ? 12.938  -25.560 -28.846 1.00 9.67   ? 244 ASN B O   1 
ATOM   4264 C  CB  . ASN B 1 243 ? 12.242  -26.159 -26.228 1.00 9.49   ? 244 ASN B CB  1 
ATOM   4265 C  CG  . ASN B 1 243 ? 13.706  -26.382 -25.959 1.00 9.41   ? 244 ASN B CG  1 
ATOM   4266 O  OD1 . ASN B 1 243 ? 14.375  -27.219 -26.573 1.00 10.51  ? 244 ASN B OD1 1 
ATOM   4267 N  ND2 . ASN B 1 243 ? 14.236  -25.585 -25.037 1.00 14.63  ? 244 ASN B ND2 1 
ATOM   4268 N  N   . TRP B 1 244 ? 11.960  -27.358 -29.803 1.00 8.09   ? 245 TRP B N   1 
ATOM   4269 C  CA  . TRP B 1 244 ? 12.424  -27.086 -31.149 1.00 7.85   ? 245 TRP B CA  1 
ATOM   4270 C  C   . TRP B 1 244 ? 11.221  -27.010 -32.060 1.00 8.71   ? 245 TRP B C   1 
ATOM   4271 O  O   . TRP B 1 244 ? 10.209  -27.723 -31.910 1.00 10.06  ? 245 TRP B O   1 
ATOM   4272 C  CB  . TRP B 1 244 ? 13.384  -28.191 -31.680 1.00 8.05   ? 245 TRP B CB  1 
ATOM   4273 C  CG  . TRP B 1 244 ? 12.906  -29.583 -31.489 1.00 8.20   ? 245 TRP B CG  1 
ATOM   4274 C  CD1 . TRP B 1 244 ? 13.008  -30.353 -30.356 1.00 8.47   ? 245 TRP B CD1 1 
ATOM   4275 C  CD2 . TRP B 1 244 ? 12.320  -30.471 -32.466 1.00 8.38   ? 245 TRP B CD2 1 
ATOM   4276 N  NE1 . TRP B 1 244 ? 12.501  -31.624 -30.530 1.00 8.67   ? 245 TRP B NE1 1 
ATOM   4277 C  CE2 . TRP B 1 244 ? 12.067  -31.741 -31.827 1.00 9.22   ? 245 TRP B CE2 1 
ATOM   4278 C  CE3 . TRP B 1 244 ? 12.005  -30.324 -33.813 1.00 9.80   ? 245 TRP B CE3 1 
ATOM   4279 C  CZ2 . TRP B 1 244 ? 11.498  -32.785 -32.500 1.00 10.13  ? 245 TRP B CZ2 1 
ATOM   4280 C  CZ3 . TRP B 1 244 ? 11.446  -31.378 -34.485 1.00 11.08  ? 245 TRP B CZ3 1 
ATOM   4281 C  CH2 . TRP B 1 244 ? 11.172  -32.617 -33.820 1.00 11.55  ? 245 TRP B CH2 1 
ATOM   4282 N  N   . ARG B 1 245 ? 11.318  -26.136 -33.065 1.00 8.02   ? 246 ARG B N   1 
ATOM   4283 C  CA  . ARG B 1 245 ? 10.374  -25.993 -34.164 1.00 8.50   ? 246 ARG B CA  1 
ATOM   4284 C  C   . ARG B 1 245 ? 10.847  -26.929 -35.298 1.00 7.78   ? 246 ARG B C   1 
ATOM   4285 O  O   . ARG B 1 245 ? 12.043  -26.914 -35.627 1.00 9.22   ? 246 ARG B O   1 
ATOM   4286 C  CB  . ARG B 1 245 ? 10.304  -24.561 -34.646 1.00 7.78   ? 246 ARG B CB  1 
ATOM   4287 C  CG  . ARG B 1 245 ? 9.205   -24.306 -35.675 1.00 8.33   ? 246 ARG B CG  1 
ATOM   4288 C  CD  . ARG B 1 245 ? 9.274   -22.976 -36.327 1.00 9.11   ? 246 ARG B CD  1 
ATOM   4289 N  NE  . ARG B 1 245 ? 8.008   -22.612 -36.953 1.00 9.85   ? 246 ARG B NE  1 
ATOM   4290 C  CZ  . ARG B 1 245 ? 7.827   -21.603 -37.806 1.00 9.19   ? 246 ARG B CZ  1 
ATOM   4291 N  NH1 . ARG B 1 245 ? 8.838   -20.826 -38.176 1.00 9.82   ? 246 ARG B NH1 1 
ATOM   4292 N  NH2 . ARG B 1 245 ? 6.616   -21.378 -38.294 1.00 11.46  ? 246 ARG B NH2 1 
ATOM   4293 N  N   A PRO B 1 246 ? 9.944   -27.692 -35.913 0.50 9.31   ? 247 PRO B N   1 
ATOM   4294 N  N   B PRO B 1 246 ? 9.953   -27.730 -35.901 0.50 8.93   ? 247 PRO B N   1 
ATOM   4295 C  CA  A PRO B 1 246 ? 10.306  -28.536 -37.054 0.50 9.10   ? 247 PRO B CA  1 
ATOM   4296 C  CA  B PRO B 1 246 ? 10.420  -28.537 -37.032 0.50 10.15  ? 247 PRO B CA  1 
ATOM   4297 C  C   A PRO B 1 246 ? 10.705  -27.732 -38.284 0.50 8.98   ? 247 PRO B C   1 
ATOM   4298 C  C   B PRO B 1 246 ? 10.775  -27.720 -38.260 0.50 8.77   ? 247 PRO B C   1 
ATOM   4299 O  O   A PRO B 1 246 ? 10.308  -26.533 -38.431 0.50 8.92   ? 247 PRO B O   1 
ATOM   4300 O  O   B PRO B 1 246 ? 10.399  -26.523 -38.398 0.50 9.86   ? 247 PRO B O   1 
ATOM   4301 C  CB  A PRO B 1 246 ? 9.058   -29.342 -37.305 0.50 12.51  ? 247 PRO B CB  1 
ATOM   4302 C  CB  B PRO B 1 246 ? 9.259   -29.448 -37.334 0.50 13.26  ? 247 PRO B CB  1 
ATOM   4303 C  CG  A PRO B 1 246 ? 8.350   -29.305 -35.997 0.50 11.04  ? 247 PRO B CG  1 
ATOM   4304 C  CG  B PRO B 1 246 ? 8.081   -28.646 -36.916 0.50 15.02  ? 247 PRO B CG  1 
ATOM   4305 C  CD  A PRO B 1 246 ? 8.550   -27.911 -35.506 0.50 10.78  ? 247 PRO B CD  1 
ATOM   4306 C  CD  B PRO B 1 246 ? 8.503   -27.888 -35.686 0.50 12.46  ? 247 PRO B CD  1 
ATOM   4307 N  N   . ALA B 1 247 ? 11.373  -28.396 -39.223 1.00 9.62   ? 248 ALA B N   1 
ATOM   4308 C  CA  . ALA B 1 247 ? 11.725  -27.738 -40.497 1.00 9.89   ? 248 ALA B CA  1 
ATOM   4309 C  C   . ALA B 1 247 ? 10.485  -27.239 -41.232 1.00 9.72   ? 248 ALA B C   1 
ATOM   4310 O  O   . ALA B 1 247 ? 9.428   -27.898 -41.261 1.00 10.92  ? 248 ALA B O   1 
ATOM   4311 C  CB  . ALA B 1 247 ? 12.487  -28.754 -41.384 1.00 12.59  ? 248 ALA B CB  1 
ATOM   4312 N  N   . GLN B 1 248 ? 10.589  -26.027 -41.816 1.00 8.92   ? 249 GLN B N   1 
ATOM   4313 C  CA  . GLN B 1 248 ? 9.518   -25.321 -42.520 1.00 9.44   ? 249 GLN B CA  1 
ATOM   4314 C  C   . GLN B 1 248 ? 9.817   -25.337 -44.004 1.00 9.50   ? 249 GLN B C   1 
ATOM   4315 O  O   . GLN B 1 248 ? 10.961  -25.554 -44.463 1.00 10.72  ? 249 GLN B O   1 
ATOM   4316 C  CB  . GLN B 1 248 ? 9.493   -23.857 -41.981 1.00 10.59  ? 249 GLN B CB  1 
ATOM   4317 C  CG  . GLN B 1 248 ? 9.167   -23.792 -40.496 1.00 10.66  ? 249 GLN B CG  1 
ATOM   4318 C  CD  . GLN B 1 248 ? 7.863   -24.469 -40.165 1.00 11.60  ? 249 GLN B CD  1 
ATOM   4319 O  OE1 . GLN B 1 248 ? 6.825   -24.110 -40.736 1.00 14.12  ? 249 GLN B OE1 1 
ATOM   4320 N  NE2 . GLN B 1 248 ? 7.853   -25.423 -39.216 1.00 12.69  ? 249 GLN B NE2 1 
ATOM   4321 N  N   . PRO B 1 249 ? 8.836   -25.005 -44.840 1.00 12.05  ? 250 PRO B N   1 
ATOM   4322 C  CA  . PRO B 1 249 ? 9.039   -25.071 -46.314 1.00 14.34  ? 250 PRO B CA  1 
ATOM   4323 C  C   . PRO B 1 249 ? 10.113  -24.073 -46.765 1.00 11.12  ? 250 PRO B C   1 
ATOM   4324 O  O   . PRO B 1 249 ? 10.090  -22.890 -46.397 1.00 11.46  ? 250 PRO B O   1 
ATOM   4325 C  CB  . PRO B 1 249 ? 7.630   -24.717 -46.890 1.00 16.89  ? 250 PRO B CB  1 
ATOM   4326 C  CG  . PRO B 1 249 ? 6.712   -25.031 -45.804 1.00 18.64  ? 250 PRO B CG  1 
ATOM   4327 C  CD  . PRO B 1 249 ? 7.415   -24.843 -44.466 1.00 16.69  ? 250 PRO B CD  1 
ATOM   4328 N  N   . LEU B 1 250 ? 10.995  -24.550 -47.648 1.00 12.11  ? 251 LEU B N   1 
ATOM   4329 C  CA  . LEU B 1 250 ? 12.059  -23.668 -48.154 1.00 10.92  ? 251 LEU B CA  1 
ATOM   4330 C  C   . LEU B 1 250 ? 11.510  -22.626 -49.075 1.00 11.23  ? 251 LEU B C   1 
ATOM   4331 O  O   . LEU B 1 250 ? 12.075  -21.521 -49.157 1.00 11.33  ? 251 LEU B O   1 
ATOM   4332 C  CB  . LEU B 1 250 ? 13.075  -24.563 -48.889 1.00 13.59  ? 251 LEU B CB  1 
ATOM   4333 C  CG  . LEU B 1 250 ? 14.355  -23.825 -49.334 1.00 13.71  ? 251 LEU B CG  1 
ATOM   4334 C  CD1 . LEU B 1 250 ? 15.173  -23.306 -48.143 1.00 14.94  ? 251 LEU B CD1 1 
ATOM   4335 C  CD2 . LEU B 1 250 ? 15.251  -24.776 -50.114 1.00 18.54  ? 251 LEU B CD2 1 
ATOM   4336 N  N   . LYS B 1 251 ? 10.419  -22.886 -49.799 1.00 13.53  ? 252 LYS B N   1 
ATOM   4337 C  CA  . LYS B 1 251 ? 9.794   -21.867 -50.706 1.00 14.62  ? 252 LYS B CA  1 
ATOM   4338 C  C   . LYS B 1 251 ? 10.814  -21.319 -51.675 1.00 15.53  ? 252 LYS B C   1 
ATOM   4339 O  O   . LYS B 1 251 ? 11.593  -22.129 -52.209 1.00 17.73  ? 252 LYS B O   1 
ATOM   4340 C  CB  . LYS B 1 251 ? 9.049   -20.796 -49.899 1.00 16.59  ? 252 LYS B CB  1 
ATOM   4341 C  CG  . LYS B 1 251 ? 7.939   -21.476 -49.115 1.00 20.29  ? 252 LYS B CG  1 
ATOM   4342 C  CD  . LYS B 1 251 ? 6.956   -20.515 -48.509 1.00 22.00  ? 252 LYS B CD  1 
ATOM   4343 C  CE  . LYS B 1 251 ? 5.868   -21.281 -47.897 1.00 26.66  ? 252 LYS B CE  1 
ATOM   4344 N  NZ  . LYS B 1 251 ? 4.935   -20.389 -47.156 1.00 30.33  ? 252 LYS B NZ  1 
ATOM   4345 N  N   . ASN B 1 252 ? 10.878  -20.024 -51.888 1.00 14.60  ? 253 ASN B N   1 
ATOM   4346 C  CA  . ASN B 1 252 ? 11.696  -19.529 -52.928 1.00 23.10  ? 253 ASN B CA  1 
ATOM   4347 C  C   . ASN B 1 252 ? 13.015  -19.111 -52.328 1.00 21.17  ? 253 ASN B C   1 
ATOM   4348 O  O   . ASN B 1 252 ? 13.197  -17.806 -52.337 1.00 24.03  ? 253 ASN B O   1 
ATOM   4349 C  CB  . ASN B 1 252 ? 10.976  -18.311 -53.605 1.00 29.66  ? 253 ASN B CB  1 
ATOM   4350 C  CG  . ASN B 1 252 ? 11.746  -17.757 -54.808 1.00 29.06  ? 253 ASN B CG  1 
ATOM   4351 O  OD1 . ASN B 1 252 ? 12.245  -18.517 -55.643 1.00 48.55  ? 253 ASN B OD1 1 
ATOM   4352 N  ND2 . ASN B 1 252 ? 11.843  -16.438 -54.911 1.00 42.62  ? 253 ASN B ND2 1 
ATOM   4353 N  N   . ARG B 1 253 ? 13.819  -20.117 -51.721 1.00 16.52  ? 254 ARG B N   1 
ATOM   4354 C  CA  . ARG B 1 253 ? 15.122  -19.794 -51.226 1.00 11.76  ? 254 ARG B CA  1 
ATOM   4355 C  C   . ARG B 1 253 ? 16.200  -20.714 -51.649 1.00 12.98  ? 254 ARG B C   1 
ATOM   4356 O  O   . ARG B 1 253 ? 15.981  -21.919 -51.825 1.00 21.78  ? 254 ARG B O   1 
ATOM   4357 C  CB  . ARG B 1 253 ? 15.098  -19.748 -49.703 1.00 11.67  ? 254 ARG B CB  1 
ATOM   4358 C  CG  . ARG B 1 253 ? 14.179  -18.625 -49.192 1.00 11.86  ? 254 ARG B CG  1 
ATOM   4359 C  CD  . ARG B 1 253 ? 14.034  -18.648 -47.694 1.00 10.18  ? 254 ARG B CD  1 
ATOM   4360 N  NE  . ARG B 1 253 ? 13.187  -19.752 -47.224 1.00 10.14  ? 254 ARG B NE  1 
ATOM   4361 C  CZ  . ARG B 1 253 ? 12.954  -20.003 -45.947 1.00 8.78   ? 254 ARG B CZ  1 
ATOM   4362 N  NH1 . ARG B 1 253 ? 13.568  -19.329 -44.964 1.00 8.84   ? 254 ARG B NH1 1 
ATOM   4363 N  NH2 . ARG B 1 253 ? 12.130  -20.994 -45.602 1.00 9.04   ? 254 ARG B NH2 1 
ATOM   4364 N  N   . GLN B 1 254 ? 17.405  -20.194 -51.727 1.00 12.98  ? 255 GLN B N   1 
ATOM   4365 C  CA  . GLN B 1 254 ? 18.614  -20.944 -51.990 1.00 14.14  ? 255 GLN B CA  1 
ATOM   4366 C  C   . GLN B 1 254 ? 19.492  -20.971 -50.739 1.00 11.76  ? 255 GLN B C   1 
ATOM   4367 O  O   . GLN B 1 254 ? 19.716  -19.940 -50.101 1.00 16.13  ? 255 GLN B O   1 
ATOM   4368 C  CB  . GLN B 1 254 ? 19.431  -20.301 -53.114 1.00 20.16  ? 255 GLN B CB  1 
ATOM   4369 C  CG  . GLN B 1 254 ? 18.976  -20.691 -54.493 1.00 29.15  ? 255 GLN B CG  1 
ATOM   4370 C  CD  . GLN B 1 254 ? 20.168  -20.695 -55.410 1.00 34.59  ? 255 GLN B CD  1 
ATOM   4371 O  OE1 . GLN B 1 254 ? 20.720  -21.758 -55.723 1.00 45.06  ? 255 GLN B OE1 1 
ATOM   4372 N  NE2 . GLN B 1 254 ? 20.626  -19.522 -55.795 1.00 46.83  ? 255 GLN B NE2 1 
ATOM   4373 N  N   A ILE B 1 255 ? 19.963  -22.171 -50.378 0.50 10.49  ? 256 ILE B N   1 
ATOM   4374 N  N   B ILE B 1 255 ? 19.933  -22.159 -50.364 0.50 10.52  ? 256 ILE B N   1 
ATOM   4375 C  CA  A ILE B 1 255 ? 20.944  -22.330 -49.320 0.50 10.08  ? 256 ILE B CA  1 
ATOM   4376 C  CA  B ILE B 1 255 ? 20.946  -22.322 -49.329 0.50 10.09  ? 256 ILE B CA  1 
ATOM   4377 C  C   A ILE B 1 255 ? 22.343  -22.351 -50.008 0.50 10.94  ? 256 ILE B C   1 
ATOM   4378 C  C   B ILE B 1 255 ? 22.334  -22.375 -50.005 0.50 10.95  ? 256 ILE B C   1 
ATOM   4379 O  O   A ILE B 1 255 ? 22.546  -23.077 -51.006 0.50 13.01  ? 256 ILE B O   1 
ATOM   4380 O  O   B ILE B 1 255 ? 22.517  -23.095 -51.001 0.50 13.02  ? 256 ILE B O   1 
ATOM   4381 C  CB  A ILE B 1 255 ? 20.676  -23.570 -48.517 0.50 11.31  ? 256 ILE B CB  1 
ATOM   4382 C  CB  B ILE B 1 255 ? 20.683  -23.570 -48.514 0.50 11.31  ? 256 ILE B CB  1 
ATOM   4383 C  CG1 A ILE B 1 255 ? 19.245  -23.542 -47.946 0.50 11.69  ? 256 ILE B CG1 1 
ATOM   4384 C  CG1 B ILE B 1 255 ? 19.245  -23.557 -47.966 0.50 11.76  ? 256 ILE B CG1 1 
ATOM   4385 C  CG2 A ILE B 1 255 ? 21.736  -23.735 -47.404 0.50 10.90  ? 256 ILE B CG2 1 
ATOM   4386 C  CG2 B ILE B 1 255 ? 21.764  -23.742 -47.443 0.50 10.95  ? 256 ILE B CG2 1 
ATOM   4387 C  CD1 A ILE B 1 255 ? 18.935  -24.783 -47.126 0.50 11.08  ? 256 ILE B CD1 1 
ATOM   4388 C  CD1 B ILE B 1 255 ? 19.107  -22.823 -46.699 0.50 15.58  ? 256 ILE B CD1 1 
ATOM   4389 N  N   . LYS B 1 256 ? 23.235  -21.529 -49.521 1.00 10.45  ? 257 LYS B N   1 
ATOM   4390 C  CA  . LYS B 1 256 ? 24.583  -21.430 -50.065 1.00 10.46  ? 257 LYS B CA  1 
ATOM   4391 C  C   . LYS B 1 256 ? 25.583  -22.055 -49.094 1.00 9.93   ? 257 LYS B C   1 
ATOM   4392 O  O   . LYS B 1 256 ? 25.420  -21.915 -47.894 1.00 13.37  ? 257 LYS B O   1 
ATOM   4393 C  CB  . LYS B 1 256 ? 24.951  -19.953 -50.356 1.00 12.47  ? 257 LYS B CB  1 
ATOM   4394 C  CG  . LYS B 1 256 ? 23.983  -19.385 -51.409 1.00 16.75  ? 257 LYS B CG  1 
ATOM   4395 C  CD  . LYS B 1 256 ? 24.195  -18.026 -51.852 1.00 20.73  ? 257 LYS B CD  1 
ATOM   4396 C  CE  . LYS B 1 256 ? 22.990  -17.663 -52.744 1.00 24.07  ? 257 LYS B CE  1 
ATOM   4397 N  NZ  . LYS B 1 256 ? 22.920  -16.217 -53.195 1.00 29.65  ? 257 LYS B NZ  1 
ATOM   4398 N  N   . ALA B 1 257 ? 26.605  -22.675 -49.632 1.00 11.02  ? 258 ALA B N   1 
ATOM   4399 C  CA  . ALA B 1 257 ? 27.678  -23.290 -48.862 1.00 10.85  ? 258 ALA B CA  1 
ATOM   4400 C  C   . ALA B 1 257 ? 28.962  -22.481 -49.007 1.00 10.60  ? 258 ALA B C   1 
ATOM   4401 O  O   . ALA B 1 257 ? 29.321  -22.053 -50.129 1.00 12.65  ? 258 ALA B O   1 
ATOM   4402 C  CB  . ALA B 1 257 ? 27.964  -24.739 -49.290 1.00 13.80  ? 258 ALA B CB  1 
ATOM   4403 N  N   . SER B 1 258 ? 29.691  -22.305 -47.896 1.00 10.96  ? 259 SER B N   1 
ATOM   4404 C  CA  . SER B 1 258 ? 30.953  -21.608 -47.928 1.00 12.47  ? 259 SER B CA  1 
ATOM   4405 C  C   . SER B 1 258 ? 32.116  -22.515 -48.349 1.00 12.63  ? 259 SER B C   1 
ATOM   4406 O  O   . SER B 1 258 ? 33.225  -21.996 -48.523 1.00 17.23  ? 259 SER B O   1 
ATOM   4407 C  CB  . SER B 1 258 ? 31.298  -21.021 -46.567 1.00 13.47  ? 259 SER B CB  1 
ATOM   4408 O  OG  . SER B 1 258 ? 31.693  -22.064 -45.658 1.00 12.25  ? 259 SER B OG  1 
ATOM   4409 N  N   . PHE B 1 259 ? 31.843  -23.791 -48.595 1.00 14.37  ? 260 PHE B N   1 
ATOM   4410 C  CA  . PHE B 1 259 ? 32.899  -24.800 -48.775 1.00 17.42  ? 260 PHE B CA  1 
ATOM   4411 C  C   . PHE B 1 259 ? 32.506  -25.725 -49.898 1.00 19.54  ? 260 PHE B C   1 
ATOM   4412 O  O   . PHE B 1 259 ? 31.314  -25.884 -50.182 1.00 20.23  ? 260 PHE B O   1 
ATOM   4413 C  CB  . PHE B 1 259 ? 33.076  -25.613 -47.473 1.00 16.87  ? 260 PHE B CB  1 
ATOM   4414 C  CG  . PHE B 1 259 ? 31.798  -26.332 -47.069 1.00 15.24  ? 260 PHE B CG  1 
ATOM   4415 C  CD1 . PHE B 1 259 ? 30.818  -25.655 -46.332 1.00 13.75  ? 260 PHE B CD1 1 
ATOM   4416 C  CD2 . PHE B 1 259 ? 31.540  -27.640 -47.478 1.00 19.17  ? 260 PHE B CD2 1 
ATOM   4417 C  CE1 . PHE B 1 259 ? 29.560  -26.276 -46.045 1.00 15.75  ? 260 PHE B CE1 1 
ATOM   4418 C  CE2 . PHE B 1 259 ? 30.331  -28.236 -47.175 1.00 19.81  ? 260 PHE B CE2 1 
ATOM   4419 C  CZ  . PHE B 1 259 ? 29.334  -27.583 -46.483 1.00 19.24  ? 260 PHE B CZ  1 
ATOM   4420 N  N   . LYS B 1 260 ? 33.513  -26.398 -50.461 1.00 27.58  ? 261 LYS B N   1 
ATOM   4421 C  CA  . LYS B 1 260 ? 33.385  -27.546 -51.387 1.00 36.54  ? 261 LYS B CA  1 
ATOM   4422 C  C   . LYS B 1 260 ? 32.662  -27.329 -52.722 1.00 45.83  ? 261 LYS B C   1 
ATOM   4423 O  O   . LYS B 1 260 ? 31.440  -27.208 -52.800 0.01 35.52  ? 261 LYS B O   1 
ATOM   4424 C  CB  . LYS B 1 260 ? 32.893  -28.848 -50.714 1.00 46.35  ? 261 LYS B CB  1 
ATOM   4425 C  CG  . LYS B 1 260 ? 33.791  -29.374 -49.600 1.00 48.92  ? 261 LYS B CG  1 
ATOM   4426 C  CD  . LYS B 1 260 ? 33.443  -30.833 -49.224 1.00 55.70  ? 261 LYS B CD  1 
ATOM   4427 C  CE  . LYS B 1 260 ? 32.032  -31.026 -48.625 1.00 42.89  ? 261 LYS B CE  1 
ATOM   4428 N  NZ  . LYS B 1 260 ? 31.712  -32.432 -48.201 1.00 56.12  ? 261 LYS B NZ  1 
ATOM   4429 O  OXT . LYS B 1 260 ? 33.334  -27.303 -53.758 1.00 66.51  ? 261 LYS B OXT 1 
HETATM 4430 ZN ZN  . ZN  C 2 .   ? 3.537   0.061   -0.476  1.00 6.55   ? 301 ZN  A ZN  1 
HETATM 4431 S  S   . DMS D 3 .   ? 11.557  -9.930  -0.865  1.00 21.44  ? 302 DMS A S   1 
HETATM 4432 O  O   . DMS D 3 .   ? 12.119  -11.296 -1.268  1.00 26.87  ? 302 DMS A O   1 
HETATM 4433 C  C1  . DMS D 3 .   ? 11.881  -9.730  0.778   1.00 18.55  ? 302 DMS A C1  1 
HETATM 4434 C  C2  . DMS D 3 .   ? 12.671  -8.708  -1.286  1.00 22.89  ? 302 DMS A C2  1 
HETATM 4435 N  N1  . BCN E 4 .   ? -10.287 -12.978 7.631   1.00 25.47  ? 303 BCN A N1  1 
HETATM 4436 C  C1  . BCN E 4 .   ? -9.296  -12.427 8.572   1.00 23.97  ? 303 BCN A C1  1 
HETATM 4437 C  C2  . BCN E 4 .   ? -9.671  -13.320 9.775   1.00 23.08  ? 303 BCN A C2  1 
HETATM 4438 O  O21 . BCN E 4 .   ? -10.618 -14.168 9.723   1.00 29.23  ? 303 BCN A O21 1 
HETATM 4439 O  O22 . BCN E 4 .   ? -9.065  -13.213 10.822  1.00 25.63  ? 303 BCN A O22 1 
HETATM 4440 C  C3  . BCN E 4 .   ? -11.403 -12.128 7.312   1.00 17.03  ? 303 BCN A C3  1 
HETATM 4441 C  C4  . BCN E 4 .   ? -12.049 -12.263 5.953   1.00 32.66  ? 303 BCN A C4  1 
HETATM 4442 O  O4  . BCN E 4 .   ? -13.395 -12.795 6.013   1.00 49.46  ? 303 BCN A O4  1 
HETATM 4443 C  C5  . BCN E 4 .   ? -9.757  -13.772 6.544   1.00 15.39  ? 303 BCN A C5  1 
HETATM 4444 C  C6  . BCN E 4 .   ? -10.440 -14.889 5.781   1.00 32.77  ? 303 BCN A C6  1 
HETATM 4445 O  O6  . BCN E 4 .   ? -10.651 -14.523 4.375   1.00 32.94  ? 303 BCN A O6  1 
HETATM 4446 C  C1  . PEG F 5 .   ? 11.766  -13.614 3.610   1.00 41.22  ? 304 PEG A C1  1 
HETATM 4447 O  O1  . PEG F 5 .   ? 12.117  -14.311 2.405   1.00 43.66  ? 304 PEG A O1  1 
HETATM 4448 C  C2  . PEG F 5 .   ? 12.716  -12.454 3.968   1.00 32.27  ? 304 PEG A C2  1 
HETATM 4449 O  O2  . PEG F 5 .   ? 12.645  -12.227 5.382   1.00 31.06  ? 304 PEG A O2  1 
HETATM 4450 C  C3  . PEG F 5 .   ? 13.896  -11.606 5.907   1.00 32.16  ? 304 PEG A C3  1 
HETATM 4451 C  C4  . PEG F 5 .   ? 13.522  -10.989 7.268   1.00 30.33  ? 304 PEG A C4  1 
HETATM 4452 O  O4  . PEG F 5 .   ? 14.368  -9.880  7.704   1.00 31.64  ? 304 PEG A O4  1 
HETATM 4453 C  C1  . MLA G 6 .   ? 5.058   10.605  -5.518  1.00 42.37  ? 305 MLA A C1  1 
HETATM 4454 O  O1A . MLA G 6 .   ? 5.854   10.214  -4.621  1.00 47.29  ? 305 MLA A O1A 1 
HETATM 4455 O  O1B . MLA G 6 .   ? 5.444   10.962  -6.663  1.00 51.35  ? 305 MLA A O1B 1 
HETATM 4456 C  C2  . MLA G 6 .   ? 3.602   10.467  -5.216  1.00 38.67  ? 305 MLA A C2  1 
HETATM 4457 C  C3  . MLA G 6 .   ? 3.653   9.026   -4.750  1.00 40.32  ? 305 MLA A C3  1 
HETATM 4458 O  O3A . MLA G 6 .   ? 3.857   8.059   -5.526  1.00 30.68  ? 305 MLA A O3A 1 
HETATM 4459 O  O3B . MLA G 6 .   ? 3.481   8.700   -3.550  1.00 35.75  ? 305 MLA A O3B 1 
HETATM 4460 O  O12 . 6YH H 7 .   ? 5.835   8.071   -2.555  1.00 17.34  ? 306 6YH A O12 1 
HETATM 4461 C  C11 . 6YH H 7 .   ? 6.542   7.097   -2.283  1.00 13.40  ? 306 6YH A C11 1 
HETATM 4462 C  C4  . 6YH H 7 .   ? 6.016   5.975   -1.480  1.00 11.40  ? 306 6YH A C4  1 
HETATM 4463 C  C3  . 6YH H 7 .   ? 4.681   6.039   -1.090  1.00 10.14  ? 306 6YH A C3  1 
HETATM 4464 C  C2  . 6YH H 7 .   ? 4.196   4.992   -0.294  1.00 9.19   ? 306 6YH A C2  1 
HETATM 4465 C  C5  . 6YH H 7 .   ? 6.836   4.930   -1.052  1.00 12.36  ? 306 6YH A C5  1 
HETATM 4466 C  C6  . 6YH H 7 .   ? 6.343   3.906   -0.275  1.00 10.76  ? 306 6YH A C6  1 
HETATM 4467 C  C1  . 6YH H 7 .   ? 4.982   3.913   0.060   1.00 8.82   ? 306 6YH A C1  1 
HETATM 4468 S  S7  . 6YH H 7 .   ? 4.310   2.588   1.018   1.00 7.04   ? 306 6YH A S7  1 
HETATM 4469 O  O9  . 6YH H 7 .   ? 4.906   2.767   2.342   1.00 7.38   ? 306 6YH A O9  1 
HETATM 4470 N  N10 . 6YH H 7 .   ? 4.822   1.217   0.369   1.00 6.90   ? 306 6YH A N10 1 
HETATM 4471 O  O8  . 6YH H 7 .   ? 2.907   2.687   0.912   1.00 7.20   ? 306 6YH A O8  1 
HETATM 4472 C  C13 . 6YH H 7 .   ? 8.038   7.106   -2.415  1.00 16.16  ? 306 6YH A C13 1 
HETATM 4473 N  N14 . 6YH H 7 .   ? 8.407   8.340   -3.135  1.00 16.67  ? 306 6YH A N14 1 
HETATM 4474 C  C18 . 6YH H 7 .   ? 8.674   9.513   -2.480  1.00 16.31  ? 306 6YH A C18 1 
HETATM 4475 C  C20 . 6YH H 7 .   ? 8.744   9.769   -1.166  1.00 16.08  ? 306 6YH A C20 1 
HETATM 4476 C  C21 . 6YH H 7 .   ? 9.105   11.043  -0.750  1.00 17.74  ? 306 6YH A C21 1 
HETATM 4477 C  C22 . 6YH H 7 .   ? 9.332   12.051  -1.673  1.00 19.93  ? 306 6YH A C22 1 
HETATM 4478 C  C23 . 6YH H 7 .   ? 9.279   11.796  -3.030  1.00 21.73  ? 306 6YH A C23 1 
HETATM 4479 C  C19 . 6YH H 7 .   ? 8.951   10.471  -3.402  1.00 18.41  ? 306 6YH A C19 1 
HETATM 4480 N  N17 . 6YH H 7 .   ? 8.828   9.942   -4.643  1.00 19.87  ? 306 6YH A N17 1 
HETATM 4481 C  C16 . 6YH H 7 .   ? 8.405   8.652   -4.440  1.00 20.51  ? 306 6YH A C16 1 
HETATM 4482 ZN ZN  . ZN  I 2 .   ? 16.919  -20.512 -31.204 1.00 7.06   ? 301 ZN  B ZN  1 
HETATM 4483 S  S   . DMS J 3 .   ? 8.907   -30.470 -30.799 1.00 21.64  ? 302 DMS B S   1 
HETATM 4484 O  O   . DMS J 3 .   ? 7.848   -29.604 -30.152 1.00 68.64  ? 302 DMS B O   1 
HETATM 4485 C  C1  . DMS J 3 .   ? 8.308   -31.997 -30.472 1.00 22.40  ? 302 DMS B C1  1 
HETATM 4486 C  C2  . DMS J 3 .   ? 8.640   -30.289 -32.441 1.00 18.27  ? 302 DMS B C2  1 
HETATM 4487 N  N1  . BCN K 4 .   ? 30.831  -33.515 -39.324 1.00 26.99  ? 303 BCN B N1  1 
HETATM 4488 C  C1  . BCN K 4 .   ? 30.277  -34.356 -38.244 1.00 16.26  ? 303 BCN B C1  1 
HETATM 4489 C  C2  . BCN K 4 .   ? 31.274  -35.165 -37.412 1.00 58.69  ? 303 BCN B C2  1 
HETATM 4490 O  O21 . BCN K 4 .   ? 31.981  -36.026 -38.008 1.00 115.64 ? 303 BCN B O21 1 
HETATM 4491 O  O22 . BCN K 4 .   ? 31.367  -35.006 -36.137 1.00 42.89  ? 303 BCN B O22 1 
HETATM 4492 C  C3  . BCN K 4 .   ? 29.978  -32.854 -40.314 1.00 26.07  ? 303 BCN B C3  1 
HETATM 4493 C  C4  . BCN K 4 .   ? 30.433  -33.879 -41.379 1.00 32.37  ? 303 BCN B C4  1 
HETATM 4494 O  O4  . BCN K 4 .   ? 29.526  -33.828 -42.415 1.00 27.01  ? 303 BCN B O4  1 
HETATM 4495 C  C5  . BCN K 4 .   ? 31.962  -32.731 -38.876 1.00 19.01  ? 303 BCN B C5  1 
HETATM 4496 C  C6  . BCN K 4 .   ? 32.090  -31.351 -39.523 1.00 31.11  ? 303 BCN B C6  1 
HETATM 4497 O  O6  . BCN K 4 .   ? 32.873  -31.225 -40.729 1.00 37.84  ? 303 BCN B O6  1 
HETATM 4498 C  C1  . MLA L 6 .   ? 16.731  -11.672 -27.019 1.00 39.83  ? 304 MLA B C1  1 
HETATM 4499 O  O1A . MLA L 6 .   ? 16.529  -12.493 -26.127 1.00 33.31  ? 304 MLA B O1A 1 
HETATM 4500 O  O1B . MLA L 6 .   ? 16.644  -12.091 -28.186 1.00 39.48  ? 304 MLA B O1B 1 
HETATM 4501 C  C2  . MLA L 6 .   ? 17.125  -10.233 -26.733 1.00 33.12  ? 304 MLA B C2  1 
HETATM 4502 C  C3  . MLA L 6 .   ? 15.825  -9.561  -26.420 1.00 34.21  ? 304 MLA B C3  1 
HETATM 4503 O  O3A . MLA L 6 .   ? 14.780  -10.243 -26.759 1.00 41.65  ? 304 MLA B O3A 1 
HETATM 4504 O  O3B . MLA L 6 .   ? 15.816  -8.418  -25.860 1.00 54.09  ? 304 MLA B O3B 1 
HETATM 4505 O  O12 . 6YH M 7 .   ? 14.612  -12.471 -29.130 1.00 17.44  ? 305 6YH B O12 1 
HETATM 4506 C  C11 . 6YH M 7 .   ? 13.874  -13.448 -29.429 1.00 14.96  ? 305 6YH B C11 1 
HETATM 4507 C  C4  . 6YH M 7 .   ? 14.420  -14.572 -30.229 1.00 11.89  ? 305 6YH B C4  1 
HETATM 4508 C  C3  . 6YH M 7 .   ? 13.607  -15.615 -30.615 1.00 12.59  ? 305 6YH B C3  1 
HETATM 4509 C  C2  . 6YH M 7 .   ? 14.128  -16.648 -31.401 1.00 10.98  ? 305 6YH B C2  1 
HETATM 4510 C  C5  . 6YH M 7 .   ? 15.762  -14.520 -30.608 1.00 10.70  ? 305 6YH B C5  1 
HETATM 4511 C  C6  . 6YH M 7 .   ? 16.301  -15.589 -31.390 1.00 9.85   ? 305 6YH B C6  1 
HETATM 4512 C  C1  . 6YH M 7 .   ? 15.542  -16.671 -31.742 1.00 9.36   ? 305 6YH B C1  1 
HETATM 4513 S  S7  . 6YH M 7 .   ? 16.136  -17.989 -32.698 1.00 7.52   ? 305 6YH B S7  1 
HETATM 4514 O  O9  . 6YH M 7 .   ? 15.547  -17.800 -34.013 1.00 7.86   ? 305 6YH B O9  1 
HETATM 4515 N  N10 . 6YH M 7 .   ? 15.616  -19.344 -32.039 1.00 7.16   ? 305 6YH B N10 1 
HETATM 4516 O  O8  . 6YH M 7 .   ? 17.565  -17.918 -32.599 1.00 8.00   ? 305 6YH B O8  1 
HETATM 4517 C  C13 . 6YH M 7 .   ? 12.416  -13.428 -29.232 1.00 18.43  ? 305 6YH B C13 1 
HETATM 4518 N  N14 . 6YH M 7 .   ? 12.078  -12.204 -28.485 1.00 17.03  ? 305 6YH B N14 1 
HETATM 4519 C  C18 . 6YH M 7 .   ? 11.797  -11.072 -29.172 1.00 16.97  ? 305 6YH B C18 1 
HETATM 4520 C  C20 . 6YH M 7 .   ? 11.714  -10.766 -30.495 1.00 15.92  ? 305 6YH B C20 1 
HETATM 4521 C  C21 . 6YH M 7 .   ? 11.370  -9.515  -30.910 1.00 17.92  ? 305 6YH B C21 1 
HETATM 4522 C  C22 . 6YH M 7 .   ? 11.131  -8.472  -29.975 1.00 18.62  ? 305 6YH B C22 1 
HETATM 4523 C  C23 . 6YH M 7 .   ? 11.191  -8.735  -28.622 1.00 20.61  ? 305 6YH B C23 1 
HETATM 4524 C  C19 . 6YH M 7 .   ? 11.568  -10.060 -28.248 1.00 19.79  ? 305 6YH B C19 1 
HETATM 4525 N  N17 . 6YH M 7 .   ? 11.657  -10.595 -27.002 1.00 20.84  ? 305 6YH B N17 1 
HETATM 4526 C  C16 . 6YH M 7 .   ? 12.053  -11.917 -27.177 1.00 22.19  ? 305 6YH B C16 1 
HETATM 4527 O  O   . HOH N 8 .   ? -14.822 11.395  -2.897  1.00 27.69  ? 401 HOH A O   1 
HETATM 4528 O  O   . HOH N 8 .   ? 24.173  -1.311  -5.243  1.00 40.13  ? 402 HOH A O   1 
HETATM 4529 O  O   . HOH N 8 .   ? 16.689  -4.062  -12.805 1.00 44.69  ? 403 HOH A O   1 
HETATM 4530 O  O   . HOH N 8 .   ? 19.648  3.904   -3.775  1.00 34.07  ? 404 HOH A O   1 
HETATM 4531 O  O   . HOH N 8 .   ? -7.576  20.930  -9.780  1.00 17.94  ? 405 HOH A O   1 
HETATM 4532 O  O   . HOH N 8 .   ? 17.136  2.945   16.041  1.00 40.98  ? 406 HOH A O   1 
HETATM 4533 O  O   . HOH N 8 .   ? -14.175 -7.682  11.446  1.00 43.68  ? 407 HOH A O   1 
HETATM 4534 O  O   . HOH N 8 .   ? -18.054 8.244   -0.273  1.00 43.41  ? 408 HOH A O   1 
HETATM 4535 O  O   . HOH N 8 .   ? 6.754   19.852  5.686   1.00 20.64  ? 409 HOH A O   1 
HETATM 4536 O  O   . HOH N 8 .   ? -0.227  -4.090  22.574  1.00 30.50  ? 410 HOH A O   1 
HETATM 4537 O  O   . HOH N 8 .   ? 13.410  4.651   -7.567  1.00 35.79  ? 411 HOH A O   1 
HETATM 4538 O  O   . HOH N 8 .   ? 4.091   -9.872  20.636  1.00 35.34  ? 412 HOH A O   1 
HETATM 4539 O  O   . HOH N 8 .   ? -5.105  -8.523  21.685  1.00 33.10  ? 413 HOH A O   1 
HETATM 4540 O  O   . HOH N 8 .   ? 20.871  -7.689  -6.298  1.00 54.77  ? 414 HOH A O   1 
HETATM 4541 O  O   . HOH N 8 .   ? -0.860  -13.431 18.489  1.00 27.84  ? 415 HOH A O   1 
HETATM 4542 O  O   . HOH N 8 .   ? 7.079   7.536   -18.156 1.00 31.44  ? 416 HOH A O   1 
HETATM 4543 O  O   . HOH N 8 .   ? -13.869 -1.591  13.718  1.00 30.44  ? 417 HOH A O   1 
HETATM 4544 O  O   . HOH N 8 .   ? -15.328 -8.805  1.946   1.00 25.41  ? 418 HOH A O   1 
HETATM 4545 O  O   . HOH N 8 .   ? 7.220   -17.721 -9.530  1.00 31.70  ? 419 HOH A O   1 
HETATM 4546 O  O   . HOH N 8 .   ? -10.675 9.696   -13.970 1.00 22.75  ? 420 HOH A O   1 
HETATM 4547 O  O   . HOH N 8 .   ? -17.704 -10.171 0.648   1.00 38.47  ? 421 HOH A O   1 
HETATM 4548 O  O   . HOH N 8 .   ? 8.930   -2.372  -0.057  1.00 9.21   ? 422 HOH A O   1 
HETATM 4549 O  O   . HOH N 8 .   ? -1.915  12.535  -9.994  1.00 31.34  ? 423 HOH A O   1 
HETATM 4550 O  O   . HOH N 8 .   ? 4.100   -2.852  -22.160 1.00 63.23  ? 424 HOH A O   1 
HETATM 4551 O  O   . HOH N 8 .   ? 21.468  -5.262  6.572   1.00 29.49  ? 425 HOH A O   1 
HETATM 4552 O  O   . HOH N 8 .   ? 12.241  9.837   12.257  1.00 35.89  ? 426 HOH A O   1 
HETATM 4553 O  O   . HOH N 8 .   ? 13.779  -11.910 -3.166  1.00 42.18  ? 427 HOH A O   1 
HETATM 4554 O  O   . HOH N 8 .   ? -2.802  1.000   -21.752 1.00 34.84  ? 428 HOH A O   1 
HETATM 4555 O  O   . HOH N 8 .   ? 18.382  -4.012  -26.363 1.00 34.32  ? 429 HOH A O   1 
HETATM 4556 O  O   . HOH N 8 .   ? 19.901  -3.087  -23.821 1.00 39.10  ? 430 HOH A O   1 
HETATM 4557 O  O   . HOH N 8 .   ? -2.224  14.229  13.481  1.00 25.84  ? 431 HOH A O   1 
HETATM 4558 O  O   . HOH N 8 .   ? -13.851 1.824   -14.591 1.00 33.33  ? 432 HOH A O   1 
HETATM 4559 O  O   . HOH N 8 .   ? 10.907  -7.742  -21.319 1.00 35.39  ? 433 HOH A O   1 
HETATM 4560 O  O   . HOH N 8 .   ? 7.747   -1.432  -4.375  1.00 24.25  ? 434 HOH A O   1 
HETATM 4561 O  O   . HOH N 8 .   ? -6.635  -12.228 10.622  1.00 16.67  ? 435 HOH A O   1 
HETATM 4562 O  O   . HOH N 8 .   ? 1.297   8.492   -19.505 1.00 33.80  ? 436 HOH A O   1 
HETATM 4563 O  O   . HOH N 8 .   ? -17.021 -3.767  11.711  1.00 39.01  ? 437 HOH A O   1 
HETATM 4564 O  O   . HOH N 8 .   ? -8.709  3.748   24.980  1.00 40.22  ? 438 HOH A O   1 
HETATM 4565 O  O   . HOH N 8 .   ? -5.585  5.361   19.607  1.00 32.78  ? 439 HOH A O   1 
HETATM 4566 O  O   . HOH N 8 .   ? -6.069  7.232   -23.938 1.00 34.48  ? 440 HOH A O   1 
HETATM 4567 O  O   . HOH N 8 .   ? 21.850  1.435   0.263   1.00 25.01  ? 441 HOH A O   1 
HETATM 4568 O  O   . HOH N 8 .   ? 1.538   -2.092  -7.919  1.00 10.15  ? 442 HOH A O   1 
HETATM 4569 O  O   . HOH N 8 .   ? 13.863  6.800   14.093  1.00 19.61  ? 443 HOH A O   1 
HETATM 4570 O  O   . HOH N 8 .   ? 10.693  8.664   14.306  1.00 34.40  ? 444 HOH A O   1 
HETATM 4571 O  O   . HOH N 8 .   ? -10.856 -5.047  -17.715 1.00 38.25  ? 445 HOH A O   1 
HETATM 4572 O  O   . HOH N 8 .   ? -9.810  -14.824 -12.881 1.00 27.59  ? 446 HOH A O   1 
HETATM 4573 O  O   . HOH N 8 .   ? -7.012  -5.551  23.741  1.00 76.00  ? 447 HOH A O   1 
HETATM 4574 O  O   . HOH N 8 .   ? -13.926 10.320  4.427   1.00 18.22  ? 448 HOH A O   1 
HETATM 4575 O  O   . HOH N 8 .   ? 9.025   10.961  12.286  1.00 28.60  ? 449 HOH A O   1 
HETATM 4576 O  O   . HOH N 8 .   ? 14.676  -0.756  13.227  1.00 23.67  ? 450 HOH A O   1 
HETATM 4577 O  O   . HOH N 8 .   ? -0.419  10.472  9.838   1.00 9.16   ? 451 HOH A O   1 
HETATM 4578 O  O   . HOH N 8 .   ? -0.753  -17.842 -8.550  1.00 23.90  ? 452 HOH A O   1 
HETATM 4579 O  O   . HOH N 8 .   ? -15.710 -4.530  -2.707  1.00 27.78  ? 453 HOH A O   1 
HETATM 4580 O  O   . HOH N 8 .   ? 14.837  0.787   -21.216 1.00 32.52  ? 454 HOH A O   1 
HETATM 4581 O  O   . HOH N 8 .   ? 5.453   -10.250 16.380  1.00 18.82  ? 455 HOH A O   1 
HETATM 4582 O  O   . HOH N 8 .   ? -8.432  -10.425 -19.436 1.00 25.45  ? 456 HOH A O   1 
HETATM 4583 O  O   . HOH N 8 .   ? 0.353   3.410   23.252  1.00 36.00  ? 457 HOH A O   1 
HETATM 4584 O  O   . HOH N 8 .   ? 14.524  -1.647  10.709  1.00 18.81  ? 458 HOH A O   1 
HETATM 4585 O  O   . HOH N 8 .   ? -7.216  -14.406 6.265   1.00 17.24  ? 459 HOH A O   1 
HETATM 4586 O  O   . HOH N 8 .   ? 11.291  16.566  8.488   1.00 27.24  ? 460 HOH A O   1 
HETATM 4587 O  O   . HOH N 8 .   ? 3.209   7.693   -9.548  1.00 20.27  ? 461 HOH A O   1 
HETATM 4588 O  O   . HOH N 8 .   ? 10.105  2.843   18.724  1.00 26.83  ? 462 HOH A O   1 
HETATM 4589 O  O   . HOH N 8 .   ? -2.128  17.941  -7.583  1.00 35.89  ? 463 HOH A O   1 
HETATM 4590 O  O   . HOH N 8 .   ? 10.708  21.347  1.817   1.00 34.31  ? 464 HOH A O   1 
HETATM 4591 O  O   . HOH N 8 .   ? -10.167 12.455  11.081  1.00 17.52  ? 465 HOH A O   1 
HETATM 4592 O  O   . HOH N 8 .   ? 1.113   7.705   13.314  1.00 17.49  ? 466 HOH A O   1 
HETATM 4593 O  O   . HOH N 8 .   ? 3.455   -13.181 15.859  1.00 26.36  ? 467 HOH A O   1 
HETATM 4594 O  O   . HOH N 8 .   ? 2.209   -13.682 -4.433  1.00 10.07  ? 468 HOH A O   1 
HETATM 4595 O  O   . HOH N 8 .   ? 16.419  -9.368  -0.390  1.00 39.82  ? 469 HOH A O   1 
HETATM 4596 O  O   . HOH N 8 .   ? 8.221   -2.883  -23.003 1.00 29.71  ? 470 HOH A O   1 
HETATM 4597 O  O   . HOH N 8 .   ? -8.318  -19.408 -1.093  1.00 19.19  ? 471 HOH A O   1 
HETATM 4598 O  O   . HOH N 8 .   ? -16.133 -5.823  14.569  1.00 40.83  ? 472 HOH A O   1 
HETATM 4599 O  O   . HOH N 8 .   ? -2.615  14.939  16.101  1.00 32.36  ? 473 HOH A O   1 
HETATM 4600 O  O   . HOH N 8 .   ? -11.950 -16.497 -2.293  1.00 19.02  ? 474 HOH A O   1 
HETATM 4601 O  O   . HOH N 8 .   ? -5.265  10.805  -17.940 1.00 26.09  ? 475 HOH A O   1 
HETATM 4602 O  O   . HOH N 8 .   ? -4.164  -14.838 13.335  1.00 22.76  ? 476 HOH A O   1 
HETATM 4603 O  O   . HOH N 8 .   ? 7.780   -17.467 5.733   1.00 24.21  ? 477 HOH A O   1 
HETATM 4604 O  O   . HOH N 8 .   ? 10.376  0.659   -20.581 1.00 21.71  ? 478 HOH A O   1 
HETATM 4605 O  O   . HOH N 8 .   ? -2.786  -20.465 -7.308  1.00 24.41  ? 479 HOH A O   1 
HETATM 4606 O  O   . HOH N 8 .   ? -3.686  12.068  12.172  1.00 16.26  ? 480 HOH A O   1 
HETATM 4607 O  O   . HOH N 8 .   ? 12.100  -13.898 -6.511  1.00 22.26  ? 481 HOH A O   1 
HETATM 4608 O  O   . HOH N 8 .   ? 5.098   3.916   21.782  1.00 39.78  ? 482 HOH A O   1 
HETATM 4609 O  O   . HOH N 8 .   ? 9.445   11.551  -6.756  1.00 36.99  ? 483 HOH A O   1 
HETATM 4610 O  O   . HOH N 8 .   ? -9.779  17.592  3.232   1.00 24.80  ? 484 HOH A O   1 
HETATM 4611 O  O   . HOH N 8 .   ? -5.238  -20.081 -2.692  1.00 13.00  ? 485 HOH A O   1 
HETATM 4612 O  O   . HOH N 8 .   ? 12.767  -11.455 -10.680 1.00 22.07  ? 486 HOH A O   1 
HETATM 4613 O  O   . HOH N 8 .   ? -9.411  16.680  0.789   1.00 24.35  ? 487 HOH A O   1 
HETATM 4614 O  O   . HOH N 8 .   ? -11.801 -12.326 2.733   1.00 27.52  ? 488 HOH A O   1 
HETATM 4615 O  O   . HOH N 8 .   ? 12.923  3.106   -18.169 1.00 39.42  ? 489 HOH A O   1 
HETATM 4616 O  O   . HOH N 8 .   ? -10.394 9.923   14.461  1.00 29.54  ? 490 HOH A O   1 
HETATM 4617 O  O   . HOH N 8 .   ? 9.716   15.792  0.128   1.00 26.84  ? 491 HOH A O   1 
HETATM 4618 O  O   . HOH N 8 .   ? -12.756 -16.048 5.241   1.00 41.72  ? 492 HOH A O   1 
HETATM 4619 O  O   . HOH N 8 .   ? -0.191  -16.521 1.305   1.00 10.60  ? 493 HOH A O   1 
HETATM 4620 O  O   . HOH N 8 .   ? -7.738  -18.617 -7.837  1.00 12.74  ? 494 HOH A O   1 
HETATM 4621 O  O   . HOH N 8 .   ? -15.723 7.935   11.235  1.00 25.67  ? 495 HOH A O   1 
HETATM 4622 O  O   . HOH N 8 .   ? -6.828  -6.647  4.601   1.00 8.25   ? 496 HOH A O   1 
HETATM 4623 O  O   . HOH N 8 .   ? 5.633   -11.781 2.283   1.00 8.64   ? 497 HOH A O   1 
HETATM 4624 O  O   . HOH N 8 .   ? -2.075  -2.188  22.021  1.00 31.89  ? 498 HOH A O   1 
HETATM 4625 O  O   . HOH N 8 .   ? -2.740  -6.946  -19.133 1.00 30.27  ? 499 HOH A O   1 
HETATM 4626 O  O   . HOH N 8 .   ? 16.912  1.348   -17.023 1.00 51.36  ? 500 HOH A O   1 
HETATM 4627 O  O   . HOH N 8 .   ? -11.418 -5.434  7.870   1.00 11.52  ? 501 HOH A O   1 
HETATM 4628 O  O   . HOH N 8 .   ? 15.160  -1.656  -12.977 1.00 33.09  ? 502 HOH A O   1 
HETATM 4629 O  O   . HOH N 8 .   ? 12.853  -2.612  -8.075  1.00 21.49  ? 503 HOH A O   1 
HETATM 4630 O  O   . HOH N 8 .   ? 14.238  1.451   -10.516 1.00 42.47  ? 504 HOH A O   1 
HETATM 4631 O  O   . HOH N 8 .   ? 9.679   12.588  7.587   1.00 15.24  ? 505 HOH A O   1 
HETATM 4632 O  O   . HOH N 8 .   ? -17.191 -5.820  10.347  1.00 35.01  ? 506 HOH A O   1 
HETATM 4633 O  O   . HOH N 8 .   ? -12.744 -13.042 0.278   1.00 28.54  ? 507 HOH A O   1 
HETATM 4634 O  O   . HOH N 8 .   ? 6.672   -9.410  5.115   1.00 9.27   ? 508 HOH A O   1 
HETATM 4635 O  O   . HOH N 8 .   ? 6.694   -11.173 -18.646 1.00 25.42  ? 509 HOH A O   1 
HETATM 4636 O  O   . HOH N 8 .   ? -3.326  -7.072  -21.263 1.00 33.15  ? 510 HOH A O   1 
HETATM 4637 O  O   . HOH N 8 .   ? -4.810  21.828  1.959   1.00 14.81  ? 511 HOH A O   1 
HETATM 4638 O  O   . HOH N 8 .   ? 5.984   -6.769  15.401  1.00 18.33  ? 512 HOH A O   1 
HETATM 4639 O  O   . HOH N 8 .   ? 7.707   -6.992  13.353  1.00 10.96  ? 513 HOH A O   1 
HETATM 4640 O  O   . HOH N 8 .   ? -6.340  -13.579 17.174  1.00 41.52  ? 514 HOH A O   1 
HETATM 4641 O  O   . HOH N 8 .   ? 11.507  -10.034 9.317   1.00 24.78  ? 515 HOH A O   1 
HETATM 4642 O  O   . HOH N 8 .   ? 19.534  9.352   2.554   1.00 40.62  ? 516 HOH A O   1 
HETATM 4643 O  O   . HOH N 8 .   ? 3.618   -3.508  21.665  1.00 18.02  ? 517 HOH A O   1 
HETATM 4644 O  O   . HOH N 8 .   ? -11.856 5.767   -18.803 1.00 30.90  ? 518 HOH A O   1 
HETATM 4645 O  O   . HOH N 8 .   ? 5.301   2.080   -5.919  1.00 33.96  ? 519 HOH A O   1 
HETATM 4646 O  O   . HOH N 8 .   ? -15.484 0.738   19.267  1.00 29.92  ? 520 HOH A O   1 
HETATM 4647 O  O   . HOH N 8 .   ? 7.661   -16.294 15.254  1.00 23.08  ? 521 HOH A O   1 
HETATM 4648 O  O   . HOH N 8 .   ? 1.617   -13.648 20.908  1.00 31.38  ? 522 HOH A O   1 
HETATM 4649 O  O   . HOH N 8 .   ? 11.103  6.604   -3.711  1.00 34.83  ? 523 HOH A O   1 
HETATM 4650 O  O   . HOH N 8 .   ? -7.742  12.529  -4.481  1.00 14.98  ? 524 HOH A O   1 
HETATM 4651 O  O   . HOH N 8 .   ? -10.217 15.600  13.156  1.00 42.90  ? 525 HOH A O   1 
HETATM 4652 O  O   . HOH N 8 .   ? -8.963  5.310   -19.145 1.00 30.40  ? 526 HOH A O   1 
HETATM 4653 O  O   . HOH N 8 .   ? 6.813   -11.526 9.381   1.00 10.46  ? 527 HOH A O   1 
HETATM 4654 O  O   . HOH N 8 .   ? -6.019  17.607  8.013   1.00 15.81  ? 528 HOH A O   1 
HETATM 4655 O  O   . HOH N 8 .   ? -14.627 -5.875  -6.809  1.00 18.85  ? 529 HOH A O   1 
HETATM 4656 O  O   . HOH N 8 .   ? 3.406   22.716  3.778   1.00 10.90  ? 530 HOH A O   1 
HETATM 4657 O  O   . HOH N 8 .   ? -0.144  15.277  -6.953  1.00 26.41  ? 531 HOH A O   1 
HETATM 4658 O  O   . HOH N 8 .   ? 1.946   2.516   -22.373 1.00 32.15  ? 532 HOH A O   1 
HETATM 4659 O  O   . HOH N 8 .   ? -8.266  -1.932  -18.519 1.00 30.30  ? 533 HOH A O   1 
HETATM 4660 O  O   . HOH N 8 .   ? 8.815   6.108   -20.789 1.00 38.45  ? 534 HOH A O   1 
HETATM 4661 O  O   . HOH N 8 .   ? -12.544 -3.997  -13.126 1.00 22.99  ? 535 HOH A O   1 
HETATM 4662 O  O   . HOH N 8 .   ? -15.506 -1.684  16.360  1.00 39.12  ? 536 HOH A O   1 
HETATM 4663 O  O   . HOH N 8 .   ? -4.595  7.858   16.907  1.00 35.29  ? 537 HOH A O   1 
HETATM 4664 O  O   . HOH N 8 .   ? -0.405  10.397  -8.049  1.00 24.84  ? 538 HOH A O   1 
HETATM 4665 O  O   . HOH N 8 .   ? -9.645  -2.530  25.650  1.00 36.23  ? 539 HOH A O   1 
HETATM 4666 O  O   . HOH N 8 .   ? -13.198 -9.253  1.274   1.00 24.26  ? 540 HOH A O   1 
HETATM 4667 O  O   . HOH N 8 .   ? -3.816  16.018  11.493  1.00 22.21  ? 541 HOH A O   1 
HETATM 4668 O  O   . HOH N 8 .   ? 23.604  2.090   8.725   1.00 20.16  ? 542 HOH A O   1 
HETATM 4669 O  O   . HOH N 8 .   ? -5.869  -10.576 8.665   1.00 12.74  ? 543 HOH A O   1 
HETATM 4670 O  O   . HOH N 8 .   ? 18.800  -2.017  5.267   1.00 15.71  ? 544 HOH A O   1 
HETATM 4671 O  O   . HOH N 8 .   ? 14.547  -4.841  -7.964  1.00 27.81  ? 545 HOH A O   1 
HETATM 4672 O  O   . HOH N 8 .   ? 6.389   -14.147 8.594   1.00 12.02  ? 546 HOH A O   1 
HETATM 4673 O  O   . HOH N 8 .   ? -3.634  21.730  -0.571  1.00 14.93  ? 547 HOH A O   1 
HETATM 4674 O  O   . HOH N 8 .   ? -13.043 1.438   18.747  1.00 29.40  ? 548 HOH A O   1 
HETATM 4675 O  O   . HOH N 8 .   ? -0.498  -17.674 4.325   1.00 13.86  ? 549 HOH A O   1 
HETATM 4676 O  O   . HOH N 8 .   ? -13.049 -1.148  -9.188  1.00 21.00  ? 550 HOH A O   1 
HETATM 4677 O  O   . HOH N 8 .   ? -11.574 7.583   -11.088 1.00 19.96  ? 551 HOH A O   1 
HETATM 4678 O  O   . HOH N 8 .   ? 0.969   -8.284  -17.019 1.00 22.92  ? 552 HOH A O   1 
HETATM 4679 O  O   . HOH N 8 .   ? -3.262  -16.756 -1.216  1.00 12.26  ? 553 HOH A O   1 
HETATM 4680 O  O   . HOH N 8 .   ? -15.980 5.130   -0.332  1.00 29.67  ? 554 HOH A O   1 
HETATM 4681 O  O   . HOH N 8 .   ? 2.099   -20.438 -5.301  1.00 18.77  ? 555 HOH A O   1 
HETATM 4682 O  O   . HOH N 8 .   ? 2.994   -14.990 -14.410 1.00 22.60  ? 556 HOH A O   1 
HETATM 4683 O  O   . HOH N 8 .   ? -9.068  11.850  -6.887  1.00 13.92  ? 557 HOH A O   1 
HETATM 4684 O  O   . HOH N 8 .   ? 9.957   -18.768 -0.789  1.00 37.91  ? 558 HOH A O   1 
HETATM 4685 O  O   . HOH N 8 .   ? -4.522  -16.776 2.936   1.00 12.75  ? 559 HOH A O   1 
HETATM 4686 O  O   . HOH N 8 .   ? 0.030   16.548  -3.517  1.00 16.49  ? 560 HOH A O   1 
HETATM 4687 O  O   . HOH N 8 .   ? 2.864   -6.911  16.895  1.00 17.58  ? 561 HOH A O   1 
HETATM 4688 O  O   . HOH N 8 .   ? 2.892   9.866   13.895  1.00 30.93  ? 562 HOH A O   1 
HETATM 4689 O  O   . HOH N 8 .   ? 15.589  8.954   4.516   1.00 17.24  ? 563 HOH A O   1 
HETATM 4690 O  O   . HOH N 8 .   ? 5.516   -14.157 -15.037 1.00 27.67  ? 564 HOH A O   1 
HETATM 4691 O  O   . HOH N 8 .   ? 15.953  2.606   -7.345  1.00 28.47  ? 565 HOH A O   1 
HETATM 4692 O  O   . HOH N 8 .   ? 15.113  -3.057  5.169   1.00 14.36  ? 566 HOH A O   1 
HETATM 4693 O  O   . HOH N 8 .   ? -0.870  2.903   17.730  1.00 22.32  ? 567 HOH A O   1 
HETATM 4694 O  O   . HOH N 8 .   ? 5.835   -3.047  -4.592  1.00 19.57  ? 568 HOH A O   1 
HETATM 4695 O  O   . HOH N 8 .   ? -2.860  -15.090 10.967  1.00 13.08  ? 569 HOH A O   1 
HETATM 4696 O  O   . HOH N 8 .   ? -6.148  -8.134  17.229  1.00 19.06  ? 570 HOH A O   1 
HETATM 4697 O  O   . HOH N 8 .   ? 12.782  -9.640  -6.313  1.00 24.00  ? 571 HOH A O   1 
HETATM 4698 O  O   . HOH N 8 .   ? -7.285  8.005   22.695  1.00 38.28  ? 572 HOH A O   1 
HETATM 4699 O  O   . HOH N 8 .   ? 26.020  4.539   5.089   1.00 29.87  ? 573 HOH A O   1 
HETATM 4700 O  O   . HOH N 8 .   ? 21.441  3.166   10.223  1.00 20.96  ? 574 HOH A O   1 
HETATM 4701 O  O   . HOH N 8 .   ? 18.410  4.838   11.980  1.00 28.03  ? 575 HOH A O   1 
HETATM 4702 O  O   . HOH N 8 .   ? 8.791   3.583   -4.178  1.00 20.98  ? 576 HOH A O   1 
HETATM 4703 O  O   . HOH N 8 .   ? -1.788  4.503   15.161  1.00 17.56  ? 577 HOH A O   1 
HETATM 4704 O  O   . HOH N 8 .   ? 9.098   -4.384  20.661  1.00 27.67  ? 578 HOH A O   1 
HETATM 4705 O  O   . HOH N 8 .   ? -13.215 -11.394 -4.548  1.00 20.91  ? 579 HOH A O   1 
HETATM 4706 O  O   . HOH N 8 .   ? -16.565 -0.629  -1.341  1.00 18.86  ? 580 HOH A O   1 
HETATM 4707 O  O   . HOH N 8 .   ? -0.410  22.577  9.271   1.00 16.45  ? 581 HOH A O   1 
HETATM 4708 O  O   . HOH N 8 .   ? 10.199  -12.532 15.453  1.00 28.69  ? 582 HOH A O   1 
HETATM 4709 O  O   . HOH N 8 .   ? 3.910   -18.008 8.097   1.00 18.65  ? 583 HOH A O   1 
HETATM 4710 O  O   . HOH N 8 .   ? 16.901  -4.044  -9.133  1.00 32.45  ? 584 HOH A O   1 
HETATM 4711 O  O   . HOH N 8 .   ? -16.648 -2.192  9.261   1.00 20.82  ? 585 HOH A O   1 
HETATM 4712 O  O   . HOH N 8 .   ? -13.853 1.035   10.748  1.00 17.33  ? 586 HOH A O   1 
HETATM 4713 O  O   . HOH N 8 .   ? 9.329   -15.668 2.200   1.00 29.09  ? 587 HOH A O   1 
HETATM 4714 O  O   . HOH N 8 .   ? 11.437  10.614  8.553   1.00 17.95  ? 588 HOH A O   1 
HETATM 4715 O  O   . HOH N 8 .   ? -14.327 6.632   -7.560  1.00 38.34  ? 589 HOH A O   1 
HETATM 4716 O  O   . HOH N 8 .   ? 9.955   -12.561 6.385   1.00 19.78  ? 590 HOH A O   1 
HETATM 4717 O  O   . HOH N 8 .   ? 1.681   -18.100 10.972  1.00 17.60  ? 591 HOH A O   1 
HETATM 4718 O  O   . HOH N 8 .   ? -15.874 14.053  -2.472  1.00 36.49  ? 592 HOH A O   1 
HETATM 4719 O  O   . HOH N 8 .   ? 4.991   -11.876 18.564  1.00 36.55  ? 593 HOH A O   1 
HETATM 4720 O  O   . HOH N 8 .   ? -13.531 1.045   -11.895 1.00 28.37  ? 594 HOH A O   1 
HETATM 4721 O  O   . HOH N 8 .   ? 11.867  -4.472  18.627  1.00 24.50  ? 595 HOH A O   1 
HETATM 4722 O  O   . HOH N 8 .   ? -10.999 -17.828 -9.236  1.00 22.84  ? 596 HOH A O   1 
HETATM 4723 O  O   . HOH N 8 .   ? 3.354   -6.744  -22.880 1.00 63.11  ? 597 HOH A O   1 
HETATM 4724 O  O   . HOH N 8 .   ? -9.017  22.130  -10.646 1.00 29.89  ? 598 HOH A O   1 
HETATM 4725 O  O   . HOH N 8 .   ? -2.401  -16.568 16.606  1.00 29.41  ? 599 HOH A O   1 
HETATM 4726 O  O   . HOH N 8 .   ? -13.811 -16.026 -9.453  1.00 41.14  ? 600 HOH A O   1 
HETATM 4727 O  O   . HOH N 8 .   ? -3.510  16.796  -9.971  1.00 40.43  ? 601 HOH A O   1 
HETATM 4728 O  O   . HOH N 8 .   ? -2.658  9.626   13.166  1.00 22.63  ? 602 HOH A O   1 
HETATM 4729 O  O   . HOH N 8 .   ? 7.681   6.195   -7.694  1.00 31.09  ? 603 HOH A O   1 
HETATM 4730 O  O   . HOH N 8 .   ? 11.746  -15.933 -2.150  1.00 41.76  ? 604 HOH A O   1 
HETATM 4731 O  O   . HOH N 8 .   ? 11.491  0.166   13.649  1.00 13.26  ? 605 HOH A O   1 
HETATM 4732 O  O   . HOH N 8 .   ? 4.247   19.530  11.819  1.00 28.36  ? 606 HOH A O   1 
HETATM 4733 O  O   . HOH N 8 .   ? 23.242  -4.012  8.467   1.00 23.89  ? 607 HOH A O   1 
HETATM 4734 O  O   . HOH N 8 .   ? -3.116  -14.643 -16.104 1.00 38.52  ? 608 HOH A O   1 
HETATM 4735 O  O   . HOH N 8 .   ? 9.545   -6.806  16.753  1.00 24.95  ? 609 HOH A O   1 
HETATM 4736 O  O   . HOH N 8 .   ? -12.634 17.054  3.265   1.00 39.50  ? 610 HOH A O   1 
HETATM 4737 O  O   . HOH N 8 .   ? 8.126   -10.557 7.066   1.00 10.12  ? 611 HOH A O   1 
HETATM 4738 O  O   . HOH N 8 .   ? 1.130   -4.034  20.213  1.00 18.39  ? 612 HOH A O   1 
HETATM 4739 O  O   . HOH N 8 .   ? -2.330  21.536  13.797  1.00 53.76  ? 613 HOH A O   1 
HETATM 4740 O  O   . HOH N 8 .   ? -1.023  19.324  -3.409  1.00 21.18  ? 614 HOH A O   1 
HETATM 4741 O  O   . HOH N 8 .   ? 12.866  -12.600 -21.891 1.00 37.33  ? 615 HOH A O   1 
HETATM 4742 O  O   . HOH N 8 .   ? -6.748  -9.617  20.813  1.00 29.67  ? 616 HOH A O   1 
HETATM 4743 O  O   . HOH N 8 .   ? 4.128   17.107  -3.880  1.00 28.98  ? 617 HOH A O   1 
HETATM 4744 O  O   . HOH N 8 .   ? 11.575  4.854   -9.866  1.00 34.21  ? 618 HOH A O   1 
HETATM 4745 O  O   . HOH N 8 .   ? 1.996   -17.598 5.927   1.00 11.90  ? 619 HOH A O   1 
HETATM 4746 O  O   . HOH N 8 .   ? 3.205   3.262   19.406  1.00 23.86  ? 620 HOH A O   1 
HETATM 4747 O  O   . HOH N 8 .   ? -14.646 -8.347  -0.728  1.00 39.47  ? 621 HOH A O   1 
HETATM 4748 O  O   . HOH N 8 .   ? -12.777 -9.870  -1.879  1.00 21.30  ? 622 HOH A O   1 
HETATM 4749 O  O   . HOH N 8 .   ? 2.837   -6.831  -18.249 1.00 30.92  ? 623 HOH A O   1 
HETATM 4750 O  O   . HOH N 8 .   ? -11.540 21.332  -3.669  1.00 26.09  ? 624 HOH A O   1 
HETATM 4751 O  O   . HOH N 8 .   ? 17.805  7.896   5.915   1.00 16.18  ? 625 HOH A O   1 
HETATM 4752 O  O   . HOH N 8 .   ? 15.381  -5.392  6.563   1.00 31.56  ? 626 HOH A O   1 
HETATM 4753 O  O   . HOH N 8 .   ? 3.401   16.579  13.444  1.00 30.96  ? 627 HOH A O   1 
HETATM 4754 O  O   . HOH N 8 .   ? -14.688 -9.396  8.199   1.00 33.83  ? 628 HOH A O   1 
HETATM 4755 O  O   . HOH N 8 .   ? -5.003  -18.256 7.375   1.00 26.51  ? 629 HOH A O   1 
HETATM 4756 O  O   . HOH N 8 .   ? 15.119  -11.173 -21.651 1.00 27.40  ? 630 HOH A O   1 
HETATM 4757 O  O   . HOH N 8 .   ? 1.895   9.137   -7.573  1.00 33.04  ? 631 HOH A O   1 
HETATM 4758 O  O   . HOH N 8 .   ? -11.659 21.277  1.408   1.00 34.91  ? 632 HOH A O   1 
HETATM 4759 O  O   . HOH N 8 .   ? -2.105  5.745   -22.577 1.00 102.17 ? 633 HOH A O   1 
HETATM 4760 O  O   . HOH N 8 .   ? 24.256  7.556   3.703   1.00 48.96  ? 634 HOH A O   1 
HETATM 4761 O  O   . HOH N 8 .   ? 0.656   -6.184  18.423  1.00 19.72  ? 635 HOH A O   1 
HETATM 4762 O  O   . HOH N 8 .   ? 22.910  -2.254  12.757  1.00 46.93  ? 636 HOH A O   1 
HETATM 4763 O  O   . HOH N 8 .   ? 3.809   -17.640 -10.325 1.00 32.68  ? 637 HOH A O   1 
HETATM 4764 O  O   . HOH N 8 .   ? -14.939 10.487  10.352  1.00 31.29  ? 638 HOH A O   1 
HETATM 4765 O  O   . HOH N 8 .   ? -15.500 2.559   16.865  1.00 47.79  ? 639 HOH A O   1 
HETATM 4766 O  O   . HOH N 8 .   ? -6.450  19.809  -11.814 1.00 47.68  ? 640 HOH A O   1 
HETATM 4767 O  O   . HOH N 8 .   ? -9.408  19.600  1.928   1.00 34.73  ? 641 HOH A O   1 
HETATM 4768 O  O   . HOH N 8 .   ? 21.674  -17.765 -8.028  1.00 37.08  ? 642 HOH A O   1 
HETATM 4769 O  O   . HOH N 8 .   ? 4.865   3.742   -4.013  1.00 85.02  ? 643 HOH A O   1 
HETATM 4770 O  O   . HOH N 8 .   ? 18.419  -6.814  -15.985 1.00 32.36  ? 644 HOH A O   1 
HETATM 4771 O  O   . HOH N 8 .   ? 4.792   5.237   -21.578 1.00 64.22  ? 645 HOH A O   1 
HETATM 4772 O  O   . HOH N 8 .   ? 6.164   1.800   -2.401  1.00 26.04  ? 646 HOH A O   1 
HETATM 4773 O  O   . HOH N 8 .   ? 20.335  -0.777  -1.882  1.00 25.88  ? 647 HOH A O   1 
HETATM 4774 O  O   . HOH N 8 .   ? 8.662   13.102  10.086  1.00 25.90  ? 648 HOH A O   1 
HETATM 4775 O  O   . HOH N 8 .   ? -6.853  -2.765  -21.392 1.00 48.45  ? 649 HOH A O   1 
HETATM 4776 O  O   . HOH N 8 .   ? 7.493   1.613   -5.468  1.00 24.50  ? 650 HOH A O   1 
HETATM 4777 O  O   . HOH N 8 .   ? -12.499 -7.822  9.498   1.00 22.08  ? 651 HOH A O   1 
HETATM 4778 O  O   . HOH N 8 .   ? -13.612 1.550   15.981  1.00 37.21  ? 652 HOH A O   1 
HETATM 4779 O  O   . HOH N 8 .   ? 7.434   -13.141 17.076  1.00 26.88  ? 653 HOH A O   1 
HETATM 4780 O  O   . HOH N 8 .   ? 21.578  -1.935  -8.105  1.00 40.78  ? 654 HOH A O   1 
HETATM 4781 O  O   . HOH N 8 .   ? -13.368 10.040  -12.284 1.00 25.77  ? 655 HOH A O   1 
HETATM 4782 O  O   . HOH N 8 .   ? -2.714  -15.437 1.103   1.00 10.75  ? 656 HOH A O   1 
HETATM 4783 O  O   . HOH N 8 .   ? 6.085   5.672   -5.588  1.00 41.87  ? 657 HOH A O   1 
HETATM 4784 O  O   . HOH N 8 .   ? -8.203  -7.246  18.893  1.00 32.67  ? 658 HOH A O   1 
HETATM 4785 O  O   . HOH N 8 .   ? 10.839  2.406   -22.583 1.00 30.94  ? 659 HOH A O   1 
HETATM 4786 O  O   . HOH N 8 .   ? 8.908   19.781  -0.557  1.00 32.51  ? 660 HOH A O   1 
HETATM 4787 O  O   . HOH N 8 .   ? -2.814  20.586  -3.650  1.00 32.95  ? 661 HOH A O   1 
HETATM 4788 O  O   . HOH N 8 .   ? -15.153 12.847  3.839   1.00 27.94  ? 662 HOH A O   1 
HETATM 4789 O  O   . HOH N 8 .   ? -6.751  21.446  5.935   1.00 77.39  ? 663 HOH A O   1 
HETATM 4790 O  O   . HOH N 8 .   ? 4.537   -10.651 -20.998 1.00 34.06  ? 664 HOH A O   1 
HETATM 4791 O  O   . HOH N 8 .   ? 18.747  -2.884  7.890   1.00 26.99  ? 665 HOH A O   1 
HETATM 4792 O  O   . HOH N 8 .   ? 10.200  -13.610 11.256  1.00 45.80  ? 666 HOH A O   1 
HETATM 4793 O  O   . HOH N 8 .   ? 15.221  -9.051  2.518   1.00 56.43  ? 667 HOH A O   1 
HETATM 4794 O  O   . HOH N 8 .   ? 10.959  -10.680 -22.849 1.00 36.96  ? 668 HOH A O   1 
HETATM 4795 O  O   . HOH N 8 .   ? 9.679   15.634  11.607  1.00 33.21  ? 669 HOH A O   1 
HETATM 4796 O  O   . HOH N 8 .   ? -5.227  -14.443 9.736   1.00 37.62  ? 670 HOH A O   1 
HETATM 4797 O  O   . HOH N 8 .   ? -6.687  -12.251 21.916  1.00 36.46  ? 671 HOH A O   1 
HETATM 4798 O  O   . HOH N 8 .   ? -12.264 -10.479 9.128   1.00 28.06  ? 672 HOH A O   1 
HETATM 4799 O  O   . HOH N 8 .   ? -7.458  7.497   19.229  1.00 40.71  ? 673 HOH A O   1 
HETATM 4800 O  O   . HOH N 8 .   ? 19.875  1.860   -1.314  1.00 31.81  ? 674 HOH A O   1 
HETATM 4801 O  O   . HOH N 8 .   ? -6.465  -12.647 13.186  1.00 36.02  ? 675 HOH A O   1 
HETATM 4802 O  O   . HOH N 8 .   ? 20.131  -3.732  -21.636 1.00 42.82  ? 676 HOH A O   1 
HETATM 4803 O  O   . HOH N 8 .   ? 12.548  -7.832  13.838  1.00 41.88  ? 677 HOH A O   1 
HETATM 4804 O  O   . HOH N 8 .   ? 16.220  -7.819  5.424   1.00 41.00  ? 678 HOH A O   1 
HETATM 4805 O  O   . HOH N 8 .   ? 13.023  -11.558 -7.735  1.00 29.00  ? 679 HOH A O   1 
HETATM 4806 O  O   . HOH N 8 .   ? 12.289  9.593   -3.467  1.00 33.68  ? 680 HOH A O   1 
HETATM 4807 O  O   . HOH N 8 .   ? -7.590  21.747  1.694   1.00 21.45  ? 681 HOH A O   1 
HETATM 4808 O  O   . HOH N 8 .   ? 22.078  -4.713  -7.972  1.00 31.46  ? 682 HOH A O   1 
HETATM 4809 O  O   . HOH N 8 .   ? -7.115  -6.825  -22.052 1.00 33.95  ? 683 HOH A O   1 
HETATM 4810 O  O   . HOH N 8 .   ? 8.765   -11.332 11.360  1.00 24.47  ? 684 HOH A O   1 
HETATM 4811 O  O   . HOH N 8 .   ? 10.701  -14.291 8.131   1.00 34.23  ? 685 HOH A O   1 
HETATM 4812 O  O   . HOH N 8 .   ? 16.454  -3.769  11.537  1.00 38.82  ? 686 HOH A O   1 
HETATM 4813 O  O   . HOH N 8 .   ? -7.699  -10.389 15.822  1.00 35.31  ? 687 HOH A O   1 
HETATM 4814 O  O   . HOH N 8 .   ? 4.930   -14.681 18.970  1.00 39.43  ? 688 HOH A O   1 
HETATM 4815 O  O   . HOH N 8 .   ? -6.847  -16.137 4.339   1.00 20.35  ? 689 HOH A O   1 
HETATM 4816 O  O   . HOH N 8 .   ? 5.306   22.306  5.752   1.00 17.05  ? 690 HOH A O   1 
HETATM 4817 O  O   . HOH N 8 .   ? -6.523  -15.939 8.381   1.00 24.41  ? 691 HOH A O   1 
HETATM 4818 O  O   . HOH N 8 .   ? 8.241   -15.752 9.815   1.00 25.33  ? 692 HOH A O   1 
HETATM 4819 O  O   . HOH N 8 .   ? -3.813  5.367   17.440  1.00 25.70  ? 693 HOH A O   1 
HETATM 4820 O  O   . HOH N 8 .   ? 8.145   -15.713 -10.661 1.00 41.62  ? 694 HOH A O   1 
HETATM 4821 O  O   . HOH N 8 .   ? 0.912   4.798   19.111  1.00 25.90  ? 695 HOH A O   1 
HETATM 4822 O  O   . HOH N 8 .   ? 10.099  5.291   -5.719  1.00 35.30  ? 696 HOH A O   1 
HETATM 4823 O  O   . HOH N 8 .   ? 11.919  14.198  6.932   1.00 26.42  ? 697 HOH A O   1 
HETATM 4824 O  O   . HOH N 8 .   ? 13.580  4.415   -15.886 1.00 31.75  ? 698 HOH A O   1 
HETATM 4825 O  O   . HOH N 8 .   ? -15.674 13.540  1.250   1.00 37.89  ? 699 HOH A O   1 
HETATM 4826 O  O   . HOH N 8 .   ? -14.080 15.346  4.623   1.00 37.04  ? 700 HOH A O   1 
HETATM 4827 O  O   . HOH N 8 .   ? -9.610  -0.179  27.251  1.00 45.15  ? 701 HOH A O   1 
HETATM 4828 O  O   . HOH N 8 .   ? 25.478  0.521   10.199  1.00 21.49  ? 702 HOH A O   1 
HETATM 4829 O  O   . HOH N 8 .   ? -1.002  -9.193  -18.657 1.00 37.19  ? 703 HOH A O   1 
HETATM 4830 O  O   . HOH N 8 .   ? 8.144   -10.139 15.794  1.00 29.60  ? 704 HOH A O   1 
HETATM 4831 O  O   . HOH N 8 .   ? -13.915 -5.230  -15.574 1.00 41.02  ? 705 HOH A O   1 
HETATM 4832 O  O   . HOH N 8 .   ? 24.838  4.623   7.981   1.00 25.80  ? 706 HOH A O   1 
HETATM 4833 O  O   . HOH N 8 .   ? 8.952   -11.463 17.343  1.00 24.65  ? 707 HOH A O   1 
HETATM 4834 O  O   . HOH N 8 .   ? 4.162   22.091  10.500  1.00 26.23  ? 708 HOH A O   1 
HETATM 4835 O  O   . HOH N 8 .   ? 11.713  4.977   -20.652 1.00 42.72  ? 709 HOH A O   1 
HETATM 4836 O  O   . HOH N 8 .   ? -1.486  2.926   -23.501 1.00 35.17  ? 710 HOH A O   1 
HETATM 4837 O  O   . HOH N 8 .   ? 11.574  11.410  11.188  1.00 31.32  ? 711 HOH A O   1 
HETATM 4838 O  O   . HOH N 8 .   ? 10.200  -5.445  -23.160 1.00 37.98  ? 712 HOH A O   1 
HETATM 4839 O  O   . HOH N 8 .   ? -7.890  4.740   -22.156 1.00 48.37  ? 713 HOH A O   1 
HETATM 4840 O  O   . HOH N 8 .   ? 7.814   18.015  -3.538  1.00 30.47  ? 714 HOH A O   1 
HETATM 4841 O  O   . HOH N 8 .   ? 4.841   -7.691  18.686  1.00 41.25  ? 715 HOH A O   1 
HETATM 4842 O  O   . HOH N 8 .   ? 6.528   -13.833 -18.188 1.00 33.79  ? 716 HOH A O   1 
HETATM 4843 O  O   . HOH N 8 .   ? 12.502  14.612  4.288   1.00 44.39  ? 717 HOH A O   1 
HETATM 4844 O  O   . HOH N 8 .   ? -1.826  15.266  -10.796 1.00 36.62  ? 718 HOH A O   1 
HETATM 4845 O  O   . HOH N 8 .   ? -11.046 22.372  -1.149  1.00 23.28  ? 719 HOH A O   1 
HETATM 4846 O  O   . HOH N 8 .   ? 2.972   -8.356  -20.551 1.00 34.83  ? 720 HOH A O   1 
HETATM 4847 O  O   . HOH N 8 .   ? 5.647   -6.306  -24.296 1.00 42.76  ? 721 HOH A O   1 
HETATM 4848 O  O   . HOH N 8 .   ? 9.012   -9.409  13.241  1.00 17.11  ? 722 HOH A O   1 
HETATM 4849 O  O   . HOH N 8 .   ? -2.758  23.366  10.403  1.00 20.66  ? 723 HOH A O   1 
HETATM 4850 O  O   . HOH N 8 .   ? -1.409  12.805  -14.980 1.00 30.41  ? 724 HOH A O   1 
HETATM 4851 O  O   . HOH N 8 .   ? 8.573   4.946   -22.902 1.00 32.80  ? 725 HOH A O   1 
HETATM 4852 O  O   . HOH N 8 .   ? 13.238  8.097   16.628  1.00 42.88  ? 726 HOH A O   1 
HETATM 4853 O  O   . HOH N 8 .   ? 22.397  5.938   11.675  1.00 35.15  ? 727 HOH A O   1 
HETATM 4854 O  O   . HOH N 8 .   ? -18.925 -2.041  -2.442  1.00 27.61  ? 728 HOH A O   1 
HETATM 4855 O  O   . HOH N 8 .   ? 9.194   15.604  -2.865  1.00 36.21  ? 729 HOH A O   1 
HETATM 4856 O  O   . HOH N 8 .   ? 4.518   -16.385 -12.301 1.00 40.32  ? 730 HOH A O   1 
HETATM 4857 O  O   . HOH N 8 .   ? 16.723  10.248  2.218   1.00 33.78  ? 731 HOH A O   1 
HETATM 4858 O  O   . HOH N 8 .   ? 9.306   8.336   16.328  1.00 38.14  ? 732 HOH A O   1 
HETATM 4859 O  O   . HOH N 8 .   ? 10.194  13.535  12.179  1.00 40.54  ? 733 HOH A O   1 
HETATM 4860 O  O   . HOH N 8 .   ? 7.890   -7.398  18.948  1.00 36.12  ? 734 HOH A O   1 
HETATM 4861 O  O   . HOH N 8 .   ? -17.406 1.880   -0.681  1.00 28.72  ? 735 HOH A O   1 
HETATM 4862 O  O   . HOH N 8 .   ? 6.943   -18.558 14.004  1.00 35.60  ? 736 HOH A O   1 
HETATM 4863 O  O   . HOH N 8 .   ? 24.877  -5.090  -8.007  1.00 33.61  ? 737 HOH A O   1 
HETATM 4864 O  O   . HOH N 8 .   ? 6.788   -18.223 11.325  1.00 36.68  ? 738 HOH A O   1 
HETATM 4865 O  O   . HOH N 8 .   ? 21.912  2.430   12.870  1.00 37.85  ? 739 HOH A O   1 
HETATM 4866 O  O   . HOH N 8 .   ? 15.611  10.961  6.065   1.00 31.06  ? 740 HOH A O   1 
HETATM 4867 O  O   . HOH N 8 .   ? 24.287  0.372   12.813  1.00 29.67  ? 741 HOH A O   1 
HETATM 4868 O  O   . HOH N 8 .   ? 7.673   -10.482 19.088  1.00 40.80  ? 742 HOH A O   1 
HETATM 4869 O  O   . HOH N 8 .   ? 14.007  11.620  8.116   1.00 32.81  ? 743 HOH A O   1 
HETATM 4870 O  O   . HOH N 8 .   ? 22.010  -5.083  -18.154 1.00 36.95  ? 744 HOH A O   1 
HETATM 4871 O  O   . HOH N 8 .   ? 24.439  6.685   9.356   1.00 32.38  ? 745 HOH A O   1 
HETATM 4872 O  O   . HOH O 8 .   ? -6.297  -27.608 -27.061 1.00 29.37  ? 601 HOH B O   1 
HETATM 4873 O  O   . HOH O 8 .   ? 13.689  -0.701  -37.331 1.00 21.93  ? 602 HOH B O   1 
HETATM 4874 O  O   . HOH O 8 .   ? 14.611  -20.427 -53.754 1.00 26.28  ? 603 HOH B O   1 
HETATM 4875 O  O   . HOH O 8 .   ? 18.764  -34.305 -48.837 1.00 27.59  ? 604 HOH B O   1 
HETATM 4876 O  O   . HOH O 8 .   ? 35.190  -9.154  -28.728 1.00 33.31  ? 605 HOH B O   1 
HETATM 4877 O  O   . HOH O 8 .   ? 28.080  0.355   -21.876 1.00 18.66  ? 606 HOH B O   1 
HETATM 4878 O  O   . HOH O 8 .   ? 16.509  -30.471 -52.507 1.00 32.69  ? 607 HOH B O   1 
HETATM 4879 O  O   . HOH O 8 .   ? 25.435  -29.159 -53.438 1.00 27.77  ? 608 HOH B O   1 
HETATM 4880 O  O   . HOH O 8 .   ? 34.459  -4.944  -35.392 1.00 51.74  ? 609 HOH B O   1 
HETATM 4881 O  O   . HOH O 8 .   ? 13.452  -13.129 -13.321 1.00 33.90  ? 610 HOH B O   1 
HETATM 4882 O  O   . HOH O 8 .   ? 34.355  -28.480 -43.341 1.00 41.42  ? 611 HOH B O   1 
HETATM 4883 O  O   . HOH O 8 .   ? 20.704  -24.607 -54.283 1.00 27.50  ? 612 HOH B O   1 
HETATM 4884 O  O   . HOH O 8 .   ? 1.457   -30.110 -25.140 1.00 33.88  ? 613 HOH B O   1 
HETATM 4885 O  O   . HOH O 8 .   ? 20.169  -17.248 -55.000 1.00 27.17  ? 614 HOH B O   1 
HETATM 4886 O  O   . HOH O 8 .   ? 29.422  -4.780  -25.088 1.00 31.65  ? 615 HOH B O   1 
HETATM 4887 O  O   . HOH O 8 .   ? 35.825  -29.425 -33.645 1.00 25.41  ? 616 HOH B O   1 
HETATM 4888 O  O   . HOH O 8 .   ? 34.328  -18.786 -17.218 1.00 33.82  ? 617 HOH B O   1 
HETATM 4889 O  O   . HOH O 8 .   ? 22.279  -9.123  -9.998  1.00 47.71  ? 618 HOH B O   1 
HETATM 4890 O  O   . HOH O 8 .   ? 31.244  -25.608 -13.980 1.00 74.55  ? 619 HOH B O   1 
HETATM 4891 O  O   . HOH O 8 .   ? 11.530  -22.929 -31.623 1.00 9.96   ? 620 HOH B O   1 
HETATM 4892 O  O   . HOH O 8 .   ? 22.622  -6.326  -45.152 1.00 25.07  ? 621 HOH B O   1 
HETATM 4893 O  O   . HOH O 8 .   ? 22.475  -2.746  -24.160 1.00 38.98  ? 622 HOH B O   1 
HETATM 4894 O  O   . HOH O 8 .   ? 30.185  -3.006  -34.911 1.00 28.59  ? 623 HOH B O   1 
HETATM 4895 O  O   . HOH O 8 .   ? 26.498  -13.246 -7.692  1.00 40.62  ? 624 HOH B O   1 
HETATM 4896 O  O   . HOH O 8 .   ? 31.215  -10.900 -17.743 1.00 23.60  ? 625 HOH B O   1 
HETATM 4897 O  O   . HOH O 8 .   ? 16.420  -23.353 -9.459  1.00 30.83  ? 626 HOH B O   1 
HETATM 4898 O  O   . HOH O 8 .   ? 9.653   -11.519 -45.575 1.00 33.82  ? 627 HOH B O   1 
HETATM 4899 O  O   . HOH O 8 .   ? 24.418  -27.425 -10.320 1.00 49.48  ? 628 HOH B O   1 
HETATM 4900 O  O   . HOH O 8 .   ? 12.783  -21.973 -27.320 1.00 24.54  ? 629 HOH B O   1 
HETATM 4901 O  O   . HOH O 8 .   ? 34.302  -21.863 -45.112 1.00 48.57  ? 630 HOH B O   1 
HETATM 4902 O  O   . HOH O 8 .   ? 9.472   -28.157 -10.379 1.00 43.84  ? 631 HOH B O   1 
HETATM 4903 O  O   . HOH O 8 .   ? 5.821   -21.300 -44.869 1.00 23.71  ? 632 HOH B O   1 
HETATM 4904 O  O   . HOH O 8 .   ? 13.067  -38.152 -22.142 1.00 32.09  ? 633 HOH B O   1 
HETATM 4905 O  O   . HOH O 8 .   ? 23.027  -5.589  -47.793 1.00 31.31  ? 634 HOH B O   1 
HETATM 4906 O  O   . HOH O 8 .   ? 11.559  -9.058  -24.872 1.00 36.35  ? 635 HOH B O   1 
HETATM 4907 O  O   . HOH O 8 .   ? 18.913  -22.657 -23.775 1.00 10.18  ? 636 HOH B O   1 
HETATM 4908 O  O   . HOH O 8 .   ? 32.362  -37.066 -29.361 1.00 22.33  ? 637 HOH B O   1 
HETATM 4909 O  O   . HOH O 8 .   ? 15.665  -15.581 -10.412 1.00 78.65  ? 638 HOH B O   1 
HETATM 4910 O  O   . HOH O 8 .   ? 30.889  -10.585 -45.952 1.00 30.13  ? 639 HOH B O   1 
HETATM 4911 O  O   . HOH O 8 .   ? 41.170  -31.431 -37.329 1.00 47.50  ? 640 HOH B O   1 
HETATM 4912 O  O   . HOH O 8 .   ? 29.524  -39.581 -21.020 1.00 27.15  ? 641 HOH B O   1 
HETATM 4913 O  O   . HOH O 8 .   ? -1.120  -25.866 -38.309 1.00 32.06  ? 642 HOH B O   1 
HETATM 4914 O  O   . HOH O 8 .   ? 30.619  -8.104  -42.685 1.00 16.95  ? 643 HOH B O   1 
HETATM 4915 O  O   . HOH O 8 .   ? 23.287  -41.014 -24.405 1.00 26.94  ? 644 HOH B O   1 
HETATM 4916 O  O   . HOH O 8 .   ? 15.540  -32.372 -50.357 1.00 38.01  ? 645 HOH B O   1 
HETATM 4917 O  O   . HOH O 8 .   ? 20.874  -10.106 -41.503 1.00 9.98   ? 646 HOH B O   1 
HETATM 4918 O  O   . HOH O 8 .   ? 4.189   -29.960 -31.598 1.00 41.20  ? 647 HOH B O   1 
HETATM 4919 O  O   . HOH O 8 .   ? 10.391  -17.667 -50.381 1.00 30.11  ? 648 HOH B O   1 
HETATM 4920 O  O   . HOH O 8 .   ? 20.188  -2.956  -45.596 1.00 30.11  ? 649 HOH B O   1 
HETATM 4921 O  O   . HOH O 8 .   ? 5.901   -22.231 -42.395 1.00 19.27  ? 650 HOH B O   1 
HETATM 4922 O  O   . HOH O 8 .   ? 3.632   -19.324 -14.646 1.00 41.09  ? 651 HOH B O   1 
HETATM 4923 O  O   . HOH O 8 .   ? 19.368  -12.880 -44.995 1.00 17.14  ? 652 HOH B O   1 
HETATM 4924 O  O   . HOH O 8 .   ? 10.017  -19.917 -11.128 1.00 21.42  ? 653 HOH B O   1 
HETATM 4925 O  O   . HOH O 8 .   ? 34.402  -10.274 -36.059 1.00 18.81  ? 654 HOH B O   1 
HETATM 4926 O  O   . HOH O 8 .   ? 28.824  -39.998 -30.560 1.00 20.76  ? 655 HOH B O   1 
HETATM 4927 O  O   . HOH O 8 .   ? 24.541  -35.507 -45.033 1.00 24.81  ? 656 HOH B O   1 
HETATM 4928 O  O   . HOH O 8 .   ? 6.534   -13.804 -45.712 1.00 20.16  ? 657 HOH B O   1 
HETATM 4929 O  O   . HOH O 8 .   ? 36.111  -12.655 -42.938 1.00 24.45  ? 658 HOH B O   1 
HETATM 4930 O  O   . HOH O 8 .   ? 14.990  -30.792 -48.042 1.00 20.19  ? 659 HOH B O   1 
HETATM 4931 O  O   . HOH O 8 .   ? 12.234  -23.482 -8.786  1.00 28.69  ? 660 HOH B O   1 
HETATM 4932 O  O   . HOH O 8 .   ? 11.420  -9.530  -43.903 1.00 27.57  ? 661 HOH B O   1 
HETATM 4933 O  O   . HOH O 8 .   ? 10.511  -17.877 -4.967  1.00 30.34  ? 662 HOH B O   1 
HETATM 4934 O  O   . HOH O 8 .   ? 30.373  -1.839  -38.867 1.00 34.90  ? 663 HOH B O   1 
HETATM 4935 O  O   . HOH O 8 .   ? 17.245  -12.855 -22.175 1.00 22.73  ? 664 HOH B O   1 
HETATM 4936 O  O   . HOH O 8 .   ? 27.682  -35.003 -37.936 1.00 19.13  ? 665 HOH B O   1 
HETATM 4937 O  O   . HOH O 8 .   ? 17.153  -33.715 -47.557 1.00 30.44  ? 666 HOH B O   1 
HETATM 4938 O  O   . HOH O 8 .   ? -1.431  -19.193 -31.840 1.00 25.91  ? 667 HOH B O   1 
HETATM 4939 O  O   . HOH O 8 .   ? 9.165   -4.156  -40.218 1.00 30.20  ? 668 HOH B O   1 
HETATM 4940 O  O   . HOH O 8 .   ? 27.043  -32.750 -42.307 1.00 18.55  ? 669 HOH B O   1 
HETATM 4941 O  O   . HOH O 8 .   ? 9.222   -13.874 -28.053 1.00 35.16  ? 670 HOH B O   1 
HETATM 4942 O  O   . HOH O 8 .   ? 7.696   -32.021 -21.028 1.00 23.19  ? 671 HOH B O   1 
HETATM 4943 O  O   . HOH O 8 .   ? 25.694  -9.810  -13.704 1.00 26.43  ? 672 HOH B O   1 
HETATM 4944 O  O   . HOH O 8 .   ? 18.244  -34.261 -27.255 1.00 10.41  ? 673 HOH B O   1 
HETATM 4945 O  O   . HOH O 8 .   ? 37.830  -16.091 -39.622 1.00 31.65  ? 674 HOH B O   1 
HETATM 4946 O  O   . HOH O 8 .   ? 0.433   -23.623 -7.991  1.00 33.12  ? 675 HOH B O   1 
HETATM 4947 O  O   . HOH O 8 .   ? 14.536  -27.325 -47.103 1.00 19.52  ? 676 HOH B O   1 
HETATM 4948 O  O   . HOH O 8 .   ? 30.016  -23.193 -57.264 1.00 78.99  ? 677 HOH B O   1 
HETATM 4949 O  O   . HOH O 8 .   ? 20.669  -37.116 -33.005 1.00 11.56  ? 678 HOH B O   1 
HETATM 4950 O  O   . HOH O 8 .   ? 7.592   -23.163 -23.586 1.00 21.42  ? 679 HOH B O   1 
HETATM 4951 O  O   . HOH O 8 .   ? 8.417   -34.397 -25.127 1.00 24.60  ? 680 HOH B O   1 
HETATM 4952 O  O   . HOH O 8 .   ? 20.616  -5.457  -24.689 1.00 29.49  ? 681 HOH B O   1 
HETATM 4953 O  O   . HOH O 8 .   ? 15.788  -16.578 -27.818 1.00 89.43  ? 682 HOH B O   1 
HETATM 4954 O  O   . HOH O 8 .   ? 22.258  -9.380  -19.031 1.00 23.55  ? 683 HOH B O   1 
HETATM 4955 O  O   . HOH O 8 .   ? 2.038   -24.725 -5.332  1.00 30.79  ? 684 HOH B O   1 
HETATM 4956 O  O   . HOH O 8 .   ? 27.296  -27.228 -36.304 1.00 9.27   ? 685 HOH B O   1 
HETATM 4957 O  O   . HOH O 8 .   ? 24.037  1.118   -31.079 1.00 16.25  ? 686 HOH B O   1 
HETATM 4958 O  O   . HOH O 8 .   ? 12.742  -27.564 -45.010 1.00 11.68  ? 687 HOH B O   1 
HETATM 4959 O  O   . HOH O 8 .   ? 32.805  -3.573  -35.349 1.00 33.22  ? 688 HOH B O   1 
HETATM 4960 O  O   . HOH O 8 .   ? 28.215  -8.155  -27.204 1.00 15.93  ? 689 HOH B O   1 
HETATM 4961 O  O   . HOH O 8 .   ? 28.229  -39.205 -23.861 1.00 13.93  ? 690 HOH B O   1 
HETATM 4962 O  O   . HOH O 8 .   ? 25.208  1.270   -33.640 1.00 16.50  ? 691 HOH B O   1 
HETATM 4963 O  O   . HOH O 8 .   ? 24.159  -8.522  -43.848 1.00 17.48  ? 692 HOH B O   1 
HETATM 4964 O  O   . HOH O 8 .   ? 35.961  -19.948 -51.010 1.00 28.76  ? 693 HOH B O   1 
HETATM 4965 O  O   . HOH O 8 .   ? 8.836   -15.764 -21.537 1.00 35.99  ? 694 HOH B O   1 
HETATM 4966 O  O   . HOH O 8 .   ? 13.776  -29.982 -36.817 1.00 9.98   ? 695 HOH B O   1 
HETATM 4967 O  O   . HOH O 8 .   ? 7.267   -15.818 -24.244 1.00 44.00  ? 696 HOH B O   1 
HETATM 4968 O  O   . HOH O 8 .   ? 14.833  -32.351 -33.967 1.00 9.49   ? 697 HOH B O   1 
HETATM 4969 O  O   . HOH O 8 .   ? 30.627  -4.966  -44.896 1.00 44.88  ? 698 HOH B O   1 
HETATM 4970 O  O   . HOH O 8 .   ? 9.011   -30.609 -40.989 1.00 23.35  ? 699 HOH B O   1 
HETATM 4971 O  O   . HOH O 8 .   ? 20.920  -10.207 -23.580 1.00 25.83  ? 700 HOH B O   1 
HETATM 4972 O  O   . HOH O 8 .   ? 31.879  -26.011 -39.559 1.00 12.34  ? 701 HOH B O   1 
HETATM 4973 O  O   . HOH O 8 .   ? 28.817  -22.546 -13.214 1.00 28.33  ? 702 HOH B O   1 
HETATM 4974 O  O   . HOH O 8 .   ? 17.064  2.159   -35.469 1.00 12.31  ? 703 HOH B O   1 
HETATM 4975 O  O   . HOH O 8 .   ? 33.067  -24.616 -18.549 1.00 22.71  ? 704 HOH B O   1 
HETATM 4976 O  O   . HOH O 8 .   ? 25.156  -12.607 -48.642 1.00 33.44  ? 705 HOH B O   1 
HETATM 4977 O  O   . HOH O 8 .   ? 26.454  -2.970  -39.664 1.00 17.46  ? 706 HOH B O   1 
HETATM 4978 O  O   . HOH O 8 .   ? 33.427  -19.266 -50.405 1.00 27.69  ? 707 HOH B O   1 
HETATM 4979 O  O   . HOH O 8 .   ? 13.816  -31.766 -12.997 1.00 25.70  ? 708 HOH B O   1 
HETATM 4980 O  O   . HOH O 8 .   ? 10.785  -4.778  -31.742 1.00 26.87  ? 709 HOH B O   1 
HETATM 4981 O  O   . HOH O 8 .   ? 35.948  -22.159 -48.015 1.00 37.11  ? 710 HOH B O   1 
HETATM 4982 O  O   . HOH O 8 .   ? 12.578  -37.948 -37.360 1.00 28.71  ? 711 HOH B O   1 
HETATM 4983 O  O   . HOH O 8 .   ? 16.875  -24.062 -53.351 1.00 18.60  ? 712 HOH B O   1 
HETATM 4984 O  O   . HOH O 8 .   ? 10.738  -7.943  -39.294 1.00 16.96  ? 713 HOH B O   1 
HETATM 4985 O  O   . HOH O 8 .   ? 35.084  -26.442 -24.876 1.00 20.91  ? 714 HOH B O   1 
HETATM 4986 O  O   . HOH O 8 .   ? -3.200  -18.479 -40.375 1.00 23.02  ? 715 HOH B O   1 
HETATM 4987 O  O   . HOH O 8 .   ? 35.140  -14.033 -24.288 1.00 38.16  ? 716 HOH B O   1 
HETATM 4988 O  O   . HOH O 8 .   ? 17.523  -35.572 -17.368 1.00 21.84  ? 717 HOH B O   1 
HETATM 4989 O  O   . HOH O 8 .   ? 24.246  -4.614  -43.175 1.00 23.14  ? 718 HOH B O   1 
HETATM 4990 O  O   . HOH O 8 .   ? 13.643  -32.102 -41.069 1.00 11.28  ? 719 HOH B O   1 
HETATM 4991 O  O   . HOH O 8 .   ? 14.942  -34.747 -16.652 1.00 28.46  ? 720 HOH B O   1 
HETATM 4992 O  O   . HOH O 8 .   ? 18.692  -18.029 -9.321  1.00 31.76  ? 721 HOH B O   1 
HETATM 4993 O  O   . HOH O 8 .   ? 20.952  2.908   -36.015 1.00 15.04  ? 722 HOH B O   1 
HETATM 4994 O  O   . HOH O 8 .   ? 1.686   -22.601 -36.945 1.00 17.25  ? 723 HOH B O   1 
HETATM 4995 O  O   . HOH O 8 .   ? 32.319  -32.900 -34.574 1.00 31.85  ? 724 HOH B O   1 
HETATM 4996 O  O   . HOH O 8 .   ? 26.355  -31.158 -40.325 1.00 13.61  ? 725 HOH B O   1 
HETATM 4997 O  O   . HOH O 8 .   ? 11.331  -24.905 -52.351 1.00 27.08  ? 726 HOH B O   1 
HETATM 4998 O  O   . HOH O 8 .   ? -5.667  -15.464 -31.360 1.00 29.59  ? 727 HOH B O   1 
HETATM 4999 O  O   . HOH O 8 .   ? 25.700  0.527   -28.994 1.00 15.33  ? 728 HOH B O   1 
HETATM 5000 O  O   . HOH O 8 .   ? 7.725   -30.183 -25.327 1.00 24.39  ? 729 HOH B O   1 
HETATM 5001 O  O   . HOH O 8 .   ? 24.974  -37.345 -34.615 1.00 13.58  ? 730 HOH B O   1 
HETATM 5002 O  O   . HOH O 8 .   ? 33.691  -29.861 -32.978 1.00 27.54  ? 731 HOH B O   1 
HETATM 5003 O  O   . HOH O 8 .   ? 33.520  -21.739 -22.531 1.00 24.21  ? 732 HOH B O   1 
HETATM 5004 O  O   . HOH O 8 .   ? 15.064  -18.339 -25.802 1.00 35.11  ? 733 HOH B O   1 
HETATM 5005 O  O   . HOH O 8 .   ? 32.058  -13.010 -20.628 1.00 18.96  ? 734 HOH B O   1 
HETATM 5006 O  O   . HOH O 8 .   ? 4.840   -11.629 -36.155 1.00 20.36  ? 735 HOH B O   1 
HETATM 5007 O  O   . HOH O 8 .   ? 14.053  -34.703 -40.257 1.00 13.00  ? 736 HOH B O   1 
HETATM 5008 O  O   . HOH O 8 .   ? 33.326  -33.636 -31.929 1.00 37.52  ? 737 HOH B O   1 
HETATM 5009 O  O   . HOH O 8 .   ? 23.735  -37.351 -30.481 1.00 13.68  ? 738 HOH B O   1 
HETATM 5010 O  O   . HOH O 8 .   ? 17.607  -27.460 -48.576 1.00 17.11  ? 739 HOH B O   1 
HETATM 5011 O  O   . HOH O 8 .   ? 21.300  -17.703 -49.427 1.00 22.58  ? 740 HOH B O   1 
HETATM 5012 O  O   . HOH O 8 .   ? 26.577  -28.743 -48.917 1.00 18.58  ? 741 HOH B O   1 
HETATM 5013 O  O   . HOH O 8 .   ? 33.708  -32.011 -27.154 1.00 20.18  ? 742 HOH B O   1 
HETATM 5014 O  O   . HOH O 8 .   ? 25.989  -15.041 -51.199 1.00 33.29  ? 743 HOH B O   1 
HETATM 5015 O  O   . HOH O 8 .   ? 23.595  -19.484 -9.732  1.00 34.71  ? 744 HOH B O   1 
HETATM 5016 O  O   . HOH O 8 .   ? 14.612  -23.594 -27.052 1.00 21.86  ? 745 HOH B O   1 
HETATM 5017 O  O   . HOH O 8 .   ? 19.559  -28.846 -14.649 1.00 23.21  ? 746 HOH B O   1 
HETATM 5018 O  O   . HOH O 8 .   ? 37.125  -22.742 -40.934 1.00 21.48  ? 747 HOH B O   1 
HETATM 5019 O  O   . HOH O 8 .   ? 29.518  -8.729  -24.784 1.00 15.12  ? 748 HOH B O   1 
HETATM 5020 O  O   . HOH O 8 .   ? 5.331   -26.245 -38.199 1.00 30.34  ? 749 HOH B O   1 
HETATM 5021 O  O   . HOH O 8 .   ? 22.323  -16.041 -46.847 1.00 17.93  ? 750 HOH B O   1 
HETATM 5022 O  O   . HOH O 8 .   ? -5.115  -21.232 -30.311 1.00 21.76  ? 751 HOH B O   1 
HETATM 5023 O  O   . HOH O 8 .   ? 11.642  -16.972 -27.508 1.00 22.58  ? 752 HOH B O   1 
HETATM 5024 O  O   . HOH O 8 .   ? 5.356   -23.648 -36.870 1.00 14.87  ? 753 HOH B O   1 
HETATM 5025 O  O   . HOH O 8 .   ? 18.833  -34.341 -52.587 1.00 30.37  ? 754 HOH B O   1 
HETATM 5026 O  O   . HOH O 8 .   ? 23.079  -10.948 -44.781 1.00 22.80  ? 755 HOH B O   1 
HETATM 5027 O  O   . HOH O 8 .   ? 16.552  -38.541 -39.718 1.00 19.88  ? 756 HOH B O   1 
HETATM 5028 O  O   . HOH O 8 .   ? 37.803  -26.498 -41.898 1.00 33.73  ? 757 HOH B O   1 
HETATM 5029 O  O   . HOH O 8 .   ? 16.166  -1.586  -43.564 1.00 31.96  ? 758 HOH B O   1 
HETATM 5030 O  O   . HOH O 8 .   ? 20.354  -4.037  -28.147 1.00 17.27  ? 759 HOH B O   1 
HETATM 5031 O  O   . HOH O 8 .   ? 27.089  0.086   -37.994 1.00 56.35  ? 760 HOH B O   1 
HETATM 5032 O  O   . HOH O 8 .   ? -0.986  -17.379 -41.879 1.00 24.34  ? 761 HOH B O   1 
HETATM 5033 O  O   . HOH O 8 .   ? -2.760  -22.574 -29.310 1.00 36.61  ? 762 HOH B O   1 
HETATM 5034 O  O   . HOH O 8 .   ? 37.326  -29.672 -38.575 1.00 39.87  ? 763 HOH B O   1 
HETATM 5035 O  O   . HOH O 8 .   ? 21.337  -38.291 -23.060 1.00 25.97  ? 764 HOH B O   1 
HETATM 5036 O  O   . HOH O 8 .   ? -2.805  -24.563 -40.235 1.00 27.08  ? 765 HOH B O   1 
HETATM 5037 O  O   . HOH O 8 .   ? 23.685  -35.290 -15.689 1.00 38.70  ? 766 HOH B O   1 
HETATM 5038 O  O   . HOH O 8 .   ? 11.298  -36.112 -33.869 1.00 84.47  ? 767 HOH B O   1 
HETATM 5039 O  O   . HOH O 8 .   ? 8.600   -25.051 -50.333 1.00 24.70  ? 768 HOH B O   1 
HETATM 5040 O  O   . HOH O 8 .   ? 23.334  -35.672 -42.597 1.00 13.72  ? 769 HOH B O   1 
HETATM 5041 O  O   . HOH O 8 .   ? 23.086  -27.594 -12.532 1.00 32.98  ? 770 HOH B O   1 
HETATM 5042 O  O   . HOH O 8 .   ? 6.009   -25.383 -23.677 1.00 27.63  ? 771 HOH B O   1 
HETATM 5043 O  O   . HOH O 8 .   ? 34.002  -19.520 -19.806 1.00 25.07  ? 772 HOH B O   1 
HETATM 5044 O  O   . HOH O 8 .   ? 31.527  -18.066 -16.168 1.00 33.70  ? 773 HOH B O   1 
HETATM 5045 O  O   . HOH O 8 .   ? 20.871  2.021   -40.946 1.00 18.95  ? 774 HOH B O   1 
HETATM 5046 O  O   . HOH O 8 .   ? 1.994   -15.730 -43.705 1.00 32.90  ? 775 HOH B O   1 
HETATM 5047 O  O   . HOH O 8 .   ? 34.307  -19.544 -42.420 1.00 16.80  ? 776 HOH B O   1 
HETATM 5048 O  O   . HOH O 8 .   ? 27.292  -19.970 -56.160 1.00 35.14  ? 777 HOH B O   1 
HETATM 5049 O  O   . HOH O 8 .   ? 36.726  -26.218 -46.398 1.00 94.35  ? 778 HOH B O   1 
HETATM 5050 O  O   . HOH O 8 .   ? 33.001  -28.375 -41.218 1.00 22.74  ? 779 HOH B O   1 
HETATM 5051 O  O   . HOH O 8 .   ? 8.994   -20.378 -45.325 1.00 13.82  ? 780 HOH B O   1 
HETATM 5052 O  O   . HOH O 8 .   ? 7.290   -17.509 -13.544 1.00 50.38  ? 781 HOH B O   1 
HETATM 5053 O  O   . HOH O 8 .   ? 18.765  -38.673 -42.627 1.00 19.80  ? 782 HOH B O   1 
HETATM 5054 O  O   . HOH O 8 .   ? 12.630  -14.392 -23.850 1.00 88.98  ? 783 HOH B O   1 
HETATM 5055 O  O   . HOH O 8 .   ? 3.217   -22.387 -45.948 1.00 35.98  ? 784 HOH B O   1 
HETATM 5056 O  O   . HOH O 8 .   ? 18.297  0.150   -26.367 1.00 20.04  ? 785 HOH B O   1 
HETATM 5057 O  O   . HOH O 8 .   ? 12.897  -36.897 -46.971 1.00 25.85  ? 786 HOH B O   1 
HETATM 5058 O  O   . HOH O 8 .   ? 8.991   -9.973  -40.275 1.00 18.37  ? 787 HOH B O   1 
HETATM 5059 O  O   . HOH O 8 .   ? 10.790  -27.333 -48.457 1.00 24.01  ? 788 HOH B O   1 
HETATM 5060 O  O   . HOH O 8 .   ? 39.837  -12.079 -23.229 1.00 47.43  ? 789 HOH B O   1 
HETATM 5061 O  O   . HOH O 8 .   ? 18.419  -11.409 -24.200 1.00 36.02  ? 790 HOH B O   1 
HETATM 5062 O  O   . HOH O 8 .   ? 10.543  -39.363 -30.576 1.00 39.50  ? 791 HOH B O   1 
HETATM 5063 O  O   . HOH O 8 .   ? 35.608  -7.709  -35.527 1.00 30.74  ? 792 HOH B O   1 
HETATM 5064 O  O   . HOH O 8 .   ? 16.770  -38.177 -21.400 1.00 34.17  ? 793 HOH B O   1 
HETATM 5065 O  O   . HOH O 8 .   ? 33.286  -30.443 -29.927 1.00 22.38  ? 794 HOH B O   1 
HETATM 5066 O  O   . HOH O 8 .   ? 12.326  -31.125 -38.756 1.00 10.94  ? 795 HOH B O   1 
HETATM 5067 O  O   . HOH O 8 .   ? 16.286  -3.595  -27.793 1.00 30.09  ? 796 HOH B O   1 
HETATM 5068 O  O   . HOH O 8 .   ? 3.583   -24.631 -22.468 1.00 32.21  ? 797 HOH B O   1 
HETATM 5069 O  O   . HOH O 8 .   ? 16.937  -27.254 -8.850  1.00 36.42  ? 798 HOH B O   1 
HETATM 5070 O  O   . HOH O 8 .   ? 31.917  0.763   -28.118 1.00 27.68  ? 799 HOH B O   1 
HETATM 5071 O  O   . HOH O 8 .   ? 19.362  -24.625 -51.897 1.00 18.12  ? 800 HOH B O   1 
HETATM 5072 O  O   . HOH O 8 .   ? 31.531  -38.470 -22.486 1.00 24.23  ? 801 HOH B O   1 
HETATM 5073 O  O   . HOH O 8 .   ? 10.567  -33.131 -38.049 1.00 21.24  ? 802 HOH B O   1 
HETATM 5074 O  O   . HOH O 8 .   ? 29.094  -15.198 -12.289 1.00 86.14  ? 803 HOH B O   1 
HETATM 5075 O  O   . HOH O 8 .   ? 4.588   -17.858 -24.183 1.00 36.36  ? 804 HOH B O   1 
HETATM 5076 O  O   . HOH O 8 .   ? 4.535   -21.686 -22.537 1.00 39.09  ? 805 HOH B O   1 
HETATM 5077 O  O   . HOH O 8 .   ? 2.595   -12.690 -37.586 1.00 17.86  ? 806 HOH B O   1 
HETATM 5078 O  O   . HOH O 8 .   ? 0.019   -31.952 -25.325 1.00 43.46  ? 807 HOH B O   1 
HETATM 5079 O  O   . HOH O 8 .   ? 25.477  -38.842 -39.015 1.00 30.30  ? 808 HOH B O   1 
HETATM 5080 O  O   . HOH O 8 .   ? 17.276  -17.281 -51.043 1.00 27.73  ? 809 HOH B O   1 
HETATM 5081 O  O   . HOH O 8 .   ? 21.609  -7.220  -22.834 1.00 37.20  ? 810 HOH B O   1 
HETATM 5082 O  O   . HOH O 8 .   ? 22.922  -15.077 -9.001  1.00 33.37  ? 811 HOH B O   1 
HETATM 5083 O  O   . HOH O 8 .   ? 5.325   -31.758 -10.034 1.00 26.11  ? 812 HOH B O   1 
HETATM 5084 O  O   . HOH O 8 .   ? 36.144  -10.648 -22.267 1.00 36.10  ? 813 HOH B O   1 
HETATM 5085 O  O   . HOH O 8 .   ? 21.397  -1.314  -28.179 1.00 23.85  ? 814 HOH B O   1 
HETATM 5086 O  O   . HOH O 8 .   ? 33.777  -40.158 -26.153 1.00 41.53  ? 815 HOH B O   1 
HETATM 5087 O  O   . HOH O 8 .   ? 19.801  -26.781 -50.076 1.00 22.23  ? 816 HOH B O   1 
HETATM 5088 O  O   . HOH O 8 .   ? 10.105  -20.704 -55.415 1.00 71.05  ? 817 HOH B O   1 
HETATM 5089 O  O   . HOH O 8 .   ? 34.975  -28.284 -17.784 1.00 26.28  ? 818 HOH B O   1 
HETATM 5090 O  O   . HOH O 8 .   ? 15.782  -31.343 -10.720 1.00 31.66  ? 819 HOH B O   1 
HETATM 5091 O  O   . HOH O 8 .   ? 17.699  -27.531 -13.423 1.00 34.59  ? 820 HOH B O   1 
HETATM 5092 O  O   . HOH O 8 .   ? 37.138  -15.737 -36.856 1.00 79.93  ? 821 HOH B O   1 
HETATM 5093 O  O   . HOH O 8 .   ? 29.119  -6.606  -28.879 1.00 37.90  ? 822 HOH B O   1 
HETATM 5094 O  O   . HOH O 8 .   ? 2.140   -27.330 -15.551 1.00 44.36  ? 823 HOH B O   1 
HETATM 5095 O  O   . HOH O 8 .   ? 34.003  -18.965 -47.734 1.00 40.00  ? 824 HOH B O   1 
HETATM 5096 O  O   . HOH O 8 .   ? 14.482  -14.863 -26.091 1.00 37.59  ? 825 HOH B O   1 
HETATM 5097 O  O   . HOH O 8 .   ? 12.984  -33.809 -48.696 1.00 27.47  ? 826 HOH B O   1 
HETATM 5098 O  O   . HOH O 8 .   ? 14.281  -18.773 -29.235 1.00 27.40  ? 827 HOH B O   1 
HETATM 5099 O  O   . HOH O 8 .   ? 0.144   -21.347 -29.858 1.00 28.13  ? 828 HOH B O   1 
HETATM 5100 O  O   . HOH O 8 .   ? 23.136  -0.022  -28.174 1.00 27.10  ? 829 HOH B O   1 
HETATM 5101 O  O   . HOH O 8 .   ? 11.759  -7.413  -41.744 1.00 27.35  ? 830 HOH B O   1 
HETATM 5102 O  O   . HOH O 8 .   ? 3.372   -15.141 -51.247 1.00 66.66  ? 831 HOH B O   1 
HETATM 5103 O  O   . HOH O 8 .   ? 8.914   -16.158 -51.741 1.00 53.81  ? 832 HOH B O   1 
HETATM 5104 O  O   . HOH O 8 .   ? 23.183  -36.023 -32.785 1.00 11.43  ? 833 HOH B O   1 
HETATM 5105 O  O   . HOH O 8 .   ? 28.732  -27.813 -50.597 1.00 31.40  ? 834 HOH B O   1 
HETATM 5106 O  O   . HOH O 8 .   ? 9.570   -18.253 -9.063  1.00 30.99  ? 835 HOH B O   1 
HETATM 5107 O  O   . HOH O 8 .   ? -0.003  -27.320 -24.121 1.00 33.65  ? 836 HOH B O   1 
HETATM 5108 O  O   . HOH O 8 .   ? -5.332  -28.907 -30.625 1.00 50.16  ? 837 HOH B O   1 
HETATM 5109 O  O   . HOH O 8 .   ? 1.693   -23.384 -39.579 1.00 25.56  ? 838 HOH B O   1 
HETATM 5110 O  O   . HOH O 8 .   ? 13.127  -19.026 -26.301 1.00 26.27  ? 839 HOH B O   1 
HETATM 5111 O  O   . HOH O 8 .   ? 17.858  -23.485 -56.003 1.00 30.04  ? 840 HOH B O   1 
HETATM 5112 O  O   . HOH O 8 .   ? 6.707   -11.802 -28.668 1.00 46.08  ? 841 HOH B O   1 
HETATM 5113 O  O   . HOH O 8 .   ? 34.135  -8.456  -43.291 1.00 52.23  ? 842 HOH B O   1 
HETATM 5114 O  O   . HOH O 8 .   ? 37.969  -20.177 -24.540 1.00 39.24  ? 843 HOH B O   1 
HETATM 5115 O  O   . HOH O 8 .   ? 33.840  -22.156 -19.750 1.00 41.49  ? 844 HOH B O   1 
HETATM 5116 O  O   . HOH O 8 .   ? 18.501  2.992   -37.627 1.00 13.46  ? 845 HOH B O   1 
HETATM 5117 O  O   . HOH O 8 .   ? 3.853   -24.275 -19.492 1.00 34.92  ? 846 HOH B O   1 
HETATM 5118 O  O   . HOH O 8 .   ? 21.472  -29.778 -13.011 1.00 36.87  ? 847 HOH B O   1 
HETATM 5119 O  O   . HOH O 8 .   ? -5.947  -25.133 -29.012 1.00 28.72  ? 848 HOH B O   1 
HETATM 5120 O  O   . HOH O 8 .   ? 26.886  -33.483 -44.756 1.00 32.34  ? 849 HOH B O   1 
HETATM 5121 O  O   . HOH O 8 .   ? 36.835  -16.207 -55.434 1.00 47.30  ? 850 HOH B O   1 
HETATM 5122 O  O   . HOH O 8 .   ? 27.978  -23.379 -10.753 1.00 32.82  ? 851 HOH B O   1 
HETATM 5123 O  O   . HOH O 8 .   ? 26.545  -2.049  -42.426 1.00 38.80  ? 852 HOH B O   1 
HETATM 5124 O  O   . HOH O 8 .   ? 28.089  1.150   -33.417 1.00 23.57  ? 853 HOH B O   1 
HETATM 5125 O  O   . HOH O 8 .   ? 6.832   -32.638 -28.333 1.00 35.60  ? 854 HOH B O   1 
HETATM 5126 O  O   . HOH O 8 .   ? 25.680  -35.054 -41.581 1.00 32.72  ? 855 HOH B O   1 
HETATM 5127 O  O   . HOH O 8 .   ? 35.329  -10.055 -42.024 1.00 38.37  ? 856 HOH B O   1 
HETATM 5128 O  O   . HOH O 8 .   ? -1.526  -25.149 -23.407 1.00 46.02  ? 857 HOH B O   1 
HETATM 5129 O  O   . HOH O 8 .   ? 27.763  -27.454 -9.604  1.00 28.58  ? 858 HOH B O   1 
HETATM 5130 O  O   . HOH O 8 .   ? 7.387   -32.188 -23.902 1.00 31.47  ? 859 HOH B O   1 
HETATM 5131 O  O   . HOH O 8 .   ? 37.371  -25.475 -23.703 1.00 41.49  ? 860 HOH B O   1 
HETATM 5132 O  O   . HOH O 8 .   ? 28.235  -30.987 -47.498 1.00 35.66  ? 861 HOH B O   1 
HETATM 5133 O  O   . HOH O 8 .   ? 11.544  -31.883 -42.899 1.00 23.46  ? 862 HOH B O   1 
HETATM 5134 O  O   . HOH O 8 .   ? 22.685  -12.268 -47.227 1.00 37.79  ? 863 HOH B O   1 
HETATM 5135 O  O   . HOH O 8 .   ? 15.088  1.748   -37.455 1.00 20.66  ? 864 HOH B O   1 
HETATM 5136 O  O   . HOH O 8 .   ? 9.280   -15.661 -17.748 1.00 37.51  ? 865 HOH B O   1 
HETATM 5137 O  O   . HOH O 8 .   ? 27.213  -36.702 -36.025 1.00 20.66  ? 866 HOH B O   1 
HETATM 5138 O  O   . HOH O 8 .   ? 11.989  -15.694 -8.665  1.00 31.95  ? 867 HOH B O   1 
HETATM 5139 O  O   . HOH O 8 .   ? 26.953  -36.592 -39.982 1.00 30.35  ? 868 HOH B O   1 
HETATM 5140 O  O   . HOH O 8 .   ? 3.778   -24.123 -43.252 1.00 36.55  ? 869 HOH B O   1 
HETATM 5141 O  O   . HOH O 8 .   ? 20.888  -13.940 -46.899 1.00 25.24  ? 870 HOH B O   1 
HETATM 5142 O  O   . HOH O 8 .   ? 9.438   -34.832 -39.787 1.00 43.52  ? 871 HOH B O   1 
HETATM 5143 O  O   . HOH O 8 .   ? 12.233  -36.384 -41.516 1.00 25.05  ? 872 HOH B O   1 
HETATM 5144 O  O   . HOH O 8 .   ? 38.185  -13.812 -41.066 1.00 38.47  ? 873 HOH B O   1 
HETATM 5145 O  O   . HOH O 8 .   ? 39.736  -10.980 -36.795 1.00 48.86  ? 874 HOH B O   1 
HETATM 5146 O  O   . HOH O 8 .   ? 6.972   -16.189 -15.785 1.00 33.79  ? 875 HOH B O   1 
HETATM 5147 O  O   . HOH O 8 .   ? 10.422  -15.334 -25.980 1.00 34.50  ? 876 HOH B O   1 
HETATM 5148 O  O   . HOH O 8 .   ? 8.506   -6.371  -38.543 1.00 27.49  ? 877 HOH B O   1 
HETATM 5149 O  O   . HOH O 8 .   ? 17.402  -34.560 -54.589 1.00 25.47  ? 878 HOH B O   1 
HETATM 5150 O  O   . HOH O 8 .   ? 11.403  -32.057 -49.058 1.00 25.56  ? 879 HOH B O   1 
HETATM 5151 O  O   . HOH O 8 .   ? 8.789   -9.286  -42.899 1.00 34.88  ? 880 HOH B O   1 
HETATM 5152 O  O   . HOH O 8 .   ? 19.534  -15.756 -50.742 1.00 27.17  ? 881 HOH B O   1 
HETATM 5153 O  O   . HOH O 8 .   ? 16.305  1.530   -42.197 1.00 25.13  ? 882 HOH B O   1 
HETATM 5154 O  O   . HOH O 8 .   ? 34.372  -25.904 -16.063 1.00 35.06  ? 883 HOH B O   1 
HETATM 5155 O  O   . HOH O 8 .   ? 12.510  -30.557 -47.510 1.00 31.05  ? 884 HOH B O   1 
HETATM 5156 O  O   . HOH O 8 .   ? 11.219  -36.284 -14.030 1.00 36.55  ? 885 HOH B O   1 
HETATM 5157 O  O   . HOH O 8 .   ? 17.613  -28.900 -11.177 1.00 32.87  ? 886 HOH B O   1 
HETATM 5158 O  O   . HOH O 8 .   ? 8.400   -28.485 -47.334 1.00 38.44  ? 887 HOH B O   1 
HETATM 5159 O  O   . HOH O 8 .   ? 38.099  -23.002 -24.771 1.00 39.59  ? 888 HOH B O   1 
HETATM 5160 O  O   . HOH O 8 .   ? 16.157  -36.973 -19.575 1.00 47.60  ? 889 HOH B O   1 
HETATM 5161 O  O   . HOH O 8 .   ? 14.157  -34.276 -13.417 1.00 34.28  ? 890 HOH B O   1 
HETATM 5162 O  O   . HOH O 8 .   ? 21.756  -7.878  -16.538 1.00 30.93  ? 891 HOH B O   1 
HETATM 5163 O  O   . HOH O 8 .   ? 24.306  -15.207 -49.140 1.00 29.76  ? 892 HOH B O   1 
HETATM 5164 O  O   . HOH O 8 .   ? 8.181   -32.941 -36.671 1.00 34.28  ? 893 HOH B O   1 
HETATM 5165 O  O   . HOH O 8 .   ? 11.409  -30.017 -44.901 1.00 17.52  ? 894 HOH B O   1 
HETATM 5166 O  O   . HOH O 8 .   ? 31.562  -39.398 -30.520 1.00 29.20  ? 895 HOH B O   1 
HETATM 5167 O  O   . HOH O 8 .   ? 14.898  -26.648 -7.408  1.00 33.72  ? 896 HOH B O   1 
HETATM 5168 O  O   . HOH O 8 .   ? 37.067  -20.048 -41.884 1.00 22.96  ? 897 HOH B O   1 
HETATM 5169 O  O   . HOH O 8 .   ? 10.864  -25.839 -8.355  1.00 47.87  ? 898 HOH B O   1 
HETATM 5170 O  O   . HOH O 8 .   ? 3.819   -13.346 -44.485 1.00 38.00  ? 899 HOH B O   1 
HETATM 5171 O  O   . HOH O 8 .   ? 3.636   -10.348 -33.897 1.00 31.79  ? 900 HOH B O   1 
HETATM 5172 O  O   . HOH O 8 .   ? 14.315  -28.376 -49.720 1.00 45.19  ? 901 HOH B O   1 
HETATM 5173 O  O   . HOH O 8 .   ? 23.177  -38.362 -42.059 1.00 20.40  ? 902 HOH B O   1 
HETATM 5174 O  O   . HOH O 8 .   ? 6.112   -30.575 -38.931 1.00 42.42  ? 903 HOH B O   1 
HETATM 5175 O  O   . HOH O 8 .   ? 27.548  -7.628  -13.956 1.00 28.11  ? 904 HOH B O   1 
HETATM 5176 O  O   . HOH O 8 .   ? 38.348  -20.122 -44.310 1.00 31.74  ? 905 HOH B O   1 
HETATM 5177 O  O   . HOH O 8 .   ? 40.028  -14.651 -43.181 1.00 37.53  ? 906 HOH B O   1 
HETATM 5178 O  O   . HOH O 8 .   ? 5.250   -25.426 -49.466 1.00 47.49  ? 907 HOH B 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   . MET A 1   ? 0.6148 0.5303 0.5644 -0.0289 0.0489  -0.0137 1   MET A N   
2    C  CA  . MET A 1   ? 0.3794 0.4751 0.4884 -0.0063 -0.0644 -0.0055 1   MET A CA  
3    C  C   . MET A 1   ? 0.4598 0.4431 0.5812 -0.0141 -0.0531 -0.0228 1   MET A C   
4    O  O   . MET A 1   ? 0.4589 0.4496 0.4812 -0.0236 -0.0271 -0.0546 1   MET A O   
5    C  CB  . MET A 1   ? 0.2793 0.3546 0.3332 -0.0154 -0.0142 0.0006  1   MET A CB  
6    C  CG  . MET A 1   ? 0.4490 0.3743 0.3749 -0.0283 -0.0167 -0.0359 1   MET A CG  
7    S  SD  . MET A 1   ? 0.3837 0.3788 0.4108 -0.0164 -0.0017 -0.0049 1   MET A SD  
8    C  CE  . MET A 1   ? 0.3887 0.3483 0.3842 -0.0115 0.0216  0.0138  1   MET A CE  
9    N  N   . SER A 2   ? 0.5303 0.6825 0.7520 -0.0417 -0.1289 0.0266  2   SER A N   
10   C  CA  . SER A 2   ? 0.4465 0.5715 0.5655 0.0097  -0.0399 0.0269  2   SER A CA  
11   C  C   . SER A 2   ? 0.4997 0.6104 0.5514 -0.0485 -0.0815 0.0010  2   SER A C   
12   O  O   . SER A 2   ? 0.5189 0.7501 0.6586 -0.0676 -0.0926 0.0238  2   SER A O   
13   C  CB  . SER A 2   ? 0.4079 0.4327 0.4621 -0.0335 -0.0225 0.0289  2   SER A CB  
14   O  OG  . SER A 2   ? 0.4257 0.4447 0.4460 -0.0445 0.0309  0.0055  2   SER A OG  
15   N  N   . HIS A 3   ? 0.6717 0.7613 0.6597 0.0812  0.0966  -0.0876 3   HIS A N   
16   C  CA  . HIS A 3   ? 0.2390 0.3838 0.4052 -0.0277 -0.1460 0.0904  3   HIS A CA  
17   C  C   . HIS A 3   ? 0.3905 0.3680 0.5667 0.1714  -0.0625 0.0786  3   HIS A C   
18   O  O   . HIS A 3   ? 0.4835 0.8971 0.7192 -0.3792 0.1084  -0.0835 3   HIS A O   
19   C  CB  . HIS A 3   ? 0.4384 0.5227 0.4471 -0.0248 -0.0320 0.0562  3   HIS A CB  
20   N  N   . HIS A 4   ? 0.2426 0.2937 0.6482 0.0274  0.1658  0.1557  4   HIS A N   
21   C  CA  . HIS A 4   ? 0.2569 0.2288 0.3971 -0.0054 0.1058  0.0799  4   HIS A CA  
22   C  C   . HIS A 4   ? 0.2145 0.1938 0.3655 -0.0350 0.0811  0.0439  4   HIS A C   
23   O  O   . HIS A 4   ? 0.2601 0.2269 0.3673 -0.0126 0.1396  0.0028  4   HIS A O   
24   C  CB  . HIS A 4   ? 0.2247 0.3569 0.4435 0.0043  0.1024  0.0359  4   HIS A CB  
25   C  CG  . HIS A 4   ? 0.5598 0.6026 0.6432 -0.0113 -0.1728 0.2680  4   HIS A CG  
26   N  ND1 . HIS A 4   ? 0.3939 0.4955 0.9829 -0.0357 -0.2973 -0.0895 4   HIS A ND1 
27   C  CD2 . HIS A 4   ? 0.3203 0.8820 1.0040 0.0228  -0.2446 -0.0469 4   HIS A CD2 
28   C  CE1 . HIS A 4   ? 0.7317 1.0296 1.2115 0.1849  -0.6782 0.1536  4   HIS A CE1 
29   N  NE2 . HIS A 4   ? 0.3003 1.6619 1.0190 -0.3203 -0.4009 -0.2518 4   HIS A NE2 
30   N  N   . TRP A 5   ? 0.1784 0.1962 0.3662 -0.0313 0.0768  0.0270  5   TRP A N   
31   C  CA  . TRP A 5   ? 0.1553 0.1473 0.2809 -0.0010 0.0703  0.0184  5   TRP A CA  
32   C  C   . TRP A 5   ? 0.1738 0.1757 0.3091 0.0161  0.1036  0.0076  5   TRP A C   
33   O  O   . TRP A 5   ? 0.2181 0.1680 0.3174 -0.0368 0.0916  0.0119  5   TRP A O   
34   C  CB  . TRP A 5   ? 0.1897 0.1435 0.3113 -0.0035 0.0749  -0.0397 5   TRP A CB  
35   C  CG  . TRP A 5   ? 0.1900 0.1372 0.2396 -0.0373 0.0930  0.0035  5   TRP A CG  
36   C  CD1 . TRP A 5   ? 0.2008 0.1647 0.2560 -0.0443 0.0544  0.0000  5   TRP A CD1 
37   C  CD2 . TRP A 5   ? 0.1371 0.1625 0.2182 0.0215  0.0625  -0.0153 5   TRP A CD2 
38   N  NE1 . TRP A 5   ? 0.2173 0.1670 0.2270 -0.0164 0.0619  0.0144  5   TRP A NE1 
39   C  CE2 . TRP A 5   ? 0.1425 0.1791 0.2128 0.0012  0.0308  -0.0189 5   TRP A CE2 
40   C  CE3 . TRP A 5   ? 0.1527 0.1699 0.2051 -0.0176 0.0595  -0.0454 5   TRP A CE3 
41   C  CZ2 . TRP A 5   ? 0.1692 0.2215 0.1746 0.0027  0.0328  -0.0304 5   TRP A CZ2 
42   C  CZ3 . TRP A 5   ? 0.1559 0.1690 0.2123 -0.0073 0.0472  -0.0737 5   TRP A CZ3 
43   C  CH2 . TRP A 5   ? 0.1509 0.2320 0.1811 -0.0122 0.0386  -0.0623 5   TRP A CH2 
44   N  N   . GLY A 6   ? 0.1697 0.1279 0.2691 0.0017  0.0957  -0.0346 6   GLY A N   
45   C  CA  . GLY A 6   ? 0.1843 0.1435 0.2673 -0.0346 0.0935  -0.0353 6   GLY A CA  
46   C  C   . GLY A 6   ? 0.1608 0.1460 0.2876 -0.0298 0.1324  -0.0383 6   GLY A C   
47   O  O   . GLY A 6   ? 0.1302 0.1580 0.2531 0.0038  0.0817  0.0038  6   GLY A O   
48   N  N   A TYR A 7   ? 0.2204 0.1092 0.3560 -0.0284 0.1761  -0.0740 7   TYR A N   
49   N  N   B TYR A 7   ? 0.2313 0.1482 0.4092 -0.0746 0.1414  -0.0811 7   TYR A N   
50   C  CA  A TYR A 7   ? 0.1543 0.0736 0.4729 -0.0454 0.1490  -0.0322 7   TYR A CA  
51   C  CA  B TYR A 7   ? 0.2599 0.1360 0.4368 -0.0076 0.1309  -0.0249 7   TYR A CA  
52   C  C   A TYR A 7   ? 0.2129 0.1182 0.7156 0.0013  0.1972  -0.0575 7   TYR A C   
53   C  C   B TYR A 7   ? 0.1977 0.1189 0.5645 -0.0666 0.1634  -0.0905 7   TYR A C   
54   O  O   A TYR A 7   ? 0.2342 0.1327 1.1252 -0.0093 0.2047  -0.0863 7   TYR A O   
55   O  O   B TYR A 7   ? 0.0582 0.1264 0.5927 -0.0366 0.0100  -0.0881 7   TYR A O   
56   C  CB  A TYR A 7   ? 0.1792 0.1092 0.3650 -0.0549 0.1492  -0.0722 7   TYR A CB  
57   C  CB  B TYR A 7   ? 0.2770 0.1247 0.3691 -0.0342 0.1398  -0.0520 7   TYR A CB  
58   C  CG  A TYR A 7   ? 0.1169 0.1178 0.2256 -0.0505 0.0754  -0.0649 7   TYR A CG  
59   C  CG  B TYR A 7   ? 0.1421 0.1185 0.2245 -0.0568 0.0511  -0.0472 7   TYR A CG  
60   C  CD1 A TYR A 7   ? 0.1097 0.1164 0.2254 -0.0518 0.0675  -0.0467 7   TYR A CD1 
61   C  CD1 B TYR A 7   ? 0.1191 0.1352 0.2290 -0.0265 0.0555  -0.0430 7   TYR A CD1 
62   C  CD2 A TYR A 7   ? 0.1900 0.0950 0.2254 -0.0428 0.0716  -0.0392 7   TYR A CD2 
63   C  CD2 B TYR A 7   ? 0.2035 0.0973 0.2558 -0.0324 0.0643  -0.0065 7   TYR A CD2 
64   C  CE1 A TYR A 7   ? 0.0957 0.1022 0.1758 -0.0392 0.0419  -0.0318 7   TYR A CE1 
65   C  CE1 B TYR A 7   ? 0.1283 0.1189 0.1618 -0.0204 0.0355  -0.0447 7   TYR A CE1 
66   C  CE2 A TYR A 7   ? 0.1570 0.1449 0.1390 -0.0511 0.0795  -0.0450 7   TYR A CE2 
67   C  CE2 B TYR A 7   ? 0.1762 0.1547 0.1665 -0.0399 0.0263  -0.0392 7   TYR A CE2 
68   C  CZ  A TYR A 7   ? 0.1038 0.1150 0.1297 -0.0544 0.0460  -0.0317 7   TYR A CZ  
69   C  CZ  B TYR A 7   ? 0.1413 0.1150 0.1748 -0.0379 0.0274  -0.0204 7   TYR A CZ  
70   O  OH  A TYR A 7   ? 0.1304 0.1083 0.1389 -0.0310 0.0432  -0.0238 7   TYR A OH  
71   O  OH  B TYR A 7   ? 0.1667 0.1579 0.1651 -0.0151 0.0335  -0.0406 7   TYR A OH  
72   N  N   A GLY A 8   ? 0.1927 0.1805 0.7418 -0.0247 0.1898  -0.1791 8   GLY A N   
73   N  N   B GLY A 8   ? 0.1870 0.1228 0.5691 -0.0456 0.1733  -0.0719 8   GLY A N   
74   C  CA  A GLY A 8   ? 0.1446 0.1317 0.5067 -0.0662 0.1147  -0.0870 8   GLY A CA  
75   C  CA  B GLY A 8   ? 0.0722 0.1841 0.4433 0.0031  0.0307  -0.0689 8   GLY A CA  
76   C  C   A GLY A 8   ? 0.1762 0.1791 0.4462 -0.0071 0.1729  -0.1125 8   GLY A C   
77   C  C   B GLY A 8   ? 0.2285 0.2354 0.3867 -0.0317 0.0395  -0.1002 8   GLY A C   
78   O  O   A GLY A 8   ? 0.1881 0.1841 0.5274 -0.0974 0.1770  -0.1436 8   GLY A O   
79   O  O   B GLY A 8   ? 0.2599 0.2197 0.5368 -0.0285 0.1577  -0.1974 8   GLY A O   
80   N  N   A LYS A 9   ? 0.1586 0.1759 0.4641 -0.0212 0.1160  -0.1592 9   LYS A N   
81   N  N   B LYS A 9   ? 0.2278 0.2091 0.4413 -0.0098 -0.0520 -0.0842 9   LYS A N   
82   C  CA  A LYS A 9   ? 0.2660 0.2662 0.6463 -0.0082 -0.0153 -0.1247 9   LYS A CA  
83   C  CA  B LYS A 9   ? 0.1798 0.3246 0.5422 -0.0819 -0.1852 -0.1649 9   LYS A CA  
84   C  C   A LYS A 9   ? 0.1713 0.3149 0.4771 -0.0377 0.0097  -0.0302 9   LYS A C   
85   C  C   B LYS A 9   ? 0.1383 0.3172 0.4239 -0.1259 -0.0454 -0.0489 9   LYS A C   
86   O  O   A LYS A 9   ? 0.1516 0.2579 0.4774 0.0405  0.1392  -0.0392 9   LYS A O   
87   O  O   B LYS A 9   ? 0.3118 0.3481 0.3944 -0.1819 -0.0263 -0.0688 9   LYS A O   
88   C  CB  A LYS A 9   ? 0.4660 0.0901 0.7157 -0.0697 0.0658  -0.0852 9   LYS A CB  
89   C  CB  B LYS A 9   ? 0.2144 0.3172 0.5957 -0.1084 0.0057  -0.0975 9   LYS A CB  
90   C  CG  A LYS A 9   ? 0.2994 0.3661 0.7973 -0.0996 0.1491  -0.2431 9   LYS A CG  
91   C  CG  B LYS A 9   ? 0.5052 0.2746 0.7986 -0.0732 0.1699  -0.0869 9   LYS A CG  
92   C  CD  A LYS A 9   ? 0.9708 0.3610 0.7110 0.0829  0.2277  -0.1748 9   LYS A CD  
93   C  CD  B LYS A 9   ? 0.7041 0.4356 1.0185 0.2281  0.1133  -0.1458 9   LYS A CD  
94   C  CE  A LYS A 9   ? 0.8432 0.7605 0.6244 0.0460  0.1976  -0.3185 9   LYS A CE  
95   C  CE  B LYS A 9   ? 0.7419 0.6352 1.0576 0.0711  0.0108  -0.1800 9   LYS A CE  
96   N  NZ  A LYS A 9   ? 1.0707 0.9704 0.2741 0.1934  0.1761  -0.1119 9   LYS A NZ  
97   N  NZ  B LYS A 9   ? 0.2989 1.4185 0.9884 0.2680  0.1207  -0.0656 9   LYS A NZ  
98   N  N   A HIS A 10  ? 0.2195 0.1389 0.5964 0.0844  0.1833  -0.0951 10  HIS A N   
99   N  N   B HIS A 10  ? 0.2130 0.2567 0.5106 -0.0197 0.1535  -0.0531 10  HIS A N   
100  C  CA  A HIS A 10  ? 0.3100 0.1873 0.5648 0.0087  0.2592  -0.0286 10  HIS A CA  
101  C  CA  B HIS A 10  ? 0.2773 0.1552 0.5511 0.0164  0.2676  -0.0167 10  HIS A CA  
102  C  C   A HIS A 10  ? 0.1951 0.1879 0.4607 0.0399  0.2211  0.0461  10  HIS A C   
103  C  C   B HIS A 10  ? 0.2130 0.1774 0.4356 0.0614  0.2090  0.0373  10  HIS A C   
104  O  O   A HIS A 10  ? 0.1577 0.2734 0.4861 0.0666  0.1033  0.1005  10  HIS A O   
105  O  O   B HIS A 10  ? 0.2545 0.2511 0.4738 0.0733  0.1704  -0.0267 10  HIS A O   
106  C  CB  A HIS A 10  ? 0.1986 0.1656 0.6610 0.0124  0.2878  -0.0153 10  HIS A CB  
107  C  CB  B HIS A 10  ? 0.3255 0.1870 0.5778 0.0138  0.3102  -0.0210 10  HIS A CB  
108  C  CG  A HIS A 10  ? 0.1376 0.2356 0.2691 0.0489  0.0505  -0.0121 10  HIS A CG  
109  C  CG  B HIS A 10  ? 0.1999 0.2870 0.3095 0.0531  -0.0027 0.0564  10  HIS A CG  
110  N  ND1 A HIS A 10  ? 0.0712 0.2590 0.4167 -0.0131 0.0059  -0.0443 10  HIS A ND1 
111  N  ND1 B HIS A 10  ? 0.2703 0.2450 0.3745 0.0815  -0.0936 -0.0747 10  HIS A ND1 
112  C  CD2 A HIS A 10  ? 0.1534 0.2186 0.3479 0.0192  0.1794  -0.0895 10  HIS A CD2 
113  C  CD2 B HIS A 10  ? 0.2215 0.2957 0.3741 -0.0693 0.1759  0.0668  10  HIS A CD2 
114  C  CE1 A HIS A 10  ? 0.3199 0.2651 0.2340 0.1280  -0.1146 -0.0125 10  HIS A CE1 
115  C  CE1 B HIS A 10  ? 0.2364 0.2788 0.3589 0.1474  -0.0055 -0.0597 10  HIS A CE1 
116  N  NE2 A HIS A 10  ? 0.0971 0.1864 0.2913 0.0138  0.0212  -0.0693 10  HIS A NE2 
117  N  NE2 B HIS A 10  ? 0.2407 0.2897 0.3106 -0.0161 0.0690  -0.0353 10  HIS A NE2 
118  N  N   . ASN A 11  ? 0.2139 0.1570 0.5181 0.0313  0.2305  0.0136  11  ASN A N   
119  C  CA  . ASN A 11  ? 0.1798 0.1640 0.4151 0.0414  0.1649  0.0046  11  ASN A CA  
120  C  C   . ASN A 11  ? 0.1719 0.1430 0.3434 0.0165  0.1348  0.0174  11  ASN A C   
121  O  O   . ASN A 11  ? 0.1738 0.1589 0.3601 0.0315  0.1352  0.0105  11  ASN A O   
122  C  CB  . ASN A 11  ? 0.1552 0.1697 0.3932 -0.0282 0.1535  -0.0491 11  ASN A CB  
123  C  CG  . ASN A 11  ? 0.1988 0.1719 0.3440 -0.0071 0.1564  -0.0353 11  ASN A CG  
124  O  OD1 . ASN A 11  ? 0.2338 0.1859 0.5077 -0.0208 0.1849  -0.0230 11  ASN A OD1 
125  N  ND2 . ASN A 11  ? 0.2416 0.2074 0.3558 -0.0456 0.1331  -0.0432 11  ASN A ND2 
126  N  N   . GLY A 12  ? 0.1466 0.1525 0.3763 0.0252  0.1304  0.0142  12  GLY A N   
127  C  CA  . GLY A 12  ? 0.1208 0.1922 0.3131 0.0274  0.1033  -0.0438 12  GLY A CA  
128  C  C   . GLY A 12  ? 0.1172 0.1120 0.3246 -0.0008 0.0675  0.0239  12  GLY A C   
129  O  O   . GLY A 12  ? 0.1009 0.1209 0.3662 0.0262  0.0597  0.0205  12  GLY A O   
130  N  N   . PRO A 13  ? 0.1203 0.1128 0.2869 0.0197  0.0847  -0.0104 13  PRO A N   
131  C  CA  . PRO A 13  ? 0.1036 0.1038 0.3212 0.0000  0.0546  -0.0092 13  PRO A CA  
132  C  C   . PRO A 13  ? 0.1536 0.0983 0.2563 0.0115  0.0648  -0.0153 13  PRO A C   
133  O  O   . PRO A 13  ? 0.0882 0.1489 0.2870 -0.0008 0.0518  -0.0372 13  PRO A O   
134  C  CB  . PRO A 13  ? 0.1214 0.1358 0.2691 -0.0234 0.0656  -0.0342 13  PRO A CB  
135  C  CG  . PRO A 13  ? 0.1360 0.1217 0.2614 -0.0066 0.0706  -0.0083 13  PRO A CG  
136  C  CD  . PRO A 13  ? 0.1065 0.1658 0.2894 0.0001  0.0829  -0.0165 13  PRO A CD  
137  N  N   . GLU A 14  ? 0.1257 0.1232 0.3194 0.0104  0.0639  -0.0113 14  GLU A N   
138  C  CA  . GLU A 14  ? 0.1643 0.1451 0.3115 0.0350  0.0542  0.0182  14  GLU A CA  
139  C  C   . GLU A 14  ? 0.0850 0.1552 0.3183 0.0373  0.0276  0.0093  14  GLU A C   
140  O  O   . GLU A 14  ? 0.1464 0.1466 0.3461 0.0405  0.0340  0.0410  14  GLU A O   
141  C  CB  . GLU A 14  ? 0.3195 0.1128 0.3671 -0.0063 0.0350  -0.0153 14  GLU A CB  
142  C  CG  . GLU A 14  ? 0.1926 0.3075 0.3776 0.0055  -0.0322 -0.0575 14  GLU A CG  
143  C  CD  . GLU A 14  ? 0.1817 0.4097 0.4029 0.0832  -0.0339 -0.0494 14  GLU A CD  
144  O  OE1 . GLU A 14  ? 0.2317 0.2362 0.3905 0.1270  -0.0557 -0.1271 14  GLU A OE1 
145  O  OE2 . GLU A 14  ? 1.5200 0.2531 0.7447 0.2563  0.5527  0.0077  14  GLU A OE2 
146  N  N   . HIS A 15  ? 0.0991 0.1239 0.3116 0.0155  0.0485  -0.0141 15  HIS A N   
147  C  CA  . HIS A 15  ? 0.0750 0.1216 0.3456 0.0287  0.0199  0.0089  15  HIS A CA  
148  C  C   . HIS A 15  ? 0.0678 0.1408 0.3212 0.0306  0.0366  -0.0027 15  HIS A C   
149  O  O   . HIS A 15  ? 0.0596 0.1532 0.3840 0.0239  0.0434  0.0335  15  HIS A O   
150  C  CB  . HIS A 15  ? 0.1076 0.1751 0.3567 0.0529  0.0588  0.0153  15  HIS A CB  
151  C  CG  . HIS A 15  ? 0.1234 0.1701 0.3377 0.0533  0.0566  0.0122  15  HIS A CG  
152  N  ND1 . HIS A 15  ? 0.1335 0.2493 0.3393 0.0861  0.0436  -0.0023 15  HIS A ND1 
153  C  CD2 . HIS A 15  ? 0.1661 0.1588 0.3449 0.0688  0.0617  0.0125  15  HIS A CD2 
154  C  CE1 . HIS A 15  ? 0.2240 0.3165 0.3219 0.1729  0.0467  0.0074  15  HIS A CE1 
155  N  NE2 . HIS A 15  ? 0.2768 0.2351 0.3998 0.1614  0.1089  0.0041  15  HIS A NE2 
156  N  N   . TRP A 16  ? 0.0706 0.1024 0.3043 0.0175  0.0285  0.0201  16  TRP A N   
157  C  CA  . TRP A 16  ? 0.0513 0.0948 0.3034 0.0165  0.0077  -0.0066 16  TRP A CA  
158  C  C   . TRP A 16  ? 0.0442 0.1261 0.2779 0.0240  -0.0006 0.0063  16  TRP A C   
159  O  O   . TRP A 16  ? 0.0694 0.1223 0.3134 0.0087  -0.0185 0.0087  16  TRP A O   
160  C  CB  . TRP A 16  ? 0.0517 0.1545 0.2535 0.0148  0.0115  -0.0243 16  TRP A CB  
161  C  CG  . TRP A 16  ? 0.0816 0.0894 0.2240 0.0076  0.0186  -0.0083 16  TRP A CG  
162  C  CD1 . TRP A 16  ? 0.1160 0.1370 0.2175 0.0110  0.0386  0.0318  16  TRP A CD1 
163  C  CD2 . TRP A 16  ? 0.0609 0.1038 0.2326 0.0217  0.0320  -0.0168 16  TRP A CD2 
164  N  NE1 . TRP A 16  ? 0.1006 0.1270 0.2416 0.0197  0.0636  -0.0226 16  TRP A NE1 
165  C  CE2 . TRP A 16  ? 0.0816 0.0939 0.2301 0.0119  0.0472  -0.0162 16  TRP A CE2 
166  C  CE3 . TRP A 16  ? 0.0600 0.1008 0.2366 0.0024  0.0399  0.0020  16  TRP A CE3 
167  C  CZ2 . TRP A 16  ? 0.0851 0.0995 0.2259 0.0013  0.0586  -0.0160 16  TRP A CZ2 
168  C  CZ3 . TRP A 16  ? 0.0656 0.1022 0.2426 0.0081  0.0502  -0.0254 16  TRP A CZ3 
169  C  CH2 . TRP A 16  ? 0.0847 0.0847 0.2306 0.0185  0.0496  -0.0192 16  TRP A CH2 
170  N  N   . HIS A 17  ? 0.0447 0.1568 0.2728 0.0200  -0.0057 -0.0024 17  HIS A N   
171  C  CA  . HIS A 17  ? 0.0630 0.1482 0.2615 0.0015  -0.0146 0.0231  17  HIS A CA  
172  C  C   . HIS A 17  ? 0.0807 0.1266 0.3282 0.0120  0.0093  0.0315  17  HIS A C   
173  O  O   . HIS A 17  ? 0.0668 0.1568 0.3366 0.0043  -0.0142 0.0152  17  HIS A O   
174  C  CB  . HIS A 17  ? 0.0481 0.1771 0.3001 0.0021  -0.0076 -0.0078 17  HIS A CB  
175  C  CG  . HIS A 17  ? 0.0549 0.1651 0.3619 -0.0005 0.0041  0.0425  17  HIS A CG  
176  N  ND1 . HIS A 17  ? 0.0459 0.2389 0.3689 0.0040  -0.0065 0.0447  17  HIS A ND1 
177  C  CD2 . HIS A 17  ? 0.1031 0.1719 0.3729 0.0401  0.0295  0.0579  17  HIS A CD2 
178  C  CE1 . HIS A 17  ? 0.0472 0.2425 0.3876 0.0339  0.0109  0.0414  17  HIS A CE1 
179  N  NE2 . HIS A 17  ? 0.0900 0.1891 0.3375 0.0137  0.0063  0.0644  17  HIS A NE2 
180  N  N   . LYS A 18  ? 0.0373 0.1676 0.3628 0.0057  0.0010  0.0383  18  LYS A N   
181  C  CA  . LYS A 18  ? 0.0529 0.2112 0.3389 -0.0063 -0.0007 0.0606  18  LYS A CA  
182  C  C   . LYS A 18  ? 0.0571 0.2004 0.3517 -0.0241 -0.0071 0.0456  18  LYS A C   
183  O  O   . LYS A 18  ? 0.1080 0.2249 0.5184 -0.0584 -0.0538 0.1014  18  LYS A O   
184  C  CB  . LYS A 18  ? 0.0785 0.1945 0.4038 0.0108  0.0287  0.0886  18  LYS A CB  
185  C  CG  . LYS A 18  ? 0.1138 0.1760 0.4499 0.0786  0.0478  0.0685  18  LYS A CG  
186  C  CD  . LYS A 18  ? 0.0698 0.2427 0.3740 0.0282  0.0140  0.0815  18  LYS A CD  
187  C  CE  . LYS A 18  ? 0.0950 0.2355 0.3377 0.0359  0.0196  0.0922  18  LYS A CE  
188  N  NZ  . LYS A 18  ? 0.0577 0.2802 0.3555 0.0878  0.0383  0.1052  18  LYS A NZ  
189  N  N   . ASP A 19  ? 0.0641 0.1720 0.3431 0.0026  -0.0043 0.0364  19  ASP A N   
190  C  CA  . ASP A 19  ? 0.0977 0.1565 0.3454 0.0148  0.0046  0.0601  19  ASP A CA  
191  C  C   . ASP A 19  ? 0.0680 0.1235 0.3758 0.0030  0.0153  0.0291  19  ASP A C   
192  O  O   . ASP A 19  ? 0.1105 0.1252 0.4201 -0.0177 0.0147  0.0390  19  ASP A O   
193  C  CB  . ASP A 19  ? 0.1164 0.2493 0.3713 0.0469  -0.0239 0.0085  19  ASP A CB  
194  C  CG  . ASP A 19  ? 0.1450 0.3772 0.3894 0.0763  0.0166  -0.0395 19  ASP A CG  
195  O  OD1 . ASP A 19  ? 0.1374 0.4454 0.4855 0.0248  0.0315  0.0715  19  ASP A OD1 
196  O  OD2 . ASP A 19  ? 0.2764 0.6787 0.5188 -0.0807 0.0566  -0.1370 19  ASP A OD2 
197  N  N   . PHE A 20  ? 0.0641 0.1489 0.3269 0.0066  -0.0007 0.0454  20  PHE A N   
198  C  CA  . PHE A 20  ? 0.0540 0.1604 0.3481 0.0034  0.0093  0.0311  20  PHE A CA  
199  C  C   . PHE A 20  ? 0.0450 0.1498 0.3244 -0.0027 0.0010  0.0176  20  PHE A C   
200  O  O   . PHE A 20  ? 0.0772 0.1189 0.2994 0.0013  0.0007  0.0116  20  PHE A O   
201  C  CB  . PHE A 20  ? 0.0601 0.1683 0.3061 -0.0088 0.0021  0.0242  20  PHE A CB  
202  C  CG  . PHE A 20  ? 0.0631 0.1913 0.3032 -0.0436 0.0087  0.0201  20  PHE A CG  
203  C  CD1 . PHE A 20  ? 0.1171 0.2164 0.3352 -0.0480 -0.0197 0.0445  20  PHE A CD1 
204  C  CD2 . PHE A 20  ? 0.0859 0.2462 0.3072 -0.0177 0.0231  0.0130  20  PHE A CD2 
205  C  CE1 . PHE A 20  ? 0.1232 0.2924 0.3314 -0.0348 -0.0182 0.0692  20  PHE A CE1 
206  C  CE2 . PHE A 20  ? 0.0775 0.3379 0.3312 0.0049  0.0329  0.0593  20  PHE A CE2 
207  C  CZ  . PHE A 20  ? 0.0961 0.3118 0.3337 -0.0496 -0.0059 0.0759  20  PHE A CZ  
208  N  N   . PRO A 21  ? 0.0807 0.1525 0.3316 -0.0183 -0.0074 0.0200  21  PRO A N   
209  C  CA  . PRO A 21  ? 0.0529 0.1965 0.2843 -0.0219 -0.0170 0.0003  21  PRO A CA  
210  C  C   . PRO A 21  ? 0.0984 0.1557 0.2888 -0.0031 -0.0287 -0.0187 21  PRO A C   
211  O  O   . PRO A 21  ? 0.0693 0.1848 0.2892 -0.0052 -0.0395 -0.0088 21  PRO A O   
212  C  CB  . PRO A 21  ? 0.1088 0.2980 0.3422 -0.0883 -0.0579 0.0445  21  PRO A CB  
213  C  CG  . PRO A 21  ? 0.3289 0.2736 0.4065 -0.1719 -0.1124 0.0428  21  PRO A CG  
214  C  CD  . PRO A 21  ? 0.0975 0.1845 0.3720 -0.0540 -0.0445 0.0441  21  PRO A CD  
215  N  N   A ILE A 22  ? 0.0716 0.1119 0.2919 -0.0342 -0.0395 -0.0298 22  ILE A N   
216  N  N   B ILE A 22  ? 0.0716 0.1228 0.3003 -0.0272 -0.0428 -0.0362 22  ILE A N   
217  C  CA  A ILE A 22  ? 0.0952 0.1090 0.2820 0.0057  -0.0283 -0.0229 22  ILE A CA  
218  C  CA  B ILE A 22  ? 0.0822 0.1225 0.2867 0.0043  -0.0443 -0.0282 22  ILE A CA  
219  C  C   A ILE A 22  ? 0.0694 0.1101 0.2338 -0.0074 -0.0293 -0.0201 22  ILE A C   
220  C  C   B ILE A 22  ? 0.0812 0.1142 0.2390 -0.0043 -0.0248 -0.0241 22  ILE A C   
221  O  O   A ILE A 22  ? 0.0643 0.1301 0.2493 0.0048  -0.0174 -0.0287 22  ILE A O   
222  O  O   B ILE A 22  ? 0.0749 0.1313 0.2504 0.0104  -0.0152 -0.0379 22  ILE A O   
223  C  CB  A ILE A 22  ? 0.0825 0.1101 0.2691 -0.0109 -0.0344 -0.0087 22  ILE A CB  
224  C  CB  B ILE A 22  ? 0.0898 0.1360 0.2682 0.0015  -0.0555 -0.0197 22  ILE A CB  
225  C  CG1 A ILE A 22  ? 0.1272 0.1151 0.2469 0.0007  -0.0412 -0.0727 22  ILE A CG1 
226  C  CG1 B ILE A 22  ? 0.1108 0.1870 0.2887 0.0707  -0.0432 -0.0265 22  ILE A CG1 
227  C  CG2 A ILE A 22  ? 0.0703 0.1477 0.2448 -0.0124 -0.0087 -0.0132 22  ILE A CG2 
228  C  CG2 B ILE A 22  ? 0.1160 0.1347 0.2594 -0.0276 -0.0641 -0.0110 22  ILE A CG2 
229  C  CD1 A ILE A 22  ? 0.1108 0.1404 0.2240 -0.0173 -0.0430 0.0102  22  ILE A CD1 
230  C  CD1 B ILE A 22  ? 0.2003 0.2412 0.2714 -0.0350 -0.0469 0.0397  22  ILE A CD1 
231  N  N   . ALA A 23  ? 0.0599 0.1176 0.2493 0.0000  -0.0364 -0.0175 23  ALA A N   
232  C  CA  . ALA A 23  ? 0.0790 0.1119 0.2407 0.0048  -0.0017 -0.0129 23  ALA A CA  
233  C  C   . ALA A 23  ? 0.0544 0.1230 0.2578 -0.0017 -0.0228 -0.0211 23  ALA A C   
234  O  O   . ALA A 23  ? 0.0687 0.1264 0.2396 -0.0037 -0.0041 -0.0131 23  ALA A O   
235  C  CB  . ALA A 23  ? 0.0517 0.1608 0.2685 0.0197  -0.0375 -0.0302 23  ALA A CB  
236  N  N   . LYS A 24  ? 0.0878 0.1482 0.2250 0.0037  -0.0331 -0.0116 24  LYS A N   
237  C  CA  . LYS A 24  ? 0.0767 0.1753 0.2558 0.0104  -0.0216 -0.0135 24  LYS A CA  
238  C  C   . LYS A 24  ? 0.1099 0.1936 0.2484 -0.0203 -0.0428 -0.0198 24  LYS A C   
239  O  O   . LYS A 24  ? 0.1250 0.2569 0.2680 0.0049  -0.0634 -0.0315 24  LYS A O   
240  C  CB  . LYS A 24  ? 0.0864 0.1775 0.2951 0.0153  -0.0403 0.0105  24  LYS A CB  
241  C  CG  . LYS A 24  ? 0.1365 0.2360 0.2741 0.0676  -0.0154 0.0260  24  LYS A CG  
242  C  CD  . LYS A 24  ? 0.1225 0.3668 0.3971 0.0940  0.0144  0.0397  24  LYS A CD  
243  C  CE  . LYS A 24  ? 0.1554 0.3330 0.3955 0.0674  0.0147  0.0829  24  LYS A CE  
244  N  NZ  . LYS A 24  ? 0.2958 0.3472 0.5575 -0.1028 0.0964  -0.0581 24  LYS A NZ  
245  N  N   . GLY A 25  ? 0.1013 0.1650 0.2619 0.0137  -0.0362 -0.0390 25  GLY A N   
246  C  CA  . GLY A 25  ? 0.1272 0.1710 0.2597 -0.0366 -0.0287 -0.0586 25  GLY A CA  
247  C  C   . GLY A 25  ? 0.1218 0.1773 0.2012 0.0144  -0.0423 -0.0500 25  GLY A C   
248  O  O   . GLY A 25  ? 0.1259 0.2026 0.2114 0.0093  -0.0623 -0.0306 25  GLY A O   
249  N  N   . GLU A 26  ? 0.0977 0.2374 0.1947 0.0143  -0.0564 -0.0631 26  GLU A N   
250  C  CA  . GLU A 26  ? 0.1514 0.2326 0.1749 0.0104  -0.0524 -0.0474 26  GLU A CA  
251  C  C   . GLU A 26  ? 0.1306 0.1695 0.1466 0.0328  -0.0527 -0.0361 26  GLU A C   
252  O  O   . GLU A 26  ? 0.1807 0.1987 0.1378 0.0137  -0.0586 -0.0161 26  GLU A O   
253  C  CB  . GLU A 26  ? 0.1739 0.3064 0.2069 -0.0087 -0.0741 -0.1224 26  GLU A CB  
254  C  CG  . GLU A 26  ? 0.1807 0.3547 0.2324 -0.0010 -0.0905 -0.0839 26  GLU A CG  
255  C  CD  . GLU A 26  ? 0.2684 0.4329 0.3169 -0.0093 -0.1617 -0.0688 26  GLU A CD  
256  O  OE1 . GLU A 26  ? 0.3849 0.5004 0.4442 -0.1118 -0.1474 -0.0187 26  GLU A OE1 
257  O  OE2 . GLU A 26  ? 0.3001 0.4395 0.4832 0.0864  -0.1120 -0.0390 26  GLU A OE2 
258  N  N   . ARG A 27  ? 0.1151 0.1070 0.1495 0.0142  -0.0480 -0.0344 27  ARG A N   
259  C  CA  . ARG A 27  ? 0.0812 0.1264 0.1380 0.0362  -0.0478 -0.0447 27  ARG A CA  
260  C  C   . ARG A 27  ? 0.0851 0.1029 0.1315 0.0109  -0.0288 -0.0329 27  ARG A C   
261  O  O   . ARG A 27  ? 0.0882 0.1092 0.1367 0.0230  -0.0355 -0.0216 27  ARG A O   
262  C  CB  . ARG A 27  ? 0.1525 0.1419 0.1720 0.0324  -0.0524 -0.0599 27  ARG A CB  
263  C  CG  . ARG A 27  ? 0.2220 0.1958 0.2148 0.0275  -0.0399 -0.0226 27  ARG A CG  
264  C  CD  . ARG A 27  ? 0.2928 0.3140 0.1959 0.1441  -0.0546 0.0055  27  ARG A CD  
265  N  NE  . ARG A 27  ? 0.2193 0.1649 0.1884 0.0000  0.0129  -0.0105 27  ARG A NE  
266  C  CZ  . ARG A 27  ? 0.1555 0.2130 0.1387 0.0087  -0.0208 -0.0035 27  ARG A CZ  
267  N  NH1 . ARG A 27  ? 0.1601 0.2621 0.1992 0.0287  -0.0020 -0.1176 27  ARG A NH1 
268  N  NH2 . ARG A 27  ? 0.1606 0.1595 0.1891 -0.0348 -0.0183 -0.0207 27  ARG A NH2 
269  N  N   . GLN A 28  ? 0.0905 0.0847 0.1311 0.0055  -0.0313 -0.0204 28  GLN A N   
270  C  CA  . GLN A 28  ? 0.0504 0.0989 0.1388 0.0023  -0.0309 -0.0300 28  GLN A CA  
271  C  C   . GLN A 28  ? 0.0544 0.0904 0.1371 0.0012  -0.0166 -0.0147 28  GLN A C   
272  O  O   . GLN A 28  ? 0.0961 0.1088 0.1172 0.0015  -0.0203 -0.0149 28  GLN A O   
273  C  CB  . GLN A 28  ? 0.0452 0.1169 0.1723 -0.0071 -0.0255 -0.0252 28  GLN A CB  
274  C  CG  . GLN A 28  ? 0.0544 0.1207 0.1897 -0.0076 -0.0239 -0.0254 28  GLN A CG  
275  C  CD  . GLN A 28  ? 0.0485 0.1002 0.1583 -0.0063 -0.0297 -0.0294 28  GLN A CD  
276  O  OE1 . GLN A 28  ? 0.0768 0.0938 0.1609 -0.0083 -0.0104 -0.0366 28  GLN A OE1 
277  N  NE2 . GLN A 28  ? 0.0608 0.0970 0.1848 0.0020  -0.0214 -0.0406 28  GLN A NE2 
278  N  N   . SER A 29  ? 0.0581 0.0839 0.1259 0.0161  -0.0317 -0.0137 29  SER A N   
279  C  CA  . SER A 29  ? 0.0469 0.0820 0.1288 0.0156  -0.0217 -0.0222 29  SER A CA  
280  C  C   . SER A 29  ? 0.0599 0.0649 0.1093 0.0198  -0.0096 -0.0132 29  SER A C   
281  O  O   . SER A 29  ? 0.0656 0.0776 0.1295 0.0031  -0.0035 -0.0232 29  SER A O   
282  C  CB  . SER A 29  ? 0.0579 0.0806 0.1259 0.0153  -0.0207 -0.0194 29  SER A CB  
283  O  OG  . SER A 29  ? 0.0710 0.0751 0.1133 0.0076  -0.0085 -0.0199 29  SER A OG  
284  N  N   . PRO A 30  ? 0.0586 0.0736 0.1144 0.0177  -0.0156 -0.0120 30  PRO A N   
285  C  CA  . PRO A 30  ? 0.0744 0.0737 0.1076 0.0068  -0.0103 -0.0035 30  PRO A CA  
286  C  C   . PRO A 30  ? 0.0649 0.0654 0.1050 0.0155  -0.0126 -0.0185 30  PRO A C   
287  O  O   . PRO A 30  ? 0.0759 0.0797 0.1259 0.0175  -0.0190 -0.0115 30  PRO A O   
288  C  CB  . PRO A 30  ? 0.0628 0.0760 0.1200 0.0122  -0.0118 -0.0245 30  PRO A CB  
289  C  CG  . PRO A 30  ? 0.0683 0.0844 0.1270 0.0041  0.0013  -0.0089 30  PRO A CG  
290  C  CD  . PRO A 30  ? 0.0905 0.0653 0.1203 -0.0017 -0.0040 -0.0317 30  PRO A CD  
291  N  N   . VAL A 31  ? 0.0847 0.0737 0.1092 0.0137  -0.0024 -0.0003 31  VAL A N   
292  C  CA  . VAL A 31  ? 0.1033 0.0732 0.1002 0.0088  -0.0082 0.0087  31  VAL A CA  
293  C  C   . VAL A 31  ? 0.0837 0.0745 0.1208 0.0131  -0.0179 0.0052  31  VAL A C   
294  O  O   . VAL A 31  ? 0.0998 0.0895 0.1238 0.0138  -0.0183 0.0147  31  VAL A O   
295  C  CB  . VAL A 31  ? 0.1239 0.0760 0.1189 0.0110  -0.0205 -0.0085 31  VAL A CB  
296  C  CG1 . VAL A 31  ? 0.1282 0.0776 0.1435 0.0062  -0.0120 -0.0118 31  VAL A CG1 
297  C  CG2 . VAL A 31  ? 0.1058 0.0962 0.1437 0.0093  -0.0068 0.0108  31  VAL A CG2 
298  N  N   . ASP A 32  ? 0.1036 0.0597 0.1181 0.0043  -0.0244 0.0052  32  ASP A N   
299  C  CA  . ASP A 32  ? 0.1180 0.0640 0.1083 0.0118  -0.0028 0.0094  32  ASP A CA  
300  C  C   . ASP A 32  ? 0.1169 0.0860 0.1045 0.0094  -0.0207 0.0160  32  ASP A C   
301  O  O   . ASP A 32  ? 0.1230 0.1315 0.1385 0.0162  -0.0263 -0.0205 32  ASP A O   
302  C  CB  . ASP A 32  ? 0.1695 0.0715 0.1286 0.0194  -0.0243 0.0182  32  ASP A CB  
303  C  CG  . ASP A 32  ? 0.1181 0.1013 0.1298 0.0249  -0.0208 0.0026  32  ASP A CG  
304  O  OD1 . ASP A 32  ? 0.1250 0.0855 0.1444 0.0175  -0.0305 0.0113  32  ASP A OD1 
305  O  OD2 . ASP A 32  ? 0.2186 0.1112 0.1428 -0.0297 -0.0386 0.0220  32  ASP A OD2 
306  N  N   . ILE A 33  ? 0.1026 0.0964 0.1114 0.0161  -0.0087 0.0076  33  ILE A N   
307  C  CA  . ILE A 33  ? 0.1196 0.0914 0.1098 0.0155  -0.0040 0.0010  33  ILE A CA  
308  C  C   . ILE A 33  ? 0.1365 0.0764 0.1205 0.0142  0.0026  -0.0043 33  ILE A C   
309  O  O   . ILE A 33  ? 0.1457 0.0887 0.1282 0.0126  0.0071  0.0043  33  ILE A O   
310  C  CB  . ILE A 33  ? 0.1017 0.0945 0.1313 0.0157  -0.0094 0.0062  33  ILE A CB  
311  C  CG1 . ILE A 33  ? 0.1165 0.0832 0.1458 0.0238  -0.0269 0.0149  33  ILE A CG1 
312  C  CG2 . ILE A 33  ? 0.1246 0.1218 0.1767 0.0198  0.0252  0.0111  33  ILE A CG2 
313  C  CD1 . ILE A 33  ? 0.1040 0.1140 0.1491 0.0013  -0.0206 0.0200  33  ILE A CD1 
314  N  N   A ASP A 34  ? 0.1667 0.1194 0.1137 0.0238  0.0006  0.0104  34  ASP A N   
315  N  N   B ASP A 34  ? 0.1720 0.1103 0.1111 0.0269  0.0019  0.0147  34  ASP A N   
316  C  CA  A ASP A 34  ? 0.2090 0.1390 0.1207 0.0368  0.0197  0.0259  34  ASP A CA  
317  C  CA  B ASP A 34  ? 0.2107 0.1333 0.1054 0.0344  0.0038  0.0297  34  ASP A CA  
318  C  C   A ASP A 34  ? 0.2311 0.1331 0.1205 0.0392  0.0307  0.0326  34  ASP A C   
319  C  C   B ASP A 34  ? 0.2398 0.1230 0.1076 0.0390  0.0269  0.0416  34  ASP A C   
320  O  O   A ASP A 34  ? 0.2466 0.1741 0.1221 0.0741  0.0324  0.0120  34  ASP A O   
321  O  O   B ASP A 34  ? 0.2809 0.1789 0.1291 0.0557  0.0237  -0.0034 34  ASP A O   
322  C  CB  A ASP A 34  ? 0.2536 0.1537 0.1306 0.0652  0.0089  0.0129  34  ASP A CB  
323  C  CB  B ASP A 34  ? 0.2630 0.1241 0.1349 0.0074  -0.0263 0.0280  34  ASP A CB  
324  C  CG  A ASP A 34  ? 0.2565 0.1787 0.2487 0.0230  0.0452  0.0445  34  ASP A CG  
325  C  CG  B ASP A 34  ? 0.3003 0.1931 0.1272 -0.0020 -0.0245 0.0474  34  ASP A CG  
326  O  OD1 A ASP A 34  ? 0.3892 0.1173 0.1826 0.0362  0.0593  0.0410  34  ASP A OD1 
327  O  OD1 B ASP A 34  ? 0.2574 0.3131 0.1464 0.0661  0.0100  0.0979  34  ASP A OD1 
328  O  OD2 A ASP A 34  ? 0.3729 0.2026 0.2308 0.1099  0.0104  0.0582  34  ASP A OD2 
329  O  OD2 B ASP A 34  ? 0.3197 0.2732 0.1608 0.0584  -0.0172 0.0988  34  ASP A OD2 
330  N  N   . THR A 35  ? 0.2240 0.1469 0.1408 0.0377  0.0160  0.0423  35  THR A N   
331  C  CA  . THR A 35  ? 0.2389 0.1811 0.1428 0.0694  0.0401  0.0276  35  THR A CA  
332  C  C   . THR A 35  ? 0.2205 0.1394 0.1407 0.0584  0.0432  0.0209  35  THR A C   
333  O  O   . THR A 35  ? 0.2924 0.1776 0.1832 0.0895  0.0803  0.0467  35  THR A O   
334  C  CB  . THR A 35  ? 0.2064 0.1687 0.1866 0.0595  0.0395  0.0502  35  THR A CB  
335  O  OG1 . THR A 35  ? 0.2216 0.1890 0.1844 0.0226  0.0359  0.0333  35  THR A OG1 
336  C  CG2 . THR A 35  ? 0.2414 0.2606 0.1755 0.0593  0.0326  0.0619  35  THR A CG2 
337  N  N   . HIS A 36  ? 0.2989 0.1504 0.1349 0.0621  0.0493  0.0368  36  HIS A N   
338  C  CA  . HIS A 36  ? 0.3512 0.1561 0.1513 0.0410  0.0582  0.0480  36  HIS A CA  
339  C  C   . HIS A 36  ? 0.4142 0.2193 0.1164 0.0516  0.0472  0.0157  36  HIS A C   
340  O  O   . HIS A 36  ? 0.3111 0.3641 0.1692 0.1307  0.0083  0.0406  36  HIS A O   
341  C  CB  . HIS A 36  ? 0.4429 0.1997 0.1593 0.0526  0.0174  0.0715  36  HIS A CB  
342  C  CG  . HIS A 36  ? 0.4657 0.1480 0.2231 0.0493  -0.0463 0.0676  36  HIS A CG  
343  N  ND1 . HIS A 36  ? 0.6369 0.2344 0.2372 0.1367  -0.0885 0.0837  36  HIS A ND1 
344  C  CD2 . HIS A 36  ? 0.4774 0.2531 0.1944 -0.0496 -0.1005 0.0421  36  HIS A CD2 
345  C  CE1 . HIS A 36  ? 0.7779 0.2096 0.2818 0.1333  -0.0851 0.0049  36  HIS A CE1 
346  N  NE2 . HIS A 36  ? 0.5940 0.2842 0.2971 -0.0630 -0.1949 0.0256  36  HIS A NE2 
347  N  N   . THR A 37  ? 0.3547 0.1553 0.1914 0.0986  0.0661  0.0348  37  THR A N   
348  C  CA  . THR A 37  ? 0.3901 0.1676 0.1706 0.1218  0.0294  0.0471  37  THR A CA  
349  C  C   . THR A 37  ? 0.2687 0.1999 0.1484 0.0855  0.0361  0.0230  37  THR A C   
350  O  O   . THR A 37  ? 0.3713 0.2197 0.1755 0.1093  -0.0286 -0.0147 37  THR A O   
351  C  CB  . THR A 37  ? 0.4207 0.3242 0.2975 0.2083  0.0412  0.0480  37  THR A CB  
352  O  OG1 . THR A 37  ? 0.5042 0.2763 0.3032 0.1926  0.0234  0.0575  37  THR A OG1 
353  C  CG2 . THR A 37  ? 0.3476 0.1974 0.5109 0.0668  -0.0749 0.0529  37  THR A CG2 
354  N  N   . ALA A 38  ? 0.2833 0.1622 0.1241 0.0683  0.0297  0.0339  38  ALA A N   
355  C  CA  . ALA A 38  ? 0.2849 0.1586 0.1254 0.0733  0.0373  0.0333  38  ALA A CA  
356  C  C   . ALA A 38  ? 0.3154 0.1358 0.2229 0.0608  0.0689  0.0615  38  ALA A C   
357  O  O   . ALA A 38  ? 0.3955 0.1859 0.3544 0.0362  0.1785  0.0416  38  ALA A O   
358  C  CB  . ALA A 38  ? 0.2673 0.1425 0.1516 0.0274  -0.0148 0.0264  38  ALA A CB  
359  N  N   . LYS A 39  ? 0.2576 0.2071 0.1778 0.1076  -0.0006 -0.0108 39  LYS A N   
360  C  CA  . LYS A 39  ? 0.2565 0.3731 0.1712 0.1551  -0.0206 -0.0408 39  LYS A CA  
361  C  C   . LYS A 39  ? 0.2374 0.2284 0.1483 0.0908  0.0223  0.0005  39  LYS A C   
362  O  O   . LYS A 39  ? 0.2190 0.2205 0.1297 0.0549  -0.0083 -0.0059 39  LYS A O   
363  C  CB  . LYS A 39  ? 0.2752 0.4625 0.2694 0.1520  -0.1419 -0.0926 39  LYS A CB  
364  C  CG  . LYS A 39  ? 0.3648 0.4526 0.2574 0.0623  0.0103  0.0225  39  LYS A CG  
365  C  CD  . LYS A 39  ? 0.2576 0.5787 0.3795 0.2340  0.0494  0.1678  39  LYS A CD  
366  C  CE  . LYS A 39  ? 0.3208 0.5005 0.2777 0.0275  -0.0324 0.0939  39  LYS A CE  
367  N  NZ  . LYS A 39  ? 0.2515 0.5946 0.3476 0.1436  0.0597  0.2172  39  LYS A NZ  
368  N  N   . TYR A 40  ? 0.2930 0.2560 0.1416 0.0121  0.0020  0.0144  40  TYR A N   
369  C  CA  . TYR A 40  ? 0.2664 0.2029 0.1343 0.0124  0.0709  0.0097  40  TYR A CA  
370  C  C   . TYR A 40  ? 0.1807 0.2380 0.1298 -0.0126 0.0000  -0.0013 40  TYR A C   
371  O  O   . TYR A 40  ? 0.2089 0.3237 0.1324 0.0465  0.0129  -0.0153 40  TYR A O   
372  C  CB  . TYR A 40  ? 0.3303 0.2937 0.1625 -0.0608 0.0838  0.0306  40  TYR A CB  
373  C  CG  . TYR A 40  ? 0.3219 0.3522 0.2150 -0.0813 0.1155  -0.0105 40  TYR A CG  
374  C  CD1 . TYR A 40  ? 0.2992 0.2743 0.2256 -0.0692 0.0896  -0.0335 40  TYR A CD1 
375  C  CD2 . TYR A 40  ? 0.3043 0.5206 0.2371 -0.0081 0.0983  -0.0447 40  TYR A CD2 
376  C  CE1 . TYR A 40  ? 0.2865 0.4765 0.2139 -0.0291 0.0846  -0.0702 40  TYR A CE1 
377  C  CE2 . TYR A 40  ? 0.2669 0.5756 0.2306 -0.0034 0.1176  -0.0432 40  TYR A CE2 
378  C  CZ  . TYR A 40  ? 0.1931 0.6236 0.2333 -0.0614 0.0584  -0.0430 40  TYR A CZ  
379  O  OH  . TYR A 40  ? 0.2037 0.8176 0.3643 0.0137  0.0725  -0.1253 40  TYR A OH  
380  N  N   . ASP A 41  ? 0.1729 0.2028 0.1446 0.0148  0.0372  -0.0082 41  ASP A N   
381  C  CA  . ASP A 41  ? 0.1694 0.1877 0.1595 -0.0137 0.0000  -0.0077 41  ASP A CA  
382  C  C   . ASP A 41  ? 0.1723 0.2538 0.1764 0.0071  0.0148  -0.0377 41  ASP A C   
383  O  O   . ASP A 41  ? 0.1699 0.2653 0.1819 0.0136  0.0041  -0.0124 41  ASP A O   
384  C  CB  . ASP A 41  ? 0.1836 0.2202 0.2222 -0.0357 -0.0023 -0.0348 41  ASP A CB  
385  C  CG  . ASP A 41  ? 0.2242 0.2346 0.2648 -0.0493 0.0118  -0.0456 41  ASP A CG  
386  O  OD1 . ASP A 41  ? 0.2410 0.2748 0.2569 -0.0024 -0.0027 -0.0617 41  ASP A OD1 
387  O  OD2 . ASP A 41  ? 0.2399 0.3118 0.2861 -0.0606 -0.0105 -0.0049 41  ASP A OD2 
388  N  N   . PRO A 42  ? 0.1834 0.3980 0.1861 0.0524  0.0227  -0.0350 42  PRO A N   
389  C  CA  . PRO A 42  ? 0.2213 0.4330 0.2531 0.0863  0.0529  0.0661  42  PRO A CA  
390  C  C   . PRO A 42  ? 0.2685 0.3910 0.2207 0.1098  0.0586  0.0269  42  PRO A C   
391  O  O   . PRO A 42  ? 0.2858 0.5717 0.3533 0.1878  0.0826  0.0331  42  PRO A O   
392  C  CB  . PRO A 42  ? 0.3152 0.7193 0.2457 0.1477  0.1061  0.0406  42  PRO A CB  
393  C  CG  . PRO A 42  ? 0.2788 0.5221 0.2293 0.0869  0.1048  -0.0054 42  PRO A CG  
394  C  CD  . PRO A 42  ? 0.2383 0.3262 0.1985 0.0483  0.0771  0.0099  42  PRO A CD  
395  N  N   . SER A 43  ? 0.2518 0.3531 0.2278 0.1118  0.0001  -0.0496 43  SER A N   
396  C  CA  . SER A 43  ? 0.2939 0.3185 0.2736 0.0759  -0.0119 -0.0625 43  SER A CA  
397  C  C   . SER A 43  ? 0.2824 0.2804 0.2441 0.0797  0.0211  -0.0269 43  SER A C   
398  O  O   . SER A 43  ? 0.4850 0.2872 0.3535 0.1543  -0.0179 -0.0003 43  SER A O   
399  C  CB  . SER A 43  ? 0.2714 0.3222 0.3693 -0.0553 0.0511  -0.0370 43  SER A CB  
400  O  OG  . SER A 43  ? 0.3935 0.3064 0.3287 -0.0329 -0.0027 -0.0877 43  SER A OG  
401  N  N   . LEU A 44  ? 0.3350 0.3226 0.1934 0.0873  -0.0034 -0.0733 44  LEU A N   
402  C  CA  . LEU A 44  ? 0.2231 0.2933 0.1914 0.0945  -0.0076 0.0074  44  LEU A CA  
403  C  C   . LEU A 44  ? 0.1640 0.3328 0.2903 0.1009  0.0233  0.0467  44  LEU A C   
404  O  O   . LEU A 44  ? 0.1821 0.4593 0.3504 -0.0179 -0.0140 0.1053  44  LEU A O   
405  C  CB  . LEU A 44  ? 0.1764 0.2457 0.2048 0.0297  0.0230  -0.0182 44  LEU A CB  
406  C  CG  . LEU A 44  ? 0.1829 0.2168 0.1651 0.0070  -0.0221 0.0197  44  LEU A CG  
407  C  CD1 . LEU A 44  ? 0.1956 0.2515 0.1862 0.0137  0.0192  -0.0438 44  LEU A CD1 
408  C  CD2 . LEU A 44  ? 0.2435 0.1875 0.2178 -0.0199 0.0052  0.0104  44  LEU A CD2 
409  N  N   . LYS A 45  ? 0.1938 0.2732 0.2858 0.0362  -0.0320 0.0379  45  LYS A N   
410  C  CA  . LYS A 45  ? 0.1996 0.2308 0.2870 0.0469  -0.0527 -0.0366 45  LYS A CA  
411  C  C   . LYS A 45  ? 0.1647 0.2924 0.2414 0.0953  0.0015  0.0143  45  LYS A C   
412  O  O   . LYS A 45  ? 0.1422 0.2563 0.2973 0.0342  0.0051  -0.0300 45  LYS A O   
413  C  CB  . LYS A 45  ? 0.2703 0.2299 0.2863 0.1133  -0.0355 -0.0093 45  LYS A CB  
414  C  CG  . LYS A 45  ? 0.3388 0.3819 0.3702 -0.0164 -0.0710 -0.0807 45  LYS A CG  
415  C  CD  . LYS A 45  ? 0.5805 0.4237 0.4893 -0.0926 -0.1430 -0.0654 45  LYS A CD  
416  C  CE  . LYS A 45  ? 0.6633 0.5230 0.6593 0.0237  -0.0027 -0.1295 45  LYS A CE  
417  N  NZ  . LYS A 45  ? 0.7105 0.7706 0.6840 -0.0318 -0.1182 -0.1298 45  LYS A NZ  
418  N  N   . PRO A 46  ? 0.1354 0.2723 0.2727 -0.0135 0.0000  0.0210  46  PRO A N   
419  C  CA  . PRO A 46  ? 0.1413 0.3368 0.2402 -0.0204 0.0034  0.0449  46  PRO A CA  
420  C  C   . PRO A 46  ? 0.1449 0.1601 0.2195 -0.0017 0.0302  0.0154  46  PRO A C   
421  O  O   . PRO A 46  ? 0.0697 0.2371 0.2626 -0.0115 -0.0156 -0.0046 46  PRO A O   
422  C  CB  . PRO A 46  ? 0.1324 0.2707 0.2452 -0.0362 0.0080  0.0131  46  PRO A CB  
423  C  CG  . PRO A 46  ? 0.1326 0.3955 0.2964 -0.0172 0.0031  -0.0326 46  PRO A CG  
424  C  CD  . PRO A 46  ? 0.1467 0.3485 0.2879 0.0127  0.0091  -0.0635 46  PRO A CD  
425  N  N   A LEU A 47  ? 0.1446 0.1907 0.2436 0.0043  -0.0043 0.0065  47  LEU A N   
426  N  N   B LEU A 47  ? 0.1448 0.1920 0.2439 0.0037  -0.0037 0.0065  47  LEU A N   
427  C  CA  A LEU A 47  ? 0.0706 0.2177 0.2504 0.0015  0.0060  0.0137  47  LEU A CA  
428  C  CA  B LEU A 47  ? 0.0715 0.2182 0.2500 0.0021  0.0065  0.0130  47  LEU A CA  
429  C  C   A LEU A 47  ? 0.0344 0.2506 0.3497 -0.0226 -0.0173 0.0782  47  LEU A C   
430  C  C   B LEU A 47  ? 0.0353 0.2511 0.3497 -0.0225 -0.0175 0.0777  47  LEU A C   
431  O  O   A LEU A 47  ? 0.0808 0.2461 0.4345 -0.0405 -0.0762 0.1165  47  LEU A O   
432  O  O   B LEU A 47  ? 0.0820 0.2462 0.4345 -0.0403 -0.0760 0.1156  47  LEU A O   
433  C  CB  A LEU A 47  ? 0.1861 0.2182 0.2955 0.0632  0.0192  0.0342  47  LEU A CB  
434  C  CB  B LEU A 47  ? 0.1875 0.2190 0.2937 0.0573  0.0232  0.0346  47  LEU A CB  
435  C  CG  A LEU A 47  ? 0.1992 0.2477 0.3526 -0.0329 0.0286  -0.0419 47  LEU A CG  
436  C  CG  B LEU A 47  ? 0.1150 0.1977 0.2883 -0.0469 -0.0087 -0.0474 47  LEU A CG  
437  C  CD1 A LEU A 47  ? 0.1780 0.2504 0.4230 0.0198  0.0384  -0.0776 47  LEU A CD1 
438  C  CD1 B LEU A 47  ? 0.0941 0.1812 0.3702 -0.0267 0.0203  -0.0559 47  LEU A CD1 
439  C  CD2 A LEU A 47  ? 0.1658 0.2196 0.4111 -0.0287 0.0054  -0.0100 47  LEU A CD2 
440  C  CD2 B LEU A 47  ? 0.0914 0.2146 0.3991 -0.0443 -0.0153 -0.0961 47  LEU A CD2 
441  N  N   . SER A 48  ? 0.0941 0.2017 0.2412 -0.0200 0.0038  0.0595  48  SER A N   
442  C  CA  . SER A 48  ? 0.0925 0.1996 0.2270 -0.0054 -0.0133 0.0307  48  SER A CA  
443  C  C   . SER A 48  ? 0.0760 0.2008 0.2274 -0.0130 -0.0071 0.0041  48  SER A C   
444  O  O   . SER A 48  ? 0.0922 0.1868 0.2295 -0.0205 0.0057  -0.0131 48  SER A O   
445  C  CB  . SER A 48  ? 0.1712 0.2039 0.2576 -0.0110 -0.0066 0.0381  48  SER A CB  
446  O  OG  . SER A 48  ? 0.1708 0.2335 0.2996 0.0264  0.0359  0.0579  48  SER A OG  
447  N  N   . VAL A 49  ? 0.1485 0.1678 0.2547 -0.0568 -0.0109 0.0231  49  VAL A N   
448  C  CA  . VAL A 49  ? 0.1243 0.1960 0.2637 -0.0557 -0.0209 -0.0055 49  VAL A CA  
449  C  C   . VAL A 49  ? 0.1493 0.2299 0.3093 -0.0931 -0.0452 -0.0024 49  VAL A C   
450  O  O   . VAL A 49  ? 0.1595 0.3226 0.3598 -0.1253 -0.0700 0.0111  49  VAL A O   
451  C  CB  . VAL A 49  ? 0.3249 0.1949 0.2116 -0.0895 0.0460  -0.0091 49  VAL A CB  
452  C  CG1 . VAL A 49  ? 0.3944 0.2673 0.2490 -0.0895 0.0795  -0.0120 49  VAL A CG1 
453  C  CG2 . VAL A 49  ? 0.2196 0.2236 0.3195 -0.0469 0.0564  0.0254  49  VAL A CG2 
454  N  N   . SER A 50  ? 0.1554 0.2426 0.2680 -0.0676 -0.0496 -0.0020 50  SER A N   
455  C  CA  . SER A 50  ? 0.1376 0.3219 0.3533 -0.0070 -0.0350 0.0037  50  SER A CA  
456  C  C   . SER A 50  ? 0.1015 0.2781 0.3125 -0.0307 -0.0976 0.0037  50  SER A C   
457  O  O   . SER A 50  ? 0.1828 0.2486 0.2892 -0.0621 -0.0727 0.0359  50  SER A O   
458  C  CB  . SER A 50  ? 0.1983 0.2985 0.4550 -0.0456 0.0599  0.0296  50  SER A CB  
459  O  OG  . SER A 50  ? 0.1872 0.3896 0.4772 0.0034  -0.0060 -0.0192 50  SER A OG  
460  N  N   . TYR A 51  ? 0.1407 0.2366 0.2806 -0.0518 -0.0821 0.0219  51  TYR A N   
461  C  CA  . TYR A 51  ? 0.1528 0.2069 0.2734 -0.0043 -0.0725 0.0176  51  TYR A CA  
462  C  C   . TYR A 51  ? 0.1658 0.2621 0.3188 -0.0518 -0.0676 0.0874  51  TYR A C   
463  O  O   . TYR A 51  ? 0.2207 0.2427 0.2833 -0.0152 -0.1064 0.0688  51  TYR A O   
464  C  CB  . TYR A 51  ? 0.1433 0.1902 0.2545 -0.0116 -0.0731 -0.0258 51  TYR A CB  
465  C  CG  . TYR A 51  ? 0.1581 0.1775 0.1757 -0.0566 -0.0522 0.0071  51  TYR A CG  
466  C  CD1 . TYR A 51  ? 0.1351 0.1482 0.2603 -0.0274 -0.0842 0.0168  51  TYR A CD1 
467  C  CD2 . TYR A 51  ? 0.1606 0.1590 0.1796 -0.0423 -0.0432 0.0099  51  TYR A CD2 
468  C  CE1 . TYR A 51  ? 0.1404 0.1538 0.2069 -0.0093 -0.0423 0.0379  51  TYR A CE1 
469  C  CE2 . TYR A 51  ? 0.1545 0.1308 0.1836 -0.0368 -0.0507 -0.0074 51  TYR A CE2 
470  C  CZ  . TYR A 51  ? 0.1319 0.1365 0.1645 -0.0219 -0.0377 -0.0195 51  TYR A CZ  
471  O  OH  . TYR A 51  ? 0.1343 0.1331 0.1913 -0.0222 -0.0478 0.0019  51  TYR A OH  
472  N  N   . ASP A 52  ? 0.1108 0.3373 0.3585 -0.0859 -0.0935 0.1224  52  ASP A N   
473  C  CA  . ASP A 52  ? 0.1699 0.3725 0.4022 -0.0401 -0.1155 0.1611  52  ASP A CA  
474  C  C   . ASP A 52  ? 0.2915 0.2680 0.3842 -0.0458 -0.1453 0.1149  52  ASP A C   
475  O  O   . ASP A 52  ? 0.3519 0.4185 0.4131 -0.1014 -0.2353 0.1579  52  ASP A O   
476  C  CB  . ASP A 52  ? 0.1502 0.3587 0.5270 -0.0219 -0.1216 0.1856  52  ASP A CB  
477  C  CG  . ASP A 52  ? 0.1083 0.5601 0.7930 0.0515  -0.0679 -0.0206 52  ASP A CG  
478  O  OD1 . ASP A 52  ? 0.2375 0.4862 0.7080 -0.0098 -0.0127 -0.0680 52  ASP A OD1 
479  O  OD2 . ASP A 52  ? 0.6664 0.6334 1.0309 0.2333  0.0929  0.4156  52  ASP A OD2 
480  N  N   . GLN A 53  ? 0.1954 0.2116 0.4463 -0.0027 -0.0998 0.1002  53  GLN A N   
481  C  CA  . GLN A 53  ? 0.2279 0.2378 0.4189 -0.0344 -0.1450 0.0768  53  GLN A CA  
482  C  C   . GLN A 53  ? 0.2362 0.1880 0.2833 -0.0395 -0.0737 0.0494  53  GLN A C   
483  O  O   . GLN A 53  ? 0.2154 0.1949 0.3346 -0.0024 -0.0898 0.0608  53  GLN A O   
484  C  CB  . GLN A 53  ? 0.2587 0.2544 0.4487 0.0278  -0.0333 0.0839  53  GLN A CB  
485  C  CG  . GLN A 53  ? 0.2060 0.3734 0.6696 -0.1064 -0.1032 0.0797  53  GLN A CG  
486  C  CD  . GLN A 53  ? 0.2669 0.7971 0.6897 0.0820  -0.1345 0.0516  53  GLN A CD  
487  O  OE1 . GLN A 53  ? 0.5163 0.7455 0.8510 0.2387  0.2425  -0.0634 53  GLN A OE1 
488  N  NE2 . GLN A 53  ? 0.3097 0.9624 0.6523 0.1307  -0.1172 0.2569  53  GLN A NE2 
489  N  N   . ALA A 54  ? 0.2619 0.1555 0.2913 -0.0441 -0.1080 0.0308  54  ALA A N   
490  C  CA  . ALA A 54  ? 0.2175 0.1608 0.2642 -0.0285 -0.1102 -0.0296 54  ALA A CA  
491  C  C   . ALA A 54  ? 0.3271 0.1602 0.2462 -0.0122 -0.0920 -0.0467 54  ALA A C   
492  O  O   . ALA A 54  ? 0.3452 0.2583 0.2836 -0.0176 -0.1151 -0.0851 54  ALA A O   
493  C  CB  . ALA A 54  ? 0.2633 0.1465 0.3355 0.0102  -0.0509 -0.0093 54  ALA A CB  
494  N  N   . THR A 55  ? 0.2585 0.1387 0.1954 0.0293  -0.0753 0.0147  55  THR A N   
495  C  CA  . THR A 55  ? 0.3343 0.1902 0.2055 0.0808  -0.1096 0.0015  55  THR A CA  
496  C  C   . THR A 55  ? 0.3278 0.1026 0.1656 0.0060  -0.1150 0.0142  55  THR A C   
497  O  O   . THR A 55  ? 0.2917 0.1089 0.1663 0.0372  -0.0685 0.0144  55  THR A O   
498  C  CB  . THR A 55  ? 0.5000 0.2487 0.2698 0.1018  -0.0195 0.0936  55  THR A CB  
499  O  OG1 . THR A 55  ? 0.5144 0.2039 0.5841 0.0969  -0.2739 -0.0432 55  THR A OG1 
500  C  CG2 . THR A 55  ? 0.5956 0.2238 0.2590 0.1521  -0.0697 0.0812  55  THR A CG2 
501  N  N   . SER A 56  ? 0.4332 0.0938 0.2029 0.0430  -0.1609 0.0292  56  SER A N   
502  C  CA  . SER A 56  ? 0.4492 0.1018 0.1450 0.0368  -0.0974 0.0186  56  SER A CA  
503  C  C   . SER A 56  ? 0.3776 0.1080 0.1990 0.0724  -0.0335 0.0353  56  SER A C   
504  O  O   . SER A 56  ? 0.5040 0.1088 0.1924 0.0829  -0.1464 0.0160  56  SER A O   
505  C  CB  . SER A 56  ? 0.4492 0.0953 0.1744 0.0237  -0.1298 0.0226  56  SER A CB  
506  O  OG  . SER A 56  ? 0.4674 0.0989 0.1978 0.0243  -0.1671 0.0080  56  SER A OG  
507  N  N   . LEU A 57  ? 0.3109 0.0925 0.1261 0.0342  -0.0342 0.0082  57  LEU A N   
508  C  CA  . LEU A 57  ? 0.3668 0.1081 0.1667 0.0299  -0.0295 -0.0010 57  LEU A CA  
509  C  C   . LEU A 57  ? 0.3986 0.1146 0.1327 0.0208  -0.0414 0.0017  57  LEU A C   
510  O  O   . LEU A 57  ? 0.5285 0.1189 0.1265 0.0313  -0.0361 0.0298  57  LEU A O   
511  C  CB  . LEU A 57  ? 0.4207 0.1808 0.2039 -0.0498 -0.0210 0.0737  57  LEU A CB  
512  C  CG  . LEU A 57  ? 0.6480 0.1155 0.2569 0.0026  -0.0555 -0.0342 57  LEU A CG  
513  C  CD1 . LEU A 57  ? 0.6855 0.2234 0.2955 -0.0718 0.0507  0.0027  57  LEU A CD1 
514  C  CD2 . LEU A 57  ? 1.8739 0.2069 1.1627 -0.1079 -1.0615 0.1897  57  LEU A CD2 
515  N  N   . ARG A 58  ? 0.3368 0.1457 0.1599 0.0584  -0.0296 0.0242  58  ARG A N   
516  C  CA  . ARG A 58  ? 0.2304 0.1604 0.1956 -0.0017 -0.0225 0.0920  58  ARG A CA  
517  C  C   . ARG A 58  ? 0.3282 0.1155 0.1184 -0.0097 -0.0315 0.0211  58  ARG A C   
518  O  O   . ARG A 58  ? 0.4205 0.1237 0.1108 0.0507  0.0074  0.0179  58  ARG A O   
519  C  CB  . ARG A 58  ? 0.1782 0.2746 0.1713 -0.0531 0.0153  0.0027  58  ARG A CB  
520  C  CG  . ARG A 58  ? 0.1622 0.1500 0.3582 -0.0208 0.0287  0.1319  58  ARG A CG  
521  C  CD  . ARG A 58  ? 0.2511 0.3154 0.2208 -0.1112 -0.0214 0.0307  58  ARG A CD  
522  N  NE  . ARG A 58  ? 0.1889 0.2558 0.1981 -0.0013 -0.0098 -0.0017 58  ARG A NE  
523  C  CZ  . ARG A 58  ? 0.1435 0.2745 0.1835 -0.0856 -0.0368 0.0649  58  ARG A CZ  
524  N  NH1 . ARG A 58  ? 0.2761 0.3023 0.2283 -0.1202 -0.0177 0.0421  58  ARG A NH1 
525  N  NH2 . ARG A 58  ? 0.1741 0.2302 0.2126 -0.0094 -0.0114 0.0205  58  ARG A NH2 
526  N  N   . ILE A 59  ? 0.4113 0.1198 0.0988 0.0293  0.0049  0.0179  59  ILE A N   
527  C  CA  . ILE A 59  ? 0.3416 0.1062 0.1304 -0.0148 -0.0104 0.0441  59  ILE A CA  
528  C  C   . ILE A 59  ? 0.2930 0.0964 0.1177 0.0065  -0.0372 0.0181  59  ILE A C   
529  O  O   . ILE A 59  ? 0.3720 0.1519 0.0918 0.0175  -0.0196 0.0175  59  ILE A O   
530  C  CB  . ILE A 59  ? 0.3492 0.0986 0.1181 -0.0006 -0.0351 0.0248  59  ILE A CB  
531  C  CG1 . ILE A 59  ? 0.3181 0.1001 0.1178 -0.0115 -0.0494 0.0189  59  ILE A CG1 
532  C  CG2 . ILE A 59  ? 0.4399 0.1101 0.1159 0.0081  -0.0832 0.0070  59  ILE A CG2 
533  C  CD1 . ILE A 59  ? 0.3433 0.0869 0.1232 0.0049  -0.0328 0.0132  59  ILE A CD1 
534  N  N   . LEU A 60  ? 0.2159 0.1102 0.1872 -0.0296 -0.0368 -0.0156 60  LEU A N   
535  C  CA  . LEU A 60  ? 0.2730 0.1050 0.1045 -0.0146 -0.0557 0.0242  60  LEU A CA  
536  C  C   . LEU A 60  ? 0.2913 0.0991 0.1297 -0.0256 -0.0044 -0.0021 60  LEU A C   
537  O  O   . LEU A 60  ? 0.2763 0.1347 0.1026 -0.0450 0.0100  0.0283  60  LEU A O   
538  C  CB  . LEU A 60  ? 0.2653 0.0957 0.2134 -0.0458 -0.0148 0.0163  60  LEU A CB  
539  C  CG  . LEU A 60  ? 0.2784 0.1008 0.1988 -0.0482 -0.0388 0.0412  60  LEU A CG  
540  C  CD1 . LEU A 60  ? 0.2481 0.1537 0.2234 -0.0644 -0.0026 0.0269  60  LEU A CD1 
541  C  CD2 . LEU A 60  ? 0.3379 0.1174 0.2296 -0.0533 -0.0232 0.0148  60  LEU A CD2 
542  N  N   . ASN A 61  ? 0.2991 0.1038 0.1378 -0.0397 0.0242  0.0219  61  ASN A N   
543  C  CA  . ASN A 61  ? 0.2608 0.1695 0.1360 -0.0744 0.0564  -0.0531 61  ASN A CA  
544  C  C   . ASN A 61  ? 0.2718 0.1440 0.1289 -0.0586 0.0493  -0.0184 61  ASN A C   
545  O  O   . ASN A 61  ? 0.4115 0.1264 0.1397 -0.0856 0.0741  0.0120  61  ASN A O   
546  C  CB  . ASN A 61  ? 0.3916 0.1002 0.1634 -0.0428 0.0390  0.0063  61  ASN A CB  
547  C  CG  . ASN A 61  ? 0.2845 0.1565 0.1194 -0.0926 0.0527  -0.0377 61  ASN A CG  
548  O  OD1 . ASN A 61  ? 0.2998 0.1356 0.1649 -0.0755 0.0751  -0.0148 61  ASN A OD1 
549  N  ND2 . ASN A 61  ? 0.3323 0.1274 0.1464 -0.0722 0.0817  -0.0361 61  ASN A ND2 
550  N  N   . ASN A 62  ? 0.3779 0.1053 0.1265 -0.0852 0.0487  -0.0111 62  ASN A N   
551  C  CA  . ASN A 62  ? 0.2294 0.1838 0.1547 -0.0315 -0.0083 0.0217  62  ASN A CA  
552  C  C   . ASN A 62  ? 0.1512 0.1954 0.1487 -0.0945 -0.0046 0.0076  62  ASN A C   
553  O  O   . ASN A 62  ? 0.2159 0.2682 0.2135 -0.0960 -0.0167 0.0423  62  ASN A O   
554  C  CB  . ASN A 62  ? 0.3869 0.1284 0.1607 -0.0890 -0.0005 -0.0024 62  ASN A CB  
555  C  CG  . ASN A 62  ? 0.3643 0.1270 0.1279 -0.1001 -0.0229 -0.0129 62  ASN A CG  
556  O  OD1 . ASN A 62  ? 0.3361 0.1239 0.1518 -0.0701 0.0432  -0.0149 62  ASN A OD1 
557  N  ND2 . ASN A 62  ? 0.4891 0.1367 0.1669 -0.0597 0.0386  -0.0119 62  ASN A ND2 
558  N  N   . GLY A 63  ? 0.2322 0.1875 0.1746 -0.0417 0.0285  -0.0020 63  GLY A N   
559  C  CA  . GLY A 63  ? 0.1360 0.1880 0.1483 -0.0942 0.0068  -0.0043 63  GLY A CA  
560  C  C   . GLY A 63  ? 0.2213 0.1523 0.2064 -0.0883 0.0227  -0.0318 63  GLY A C   
561  O  O   . GLY A 63  ? 0.2390 0.2306 0.2161 -0.0887 0.0582  -0.0493 63  GLY A O   
562  N  N   . HIS A 64  ? 0.2306 0.1501 0.1498 -0.0751 0.0467  -0.0055 64  HIS A N   
563  C  CA  . HIS A 64  ? 0.2299 0.1760 0.1525 -0.0712 0.0346  -0.0019 64  HIS A CA  
564  C  C   . HIS A 64  ? 0.2128 0.1412 0.1688 -0.0674 0.0498  0.0103  64  HIS A C   
565  O  O   . HIS A 64  ? 0.1767 0.1981 0.3492 -0.0238 0.0320  0.1230  64  HIS A O   
566  C  CB  . HIS A 64  ? 0.1891 0.2020 0.1592 -0.0494 0.0204  -0.0063 64  HIS A CB  
567  C  CG  . HIS A 64  ? 0.2448 0.2382 0.1721 -0.0592 0.0322  0.0254  64  HIS A CG  
568  N  ND1 . HIS A 64  ? 0.2433 0.2746 0.2021 -0.0511 0.0280  -0.0588 64  HIS A ND1 
569  C  CD2 . HIS A 64  ? 0.2685 0.2204 0.1755 -0.0741 0.0463  -0.0285 64  HIS A CD2 
570  C  CE1 . HIS A 64  ? 0.2243 0.3082 0.2434 -0.0808 0.0627  -0.0505 64  HIS A CE1 
571  N  NE2 . HIS A 64  ? 0.2685 0.2849 0.2865 -0.0891 0.0852  -0.0724 64  HIS A NE2 
572  N  N   . ALA A 65  ? 0.2168 0.1374 0.1408 -0.0443 0.0115  0.0051  65  ALA A N   
573  C  CA  . ALA A 65  ? 0.2069 0.1203 0.1369 -0.0537 0.0261  -0.0046 65  ALA A CA  
574  C  C   . ALA A 65  ? 0.2833 0.0953 0.0998 -0.0601 0.0267  -0.0035 65  ALA A C   
575  O  O   . ALA A 65  ? 0.2883 0.1272 0.1406 -0.0502 0.0604  0.0000  65  ALA A O   
576  C  CB  . ALA A 65  ? 0.1977 0.1808 0.1509 -0.0439 0.0155  -0.0136 65  ALA A CB  
577  N  N   . PHE A 66  ? 0.2504 0.0917 0.1178 -0.0472 0.0080  0.0032  66  PHE A N   
578  C  CA  . PHE A 66  ? 0.2542 0.0992 0.0983 -0.0322 -0.0038 0.0077  66  PHE A CA  
579  C  C   . PHE A 66  ? 0.2696 0.0948 0.0822 -0.0317 -0.0137 0.0030  66  PHE A C   
580  O  O   . PHE A 66  ? 0.2635 0.0964 0.1020 -0.0414 0.0074  0.0026  66  PHE A O   
581  C  CB  . PHE A 66  ? 0.2549 0.1527 0.1286 -0.0701 -0.0170 0.0020  66  PHE A CB  
582  C  CG  . PHE A 66  ? 0.2840 0.1277 0.1029 -0.0410 -0.0219 -0.0111 66  PHE A CG  
583  C  CD1 . PHE A 66  ? 0.2648 0.1432 0.0988 -0.0368 -0.0198 0.0059  66  PHE A CD1 
584  C  CD2 . PHE A 66  ? 0.2427 0.1390 0.0983 -0.0094 0.0046  -0.0251 66  PHE A CD2 
585  C  CE1 . PHE A 66  ? 0.2493 0.1432 0.1198 -0.0162 -0.0445 -0.0052 66  PHE A CE1 
586  C  CE2 . PHE A 66  ? 0.2775 0.1270 0.1135 -0.0184 -0.0024 -0.0276 66  PHE A CE2 
587  C  CZ  . PHE A 66  ? 0.2615 0.1386 0.1261 -0.0493 -0.0335 -0.0250 66  PHE A CZ  
588  N  N   . ASN A 67  ? 0.2353 0.0979 0.1094 -0.0262 -0.0171 0.0259  67  ASN A N   
589  C  CA  . ASN A 67  ? 0.2675 0.0785 0.1252 -0.0355 -0.0165 -0.0021 67  ASN A CA  
590  C  C   . ASN A 67  ? 0.2408 0.0689 0.1032 0.0135  -0.0472 0.0131  67  ASN A C   
591  O  O   . ASN A 67  ? 0.3188 0.1464 0.1036 -0.0197 -0.0223 0.0397  67  ASN A O   
592  C  CB  . ASN A 67  ? 0.2845 0.1489 0.1316 -0.0920 -0.0153 -0.0003 67  ASN A CB  
593  C  CG  . ASN A 67  ? 0.2481 0.1877 0.1583 -0.1018 0.0122  -0.0049 67  ASN A CG  
594  O  OD1 . ASN A 67  ? 0.2982 0.2041 0.1604 -0.0973 -0.0230 0.0364  67  ASN A OD1 
595  N  ND2 . ASN A 67  ? 0.2572 0.2378 0.2876 -0.1141 -0.0406 -0.0187 67  ASN A ND2 
596  N  N   . VAL A 68  ? 0.2384 0.1111 0.1151 0.0068  0.0130  -0.0109 68  VAL A N   
597  C  CA  . VAL A 68  ? 0.2831 0.0941 0.0983 0.0777  -0.0461 -0.0038 68  VAL A CA  
598  C  C   . VAL A 68  ? 0.3558 0.0863 0.1119 0.0375  -0.0292 0.0085  68  VAL A C   
599  O  O   . VAL A 68  ? 0.2861 0.0835 0.1035 0.0299  -0.0269 0.0102  68  VAL A O   
600  C  CB  . VAL A 68  ? 0.2782 0.0811 0.1873 0.0231  -0.0511 0.0026  68  VAL A CB  
601  C  CG1 . VAL A 68  ? 0.3310 0.1500 0.1295 0.0939  -0.0688 -0.0161 68  VAL A CG1 
602  C  CG2 . VAL A 68  ? 0.2720 0.1315 0.1464 0.0399  -0.0639 -0.0286 68  VAL A CG2 
603  N  N   . GLU A 69  ? 0.3943 0.1062 0.0957 0.0612  0.0006  0.0051  69  GLU A N   
604  C  CA  . GLU A 69  ? 0.2991 0.1068 0.1092 0.0091  0.0065  0.0026  69  GLU A CA  
605  C  C   . GLU A 69  ? 0.3639 0.0740 0.1732 0.0759  -0.0701 0.0153  69  GLU A C   
606  O  O   . GLU A 69  ? 0.3391 0.1243 0.1622 0.0494  -0.0456 -0.0012 69  GLU A O   
607  C  CB  . GLU A 69  ? 0.1498 0.2208 0.2269 0.0588  0.0432  0.0472  69  GLU A CB  
608  C  CG  . GLU A 69  ? 0.1044 0.2231 0.2356 -0.0381 0.0054  0.0612  69  GLU A CG  
609  C  CD  . GLU A 69  ? 0.1525 0.2206 0.2490 -0.0172 0.0082  0.0449  69  GLU A CD  
610  O  OE1 . GLU A 69  ? 0.2324 0.2297 0.2296 0.0148  0.0207  0.0776  69  GLU A OE1 
611  O  OE2 . GLU A 69  ? 0.1450 0.2277 0.3212 -0.0351 0.0092  0.0794  69  GLU A OE2 
612  N  N   . PHE A 70  ? 0.2885 0.0883 0.1306 0.0049  -0.0254 0.0093  70  PHE A N   
613  C  CA  . PHE A 70  ? 0.2423 0.0667 0.1710 0.0255  -0.0772 -0.0013 70  PHE A CA  
614  C  C   . PHE A 70  ? 0.2581 0.0977 0.1741 0.0070  -0.0560 -0.0046 70  PHE A C   
615  O  O   . PHE A 70  ? 0.2658 0.0860 0.1853 0.0194  -0.0562 0.0247  70  PHE A O   
616  C  CB  . PHE A 70  ? 0.2529 0.1011 0.1376 0.0035  -0.0750 0.0133  70  PHE A CB  
617  C  CG  . PHE A 70  ? 0.2795 0.0750 0.1559 0.0340  -0.0940 0.0164  70  PHE A CG  
618  C  CD1 . PHE A 70  ? 0.2509 0.0977 0.1457 0.0324  -0.0579 0.0350  70  PHE A CD1 
619  C  CD2 . PHE A 70  ? 0.2698 0.0939 0.1505 0.0454  -0.0828 0.0086  70  PHE A CD2 
620  C  CE1 . PHE A 70  ? 0.2590 0.0917 0.1579 0.0278  -0.0251 0.0351  70  PHE A CE1 
621  C  CE2 . PHE A 70  ? 0.2538 0.0982 0.1552 0.0135  -0.0562 0.0077  70  PHE A CE2 
622  C  CZ  . PHE A 70  ? 0.2703 0.1018 0.1692 0.0245  -0.0333 0.0000  70  PHE A CZ  
623  N  N   . ASP A 71  ? 0.3145 0.0838 0.2152 0.0298  -0.1124 0.0154  71  ASP A N   
624  C  CA  . ASP A 71  ? 0.3169 0.0797 0.2324 0.0308  -0.1006 0.0221  71  ASP A CA  
625  C  C   . ASP A 71  ? 0.2822 0.0458 0.3253 -0.0231 -0.0491 0.0049  71  ASP A C   
626  O  O   . ASP A 71  ? 0.2894 0.1446 0.3743 -0.0298 -0.0408 -0.0300 71  ASP A O   
627  C  CB  . ASP A 71  ? 0.4104 0.1011 0.4203 0.0115  -0.2351 0.0636  71  ASP A CB  
628  C  CG  . ASP A 71  ? 0.4950 0.1252 0.5692 -0.0121 -0.3005 0.0692  71  ASP A CG  
629  O  OD1 . ASP A 71  ? 0.3802 0.0957 0.4111 0.0571  -0.1171 0.0434  71  ASP A OD1 
630  O  OD2 . ASP A 71  ? 1.1778 0.4253 2.1900 -0.1708 -1.4344 0.1773  71  ASP A OD2 
631  N  N   . ASP A 72  ? 0.1990 0.0518 0.2446 0.0000  -0.0060 0.0181  72  ASP A N   
632  C  CA  . ASP A 72  ? 0.2308 0.0768 0.2531 -0.0038 0.0043  -0.0032 72  ASP A CA  
633  C  C   . ASP A 72  ? 0.2001 0.0891 0.2822 0.0153  0.0059  0.0140  72  ASP A C   
634  O  O   . ASP A 72  ? 0.2996 0.0935 0.2700 0.0052  0.0258  -0.0167 72  ASP A O   
635  C  CB  . ASP A 72  ? 0.2249 0.1110 0.2102 0.0120  0.0388  0.0245  72  ASP A CB  
636  C  CG  . ASP A 72  ? 0.2117 0.1292 0.1674 0.0041  0.0098  0.0043  72  ASP A CG  
637  O  OD1 . ASP A 72  ? 0.1934 0.2129 0.2096 -0.0159 -0.0239 0.0502  72  ASP A OD1 
638  O  OD2 . ASP A 72  ? 0.2204 0.1631 0.1613 -0.0200 -0.0211 -0.0091 72  ASP A OD2 
639  N  N   . SER A 73  ? 0.2560 0.0772 0.3163 0.0208  -0.0315 0.0318  73  SER A N   
640  C  CA  . SER A 73  ? 0.2755 0.0790 0.3097 -0.0142 -0.0071 -0.0031 73  SER A CA  
641  C  C   . SER A 73  ? 0.2236 0.0851 0.3215 -0.0311 -0.0238 -0.0208 73  SER A C   
642  O  O   . SER A 73  ? 0.2520 0.0939 0.2935 0.0087  -0.0317 0.0000  73  SER A O   
643  C  CB  . SER A 73  ? 0.3964 0.1047 0.4005 0.0100  0.0040  0.0878  73  SER A CB  
644  O  OG  . SER A 73  ? 0.3686 0.1417 0.3373 0.0553  0.0870  0.0772  73  SER A OG  
645  N  N   . GLN A 74  ? 0.1850 0.1187 0.4523 0.0218  0.0076  0.0132  74  GLN A N   
646  C  CA  . GLN A 74  ? 0.2181 0.1733 0.4205 0.0239  0.0518  0.0331  74  GLN A CA  
647  C  C   . GLN A 74  ? 0.1983 0.2015 0.2809 0.0272  0.0038  0.0080  74  GLN A C   
648  O  O   . GLN A 74  ? 0.1744 0.1609 0.2479 -0.0322 -0.0562 0.0019  74  GLN A O   
649  C  CB  . GLN A 74  ? 0.2139 0.1968 0.4853 0.0276  0.0137  0.0511  74  GLN A CB  
650  C  CG  . GLN A 74  ? 0.2939 0.1830 0.5645 0.0118  0.0073  0.0804  74  GLN A CG  
651  C  CD  . GLN A 74  ? 0.4372 0.5115 0.7394 -0.1507 -0.1615 0.0417  74  GLN A CD  
652  O  OE1 . GLN A 74  ? 0.4250 0.3808 0.6093 -0.0795 -0.2870 0.0940  74  GLN A OE1 
653  N  NE2 . GLN A 74  ? 0.3147 0.5242 0.6762 -0.1019 -0.1807 0.2827  74  GLN A NE2 
654  N  N   . ASP A 75  ? 0.2538 0.2497 0.2748 -0.0749 0.0021  -0.0381 75  ASP A N   
655  C  CA  . ASP A 75  ? 0.2069 0.1638 0.2694 -0.0148 -0.0043 -0.0154 75  ASP A CA  
656  C  C   . ASP A 75  ? 0.1848 0.2251 0.3212 -0.0185 -0.0148 -0.0467 75  ASP A C   
657  O  O   . ASP A 75  ? 0.1983 0.2996 0.4262 0.0434  -0.0259 0.0337  75  ASP A O   
658  C  CB  . ASP A 75  ? 0.2506 0.2207 0.2802 0.0687  0.0255  0.0170  75  ASP A CB  
659  C  CG  . ASP A 75  ? 0.4704 0.2392 0.3303 -0.0531 -0.0646 0.1308  75  ASP A CG  
660  O  OD1 . ASP A 75  ? 0.1832 0.3084 0.4959 0.0013  -0.0636 0.1648  75  ASP A OD1 
661  O  OD2 . ASP A 75  ? 0.4234 0.5339 0.6571 -0.0412 0.0798  0.0076  75  ASP A OD2 
662  N  N   . LYS A 76  ? 0.2324 0.1611 0.2378 -0.0148 -0.0562 0.0340  76  LYS A N   
663  C  CA  . LYS A 76  ? 0.2773 0.1431 0.2854 0.0096  -0.0640 0.0070  76  LYS A CA  
664  C  C   . LYS A 76  ? 0.9375 0.0912 0.5224 0.0164  -0.1260 0.0377  76  LYS A C   
665  O  O   . LYS A 76  ? 0.9376 0.8120 0.7954 -0.0121 -0.1641 0.1532  76  LYS A O   
666  C  CB  . LYS A 76  ? 0.3165 0.1263 0.2881 -0.0234 -0.1141 0.0049  76  LYS A CB  
667  C  CG  . LYS A 76  ? 0.6389 0.1527 0.3876 -0.0315 -0.2134 0.0351  76  LYS A CG  
668  C  CD  . LYS A 76  ? 0.8633 0.2119 0.2811 -0.1861 -0.1847 0.0000  76  LYS A CD  
669  C  CE  . LYS A 76  ? 0.6574 0.2967 0.4208 -0.0656 -0.1079 0.0234  76  LYS A CE  
670  N  NZ  . LYS A 76  ? 0.9244 0.3605 0.4955 0.1083  0.1024  0.1798  76  LYS A NZ  
671  N  N   . ALA A 77  ? 0.2942 0.2484 0.3785 0.0650  -0.2099 0.0346  77  ALA A N   
672  C  CA  . ALA A 77  ? 0.2105 0.2256 0.2310 0.0020  -0.0952 0.0100  77  ALA A CA  
673  C  C   . ALA A 77  ? 0.1058 0.1548 0.2407 -0.0217 -0.0838 -0.0041 77  ALA A C   
674  O  O   . ALA A 77  ? 0.1263 0.3549 0.2818 0.0028  -0.0625 -0.1326 77  ALA A O   
675  C  CB  . ALA A 77  ? 0.1819 0.2163 0.2347 -0.0289 -0.0864 0.0133  77  ALA A CB  
676  N  N   . VAL A 78  ? 0.1644 0.1352 0.2204 -0.0155 -0.0719 0.0296  78  VAL A N   
677  C  CA  . VAL A 78  ? 0.1904 0.1155 0.2066 -0.0073 -0.0697 0.0270  78  VAL A CA  
678  C  C   . VAL A 78  ? 0.0926 0.1092 0.2410 -0.0031 -0.0357 0.0230  78  VAL A C   
679  O  O   . VAL A 78  ? 0.1286 0.1390 0.2705 -0.0368 -0.0694 0.0097  78  VAL A O   
680  C  CB  . VAL A 78  ? 0.3998 0.0995 0.2561 0.0215  -0.1221 -0.0017 78  VAL A CB  
681  C  CG1 . VAL A 78  ? 0.3501 0.1938 0.2894 0.0096  -0.0071 -0.0331 78  VAL A CG1 
682  C  CG2 . VAL A 78  ? 0.4151 0.1808 0.3093 0.0264  -0.0769 0.0939  78  VAL A CG2 
683  N  N   . LEU A 79  ? 0.1011 0.1243 0.1861 0.0170  -0.0162 0.0148  79  LEU A N   
684  C  CA  . LEU A 79  ? 0.1158 0.1248 0.1810 -0.0151 -0.0240 0.0102  79  LEU A CA  
685  C  C   . LEU A 79  ? 0.1284 0.1264 0.1530 -0.0196 -0.0051 -0.0046 79  LEU A C   
686  O  O   . LEU A 79  ? 0.1543 0.1394 0.1819 -0.0211 0.0077  -0.0140 79  LEU A O   
687  C  CB  . LEU A 79  ? 0.1070 0.1665 0.2190 -0.0010 -0.0357 0.0366  79  LEU A CB  
688  C  CG  . LEU A 79  ? 0.1146 0.1351 0.1979 0.0113  -0.0091 0.0046  79  LEU A CG  
689  C  CD1 . LEU A 79  ? 0.1266 0.1377 0.3774 -0.0049 0.0059  0.0636  79  LEU A CD1 
690  C  CD2 . LEU A 79  ? 0.1050 0.1327 0.1818 0.0051  -0.0031 -0.0137 79  LEU A CD2 
691  N  N   . LYS A 80  ? 0.1414 0.1577 0.1730 -0.0078 0.0038  -0.0041 80  LYS A N   
692  C  CA  . LYS A 80  ? 0.1264 0.1376 0.2098 -0.0080 -0.0073 0.0060  80  LYS A CA  
693  C  C   . LYS A 80  ? 0.0959 0.1475 0.2366 0.0153  0.0329  0.0176  80  LYS A C   
694  O  O   . LYS A 80  ? 0.1120 0.1493 0.2355 -0.0059 0.0049  0.0200  80  LYS A O   
695  C  CB  . LYS A 80  ? 0.1705 0.1534 0.2743 -0.0038 -0.0006 0.0057  80  LYS A CB  
696  C  CG  . LYS A 80  ? 0.1190 0.1512 0.3596 0.0337  0.0073  0.0248  80  LYS A CG  
697  C  CD  . LYS A 80  ? 0.4636 0.1553 0.5637 0.0419  -0.0604 0.0996  80  LYS A CD  
698  C  CE  . LYS A 80  ? 0.6333 0.4257 0.8105 0.1970  0.0452  0.0925  80  LYS A CE  
699  N  NZ  . LYS A 80  ? 0.4246 0.5995 1.1382 0.1993  -0.1506 0.0271  80  LYS A NZ  
700  N  N   . GLY A 81  ? 0.1626 0.1692 0.2056 0.0190  0.0295  0.0041  81  GLY A N   
701  C  CA  . GLY A 81  ? 0.1414 0.2012 0.2304 0.0225  0.0579  0.0417  81  GLY A CA  
702  C  C   . GLY A 81  ? 0.1356 0.1677 0.2339 0.0274  0.0553  0.0304  81  GLY A C   
703  O  O   . GLY A 81  ? 0.1235 0.1710 0.2143 -0.0111 0.0188  -0.0248 81  GLY A O   
704  N  N   . GLY A 82  ? 0.1690 0.1832 0.3465 0.0068  0.0724  0.0494  82  GLY A N   
705  C  CA  . GLY A 82  ? 0.1941 0.1685 0.3914 0.0118  0.0417  0.0318  82  GLY A CA  
706  C  C   . GLY A 82  ? 0.1717 0.1677 0.3172 0.0412  0.0683  0.0582  82  GLY A C   
707  O  O   . GLY A 82  ? 0.1967 0.3765 0.3219 0.1367  0.0952  0.1121  82  GLY A O   
708  N  N   . PRO A 83  ? 0.1467 0.1717 0.2448 0.0196  0.0266  0.0291  83  PRO A N   
709  C  CA  . PRO A 83  ? 0.1929 0.1768 0.1956 0.0650  0.0044  0.0234  83  PRO A CA  
710  C  C   . PRO A 83  ? 0.1679 0.2326 0.1909 0.0760  -0.0273 -0.0287 83  PRO A C   
711  O  O   . PRO A 83  ? 0.1855 0.2471 0.2247 0.0509  -0.0447 -0.0012 83  PRO A O   
712  C  CB  . PRO A 83  ? 0.2069 0.1830 0.2042 0.0566  -0.0276 -0.0044 83  PRO A CB  
713  C  CG  . PRO A 83  ? 0.1547 0.1527 0.1994 0.0641  0.0032  -0.0040 83  PRO A CG  
714  C  CD  . PRO A 83  ? 0.1191 0.1399 0.2614 0.0204  0.0454  -0.0102 83  PRO A CD  
715  N  N   . LEU A 84  ? 0.1317 0.1486 0.1859 0.0296  -0.0020 -0.0020 84  LEU A N   
716  C  CA  . LEU A 84  ? 0.1852 0.1117 0.1773 0.0251  -0.0065 -0.0331 84  LEU A CA  
717  C  C   . LEU A 84  ? 0.1351 0.1741 0.2198 0.0540  -0.0247 -0.0579 84  LEU A C   
718  O  O   . LEU A 84  ? 0.1830 0.1649 0.2673 0.0340  0.0337  -0.0641 84  LEU A O   
719  C  CB  . LEU A 84  ? 0.1029 0.1205 0.1789 0.0193  0.0233  -0.0204 84  LEU A CB  
720  C  CG  . LEU A 84  ? 0.1126 0.1027 0.1741 0.0122  0.0205  -0.0204 84  LEU A CG  
721  C  CD1 . LEU A 84  ? 0.1307 0.1306 0.1748 0.0126  -0.0041 -0.0085 84  LEU A CD1 
722  C  CD2 . LEU A 84  ? 0.1182 0.1205 0.1598 -0.0024 0.0208  -0.0259 84  LEU A CD2 
723  N  N   . ASP A 85  ? 0.2443 0.1376 0.2017 0.0271  0.0063  -0.0610 85  ASP A N   
724  C  CA  . ASP A 85  ? 0.2991 0.1349 0.2737 -0.0178 0.0373  -0.0944 85  ASP A CA  
725  C  C   . ASP A 85  ? 0.1862 0.0887 0.3680 0.0216  0.0366  -0.0071 85  ASP A C   
726  O  O   . ASP A 85  ? 0.2782 0.2423 0.3519 0.0248  0.0615  -0.0816 85  ASP A O   
727  C  CB  . ASP A 85  ? 0.4038 0.1283 0.2919 -0.0015 0.0127  -0.0445 85  ASP A CB  
728  C  CG  . ASP A 85  ? 0.5741 0.3215 0.4553 -0.1026 0.2226  0.0914  85  ASP A CG  
729  O  OD1 . ASP A 85  ? 0.4700 0.5881 0.3447 -0.0551 0.1598  0.0275  85  ASP A OD1 
730  O  OD2 . ASP A 85  ? 0.4061 0.5124 0.9848 0.1638  0.0509  -0.3018 85  ASP A OD2 
731  N  N   . GLY A 86  ? 0.3233 0.2216 0.3869 0.0659  0.0052  0.0653  86  GLY A N   
732  C  CA  . GLY A 86  ? 0.3431 0.2640 0.2254 -0.0269 0.0031  -0.0093 86  GLY A CA  
733  C  C   . GLY A 86  ? 0.1941 0.2658 0.2344 -0.0745 -0.0478 0.0043  86  GLY A C   
734  O  O   . GLY A 86  ? 0.3964 0.3397 0.2703 -0.2072 -0.0270 0.0223  86  GLY A O   
735  N  N   A THR A 87  ? 0.1674 0.1331 0.2198 0.0077  0.0082  -0.0283 87  THR A N   
736  N  N   B THR A 87  ? 0.1660 0.1377 0.2214 0.0094  0.0082  -0.0282 87  THR A N   
737  C  CA  A THR A 87  ? 0.1232 0.1369 0.2504 0.0346  0.0099  -0.0454 87  THR A CA  
738  C  CA  B THR A 87  ? 0.1396 0.1534 0.2529 0.0203  -0.0017 -0.0348 87  THR A CA  
739  C  C   A THR A 87  ? 0.0922 0.1004 0.2211 0.0187  -0.0054 -0.0296 87  THR A C   
740  C  C   B THR A 87  ? 0.1098 0.1054 0.2241 0.0076  -0.0115 -0.0322 87  THR A C   
741  O  O   A THR A 87  ? 0.1304 0.0865 0.2263 0.0127  0.0096  -0.0274 87  THR A O   
742  O  O   B THR A 87  ? 0.1377 0.0886 0.2270 0.0089  0.0148  -0.0241 87  THR A O   
743  C  CB  A THR A 87  ? 0.1058 0.1270 0.2908 0.0403  0.0253  -0.0482 87  THR A CB  
744  C  CB  B THR A 87  ? 0.1688 0.2396 0.2937 0.0864  -0.0173 -0.0526 87  THR A CB  
745  O  OG1 A THR A 87  ? 0.1474 0.1237 0.2132 0.0348  0.0299  0.0299  87  THR A OG1 
746  O  OG1 B THR A 87  ? 0.1947 0.2917 0.3291 0.0834  -0.0083 -0.1140 87  THR A OG1 
747  C  CG2 A THR A 87  ? 0.1284 0.3176 0.2698 0.0929  0.0068  -0.0922 87  THR A CG2 
748  C  CG2 B THR A 87  ? 0.3156 0.2980 0.2581 0.1061  -0.0209 -0.0658 87  THR A CG2 
749  N  N   . TYR A 88  ? 0.0917 0.1027 0.1685 0.0094  -0.0164 -0.0115 88  TYR A N   
750  C  CA  . TYR A 88  ? 0.0961 0.1049 0.1553 0.0195  -0.0115 0.0023  88  TYR A CA  
751  C  C   . TYR A 88  ? 0.0989 0.0980 0.1669 0.0114  -0.0217 0.0080  88  TYR A C   
752  O  O   . TYR A 88  ? 0.1261 0.1855 0.1952 -0.0535 -0.0417 0.0163  88  TYR A O   
753  C  CB  . TYR A 88  ? 0.1137 0.0709 0.1638 0.0089  -0.0201 -0.0113 88  TYR A CB  
754  C  CG  . TYR A 88  ? 0.0977 0.0689 0.1380 -0.0046 -0.0098 -0.0041 88  TYR A CG  
755  C  CD1 . TYR A 88  ? 0.1153 0.0966 0.1475 0.0149  0.0003  -0.0109 88  TYR A CD1 
756  C  CD2 . TYR A 88  ? 0.0887 0.0529 0.1597 0.0087  -0.0138 -0.0063 88  TYR A CD2 
757  C  CE1 . TYR A 88  ? 0.1079 0.1094 0.1528 0.0177  0.0122  -0.0284 88  TYR A CE1 
758  C  CE2 . TYR A 88  ? 0.0887 0.0627 0.1361 0.0063  -0.0052 -0.0109 88  TYR A CE2 
759  C  CZ  . TYR A 88  ? 0.1117 0.0710 0.1347 0.0115  0.0003  -0.0148 88  TYR A CZ  
760  O  OH  . TYR A 88  ? 0.1105 0.0984 0.1378 0.0111  -0.0077 -0.0192 88  TYR A OH  
761  N  N   . ARG A 89  ? 0.1049 0.0731 0.1464 0.0233  -0.0125 -0.0111 89  ARG A N   
762  C  CA  . ARG A 89  ? 0.1200 0.0746 0.1501 0.0148  -0.0300 0.0046  89  ARG A CA  
763  C  C   . ARG A 89  ? 0.1041 0.0599 0.1132 -0.0012 -0.0215 0.0107  89  ARG A C   
764  O  O   . ARG A 89  ? 0.1024 0.0636 0.1387 0.0109  -0.0204 0.0052  89  ARG A O   
765  C  CB  . ARG A 89  ? 0.2062 0.0674 0.1701 0.0070  -0.0307 0.0122  89  ARG A CB  
766  C  CG  . ARG A 89  ? 0.1814 0.1110 0.2010 -0.0196 -0.0445 0.0023  89  ARG A CG  
767  C  CD  . ARG A 89  ? 0.1717 0.1274 0.1994 0.0207  0.0010  0.0196  89  ARG A CD  
768  N  NE  . ARG A 89  ? 0.1941 0.1404 0.1978 -0.0098 -0.0005 0.0410  89  ARG A NE  
769  C  CZ  . ARG A 89  ? 0.2168 0.1178 0.1884 -0.0097 0.0080  -0.0019 89  ARG A CZ  
770  N  NH1 . ARG A 89  ? 0.2236 0.1417 0.2345 -0.0026 0.0137  0.0170  89  ARG A NH1 
771  N  NH2 . ARG A 89  ? 0.2187 0.1295 0.2233 0.0000  -0.0088 -0.0001 89  ARG A NH2 
772  N  N   . LEU A 90  ? 0.1160 0.0776 0.1243 -0.0063 -0.0351 -0.0015 90  LEU A N   
773  C  CA  . LEU A 90  ? 0.1423 0.0848 0.1040 -0.0093 -0.0258 -0.0087 90  LEU A CA  
774  C  C   . LEU A 90  ? 0.1317 0.0904 0.1106 -0.0074 -0.0288 0.0006  90  LEU A C   
775  O  O   . LEU A 90  ? 0.1518 0.1026 0.1397 0.0035  -0.0260 0.0278  90  LEU A O   
776  C  CB  . LEU A 90  ? 0.1413 0.0970 0.1329 -0.0088 -0.0401 0.0052  90  LEU A CB  
777  C  CG  . LEU A 90  ? 0.1722 0.0829 0.1422 -0.0184 -0.0364 0.0024  90  LEU A CG  
778  C  CD1 . LEU A 90  ? 0.2060 0.0702 0.1597 0.0137  -0.0326 0.0054  90  LEU A CD1 
779  C  CD2 . LEU A 90  ? 0.1817 0.1546 0.1563 -0.0399 -0.0474 -0.0206 90  LEU A CD2 
780  N  N   . ILE A 91  ? 0.1449 0.0666 0.1256 0.0027  -0.0062 -0.0003 91  ILE A N   
781  C  CA  . ILE A 91  ? 0.1407 0.0608 0.1280 -0.0017 -0.0068 -0.0003 91  ILE A CA  
782  C  C   . ILE A 91  ? 0.1448 0.0608 0.1146 0.0100  -0.0244 0.0156  91  ILE A C   
783  O  O   . ILE A 91  ? 0.1854 0.0586 0.1092 -0.0063 -0.0170 0.0100  91  ILE A O   
784  C  CB  . ILE A 91  ? 0.1669 0.0816 0.1178 -0.0182 -0.0052 0.0097  91  ILE A CB  
785  C  CG1 . ILE A 91  ? 0.2082 0.1316 0.1571 -0.0688 0.0017  -0.0186 91  ILE A CG1 
786  C  CG2 . ILE A 91  ? 0.1575 0.0680 0.1484 -0.0218 -0.0305 0.0119  91  ILE A CG2 
787  C  CD1 . ILE A 91  ? 0.2272 0.1559 0.1712 -0.0821 0.0099  -0.0392 91  ILE A CD1 
788  N  N   . GLN A 92  ? 0.1388 0.0533 0.1033 -0.0020 -0.0131 0.0060  92  GLN A N   
789  C  CA  . GLN A 92  ? 0.1755 0.0503 0.1041 0.0071  -0.0184 0.0078  92  GLN A CA  
790  C  C   . GLN A 92  ? 0.1495 0.0582 0.1033 -0.0030 -0.0049 0.0027  92  GLN A C   
791  O  O   . GLN A 92  ? 0.1504 0.0587 0.0975 -0.0083 -0.0086 0.0015  92  GLN A O   
792  C  CB  . GLN A 92  ? 0.2275 0.0701 0.1135 -0.0074 0.0024  0.0197  92  GLN A CB  
793  C  CG  . GLN A 92  ? 0.1697 0.0640 0.1617 -0.0094 -0.0006 0.0066  92  GLN A CG  
794  C  CD  . GLN A 92  ? 0.1586 0.0903 0.1498 -0.0206 0.0087  0.0140  92  GLN A CD  
795  O  OE1 . GLN A 92  ? 0.1978 0.0749 0.1462 0.0051  -0.0091 0.0223  92  GLN A OE1 
796  N  NE2 . GLN A 92  ? 0.1656 0.1058 0.2285 -0.0001 0.0055  0.0046  92  GLN A NE2 
797  N  N   . PHE A 93  ? 0.1692 0.0474 0.0993 0.0048  -0.0199 0.0074  93  PHE A N   
798  C  CA  . PHE A 93  ? 0.1455 0.0483 0.0891 -0.0013 -0.0239 -0.0028 93  PHE A CA  
799  C  C   . PHE A 93  ? 0.1534 0.0533 0.0799 -0.0166 -0.0216 0.0059  93  PHE A C   
800  O  O   . PHE A 93  ? 0.2048 0.0670 0.0885 0.0043  -0.0120 0.0043  93  PHE A O   
801  C  CB  . PHE A 93  ? 0.1602 0.0755 0.1115 -0.0057 -0.0392 0.0153  93  PHE A CB  
802  C  CG  . PHE A 93  ? 0.1658 0.0789 0.1023 0.0031  -0.0478 0.0076  93  PHE A CG  
803  C  CD1 . PHE A 93  ? 0.2159 0.0657 0.1151 -0.0177 -0.0434 -0.0031 93  PHE A CD1 
804  C  CD2 . PHE A 93  ? 0.1775 0.1008 0.1304 0.0102  -0.0747 0.0299  93  PHE A CD2 
805  C  CE1 . PHE A 93  ? 0.2402 0.0806 0.1185 0.0211  -0.0666 -0.0147 93  PHE A CE1 
806  C  CE2 . PHE A 93  ? 0.2369 0.0961 0.1345 0.0373  -0.0834 -0.0001 93  PHE A CE2 
807  C  CZ  . PHE A 93  ? 0.2759 0.0764 0.1464 0.0275  -0.0927 -0.0097 93  PHE A CZ  
808  N  N   . HIS A 94  ? 0.1523 0.0516 0.0966 -0.0082 -0.0346 0.0093  94  HIS A N   
809  C  CA  . HIS A 94  ? 0.1349 0.0632 0.0861 -0.0116 -0.0204 0.0003  94  HIS A CA  
810  C  C   . HIS A 94  ? 0.1194 0.0584 0.0692 -0.0142 -0.0260 -0.0024 94  HIS A C   
811  O  O   . HIS A 94  ? 0.1280 0.0583 0.0804 -0.0038 -0.0041 0.0044  94  HIS A O   
812  C  CB  . HIS A 94  ? 0.1360 0.0795 0.1045 -0.0214 -0.0124 -0.0019 94  HIS A CB  
813  C  CG  . HIS A 94  ? 0.1430 0.0636 0.0916 -0.0071 -0.0010 -0.0026 94  HIS A CG  
814  N  ND1 . HIS A 94  ? 0.1308 0.0716 0.0921 -0.0028 -0.0037 0.0055  94  HIS A ND1 
815  C  CD2 . HIS A 94  ? 0.1160 0.1033 0.0799 -0.0244 -0.0154 -0.0030 94  HIS A CD2 
816  C  CE1 . HIS A 94  ? 0.1015 0.0537 0.1207 -0.0065 -0.0087 0.0163  94  HIS A CE1 
817  N  NE2 . HIS A 94  ? 0.1061 0.0645 0.0842 -0.0038 -0.0164 0.0141  94  HIS A NE2 
818  N  N   . PHE A 95  ? 0.1298 0.0530 0.1081 -0.0041 -0.0109 0.0007  95  PHE A N   
819  C  CA  . PHE A 95  ? 0.1288 0.0485 0.1009 -0.0082 -0.0157 0.0019  95  PHE A CA  
820  C  C   . PHE A 95  ? 0.1336 0.0671 0.0877 -0.0083 0.0008  -0.0049 95  PHE A C   
821  O  O   . PHE A 95  ? 0.1110 0.0800 0.1047 -0.0060 -0.0044 0.0078  95  PHE A O   
822  C  CB  . PHE A 95  ? 0.1371 0.0646 0.1081 -0.0065 -0.0197 -0.0133 95  PHE A CB  
823  C  CG  . PHE A 95  ? 0.1336 0.0575 0.0927 -0.0062 -0.0161 -0.0130 95  PHE A CG  
824  C  CD1 . PHE A 95  ? 0.1688 0.0684 0.1092 -0.0031 -0.0250 -0.0046 95  PHE A CD1 
825  C  CD2 . PHE A 95  ? 0.1254 0.0661 0.1189 -0.0238 -0.0260 -0.0200 95  PHE A CD2 
826  C  CE1 . PHE A 95  ? 0.1629 0.0869 0.1178 -0.0038 -0.0364 -0.0170 95  PHE A CE1 
827  C  CE2 . PHE A 95  ? 0.1446 0.0775 0.1225 -0.0057 -0.0294 -0.0241 95  PHE A CE2 
828  C  CZ  . PHE A 95  ? 0.1606 0.0864 0.1376 -0.0082 -0.0454 -0.0265 95  PHE A CZ  
829  N  N   . HIS A 96  ? 0.1216 0.0561 0.0881 0.0020  -0.0114 -0.0046 96  HIS A N   
830  C  CA  . HIS A 96  ? 0.1089 0.0566 0.1054 -0.0063 0.0012  -0.0019 96  HIS A CA  
831  C  C   . HIS A 96  ? 0.1010 0.0688 0.0950 -0.0093 -0.0006 -0.0041 96  HIS A C   
832  O  O   . HIS A 96  ? 0.1081 0.0553 0.1070 -0.0078 0.0000  -0.0065 96  HIS A O   
833  C  CB  . HIS A 96  ? 0.1146 0.0698 0.1124 -0.0126 -0.0165 -0.0173 96  HIS A CB  
834  C  CG  . HIS A 96  ? 0.1022 0.0745 0.0997 -0.0088 -0.0041 -0.0147 96  HIS A CG  
835  N  ND1 . HIS A 96  ? 0.1031 0.0623 0.1509 -0.0062 0.0000  -0.0136 96  HIS A ND1 
836  C  CD2 . HIS A 96  ? 0.1130 0.0494 0.0993 -0.0044 -0.0121 -0.0228 96  HIS A CD2 
837  C  CE1 . HIS A 96  ? 0.1084 0.0663 0.1324 -0.0111 0.0020  -0.0186 96  HIS A CE1 
838  N  NE2 . HIS A 96  ? 0.1062 0.0680 0.0996 -0.0161 -0.0005 -0.0030 96  HIS A NE2 
839  N  N   . TRP A 97  ? 0.1144 0.0526 0.0968 -0.0043 -0.0046 -0.0078 97  TRP A N   
840  C  CA  . TRP A 97  ? 0.1106 0.0562 0.1221 0.0043  0.0008  -0.0137 97  TRP A CA  
841  C  C   . TRP A 97  ? 0.1036 0.0617 0.1029 -0.0124 0.0098  -0.0136 97  TRP A C   
842  O  O   . TRP A 97  ? 0.1112 0.0653 0.1246 -0.0129 0.0215  -0.0196 97  TRP A O   
843  C  CB  . TRP A 97  ? 0.1398 0.0800 0.0997 -0.0211 0.0030  -0.0143 97  TRP A CB  
844  C  CG  . TRP A 97  ? 0.1437 0.0599 0.0938 -0.0154 -0.0013 -0.0149 97  TRP A CG  
845  C  CD1 . TRP A 97  ? 0.1841 0.0917 0.1032 -0.0237 0.0266  -0.0247 97  TRP A CD1 
846  C  CD2 . TRP A 97  ? 0.1737 0.0670 0.1058 -0.0294 0.0157  -0.0147 97  TRP A CD2 
847  N  NE1 . TRP A 97  ? 0.2064 0.0866 0.1036 -0.0326 0.0289  -0.0260 97  TRP A NE1 
848  C  CE2 . TRP A 97  ? 0.1821 0.0842 0.1168 -0.0337 0.0243  -0.0335 97  TRP A CE2 
849  C  CE3 . TRP A 97  ? 0.1474 0.0725 0.1040 0.0006  -0.0100 -0.0013 97  TRP A CE3 
850  C  CZ2 . TRP A 97  ? 0.2093 0.0952 0.1108 -0.0476 0.0205  -0.0170 97  TRP A CZ2 
851  C  CZ3 . TRP A 97  ? 0.1920 0.0825 0.0984 -0.0373 -0.0076 -0.0082 97  TRP A CZ3 
852  C  CH2 . TRP A 97  ? 0.2390 0.0837 0.1013 -0.0436 0.0186  -0.0186 97  TRP A CH2 
853  N  N   . GLY A 98  ? 0.1328 0.0562 0.1099 -0.0054 0.0127  -0.0136 98  GLY A N   
854  C  CA  . GLY A 98  ? 0.1146 0.0724 0.1261 0.0052  0.0182  -0.0193 98  GLY A CA  
855  C  C   . GLY A 98  ? 0.1313 0.0693 0.1525 -0.0087 0.0044  -0.0344 98  GLY A C   
856  O  O   . GLY A 98  ? 0.1624 0.0791 0.1446 -0.0203 0.0093  -0.0320 98  GLY A O   
857  N  N   . SER A 99  ? 0.1358 0.0898 0.1385 -0.0020 0.0205  -0.0403 99  SER A N   
858  C  CA  . SER A 99  ? 0.1746 0.1044 0.1489 -0.0143 0.0329  -0.0546 99  SER A CA  
859  C  C   . SER A 99  ? 0.1969 0.0741 0.1586 0.0031  -0.0007 -0.0478 99  SER A C   
860  O  O   . SER A 99  ? 0.2170 0.1074 0.1746 0.0012  0.0159  -0.0511 99  SER A O   
861  C  CB  . SER A 99  ? 0.1641 0.1329 0.1911 -0.0218 0.0419  -0.0732 99  SER A CB  
862  O  OG  . SER A 99  ? 0.1297 0.0971 0.2387 0.0003  0.0310  -0.0507 99  SER A OG  
863  N  N   . LEU A 100 ? 0.1239 0.1031 0.1829 -0.0119 0.0092  -0.0474 100 LEU A N   
864  C  CA  . LEU A 100 ? 0.1927 0.0672 0.2144 -0.0028 0.0441  -0.0348 100 LEU A CA  
865  C  C   . LEU A 100 ? 0.1642 0.0702 0.1678 0.0041  0.0142  -0.0286 100 LEU A C   
866  O  O   . LEU A 100 ? 0.1468 0.0754 0.1765 -0.0003 0.0121  -0.0344 100 LEU A O   
867  C  CB  . LEU A 100 ? 0.2673 0.1808 0.2960 0.0627  0.0812  0.0723  100 LEU A CB  
868  C  CG  . LEU A 100 ? 0.1809 0.2594 0.3228 0.0217  0.0062  0.0529  100 LEU A CG  
869  C  CD1 . LEU A 100 ? 0.2558 0.5408 0.4214 0.2041  -0.0443 -0.0183 100 LEU A CD1 
870  C  CD2 . LEU A 100 ? 0.4553 0.1820 0.4417 0.0295  0.2360  -0.0772 100 LEU A CD2 
871  N  N   . ASP A 101 ? 0.1351 0.0816 0.1773 -0.0060 0.0027  -0.0206 101 ASP A N   
872  C  CA  . ASP A 101 ? 0.1507 0.0835 0.1674 -0.0173 0.0054  -0.0017 101 ASP A CA  
873  C  C   . ASP A 101 ? 0.1430 0.0766 0.1554 0.0003  0.0151  -0.0131 101 ASP A C   
874  O  O   . ASP A 101 ? 0.1789 0.0961 0.1696 0.0252  0.0087  0.0015  101 ASP A O   
875  C  CB  . ASP A 101 ? 0.1719 0.0842 0.1917 -0.0204 -0.0173 -0.0052 101 ASP A CB  
876  C  CG  . ASP A 101 ? 0.1482 0.1045 0.2214 -0.0201 -0.0430 0.0024  101 ASP A CG  
877  O  OD1 . ASP A 101 ? 0.2177 0.1140 0.1884 -0.0137 -0.0164 0.0049  101 ASP A OD1 
878  O  OD2 . ASP A 101 ? 0.2247 0.1701 0.2545 -0.0938 -0.0529 0.0032  101 ASP A OD2 
879  N  N   . GLY A 102 ? 0.1616 0.0751 0.1847 -0.0024 -0.0110 0.0109  102 GLY A N   
880  C  CA  . GLY A 102 ? 0.1451 0.0623 0.1965 0.0049  -0.0035 0.0082  102 GLY A CA  
881  C  C   . GLY A 102 ? 0.1460 0.0703 0.1536 0.0152  0.0046  0.0104  102 GLY A C   
882  O  O   . GLY A 102 ? 0.1624 0.0781 0.1658 0.0040  0.0102  0.0175  102 GLY A O   
883  N  N   . GLN A 103 ? 0.1228 0.0600 0.1563 -0.0027 0.0043  0.0000  103 GLN A N   
884  C  CA  . GLN A 103 ? 0.1247 0.0676 0.1354 0.0149  -0.0171 -0.0137 103 GLN A CA  
885  C  C   . GLN A 103 ? 0.1009 0.0593 0.1377 -0.0019 0.0021  -0.0049 103 GLN A C   
886  O  O   . GLN A 103 ? 0.1194 0.0710 0.1292 0.0019  0.0051  -0.0162 103 GLN A O   
887  C  CB  . GLN A 103 ? 0.1211 0.0945 0.1668 0.0241  0.0089  0.0057  103 GLN A CB  
888  C  CG  . GLN A 103 ? 0.1365 0.1189 0.1753 0.0280  0.0155  -0.0157 103 GLN A CG  
889  C  CD  . GLN A 103 ? 0.1846 0.1061 0.2101 0.0406  0.0366  0.0272  103 GLN A CD  
890  O  OE1 . GLN A 103 ? 0.2363 0.2698 0.3955 0.1564  0.1250  0.1750  103 GLN A OE1 
891  N  NE2 . GLN A 103 ? 0.1507 0.1426 0.2545 0.0245  0.0300  0.0232  103 GLN A NE2 
892  N  N   . GLY A 104 ? 0.0934 0.0591 0.1214 0.0051  0.0110  -0.0046 104 GLY A N   
893  C  CA  . GLY A 104 ? 0.1047 0.0566 0.1063 0.0074  -0.0021 -0.0024 104 GLY A CA  
894  C  C   . GLY A 104 ? 0.0966 0.0606 0.1261 0.0059  -0.0055 -0.0023 104 GLY A C   
895  O  O   . GLY A 104 ? 0.0968 0.0709 0.1308 -0.0055 -0.0068 0.0052  104 GLY A O   
896  N  N   . SER A 105 ? 0.0790 0.0777 0.1017 -0.0035 -0.0003 -0.0115 105 SER A N   
897  C  CA  . SER A 105 ? 0.0830 0.0634 0.1137 0.0000  -0.0035 -0.0135 105 SER A CA  
898  C  C   . SER A 105 ? 0.0716 0.0627 0.1094 -0.0038 0.0010  -0.0062 105 SER A C   
899  O  O   . SER A 105 ? 0.0986 0.0615 0.1263 0.0104  -0.0197 -0.0109 105 SER A O   
900  C  CB  . SER A 105 ? 0.0859 0.0709 0.1074 -0.0052 0.0013  0.0073  105 SER A CB  
901  O  OG  . SER A 105 ? 0.0952 0.0617 0.1171 -0.0054 0.0081  0.0035  105 SER A OG  
902  N  N   . GLU A 106 ? 0.0808 0.0654 0.1000 -0.0059 -0.0071 -0.0148 106 GLU A N   
903  C  CA  . GLU A 106 ? 0.0824 0.0671 0.0996 -0.0054 -0.0118 -0.0096 106 GLU A CA  
904  C  C   . GLU A 106 ? 0.0860 0.0601 0.1150 -0.0094 -0.0055 -0.0054 106 GLU A C   
905  O  O   . GLU A 106 ? 0.0878 0.0714 0.1147 0.0110  -0.0113 -0.0115 106 GLU A O   
906  C  CB  . GLU A 106 ? 0.0991 0.0586 0.1063 -0.0086 -0.0041 -0.0031 106 GLU A CB  
907  C  CG  . GLU A 106 ? 0.1448 0.0771 0.1259 -0.0113 0.0318  -0.0127 106 GLU A CG  
908  C  CD  . GLU A 106 ? 0.0793 0.0719 0.1291 -0.0066 0.0003  -0.0217 106 GLU A CD  
909  O  OE1 . GLU A 106 ? 0.0793 0.0733 0.1282 -0.0030 -0.0063 -0.0089 106 GLU A OE1 
910  O  OE2 . GLU A 106 ? 0.0865 0.0857 0.1575 0.0043  0.0091  -0.0232 106 GLU A OE2 
911  N  N   . HIS A 107 ? 0.0771 0.0632 0.1029 -0.0026 -0.0066 0.0015  107 HIS A N   
912  C  CA  . HIS A 107 ? 0.0892 0.0578 0.0961 0.0185  -0.0051 -0.0041 107 HIS A CA  
913  C  C   . HIS A 107 ? 0.0714 0.0703 0.0973 0.0142  -0.0065 0.0006  107 HIS A C   
914  O  O   . HIS A 107 ? 0.0777 0.0706 0.1061 0.0066  -0.0041 -0.0026 107 HIS A O   
915  C  CB  . HIS A 107 ? 0.0843 0.0582 0.1120 0.0142  -0.0034 -0.0087 107 HIS A CB  
916  C  CG  . HIS A 107 ? 0.0599 0.0681 0.1054 0.0258  -0.0080 -0.0063 107 HIS A CG  
917  N  ND1 . HIS A 107 ? 0.0864 0.0527 0.1128 0.0156  -0.0132 0.0024  107 HIS A ND1 
918  C  CD2 . HIS A 107 ? 0.0736 0.0586 0.1142 0.0342  -0.0159 -0.0113 107 HIS A CD2 
919  C  CE1 . HIS A 107 ? 0.0842 0.0615 0.1124 0.0258  -0.0248 -0.0119 107 HIS A CE1 
920  N  NE2 . HIS A 107 ? 0.0754 0.0732 0.1177 0.0194  -0.0179 -0.0141 107 HIS A NE2 
921  N  N   . THR A 108 ? 0.0995 0.0603 0.1045 0.0137  -0.0010 0.0038  108 THR A N   
922  C  CA  . THR A 108 ? 0.1031 0.0502 0.1226 0.0214  0.0010  0.0055  108 THR A CA  
923  C  C   . THR A 108 ? 0.0939 0.0659 0.1114 0.0116  -0.0253 -0.0003 108 THR A C   
924  O  O   . THR A 108 ? 0.1002 0.0701 0.1088 0.0114  -0.0171 -0.0035 108 THR A O   
925  C  CB  . THR A 108 ? 0.0984 0.0993 0.1196 0.0272  -0.0172 -0.0093 108 THR A CB  
926  O  OG1 . THR A 108 ? 0.1223 0.0797 0.1226 0.0230  -0.0331 -0.0052 108 THR A OG1 
927  C  CG2 . THR A 108 ? 0.0744 0.1129 0.1247 0.0222  -0.0100 -0.0046 108 THR A CG2 
928  N  N   . VAL A 109 ? 0.1132 0.0571 0.1214 0.0046  -0.0155 0.0081  109 VAL A N   
929  C  CA  . VAL A 109 ? 0.1135 0.0698 0.1178 -0.0155 -0.0109 0.0230  109 VAL A CA  
930  C  C   . VAL A 109 ? 0.1035 0.0688 0.1302 -0.0060 -0.0003 0.0102  109 VAL A C   
931  O  O   . VAL A 109 ? 0.1126 0.0688 0.1378 -0.0019 -0.0070 0.0177  109 VAL A O   
932  C  CB  . VAL A 109 ? 0.0959 0.0776 0.1412 0.0037  -0.0165 0.0071  109 VAL A CB  
933  C  CG1 . VAL A 109 ? 0.1162 0.1119 0.1656 0.0001  0.0164  0.0237  109 VAL A CG1 
934  C  CG2 . VAL A 109 ? 0.1275 0.0874 0.1561 0.0208  -0.0225 0.0157  109 VAL A CG2 
935  N  N   . ASP A 110 ? 0.1401 0.1022 0.1123 0.0258  0.0026  0.0248  110 ASP A N   
936  C  CA  . ASP A 110 ? 0.1557 0.0891 0.1187 0.0286  0.0065  0.0266  110 ASP A CA  
937  C  C   . ASP A 110 ? 0.1663 0.0747 0.1241 0.0136  -0.0013 0.0115  110 ASP A C   
938  O  O   . ASP A 110 ? 0.1713 0.0731 0.1448 0.0126  -0.0103 0.0199  110 ASP A O   
939  C  CB  . ASP A 110 ? 0.2012 0.1146 0.1512 0.0247  0.0410  0.0441  110 ASP A CB  
940  C  CG  . ASP A 110 ? 0.2161 0.1527 0.1615 0.0337  0.0395  0.0537  110 ASP A CG  
941  O  OD1 . ASP A 110 ? 0.2436 0.1342 0.1983 0.0348  0.0483  0.0373  110 ASP A OD1 
942  O  OD2 . ASP A 110 ? 0.2019 0.1924 0.1994 0.0211  0.0120  0.0093  110 ASP A OD2 
943  N  N   . LYS A 111 ? 0.1327 0.0912 0.1176 0.0157  -0.0148 0.0161  111 LYS A N   
944  C  CA  . LYS A 111 ? 0.1417 0.0877 0.1239 0.0337  -0.0219 0.0142  111 LYS A CA  
945  C  C   . LYS A 111 ? 0.1450 0.0628 0.1261 0.0127  -0.0131 0.0173  111 LYS A C   
946  O  O   . LYS A 111 ? 0.1345 0.1068 0.1510 0.0133  -0.0015 -0.0043 111 LYS A O   
947  C  CB  . LYS A 111 ? 0.1541 0.1430 0.1552 0.0491  -0.0277 0.0300  111 LYS A CB  
948  C  CG  . LYS A 111 ? 0.2321 0.1555 0.1920 0.0662  -0.0648 0.0078  111 LYS A CG  
949  C  CD  . LYS A 111 ? 0.2134 0.2078 0.2635 0.0434  -0.1138 -0.0571 111 LYS A CD  
950  C  CE  . LYS A 111 ? 0.3050 0.2736 0.2727 0.0756  -0.1442 -0.0559 111 LYS A CE  
951  N  NZ  . LYS A 111 ? 0.2495 0.3470 0.2834 0.0527  -0.0926 0.0560  111 LYS A NZ  
952  N  N   . LYS A 112 ? 0.1345 0.0653 0.1221 0.0136  -0.0094 0.0137  112 LYS A N   
953  C  CA  . LYS A 112 ? 0.1257 0.0921 0.1193 -0.0007 -0.0082 -0.0031 112 LYS A CA  
954  C  C   . LYS A 112 ? 0.1041 0.0640 0.1304 0.0111  -0.0186 -0.0049 112 LYS A C   
955  O  O   . LYS A 112 ? 0.1256 0.0617 0.1189 0.0066  -0.0077 -0.0091 112 LYS A O   
956  C  CB  . LYS A 112 ? 0.1256 0.0968 0.1570 -0.0068 -0.0126 -0.0087 112 LYS A CB  
957  C  CG  . LYS A 112 ? 0.1137 0.1385 0.1498 -0.0214 0.0031  -0.0364 112 LYS A CG  
958  C  CD  . LYS A 112 ? 0.1144 0.1890 0.1757 -0.0074 -0.0227 -0.0017 112 LYS A CD  
959  C  CE  . LYS A 112 ? 0.1625 0.1203 0.2041 -0.0104 -0.0408 -0.0221 112 LYS A CE  
960  N  NZ  . LYS A 112 ? 0.1760 0.1256 0.1978 0.0062  -0.0203 0.0187  112 LYS A NZ  
961  N  N   A LYS A 113 ? 0.1049 0.0763 0.1129 0.0219  -0.0185 0.0071  113 LYS A N   
962  N  N   B LYS A 113 ? 0.1059 0.0781 0.1142 0.0203  -0.0160 0.0065  113 LYS A N   
963  C  CA  A LYS A 113 ? 0.0996 0.0715 0.1238 0.0148  -0.0131 0.0082  113 LYS A CA  
964  C  CA  B LYS A 113 ? 0.1005 0.0700 0.1238 0.0141  -0.0124 0.0049  113 LYS A CA  
965  C  C   A LYS A 113 ? 0.1072 0.0502 0.1277 0.0070  -0.0038 0.0115  113 LYS A C   
966  C  C   B LYS A 113 ? 0.1062 0.0502 0.1280 0.0082  -0.0038 0.0109  113 LYS A C   
967  O  O   A LYS A 113 ? 0.1642 0.0398 0.1676 0.0115  -0.0271 0.0054  113 LYS A O   
968  O  O   B LYS A 113 ? 0.1653 0.0424 0.1683 0.0127  -0.0322 0.0021  113 LYS A O   
969  C  CB  A LYS A 113 ? 0.1022 0.0797 0.1347 0.0114  -0.0080 0.0037  113 LYS A CB  
970  C  CB  B LYS A 113 ? 0.1011 0.0870 0.1353 0.0109  -0.0074 0.0023  113 LYS A CB  
971  C  CG  A LYS A 113 ? 0.0966 0.1196 0.1527 0.0164  -0.0136 0.0020  113 LYS A CG  
972  C  CG  B LYS A 113 ? 0.0959 0.1187 0.1523 0.0160  -0.0130 0.0027  113 LYS A CG  
973  C  CD  A LYS A 113 ? 0.0813 0.1324 0.2232 0.0078  0.0020  -0.0119 113 LYS A CD  
974  C  CD  B LYS A 113 ? 0.0887 0.1177 0.2326 0.0194  0.0005  -0.0131 113 LYS A CD  
975  C  CE  A LYS A 113 ? 0.0790 0.1631 0.2745 0.0076  -0.0196 -0.0133 113 LYS A CE  
976  C  CE  B LYS A 113 ? 0.0843 0.1990 0.2657 -0.0031 -0.0115 -0.0138 113 LYS A CE  
977  N  NZ  A LYS A 113 ? 0.0725 0.2169 0.2653 0.0421  -0.0461 -0.0234 113 LYS A NZ  
978  N  NZ  B LYS A 113 ? 0.1241 0.2328 0.3125 0.0405  -0.0353 -0.0535 113 LYS A NZ  
979  N  N   . TYR A 114 ? 0.0930 0.0511 0.1230 0.0021  -0.0165 0.0017  114 TYR A N   
980  C  CA  . TYR A 114 ? 0.1097 0.0715 0.1153 0.0013  -0.0196 0.0043  114 TYR A CA  
981  C  C   . TYR A 114 ? 0.0959 0.0476 0.1270 0.0078  -0.0109 -0.0082 114 TYR A C   
982  O  O   . TYR A 114 ? 0.0846 0.0873 0.1232 -0.0023 -0.0015 -0.0070 114 TYR A O   
983  C  CB  . TYR A 114 ? 0.0876 0.0714 0.1284 0.0085  -0.0159 0.0043  114 TYR A CB  
984  C  CG  . TYR A 114 ? 0.0997 0.0542 0.1261 0.0126  -0.0126 0.0147  114 TYR A CG  
985  C  CD1 . TYR A 114 ? 0.1331 0.0648 0.1449 0.0221  0.0000  0.0081  114 TYR A CD1 
986  C  CD2 . TYR A 114 ? 0.0844 0.0733 0.1713 0.0086  0.0034  0.0129  114 TYR A CD2 
987  C  CE1 . TYR A 114 ? 0.1717 0.0943 0.1432 0.0212  0.0109  0.0173  114 TYR A CE1 
988  C  CE2 . TYR A 114 ? 0.1142 0.1067 0.1889 0.0071  0.0133  0.0226  114 TYR A CE2 
989  C  CZ  . TYR A 114 ? 0.1498 0.1056 0.1757 0.0082  0.0337  0.0132  114 TYR A CZ  
990  O  OH  . TYR A 114 ? 0.1974 0.1868 0.2143 -0.0081 0.0729  -0.0092 114 TYR A OH  
991  N  N   . ALA A 115 ? 0.1068 0.0599 0.1120 -0.0098 -0.0221 0.0010  115 ALA A N   
992  C  CA  . ALA A 115 ? 0.1151 0.0564 0.1096 0.0028  -0.0052 -0.0041 115 ALA A CA  
993  C  C   . ALA A 115 ? 0.1203 0.0641 0.1053 -0.0098 -0.0060 -0.0120 115 ALA A C   
994  O  O   . ALA A 115 ? 0.1151 0.0656 0.1264 -0.0121 0.0013  -0.0099 115 ALA A O   
995  C  CB  . ALA A 115 ? 0.1460 0.0693 0.1377 -0.0225 -0.0195 -0.0054 115 ALA A CB  
996  N  N   . ALA A 116 ? 0.1023 0.0480 0.1105 0.0031  -0.0035 0.0030  116 ALA A N   
997  C  CA  . ALA A 116 ? 0.1056 0.0527 0.1001 -0.0078 -0.0046 0.0003  116 ALA A CA  
998  C  C   . ALA A 116 ? 0.1023 0.0643 0.0896 0.0006  -0.0043 0.0081  116 ALA A C   
999  O  O   . ALA A 116 ? 0.0938 0.0631 0.1013 -0.0049 -0.0059 0.0046  116 ALA A O   
1000 C  CB  . ALA A 116 ? 0.1268 0.0764 0.1038 -0.0052 -0.0148 0.0007  116 ALA A CB  
1001 N  N   . GLU A 117 ? 0.1099 0.0416 0.1044 -0.0007 -0.0114 -0.0008 117 GLU A N   
1002 C  CA  . GLU A 117 ? 0.1072 0.0379 0.0907 -0.0027 -0.0147 -0.0052 117 GLU A CA  
1003 C  C   . GLU A 117 ? 0.1194 0.0646 0.0798 -0.0104 -0.0104 -0.0035 117 GLU A C   
1004 O  O   . GLU A 117 ? 0.1023 0.0879 0.1135 0.0119  0.0019  0.0230  117 GLU A O   
1005 C  CB  . GLU A 117 ? 0.0975 0.0741 0.0962 -0.0037 -0.0024 -0.0003 117 GLU A CB  
1006 C  CG  . GLU A 117 ? 0.0998 0.0747 0.1077 0.0035  -0.0166 -0.0038 117 GLU A CG  
1007 C  CD  . GLU A 117 ? 0.0804 0.0675 0.0998 0.0080  -0.0008 -0.0051 117 GLU A CD  
1008 O  OE1 . GLU A 117 ? 0.0869 0.0802 0.1196 0.0163  -0.0109 -0.0097 117 GLU A OE1 
1009 O  OE2 . GLU A 117 ? 0.1036 0.0750 0.1074 0.0028  -0.0208 -0.0070 117 GLU A OE2 
1010 N  N   . LEU A 118 ? 0.0966 0.0564 0.0912 -0.0031 -0.0244 -0.0003 118 LEU A N   
1011 C  CA  . LEU A 118 ? 0.1089 0.0557 0.0863 0.0001  -0.0300 0.0034  118 LEU A CA  
1012 C  C   . LEU A 118 ? 0.0988 0.0588 0.0914 -0.0120 -0.0175 -0.0027 118 LEU A C   
1013 O  O   . LEU A 118 ? 0.0873 0.0562 0.0869 -0.0006 -0.0097 -0.0054 118 LEU A O   
1014 C  CB  . LEU A 118 ? 0.1311 0.0590 0.1072 0.0071  -0.0176 0.0049  118 LEU A CB  
1015 C  CG  . LEU A 118 ? 0.1011 0.0781 0.1230 0.0194  -0.0324 0.0262  118 LEU A CG  
1016 C  CD1 . LEU A 118 ? 0.1577 0.0556 0.1144 0.0054  -0.0399 0.0178  118 LEU A CD1 
1017 C  CD2 . LEU A 118 ? 0.1110 0.1099 0.1398 0.0097  -0.0348 0.0074  118 LEU A CD2 
1018 N  N   . HIS A 119 ? 0.1092 0.0384 0.0982 -0.0028 -0.0225 -0.0027 119 HIS A N   
1019 C  CA  . HIS A 119 ? 0.0866 0.0454 0.0935 -0.0082 -0.0170 -0.0001 119 HIS A CA  
1020 C  C   . HIS A 119 ? 0.0975 0.0494 0.0777 -0.0174 -0.0184 0.0100  119 HIS A C   
1021 O  O   . HIS A 119 ? 0.1160 0.0573 0.0923 0.0027  -0.0141 0.0108  119 HIS A O   
1022 C  CB  . HIS A 119 ? 0.0900 0.0535 0.1042 0.0049  -0.0110 0.0030  119 HIS A CB  
1023 C  CG  . HIS A 119 ? 0.0850 0.0590 0.0813 -0.0031 -0.0051 -0.0082 119 HIS A CG  
1024 N  ND1 . HIS A 119 ? 0.0788 0.0586 0.0917 -0.0121 0.0038  0.0035  119 HIS A ND1 
1025 C  CD2 . HIS A 119 ? 0.0878 0.0606 0.0979 0.0043  -0.0138 -0.0015 119 HIS A CD2 
1026 C  CE1 . HIS A 119 ? 0.0984 0.0722 0.0917 -0.0051 -0.0059 -0.0060 119 HIS A CE1 
1027 N  NE2 . HIS A 119 ? 0.0832 0.0667 0.0984 0.0070  -0.0155 0.0068  119 HIS A NE2 
1028 N  N   . LEU A 120 ? 0.0885 0.0442 0.0977 -0.0038 -0.0187 -0.0063 120 LEU A N   
1029 C  CA  . LEU A 120 ? 0.0965 0.0474 0.1191 0.0000  -0.0287 0.0010  120 LEU A CA  
1030 C  C   . LEU A 120 ? 0.0764 0.0481 0.0939 0.0133  -0.0093 0.0010  120 LEU A C   
1031 O  O   . LEU A 120 ? 0.0825 0.0573 0.1002 -0.0026 -0.0108 -0.0013 120 LEU A O   
1032 C  CB  . LEU A 120 ? 0.0886 0.0542 0.1352 0.0060  -0.0313 -0.0054 120 LEU A CB  
1033 C  CG  . LEU A 120 ? 0.1190 0.0848 0.1337 -0.0240 -0.0482 0.0006  120 LEU A CG  
1034 C  CD1 . LEU A 120 ? 0.2049 0.1033 0.1606 -0.0684 -0.0335 0.0054  120 LEU A CD1 
1035 C  CD2 . LEU A 120 ? 0.1471 0.1099 0.1512 0.0125  -0.0759 -0.0116 120 LEU A CD2 
1036 N  N   . VAL A 121 ? 0.0839 0.0559 0.1005 -0.0096 -0.0173 0.0046  121 VAL A N   
1037 C  CA  . VAL A 121 ? 0.0973 0.0477 0.1102 -0.0031 -0.0185 0.0104  121 VAL A CA  
1038 C  C   . VAL A 121 ? 0.0847 0.0487 0.1065 -0.0068 -0.0153 -0.0010 121 VAL A C   
1039 O  O   . VAL A 121 ? 0.1153 0.0575 0.0995 0.0054  -0.0107 0.0096  121 VAL A O   
1040 C  CB  . VAL A 121 ? 0.1040 0.0455 0.1230 -0.0135 -0.0010 -0.0081 121 VAL A CB  
1041 C  CG1 . VAL A 121 ? 0.1137 0.0856 0.1286 -0.0241 -0.0124 -0.0048 121 VAL A CG1 
1042 C  CG2 . VAL A 121 ? 0.1171 0.0680 0.1207 0.0099  -0.0017 0.0037  121 VAL A CG2 
1043 N  N   . HIS A 122 ? 0.0948 0.0491 0.1022 -0.0015 -0.0142 -0.0068 122 HIS A N   
1044 C  CA  . HIS A 122 ? 0.0961 0.0525 0.1124 0.0015  -0.0114 -0.0010 122 HIS A CA  
1045 C  C   . HIS A 122 ? 0.1062 0.0557 0.1084 0.0109  -0.0082 0.0026  122 HIS A C   
1046 O  O   . HIS A 122 ? 0.1180 0.0529 0.1264 -0.0049 -0.0239 0.0013  122 HIS A O   
1047 C  CB  . HIS A 122 ? 0.1040 0.0483 0.1333 0.0006  -0.0091 -0.0094 122 HIS A CB  
1048 C  CG  . HIS A 122 ? 0.0820 0.0575 0.1172 0.0032  -0.0024 -0.0020 122 HIS A CG  
1049 N  ND1 . HIS A 122 ? 0.0860 0.0568 0.1353 0.0017  -0.0115 0.0057  122 HIS A ND1 
1050 C  CD2 . HIS A 122 ? 0.1040 0.0847 0.1180 -0.0063 -0.0232 -0.0001 122 HIS A CD2 
1051 C  CE1 . HIS A 122 ? 0.0857 0.0901 0.1403 -0.0020 -0.0124 -0.0108 122 HIS A CE1 
1052 N  NE2 . HIS A 122 ? 0.0948 0.0841 0.1467 -0.0032 -0.0216 -0.0015 122 HIS A NE2 
1053 N  N   . TRP A 123 ? 0.0984 0.0511 0.1203 0.0005  -0.0165 -0.0051 123 TRP A N   
1054 C  CA  . TRP A 123 ? 0.1117 0.0540 0.1132 0.0006  -0.0113 -0.0111 123 TRP A CA  
1055 C  C   . TRP A 123 ? 0.0804 0.0652 0.1185 0.0081  -0.0044 0.0032  123 TRP A C   
1056 O  O   . TRP A 123 ? 0.0891 0.0574 0.1489 0.0031  -0.0175 -0.0142 123 TRP A O   
1057 C  CB  . TRP A 123 ? 0.1169 0.1040 0.1252 -0.0233 -0.0063 -0.0003 123 TRP A CB  
1058 C  CG  . TRP A 123 ? 0.1290 0.0663 0.1340 -0.0197 0.0098  -0.0063 123 TRP A CG  
1059 C  CD1 . TRP A 123 ? 0.1435 0.0873 0.1223 -0.0153 -0.0054 -0.0003 123 TRP A CD1 
1060 C  CD2 . TRP A 123 ? 0.1832 0.0544 0.1239 -0.0222 0.0098  -0.0020 123 TRP A CD2 
1061 N  NE1 . TRP A 123 ? 0.1996 0.0599 0.1473 -0.0125 -0.0201 -0.0040 123 TRP A NE1 
1062 C  CE2 . TRP A 123 ? 0.1915 0.0608 0.1401 -0.0153 -0.0073 0.0001  123 TRP A CE2 
1063 C  CE3 . TRP A 123 ? 0.1753 0.0522 0.1428 -0.0249 0.0132  -0.0080 123 TRP A CE3 
1064 C  CZ2 . TRP A 123 ? 0.2217 0.0574 0.1780 -0.0027 0.0122  0.0065  123 TRP A CZ2 
1065 C  CZ3 . TRP A 123 ? 0.2526 0.0525 0.1629 -0.0214 0.0141  -0.0015 123 TRP A CZ3 
1066 C  CH2 . TRP A 123 ? 0.2615 0.0574 0.1659 -0.0108 0.0087  0.0091  123 TRP A CH2 
1067 N  N   . ASN A 124 ? 0.0968 0.0578 0.1306 0.0065  -0.0098 -0.0168 124 ASN A N   
1068 C  CA  . ASN A 124 ? 0.1270 0.0595 0.1232 0.0187  -0.0098 -0.0187 124 ASN A CA  
1069 C  C   . ASN A 124 ? 0.0988 0.0688 0.1333 0.0160  -0.0065 -0.0223 124 ASN A C   
1070 O  O   . ASN A 124 ? 0.1098 0.0795 0.1358 0.0060  -0.0003 -0.0126 124 ASN A O   
1071 C  CB  . ASN A 124 ? 0.1162 0.0799 0.1259 0.0155  -0.0020 -0.0105 124 ASN A CB  
1072 C  CG  . ASN A 124 ? 0.1272 0.0600 0.1331 0.0027  -0.0041 -0.0071 124 ASN A CG  
1073 O  OD1 . ASN A 124 ? 0.1331 0.0766 0.1511 0.0229  0.0001  -0.0141 124 ASN A OD1 
1074 N  ND2 . ASN A 124 ? 0.1832 0.0842 0.1331 0.0043  -0.0089 -0.0149 124 ASN A ND2 
1075 N  N   . THR A 125 ? 0.1085 0.0710 0.1521 0.0263  -0.0142 -0.0063 125 THR A N   
1076 C  CA  . THR A 125 ? 0.1259 0.0560 0.1864 0.0195  -0.0017 0.0006  125 THR A CA  
1077 C  C   . THR A 125 ? 0.1448 0.0636 0.1823 0.0388  0.0015  0.0006  125 THR A C   
1078 O  O   . THR A 125 ? 0.1744 0.0663 0.1918 0.0184  -0.0114 0.0124  125 THR A O   
1079 C  CB  . THR A 125 ? 0.1162 0.1077 0.2326 0.0293  -0.0234 0.0177  125 THR A CB  
1080 O  OG1 . THR A 125 ? 0.1681 0.1495 0.3289 0.0577  0.0674  0.0234  125 THR A OG1 
1081 C  CG2 . THR A 125 ? 0.1473 0.1337 0.2777 0.0006  -0.0852 -0.0046 125 THR A CG2 
1082 N  N   . LYS A 126 ? 0.1466 0.0527 0.1746 0.0147  0.0099  -0.0258 127 LYS A N   
1083 C  CA  . LYS A 126 ? 0.1785 0.0821 0.1649 -0.0015 0.0251  -0.0397 127 LYS A CA  
1084 C  C   . LYS A 126 ? 0.1784 0.0477 0.1642 0.0126  -0.0008 -0.0109 127 LYS A C   
1085 O  O   . LYS A 126 ? 0.2078 0.0674 0.1918 -0.0143 0.0153  -0.0328 127 LYS A O   
1086 C  CB  . LYS A 126 ? 0.2213 0.1270 0.1656 -0.0179 0.0113  -0.0447 127 LYS A CB  
1087 C  CG  . LYS A 126 ? 0.2195 0.1248 0.1629 -0.0285 0.0028  -0.0120 127 LYS A CG  
1088 C  CD  . LYS A 126 ? 0.3513 0.1724 0.1760 -0.0540 0.0216  -0.0342 127 LYS A CD  
1089 C  CE  . LYS A 126 ? 0.4765 0.2056 0.2827 -0.0467 -0.0428 -0.0197 127 LYS A CE  
1090 N  NZ  . LYS A 126 ? 0.9372 0.4124 0.1889 -0.2734 -0.0763 0.0310  127 LYS A NZ  
1091 N  N   . TYR A 127 ? 0.1509 0.0656 0.1487 0.0027  -0.0034 -0.0137 128 TYR A N   
1092 C  CA  . TYR A 127 ? 0.1622 0.0533 0.1398 0.0024  -0.0133 -0.0116 128 TYR A CA  
1093 C  C   . TYR A 127 ? 0.1537 0.0653 0.1615 -0.0065 -0.0038 -0.0297 128 TYR A C   
1094 O  O   . TYR A 127 ? 0.1676 0.0794 0.1507 0.0055  0.0052  -0.0113 128 TYR A O   
1095 C  CB  . TYR A 127 ? 0.1598 0.0681 0.1692 0.0073  0.0027  -0.0038 128 TYR A CB  
1096 C  CG  . TYR A 127 ? 0.1552 0.0609 0.1568 0.0171  -0.0138 -0.0038 128 TYR A CG  
1097 C  CD1 . TYR A 127 ? 0.1424 0.0785 0.1708 0.0038  -0.0209 -0.0148 128 TYR A CD1 
1098 C  CD2 . TYR A 127 ? 0.1205 0.0702 0.1505 0.0177  -0.0160 -0.0099 128 TYR A CD2 
1099 C  CE1 . TYR A 127 ? 0.1746 0.0935 0.1625 0.0065  -0.0282 -0.0289 128 TYR A CE1 
1100 C  CE2 . TYR A 127 ? 0.1448 0.0780 0.1394 0.0078  -0.0027 -0.0253 128 TYR A CE2 
1101 C  CZ  . TYR A 127 ? 0.1298 0.1144 0.1618 0.0089  -0.0167 -0.0348 128 TYR A CZ  
1102 O  OH  . TYR A 127 ? 0.1981 0.1042 0.1696 0.0252  -0.0348 -0.0392 128 TYR A OH  
1103 N  N   . GLY A 128 ? 0.1604 0.0663 0.1495 -0.0080 -0.0230 0.0115  129 GLY A N   
1104 C  CA  . GLY A 128 ? 0.2023 0.0658 0.1527 -0.0194 0.0114  -0.0048 129 GLY A CA  
1105 C  C   . GLY A 128 ? 0.2098 0.0648 0.1374 0.0144  -0.0098 0.0133  129 GLY A C   
1106 O  O   . GLY A 128 ? 0.2305 0.0740 0.1712 -0.0057 -0.0238 0.0178  129 GLY A O   
1107 N  N   . ASP A 129 ? 0.2166 0.0702 0.1351 0.0203  -0.0074 -0.0066 130 ASP A N   
1108 C  CA  . ASP A 129 ? 0.2398 0.0742 0.1356 0.0060  0.0041  -0.0109 130 ASP A CA  
1109 C  C   . ASP A 129 ? 0.2073 0.0659 0.1317 0.0031  0.0031  0.0026  130 ASP A C   
1110 O  O   . ASP A 129 ? 0.2549 0.0861 0.1257 0.0189  -0.0087 -0.0190 130 ASP A O   
1111 C  CB  . ASP A 129 ? 0.2484 0.1602 0.1841 0.0115  0.0505  0.0219  130 ASP A CB  
1112 C  CG  . ASP A 129 ? 0.2441 0.0916 0.1848 0.0551  0.0465  0.0237  130 ASP A CG  
1113 O  OD1 . ASP A 129 ? 0.3016 0.1552 0.2804 -0.0712 -0.0834 -0.0131 130 ASP A OD1 
1114 O  OD2 . ASP A 129 ? 0.2903 0.1543 0.2971 -0.0068 0.1187  0.0109  130 ASP A OD2 
1115 N  N   . PHE A 130 ? 0.2335 0.0516 0.1316 0.0057  -0.0010 -0.0066 131 PHE A N   
1116 C  CA  . PHE A 130 ? 0.1647 0.0830 0.1324 0.0063  -0.0110 -0.0065 131 PHE A CA  
1117 C  C   . PHE A 130 ? 0.1794 0.0822 0.1363 -0.0148 0.0248  -0.0115 131 PHE A C   
1118 O  O   . PHE A 130 ? 0.1681 0.0920 0.1298 -0.0181 0.0142  -0.0068 131 PHE A O   
1119 C  CB  . PHE A 130 ? 0.1789 0.0706 0.1451 -0.0010 -0.0142 -0.0274 131 PHE A CB  
1120 C  CG  . PHE A 130 ? 0.1519 0.0746 0.1356 0.0103  0.0023  -0.0210 131 PHE A CG  
1121 C  CD1 . PHE A 130 ? 0.1730 0.0961 0.1270 -0.0091 -0.0104 -0.0057 131 PHE A CD1 
1122 C  CD2 . PHE A 130 ? 0.1993 0.0964 0.1620 -0.0080 0.0086  -0.0187 131 PHE A CD2 
1123 C  CE1 . PHE A 130 ? 0.2004 0.0947 0.1695 -0.0151 -0.0185 0.0035  131 PHE A CE1 
1124 C  CE2 . PHE A 130 ? 0.2254 0.1317 0.1699 0.0311  0.0017  -0.0244 131 PHE A CE2 
1125 C  CZ  . PHE A 130 ? 0.1963 0.1462 0.1747 0.0126  -0.0311 0.0007  131 PHE A CZ  
1126 N  N   . GLY A 131 ? 0.2145 0.1126 0.1545 -0.0328 0.0659  -0.0148 132 GLY A N   
1127 C  CA  . GLY A 131 ? 0.2075 0.1286 0.1512 -0.0436 0.0645  -0.0008 132 GLY A CA  
1128 C  C   . GLY A 131 ? 0.1773 0.1326 0.1688 -0.0364 0.0544  0.0043  132 GLY A C   
1129 O  O   . GLY A 131 ? 0.1615 0.1119 0.2401 -0.0362 0.0333  -0.0436 132 GLY A O   
1130 N  N   A LYS A 132 ? 0.1708 0.0943 0.1805 -0.0233 0.0299  -0.0023 133 LYS A N   
1131 N  N   B LYS A 132 ? 0.1699 0.0948 0.1801 -0.0249 0.0306  -0.0024 133 LYS A N   
1132 C  CA  A LYS A 132 ? 0.1768 0.0740 0.1846 -0.0142 0.0177  -0.0008 133 LYS A CA  
1133 C  CA  B LYS A 132 ? 0.1762 0.0772 0.1857 -0.0236 0.0198  -0.0026 133 LYS A CA  
1134 C  C   A LYS A 132 ? 0.1286 0.0604 0.1744 -0.0065 -0.0054 -0.0147 133 LYS A C   
1135 C  C   B LYS A 132 ? 0.1300 0.0615 0.1753 -0.0094 -0.0044 -0.0130 133 LYS A C   
1136 O  O   A LYS A 132 ? 0.1383 0.0856 0.1624 -0.0274 -0.0148 -0.0175 133 LYS A O   
1137 O  O   B LYS A 132 ? 0.1383 0.0988 0.1584 -0.0273 -0.0052 -0.0071 133 LYS A O   
1138 C  CB  A LYS A 132 ? 0.1710 0.0970 0.2056 0.0015  -0.0021 -0.0098 133 LYS A CB  
1139 C  CB  B LYS A 132 ? 0.1582 0.0724 0.2177 -0.0340 -0.0129 0.0060  133 LYS A CB  
1140 C  CG  A LYS A 132 ? 0.1796 0.0907 0.2739 0.0198  -0.0166 0.0329  133 LYS A CG  
1141 C  CG  B LYS A 132 ? 0.1730 0.1191 0.3598 -0.0869 -0.0362 0.0505  133 LYS A CG  
1142 C  CD  A LYS A 132 ? 0.1764 0.1115 0.5138 0.0408  -0.0653 0.0781  133 LYS A CD  
1143 C  CD  B LYS A 132 ? 0.2390 0.1106 0.5235 -0.0882 -0.1296 0.1220  133 LYS A CD  
1144 C  CE  A LYS A 132 ? 0.3201 0.3364 0.4962 -0.0368 -0.1572 -0.0313 133 LYS A CE  
1145 C  CE  B LYS A 132 ? 0.3084 0.3070 0.4160 -0.2124 -0.0463 0.1863  133 LYS A CE  
1146 N  NZ  A LYS A 132 ? 0.4336 0.3305 0.4587 -0.0979 -0.1040 -0.0368 133 LYS A NZ  
1147 N  NZ  B LYS A 132 ? 0.3093 0.2728 0.7286 -0.0944 -0.0980 0.2312  133 LYS A NZ  
1148 N  N   . ALA A 133 ? 0.1407 0.0833 0.1406 -0.0329 0.0065  -0.0111 134 ALA A N   
1149 C  CA  . ALA A 133 ? 0.1383 0.1103 0.1234 -0.0234 -0.0074 -0.0015 134 ALA A CA  
1150 C  C   . ALA A 133 ? 0.1306 0.1014 0.1162 -0.0310 0.0046  -0.0174 134 ALA A C   
1151 O  O   . ALA A 133 ? 0.1049 0.1138 0.1238 -0.0121 0.0019  -0.0098 134 ALA A O   
1152 C  CB  . ALA A 133 ? 0.1374 0.1135 0.1247 -0.0384 -0.0176 0.0032  134 ALA A CB  
1153 N  N   . VAL A 134 ? 0.1351 0.0828 0.1394 -0.0309 0.0116  -0.0127 135 VAL A N   
1154 C  CA  . VAL A 134 ? 0.1536 0.0778 0.1478 -0.0104 0.0234  0.0132  135 VAL A CA  
1155 C  C   . VAL A 134 ? 0.0993 0.1010 0.1923 -0.0178 0.0223  -0.0078 135 VAL A C   
1156 O  O   . VAL A 134 ? 0.1270 0.1225 0.1809 0.0154  0.0302  0.0000  135 VAL A O   
1157 C  CB  . VAL A 134 ? 0.1738 0.0948 0.1780 -0.0119 0.0467  -0.0131 135 VAL A CB  
1158 C  CG1 . VAL A 134 ? 0.2060 0.1705 0.1742 -0.0597 0.0133  -0.0223 135 VAL A CG1 
1159 C  CG2 . VAL A 134 ? 0.1692 0.1054 0.1911 -0.0154 0.0458  -0.0038 135 VAL A CG2 
1160 N  N   . GLN A 135 ? 0.1178 0.0954 0.1689 -0.0164 0.0237  -0.0068 136 GLN A N   
1161 C  CA  . GLN A 135 ? 0.1108 0.1035 0.2087 -0.0190 0.0027  -0.0148 136 GLN A CA  
1162 C  C   . GLN A 135 ? 0.1114 0.1111 0.1750 -0.0155 -0.0122 0.0054  136 GLN A C   
1163 O  O   . GLN A 135 ? 0.1216 0.1855 0.2166 -0.0283 -0.0168 -0.0296 136 GLN A O   
1164 C  CB  . GLN A 135 ? 0.1318 0.1261 0.2162 -0.0487 -0.0087 0.0017  136 GLN A CB  
1165 C  CG  . GLN A 135 ? 0.1572 0.1884 0.2416 -0.0593 0.0237  0.0292  136 GLN A CG  
1166 C  CD  . GLN A 135 ? 0.1722 0.2019 0.3140 -0.0399 0.0320  0.0017  136 GLN A CD  
1167 O  OE1 . GLN A 135 ? 0.2277 0.2784 0.4278 -0.0986 -0.0333 0.0421  136 GLN A OE1 
1168 N  NE2 . GLN A 135 ? 0.2119 0.2299 0.3632 -0.0032 0.0355  0.0857  136 GLN A NE2 
1169 N  N   . GLN A 136 ? 0.1089 0.1058 0.1660 -0.0008 0.0164  -0.0055 137 GLN A N   
1170 C  CA  . GLN A 136 ? 0.1336 0.1150 0.1313 -0.0109 -0.0186 -0.0122 137 GLN A CA  
1171 C  C   . GLN A 136 ? 0.0997 0.1151 0.1313 0.0133  -0.0065 -0.0230 137 GLN A C   
1172 O  O   . GLN A 136 ? 0.1299 0.0973 0.1264 0.0068  -0.0082 -0.0216 137 GLN A O   
1173 C  CB  . GLN A 136 ? 0.1378 0.1001 0.1658 0.0142  -0.0238 -0.0141 137 GLN A CB  
1174 C  CG  . GLN A 136 ? 0.2148 0.1146 0.2346 0.0317  0.0322  -0.0035 137 GLN A CG  
1175 C  CD  . GLN A 136 ? 0.1643 0.1347 0.3774 0.0240  0.0555  0.0408  137 GLN A CD  
1176 O  OE1 . GLN A 136 ? 0.2448 0.1489 0.3806 -0.0088 -0.0727 -0.1054 137 GLN A OE1 
1177 N  NE2 . GLN A 136 ? 0.2820 0.2290 0.6708 -0.0162 0.0566  0.1782  137 GLN A NE2 
1178 N  N   . PRO A 137 ? 0.0925 0.1444 0.1277 -0.0001 -0.0218 -0.0384 138 PRO A N   
1179 C  CA  . PRO A 137 ? 0.1301 0.1613 0.1186 0.0199  -0.0113 0.0197  138 PRO A CA  
1180 C  C   . PRO A 137 ? 0.1189 0.1505 0.1230 0.0103  -0.0071 0.0126  138 PRO A C   
1181 O  O   . PRO A 137 ? 0.1710 0.1435 0.1817 0.0054  0.0008  0.0155  138 PRO A O   
1182 C  CB  . PRO A 137 ? 0.1848 0.2103 0.1268 0.0478  -0.0230 -0.0055 138 PRO A CB  
1183 C  CG  . PRO A 137 ? 0.3436 0.2383 0.1550 -0.0207 -0.0566 -0.0126 138 PRO A CG  
1184 C  CD  . PRO A 137 ? 0.1588 0.1882 0.1378 -0.0304 -0.0441 -0.0406 138 PRO A CD  
1185 N  N   . ASP A 138 ? 0.1133 0.1288 0.1114 0.0043  -0.0098 -0.0099 139 ASP A N   
1186 C  CA  . ASP A 138 ? 0.1105 0.1286 0.1059 -0.0143 -0.0035 -0.0177 139 ASP A CA  
1187 C  C   . ASP A 138 ? 0.1044 0.0798 0.1174 -0.0160 -0.0189 -0.0066 139 ASP A C   
1188 O  O   . ASP A 138 ? 0.1080 0.1014 0.1392 0.0026  -0.0212 -0.0086 139 ASP A O   
1189 C  CB  . ASP A 138 ? 0.1692 0.1297 0.1268 0.0082  0.0086  -0.0143 139 ASP A CB  
1190 C  CG  . ASP A 138 ? 0.1482 0.1561 0.1414 0.0073  0.0076  -0.0388 139 ASP A CG  
1191 O  OD1 . ASP A 138 ? 0.1464 0.1101 0.1647 0.0236  -0.0160 -0.0379 139 ASP A OD1 
1192 O  OD2 . ASP A 138 ? 0.1852 0.1940 0.1853 0.0204  0.0226  -0.0623 139 ASP A OD2 
1193 N  N   . GLY A 139 ? 0.1130 0.0837 0.0986 0.0081  -0.0130 -0.0148 140 GLY A N   
1194 C  CA  . GLY A 139 ? 0.1205 0.0771 0.1076 -0.0138 -0.0177 -0.0110 140 GLY A CA  
1195 C  C   . GLY A 139 ? 0.0819 0.0622 0.1196 0.0001  -0.0030 -0.0115 140 GLY A C   
1196 O  O   . GLY A 139 ? 0.1112 0.0667 0.1223 0.0126  -0.0188 -0.0093 140 GLY A O   
1197 N  N   . LEU A 140 ? 0.0785 0.0646 0.1135 0.0020  -0.0082 -0.0116 141 LEU A N   
1198 C  CA  . LEU A 140 ? 0.0807 0.0652 0.1088 0.0038  -0.0070 -0.0105 141 LEU A CA  
1199 C  C   . LEU A 140 ? 0.0856 0.0597 0.0997 0.0060  -0.0052 -0.0054 141 LEU A C   
1200 O  O   . LEU A 140 ? 0.0786 0.0600 0.1160 0.0038  -0.0098 -0.0012 141 LEU A O   
1201 C  CB  . LEU A 140 ? 0.0993 0.0806 0.1010 0.0087  -0.0035 -0.0046 141 LEU A CB  
1202 C  CG  . LEU A 140 ? 0.1169 0.0932 0.1544 0.0286  0.0318  0.0021  141 LEU A CG  
1203 C  CD1 . LEU A 140 ? 0.0998 0.1121 0.1514 0.0274  0.0154  -0.0013 141 LEU A CD1 
1204 C  CD2 . LEU A 140 ? 0.1836 0.1079 0.2001 0.0359  0.0267  0.0278  141 LEU A CD2 
1205 N  N   . ALA A 141 ? 0.0795 0.0586 0.1133 0.0063  -0.0060 -0.0068 142 ALA A N   
1206 C  CA  . ALA A 141 ? 0.0866 0.0577 0.1137 0.0007  -0.0054 -0.0013 142 ALA A CA  
1207 C  C   . ALA A 141 ? 0.0798 0.0658 0.1031 0.0121  -0.0051 0.0051  142 ALA A C   
1208 O  O   . ALA A 141 ? 0.0961 0.0605 0.1133 -0.0043 -0.0221 0.0019  142 ALA A O   
1209 C  CB  . ALA A 141 ? 0.0791 0.0905 0.1562 -0.0113 0.0020  0.0054  142 ALA A CB  
1210 N  N   . VAL A 142 ? 0.0719 0.0608 0.0997 0.0063  -0.0080 -0.0052 143 VAL A N   
1211 C  CA  . VAL A 142 ? 0.0732 0.0688 0.0952 -0.0013 -0.0074 -0.0041 143 VAL A CA  
1212 C  C   . VAL A 142 ? 0.0646 0.0634 0.0966 -0.0041 -0.0074 -0.0003 143 VAL A C   
1213 O  O   . VAL A 142 ? 0.0864 0.0608 0.0997 -0.0013 -0.0159 -0.0008 143 VAL A O   
1214 C  CB  . VAL A 142 ? 0.0590 0.0882 0.1024 0.0028  -0.0107 0.0038  143 VAL A CB  
1215 C  CG1 . VAL A 142 ? 0.0896 0.0882 0.1076 0.0228  -0.0093 -0.0091 143 VAL A CG1 
1216 C  CG2 . VAL A 142 ? 0.0883 0.1015 0.1212 -0.0199 -0.0157 0.0054  143 VAL A CG2 
1217 N  N   . LEU A 143 ? 0.0729 0.0468 0.1147 -0.0048 -0.0241 0.0027  144 LEU A N   
1218 C  CA  . LEU A 143 ? 0.0562 0.0690 0.1114 -0.0080 -0.0148 -0.0098 144 LEU A CA  
1219 C  C   . LEU A 143 ? 0.0745 0.0668 0.1010 -0.0068 -0.0120 0.0119  144 LEU A C   
1220 O  O   . LEU A 143 ? 0.1047 0.0658 0.0993 -0.0057 -0.0073 0.0023  144 LEU A O   
1221 C  CB  . LEU A 143 ? 0.0788 0.0975 0.1337 -0.0060 -0.0232 0.0088  144 LEU A CB  
1222 C  CG  . LEU A 143 ? 0.0909 0.1108 0.1552 -0.0040 -0.0140 -0.0006 144 LEU A CG  
1223 C  CD1 . LEU A 143 ? 0.0892 0.1450 0.1683 -0.0261 -0.0344 0.0241  144 LEU A CD1 
1224 C  CD2 . LEU A 143 ? 0.0768 0.1311 0.2024 -0.0115 -0.0313 -0.0040 144 LEU A CD2 
1225 N  N   . GLY A 144 ? 0.0750 0.0573 0.0965 0.0030  -0.0165 0.0074  145 GLY A N   
1226 C  CA  . GLY A 144 ? 0.0750 0.0577 0.1063 0.0017  -0.0166 -0.0087 145 GLY A CA  
1227 C  C   . GLY A 144 ? 0.0777 0.0612 0.0913 -0.0038 -0.0175 0.0068  145 GLY A C   
1228 O  O   . GLY A 144 ? 0.0965 0.0785 0.0941 -0.0046 -0.0055 -0.0024 145 GLY A O   
1229 N  N   . ILE A 145 ? 0.0736 0.0604 0.0975 0.0013  -0.0219 -0.0041 146 ILE A N   
1230 C  CA  . ILE A 145 ? 0.0653 0.0530 0.1124 -0.0007 -0.0244 0.0013  146 ILE A CA  
1231 C  C   . ILE A 145 ? 0.0824 0.0653 0.1018 0.0006  -0.0203 0.0085  146 ILE A C   
1232 O  O   . ILE A 145 ? 0.0929 0.0539 0.1128 0.0000  -0.0096 -0.0006 146 ILE A O   
1233 C  CB  . ILE A 145 ? 0.0806 0.0684 0.1408 0.0049  -0.0344 -0.0031 146 ILE A CB  
1234 C  CG1 . ILE A 145 ? 0.1117 0.0822 0.1573 0.0522  -0.0401 -0.0041 146 ILE A CG1 
1235 C  CG2 . ILE A 145 ? 0.0725 0.0989 0.1879 -0.0115 -0.0650 -0.0081 146 ILE A CG2 
1236 C  CD1 . ILE A 145 ? 0.0995 0.0966 0.1624 0.0296  -0.0359 0.0163  146 ILE A CD1 
1237 N  N   . PHE A 146 ? 0.0724 0.0617 0.0900 -0.0028 -0.0212 0.0030  147 PHE A N   
1238 C  CA  . PHE A 146 ? 0.0945 0.0467 0.0986 0.0165  -0.0221 0.0035  147 PHE A CA  
1239 C  C   . PHE A 146 ? 0.0913 0.0583 0.1098 -0.0024 -0.0082 0.0017  147 PHE A C   
1240 O  O   . PHE A 146 ? 0.0859 0.0716 0.1319 -0.0020 -0.0228 -0.0127 147 PHE A O   
1241 C  CB  . PHE A 146 ? 0.0738 0.0681 0.1114 -0.0031 -0.0218 0.0035  147 PHE A CB  
1242 C  CG  . PHE A 146 ? 0.0769 0.0587 0.0920 0.0013  -0.0174 0.0130  147 PHE A CG  
1243 C  CD1 . PHE A 146 ? 0.0700 0.0544 0.1259 0.0073  -0.0243 0.0041  147 PHE A CD1 
1244 C  CD2 . PHE A 146 ? 0.1178 0.0534 0.1072 0.0055  -0.0201 0.0167  147 PHE A CD2 
1245 C  CE1 . PHE A 146 ? 0.1013 0.0753 0.1081 0.0062  -0.0156 0.0124  147 PHE A CE1 
1246 C  CE2 . PHE A 146 ? 0.0945 0.0706 0.1080 0.0031  -0.0065 0.0071  147 PHE A CE2 
1247 C  CZ  . PHE A 146 ? 0.0883 0.0639 0.1171 0.0127  -0.0173 0.0177  147 PHE A CZ  
1248 N  N   . LEU A 147 ? 0.0872 0.0613 0.1063 -0.0046 -0.0114 -0.0041 148 LEU A N   
1249 C  CA  . LEU A 147 ? 0.1123 0.0571 0.1018 -0.0133 -0.0280 -0.0024 148 LEU A CA  
1250 C  C   . LEU A 147 ? 0.0887 0.0768 0.0932 -0.0102 -0.0089 -0.0026 148 LEU A C   
1251 O  O   . LEU A 147 ? 0.0872 0.0657 0.1264 -0.0057 -0.0175 0.0034  148 LEU A O   
1252 C  CB  . LEU A 147 ? 0.1403 0.0549 0.1129 0.0013  -0.0251 -0.0054 148 LEU A CB  
1253 C  CG  . LEU A 147 ? 0.1356 0.0599 0.1360 -0.0085 -0.0230 0.0052  148 LEU A CG  
1254 C  CD1 . LEU A 147 ? 0.1717 0.0661 0.1279 -0.0048 -0.0267 0.0007  148 LEU A CD1 
1255 C  CD2 . LEU A 147 ? 0.1498 0.0930 0.1247 -0.0062 -0.0309 -0.0015 148 LEU A CD2 
1256 N  N   . LYS A 148 ? 0.1056 0.0529 0.1413 -0.0143 -0.0206 -0.0107 149 LYS A N   
1257 C  CA  . LYS A 148 ? 0.1248 0.0502 0.1363 -0.0024 -0.0208 -0.0100 149 LYS A CA  
1258 C  C   . LYS A 148 ? 0.1291 0.0653 0.1365 0.0065  -0.0108 -0.0043 149 LYS A C   
1259 O  O   . LYS A 148 ? 0.1441 0.1018 0.1347 0.0193  -0.0458 -0.0167 149 LYS A O   
1260 C  CB  . LYS A 148 ? 0.1388 0.0720 0.1550 -0.0187 -0.0222 0.0186  149 LYS A CB  
1261 C  CG  . LYS A 148 ? 0.1311 0.1217 0.1791 -0.0379 -0.0114 0.0285  149 LYS A CG  
1262 C  CD  . LYS A 148 ? 0.2161 0.1958 0.2513 0.0046  0.0388  0.0518  149 LYS A CD  
1263 C  CE  . LYS A 148 ? 0.2471 0.4995 0.2746 -0.0361 0.0283  0.1407  149 LYS A CE  
1264 N  NZ  . LYS A 148 ? 0.6473 0.5214 0.4013 -0.3420 0.1275  0.0496  149 LYS A NZ  
1265 N  N   . VAL A 149 ? 0.1389 0.0689 0.1360 -0.0006 -0.0193 -0.0136 150 VAL A N   
1266 C  CA  . VAL A 149 ? 0.1598 0.0702 0.1398 -0.0052 -0.0126 -0.0174 150 VAL A CA  
1267 C  C   . VAL A 149 ? 0.1421 0.0935 0.1399 -0.0133 -0.0124 -0.0010 150 VAL A C   
1268 O  O   . VAL A 149 ? 0.1683 0.0974 0.1617 -0.0127 -0.0264 0.0115  150 VAL A O   
1269 C  CB  . VAL A 149 ? 0.1250 0.1015 0.1510 0.0100  -0.0057 -0.0151 150 VAL A CB  
1270 C  CG1 . VAL A 149 ? 0.1679 0.1356 0.1543 -0.0024 -0.0121 -0.0276 150 VAL A CG1 
1271 C  CG2 . VAL A 149 ? 0.1513 0.1286 0.1999 -0.0233 -0.0129 -0.0231 150 VAL A CG2 
1272 N  N   . GLY A 150 ? 0.1460 0.0943 0.1465 -0.0212 -0.0454 -0.0041 151 GLY A N   
1273 C  CA  . GLY A 150 ? 0.1465 0.1225 0.1683 -0.0197 -0.0487 -0.0049 151 GLY A CA  
1274 C  C   . GLY A 150 ? 0.1430 0.1042 0.1837 -0.0302 -0.0423 0.0074  151 GLY A C   
1275 O  O   . GLY A 150 ? 0.1893 0.1033 0.1870 -0.0196 -0.0487 -0.0146 151 GLY A O   
1276 N  N   . SER A 151 ? 0.1450 0.1158 0.2213 -0.0219 -0.0509 0.0074  152 SER A N   
1277 C  CA  . SER A 151 ? 0.1677 0.1367 0.2202 -0.0294 -0.0825 0.0007  152 SER A CA  
1278 C  C   . SER A 151 ? 0.1762 0.0948 0.1726 0.0006  -0.0505 -0.0320 152 SER A C   
1279 O  O   . SER A 151 ? 0.1904 0.1135 0.1638 -0.0020 -0.0577 -0.0164 152 SER A O   
1280 C  CB  . SER A 151 ? 0.0977 0.2299 0.3867 0.0083  -0.0388 0.0811  152 SER A CB  
1281 O  OG  . SER A 151 ? 0.2223 0.2992 0.5174 -0.0077 -0.0149 0.1632  152 SER A OG  
1282 N  N   . ALA A 152 ? 0.1818 0.0759 0.1841 0.0066  -0.0711 -0.0270 153 ALA A N   
1283 C  CA  . ALA A 152 ? 0.2031 0.0812 0.1598 0.0115  -0.0340 -0.0175 153 ALA A CA  
1284 C  C   . ALA A 152 ? 0.1759 0.1047 0.1565 0.0130  -0.0460 -0.0348 153 ALA A C   
1285 O  O   . ALA A 152 ? 0.2138 0.1177 0.2069 0.0214  -0.0489 -0.0366 153 ALA A O   
1286 C  CB  . ALA A 152 ? 0.2375 0.1638 0.1505 0.0318  -0.0549 -0.0135 153 ALA A CB  
1287 N  N   . LYS A 153 ? 0.1960 0.0882 0.1841 0.0006  -0.0826 -0.0236 154 LYS A N   
1288 C  CA  . LYS A 153 ? 0.2630 0.0854 0.1645 0.0320  -0.0811 -0.0186 154 LYS A CA  
1289 C  C   . LYS A 153 ? 0.2019 0.1004 0.1525 0.0535  -0.0304 -0.0173 154 LYS A C   
1290 O  O   . LYS A 153 ? 0.2001 0.1221 0.1500 0.0085  -0.0816 -0.0175 154 LYS A O   
1291 C  CB  . LYS A 153 ? 0.2667 0.0878 0.1717 0.0094  -0.0824 -0.0171 154 LYS A CB  
1292 C  CG  . LYS A 153 ? 0.3456 0.1081 0.2290 0.0329  -0.1089 -0.0198 154 LYS A CG  
1293 C  CD  . LYS A 153 ? 0.3445 0.1297 0.2259 0.0830  -0.1040 -0.0384 154 LYS A CD  
1294 C  CE  . LYS A 153 ? 0.3201 0.1386 0.2347 0.0080  -0.0377 -0.0238 154 LYS A CE  
1295 N  NZ  . LYS A 153 ? 0.1768 0.1701 0.3021 -0.0057 -0.0500 -0.0595 154 LYS A NZ  
1296 N  N   . PRO A 154 ? 0.2387 0.1268 0.1705 0.0274  -0.0649 -0.0190 155 PRO A N   
1297 C  CA  . PRO A 154 ? 0.2305 0.1422 0.1947 0.0052  -0.1023 -0.0227 155 PRO A CA  
1298 C  C   . PRO A 154 ? 0.2180 0.1735 0.1823 0.0187  -0.1140 -0.0049 155 PRO A C   
1299 O  O   . PRO A 154 ? 0.2788 0.1624 0.2081 -0.0030 -0.1229 0.0142  155 PRO A O   
1300 C  CB  . PRO A 154 ? 0.2373 0.1676 0.2648 0.0140  -0.1145 0.0147  155 PRO A CB  
1301 C  CG  . PRO A 154 ? 0.2247 0.1911 0.2831 0.0164  -0.0674 0.0107  155 PRO A CG  
1302 C  CD  . PRO A 154 ? 0.2146 0.2202 0.2105 0.0489  -0.0496 0.0284  155 PRO A CD  
1303 N  N   . GLY A 155 ? 0.2545 0.0886 0.2263 0.0432  -0.1018 -0.0071 156 GLY A N   
1304 C  CA  . GLY A 155 ? 0.2569 0.1074 0.2560 0.0197  -0.0842 -0.0052 156 GLY A CA  
1305 C  C   . GLY A 155 ? 0.2958 0.0930 0.1929 0.0258  -0.0640 0.0227  156 GLY A C   
1306 O  O   . GLY A 155 ? 0.2861 0.0975 0.3089 0.0143  -0.0868 0.0183  156 GLY A O   
1307 N  N   . LEU A 156 ? 0.2328 0.1194 0.1773 0.0164  -0.0606 -0.0176 157 LEU A N   
1308 C  CA  . LEU A 156 ? 0.2865 0.0825 0.1564 -0.0074 -0.0800 -0.0020 157 LEU A CA  
1309 C  C   . LEU A 156 ? 0.3016 0.0925 0.1704 0.0111  -0.1053 -0.0096 157 LEU A C   
1310 O  O   . LEU A 156 ? 0.2879 0.1027 0.1660 -0.0116 -0.0925 -0.0060 157 LEU A O   
1311 C  CB  . LEU A 156 ? 0.2193 0.1320 0.1738 -0.0221 -0.0839 0.0160  157 LEU A CB  
1312 C  CG  . LEU A 156 ? 0.2596 0.1042 0.1703 -0.0175 -0.0917 -0.0048 157 LEU A CG  
1313 C  CD1 . LEU A 156 ? 0.2572 0.1397 0.1696 -0.0219 -0.0951 -0.0012 157 LEU A CD1 
1314 C  CD2 . LEU A 156 ? 0.2384 0.1165 0.1756 0.0309  -0.0644 -0.0031 157 LEU A CD2 
1315 N  N   . GLN A 157 ? 0.2728 0.1093 0.1561 -0.0181 -0.0833 -0.0052 158 GLN A N   
1316 C  CA  . GLN A 157 ? 0.3409 0.1397 0.1342 -0.0723 -0.0762 -0.0208 158 GLN A CA  
1317 C  C   . GLN A 157 ? 0.3355 0.1207 0.1338 -0.0306 -0.0939 -0.0188 158 GLN A C   
1318 O  O   . GLN A 157 ? 0.2809 0.1552 0.1509 -0.0152 -0.0799 -0.0302 158 GLN A O   
1319 C  CB  . GLN A 157 ? 0.3165 0.1503 0.1801 -0.0746 -0.0776 -0.0093 158 GLN A CB  
1320 C  CG  . GLN A 157 ? 0.4154 0.1440 0.1519 -0.0173 -0.1085 -0.0254 158 GLN A CG  
1321 C  CD  . GLN A 157 ? 0.4384 0.1268 0.1771 -0.0187 -0.1208 -0.0164 158 GLN A CD  
1322 O  OE1 . GLN A 157 ? 0.4199 0.1327 0.1850 -0.0049 -0.1163 -0.0082 158 GLN A OE1 
1323 N  NE2 . GLN A 157 ? 0.4713 0.1636 0.1737 -0.0489 -0.1106 -0.0342 158 GLN A NE2 
1324 N  N   A LYS A 158 ? 0.3086 0.1108 0.1802 -0.0260 -0.1194 0.0109  159 LYS A N   
1325 N  N   B LYS A 158 ? 0.3059 0.1128 0.1868 -0.0248 -0.1253 0.0052  159 LYS A N   
1326 C  CA  A LYS A 158 ? 0.3411 0.1182 0.1773 -0.0041 -0.1037 0.0200  159 LYS A CA  
1327 C  CA  B LYS A 158 ? 0.3440 0.1207 0.1807 -0.0048 -0.1129 0.0103  159 LYS A CA  
1328 C  C   A LYS A 158 ? 0.3190 0.1329 0.1358 0.0098  -0.0898 -0.0201 159 LYS A C   
1329 C  C   B LYS A 158 ? 0.3222 0.1313 0.1354 0.0103  -0.0903 -0.0217 159 LYS A C   
1330 O  O   A LYS A 158 ? 0.3170 0.1547 0.1570 -0.0175 -0.0930 -0.0051 159 LYS A O   
1331 O  O   B LYS A 158 ? 0.3104 0.1543 0.1627 -0.0241 -0.0899 -0.0130 159 LYS A O   
1332 C  CB  A LYS A 158 ? 0.3278 0.0889 0.2308 -0.0302 -0.0948 0.0610  159 LYS A CB  
1333 C  CB  B LYS A 158 ? 0.3213 0.1592 0.2511 0.0263  -0.1622 0.0318  159 LYS A CB  
1334 C  CG  A LYS A 158 ? 0.4088 0.1101 0.2572 -0.0573 -0.1711 0.0425  159 LYS A CG  
1335 C  CG  B LYS A 158 ? 0.3887 0.1496 0.2484 0.0386  -0.1592 0.0124  159 LYS A CG  
1336 C  CD  A LYS A 158 ? 0.3538 0.1843 0.4368 -0.0120 -0.1162 -0.0074 159 LYS A CD  
1337 C  CD  B LYS A 158 ? 0.3928 0.1151 0.3450 0.0373  -0.1274 0.0487  159 LYS A CD  
1338 C  CE  A LYS A 158 ? 0.4316 0.3364 0.5795 -0.1009 -0.2395 0.0472  159 LYS A CE  
1339 C  CE  B LYS A 158 ? 0.3303 0.2736 0.3174 -0.0672 -0.1996 0.0869  159 LYS A CE  
1340 N  NZ  A LYS A 158 ? 0.3664 0.4641 0.3461 -0.1106 -0.1964 0.0666  159 LYS A NZ  
1341 N  NZ  B LYS A 158 ? 0.5383 0.1864 0.2709 -0.0551 -0.0689 0.0399  159 LYS A NZ  
1342 N  N   . VAL A 159 ? 0.3113 0.1102 0.1500 0.0181  -0.0974 -0.0234 160 VAL A N   
1343 C  CA  . VAL A 159 ? 0.3156 0.0989 0.1327 0.0104  -0.0612 0.0074  160 VAL A CA  
1344 C  C   . VAL A 159 ? 0.2673 0.0790 0.1898 0.0140  -0.0877 -0.0195 160 VAL A C   
1345 O  O   . VAL A 159 ? 0.3093 0.1214 0.1710 -0.0115 -0.0900 -0.0087 160 VAL A O   
1346 C  CB  . VAL A 159 ? 0.3513 0.0833 0.1444 -0.0296 -0.0916 -0.0068 160 VAL A CB  
1347 C  CG1 . VAL A 159 ? 0.3059 0.1597 0.1507 -0.0340 -0.0706 0.0031  160 VAL A CG1 
1348 C  CG2 . VAL A 159 ? 0.3235 0.1297 0.1680 0.0227  -0.0913 -0.0280 160 VAL A CG2 
1349 N  N   . VAL A 160 ? 0.3023 0.0850 0.1396 0.0038  -0.0696 -0.0226 161 VAL A N   
1350 C  CA  . VAL A 160 ? 0.3316 0.0847 0.1467 0.0021  -0.0465 -0.0032 161 VAL A CA  
1351 C  C   . VAL A 160 ? 0.3529 0.0850 0.1573 -0.0239 -0.0570 -0.0329 161 VAL A C   
1352 O  O   . VAL A 160 ? 0.3700 0.1171 0.1800 -0.0199 -0.0136 -0.0179 161 VAL A O   
1353 C  CB  . VAL A 160 ? 0.4336 0.1076 0.1683 -0.0122 0.0131  -0.0181 161 VAL A CB  
1354 C  CG1 . VAL A 160 ? 0.4201 0.1383 0.2533 -0.0592 -0.0006 -0.0182 161 VAL A CG1 
1355 C  CG2 . VAL A 160 ? 0.3844 0.1288 0.2184 0.0469  -0.0298 -0.0239 161 VAL A CG2 
1356 N  N   . ASP A 161 ? 0.3962 0.1369 0.1453 -0.0630 -0.0904 -0.0041 162 ASP A N   
1357 C  CA  . ASP A 161 ? 0.4390 0.2275 0.1509 -0.1287 -0.0676 -0.0231 162 ASP A CA  
1358 C  C   . ASP A 161 ? 0.4014 0.1898 0.1564 -0.1062 -0.0857 -0.0138 162 ASP A C   
1359 O  O   . ASP A 161 ? 0.5733 0.2921 0.1678 -0.1975 -0.0175 -0.0184 162 ASP A O   
1360 C  CB  . ASP A 161 ? 0.5189 0.2193 0.1645 -0.0789 -0.0883 -0.0428 162 ASP A CB  
1361 C  CG  . ASP A 161 ? 0.5067 0.1351 0.2087 -0.0111 -0.0260 -0.0229 162 ASP A CG  
1362 O  OD1 . ASP A 161 ? 0.4194 0.2206 0.3104 -0.0747 -0.0935 -0.0582 162 ASP A OD1 
1363 O  OD2 . ASP A 161 ? 0.5436 0.3332 0.2407 -0.1146 -0.0732 -0.0573 162 ASP A OD2 
1364 N  N   . VAL A 162 ? 0.4609 0.1485 0.1483 -0.0816 -0.1066 -0.0049 163 VAL A N   
1365 C  CA  . VAL A 162 ? 0.4625 0.1504 0.2125 -0.0870 -0.1296 0.0320  163 VAL A CA  
1366 C  C   . VAL A 162 ? 0.4679 0.1053 0.1255 -0.0670 -0.0302 0.0115  163 VAL A C   
1367 O  O   . VAL A 162 ? 0.5066 0.1304 0.1455 -0.0851 -0.0263 0.0054  163 VAL A O   
1368 C  CB  . VAL A 162 ? 0.4950 0.1365 0.2578 -0.0361 -0.0843 0.0220  163 VAL A CB  
1369 C  CG1 . VAL A 162 ? 0.5103 0.1230 0.2414 -0.0333 -0.1040 0.0017  163 VAL A CG1 
1370 C  CG2 . VAL A 162 ? 0.3497 0.1701 0.2904 0.0731  0.0103  0.0553  163 VAL A CG2 
1371 N  N   . LEU A 163 ? 0.4625 0.1340 0.1564 -0.0821 -0.0800 0.0186  164 LEU A N   
1372 C  CA  . LEU A 163 ? 0.4176 0.1187 0.1277 -0.0482 -0.0080 0.0093  164 LEU A CA  
1373 C  C   . LEU A 163 ? 0.4410 0.1379 0.1385 -0.0271 0.0082  -0.0076 164 LEU A C   
1374 O  O   . LEU A 163 ? 0.4593 0.1368 0.1525 -0.0366 0.0291  0.0115  164 LEU A O   
1375 C  CB  . LEU A 163 ? 0.3637 0.0927 0.1552 -0.0324 -0.0038 0.0077  164 LEU A CB  
1376 C  CG  . LEU A 163 ? 0.2741 0.0925 0.1483 -0.0209 -0.0109 0.0086  164 LEU A CG  
1377 C  CD1 . LEU A 163 ? 0.3334 0.1225 0.1769 -0.0186 -0.0331 0.0324  164 LEU A CD1 
1378 C  CD2 . LEU A 163 ? 0.3061 0.1288 0.1383 -0.0182 -0.0425 -0.0019 164 LEU A CD2 
1379 N  N   . ASP A 164 ? 0.5666 0.1455 0.1266 -0.0597 -0.0115 -0.0197 165 ASP A N   
1380 C  CA  . ASP A 164 ? 0.6276 0.1557 0.1689 -0.0500 0.0392  -0.0441 165 ASP A CA  
1381 C  C   . ASP A 164 ? 0.7103 0.2204 0.1318 -0.0082 0.0634  -0.0249 165 ASP A C   
1382 O  O   . ASP A 164 ? 0.7547 0.2108 0.2039 0.0229  0.1335  0.0003  165 ASP A O   
1383 C  CB  . ASP A 164 ? 0.8051 0.2623 0.2175 -0.1199 -0.0102 -0.0810 165 ASP A CB  
1384 C  CG  . ASP A 164 ? 0.7642 0.5210 0.5544 -0.2964 -0.2547 -0.0760 165 ASP A CG  
1385 O  OD1 . ASP A 164 ? 0.9602 1.0505 0.3370 -0.2991 -0.0408 -0.0494 165 ASP A OD1 
1386 O  OD2 . ASP A 164 ? 1.4364 1.9833 0.9892 0.2333  -0.4930 -1.1421 165 ASP A OD2 
1387 N  N   . SER A 165 ? 0.5425 0.1583 0.1342 -0.0813 -0.0181 -0.0102 166 SER A N   
1388 C  CA  . SER A 165 ? 0.6213 0.1956 0.1286 -0.0763 -0.0012 -0.0161 166 SER A CA  
1389 C  C   . SER A 165 ? 0.5935 0.1439 0.1076 -0.0727 0.0326  -0.0165 166 SER A C   
1390 O  O   . SER A 165 ? 0.5760 0.1496 0.1356 -0.0688 0.0068  0.0183  166 SER A O   
1391 C  CB  . SER A 165 ? 0.6664 0.2069 0.2035 -0.0601 0.0706  0.0024  166 SER A CB  
1392 O  OG  . SER A 165 ? 0.6934 0.1633 0.2129 0.0015  0.0791  0.0284  166 SER A OG  
1393 N  N   . ILE A 166 ? 0.4621 0.1487 0.1129 -0.0891 -0.0082 -0.0049 167 ILE A N   
1394 C  CA  . ILE A 166 ? 0.3332 0.1247 0.1774 -0.0344 0.0035  0.0148  167 ILE A CA  
1395 C  C   . ILE A 166 ? 0.2218 0.1437 0.1441 -0.0447 0.0012  -0.0192 167 ILE A C   
1396 O  O   . ILE A 166 ? 0.4074 0.1335 0.1315 -0.0579 0.0216  0.0089  167 ILE A O   
1397 C  CB  . ILE A 166 ? 0.4237 0.1117 0.1099 -0.0785 -0.0006 -0.0115 167 ILE A CB  
1398 C  CG1 . ILE A 166 ? 0.4070 0.1167 0.1279 -0.0531 0.0144  0.0026  167 ILE A CG1 
1399 C  CG2 . ILE A 166 ? 0.4255 0.1165 0.1511 -0.0480 -0.0329 -0.0015 167 ILE A CG2 
1400 C  CD1 . ILE A 166 ? 0.3497 0.1528 0.1212 -0.0214 0.0252  -0.0326 167 ILE A CD1 
1401 N  N   . LYS A 167 ? 0.4259 0.1229 0.1559 -0.0458 0.0264  0.0041  168 LYS A N   
1402 C  CA  . LYS A 167 ? 0.3163 0.1918 0.1659 -0.0108 0.0132  -0.0423 168 LYS A CA  
1403 C  C   . LYS A 167 ? 0.2872 0.1740 0.1376 -0.0197 0.0738  0.0297  168 LYS A C   
1404 O  O   . LYS A 167 ? 0.3228 0.1369 0.1368 -0.0791 0.0348  -0.0248 168 LYS A O   
1405 C  CB  . LYS A 167 ? 0.4397 0.1356 0.1516 -0.0498 0.0196  -0.0428 168 LYS A CB  
1406 C  CG  . LYS A 167 ? 0.3957 0.1360 0.1942 -0.0513 0.0639  -0.0220 168 LYS A CG  
1407 C  CD  . LYS A 167 ? 0.6223 0.2324 0.3600 -0.0233 -0.0186 -0.1827 168 LYS A CD  
1408 C  CE  . LYS A 167 ? 0.6633 0.3542 0.3788 0.1013  -0.0599 -0.2242 168 LYS A CE  
1409 N  NZ  . LYS A 167 ? 0.6062 0.4690 0.3928 0.0251  0.1193  -0.1793 168 LYS A NZ  
1410 N  N   . THR A 168 ? 0.2416 0.1844 0.1584 -0.0251 0.0259  0.0304  169 THR A N   
1411 C  CA  . THR A 168 ? 0.2055 0.1616 0.1482 0.0041  0.0284  0.0040  169 THR A CA  
1412 C  C   . THR A 168 ? 0.2322 0.1911 0.1503 0.0073  0.0498  0.0283  169 THR A C   
1413 O  O   . THR A 168 ? 0.3537 0.1202 0.1908 -0.0472 0.0821  -0.0070 169 THR A O   
1414 C  CB  . THR A 168 ? 0.2646 0.1904 0.1653 -0.0241 0.0111  -0.0463 169 THR A CB  
1415 O  OG1 . THR A 168 ? 0.4262 0.2121 0.1494 -0.0855 0.0551  -0.0302 169 THR A OG1 
1416 C  CG2 . THR A 168 ? 0.3819 0.1983 0.1906 -0.0612 0.1102  -0.0601 169 THR A CG2 
1417 N  N   A LYS A 169 ? 0.3208 0.1821 0.1627 -0.1101 0.0966  -0.0131 170 LYS A N   
1418 N  N   B LYS A 169 ? 0.3233 0.1888 0.1629 -0.1080 0.0996  -0.0167 170 LYS A N   
1419 C  CA  A LYS A 169 ? 0.2782 0.1618 0.1749 -0.0017 0.0683  -0.0052 170 LYS A CA  
1420 C  CA  B LYS A 169 ? 0.2975 0.1654 0.1827 -0.0076 0.0621  -0.0062 170 LYS A CA  
1421 C  C   A LYS A 169 ? 0.2949 0.1983 0.1647 -0.0750 0.0595  0.0203  170 LYS A C   
1422 C  C   B LYS A 169 ? 0.2949 0.1967 0.1679 -0.0719 0.0573  0.0175  170 LYS A C   
1423 O  O   A LYS A 169 ? 0.4341 0.2473 0.1598 -0.1243 0.0829  0.0013  170 LYS A O   
1424 O  O   B LYS A 169 ? 0.4068 0.2567 0.1654 -0.1158 0.0714  0.0031  170 LYS A O   
1425 C  CB  A LYS A 169 ? 0.2865 0.1103 0.1805 0.0119  0.0856  -0.0027 170 LYS A CB  
1426 C  CB  B LYS A 169 ? 0.2960 0.1234 0.1900 0.0046  0.0988  -0.0015 170 LYS A CB  
1427 C  CG  A LYS A 169 ? 0.3098 0.2093 0.2029 -0.0826 0.0027  0.0261  170 LYS A CG  
1428 C  CG  B LYS A 169 ? 0.3741 0.1755 0.2023 -0.1057 0.0000  0.0604  170 LYS A CG  
1429 C  CD  A LYS A 169 ? 0.3280 0.0993 0.1050 -0.0573 0.0471  0.0207  170 LYS A CD  
1430 C  CD  B LYS A 169 ? 0.3745 0.2782 0.2730 -0.0560 0.0209  -0.0186 170 LYS A CD  
1431 C  CE  A LYS A 169 ? 0.2290 0.3219 0.2922 -0.0109 0.0956  0.0041  170 LYS A CE  
1432 C  CE  B LYS A 169 ? 0.2651 0.4372 0.3037 0.0344  0.0370  0.0015  170 LYS A CE  
1433 N  NZ  A LYS A 169 ? 0.2725 0.4406 0.2346 -0.0754 0.0767  0.0133  170 LYS A NZ  
1434 N  NZ  B LYS A 169 ? 0.5436 0.4059 0.4981 -0.1058 -0.0654 0.0217  170 LYS A NZ  
1435 N  N   . GLY A 170 ? 0.3907 0.1371 0.1762 -0.1256 0.0597  -0.0092 171 GLY A N   
1436 C  CA  . GLY A 170 ? 0.3156 0.1110 0.2524 -0.0922 -0.0087 0.0373  171 GLY A CA  
1437 C  C   . GLY A 170 ? 0.3612 0.1676 0.1923 -0.0579 -0.0189 0.0031  171 GLY A C   
1438 O  O   . GLY A 170 ? 0.5537 0.1451 0.2720 -0.1395 0.0110  0.0560  171 GLY A O   
1439 N  N   . LYS A 171 ? 0.2603 0.0983 0.2306 -0.0416 0.0621  0.0296  172 LYS A N   
1440 C  CA  . LYS A 171 ? 0.2416 0.1624 0.3012 -0.0129 0.0266  0.0663  172 LYS A CA  
1441 C  C   . LYS A 171 ? 0.2055 0.2026 0.1738 0.0702  -0.0313 -0.0324 172 LYS A C   
1442 O  O   . LYS A 171 ? 0.3097 0.1748 0.1360 -0.0121 0.0252  0.0286  172 LYS A O   
1443 C  CB  . LYS A 171 ? 0.3907 0.1650 0.1507 -0.0214 0.0408  0.0181  172 LYS A CB  
1444 C  CG  . LYS A 171 ? 0.4388 0.1599 0.2197 -0.0285 0.0795  -0.0104 172 LYS A CG  
1445 C  CD  . LYS A 171 ? 0.7807 0.2500 0.2037 -0.1331 0.0687  -0.0324 172 LYS A CD  
1446 C  CE  . LYS A 171 ? 1.0053 0.3709 0.3501 -0.2320 -0.1334 0.0637  172 LYS A CE  
1447 N  NZ  . LYS A 171 ? 1.2106 0.3587 0.2296 -0.2858 0.2373  -0.0421 172 LYS A NZ  
1448 N  N   . SER A 172 ? 0.2116 0.1672 0.2362 -0.0410 -0.0388 0.0856  173 SER A N   
1449 C  CA  . SER A 172 ? 0.1018 0.1722 0.3424 -0.0109 -0.0210 0.0275  173 SER A CA  
1450 C  C   . SER A 172 ? 0.1410 0.1352 0.1819 0.0000  -0.0148 0.0540  173 SER A C   
1451 O  O   . SER A 172 ? 0.3443 0.2757 0.1326 0.0406  0.0066  0.0333  173 SER A O   
1452 C  CB  . SER A 172 ? 0.4503 0.1498 0.1932 -0.0194 0.0297  0.0167  173 SER A CB  
1453 O  OG  . SER A 172 ? 0.8131 0.1223 0.2213 0.0148  0.1541  0.0608  173 SER A OG  
1454 N  N   . ALA A 173 ? 0.1642 0.2290 0.3303 0.1006  0.0063  -0.0074 174 ALA A N   
1455 C  CA  . ALA A 173 ? 0.2339 0.3515 0.1881 0.1208  -0.0088 0.1259  174 ALA A CA  
1456 C  C   . ALA A 173 ? 0.0582 0.3224 0.3456 0.0731  -0.0747 -0.0242 174 ALA A C   
1457 O  O   . ALA A 173 ? 0.3664 0.1814 0.1460 0.0540  -0.0461 0.0080  174 ALA A O   
1458 C  CB  . ALA A 173 ? 0.5716 0.2457 0.1430 0.1833  -0.0500 -0.0296 174 ALA A CB  
1459 N  N   . ASP A 174 ? 0.2008 0.3488 0.1916 0.0331  0.0063  0.1353  175 ASP A N   
1460 C  CA  . ASP A 174 ? 0.2772 0.2658 0.1584 0.0540  0.0303  0.0234  175 ASP A CA  
1461 C  C   . ASP A 174 ? 0.4221 0.2032 0.2084 0.1312  0.0258  0.0513  175 ASP A C   
1462 O  O   . ASP A 174 ? 0.6463 0.2380 0.1694 0.1765  -0.0304 -0.0243 175 ASP A O   
1463 C  CB  . ASP A 174 ? 0.3346 0.3564 0.3450 0.1471  -0.0236 0.1418  175 ASP A CB  
1464 C  CG  . ASP A 174 ? 0.4607 0.5950 0.3170 -0.0148 -0.1648 0.1660  175 ASP A CG  
1465 O  OD1 . ASP A 174 ? 0.7741 0.6909 0.4144 -0.0065 -0.2926 -0.0007 175 ASP A OD1 
1466 O  OD2 . ASP A 174 ? 0.3470 0.5899 0.2935 -0.0854 -0.0868 -0.0032 175 ASP A OD2 
1467 N  N   . PHE A 175 ? 0.4648 0.1731 0.1514 0.0588  0.0000  -0.0119 176 PHE A N   
1468 C  CA  . PHE A 175 ? 0.4843 0.1239 0.1654 0.0489  -0.0710 0.0324  176 PHE A CA  
1469 C  C   . PHE A 175 ? 0.4857 0.1036 0.1480 0.0410  -0.0935 0.0027  176 PHE A C   
1470 O  O   . PHE A 175 ? 0.4943 0.1929 0.1640 0.0767  -0.1366 -0.0088 176 PHE A O   
1471 C  CB  . PHE A 175 ? 0.4937 0.1225 0.1681 0.0320  -0.0764 0.0368  176 PHE A CB  
1472 C  CG  . PHE A 175 ? 0.4476 0.1141 0.1509 0.0397  -0.0524 0.0092  176 PHE A CG  
1473 C  CD1 . PHE A 175 ? 0.4343 0.1275 0.2032 0.0138  -0.0672 -0.0074 176 PHE A CD1 
1474 C  CD2 . PHE A 175 ? 0.4447 0.1439 0.1582 0.0487  -0.0914 0.0165  176 PHE A CD2 
1475 C  CE1 . PHE A 175 ? 0.4704 0.1194 0.2112 0.0361  -0.0544 -0.0010 176 PHE A CE1 
1476 C  CE2 . PHE A 175 ? 0.4237 0.1309 0.2023 0.0450  -0.1013 0.0247  176 PHE A CE2 
1477 C  CZ  . PHE A 175 ? 0.5363 0.1390 0.2050 0.0619  -0.1184 0.0041  176 PHE A CZ  
1478 N  N   . THR A 176 ? 0.4311 0.1378 0.1174 -0.0027 -0.1014 0.0212  177 THR A N   
1479 C  CA  . THR A 176 ? 0.5159 0.0956 0.1489 0.0237  -0.0700 0.0320  177 THR A CA  
1480 C  C   . THR A 176 ? 0.3713 0.1033 0.1326 0.0043  -0.1163 0.0320  177 THR A C   
1481 O  O   . THR A 176 ? 0.4248 0.1119 0.1500 -0.0281 -0.1098 0.0272  177 THR A O   
1482 C  CB  . THR A 176 ? 0.4918 0.1412 0.1897 -0.0114 -0.1608 0.0430  177 THR A CB  
1483 O  OG1 . THR A 176 ? 0.6319 0.1853 0.1737 0.0544  -0.1387 0.0463  177 THR A OG1 
1484 C  CG2 . THR A 176 ? 0.4352 0.2252 0.3368 0.0093  -0.0908 0.1673  177 THR A CG2 
1485 N  N   . ASN A 177 ? 0.4255 0.1464 0.1426 0.0219  -0.1317 0.0205  178 ASN A N   
1486 C  CA  . ASN A 177 ? 0.4408 0.1196 0.1712 0.0141  -0.1322 0.0408  178 ASN A CA  
1487 C  C   . ASN A 177 ? 0.4700 0.1102 0.1640 0.0110  -0.1430 0.0140  178 ASN A C   
1488 O  O   . ASN A 177 ? 0.4675 0.1665 0.2973 -0.0296 -0.1990 0.1080  178 ASN A O   
1489 C  CB  . ASN A 177 ? 0.4095 0.1464 0.2247 0.0054  -0.1606 0.0606  178 ASN A CB  
1490 C  CG  . ASN A 177 ? 0.3574 0.1216 0.2189 -0.0031 -0.1216 0.0190  178 ASN A CG  
1491 O  OD1 . ASN A 177 ? 0.4383 0.1342 0.2784 0.0223  -0.1001 0.0441  178 ASN A OD1 
1492 N  ND2 . ASN A 177 ? 0.3889 0.1710 0.1920 -0.0277 -0.1402 0.0723  178 ASN A ND2 
1493 N  N   . PHE A 178 ? 0.4262 0.0826 0.1448 0.0127  -0.1229 0.0251  179 PHE A N   
1494 C  CA  . PHE A 178 ? 0.4072 0.1056 0.1534 0.0080  -0.1171 0.0449  179 PHE A CA  
1495 C  C   . PHE A 178 ? 0.3036 0.1008 0.1512 -0.0121 -0.0971 0.0285  179 PHE A C   
1496 O  O   . PHE A 178 ? 0.3443 0.1108 0.1544 -0.0003 -0.1018 0.0129  179 PHE A O   
1497 C  CB  . PHE A 178 ? 0.3912 0.1077 0.1385 0.0406  -0.0604 0.0397  179 PHE A CB  
1498 C  CG  . PHE A 178 ? 0.3840 0.0917 0.1362 0.0129  -0.0566 0.0335  179 PHE A CG  
1499 C  CD1 . PHE A 178 ? 0.4163 0.0973 0.1557 0.0242  -0.0582 0.0093  179 PHE A CD1 
1500 C  CD2 . PHE A 178 ? 0.2872 0.1146 0.1283 0.0093  -0.0461 0.0248  179 PHE A CD2 
1501 C  CE1 . PHE A 178 ? 0.4600 0.1110 0.1751 0.0206  -0.0856 0.0357  179 PHE A CE1 
1502 C  CE2 . PHE A 178 ? 0.2356 0.1040 0.1503 0.0000  -0.0379 0.0294  179 PHE A CE2 
1503 C  CZ  . PHE A 178 ? 0.2745 0.1022 0.1744 0.0057  -0.0619 0.0263  179 PHE A CZ  
1504 N  N   . ASP A 179 ? 0.2786 0.1138 0.1820 0.0074  -0.1243 0.0231  180 ASP A N   
1505 C  CA  . ASP A 179 ? 0.2721 0.1681 0.1546 0.0211  -0.1130 0.0216  180 ASP A CA  
1506 C  C   . ASP A 179 ? 0.2398 0.1053 0.1703 0.0066  -0.0855 0.0122  180 ASP A C   
1507 O  O   . ASP A 179 ? 0.2640 0.1047 0.1649 0.0015  -0.0788 0.0078  180 ASP A O   
1508 C  CB  . ASP A 179 ? 0.2576 0.1872 0.2166 0.0065  -0.1359 0.0357  180 ASP A CB  
1509 C  CG  . ASP A 179 ? 0.2444 0.1735 0.2588 0.0394  -0.1271 0.0136  180 ASP A CG  
1510 O  OD1 . ASP A 179 ? 0.2777 0.1315 0.2437 -0.0043 -0.1216 0.0372  180 ASP A OD1 
1511 O  OD2 . ASP A 179 ? 0.2035 0.4453 0.4550 -0.0037 -0.1401 0.1079  180 ASP A OD2 
1512 N  N   . PRO A 180 ? 0.2308 0.0959 0.1280 0.0000  -0.0586 0.0103  181 PRO A N   
1513 C  CA  . PRO A 180 ? 0.1505 0.1174 0.1773 0.0222  -0.0716 0.0160  181 PRO A CA  
1514 C  C   . PRO A 180 ? 0.1762 0.1306 0.1480 0.0192  -0.0680 0.0237  181 PRO A C   
1515 O  O   . PRO A 180 ? 0.1785 0.1106 0.1599 0.0104  -0.0697 0.0236  181 PRO A O   
1516 C  CB  . PRO A 180 ? 0.1500 0.1457 0.1880 0.0115  -0.0696 -0.0055 181 PRO A CB  
1517 C  CG  . PRO A 180 ? 0.1976 0.1477 0.1773 0.0000  -0.0830 0.0015  181 PRO A CG  
1518 C  CD  . PRO A 180 ? 0.2293 0.1036 0.1547 0.0007  -0.0864 0.0043  181 PRO A CD  
1519 N  N   . ARG A 181 ? 0.1653 0.1203 0.1584 0.0267  -0.0776 0.0124  182 ARG A N   
1520 C  CA  . ARG A 181 ? 0.1636 0.1178 0.1888 0.0076  -0.0551 -0.0013 182 ARG A CA  
1521 C  C   . ARG A 181 ? 0.1893 0.1234 0.1846 0.0181  -0.1146 0.0041  182 ARG A C   
1522 O  O   . ARG A 181 ? 0.2190 0.1126 0.2123 -0.0119 -0.1000 0.0212  182 ARG A O   
1523 C  CB  . ARG A 181 ? 0.1374 0.1495 0.2267 0.0063  -0.0798 -0.0035 182 ARG A CB  
1524 C  CG  . ARG A 181 ? 0.1865 0.1334 0.2563 0.0164  -0.0302 -0.0092 182 ARG A CG  
1525 C  CD  . ARG A 181 ? 0.1625 0.1970 0.3208 0.0304  -0.0388 0.0317  182 ARG A CD  
1526 N  NE  . ARG A 181 ? 0.2150 0.1879 0.3258 0.0253  -0.0115 0.1001  182 ARG A NE  
1527 C  CZ  . ARG A 181 ? 0.1913 0.2752 0.3736 0.0355  -0.0037 0.1474  182 ARG A CZ  
1528 N  NH1 . ARG A 181 ? 0.2019 0.2402 0.5077 0.0030  0.0516  0.0997  182 ARG A NH1 
1529 N  NH2 . ARG A 181 ? 0.2071 0.2637 0.3874 -0.0124 -0.0195 0.1342  182 ARG A NH2 
1530 N  N   . GLY A 182 ? 0.1897 0.1221 0.1953 0.0219  -0.1070 0.0082  183 GLY A N   
1531 C  CA  . GLY A 182 ? 0.2468 0.1214 0.2215 0.0207  -0.1370 0.0034  183 GLY A CA  
1532 C  C   . GLY A 182 ? 0.2358 0.1291 0.2091 0.0274  -0.1119 -0.0167 183 GLY A C   
1533 O  O   . GLY A 182 ? 0.3001 0.1171 0.2425 0.0357  -0.1289 -0.0155 183 GLY A O   
1534 N  N   . LEU A 183 ? 0.2082 0.1325 0.1534 0.0111  -0.0896 0.0041  184 LEU A N   
1535 C  CA  . LEU A 183 ? 0.2319 0.0954 0.1604 0.0399  -0.0878 -0.0109 184 LEU A CA  
1536 C  C   . LEU A 183 ? 0.2055 0.1074 0.1507 0.0104  -0.0760 0.0003  184 LEU A C   
1537 O  O   . LEU A 183 ? 0.1816 0.1343 0.1904 0.0207  -0.0754 0.0102  184 LEU A O   
1538 C  CB  . LEU A 183 ? 0.1866 0.1421 0.1615 0.0220  -0.0500 -0.0109 184 LEU A CB  
1539 C  CG  . LEU A 183 ? 0.2809 0.1444 0.1530 0.0676  -0.0922 0.0027  184 LEU A CG  
1540 C  CD1 . LEU A 183 ? 0.2808 0.2302 0.1729 0.0571  -0.0718 0.0549  184 LEU A CD1 
1541 C  CD2 . LEU A 183 ? 0.3222 0.1606 0.1608 0.0738  -0.0419 -0.0449 184 LEU A CD2 
1542 N  N   . LEU A 184 ? 0.1854 0.1098 0.1823 0.0181  -0.0684 -0.0032 185 LEU A N   
1543 C  CA  . LEU A 184 ? 0.1556 0.1205 0.1805 -0.0228 -0.0635 0.0318  185 LEU A CA  
1544 C  C   . LEU A 184 ? 0.1789 0.1239 0.2258 -0.0234 -0.0934 0.0562  185 LEU A C   
1545 O  O   . LEU A 184 ? 0.2466 0.2087 0.2913 -0.0788 -0.1747 0.0864  185 LEU A O   
1546 C  CB  . LEU A 184 ? 0.0939 0.1141 0.2126 -0.0107 -0.0538 0.0230  185 LEU A CB  
1547 C  CG  . LEU A 184 ? 0.0894 0.1234 0.1884 0.0165  -0.0315 0.0227  185 LEU A CG  
1548 C  CD1 . LEU A 184 ? 0.1203 0.1487 0.2042 0.0186  -0.0253 -0.0005 185 LEU A CD1 
1549 C  CD2 . LEU A 184 ? 0.1058 0.1785 0.2390 0.0147  -0.0526 0.0608  185 LEU A CD2 
1550 N  N   . PRO A 185 ? 0.1184 0.1074 0.1924 -0.0142 -0.0626 0.0313  186 PRO A N   
1551 C  CA  . PRO A 185 ? 0.1304 0.1198 0.2172 -0.0094 -0.0526 0.0524  186 PRO A CA  
1552 C  C   . PRO A 185 ? 0.1084 0.1190 0.2436 -0.0071 -0.0839 0.0573  186 PRO A C   
1553 O  O   . PRO A 185 ? 0.0929 0.1112 0.4097 0.0000  -0.0738 0.0737  186 PRO A O   
1554 C  CB  . PRO A 185 ? 0.1160 0.1337 0.1936 0.0175  -0.0480 0.0127  186 PRO A CB  
1555 C  CG  . PRO A 185 ? 0.0914 0.1279 0.1523 0.0245  -0.0252 -0.0020 186 PRO A CG  
1556 C  CD  . PRO A 185 ? 0.0935 0.1184 0.1500 0.0091  -0.0364 0.0063  186 PRO A CD  
1557 N  N   A GLU A 186 ? 0.1297 0.1252 0.2649 -0.0130 -0.0513 0.0500  187 GLU A N   
1558 N  N   B GLU A 186 ? 0.1316 0.1248 0.2646 -0.0126 -0.0502 0.0502  187 GLU A N   
1559 C  CA  A GLU A 186 ? 0.0865 0.1705 0.3177 -0.0469 -0.0733 0.0493  187 GLU A CA  
1560 C  CA  B GLU A 186 ? 0.0887 0.1755 0.3179 -0.0390 -0.0690 0.0518  187 GLU A CA  
1561 C  C   A GLU A 186 ? 0.0527 0.1465 0.2953 0.0017  -0.0289 0.0342  187 GLU A C   
1562 C  C   B GLU A 186 ? 0.0606 0.1491 0.2964 0.0057  -0.0287 0.0351  187 GLU A C   
1563 O  O   A GLU A 186 ? 0.0855 0.1703 0.3995 0.0255  -0.0383 0.0427  187 GLU A O   
1564 O  O   B GLU A 186 ? 0.0737 0.1703 0.3978 0.0250  -0.0412 0.0452  187 GLU A O   
1565 C  CB  A GLU A 186 ? 0.1615 0.2220 0.3806 -0.1130 -0.1509 0.1035  187 GLU A CB  
1566 C  CB  B GLU A 186 ? 0.2053 0.2041 0.4379 -0.0891 -0.1174 0.1115  187 GLU A CB  
1567 C  CG  A GLU A 186 ? 0.1968 0.2099 0.5662 0.0286  -0.0762 0.1269  187 GLU A CG  
1568 C  CG  B GLU A 186 ? 0.1322 0.1697 0.5874 -0.0553 -0.1772 0.0901  187 GLU A CG  
1569 C  CD  A GLU A 186 ? 0.2538 0.2511 0.6984 -0.0348 -0.2090 0.1297  187 GLU A CD  
1570 C  CD  B GLU A 186 ? 0.2326 0.2696 0.7865 -0.1523 -0.0648 0.0789  187 GLU A CD  
1571 O  OE1 A GLU A 186 ? 0.2150 0.2518 0.8018 0.0109  -0.0057 0.0781  187 GLU A OE1 
1572 O  OE1 B GLU A 186 ? 0.1792 0.1552 0.7457 -0.0267 0.0010  -0.0060 187 GLU A OE1 
1573 O  OE2 A GLU A 186 ? 0.4379 0.4602 0.9555 0.0474  0.1308  0.2696  187 GLU A OE2 
1574 O  OE2 B GLU A 186 ? 0.2529 0.2362 0.8634 -0.0333 -0.1533 0.0608  187 GLU A OE2 
1575 N  N   . SER A 187 ? 0.0671 0.1448 0.2583 -0.0181 -0.0318 0.0232  188 SER A N   
1576 C  CA  . SER A 187 ? 0.0644 0.1552 0.2824 0.0000  0.0160  0.0320  188 SER A CA  
1577 C  C   . SER A 187 ? 0.0722 0.1367 0.2412 -0.0083 -0.0068 0.0252  188 SER A C   
1578 O  O   . SER A 187 ? 0.0707 0.1816 0.2326 -0.0239 -0.0049 -0.0068 188 SER A O   
1579 C  CB  . SER A 187 ? 0.1450 0.1573 0.2299 -0.0074 -0.0120 0.0401  188 SER A CB  
1580 O  OG  . SER A 187 ? 0.0996 0.1697 0.2770 -0.0142 -0.0049 0.0544  188 SER A OG  
1581 N  N   . LEU A 188 ? 0.0711 0.1593 0.2381 -0.0063 -0.0013 0.0013  189 LEU A N   
1582 C  CA  . LEU A 188 ? 0.0729 0.1432 0.2446 0.0074  -0.0105 -0.0126 189 LEU A CA  
1583 C  C   . LEU A 188 ? 0.0842 0.1259 0.2308 -0.0205 0.0034  -0.0248 189 LEU A C   
1584 O  O   . LEU A 188 ? 0.1252 0.1541 0.2211 -0.0167 -0.0005 -0.0388 189 LEU A O   
1585 C  CB  . LEU A 188 ? 0.0997 0.1837 0.2479 -0.0023 0.0057  -0.0017 189 LEU A CB  
1586 C  CG  . LEU A 188 ? 0.0923 0.1972 0.3021 -0.0010 -0.0208 0.0776  189 LEU A CG  
1587 C  CD1 . LEU A 188 ? 0.1974 0.1774 0.3443 -0.0199 -0.0320 0.0776  189 LEU A CD1 
1588 C  CD2 . LEU A 188 ? 0.0847 0.2653 0.3113 0.0052  -0.0256 0.0593  189 LEU A CD2 
1589 N  N   . ASP A 189 ? 0.0725 0.1651 0.2001 0.0126  0.0074  -0.0170 190 ASP A N   
1590 C  CA  . ASP A 189 ? 0.1115 0.1663 0.1951 -0.0489 0.0395  -0.0102 190 ASP A CA  
1591 C  C   . ASP A 189 ? 0.1077 0.1053 0.1507 -0.0262 0.0028  -0.0076 190 ASP A C   
1592 O  O   . ASP A 189 ? 0.0786 0.1155 0.1555 -0.0032 -0.0038 -0.0192 190 ASP A O   
1593 C  CB  . ASP A 189 ? 0.1331 0.2069 0.1997 -0.0948 0.0335  0.0012  190 ASP A CB  
1594 C  CG  . ASP A 189 ? 0.1629 0.3680 0.2644 -0.0350 0.0498  0.0310  190 ASP A CG  
1595 O  OD1 . ASP A 189 ? 0.1541 0.4354 0.3637 -0.0732 0.0986  -0.0685 190 ASP A OD1 
1596 O  OD2 . ASP A 189 ? 0.1685 0.5339 0.2962 -0.1462 0.0131  0.0557  190 ASP A OD2 
1597 N  N   . TYR A 190 ? 0.0925 0.1221 0.1473 -0.0144 0.0115  -0.0031 191 TYR A N   
1598 C  CA  . TYR A 190 ? 0.0847 0.1225 0.1281 -0.0215 -0.0043 0.0068  191 TYR A CA  
1599 C  C   . TYR A 190 ? 0.1022 0.1105 0.1153 0.0078  0.0295  0.0032  191 TYR A C   
1600 O  O   . TYR A 190 ? 0.1151 0.1261 0.1133 0.0098  0.0289  0.0010  191 TYR A O   
1601 C  CB  . TYR A 190 ? 0.1052 0.1094 0.1263 -0.0099 -0.0052 -0.0038 191 TYR A CB  
1602 C  CG  . TYR A 190 ? 0.0922 0.1151 0.1331 -0.0135 0.0015  0.0038  191 TYR A CG  
1603 C  CD1 . TYR A 190 ? 0.0918 0.1241 0.1406 -0.0115 -0.0031 0.0093  191 TYR A CD1 
1604 C  CD2 . TYR A 190 ? 0.1160 0.1380 0.1423 0.0074  0.0204  0.0066  191 TYR A CD2 
1605 C  CE1 . TYR A 190 ? 0.1171 0.1368 0.1485 -0.0173 0.0012  -0.0001 191 TYR A CE1 
1606 C  CE2 . TYR A 190 ? 0.1216 0.1379 0.1667 -0.0096 -0.0057 -0.0012 191 TYR A CE2 
1607 C  CZ  . TYR A 190 ? 0.1383 0.1117 0.1334 -0.0071 0.0076  -0.0080 191 TYR A CZ  
1608 O  OH  . TYR A 190 ? 0.1625 0.1394 0.1667 0.0267  -0.0003 -0.0215 191 TYR A OH  
1609 N  N   . TRP A 191 ? 0.0905 0.0790 0.1092 0.0031  -0.0001 -0.0003 192 TRP A N   
1610 C  CA  . TRP A 191 ? 0.0948 0.0790 0.1228 0.0030  0.0038  0.0097  192 TRP A CA  
1611 C  C   . TRP A 191 ? 0.0876 0.0883 0.0881 0.0041  0.0104  -0.0001 192 TRP A C   
1612 O  O   . TRP A 191 ? 0.1047 0.1108 0.0956 -0.0080 0.0040  -0.0041 192 TRP A O   
1613 C  CB  . TRP A 191 ? 0.0939 0.0847 0.1238 -0.0019 0.0109  0.0020  192 TRP A CB  
1614 C  CG  . TRP A 191 ? 0.1036 0.0842 0.1238 0.0124  -0.0027 0.0087  192 TRP A CG  
1615 C  CD1 . TRP A 191 ? 0.1544 0.1008 0.1465 0.0105  0.0153  0.0120  192 TRP A CD1 
1616 C  CD2 . TRP A 191 ? 0.0835 0.0819 0.1389 0.0051  -0.0071 0.0055  192 TRP A CD2 
1617 N  NE1 . TRP A 191 ? 0.1613 0.0939 0.1453 -0.0031 0.0068  0.0192  192 TRP A NE1 
1618 C  CE2 . TRP A 191 ? 0.1413 0.0995 0.1513 0.0010  -0.0041 0.0109  192 TRP A CE2 
1619 C  CE3 . TRP A 191 ? 0.0766 0.1306 0.1371 0.0192  -0.0015 -0.0181 192 TRP A CE3 
1620 C  CZ2 . TRP A 191 ? 0.0866 0.0952 0.2094 -0.0068 -0.0214 0.0122  192 TRP A CZ2 
1621 C  CZ3 . TRP A 191 ? 0.0889 0.1247 0.1792 0.0046  -0.0141 -0.0190 192 TRP A CZ3 
1622 C  CH2 . TRP A 191 ? 0.1067 0.1315 0.1907 0.0057  -0.0209 -0.0182 192 TRP A CH2 
1623 N  N   . THR A 192 ? 0.0968 0.0892 0.0909 0.0015  -0.0015 -0.0013 193 THR A N   
1624 C  CA  . THR A 192 ? 0.0894 0.0824 0.1027 0.0070  -0.0052 0.0043  193 THR A CA  
1625 C  C   . THR A 192 ? 0.0952 0.0898 0.1017 0.0100  0.0001  0.0093  193 THR A C   
1626 O  O   . THR A 192 ? 0.1103 0.1126 0.0988 -0.0023 0.0030  0.0024  193 THR A O   
1627 C  CB  . THR A 192 ? 0.1214 0.0714 0.1072 0.0115  0.0096  0.0031  193 THR A CB  
1628 O  OG1 . THR A 192 ? 0.1047 0.0851 0.1186 0.0173  0.0031  0.0005  193 THR A OG1 
1629 C  CG2 . THR A 192 ? 0.1185 0.1135 0.1203 0.0247  0.0219  0.0005  193 THR A CG2 
1630 N  N   . TYR A 193 ? 0.0826 0.0821 0.1010 0.0105  -0.0115 -0.0111 194 TYR A N   
1631 C  CA  . TYR A 193 ? 0.0965 0.0923 0.0953 0.0034  -0.0118 -0.0010 194 TYR A CA  
1632 C  C   . TYR A 193 ? 0.0747 0.0806 0.1106 0.0098  -0.0206 -0.0147 194 TYR A C   
1633 O  O   . TYR A 193 ? 0.0870 0.0941 0.1011 0.0099  -0.0121 -0.0035 194 TYR A O   
1634 C  CB  . TYR A 193 ? 0.1071 0.0829 0.1020 0.0074  -0.0088 -0.0037 194 TYR A CB  
1635 C  CG  . TYR A 193 ? 0.0961 0.0782 0.1101 0.0114  -0.0156 -0.0008 194 TYR A CG  
1636 C  CD1 . TYR A 193 ? 0.0956 0.0700 0.1047 0.0165  -0.0066 0.0032  194 TYR A CD1 
1637 C  CD2 . TYR A 193 ? 0.0952 0.0847 0.1187 0.0188  -0.0277 -0.0043 194 TYR A CD2 
1638 C  CE1 . TYR A 193 ? 0.0833 0.0636 0.1135 0.0114  -0.0188 0.0000  194 TYR A CE1 
1639 C  CE2 . TYR A 193 ? 0.0877 0.0722 0.1232 0.0186  -0.0162 -0.0060 194 TYR A CE2 
1640 C  CZ  . TYR A 193 ? 0.0720 0.0679 0.1054 0.0152  -0.0242 0.0003  194 TYR A CZ  
1641 O  OH  . TYR A 193 ? 0.0903 0.0733 0.1038 0.0065  -0.0154 -0.0063 194 TYR A OH  
1642 N  N   . PRO A 194 ? 0.0754 0.0934 0.1015 0.0121  -0.0177 -0.0167 195 PRO A N   
1643 C  CA  . PRO A 194 ? 0.0934 0.0912 0.1108 0.0063  -0.0006 -0.0240 195 PRO A CA  
1644 C  C   . PRO A 194 ? 0.0601 0.0763 0.1070 0.0019  -0.0167 -0.0137 195 PRO A C   
1645 O  O   . PRO A 194 ? 0.1083 0.1090 0.1047 0.0252  -0.0283 -0.0098 195 PRO A O   
1646 C  CB  . PRO A 194 ? 0.1102 0.1308 0.1144 0.0038  -0.0093 -0.0313 195 PRO A CB  
1647 C  CG  . PRO A 194 ? 0.1289 0.1194 0.1284 -0.0076 -0.0131 -0.0231 195 PRO A CG  
1648 C  CD  . PRO A 194 ? 0.1383 0.1455 0.1067 -0.0373 -0.0222 -0.0127 195 PRO A CD  
1649 N  N   . GLY A 195 ? 0.0826 0.0847 0.0992 0.0052  -0.0052 -0.0184 196 GLY A N   
1650 C  CA  . GLY A 195 ? 0.0719 0.0913 0.1099 0.0100  -0.0092 -0.0140 196 GLY A CA  
1651 C  C   . GLY A 195 ? 0.0621 0.0750 0.0966 0.0020  -0.0089 -0.0184 196 GLY A C   
1652 O  O   . GLY A 195 ? 0.0860 0.0652 0.1144 0.0063  -0.0078 -0.0182 196 GLY A O   
1653 N  N   . SER A 196 ? 0.0577 0.0776 0.0988 0.0092  -0.0089 -0.0175 197 SER A N   
1654 C  CA  . SER A 196 ? 0.0564 0.0925 0.1128 0.0017  0.0013  -0.0238 197 SER A CA  
1655 C  C   . SER A 196 ? 0.0593 0.0625 0.1097 0.0143  -0.0137 -0.0035 197 SER A C   
1656 O  O   . SER A 196 ? 0.0644 0.0709 0.1207 0.0046  -0.0094 -0.0130 197 SER A O   
1657 C  CB  . SER A 196 ? 0.0564 0.0775 0.1367 -0.0027 -0.0188 -0.0357 197 SER A CB  
1658 O  OG  . SER A 196 ? 0.0606 0.0689 0.1523 0.0062  -0.0146 -0.0121 197 SER A OG  
1659 N  N   . LEU A 197 ? 0.0494 0.0705 0.1207 0.0108  -0.0013 -0.0094 198 LEU A N   
1660 C  CA  . LEU A 197 ? 0.0736 0.0744 0.1038 -0.0040 0.0063  -0.0208 198 LEU A CA  
1661 C  C   . LEU A 197 ? 0.0546 0.0688 0.1304 -0.0063 0.0000  -0.0198 198 LEU A C   
1662 O  O   . LEU A 197 ? 0.0571 0.0935 0.1432 -0.0001 -0.0048 -0.0245 198 LEU A O   
1663 C  CB  . LEU A 197 ? 0.0857 0.0819 0.1329 -0.0017 0.0103  -0.0021 198 LEU A CB  
1664 C  CG  . LEU A 197 ? 0.1018 0.0719 0.1421 -0.0017 0.0055  -0.0010 198 LEU A CG  
1665 C  CD1 . LEU A 197 ? 0.1205 0.1207 0.1695 -0.0401 0.0102  -0.0008 198 LEU A CD1 
1666 C  CD2 . LEU A 197 ? 0.0795 0.1045 0.1907 0.0103  0.0181  0.0152  198 LEU A CD2 
1667 N  N   . THR A 198 ? 0.0597 0.0684 0.1221 0.0076  -0.0103 -0.0184 199 THR A N   
1668 C  CA  . THR A 198 ? 0.0630 0.0659 0.1534 0.0087  0.0051  -0.0240 199 THR A CA  
1669 C  C   . THR A 198 ? 0.0555 0.0780 0.1416 0.0114  -0.0088 -0.0161 199 THR A C   
1670 O  O   . THR A 198 ? 0.0675 0.0851 0.1586 0.0126  0.0077  -0.0177 199 THR A O   
1671 C  CB  . THR A 198 ? 0.0731 0.0768 0.1264 -0.0121 -0.0143 -0.0212 199 THR A CB  
1672 O  OG1 . THR A 198 ? 0.0829 0.0725 0.1121 -0.0015 -0.0057 -0.0135 199 THR A OG1 
1673 C  CG2 . THR A 198 ? 0.0741 0.0881 0.1324 -0.0008 0.0032  -0.0154 199 THR A CG2 
1674 N  N   . THR A 199 ? 0.0773 0.0879 0.1465 0.0076  0.0170  -0.0151 200 THR A N   
1675 C  CA  . THR A 199 ? 0.0864 0.0850 0.1611 -0.0081 0.0131  -0.0237 200 THR A CA  
1676 C  C   . THR A 199 ? 0.0817 0.0920 0.1629 -0.0068 0.0181  -0.0305 200 THR A C   
1677 O  O   . THR A 199 ? 0.0751 0.0905 0.1584 -0.0121 0.0130  -0.0324 200 THR A O   
1678 C  CB  . THR A 199 ? 0.0842 0.1040 0.1550 0.0007  0.0065  -0.0165 200 THR A CB  
1679 O  OG1 . THR A 199 ? 0.1871 0.1376 0.1771 0.0540  0.0052  -0.0247 200 THR A OG1 
1680 C  CG2 . THR A 199 ? 0.1504 0.1372 0.1568 -0.0527 0.0096  -0.0212 200 THR A CG2 
1681 N  N   . PRO A 200 ? 0.0829 0.1101 0.1738 -0.0187 0.0251  -0.0293 201 PRO A N   
1682 C  CA  . PRO A 200 ? 0.0855 0.1216 0.1755 -0.0297 0.0275  -0.0208 201 PRO A CA  
1683 C  C   . PRO A 200 ? 0.1135 0.1221 0.1798 -0.0052 0.0266  -0.0226 201 PRO A C   
1684 O  O   . PRO A 200 ? 0.1331 0.1340 0.1753 -0.0176 0.0129  -0.0168 201 PRO A O   
1685 C  CB  . PRO A 200 ? 0.1225 0.1401 0.2051 0.0057  0.0432  -0.0199 201 PRO A CB  
1686 C  CG  . PRO A 200 ? 0.0803 0.1544 0.1944 -0.0151 0.0342  -0.0307 201 PRO A CG  
1687 C  CD  . PRO A 200 ? 0.0864 0.1401 0.2087 -0.0099 0.0348  -0.0527 201 PRO A CD  
1688 N  N   . PRO A 201 ? 0.0856 0.1297 0.1773 -0.0248 0.0225  -0.0099 202 PRO A N   
1689 C  CA  . PRO A 201 ? 0.0921 0.1209 0.1899 -0.0225 0.0197  -0.0187 202 PRO A CA  
1690 C  C   . PRO A 201 ? 0.0822 0.1343 0.1712 -0.0102 -0.0010 -0.0204 202 PRO A C   
1691 O  O   . PRO A 201 ? 0.0908 0.1092 0.1969 -0.0160 0.0129  -0.0211 202 PRO A O   
1692 C  CB  . PRO A 201 ? 0.1286 0.1063 0.2570 -0.0230 0.0326  0.0137  202 PRO A CB  
1693 C  CG  . PRO A 201 ? 0.1381 0.1065 0.2439 -0.0024 0.0217  -0.0333 202 PRO A CG  
1694 C  CD  . PRO A 201 ? 0.1371 0.1117 0.1780 0.0024  0.0177  -0.0076 202 PRO A CD  
1695 N  N   . LEU A 202 ? 0.0904 0.0959 0.1514 -0.0068 0.0217  -0.0074 203 LEU A N   
1696 C  CA  . LEU A 202 ? 0.0693 0.1054 0.1547 0.0105  -0.0057 -0.0240 203 LEU A CA  
1697 C  C   . LEU A 202 ? 0.0698 0.0870 0.1455 -0.0094 -0.0076 -0.0043 203 LEU A C   
1698 O  O   . LEU A 202 ? 0.0750 0.0799 0.1536 0.0049  -0.0154 -0.0140 203 LEU A O   
1699 C  CB  . LEU A 202 ? 0.0521 0.1063 0.1868 0.0076  -0.0170 -0.0461 203 LEU A CB  
1700 C  CG  . LEU A 202 ? 0.0472 0.1077 0.2026 0.0048  0.0133  -0.0494 203 LEU A CG  
1701 C  CD1 . LEU A 202 ? 0.0574 0.1230 0.2469 0.0049  0.0041  -0.0320 203 LEU A CD1 
1702 C  CD2 . LEU A 202 ? 0.0715 0.1094 0.1925 -0.0032 -0.0034 -0.0271 203 LEU A CD2 
1703 N  N   . LEU A 203 ? 0.0595 0.0798 0.1680 0.0027  -0.0098 -0.0198 204 LEU A N   
1704 C  CA  . LEU A 203 ? 0.0776 0.0754 0.1694 0.0015  -0.0038 -0.0342 204 LEU A CA  
1705 C  C   . LEU A 203 ? 0.0675 0.0749 0.1631 0.0003  -0.0089 -0.0148 204 LEU A C   
1706 O  O   . LEU A 203 ? 0.0811 0.0835 0.1446 -0.0041 -0.0137 -0.0256 204 LEU A O   
1707 C  CB  . LEU A 203 ? 0.0950 0.0813 0.1782 -0.0089 -0.0154 -0.0103 204 LEU A CB  
1708 C  CG  . LEU A 203 ? 0.1101 0.1090 0.2035 -0.0049 0.0222  -0.0116 204 LEU A CG  
1709 C  CD1 . LEU A 203 ? 0.1647 0.1002 0.2513 -0.0021 0.0423  0.0274  204 LEU A CD1 
1710 C  CD2 . LEU A 203 ? 0.0997 0.1579 0.3285 -0.0421 0.0184  0.0211  204 LEU A CD2 
1711 N  N   . GLU A 204 ? 0.0923 0.0941 0.1485 -0.0041 -0.0052 -0.0315 205 GLU A N   
1712 C  CA  . GLU A 204 ? 0.1000 0.1035 0.1316 0.0140  -0.0203 -0.0351 205 GLU A CA  
1713 C  C   . GLU A 204 ? 0.1002 0.0873 0.1505 0.0013  -0.0340 -0.0292 205 GLU A C   
1714 O  O   . GLU A 204 ? 0.1169 0.1317 0.1536 0.0320  -0.0252 -0.0553 205 GLU A O   
1715 C  CB  . GLU A 204 ? 0.1056 0.0996 0.1719 0.0153  -0.0483 -0.0351 205 GLU A CB  
1716 C  CG  . GLU A 204 ? 0.1090 0.1041 0.1917 0.0184  -0.0524 -0.0425 205 GLU A CG  
1717 C  CD  . GLU A 204 ? 0.1130 0.1173 0.1825 0.0154  -0.0460 -0.0430 205 GLU A CD  
1718 O  OE1 . GLU A 204 ? 0.1439 0.1545 0.2317 0.0412  -0.0938 -0.0693 205 GLU A OE1 
1719 O  OE2 . GLU A 204 ? 0.1119 0.1180 0.1938 0.0059  -0.0527 -0.0175 205 GLU A OE2 
1720 N  N   . CYS A 205 ? 0.0676 0.0816 0.1414 0.0032  -0.0198 -0.0138 206 CYS A N   
1721 C  CA  . CYS A 205 ? 0.0684 0.0901 0.1419 0.0012  -0.0182 -0.0043 206 CYS A CA  
1722 C  C   . CYS A 205 ? 0.0639 0.0690 0.1297 0.0088  -0.0130 -0.0182 206 CYS A C   
1723 O  O   . CYS A 205 ? 0.0914 0.0745 0.1703 0.0171  -0.0340 0.0003  206 CYS A O   
1724 C  CB  . CYS A 205 ? 0.0989 0.0732 0.1406 0.0020  -0.0060 -0.0127 206 CYS A CB  
1725 S  SG  . CYS A 205 ? 0.1193 0.0912 0.1425 0.0082  -0.0107 -0.0105 206 CYS A SG  
1726 N  N   . VAL A 206 ? 0.0732 0.0640 0.1259 -0.0035 -0.0207 -0.0089 207 VAL A N   
1727 C  CA  . VAL A 206 ? 0.0590 0.0706 0.1252 0.0054  -0.0086 -0.0089 207 VAL A CA  
1728 C  C   . VAL A 206 ? 0.0716 0.0637 0.1214 0.0273  -0.0216 -0.0030 207 VAL A C   
1729 O  O   . VAL A 206 ? 0.0782 0.0993 0.1361 0.0179  -0.0181 0.0175  207 VAL A O   
1730 C  CB  . VAL A 206 ? 0.0644 0.0816 0.1288 0.0080  0.0031  -0.0068 207 VAL A CB  
1731 C  CG1 . VAL A 206 ? 0.0676 0.0918 0.1403 0.0000  -0.0186 -0.0217 207 VAL A CG1 
1732 C  CG2 . VAL A 206 ? 0.0724 0.0939 0.1554 0.0073  0.0000  -0.0197 207 VAL A CG2 
1733 N  N   . THR A 207 ? 0.0702 0.0573 0.1117 -0.0040 -0.0175 -0.0087 208 THR A N   
1734 C  CA  . THR A 207 ? 0.0889 0.0744 0.1117 -0.0027 -0.0135 -0.0023 208 THR A CA  
1735 C  C   . THR A 207 ? 0.0883 0.0644 0.0844 -0.0105 -0.0038 0.0000  208 THR A C   
1736 O  O   . THR A 207 ? 0.0819 0.0635 0.1065 0.0059  -0.0157 -0.0087 208 THR A O   
1737 C  CB  . THR A 207 ? 0.0889 0.0667 0.1203 0.0048  0.0027  -0.0131 208 THR A CB  
1738 O  OG1 . THR A 207 ? 0.1171 0.0829 0.1308 0.0060  -0.0041 -0.0249 208 THR A OG1 
1739 C  CG2 . THR A 207 ? 0.1284 0.0952 0.1444 -0.0013 0.0051  -0.0032 208 THR A CG2 
1740 N  N   . TRP A 208 ? 0.0722 0.0540 0.0961 0.0003  -0.0098 -0.0073 209 TRP A N   
1741 C  CA  . TRP A 208 ? 0.0590 0.0577 0.1108 0.0116  -0.0124 -0.0141 209 TRP A CA  
1742 C  C   . TRP A 208 ? 0.0688 0.0577 0.0896 0.0055  -0.0093 0.0013  209 TRP A C   
1743 O  O   . TRP A 208 ? 0.0759 0.0794 0.0964 -0.0013 -0.0060 -0.0010 209 TRP A O   
1744 C  CB  . TRP A 208 ? 0.0694 0.0649 0.1089 0.0164  -0.0105 0.0003  209 TRP A CB  
1745 C  CG  . TRP A 208 ? 0.0555 0.0604 0.1099 0.0137  -0.0040 -0.0054 209 TRP A CG  
1746 C  CD1 . TRP A 208 ? 0.0675 0.0657 0.1171 0.0118  -0.0143 -0.0063 209 TRP A CD1 
1747 C  CD2 . TRP A 208 ? 0.0474 0.0625 0.1223 0.0116  -0.0076 -0.0086 209 TRP A CD2 
1748 N  NE1 . TRP A 208 ? 0.0605 0.0747 0.1263 0.0027  -0.0020 -0.0034 209 TRP A NE1 
1749 C  CE2 . TRP A 208 ? 0.0588 0.0737 0.1092 0.0140  -0.0037 -0.0007 209 TRP A CE2 
1750 C  CE3 . TRP A 208 ? 0.0511 0.0623 0.1054 0.0116  -0.0068 -0.0032 209 TRP A CE3 
1751 C  CZ2 . TRP A 208 ? 0.0676 0.0830 0.1226 0.0342  0.0059  -0.0051 209 TRP A CZ2 
1752 C  CZ3 . TRP A 208 ? 0.0788 0.0844 0.1027 0.0247  -0.0008 0.0031  209 TRP A CZ3 
1753 C  CH2 . TRP A 208 ? 0.0912 0.0702 0.1235 0.0286  0.0001  -0.0107 209 TRP A CH2 
1754 N  N   . ILE A 209 ? 0.0560 0.0650 0.0970 0.0020  -0.0104 -0.0063 210 ILE A N   
1755 C  CA  . ILE A 209 ? 0.0579 0.0657 0.1083 0.0020  -0.0082 -0.0155 210 ILE A CA  
1756 C  C   . ILE A 209 ? 0.0511 0.0715 0.0882 -0.0013 0.0035  0.0001  210 ILE A C   
1757 O  O   . ILE A 209 ? 0.1013 0.0698 0.0912 -0.0013 -0.0035 -0.0008 210 ILE A O   
1758 C  CB  . ILE A 209 ? 0.0579 0.0707 0.1392 0.0093  -0.0057 -0.0038 210 ILE A CB  
1759 C  CG1 . ILE A 209 ? 0.0869 0.0776 0.1705 0.0200  -0.0076 -0.0217 210 ILE A CG1 
1760 C  CG2 . ILE A 209 ? 0.0543 0.1205 0.1509 0.0132  -0.0094 -0.0153 210 ILE A CG2 
1761 C  CD1 . ILE A 209 ? 0.0816 0.0954 0.2366 0.0449  0.0076  0.0077  210 ILE A CD1 
1762 N  N   . VAL A 210 ? 0.0662 0.0571 0.1133 0.0057  0.0001  -0.0015 211 VAL A N   
1763 C  CA  . VAL A 210 ? 0.0646 0.0666 0.0995 0.0026  -0.0008 -0.0082 211 VAL A CA  
1764 C  C   . VAL A 210 ? 0.0700 0.0672 0.0982 0.0160  -0.0006 0.0099  211 VAL A C   
1765 O  O   . VAL A 210 ? 0.0857 0.0829 0.1020 -0.0063 0.0077  0.0020  211 VAL A O   
1766 C  CB  . VAL A 210 ? 0.0639 0.0778 0.1241 0.0034  -0.0082 -0.0048 211 VAL A CB  
1767 C  CG1 . VAL A 210 ? 0.0892 0.0701 0.1453 0.0026  0.0000  -0.0133 211 VAL A CG1 
1768 C  CG2 . VAL A 210 ? 0.0789 0.0979 0.1256 0.0038  -0.0153 -0.0060 211 VAL A CG2 
1769 N  N   . LEU A 211 ? 0.0645 0.0825 0.1187 0.0071  -0.0063 -0.0055 212 LEU A N   
1770 C  CA  . LEU A 211 ? 0.0702 0.0905 0.1232 -0.0115 -0.0097 0.0017  212 LEU A CA  
1771 C  C   . LEU A 211 ? 0.0680 0.0830 0.1180 0.0000  -0.0065 0.0006  212 LEU A C   
1772 O  O   . LEU A 211 ? 0.0847 0.0903 0.1189 0.0020  -0.0060 -0.0044 212 LEU A O   
1773 C  CB  . LEU A 211 ? 0.0702 0.1015 0.1328 -0.0038 -0.0130 0.0006  212 LEU A CB  
1774 C  CG  . LEU A 211 ? 0.0917 0.0907 0.1435 -0.0146 -0.0196 0.0077  212 LEU A CG  
1775 C  CD1 . LEU A 211 ? 0.0810 0.1446 0.1956 -0.0118 -0.0564 0.0195  212 LEU A CD1 
1776 C  CD2 . LEU A 211 ? 0.0957 0.1156 0.1672 0.0097  0.0073  0.0031  212 LEU A CD2 
1777 N  N   A LYS A 212 ? 0.0847 0.0971 0.1159 -0.0151 -0.0127 0.0085  213 LYS A N   
1778 N  N   B LYS A 212 ? 0.0896 0.0957 0.1160 -0.0114 -0.0104 0.0105  213 LYS A N   
1779 C  CA  A LYS A 212 ? 0.1001 0.0898 0.1304 -0.0225 -0.0046 0.0182  213 LYS A CA  
1780 C  CA  B LYS A 212 ? 0.1022 0.0879 0.1336 -0.0201 -0.0052 0.0172  213 LYS A CA  
1781 C  C   A LYS A 212 ? 0.0680 0.0864 0.1482 -0.0111 -0.0020 0.0148  213 LYS A C   
1782 C  C   B LYS A 212 ? 0.0703 0.0925 0.1485 -0.0070 -0.0030 0.0122  213 LYS A C   
1783 O  O   A LYS A 212 ? 0.0932 0.1006 0.1723 0.0020  -0.0318 0.0173  213 LYS A O   
1784 O  O   B LYS A 212 ? 0.0962 0.0996 0.1746 0.0003  -0.0313 0.0133  213 LYS A O   
1785 C  CB  A LYS A 212 ? 0.1333 0.1385 0.1519 -0.0476 0.0083  0.0156  213 LYS A CB  
1786 C  CB  B LYS A 212 ? 0.1428 0.1421 0.1548 -0.0478 0.0102  0.0098  213 LYS A CB  
1787 C  CG  A LYS A 212 ? 0.1776 0.1448 0.1879 -0.0236 0.0153  0.0399  213 LYS A CG  
1788 C  CG  B LYS A 212 ? 0.2162 0.1349 0.2225 -0.0113 -0.0260 0.0230  213 LYS A CG  
1789 C  CD  A LYS A 212 ? 0.3621 0.2407 0.1672 -0.1159 0.0030  0.0658  213 LYS A CD  
1790 C  CD  B LYS A 212 ? 0.3860 0.1875 0.2556 -0.1463 0.0219  -0.0948 213 LYS A CD  
1791 C  CE  A LYS A 212 ? 0.3337 0.2351 0.2493 -0.0500 0.0570  0.1045  213 LYS A CE  
1792 C  CE  B LYS A 212 ? 0.4636 0.2524 0.3181 -0.0676 0.0173  -0.0776 213 LYS A CE  
1793 N  NZ  A LYS A 212 ? 0.4587 0.3943 0.2365 -0.1009 0.0684  0.0684  213 LYS A NZ  
1794 N  NZ  B LYS A 212 ? 0.5357 0.4591 0.6434 -0.3021 -0.0513 -0.2029 213 LYS A NZ  
1795 N  N   . GLU A 213 ? 0.0755 0.0968 0.1347 0.0008  -0.0148 0.0034  214 GLU A N   
1796 C  CA  . GLU A 213 ? 0.0905 0.0997 0.1365 -0.0208 -0.0166 -0.0026 214 GLU A CA  
1797 C  C   . GLU A 213 ? 0.0593 0.0959 0.1378 -0.0078 -0.0195 0.0132  214 GLU A C   
1798 O  O   . GLU A 213 ? 0.0728 0.0824 0.1471 0.0010  -0.0131 0.0144  214 GLU A O   
1799 C  CB  . GLU A 213 ? 0.0802 0.1259 0.1652 -0.0197 -0.0355 0.0161  214 GLU A CB  
1800 C  CG  . GLU A 213 ? 0.0979 0.1389 0.1983 -0.0359 -0.0474 0.0059  214 GLU A CG  
1801 C  CD  . GLU A 213 ? 0.1101 0.2376 0.2430 -0.0489 -0.0408 -0.0289 214 GLU A CD  
1802 O  OE1 . GLU A 213 ? 0.0957 0.1631 0.3605 -0.0142 -0.0604 0.0344  214 GLU A OE1 
1803 O  OE2 . GLU A 213 ? 0.1579 0.5349 0.4713 -0.0848 -0.0926 -0.2178 214 GLU A OE2 
1804 N  N   A PRO A 214 ? 0.0887 0.0697 0.1351 -0.0049 -0.0135 0.0105  215 PRO A N   
1805 N  N   B PRO A 214 ? 0.0984 0.0826 0.1410 -0.0052 -0.0115 0.0010  215 PRO A N   
1806 C  CA  A PRO A 214 ? 0.0856 0.0775 0.1313 0.0116  -0.0188 0.0000  215 PRO A CA  
1807 C  CA  B PRO A 214 ? 0.0907 0.0833 0.1344 0.0136  -0.0186 -0.0003 215 PRO A CA  
1808 C  C   A PRO A 214 ? 0.0749 0.0961 0.1480 -0.0126 -0.0322 -0.0140 215 PRO A C   
1809 C  C   B PRO A 214 ? 0.0816 0.0954 0.1501 -0.0152 -0.0307 -0.0129 215 PRO A C   
1810 O  O   A PRO A 214 ? 0.0943 0.1309 0.1615 -0.0276 -0.0368 0.0035  215 PRO A O   
1811 O  O   B PRO A 214 ? 0.1033 0.1329 0.1629 -0.0289 -0.0351 0.0054  215 PRO A O   
1812 C  CB  A PRO A 214 ? 0.1032 0.0742 0.1426 0.0192  -0.0020 0.0243  215 PRO A CB  
1813 C  CB  B PRO A 214 ? 0.1135 0.0782 0.1687 0.0214  -0.0043 0.0131  215 PRO A CB  
1814 C  CG  A PRO A 214 ? 0.1155 0.0490 0.1433 -0.0089 0.0126  0.0003  215 PRO A CG  
1815 C  CG  B PRO A 214 ? 0.1926 0.1456 0.2048 0.0135  0.0096  -0.0165 215 PRO A CG  
1816 C  CD  A PRO A 214 ? 0.0684 0.0467 0.1451 -0.0116 0.0076  0.0071  215 PRO A CD  
1817 C  CD  B PRO A 214 ? 0.1847 0.0921 0.1985 -0.0020 0.0181  0.0383  215 PRO A CD  
1818 N  N   . ILE A 215 ? 0.1093 0.0841 0.1217 0.0020  -0.0289 -0.0102 216 ILE A N   
1819 C  CA  . ILE A 215 ? 0.1174 0.0808 0.1337 0.0093  -0.0339 -0.0303 216 ILE A CA  
1820 C  C   . ILE A 215 ? 0.1036 0.1011 0.1243 0.0097  -0.0263 -0.0203 216 ILE A C   
1821 O  O   . ILE A 215 ? 0.1115 0.0950 0.1652 -0.0008 -0.0337 -0.0192 216 ILE A O   
1822 C  CB  . ILE A 215 ? 0.1326 0.0822 0.1505 0.0142  -0.0326 -0.0099 216 ILE A CB  
1823 C  CG1 . ILE A 215 ? 0.1607 0.1004 0.1371 0.0010  -0.0388 0.0000  216 ILE A CG1 
1824 C  CG2 . ILE A 215 ? 0.1844 0.0977 0.1626 0.0307  -0.0438 -0.0105 216 ILE A CG2 
1825 C  CD1 . ILE A 215 ? 0.2141 0.0974 0.1647 0.0118  -0.0445 0.0115  216 ILE A CD1 
1826 N  N   A SER A 216 ? 0.1098 0.1063 0.1532 0.0098  -0.0351 -0.0310 217 SER A N   
1827 N  N   B SER A 216 ? 0.1061 0.1097 0.1541 0.0115  -0.0348 -0.0311 217 SER A N   
1828 C  CA  A SER A 216 ? 0.1239 0.0900 0.1372 0.0000  -0.0263 -0.0262 217 SER A CA  
1829 C  CA  B SER A 216 ? 0.1277 0.0954 0.1385 0.0000  -0.0264 -0.0278 217 SER A CA  
1830 C  C   A SER A 216 ? 0.1431 0.0639 0.1374 -0.0010 -0.0529 -0.0245 217 SER A C   
1831 C  C   B SER A 216 ? 0.1426 0.0627 0.1396 -0.0017 -0.0524 -0.0234 217 SER A C   
1832 O  O   A SER A 216 ? 0.1424 0.1044 0.1688 0.0155  -0.0494 -0.0046 217 SER A O   
1833 O  O   B SER A 216 ? 0.1425 0.1040 0.1686 0.0155  -0.0493 -0.0046 217 SER A O   
1834 C  CB  A SER A 216 ? 0.2355 0.0430 0.1728 -0.0190 -0.0031 -0.0251 217 SER A CB  
1835 C  CB  B SER A 216 ? 0.2355 0.1076 0.1954 -0.0421 0.0046  0.0241  217 SER A CB  
1836 O  OG  A SER A 216 ? 0.1453 0.0905 0.1934 -0.0571 -0.0478 -0.0006 217 SER A OG  
1837 O  OG  B SER A 216 ? 0.3133 0.1487 0.2682 -0.0487 -0.0392 -0.0313 217 SER A OG  
1838 N  N   . VAL A 217 ? 0.1491 0.0800 0.1272 -0.0162 -0.0353 -0.0141 218 VAL A N   
1839 C  CA  . VAL A 217 ? 0.1771 0.0650 0.1396 -0.0070 -0.0351 -0.0120 218 VAL A CA  
1840 C  C   . VAL A 217 ? 0.1422 0.0777 0.1327 -0.0151 -0.0274 -0.0068 218 VAL A C   
1841 O  O   . VAL A 217 ? 0.1577 0.0750 0.1410 -0.0212 -0.0359 -0.0035 218 VAL A O   
1842 C  CB  . VAL A 217 ? 0.1553 0.0597 0.1893 -0.0077 -0.0474 -0.0006 218 VAL A CB  
1843 C  CG1 . VAL A 217 ? 0.1782 0.0709 0.1710 -0.0098 -0.0348 -0.0148 218 VAL A CG1 
1844 C  CG2 . VAL A 217 ? 0.1437 0.0943 0.2152 -0.0116 -0.0265 0.0041  218 VAL A CG2 
1845 N  N   . SER A 218 ? 0.1753 0.0672 0.1340 -0.0049 -0.0390 -0.0114 219 SER A N   
1846 C  CA  . SER A 218 ? 0.1690 0.0784 0.1559 -0.0232 -0.0256 -0.0253 219 SER A CA  
1847 C  C   . SER A 218 ? 0.1773 0.0759 0.1377 -0.0181 -0.0249 -0.0081 219 SER A C   
1848 O  O   . SER A 218 ? 0.1827 0.0788 0.1528 -0.0199 -0.0304 -0.0115 219 SER A O   
1849 C  CB  . SER A 218 ? 0.1658 0.0905 0.1444 -0.0116 -0.0342 -0.0209 219 SER A CB  
1850 O  OG  . SER A 218 ? 0.2213 0.1004 0.1462 -0.0125 -0.0454 -0.0115 219 SER A OG  
1851 N  N   A SER A 219 ? 0.1663 0.0741 0.1607 -0.0093 -0.0373 -0.0198 220 SER A N   
1852 N  N   B SER A 219 ? 0.1819 0.0608 0.1744 -0.0208 -0.0219 0.0006  220 SER A N   
1853 C  CA  A SER A 219 ? 0.1722 0.0847 0.1922 -0.0211 -0.0241 -0.0333 220 SER A CA  
1854 C  CA  B SER A 219 ? 0.1938 0.0750 0.2098 -0.0198 -0.0105 0.0049  220 SER A CA  
1855 C  C   A SER A 219 ? 0.2162 0.0750 0.2098 -0.0247 -0.0286 -0.0201 220 SER A C   
1856 C  C   B SER A 219 ? 0.2310 0.0742 0.2058 -0.0262 -0.0307 -0.0019 220 SER A C   
1857 O  O   A SER A 219 ? 0.2164 0.1040 0.2241 -0.0082 0.0037  0.0031  220 SER A O   
1858 O  O   B SER A 219 ? 0.2583 0.0657 0.2443 -0.0236 -0.0166 0.0026  220 SER A O   
1859 C  CB  A SER A 219 ? 0.1817 0.0989 0.2741 -0.0172 -0.0197 -0.0208 220 SER A CB  
1860 C  CB  B SER A 219 ? 0.1817 0.0874 0.2563 -0.0421 -0.0364 0.0089  220 SER A CB  
1861 O  OG  A SER A 219 ? 0.1811 0.0794 0.2442 0.0054  -0.0087 -0.0311 220 SER A OG  
1862 O  OG  B SER A 219 ? 0.2154 0.1255 0.1974 -0.0121 -0.0093 0.0028  220 SER A OG  
1863 N  N   . GLU A 220 ? 0.2191 0.0750 0.1604 -0.0020 -0.0099 -0.0182 221 GLU A N   
1864 C  CA  . GLU A 220 ? 0.2450 0.1011 0.1841 -0.0105 -0.0162 -0.0198 221 GLU A CA  
1865 C  C   . GLU A 220 ? 0.2658 0.1070 0.1437 -0.0062 -0.0232 -0.0046 221 GLU A C   
1866 O  O   . GLU A 220 ? 0.2619 0.1112 0.1640 0.0071  0.0258  -0.0238 221 GLU A O   
1867 C  CB  . GLU A 220 ? 0.3456 0.1556 0.1843 -0.0211 -0.0463 -0.0564 221 GLU A CB  
1868 C  CG  . GLU A 220 ? 0.4029 0.1787 0.3046 -0.0812 -0.1477 -0.0755 221 GLU A CG  
1869 C  CD  . GLU A 220 ? 0.5260 0.1316 0.3319 -0.0472 0.0153  -0.1246 221 GLU A CD  
1870 O  OE1 . GLU A 220 ? 0.3037 0.1444 0.3485 -0.0617 0.0089  -0.0746 221 GLU A OE1 
1871 O  OE2 . GLU A 220 ? 1.2136 0.4350 0.8661 -0.5264 0.4023  -0.4160 221 GLU A OE2 
1872 N  N   . GLN A 221 ? 0.2064 0.0864 0.1521 -0.0093 -0.0283 -0.0229 222 GLN A N   
1873 C  CA  . GLN A 221 ? 0.2073 0.0842 0.1442 -0.0164 -0.0292 0.0059  222 GLN A CA  
1874 C  C   . GLN A 221 ? 0.1750 0.0854 0.1554 -0.0023 -0.0214 0.0032  222 GLN A C   
1875 O  O   . GLN A 221 ? 0.2087 0.1071 0.1602 -0.0344 -0.0192 0.0093  222 GLN A O   
1876 C  CB  . GLN A 221 ? 0.2078 0.1068 0.1252 -0.0144 -0.0375 -0.0178 222 GLN A CB  
1877 C  CG  . GLN A 221 ? 0.2042 0.0975 0.1283 -0.0434 -0.0397 -0.0126 222 GLN A CG  
1878 C  CD  . GLN A 221 ? 0.1881 0.0785 0.1536 -0.0217 -0.0526 -0.0015 222 GLN A CD  
1879 O  OE1 . GLN A 221 ? 0.1829 0.0941 0.1455 -0.0096 -0.0366 -0.0105 222 GLN A OE1 
1880 N  NE2 . GLN A 221 ? 0.1951 0.1031 0.1656 -0.0107 -0.0601 -0.0006 222 GLN A NE2 
1881 N  N   . VAL A 222 ? 0.1981 0.0973 0.1541 0.0081  -0.0189 0.0020  223 VAL A N   
1882 C  CA  . VAL A 222 ? 0.2017 0.1225 0.1640 -0.0073 -0.0194 0.0383  223 VAL A CA  
1883 C  C   . VAL A 222 ? 0.2087 0.0959 0.1713 -0.0093 -0.0135 0.0038  223 VAL A C   
1884 O  O   . VAL A 222 ? 0.1967 0.1282 0.1719 -0.0370 -0.0089 0.0136  223 VAL A O   
1885 C  CB  . VAL A 222 ? 0.1906 0.1365 0.1762 -0.0114 -0.0313 0.0311  223 VAL A CB  
1886 C  CG1 . VAL A 222 ? 0.1696 0.1588 0.2062 -0.0542 -0.0507 0.0706  223 VAL A CG1 
1887 C  CG2 . VAL A 222 ? 0.2089 0.1473 0.2117 0.0028  -0.0573 -0.0100 223 VAL A CG2 
1888 N  N   . LEU A 223 ? 0.1981 0.1123 0.1914 -0.0159 0.0013  0.0017  224 LEU A N   
1889 C  CA  . LEU A 223 ? 0.2240 0.1106 0.2328 -0.0234 0.0184  -0.0144 224 LEU A CA  
1890 C  C   . LEU A 223 ? 0.2890 0.1171 0.1904 -0.0229 0.0159  -0.0370 224 LEU A C   
1891 O  O   . LEU A 223 ? 0.2491 0.1704 0.2053 -0.0089 0.0261  -0.0342 224 LEU A O   
1892 C  CB  . LEU A 223 ? 0.3267 0.1017 0.2743 -0.0143 0.0480  -0.0500 224 LEU A CB  
1893 C  CG  . LEU A 223 ? 0.3337 0.1388 0.3098 -0.0340 0.0476  -0.0133 224 LEU A CG  
1894 C  CD1 . LEU A 223 ? 0.3675 0.1539 0.4165 -0.0184 -0.0313 -0.0135 224 LEU A CD1 
1895 C  CD2 . LEU A 223 ? 0.3079 0.2101 0.3968 -0.0021 0.0432  -0.0298 224 LEU A CD2 
1896 N  N   . LYS A 224 ? 0.2750 0.1115 0.1625 -0.0386 -0.0113 -0.0093 225 LYS A N   
1897 C  CA  . LYS A 224 ? 0.2524 0.1737 0.1631 -0.0120 0.0214  0.0109  225 LYS A CA  
1898 C  C   . LYS A 224 ? 0.3154 0.1282 0.1202 -0.0113 0.0144  0.0207  225 LYS A C   
1899 O  O   . LYS A 224 ? 0.2651 0.1395 0.1241 -0.0234 0.0242  0.0030  225 LYS A O   
1900 C  CB  . LYS A 224 ? 0.2714 0.2186 0.2053 0.0161  0.0008  0.0621  225 LYS A CB  
1901 C  CG  . LYS A 224 ? 0.3079 0.3876 0.2295 -0.0551 -0.0542 -0.0094 225 LYS A CG  
1902 C  CD  . LYS A 224 ? 0.4090 0.2851 0.3176 0.0074  -0.0668 -0.0755 225 LYS A CD  
1903 C  CE  . LYS A 224 ? 0.5054 0.5157 0.3912 -0.0487 -0.0582 -0.1965 225 LYS A CE  
1904 N  NZ  . LYS A 224 ? 0.4151 0.3016 0.6032 -0.0846 0.0288  -0.0896 225 LYS A NZ  
1905 N  N   . PHE A 225 ? 0.2518 0.1232 0.1177 -0.0165 0.0280  -0.0013 226 PHE A N   
1906 C  CA  . PHE A 225 ? 0.2407 0.0846 0.1504 -0.0137 0.0379  -0.0032 226 PHE A CA  
1907 C  C   . PHE A 225 ? 0.2382 0.0828 0.1449 -0.0250 0.0298  0.0008  226 PHE A C   
1908 O  O   . PHE A 225 ? 0.2481 0.1054 0.1325 -0.0329 0.0337  -0.0313 226 PHE A O   
1909 C  CB  . PHE A 225 ? 0.2197 0.1178 0.1279 0.0000  0.0227  0.0094  226 PHE A CB  
1910 C  CG  . PHE A 225 ? 0.2342 0.0926 0.1518 -0.0542 0.0353  -0.0340 226 PHE A CG  
1911 C  CD1 . PHE A 225 ? 0.2563 0.1651 0.2049 0.0085  0.0333  0.0012  226 PHE A CD1 
1912 C  CD2 . PHE A 225 ? 0.2610 0.1421 0.1665 -0.0217 0.0116  -0.0465 226 PHE A CD2 
1913 C  CE1 . PHE A 225 ? 0.3048 0.1667 0.2177 0.0401  0.0529  0.0027  226 PHE A CE1 
1914 C  CE2 . PHE A 225 ? 0.1972 0.1929 0.2286 -0.0368 0.0026  -0.0975 226 PHE A CE2 
1915 C  CZ  . PHE A 225 ? 0.2410 0.1250 0.2375 -0.0526 -0.0143 -0.0524 226 PHE A CZ  
1916 N  N   . ARG A 226 ? 0.2152 0.1020 0.1218 -0.0078 0.0013  0.0052  227 ARG A N   
1917 C  CA  . ARG A 226 ? 0.2082 0.1280 0.1306 -0.0432 0.0209  -0.0147 227 ARG A CA  
1918 C  C   . ARG A 226 ? 0.2401 0.1061 0.1638 -0.0373 0.0394  -0.0244 227 ARG A C   
1919 O  O   . ARG A 226 ? 0.2549 0.1703 0.1580 -0.0057 0.0430  -0.0065 227 ARG A O   
1920 C  CB  . ARG A 226 ? 0.2375 0.0934 0.1597 0.0131  0.0419  -0.0120 227 ARG A CB  
1921 C  CG  . ARG A 226 ? 0.2324 0.1182 0.1521 -0.0262 0.0293  0.0049  227 ARG A CG  
1922 C  CD  . ARG A 226 ? 0.2899 0.1119 0.1615 -0.0113 0.0286  0.0118  227 ARG A CD  
1923 N  NE  . ARG A 226 ? 0.1908 0.1156 0.1419 -0.0478 -0.0083 -0.0197 227 ARG A NE  
1924 C  CZ  . ARG A 226 ? 0.2153 0.1168 0.1322 -0.0631 -0.0197 -0.0116 227 ARG A CZ  
1925 N  NH1 . ARG A 226 ? 0.2675 0.1726 0.2082 -0.0925 -0.0043 -0.0666 227 ARG A NH1 
1926 N  NH2 . ARG A 226 ? 0.2445 0.1230 0.1416 -0.0604 0.0008  0.0066  227 ARG A NH2 
1927 N  N   . LYS A 227 ? 0.2195 0.1247 0.1331 -0.0476 0.0227  -0.0373 228 LYS A N   
1928 C  CA  . LYS A 227 ? 0.2558 0.1561 0.1413 -0.0666 0.0461  -0.0535 228 LYS A CA  
1929 C  C   . LYS A 227 ? 0.3379 0.1281 0.1362 -0.0465 0.0711  -0.0256 228 LYS A C   
1930 O  O   . LYS A 227 ? 0.3235 0.1712 0.1347 -0.0872 0.0438  -0.0456 228 LYS A O   
1931 C  CB  . LYS A 227 ? 0.2982 0.2148 0.1403 -0.0926 0.0091  -0.0370 228 LYS A CB  
1932 C  CG  . LYS A 227 ? 0.3366 0.2285 0.1838 -0.1035 0.0177  -0.0172 228 LYS A CG  
1933 C  CD  . LYS A 227 ? 0.4609 0.4025 0.2883 -0.0817 -0.0678 -0.1273 228 LYS A CD  
1934 C  CE  . LYS A 227 ? 0.4758 0.5802 0.3089 -0.0419 -0.1335 -0.0675 228 LYS A CE  
1935 N  NZ  . LYS A 227 ? 0.8575 0.9350 0.5462 -0.3235 -0.3786 -0.0908 228 LYS A NZ  
1936 N  N   . LEU A 228 ? 0.3111 0.1092 0.1217 -0.0630 0.0318  -0.0250 229 LEU A N   
1937 C  CA  . LEU A 228 ? 0.2897 0.1433 0.1464 -0.0671 0.0577  -0.0311 229 LEU A CA  
1938 C  C   . LEU A 228 ? 0.3634 0.1022 0.1172 -0.0608 0.0711  -0.0335 229 LEU A C   
1939 O  O   . LEU A 228 ? 0.2682 0.1200 0.1512 -0.0434 0.0696  -0.0326 229 LEU A O   
1940 C  CB  . LEU A 228 ? 0.3118 0.1328 0.1241 -0.0741 0.0480  -0.0236 229 LEU A CB  
1941 C  CG  . LEU A 228 ? 0.3055 0.1218 0.1441 -0.0130 0.0436  -0.0082 229 LEU A CG  
1942 C  CD1 . LEU A 228 ? 0.3179 0.1385 0.1476 -0.0414 0.0255  -0.0320 229 LEU A CD1 
1943 C  CD2 . LEU A 228 ? 0.4054 0.1158 0.1647 -0.0043 0.0217  0.0065  229 LEU A CD2 
1944 N  N   . ASN A 229 ? 0.2962 0.1437 0.1523 -0.0533 0.0907  -0.0283 230 ASN A N   
1945 C  CA  . ASN A 229 ? 0.2800 0.1480 0.1200 -0.0315 0.0463  -0.0353 230 ASN A CA  
1946 C  C   . ASN A 229 ? 0.3122 0.1925 0.1932 -0.1037 0.0865  -0.0636 230 ASN A C   
1947 O  O   . ASN A 229 ? 0.3337 0.1625 0.1699 -0.0819 0.0843  -0.0471 230 ASN A O   
1948 C  CB  . ASN A 229 ? 0.2879 0.1880 0.1456 -0.0794 0.0729  -0.0403 230 ASN A CB  
1949 C  CG  . ASN A 229 ? 0.3560 0.2039 0.1489 -0.0790 0.0676  -0.0610 230 ASN A CG  
1950 O  OD1 . ASN A 229 ? 0.5221 0.2189 0.1758 -0.0885 0.1424  -0.0776 230 ASN A OD1 
1951 N  ND2 . ASN A 229 ? 0.3856 0.1528 0.1778 -0.0855 0.0724  -0.0653 230 ASN A ND2 
1952 N  N   . PHE A 230 ? 0.3009 0.1733 0.1597 -0.1163 0.1072  -0.0661 231 PHE A N   
1953 C  CA  . PHE A 230 ? 0.3077 0.1575 0.1759 -0.1030 0.0657  -0.0432 231 PHE A CA  
1954 C  C   . PHE A 230 ? 0.3050 0.2085 0.2407 -0.1483 0.1200  -0.1001 231 PHE A C   
1955 O  O   . PHE A 230 ? 0.3549 0.1932 0.2231 -0.1433 0.1221  -0.0644 231 PHE A O   
1956 C  CB  . PHE A 230 ? 0.3095 0.1967 0.1947 -0.1209 0.1238  -0.0645 231 PHE A CB  
1957 C  CG  . PHE A 230 ? 0.2502 0.1577 0.1861 -0.0908 0.0606  -0.0362 231 PHE A CG  
1958 C  CD1 . PHE A 230 ? 0.2623 0.1865 0.1662 -0.0750 0.0640  -0.0518 231 PHE A CD1 
1959 C  CD2 . PHE A 230 ? 0.2071 0.2039 0.1484 -0.0142 0.0544  -0.0548 231 PHE A CD2 
1960 C  CE1 . PHE A 230 ? 0.2572 0.1776 0.2056 -0.0984 0.0570  -0.0292 231 PHE A CE1 
1961 C  CE2 . PHE A 230 ? 0.2143 0.1929 0.1523 -0.0742 0.0428  -0.0531 231 PHE A CE2 
1962 C  CZ  . PHE A 230 ? 0.1968 0.2205 0.1259 -0.0683 0.0443  -0.0344 231 PHE A CZ  
1963 N  N   . ASN A 231 ? 0.3131 0.2372 0.1965 -0.1384 0.1248  -0.0798 232 ASN A N   
1964 C  CA  . ASN A 231 ? 0.3048 0.2180 0.2297 -0.0886 0.1305  -0.0586 232 ASN A CA  
1965 C  C   . ASN A 231 ? 0.1665 0.2319 0.2062 0.0232  0.0197  -0.0755 232 ASN A C   
1966 O  O   . ASN A 231 ? 0.3061 0.2153 0.2040 -0.0812 0.0650  -0.0170 232 ASN A O   
1967 C  CB  . ASN A 231 ? 0.3677 0.1747 0.2648 -0.0976 0.1759  -0.0606 232 ASN A CB  
1968 C  CG  . ASN A 231 ? 0.3826 0.2125 0.2567 -0.1089 0.1307  -0.0247 232 ASN A CG  
1969 O  OD1 . ASN A 231 ? 0.4639 0.2211 0.2243 -0.1273 0.1722  -0.0658 232 ASN A OD1 
1970 N  ND2 . ASN A 231 ? 0.4363 0.2381 0.2272 -0.0962 0.1580  -0.0734 232 ASN A ND2 
1971 N  N   . GLY A 232 ? 0.2957 0.2047 0.2188 -0.0237 0.0935  -0.0291 233 GLY A N   
1972 C  CA  . GLY A 232 ? 0.2980 0.2055 0.2177 0.0115  0.1067  0.0063  233 GLY A CA  
1973 C  C   . GLY A 232 ? 0.1306 0.2037 0.2791 -0.0006 -0.0505 -0.0108 233 GLY A C   
1974 O  O   . GLY A 232 ? 0.3095 0.3059 0.2491 0.0234  0.1349  0.0766  233 GLY A O   
1975 N  N   . GLU A 233 ? 0.1759 0.2545 0.2042 0.0136  0.0208  -0.0197 234 GLU A N   
1976 C  CA  . GLU A 233 ? 0.2331 0.2401 0.2076 0.0000  0.0472  -0.0276 234 GLU A CA  
1977 C  C   . GLU A 233 ? 0.2563 0.2768 0.2662 0.0405  0.0606  -0.0062 234 GLU A C   
1978 O  O   . GLU A 233 ? 0.3377 0.2921 0.2205 -0.0266 0.0794  0.0043  234 GLU A O   
1979 C  CB  . GLU A 233 ? 0.3427 0.1649 0.2254 0.0003  -0.0178 0.0148  234 GLU A CB  
1980 C  CG  . GLU A 233 ? 0.2597 0.3610 0.2103 -0.1263 0.0500  -0.0357 234 GLU A CG  
1981 C  CD  . GLU A 233 ? 0.5575 0.4882 0.3964 0.0434  -0.0597 -0.1263 234 GLU A CD  
1982 O  OE1 . GLU A 233 ? 0.5099 0.4086 0.3842 -0.0869 0.1696  -0.0469 234 GLU A OE1 
1983 O  OE2 . GLU A 233 ? 0.6007 0.6220 0.4605 -0.2204 -0.0410 -0.2128 234 GLU A OE2 
1984 N  N   . GLY A 234 ? 0.4732 0.2967 0.2788 -0.0062 0.1659  -0.0636 235 GLY A N   
1985 C  CA  . GLY A 234 ? 0.3695 0.3438 0.2863 0.0579  0.0524  0.0250  235 GLY A CA  
1986 C  C   . GLY A 234 ? 0.3411 0.3968 0.2633 0.1580  0.0989  0.1102  235 GLY A C   
1987 O  O   . GLY A 234 ? 0.3628 0.7132 0.3379 -0.0182 0.1809  0.0010  235 GLY A O   
1988 N  N   . GLU A 235 ? 0.3097 0.3039 0.2904 0.0965  0.1198  0.0362  236 GLU A N   
1989 C  CA  . GLU A 235 ? 0.3244 0.1956 0.2272 0.1001  0.0877  0.0100  236 GLU A CA  
1990 C  C   . GLU A 235 ? 0.4781 0.3470 0.4065 0.0326  0.1077  0.1344  236 GLU A C   
1991 O  O   . GLU A 235 ? 0.5497 0.3059 0.3558 -0.0335 0.2612  -0.0271 236 GLU A O   
1992 C  CB  . GLU A 235 ? 0.3336 0.1979 0.2982 0.0535  0.1044  0.0188  236 GLU A CB  
1993 C  CG  . GLU A 235 ? 0.4036 0.2784 0.3779 -0.0676 0.1620  -0.0234 236 GLU A CG  
1994 C  CD  . GLU A 235 ? 0.5864 0.3170 0.5070 -0.1632 0.3055  -0.0524 236 GLU A CD  
1995 O  OE1 . GLU A 235 ? 0.4767 0.3177 0.5297 -0.1524 0.3018  -0.0798 236 GLU A OE1 
1996 O  OE2 . GLU A 235 ? 0.6330 0.3905 0.5218 -0.2454 0.2822  -0.0816 236 GLU A OE2 
1997 N  N   . PRO A 236 ? 0.2322 0.3185 0.3479 0.0538  0.1468  0.1111  237 PRO A N   
1998 C  CA  . PRO A 236 ? 0.4569 0.3781 0.4429 0.0052  0.3185  0.0799  237 PRO A CA  
1999 C  C   . PRO A 236 ? 0.4348 0.3140 0.3028 -0.1350 0.2492  -0.0864 237 PRO A C   
2000 O  O   . PRO A 236 ? 0.4271 0.2827 0.3156 -0.1055 0.2205  -0.0936 237 PRO A O   
2001 C  CB  . PRO A 236 ? 0.2933 0.5925 0.4627 0.0013  0.3005  0.0174  237 PRO A CB  
2002 C  CG  . PRO A 236 ? 0.3962 0.4659 0.5411 0.0635  0.1102  0.3434  237 PRO A CG  
2003 C  CD  . PRO A 236 ? 0.3765 0.4994 0.2601 0.0131  0.0392  -0.0177 237 PRO A CD  
2004 N  N   . GLU A 237 ? 0.4600 0.2393 0.2585 -0.0740 0.1960  -0.0856 238 GLU A N   
2005 C  CA  . GLU A 237 ? 0.3790 0.2524 0.2206 -0.0961 0.1498  -0.0768 238 GLU A CA  
2006 C  C   . GLU A 237 ? 0.3350 0.2714 0.2206 -0.1124 0.1319  -0.0526 238 GLU A C   
2007 O  O   . GLU A 237 ? 0.2421 0.3316 0.1977 -0.0888 0.0395  -0.0648 238 GLU A O   
2008 C  CB  . GLU A 237 ? 0.3621 0.1965 0.2637 -0.0125 0.0346  -0.0688 238 GLU A CB  
2009 C  CG  . GLU A 237 ? 0.3018 0.2612 0.2955 -0.0377 0.0054  -0.0447 238 GLU A CG  
2010 C  CD  . GLU A 237 ? 0.3623 0.1854 0.2333 -0.0718 0.0406  -0.0754 238 GLU A CD  
2011 O  OE1 . GLU A 237 ? 0.5690 0.2734 0.4860 0.0750  -0.0234 -0.1720 238 GLU A OE1 
2012 O  OE2 . GLU A 237 ? 0.4142 0.2157 0.2231 -0.0406 0.0447  -0.0922 238 GLU A OE2 
2013 N  N   . GLU A 238 ? 0.3343 0.2245 0.2035 -0.1243 0.1273  -0.0782 239 GLU A N   
2014 C  CA  . GLU A 238 ? 0.2730 0.3362 0.1866 -0.1614 0.1023  -0.0913 239 GLU A CA  
2015 C  C   . GLU A 238 ? 0.2311 0.2407 0.1662 -0.1187 0.0803  -0.0846 239 GLU A C   
2016 O  O   . GLU A 238 ? 0.3804 0.1879 0.1920 -0.1162 0.1080  -0.0617 239 GLU A O   
2017 C  CB  . GLU A 238 ? 0.3702 0.3675 0.3054 -0.2168 0.1425  -0.1630 239 GLU A CB  
2018 C  CG  . GLU A 238 ? 0.4442 0.2202 0.3813 -0.0362 0.1827  -0.0392 239 GLU A CG  
2019 C  CD  . GLU A 238 ? 0.5788 0.5306 0.6310 -0.0702 -0.1429 -0.0288 239 GLU A CD  
2020 O  OE1 . GLU A 238 ? 0.5256 0.4636 0.9753 -0.1733 -0.2363 -0.1491 239 GLU A OE1 
2021 O  OE2 . GLU A 238 ? 0.6218 1.0027 1.3150 -0.2234 -0.3948 0.0716  239 GLU A OE2 
2022 N  N   . LEU A 239 ? 0.2035 0.2145 0.1544 -0.0727 0.0636  -0.0584 240 LEU A N   
2023 C  CA  . LEU A 239 ? 0.1759 0.1541 0.1625 -0.0542 0.0663  -0.0344 240 LEU A CA  
2024 C  C   . LEU A 239 ? 0.2198 0.1697 0.1365 -0.0841 0.0754  -0.0392 240 LEU A C   
2025 O  O   . LEU A 239 ? 0.2035 0.1719 0.1703 -0.0566 0.0643  -0.0542 240 LEU A O   
2026 C  CB  . LEU A 239 ? 0.1430 0.1433 0.1843 -0.0115 0.0220  -0.0293 240 LEU A CB  
2027 C  CG  . LEU A 239 ? 0.1532 0.1579 0.1965 -0.0071 0.0222  -0.0555 240 LEU A CG  
2028 C  CD1 . LEU A 239 ? 0.1703 0.1543 0.4214 -0.0111 -0.0535 -0.0701 240 LEU A CD1 
2029 C  CD2 . LEU A 239 ? 0.2266 0.1668 0.2046 0.0068  -0.0107 -0.0599 240 LEU A CD2 
2030 N  N   . MET A 240 ? 0.2057 0.1408 0.1573 -0.0522 0.0772  -0.0489 241 MET A N   
2031 C  CA  . MET A 240 ? 0.2682 0.1248 0.1317 -0.0274 0.0873  -0.0216 241 MET A CA  
2032 C  C   . MET A 240 ? 0.1900 0.1342 0.1202 -0.0520 0.0608  -0.0546 241 MET A C   
2033 O  O   . MET A 240 ? 0.1694 0.1360 0.1516 -0.0309 0.0480  -0.0109 241 MET A O   
2034 C  CB  . MET A 240 ? 0.2718 0.1036 0.1626 -0.0272 0.0582  -0.0240 241 MET A CB  
2035 C  CG  . MET A 240 ? 0.2657 0.0970 0.1541 -0.0383 0.0746  -0.0215 241 MET A CG  
2036 S  SD  . MET A 240 ? 0.3077 0.1106 0.1717 -0.0533 0.0791  -0.0228 241 MET A SD  
2037 C  CE  . MET A 240 ? 0.2939 0.1340 0.1950 -0.0643 0.1024  -0.0263 241 MET A CE  
2038 N  N   . VAL A 241 ? 0.2003 0.1119 0.1180 -0.0370 0.0450  -0.0359 242 VAL A N   
2039 C  CA  . VAL A 241 ? 0.1852 0.1017 0.1135 -0.0219 0.0414  -0.0162 242 VAL A CA  
2040 C  C   . VAL A 241 ? 0.1729 0.0881 0.1422 -0.0280 0.0469  -0.0555 242 VAL A C   
2041 O  O   . VAL A 241 ? 0.1487 0.1277 0.1593 -0.0331 0.0513  -0.0460 242 VAL A O   
2042 C  CB  . VAL A 241 ? 0.1740 0.1035 0.1644 -0.0348 0.0399  -0.0461 242 VAL A CB  
2043 C  CG1 . VAL A 241 ? 0.2143 0.1117 0.1571 -0.0458 0.0320  -0.0405 242 VAL A CG1 
2044 C  CG2 . VAL A 241 ? 0.2008 0.1343 0.2035 -0.0344 0.0759  -0.0494 242 VAL A CG2 
2045 N  N   . ASP A 242 ? 0.1544 0.0759 0.1225 -0.0220 0.0364  -0.0414 243 ASP A N   
2046 C  CA  . ASP A 242 ? 0.1228 0.0829 0.1520 0.0071  0.0171  -0.0390 243 ASP A CA  
2047 C  C   . ASP A 242 ? 0.1324 0.0982 0.1293 -0.0359 0.0359  -0.0401 243 ASP A C   
2048 O  O   . ASP A 242 ? 0.1371 0.1059 0.1884 -0.0399 0.0298  -0.0498 243 ASP A O   
2049 C  CB  . ASP A 242 ? 0.1238 0.0997 0.1640 -0.0119 0.0201  -0.0291 243 ASP A CB  
2050 C  CG  . ASP A 242 ? 0.1347 0.0855 0.1689 0.0126  0.0303  -0.0357 243 ASP A CG  
2051 O  OD1 . ASP A 242 ? 0.1181 0.0904 0.1516 -0.0023 0.0247  -0.0326 243 ASP A OD1 
2052 O  OD2 . ASP A 242 ? 0.1505 0.1067 0.2218 0.0057  0.0573  -0.0478 243 ASP A OD2 
2053 N  N   . ASN A 243 ? 0.1368 0.0698 0.1365 -0.0038 0.0467  -0.0339 244 ASN A N   
2054 C  CA  . ASN A 243 ? 0.1036 0.0756 0.1529 -0.0227 0.0397  -0.0394 244 ASN A CA  
2055 C  C   . ASN A 243 ? 0.0865 0.0794 0.1351 -0.0131 0.0215  -0.0189 244 ASN A C   
2056 O  O   . ASN A 243 ? 0.1424 0.0856 0.1230 0.0115  0.0324  -0.0146 244 ASN A O   
2057 C  CB  . ASN A 243 ? 0.1658 0.1047 0.1212 -0.0375 0.0450  -0.0159 244 ASN A CB  
2058 C  CG  . ASN A 243 ? 0.1473 0.1022 0.1159 -0.0364 0.0383  -0.0230 244 ASN A CG  
2059 O  OD1 . ASN A 243 ? 0.1338 0.0977 0.1483 -0.0250 0.0220  -0.0008 244 ASN A OD1 
2060 N  ND2 . ASN A 243 ? 0.1999 0.1750 0.2301 -0.0570 0.0068  0.0820  244 ASN A ND2 
2061 N  N   . TRP A 244 ? 0.0934 0.0750 0.1226 -0.0076 0.0089  -0.0237 245 TRP A N   
2062 C  CA  . TRP A 244 ? 0.0782 0.0879 0.1207 -0.0057 0.0054  -0.0251 245 TRP A CA  
2063 C  C   . TRP A 244 ? 0.0865 0.0776 0.1261 -0.0017 0.0199  -0.0137 245 TRP A C   
2064 O  O   . TRP A 244 ? 0.0920 0.0996 0.1622 0.0114  0.0088  -0.0381 245 TRP A O   
2065 C  CB  . TRP A 244 ? 0.0905 0.0719 0.1343 0.0130  0.0186  -0.0210 245 TRP A CB  
2066 C  CG  . TRP A 244 ? 0.0736 0.0834 0.1440 0.0034  0.0133  -0.0098 245 TRP A CG  
2067 C  CD1 . TRP A 244 ? 0.1072 0.0719 0.1315 0.0012  0.0303  -0.0143 245 TRP A CD1 
2068 C  CD2 . TRP A 244 ? 0.0803 0.0856 0.1282 -0.0037 0.0144  -0.0204 245 TRP A CD2 
2069 N  NE1 . TRP A 244 ? 0.1044 0.0777 0.1362 -0.0026 0.0161  -0.0170 245 TRP A NE1 
2070 C  CE2 . TRP A 244 ? 0.1045 0.0855 0.1406 -0.0086 0.0186  -0.0038 245 TRP A CE2 
2071 C  CE3 . TRP A 244 ? 0.0938 0.0918 0.1336 0.0000  0.0137  -0.0109 245 TRP A CE3 
2072 C  CZ2 . TRP A 244 ? 0.1101 0.0794 0.1649 -0.0059 0.0048  -0.0017 245 TRP A CZ2 
2073 C  CZ3 . TRP A 244 ? 0.1243 0.0812 0.1720 0.0073  0.0148  0.0091  245 TRP A CZ3 
2074 C  CH2 . TRP A 244 ? 0.1218 0.0979 0.1705 0.0220  0.0102  0.0023  245 TRP A CH2 
2075 N  N   . ARG A 245 ? 0.0870 0.0873 0.1212 -0.0021 0.0000  -0.0265 246 ARG A N   
2076 C  CA  . ARG A 245 ? 0.0773 0.0903 0.1378 -0.0080 0.0017  -0.0234 246 ARG A CA  
2077 C  C   . ARG A 245 ? 0.0667 0.0824 0.1288 0.0124  -0.0203 -0.0392 246 ARG A C   
2078 O  O   . ARG A 245 ? 0.0758 0.0943 0.1487 0.0012  -0.0125 -0.0280 246 ARG A O   
2079 C  CB  . ARG A 245 ? 0.0614 0.0925 0.1446 0.0046  -0.0046 -0.0283 246 ARG A CB  
2080 C  CG  . ARG A 245 ? 0.0566 0.0907 0.1483 0.0140  -0.0027 -0.0337 246 ARG A CG  
2081 C  CD  . ARG A 245 ? 0.0465 0.0914 0.2021 -0.0027 -0.0046 -0.0403 246 ARG A CD  
2082 N  NE  . ARG A 245 ? 0.0597 0.1045 0.1678 0.0001  -0.0035 -0.0318 246 ARG A NE  
2083 C  CZ  . ARG A 245 ? 0.0666 0.0947 0.1500 -0.0087 -0.0008 -0.0231 246 ARG A CZ  
2084 N  NH1 . ARG A 245 ? 0.0995 0.0986 0.1658 -0.0063 0.0109  -0.0283 246 ARG A NH1 
2085 N  NH2 . ARG A 245 ? 0.0750 0.1446 0.2006 -0.0297 -0.0074 -0.0241 246 ARG A NH2 
2086 N  N   . PRO A 246 ? 0.0740 0.0910 0.1507 -0.0006 -0.0142 -0.0120 247 PRO A N   
2087 C  CA  . PRO A 246 ? 0.1259 0.0961 0.1360 0.0313  -0.0219 -0.0157 247 PRO A CA  
2088 C  C   . PRO A 246 ? 0.1027 0.0737 0.1483 0.0348  -0.0153 -0.0138 247 PRO A C   
2089 O  O   . PRO A 246 ? 0.1006 0.0920 0.1415 0.0085  -0.0179 -0.0143 247 PRO A O   
2090 C  CB  . PRO A 246 ? 0.1634 0.1401 0.1985 0.0693  0.0118  -0.0088 247 PRO A CB  
2091 C  CG  . PRO A 246 ? 0.1386 0.2405 0.3346 0.0626  0.0478  0.1257  247 PRO A CG  
2092 C  CD  . PRO A 246 ? 0.0798 0.1318 0.2090 0.0469  -0.0204 0.0001  247 PRO A CD  
2093 N  N   . ALA A 247 ? 0.1011 0.0968 0.1389 0.0201  -0.0116 -0.0126 248 ALA A N   
2094 C  CA  . ALA A 247 ? 0.0956 0.0984 0.1439 0.0108  -0.0203 -0.0107 248 ALA A CA  
2095 C  C   . ALA A 247 ? 0.0785 0.1076 0.1611 0.0285  -0.0351 0.0020  248 ALA A C   
2096 O  O   . ALA A 247 ? 0.1013 0.1297 0.1634 0.0474  -0.0283 -0.0037 248 ALA A O   
2097 C  CB  . ALA A 247 ? 0.1475 0.1252 0.1676 -0.0076 0.0003  0.0092  248 ALA A CB  
2098 N  N   . GLN A 248 ? 0.0927 0.0856 0.1412 0.0099  -0.0249 -0.0008 249 GLN A N   
2099 C  CA  . GLN A 248 ? 0.0604 0.1268 0.1604 0.0024  -0.0278 -0.0019 249 GLN A CA  
2100 C  C   . GLN A 248 ? 0.0842 0.1022 0.1541 0.0252  -0.0307 0.0034  249 GLN A C   
2101 O  O   . GLN A 248 ? 0.1121 0.1176 0.1543 0.0172  -0.0181 0.0071  249 GLN A O   
2102 C  CB  . GLN A 248 ? 0.1153 0.0909 0.1753 0.0024  -0.0232 0.0052  249 GLN A CB  
2103 C  CG  . GLN A 248 ? 0.1013 0.1196 0.1663 -0.0046 -0.0436 0.0065  249 GLN A CG  
2104 C  CD  . GLN A 248 ? 0.0795 0.1518 0.1755 -0.0127 -0.0259 0.0043  249 GLN A CD  
2105 O  OE1 . GLN A 248 ? 0.0829 0.2310 0.2144 -0.0194 -0.0223 -0.0403 249 GLN A OE1 
2106 N  NE2 . GLN A 248 ? 0.1485 0.1642 0.1732 0.0093  -0.0108 -0.0198 249 GLN A NE2 
2107 N  N   . PRO A 249 ? 0.1277 0.1483 0.1606 0.0280  -0.0529 0.0046  250 PRO A N   
2108 C  CA  . PRO A 249 ? 0.1324 0.1834 0.1891 0.0467  -0.0346 -0.0008 250 PRO A CA  
2109 C  C   . PRO A 249 ? 0.1275 0.1398 0.1482 0.0340  -0.0487 0.0054  250 PRO A C   
2110 O  O   . PRO A 249 ? 0.1149 0.1331 0.1656 0.0320  -0.0478 0.0098  250 PRO A O   
2111 C  CB  . PRO A 249 ? 0.1106 0.2445 0.2496 0.0535  -0.0701 -0.0452 250 PRO A CB  
2112 C  CG  . PRO A 249 ? 0.1674 0.3054 0.2123 0.0478  -0.0957 -0.0373 250 PRO A CG  
2113 C  CD  . PRO A 249 ? 0.0988 0.2612 0.2050 0.0430  -0.0754 -0.0318 250 PRO A CD  
2114 N  N   . LEU A 250 ? 0.1671 0.1358 0.1396 0.0434  -0.0243 -0.0031 251 LEU A N   
2115 C  CA  . LEU A 250 ? 0.1559 0.1101 0.1360 0.0185  -0.0137 -0.0071 251 LEU A CA  
2116 C  C   . LEU A 250 ? 0.1717 0.1229 0.1387 0.0357  -0.0538 0.0179  251 LEU A C   
2117 O  O   . LEU A 250 ? 0.1638 0.1097 0.1601 0.0292  -0.0626 -0.0057 251 LEU A O   
2118 C  CB  . LEU A 250 ? 0.2017 0.1432 0.1523 -0.0021 -0.0109 0.0041  251 LEU A CB  
2119 C  CG  . LEU A 250 ? 0.2099 0.1336 0.1430 0.0093  0.0189  0.0015  251 LEU A CG  
2120 C  CD1 . LEU A 250 ? 0.1169 0.2093 0.1755 -0.0322 -0.0333 -0.0089 251 LEU A CD1 
2121 C  CD2 . LEU A 250 ? 0.2852 0.1728 0.2085 -0.0392 0.0447  -0.0227 251 LEU A CD2 
2122 N  N   . LYS A 251 ? 0.1629 0.1523 0.1562 0.0452  -0.0681 -0.0038 252 LYS A N   
2123 C  CA  . LYS A 251 ? 0.1735 0.1882 0.1562 0.0412  -0.0674 -0.0220 252 LYS A CA  
2124 C  C   . LYS A 251 ? 0.1617 0.1720 0.2150 0.0204  -0.0636 -0.0057 252 LYS A C   
2125 O  O   . LYS A 251 ? 0.2229 0.2229 0.1924 -0.0089 -0.0173 -0.0295 252 LYS A O   
2126 C  CB  . LYS A 251 ? 0.2006 0.1922 0.2026 0.0074  -0.0644 -0.0190 252 LYS A CB  
2127 C  CG  . LYS A 251 ? 0.1717 0.2159 0.3452 0.0020  -0.0306 -0.0520 252 LYS A CG  
2128 C  CD  . LYS A 251 ? 0.1846 0.3212 0.3276 -0.0566 -0.0074 -0.1341 252 LYS A CD  
2129 C  CE  . LYS A 251 ? 0.1137 0.3878 0.5651 0.0010  -0.0173 -0.0762 252 LYS A CE  
2130 N  NZ  . LYS A 251 ? 0.1823 0.3337 0.5641 -0.0052 -0.0989 0.0406  252 LYS A NZ  
2131 N  N   . ASN A 252 ? 0.1996 0.1778 0.1678 0.0384  -0.0680 -0.0489 253 ASN A N   
2132 C  CA  . ASN A 252 ? 0.2126 0.4025 0.2351 0.0265  -0.0705 -0.1288 253 ASN A CA  
2133 C  C   . ASN A 252 ? 0.2281 0.3080 0.3495 0.0641  -0.1145 -0.0194 253 ASN A C   
2134 O  O   . ASN A 252 ? 0.3391 0.3079 0.3431 0.0505  -0.0313 -0.0775 253 ASN A O   
2135 C  CB  . ASN A 252 ? 0.2768 0.5228 0.2939 -0.0483 -0.1004 -0.1457 253 ASN A CB  
2136 C  CG  . ASN A 252 ? 0.3605 0.5486 0.2617 -0.0575 -0.0188 0.0188  253 ASN A CG  
2137 O  OD1 . ASN A 252 ? 1.0620 0.8123 0.4146 -0.3073 0.0926  0.1847  253 ASN A OD1 
2138 N  ND2 . ASN A 252 ? 0.2698 0.6506 0.6974 0.1045  0.0467  -0.0891 253 ASN A ND2 
2139 N  N   . ARG A 253 ? 0.1706 0.2924 0.1283 0.0414  -0.0373 0.0240  254 ARG A N   
2140 C  CA  . ARG A 253 ? 0.1439 0.1595 0.1168 0.0491  -0.0227 -0.0052 254 ARG A CA  
2141 C  C   . ARG A 253 ? 0.2004 0.1308 0.1351 0.0425  0.0111  0.0003  254 ARG A C   
2142 O  O   . ARG A 253 ? 0.2842 0.1449 0.2743 0.0476  0.0844  0.0397  254 ARG A O   
2143 C  CB  . ARG A 253 ? 0.1421 0.1618 0.1132 0.0439  -0.0153 -0.0057 254 ARG A CB  
2144 C  CG  . ARG A 253 ? 0.1782 0.1207 0.1261 0.0093  -0.0318 -0.0100 254 ARG A CG  
2145 C  CD  . ARG A 253 ? 0.1407 0.1150 0.1178 0.0167  -0.0114 -0.0310 254 ARG A CD  
2146 N  NE  . ARG A 253 ? 0.1199 0.0913 0.1315 0.0054  -0.0368 -0.0083 254 ARG A NE  
2147 C  CZ  . ARG A 253 ? 0.0896 0.1063 0.1211 0.0148  -0.0271 -0.0254 254 ARG A CZ  
2148 N  NH1 . ARG A 253 ? 0.0663 0.1010 0.1331 0.0096  -0.0412 -0.0068 254 ARG A NH1 
2149 N  NH2 . ARG A 253 ? 0.0909 0.0941 0.1356 0.0146  -0.0306 -0.0109 254 ARG A NH2 
2150 N  N   . GLN A 254 ? 0.1424 0.1865 0.1328 0.0218  -0.0313 -0.0562 255 GLN A N   
2151 C  CA  . GLN A 254 ? 0.1753 0.1821 0.1455 0.0113  -0.0282 -0.0390 255 GLN A CA  
2152 C  C   . GLN A 254 ? 0.1712 0.1347 0.1459 0.0272  -0.0311 -0.0124 255 GLN A C   
2153 O  O   . GLN A 254 ? 0.2102 0.1430 0.2184 0.0125  -0.0619 0.0006  255 GLN A O   
2154 C  CB  . GLN A 254 ? 0.2098 0.3102 0.1534 -0.0143 -0.0142 -0.0929 255 GLN A CB  
2155 C  CG  . GLN A 254 ? 0.3183 0.3650 0.2353 0.0983  -0.0969 -0.0758 255 GLN A CG  
2156 C  CD  . GLN A 254 ? 0.5169 0.4623 0.1733 0.0851  -0.0157 0.0088  255 GLN A CD  
2157 O  OE1 . GLN A 254 ? 0.5260 0.5005 0.5400 0.0732  0.0945  -0.0348 255 GLN A OE1 
2158 N  NE2 . GLN A 254 ? 0.6424 0.4789 0.3373 0.1186  -0.1773 -0.1650 255 GLN A NE2 
2159 N  N   . ILE A 255 ? 0.1352 0.1243 0.1335 0.0185  -0.0122 -0.0080 256 ILE A N   
2160 C  CA  . ILE A 255 ? 0.1439 0.1214 0.1144 0.0194  -0.0142 -0.0097 256 ILE A CA  
2161 C  C   . ILE A 255 ? 0.1356 0.1428 0.1014 0.0155  0.0006  0.0051  256 ILE A C   
2162 O  O   . ILE A 255 ? 0.1810 0.1412 0.1425 0.0179  0.0177  0.0364  256 ILE A O   
2163 C  CB  . ILE A 255 ? 0.1650 0.1147 0.1220 -0.0005 -0.0086 -0.0109 256 ILE A CB  
2164 C  CG1 . ILE A 255 ? 0.1280 0.1223 0.1564 0.0295  -0.0023 -0.0087 256 ILE A CG1 
2165 C  CG2 . ILE A 255 ? 0.1345 0.1523 0.1171 0.0037  -0.0068 0.0063  256 ILE A CG2 
2166 C  CD1 . ILE A 255 ? 0.1633 0.1475 0.1703 -0.0088 0.0077  -0.0445 256 ILE A CD1 
2167 N  N   . LYS A 256 ? 0.1146 0.1433 0.1105 0.0113  -0.0107 0.0131  257 LYS A N   
2168 C  CA  . LYS A 256 ? 0.1379 0.1282 0.1089 0.0148  0.0142  0.0168  257 LYS A CA  
2169 C  C   . LYS A 256 ? 0.1556 0.1142 0.1011 0.0054  -0.0068 0.0015  257 LYS A C   
2170 O  O   . LYS A 256 ? 0.1871 0.1737 0.1014 -0.0460 0.0026  -0.0020 257 LYS A O   
2171 C  CB  . LYS A 256 ? 0.1512 0.1530 0.1629 0.0337  0.0133  -0.0430 257 LYS A CB  
2172 C  CG  . LYS A 256 ? 0.2453 0.1783 0.2254 -0.0373 0.0260  -0.0788 257 LYS A CG  
2173 C  CD  . LYS A 256 ? 0.2824 0.2038 0.2799 0.0131  -0.0379 -0.0592 257 LYS A CD  
2174 C  CE  . LYS A 256 ? 0.2894 0.3921 0.3916 -0.1303 -0.0124 -0.1918 257 LYS A CE  
2175 N  NZ  . LYS A 256 ? 0.3240 0.3842 0.6301 -0.0703 0.1527  -0.1099 257 LYS A NZ  
2176 N  N   . ALA A 257 ? 0.1328 0.1633 0.1106 0.0133  0.0252  0.0041  258 ALA A N   
2177 C  CA  . ALA A 257 ? 0.1378 0.1498 0.1319 0.0076  -0.0031 0.0066  258 ALA A CA  
2178 C  C   . ALA A 257 ? 0.1172 0.1561 0.1378 -0.0035 0.0161  0.0118  258 ALA A C   
2179 O  O   . ALA A 257 ? 0.1640 0.1661 0.1326 0.0049  0.0386  0.0005  258 ALA A O   
2180 C  CB  . ALA A 257 ? 0.1500 0.1500 0.1692 -0.0188 0.0147  0.0071  258 ALA A CB  
2181 N  N   . SER A 258 ? 0.1160 0.1491 0.1437 -0.0080 -0.0006 0.0087  259 SER A N   
2182 C  CA  . SER A 258 ? 0.1328 0.1581 0.1690 -0.0012 0.0270  -0.0119 259 SER A CA  
2183 C  C   . SER A 258 ? 0.1115 0.2111 0.1877 -0.0296 0.0337  -0.0027 259 SER A C   
2184 O  O   . SER A 258 ? 0.1415 0.3174 0.2306 0.0041  0.0555  -0.0054 259 SER A O   
2185 C  CB  . SER A 258 ? 0.1494 0.1631 0.1615 -0.0115 -0.0142 0.0035  259 SER A CB  
2186 O  OG  . SER A 258 ? 0.1072 0.1859 0.1518 -0.0132 0.0234  -0.0203 259 SER A OG  
2187 N  N   . PHE A 259 ? 0.1527 0.2083 0.1834 -0.0445 0.0471  0.0048  260 PHE A N   
2188 C  CA  . PHE A 259 ? 0.2119 0.1985 0.2125 -0.0527 0.0537  0.0136  260 PHE A CA  
2189 C  C   . PHE A 259 ? 0.2279 0.2730 0.1997 -0.0562 0.0522  0.0035  260 PHE A C   
2190 O  O   . PHE A 259 ? 0.3018 0.2326 0.2457 -0.0724 0.0070  0.0662  260 PHE A O   
2191 C  CB  . PHE A 259 ? 0.1550 0.2182 0.2463 -0.0223 0.0368  -0.0159 260 PHE A CB  
2192 C  CG  . PHE A 259 ? 0.1493 0.1715 0.2331 -0.0141 0.0230  0.0111  260 PHE A CG  
2193 C  CD1 . PHE A 259 ? 0.1520 0.1834 0.1699 -0.0472 0.0155  -0.0348 260 PHE A CD1 
2194 C  CD2 . PHE A 259 ? 0.2685 0.1492 0.2910 -0.0454 0.0542  0.0348  260 PHE A CD2 
2195 C  CE1 . PHE A 259 ? 0.1744 0.1771 0.2453 -0.0342 0.0313  -0.0219 260 PHE A CE1 
2196 C  CE2 . PHE A 259 ? 0.2660 0.1934 0.3097 -0.0302 0.0357  0.0182  260 PHE A CE2 
2197 C  CZ  . PHE A 259 ? 0.2725 0.1602 0.2716 -0.0353 0.0051  -0.0322 260 PHE A CZ  
2198 N  N   . LYS A 260 ? 0.4260 0.4316 0.3098 -0.1096 0.1441  0.1110  261 LYS A N   
2199 C  CA  . LYS A 260 ? 0.6388 0.4189 0.2930 -0.1243 0.0137  0.0922  261 LYS A CA  
2200 C  C   . LYS A 260 ? 0.6082 0.6377 0.4505 -0.2219 -0.1194 0.1837  261 LYS A C   
2201 O  O   . LYS A 260 ? 0.5555 0.5008 0.3713 -0.2192 0.0584  0.1032  261 LYS A O   
2202 C  CB  . LYS A 260 ? 0.8794 0.3925 0.4653 -0.2637 0.1846  0.0476  261 LYS A CB  
2203 C  CG  . LYS A 260 ? 0.9031 0.4616 0.6194 -0.3761 0.1391  -0.1136 261 LYS A CG  
2204 C  CD  . LYS A 260 ? 0.9535 0.5536 0.6456 -0.1380 0.0934  -0.1246 261 LYS A CD  
2205 C  CE  . LYS A 260 ? 0.8697 0.5019 0.4900 -0.2506 0.0998  0.0403  261 LYS A CE  
2206 N  NZ  . LYS A 260 ? 1.2587 0.5271 0.4483 0.0340  -0.0017 0.1419  261 LYS A NZ  
2207 O  OXT . LYS A 260 ? 0.9834 0.7394 0.6879 -0.3479 0.2166  -0.0454 261 LYS A OXT 
2208 N  N   . SER B 2   ? 0.6306 0.7415 0.8029 0.1565  -0.0989 -0.0103 2   SER B N   
2209 C  CA  . SER B 2   ? 0.4672 0.6165 0.4993 -0.0200 -0.0280 -0.0362 2   SER B CA  
2210 C  C   . SER B 2   ? 0.4652 0.6894 0.4903 -0.0690 0.0527  -0.1231 2   SER B C   
2211 O  O   . SER B 2   ? 0.7182 0.8445 0.6977 0.0024  -0.1365 -0.0856 2   SER B O   
2212 C  CB  . SER B 2   ? 0.3966 0.3294 0.4083 -0.0006 -0.0428 -0.0469 2   SER B CB  
2213 O  OG  . SER B 2   ? 0.4571 0.4183 0.4663 0.0008  0.0223  -0.0285 2   SER B OG  
2214 N  N   . HIS B 3   ? 0.6067 0.6888 0.4878 -0.0873 0.1759  -0.0126 3   HIS B N   
2215 C  CA  . HIS B 3   ? 0.6394 0.6032 0.5356 -0.0392 0.0966  0.0342  3   HIS B CA  
2216 C  C   . HIS B 3   ? 0.5590 0.7642 0.6215 -0.0910 0.1250  -0.0307 3   HIS B C   
2217 O  O   . HIS B 3   ? 0.5922 0.8532 0.5820 -0.0566 0.0612  0.0010  3   HIS B O   
2218 C  CB  . HIS B 3   ? 0.7494 0.6388 0.5996 0.0204  -0.0044 -0.0406 3   HIS B CB  
2219 N  N   . HIS B 4   ? 0.6586 0.4871 0.6999 -0.0065 0.4095  -0.1643 4   HIS B N   
2220 C  CA  . HIS B 4   ? 0.3908 0.3188 0.6699 0.1396  0.3185  -0.0057 4   HIS B CA  
2221 C  C   . HIS B 4   ? 0.2358 0.2874 0.3874 0.0970  0.1233  0.0244  4   HIS B C   
2222 O  O   . HIS B 4   ? 0.2502 0.3273 0.3612 0.0080  0.1314  -0.0110 4   HIS B O   
2223 C  CB  . HIS B 4   ? 0.4469 0.3835 0.6851 -0.0092 0.3303  -0.1534 4   HIS B CB  
2224 C  CG  . HIS B 4   ? 1.0788 0.6697 0.9798 0.0982  0.3122  0.0921  4   HIS B CG  
2225 N  N   . TRP B 5   ? 0.1805 0.2470 0.3267 0.0698  0.0751  0.0038  5   TRP B N   
2226 C  CA  . TRP B 5   ? 0.1360 0.2089 0.3296 0.0450  0.0776  0.0021  5   TRP B CA  
2227 C  C   . TRP B 5   ? 0.1742 0.2098 0.3048 0.0049  0.1076  -0.0003 5   TRP B C   
2228 O  O   . TRP B 5   ? 0.2200 0.1907 0.3195 0.0460  0.1159  -0.0073 5   TRP B O   
2229 C  CB  . TRP B 5   ? 0.1306 0.1922 0.3208 0.0275  0.0697  0.0302  5   TRP B CB  
2230 C  CG  . TRP B 5   ? 0.1559 0.1706 0.2064 0.0432  0.0689  0.0031  5   TRP B CG  
2231 C  CD1 . TRP B 5   ? 0.2143 0.1737 0.2363 0.0063  0.0405  -0.0172 5   TRP B CD1 
2232 C  CD2 . TRP B 5   ? 0.1347 0.1832 0.2181 0.0024  0.0377  0.0115  5   TRP B CD2 
2233 N  NE1 . TRP B 5   ? 0.2502 0.1568 0.2432 -0.0020 0.0414  -0.0219 5   TRP B NE1 
2234 C  CE2 . TRP B 5   ? 0.1536 0.1947 0.2118 -0.0065 0.0348  -0.0027 5   TRP B CE2 
2235 C  CE3 . TRP B 5   ? 0.1523 0.1979 0.1929 0.0302  0.0705  0.0296  5   TRP B CE3 
2236 C  CZ2 . TRP B 5   ? 0.1686 0.2127 0.1900 0.0093  0.0282  0.0132  5   TRP B CZ2 
2237 C  CZ3 . TRP B 5   ? 0.1692 0.1832 0.1783 0.0179  0.0469  0.0406  5   TRP B CZ3 
2238 C  CH2 . TRP B 5   ? 0.1301 0.2348 0.1591 0.0131  0.0234  0.0489  5   TRP B CH2 
2239 N  N   . GLY B 6   ? 0.1760 0.1571 0.2933 0.0129  0.0900  0.0331  6   GLY B N   
2240 C  CA  . GLY B 6   ? 0.2101 0.1832 0.3091 0.0700  0.1088  0.0621  6   GLY B CA  
2241 C  C   . GLY B 6   ? 0.1554 0.1735 0.2942 0.0070  0.1155  0.0522  6   GLY B C   
2242 O  O   . GLY B 6   ? 0.1424 0.1774 0.2547 -0.0122 0.0737  0.0092  6   GLY B O   
2243 N  N   A TYR B 7   ? 0.1904 0.1879 0.3754 0.0826  0.1225  0.0795  7   TYR B N   
2244 N  N   B TYR B 7   ? 0.2143 0.1583 0.3436 0.0295  0.1658  0.0768  7   TYR B N   
2245 C  CA  A TYR B 7   ? 0.2202 0.1320 0.4835 0.0370  0.1616  0.0590  7   TYR B CA  
2246 C  CA  B TYR B 7   ? 0.1580 0.1435 0.5094 0.0487  0.1933  0.0399  7   TYR B CA  
2247 C  C   A TYR B 7   ? 0.2152 0.1268 0.6273 0.0614  0.2181  0.0863  7   TYR B C   
2248 C  C   B TYR B 7   ? 0.1945 0.1649 0.6983 0.0163  0.2026  0.1220  7   TYR B C   
2249 O  O   A TYR B 7   ? 0.3851 0.1855 0.8838 0.1035  0.1817  0.0013  7   TYR B O   
2250 O  O   B TYR B 7   ? 0.3037 0.2949 0.8253 0.0564  0.2240  0.0549  7   TYR B O   
2251 C  CB  A TYR B 7   ? 0.2349 0.1367 0.3528 0.0153  0.1334  0.0322  7   TYR B CB  
2252 C  CB  B TYR B 7   ? 0.1902 0.1706 0.3355 0.0244  0.1485  0.0251  7   TYR B CB  
2253 C  CG  A TYR B 7   ? 0.1468 0.1158 0.2347 0.0549  0.0619  0.0644  7   TYR B CG  
2254 C  CG  B TYR B 7   ? 0.1547 0.1268 0.2233 0.0315  0.0703  0.0227  7   TYR B CG  
2255 C  CD1 A TYR B 7   ? 0.0795 0.1599 0.2371 0.0445  0.0399  0.0548  7   TYR B CD1 
2256 C  CD1 B TYR B 7   ? 0.1667 0.1519 0.2337 0.0362  0.0749  0.0401  7   TYR B CD1 
2257 C  CD2 A TYR B 7   ? 0.1787 0.1304 0.2644 0.0414  0.0498  0.0516  7   TYR B CD2 
2258 C  CD2 B TYR B 7   ? 0.1440 0.1202 0.2594 0.0671  0.0300  0.0076  7   TYR B CD2 
2259 C  CE1 A TYR B 7   ? 0.0690 0.1212 0.1931 0.0284  -0.0080 0.0522  7   TYR B CE1 
2260 C  CE1 B TYR B 7   ? 0.1032 0.1347 0.1800 0.0269  0.0233  0.0315  7   TYR B CE1 
2261 C  CE2 A TYR B 7   ? 0.1579 0.1724 0.1695 0.0619  0.0727  0.0643  7   TYR B CE2 
2262 C  CE2 B TYR B 7   ? 0.1620 0.1888 0.1994 0.0555  0.0430  0.0452  7   TYR B CE2 
2263 C  CZ  A TYR B 7   ? 0.1207 0.1225 0.1456 0.0428  0.0281  0.0272  7   TYR B CZ  
2264 C  CZ  B TYR B 7   ? 0.1265 0.1295 0.1787 0.0340  0.0109  0.0065  7   TYR B CZ  
2265 O  OH  A TYR B 7   ? 0.1548 0.1185 0.1433 0.0165  0.0160  0.0258  7   TYR B OH  
2266 O  OH  B TYR B 7   ? 0.1960 0.1433 0.1599 0.0201  0.0386  0.0208  7   TYR B OH  
2267 N  N   A GLY B 8   ? 0.2256 0.1557 0.6298 0.0511  0.2347  0.0487  8   GLY B N   
2268 N  N   B GLY B 8   ? 0.1184 0.2189 0.7307 0.0275  0.1623  0.1823  8   GLY B N   
2269 C  CA  A GLY B 8   ? 0.1322 0.2162 0.5702 0.0217  0.0813  0.0807  8   GLY B CA  
2270 C  CA  B GLY B 8   ? 0.1322 0.1379 0.6611 0.0654  0.1190  0.0619  8   GLY B CA  
2271 C  C   A GLY B 8   ? 0.3700 0.2175 0.4875 -0.0103 0.0711  0.1387  8   GLY B C   
2272 C  C   B GLY B 8   ? 0.1644 0.1782 0.5496 0.0109  0.2291  0.0340  8   GLY B C   
2273 O  O   A GLY B 8   ? 0.2720 0.2121 0.5975 0.0639  0.2170  0.2017  8   GLY B O   
2274 O  O   B GLY B 8   ? 0.3659 0.4178 0.6304 0.0773  0.2118  0.1712  8   GLY B O   
2275 N  N   A LYS B 9   ? 0.2060 0.2261 0.3921 0.0560  -0.0377 0.1308  9   LYS B N   
2276 N  N   B LYS B 9   ? 0.1512 0.1807 0.4413 0.0110  0.1076  0.0562  9   LYS B N   
2277 C  CA  A LYS B 9   ? 0.2940 0.2518 0.4426 0.0549  -0.1597 0.1486  9   LYS B CA  
2278 C  CA  B LYS B 9   ? 0.3131 0.2423 0.5098 0.0041  -0.0441 0.0663  9   LYS B CA  
2279 C  C   A LYS B 9   ? 0.1717 0.2311 0.3826 0.0427  -0.0480 0.0733  9   LYS B C   
2280 C  C   B LYS B 9   ? 0.1595 0.2172 0.4167 -0.0549 0.0221  0.0727  9   LYS B C   
2281 O  O   A LYS B 9   ? 0.2344 0.3682 0.3808 0.1333  0.0386  0.0834  9   LYS B O   
2282 O  O   B LYS B 9   ? 0.2500 0.3309 0.4273 0.1615  0.0737  0.0662  9   LYS B O   
2283 C  CB  A LYS B 9   ? 0.2320 0.3260 0.3429 0.0551  -0.0863 0.0812  9   LYS B CB  
2284 C  CB  B LYS B 9   ? 0.3235 0.2969 0.3977 -0.0408 -0.0390 0.0040  9   LYS B CB  
2285 C  CG  A LYS B 9   ? 0.3740 0.3014 0.4302 -0.0601 -0.0816 0.0476  9   LYS B CG  
2286 C  CG  B LYS B 9   ? 0.3375 0.3000 0.4889 -0.1102 -0.0408 0.0340  9   LYS B CG  
2287 C  CD  A LYS B 9   ? 0.4113 0.3526 0.5989 -0.0878 -0.0010 0.0623  9   LYS B CD  
2288 C  CD  B LYS B 9   ? 0.3415 0.2976 0.5744 -0.1009 0.0588  0.0060  9   LYS B CD  
2289 C  CE  A LYS B 9   ? 0.4329 0.3463 0.6819 -0.1990 0.0040  0.0135  9   LYS B CE  
2290 C  CE  B LYS B 9   ? 0.4038 0.4505 0.7100 -0.1720 -0.0144 0.0357  9   LYS B CE  
2291 N  NZ  A LYS B 9   ? 0.4941 0.5160 0.7630 -0.1465 0.1406  0.0724  9   LYS B NZ  
2292 N  NZ  B LYS B 9   ? 0.3558 0.4886 0.8743 -0.1011 0.1062  0.0640  9   LYS B NZ  
2293 N  N   A HIS B 10  ? 0.3626 0.1688 0.6146 -0.0439 0.3267  0.0733  10  HIS B N   
2294 N  N   B HIS B 10  ? 0.2581 0.1583 0.7324 -0.1134 0.3077  -0.0447 10  HIS B N   
2295 C  CA  A HIS B 10  ? 0.2921 0.1694 0.5378 -0.0533 0.2797  0.0065  10  HIS B CA  
2296 C  CA  B HIS B 10  ? 0.3790 0.1891 0.5674 -0.0306 0.2462  -0.0027 10  HIS B CA  
2297 C  C   A HIS B 10  ? 0.2592 0.1845 0.4485 -0.0788 0.2163  -0.0476 10  HIS B C   
2298 C  C   B HIS B 10  ? 0.2594 0.2026 0.4368 -0.0764 0.2293  -0.1353 10  HIS B C   
2299 O  O   A HIS B 10  ? 0.2838 0.2046 0.5102 -0.0086 0.1601  -0.1150 10  HIS B O   
2300 O  O   B HIS B 10  ? 0.2220 0.3082 0.5127 -0.0920 0.1463  0.0034  10  HIS B O   
2301 C  CB  A HIS B 10  ? 0.2906 0.2432 0.5433 -0.0120 0.2739  -0.1089 10  HIS B CB  
2302 C  CB  B HIS B 10  ? 0.1559 0.1609 0.6664 -0.0024 0.2409  0.0671  10  HIS B CB  
2303 C  CG  A HIS B 10  ? 0.2488 0.2764 0.2736 -0.0500 0.0000  -0.0172 10  HIS B CG  
2304 C  CG  B HIS B 10  ? 0.2220 0.2727 0.3486 -0.1076 0.1032  -0.0715 10  HIS B CG  
2305 N  ND1 A HIS B 10  ? 0.2614 0.1809 0.5575 -0.1360 0.0678  -0.0452 10  HIS B ND1 
2306 N  ND1 B HIS B 10  ? 0.1243 0.3535 0.5047 -0.0571 0.0736  -0.0126 10  HIS B ND1 
2307 C  CD2 A HIS B 10  ? 0.1611 0.2436 0.2362 -0.0615 0.1088  0.0636  10  HIS B CD2 
2308 C  CD2 B HIS B 10  ? 0.2181 0.2971 0.4011 0.0480  0.1220  -0.0575 10  HIS B CD2 
2309 C  CE1 A HIS B 10  ? 0.2101 0.2439 0.3063 -0.1474 -0.1067 0.0175  10  HIS B CE1 
2310 C  CE1 B HIS B 10  ? 0.3305 0.3319 0.3384 -0.0447 -0.0272 0.0947  10  HIS B CE1 
2311 N  NE2 A HIS B 10  ? 0.1196 0.2570 0.2545 -0.0636 -0.0243 0.0065  10  HIS B NE2 
2312 N  NE2 B HIS B 10  ? 0.1500 0.3346 0.2680 0.0586  0.0364  0.0020  10  HIS B NE2 
2313 N  N   . ASN B 11  ? 0.2324 0.1667 0.5407 -0.0049 0.2415  0.0238  11  ASN B N   
2314 C  CA  . ASN B 11  ? 0.1398 0.2154 0.4156 -0.0527 0.1256  -0.0013 11  ASN B CA  
2315 C  C   . ASN B 11  ? 0.1803 0.1602 0.3718 -0.0269 0.1409  -0.0183 11  ASN B C   
2316 O  O   . ASN B 11  ? 0.1864 0.1838 0.3416 -0.0416 0.1293  -0.0193 11  ASN B O   
2317 C  CB  . ASN B 11  ? 0.2337 0.1785 0.4156 0.0198  0.1958  0.0351  11  ASN B CB  
2318 C  CG  . ASN B 11  ? 0.2784 0.1854 0.3752 -0.0193 0.1694  0.0060  11  ASN B CG  
2319 O  OD1 . ASN B 11  ? 0.2408 0.2299 0.4571 0.0447  0.1712  0.0277  11  ASN B OD1 
2320 N  ND2 . ASN B 11  ? 0.2082 0.2542 0.3555 0.0718  0.1048  0.0590  11  ASN B ND2 
2321 N  N   . GLY B 12  ? 0.1688 0.1713 0.3540 0.0205  0.1295  0.0175  12  GLY B N   
2322 C  CA  . GLY B 12  ? 0.1361 0.2249 0.3226 -0.0086 0.1164  0.0432  12  GLY B CA  
2323 C  C   . GLY B 12  ? 0.1205 0.1383 0.2962 -0.0148 0.0703  -0.0513 12  GLY B C   
2324 O  O   . GLY B 12  ? 0.1274 0.1360 0.3440 -0.0086 0.0766  -0.0203 12  GLY B O   
2325 N  N   . PRO B 13  ? 0.1428 0.1279 0.2861 0.0210  0.0966  0.0160  13  PRO B N   
2326 C  CA  . PRO B 13  ? 0.1180 0.1356 0.3000 -0.0107 0.0588  0.0073  13  PRO B CA  
2327 C  C   . PRO B 13  ? 0.1405 0.1094 0.2518 -0.0118 0.0711  0.0102  13  PRO B C   
2328 O  O   . PRO B 13  ? 0.0921 0.1688 0.2985 0.0063  0.0445  0.0408  13  PRO B O   
2329 C  CB  . PRO B 13  ? 0.1063 0.1624 0.2684 0.0216  0.0586  0.0278  13  PRO B CB  
2330 C  CG  . PRO B 13  ? 0.1547 0.1701 0.2689 0.0549  0.0746  0.0553  13  PRO B CG  
2331 C  CD  . PRO B 13  ? 0.1115 0.1911 0.2804 -0.0008 0.0635  0.0304  13  PRO B CD  
2332 N  N   . GLU B 14  ? 0.1625 0.1149 0.3152 -0.0163 0.0690  -0.0120 14  GLU B N   
2333 C  CA  . GLU B 14  ? 0.2310 0.1615 0.3274 -0.0436 0.0582  -0.0401 14  GLU B CA  
2334 C  C   . GLU B 14  ? 0.1496 0.2159 0.3242 -0.0581 0.0590  -0.0258 14  GLU B C   
2335 O  O   . GLU B 14  ? 0.1830 0.1538 0.3811 -0.0498 0.0456  -0.0225 14  GLU B O   
2336 C  CB  . GLU B 14  ? 0.2928 0.1667 0.3425 -0.0458 0.0196  -0.0196 14  GLU B CB  
2337 C  CG  . GLU B 14  ? 0.1895 0.2705 0.3443 0.0087  -0.0340 0.0621  14  GLU B CG  
2338 C  CD  . GLU B 14  ? 0.2556 0.2667 0.3582 -0.1292 -0.1040 0.0121  14  GLU B CD  
2339 O  OE1 . GLU B 14  ? 0.2204 0.2263 0.3359 -0.0991 -0.0843 0.0966  14  GLU B OE1 
2340 O  OE2 . GLU B 14  ? 0.5541 0.1762 0.2775 -0.0219 0.0698  -0.0031 14  GLU B OE2 
2341 N  N   . HIS B 15  ? 0.0970 0.1613 0.3212 -0.0228 0.0566  0.0019  15  HIS B N   
2342 C  CA  . HIS B 15  ? 0.1177 0.1658 0.3479 -0.0140 0.0372  -0.0031 15  HIS B CA  
2343 C  C   . HIS B 15  ? 0.0982 0.1658 0.3118 -0.0274 0.0498  0.0166  15  HIS B C   
2344 O  O   . HIS B 15  ? 0.0847 0.1672 0.3851 -0.0163 0.0397  -0.0361 15  HIS B O   
2345 C  CB  . HIS B 15  ? 0.1308 0.1739 0.3319 -0.0188 0.0582  -0.0414 15  HIS B CB  
2346 C  CG  . HIS B 15  ? 0.1442 0.2166 0.2901 -0.0546 0.0546  -0.0392 15  HIS B CG  
2347 N  ND1 . HIS B 15  ? 0.1539 0.2462 0.3416 -0.0835 0.0362  -0.0153 15  HIS B ND1 
2348 C  CD2 . HIS B 15  ? 0.2154 0.1879 0.3549 -0.0649 0.0930  0.0094  15  HIS B CD2 
2349 C  CE1 . HIS B 15  ? 0.3842 0.2757 0.3513 -0.1411 0.0381  0.0313  15  HIS B CE1 
2350 N  NE2 . HIS B 15  ? 0.3393 0.2394 0.3759 -0.1635 0.1225  -0.0190 15  HIS B NE2 
2351 N  N   . TRP B 16  ? 0.0812 0.1229 0.3012 -0.0052 0.0155  -0.0104 16  TRP B N   
2352 C  CA  . TRP B 16  ? 0.0649 0.1063 0.3079 -0.0066 0.0057  0.0188  16  TRP B CA  
2353 C  C   . TRP B 16  ? 0.0627 0.1307 0.2592 -0.0076 0.0131  -0.0068 16  TRP B C   
2354 O  O   . TRP B 16  ? 0.0781 0.1199 0.2949 -0.0027 -0.0068 0.0007  16  TRP B O   
2355 C  CB  . TRP B 16  ? 0.0590 0.1475 0.2502 0.0052  0.0241  0.0339  16  TRP B CB  
2356 C  CG  . TRP B 16  ? 0.0800 0.1205 0.2148 0.0157  0.0299  0.0038  16  TRP B CG  
2357 C  CD1 . TRP B 16  ? 0.1234 0.1356 0.2226 0.0012  0.0505  -0.0262 16  TRP B CD1 
2358 C  CD2 . TRP B 16  ? 0.0693 0.1092 0.2407 -0.0051 0.0241  0.0127  16  TRP B CD2 
2359 N  NE1 . TRP B 16  ? 0.1076 0.1304 0.2583 0.0152  0.0577  0.0377  16  TRP B NE1 
2360 C  CE2 . TRP B 16  ? 0.1151 0.1103 0.2214 -0.0013 0.0496  -0.0071 16  TRP B CE2 
2361 C  CE3 . TRP B 16  ? 0.0692 0.1205 0.2401 0.0062  0.0397  -0.0082 16  TRP B CE3 
2362 C  CZ2 . TRP B 16  ? 0.0957 0.1130 0.2083 0.0195  0.0491  0.0003  16  TRP B CZ2 
2363 C  CZ3 . TRP B 16  ? 0.0741 0.1254 0.2315 0.0074  0.0456  0.0142  16  TRP B CZ3 
2364 C  CH2 . TRP B 16  ? 0.1146 0.1061 0.2293 -0.0041 0.0467  0.0190  16  TRP B CH2 
2365 N  N   . HIS B 17  ? 0.0583 0.1665 0.2585 -0.0116 -0.0092 0.0085  17  HIS B N   
2366 C  CA  . HIS B 17  ? 0.0715 0.1617 0.2958 0.0167  0.0013  -0.0153 17  HIS B CA  
2367 C  C   . HIS B 17  ? 0.0468 0.1789 0.3230 0.0175  -0.0119 -0.0149 17  HIS B C   
2368 O  O   . HIS B 17  ? 0.0658 0.1740 0.3375 0.0264  -0.0200 -0.0082 17  HIS B O   
2369 C  CB  . HIS B 17  ? 0.0891 0.2028 0.2836 -0.0152 0.0059  -0.0211 17  HIS B CB  
2370 C  CG  . HIS B 17  ? 0.0688 0.2098 0.3278 -0.0035 -0.0037 -0.0582 17  HIS B CG  
2371 N  ND1 . HIS B 17  ? 0.0855 0.2544 0.3840 -0.0218 -0.0423 -0.0874 17  HIS B ND1 
2372 C  CD2 . HIS B 17  ? 0.1092 0.1889 0.3623 -0.0333 0.0450  -0.1008 17  HIS B CD2 
2373 C  CE1 . HIS B 17  ? 0.1194 0.2572 0.3553 -0.0646 0.0070  -0.1075 17  HIS B CE1 
2374 N  NE2 . HIS B 17  ? 0.1056 0.2182 0.3763 -0.0423 0.0496  -0.0834 17  HIS B NE2 
2375 N  N   . LYS B 18  ? 0.0500 0.1814 0.3761 -0.0041 0.0109  -0.0337 18  LYS B N   
2376 C  CA  . LYS B 18  ? 0.0476 0.2342 0.3341 0.0098  0.0021  -0.0439 18  LYS B CA  
2377 C  C   . LYS B 18  ? 0.0709 0.2238 0.3822 0.0276  -0.0142 -0.0286 18  LYS B C   
2378 O  O   . LYS B 18  ? 0.1405 0.2513 0.5120 0.0841  -0.0754 -0.0922 18  LYS B O   
2379 C  CB  . LYS B 18  ? 0.0697 0.2150 0.3709 -0.0120 0.0175  -0.0648 18  LYS B CB  
2380 C  CG  . LYS B 18  ? 0.0847 0.2136 0.4137 -0.0364 0.0318  -0.0395 18  LYS B CG  
2381 C  CD  . LYS B 18  ? 0.0882 0.2644 0.3454 -0.0137 0.0077  -0.0414 18  LYS B CD  
2382 C  CE  . LYS B 18  ? 0.0907 0.1938 0.3682 -0.0054 0.0221  -0.0639 18  LYS B CE  
2383 N  NZ  . LYS B 18  ? 0.0696 0.2333 0.3470 -0.0471 0.0522  -0.1164 18  LYS B NZ  
2384 N  N   . ASP B 19  ? 0.0887 0.1908 0.3269 0.0020  0.0043  -0.0237 19  ASP B N   
2385 C  CA  . ASP B 19  ? 0.1394 0.1641 0.3722 -0.0038 0.0467  -0.0531 19  ASP B CA  
2386 C  C   . ASP B 19  ? 0.0873 0.1374 0.3878 0.0245  0.0131  -0.0326 19  ASP B C   
2387 O  O   . ASP B 19  ? 0.1390 0.1406 0.4203 0.0178  0.0179  -0.0582 19  ASP B O   
2388 C  CB  . ASP B 19  ? 0.1846 0.3310 0.3555 -0.0421 0.0526  -0.0337 19  ASP B CB  
2389 C  CG  . ASP B 19  ? 0.1349 0.5012 0.3271 -0.0511 0.0107  0.0066  19  ASP B CG  
2390 O  OD1 . ASP B 19  ? 0.1583 0.5152 0.4167 0.0132  0.0296  -0.0020 19  ASP B OD1 
2391 O  OD2 . ASP B 19  ? 0.5152 0.6396 0.5479 0.0688  0.1712  0.2258  19  ASP B OD2 
2392 N  N   . PHE B 20  ? 0.0767 0.1649 0.3118 0.0054  -0.0212 -0.0273 20  PHE B N   
2393 C  CA  . PHE B 20  ? 0.0736 0.1483 0.3267 0.0148  -0.0043 -0.0273 20  PHE B CA  
2394 C  C   . PHE B 20  ? 0.0582 0.1597 0.3176 0.0065  0.0010  0.0006  20  PHE B C   
2395 O  O   . PHE B 20  ? 0.1004 0.1327 0.2759 0.0137  -0.0003 -0.0046 20  PHE B O   
2396 C  CB  . PHE B 20  ? 0.0811 0.1823 0.2655 0.0153  0.0052  -0.0219 20  PHE B CB  
2397 C  CG  . PHE B 20  ? 0.0728 0.2022 0.2922 0.0403  -0.0024 -0.0223 20  PHE B CG  
2398 C  CD1 . PHE B 20  ? 0.0903 0.2522 0.3454 0.0221  -0.0107 -0.0728 20  PHE B CD1 
2399 C  CD2 . PHE B 20  ? 0.0986 0.2603 0.2935 0.0544  0.0195  -0.0193 20  PHE B CD2 
2400 C  CE1 . PHE B 20  ? 0.1203 0.2730 0.3014 -0.0113 -0.0276 -0.0767 20  PHE B CE1 
2401 C  CE2 . PHE B 20  ? 0.0970 0.2865 0.3208 0.0054  0.0447  -0.0359 20  PHE B CE2 
2402 C  CZ  . PHE B 20  ? 0.1011 0.2700 0.3298 0.0515  0.0006  -0.0791 20  PHE B CZ  
2403 N  N   . PRO B 21  ? 0.1111 0.1688 0.3064 0.0317  -0.0034 -0.0007 21  PRO B N   
2404 C  CA  . PRO B 21  ? 0.0945 0.1821 0.2834 0.0188  -0.0209 -0.0108 21  PRO B CA  
2405 C  C   . PRO B 21  ? 0.1063 0.1861 0.2764 0.0198  -0.0370 0.0273  21  PRO B C   
2406 O  O   . PRO B 21  ? 0.0719 0.2014 0.3088 -0.0013 -0.0562 0.0044  21  PRO B O   
2407 C  CB  . PRO B 21  ? 0.1101 0.3375 0.3167 0.1191  -0.0311 -0.0351 21  PRO B CB  
2408 C  CG  . PRO B 21  ? 0.2588 0.3589 0.3772 0.1924  -0.1032 -0.0549 21  PRO B CG  
2409 C  CD  . PRO B 21  ? 0.1083 0.2125 0.3463 0.0710  -0.0289 -0.0149 21  PRO B CD  
2410 N  N   A ILE B 22  ? 0.0706 0.1597 0.3012 0.0288  -0.0351 0.0410  22  ILE B N   
2411 N  N   B ILE B 22  ? 0.0706 0.1629 0.3025 0.0258  -0.0355 0.0434  22  ILE B N   
2412 C  CA  A ILE B 22  ? 0.0687 0.1492 0.2899 0.0041  -0.0432 0.0419  22  ILE B CA  
2413 C  CA  B ILE B 22  ? 0.0692 0.1498 0.2901 0.0040  -0.0445 0.0414  22  ILE B CA  
2414 C  C   A ILE B 22  ? 0.0781 0.1313 0.2362 0.0078  -0.0300 0.0368  22  ILE B C   
2415 C  C   B ILE B 22  ? 0.0797 0.1306 0.2380 0.0065  -0.0296 0.0370  22  ILE B C   
2416 O  O   A ILE B 22  ? 0.0798 0.1480 0.2442 0.0003  -0.0250 0.0127  22  ILE B O   
2417 O  O   B ILE B 22  ? 0.0804 0.1491 0.2435 0.0001  -0.0282 0.0151  22  ILE B O   
2418 C  CB  A ILE B 22  ? 0.0802 0.1365 0.2700 0.0243  -0.0410 0.0340  22  ILE B CB  
2419 C  CB  B ILE B 22  ? 0.0925 0.1404 0.2763 0.0173  -0.0392 0.0307  22  ILE B CB  
2420 C  CG1 A ILE B 22  ? 0.1186 0.1450 0.2563 -0.0242 -0.0392 0.0604  22  ILE B CG1 
2421 C  CG1 B ILE B 22  ? 0.1577 0.1298 0.2806 0.0239  -0.0098 0.0472  22  ILE B CG1 
2422 C  CG2 A ILE B 22  ? 0.1142 0.1553 0.2576 0.0794  -0.0397 0.0533  22  ILE B CG2 
2423 C  CG2 B ILE B 22  ? 0.1247 0.1834 0.2506 0.0326  -0.0292 0.0469  22  ILE B CG2 
2424 C  CD1 A ILE B 22  ? 0.0926 0.1388 0.2468 0.0277  -0.0603 -0.0153 22  ILE B CD1 
2425 C  CD1 B ILE B 22  ? 0.1618 0.2310 0.2795 0.0178  -0.0895 -0.0916 22  ILE B CD1 
2426 N  N   . ALA B 23  ? 0.0767 0.1362 0.2443 0.0159  -0.0250 0.0116  23  ALA B N   
2427 C  CA  . ALA B 23  ? 0.1105 0.1101 0.2416 0.0078  -0.0041 0.0109  23  ALA B CA  
2428 C  C   . ALA B 23  ? 0.0601 0.1523 0.2612 0.0000  -0.0375 0.0074  23  ALA B C   
2429 O  O   . ALA B 23  ? 0.0762 0.1501 0.2351 0.0109  -0.0219 0.0136  23  ALA B O   
2430 C  CB  . ALA B 23  ? 0.0640 0.1599 0.2657 -0.0131 -0.0328 0.0375  23  ALA B CB  
2431 N  N   . LYS B 24  ? 0.1049 0.1564 0.2290 0.0052  -0.0353 -0.0017 24  LYS B N   
2432 C  CA  . LYS B 24  ? 0.1062 0.1900 0.2328 0.0013  -0.0456 0.0102  24  LYS B CA  
2433 C  C   . LYS B 24  ? 0.1165 0.2389 0.2446 0.0120  -0.0715 0.0438  24  LYS B C   
2434 O  O   . LYS B 24  ? 0.1356 0.2757 0.2856 0.0098  -0.0658 0.0377  24  LYS B O   
2435 C  CB  . LYS B 24  ? 0.1040 0.2001 0.2829 -0.0015 -0.0472 0.0160  24  LYS B CB  
2436 C  CG  . LYS B 24  ? 0.1570 0.2834 0.2333 -0.0907 0.0105  -0.0359 24  LYS B CG  
2437 C  CD  . LYS B 24  ? 0.1875 0.3413 0.3107 -0.0908 -0.0305 -0.0348 24  LYS B CD  
2438 C  CE  . LYS B 24  ? 0.2487 0.3260 0.4275 0.0054  0.0839  0.0306  24  LYS B CE  
2439 N  NZ  . LYS B 24  ? 0.2462 0.3585 0.5024 -0.0271 0.0970  0.0071  24  LYS B NZ  
2440 N  N   . GLY B 25  ? 0.1041 0.1895 0.2380 0.0006  -0.0322 0.0348  25  GLY B N   
2441 C  CA  . GLY B 25  ? 0.1171 0.1915 0.2531 0.0108  -0.0116 0.0463  25  GLY B CA  
2442 C  C   . GLY B 25  ? 0.1138 0.1958 0.2074 -0.0074 -0.0494 0.0465  25  GLY B C   
2443 O  O   . GLY B 25  ? 0.1164 0.2299 0.2181 0.0097  -0.0509 0.0449  25  GLY B O   
2444 N  N   . GLU B 26  ? 0.0971 0.2757 0.2123 -0.0099 -0.0588 0.0725  26  GLU B N   
2445 C  CA  . GLU B 26  ? 0.1553 0.2531 0.1792 -0.0032 -0.0597 0.0379  26  GLU B CA  
2446 C  C   . GLU B 26  ? 0.1367 0.2060 0.1611 0.0043  -0.0540 0.0366  26  GLU B C   
2447 O  O   . GLU B 26  ? 0.1774 0.2423 0.1399 0.0270  -0.0606 0.0052  26  GLU B O   
2448 C  CB  . GLU B 26  ? 0.2005 0.3341 0.1944 0.0625  -0.0934 0.1160  26  GLU B CB  
2449 C  CG  . GLU B 26  ? 0.1762 0.3869 0.2058 -0.0260 -0.0632 0.0681  26  GLU B CG  
2450 C  CD  . GLU B 26  ? 0.3772 0.4553 0.3021 -0.0152 -0.2518 0.0533  26  GLU B CD  
2451 O  OE1 . GLU B 26  ? 0.4577 0.6395 0.4659 0.0542  -0.2280 -0.0375 26  GLU B OE1 
2452 O  OE2 . GLU B 26  ? 0.4007 0.5781 0.6413 -0.0960 -0.2401 0.0522  26  GLU B OE2 
2453 N  N   . ARG B 27  ? 0.1347 0.1232 0.1645 0.0037  -0.0648 0.0212  27  ARG B N   
2454 C  CA  . ARG B 27  ? 0.0953 0.1316 0.1404 -0.0021 -0.0373 0.0353  27  ARG B CA  
2455 C  C   . ARG B 27  ? 0.0855 0.1112 0.1331 0.0140  -0.0267 0.0324  27  ARG B C   
2456 O  O   . ARG B 27  ? 0.0997 0.1248 0.1349 -0.0030 -0.0340 0.0109  27  ARG B O   
2457 C  CB  . ARG B 27  ? 0.1742 0.1455 0.1600 -0.0140 -0.0443 0.0322  27  ARG B CB  
2458 C  CG  . ARG B 27  ? 0.2157 0.2169 0.1765 0.0041  -0.0272 0.0142  27  ARG B CG  
2459 C  CD  . ARG B 27  ? 0.3111 0.3373 0.1911 -0.1156 -0.0640 -0.0076 27  ARG B CD  
2460 N  NE  . ARG B 27  ? 0.2098 0.1685 0.1983 -0.0028 0.0131  0.0434  27  ARG B NE  
2461 C  CZ  . ARG B 27  ? 0.1601 0.1943 0.1266 -0.0283 0.0054  0.0013  27  ARG B CZ  
2462 N  NH1 . ARG B 27  ? 0.1798 0.2554 0.1981 -0.0344 -0.0129 0.1097  27  ARG B NH1 
2463 N  NH2 . ARG B 27  ? 0.1911 0.1760 0.1565 0.0299  -0.0060 0.0048  27  ARG B NH2 
2464 N  N   . GLN B 28  ? 0.0938 0.1071 0.1289 0.0076  -0.0243 0.0229  28  GLN B N   
2465 C  CA  . GLN B 28  ? 0.0663 0.1232 0.1199 0.0008  -0.0239 0.0272  28  GLN B CA  
2466 C  C   . GLN B 28  ? 0.0754 0.0988 0.1367 0.0006  -0.0115 0.0115  28  GLN B C   
2467 O  O   . GLN B 28  ? 0.1022 0.1194 0.1135 0.0126  -0.0275 0.0114  28  GLN B O   
2468 C  CB  . GLN B 28  ? 0.0606 0.1501 0.1656 0.0125  -0.0143 0.0296  28  GLN B CB  
2469 C  CG  . GLN B 28  ? 0.0952 0.1324 0.1601 0.0068  -0.0211 0.0142  28  GLN B CG  
2470 C  CD  . GLN B 28  ? 0.0781 0.1119 0.1496 -0.0071 -0.0241 0.0218  28  GLN B CD  
2471 O  OE1 . GLN B 28  ? 0.0907 0.1142 0.1564 0.0120  -0.0115 0.0346  28  GLN B OE1 
2472 N  NE2 . GLN B 28  ? 0.0782 0.1054 0.1837 0.0054  -0.0260 0.0305  28  GLN B NE2 
2473 N  N   . SER B 29  ? 0.0776 0.1042 0.1191 -0.0044 -0.0286 0.0131  29  SER B N   
2474 C  CA  . SER B 29  ? 0.0599 0.0989 0.1284 -0.0024 -0.0275 0.0259  29  SER B CA  
2475 C  C   . SER B 29  ? 0.0741 0.0917 0.1084 -0.0021 -0.0144 0.0109  29  SER B C   
2476 O  O   . SER B 29  ? 0.0737 0.0918 0.1316 0.0012  -0.0049 0.0076  29  SER B O   
2477 C  CB  . SER B 29  ? 0.0725 0.0988 0.1257 -0.0120 -0.0243 0.0197  29  SER B CB  
2478 O  OG  . SER B 29  ? 0.0876 0.0891 0.1180 -0.0074 -0.0124 0.0198  29  SER B OG  
2479 N  N   . PRO B 30  ? 0.0681 0.0910 0.1084 -0.0070 -0.0167 0.0124  30  PRO B N   
2480 C  CA  . PRO B 30  ? 0.0791 0.0891 0.1144 0.0070  -0.0144 -0.0098 30  PRO B CA  
2481 C  C   . PRO B 30  ? 0.0680 0.0842 0.1144 -0.0060 -0.0131 0.0148  30  PRO B C   
2482 O  O   . PRO B 30  ? 0.0930 0.0877 0.1186 -0.0052 -0.0271 0.0074  30  PRO B O   
2483 C  CB  . PRO B 30  ? 0.0725 0.1068 0.1124 -0.0060 -0.0181 0.0179  30  PRO B CB  
2484 C  CG  . PRO B 30  ? 0.0864 0.1020 0.1281 0.0126  -0.0010 0.0000  30  PRO B CG  
2485 C  CD  . PRO B 30  ? 0.0993 0.0953 0.1159 0.0066  -0.0118 0.0251  30  PRO B CD  
2486 N  N   . VAL B 31  ? 0.1022 0.0829 0.1020 -0.0107 0.0012  -0.0006 31  VAL B N   
2487 C  CA  . VAL B 31  ? 0.0992 0.0820 0.1053 -0.0035 -0.0230 -0.0146 31  VAL B CA  
2488 C  C   . VAL B 31  ? 0.1047 0.0797 0.1155 -0.0162 -0.0126 -0.0175 31  VAL B C   
2489 O  O   . VAL B 31  ? 0.1053 0.1022 0.1286 -0.0082 -0.0208 -0.0199 31  VAL B O   
2490 C  CB  . VAL B 31  ? 0.1283 0.0954 0.1214 0.0007  -0.0190 0.0164  31  VAL B CB  
2491 C  CG1 . VAL B 31  ? 0.1311 0.1072 0.1275 0.0023  -0.0066 -0.0003 31  VAL B CG1 
2492 C  CG2 . VAL B 31  ? 0.1068 0.1108 0.1604 -0.0141 0.0085  -0.0135 31  VAL B CG2 
2493 N  N   . ASP B 32  ? 0.1092 0.0886 0.1135 -0.0057 -0.0219 -0.0153 32  ASP B N   
2494 C  CA  . ASP B 32  ? 0.1266 0.0907 0.1146 -0.0017 -0.0043 -0.0277 32  ASP B CA  
2495 C  C   . ASP B 32  ? 0.1189 0.0907 0.0989 -0.0165 -0.0240 -0.0077 32  ASP B C   
2496 O  O   . ASP B 32  ? 0.1252 0.1477 0.1277 0.0005  -0.0251 0.0200  32  ASP B O   
2497 C  CB  . ASP B 32  ? 0.1676 0.0925 0.1225 -0.0065 -0.0211 -0.0265 32  ASP B CB  
2498 C  CG  . ASP B 32  ? 0.1536 0.1083 0.1398 -0.0093 -0.0203 -0.0240 32  ASP B CG  
2499 O  OD1 . ASP B 32  ? 0.1394 0.1004 0.1390 0.0038  -0.0244 -0.0138 32  ASP B OD1 
2500 O  OD2 . ASP B 32  ? 0.2481 0.1194 0.1406 0.0322  -0.0307 -0.0366 32  ASP B OD2 
2501 N  N   A ILE B 33  ? 0.0957 0.1156 0.1153 -0.0157 -0.0105 -0.0114 33  ILE B N   
2502 N  N   B ILE B 33  ? 0.1024 0.1169 0.1169 -0.0141 -0.0119 -0.0122 33  ILE B N   
2503 C  CA  A ILE B 33  ? 0.1274 0.1031 0.1117 -0.0216 -0.0068 -0.0131 33  ILE B CA  
2504 C  CA  B ILE B 33  ? 0.1315 0.0997 0.1177 -0.0149 -0.0060 -0.0052 33  ILE B CA  
2505 C  C   A ILE B 33  ? 0.1674 0.0786 0.1230 -0.0355 -0.0027 -0.0071 33  ILE B C   
2506 C  C   B ILE B 33  ? 0.1717 0.0799 0.1290 -0.0348 -0.0065 -0.0041 33  ILE B C   
2507 O  O   A ILE B 33  ? 0.1437 0.1045 0.1374 -0.0230 0.0148  -0.0146 33  ILE B O   
2508 O  O   B ILE B 33  ? 0.1638 0.1045 0.1353 -0.0093 0.0189  -0.0188 33  ILE B O   
2509 C  CB  A ILE B 33  ? 0.1205 0.0910 0.1239 -0.0245 0.0063  -0.0198 33  ILE B CB  
2510 C  CB  B ILE B 33  ? 0.1307 0.0962 0.1425 -0.0168 0.0073  -0.0173 33  ILE B CB  
2511 C  CG1 A ILE B 33  ? 0.0835 0.1117 0.1133 0.0052  -0.0307 -0.0233 33  ILE B CG1 
2512 C  CG1 B ILE B 33  ? 0.1415 0.1268 0.1536 -0.0026 0.0048  -0.0277 33  ILE B CG1 
2513 C  CG2 A ILE B 33  ? 0.1124 0.1189 0.1582 -0.0247 0.0138  -0.0300 33  ILE B CG2 
2514 C  CG2 B ILE B 33  ? 0.1162 0.1221 0.1762 -0.0172 0.0160  -0.0185 33  ILE B CG2 
2515 C  CD1 A ILE B 33  ? 0.0776 0.1035 0.0957 -0.0253 -0.0178 -0.0373 33  ILE B CD1 
2516 C  CD1 B ILE B 33  ? 0.2236 0.2199 0.2017 -0.0310 -0.0489 0.0249  33  ILE B CD1 
2517 N  N   A ASP B 34  ? 0.1408 0.1412 0.1263 -0.0368 -0.0024 -0.0388 34  ASP B N   
2518 N  N   B ASP B 34  ? 0.1615 0.1353 0.1248 -0.0284 0.0071  -0.0397 34  ASP B N   
2519 C  CA  A ASP B 34  ? 0.1823 0.1333 0.1280 -0.0337 0.0032  -0.0480 34  ASP B CA  
2520 C  CA  B ASP B 34  ? 0.1949 0.1328 0.1223 -0.0275 0.0049  -0.0498 34  ASP B CA  
2521 C  C   A ASP B 34  ? 0.2180 0.1335 0.1120 -0.0472 0.0381  -0.0553 34  ASP B C   
2522 C  C   B ASP B 34  ? 0.2242 0.1406 0.1155 -0.0401 0.0384  -0.0559 34  ASP B C   
2523 O  O   A ASP B 34  ? 0.2730 0.1838 0.1406 -0.0688 0.0427  -0.0093 34  ASP B O   
2524 O  O   B ASP B 34  ? 0.2858 0.1836 0.1416 -0.0599 0.0425  -0.0151 34  ASP B O   
2525 C  CB  A ASP B 34  ? 0.2560 0.1264 0.1228 -0.0419 -0.0136 -0.0372 34  ASP B CB  
2526 C  CB  B ASP B 34  ? 0.2536 0.1458 0.1408 -0.0544 -0.0190 -0.0120 34  ASP B CB  
2527 C  CG  A ASP B 34  ? 0.3860 0.1229 0.2444 -0.0179 0.0032  -0.0719 34  ASP B CG  
2528 C  CG  B ASP B 34  ? 0.4352 0.2301 0.1753 -0.0683 -0.0331 -0.0780 34  ASP B CG  
2529 O  OD1 A ASP B 34  ? 0.5443 0.0944 0.2171 -0.0542 0.1014  -0.0487 34  ASP B OD1 
2530 O  OD1 B ASP B 34  ? 0.3752 0.5267 0.1844 -0.1172 0.0348  -0.1560 34  ASP B OD1 
2531 O  OD2 A ASP B 34  ? 0.3684 0.2833 0.4735 -0.1392 0.0373  -0.2195 34  ASP B OD2 
2532 O  OD2 B ASP B 34  ? 0.4903 0.3452 0.1731 -0.0340 -0.0745 -0.1400 34  ASP B OD2 
2533 N  N   . THR B 35  ? 0.2190 0.1717 0.1504 -0.0373 0.0296  -0.0741 35  THR B N   
2534 C  CA  . THR B 35  ? 0.2071 0.2110 0.1437 -0.0702 0.0370  -0.0540 35  THR B CA  
2535 C  C   . THR B 35  ? 0.2351 0.1478 0.1462 -0.0518 0.0582  -0.0535 35  THR B C   
2536 O  O   . THR B 35  ? 0.2971 0.1899 0.1923 -0.0962 0.0763  -0.0540 35  THR B O   
2537 C  CB  . THR B 35  ? 0.2157 0.1844 0.1861 -0.0693 0.0238  -0.0610 35  THR B CB  
2538 O  OG1 . THR B 35  ? 0.2569 0.2125 0.1868 -0.0725 0.0533  -0.0582 35  THR B OG1 
2539 C  CG2 . THR B 35  ? 0.2202 0.2675 0.1801 -0.0645 0.0337  -0.0612 35  THR B CG2 
2540 N  N   A HIS B 36  ? 0.3420 0.1495 0.1498 -0.0658 0.0625  -0.0753 36  HIS B N   
2541 N  N   B HIS B 36  ? 0.3459 0.1460 0.1487 -0.0646 0.0606  -0.0733 36  HIS B N   
2542 C  CA  A HIS B 36  ? 0.3670 0.1886 0.1550 -0.0860 0.0595  -0.0706 36  HIS B CA  
2543 C  CA  B HIS B 36  ? 0.3792 0.1803 0.1555 -0.0822 0.0625  -0.0684 36  HIS B CA  
2544 C  C   A HIS B 36  ? 0.3756 0.2574 0.1272 -0.0766 0.0328  -0.0727 36  HIS B C   
2545 C  C   B HIS B 36  ? 0.3605 0.2517 0.1291 -0.0886 0.0208  -0.0680 36  HIS B C   
2546 O  O   A HIS B 36  ? 0.4090 0.3016 0.1843 -0.0436 0.0698  -0.0302 36  HIS B O   
2547 O  O   B HIS B 36  ? 0.3610 0.3021 0.1696 -0.0750 0.0383  -0.0463 36  HIS B O   
2548 C  CB  A HIS B 36  ? 0.4138 0.1936 0.1638 -0.0489 0.0078  -0.0975 36  HIS B CB  
2549 C  CB  B HIS B 36  ? 0.4447 0.1880 0.1712 -0.0658 0.0287  -0.0892 36  HIS B CB  
2550 C  CG  A HIS B 36  ? 0.4489 0.1178 0.1423 -0.0734 -0.0434 -0.0789 36  HIS B CG  
2551 C  CG  B HIS B 36  ? 0.5486 0.1189 0.3091 -0.0671 -0.0322 -0.0759 36  HIS B CG  
2552 N  ND1 A HIS B 36  ? 0.5415 0.1503 0.1817 -0.0930 -0.0769 -0.0390 36  HIS B ND1 
2553 N  ND1 B HIS B 36  ? 0.6129 0.3375 0.3434 0.1098  -0.1523 -0.0518 36  HIS B ND1 
2554 C  CD2 A HIS B 36  ? 0.5271 0.2031 0.0714 0.0364  -0.0542 0.0085  36  HIS B CD2 
2555 C  CD2 B HIS B 36  ? 0.6373 0.2540 0.2073 -0.1617 -0.0269 -0.1105 36  HIS B CD2 
2556 C  CE1 A HIS B 36  ? 0.5625 0.1835 0.1498 -0.1108 -0.0641 0.0211  36  HIS B CE1 
2557 C  CE1 B HIS B 36  ? 0.7128 0.1507 0.3524 -0.0912 0.1243  -0.0245 36  HIS B CE1 
2558 N  NE2 A HIS B 36  ? 0.5950 0.1520 0.1620 -0.0049 -0.1316 -0.0041 36  HIS B NE2 
2559 N  NE2 B HIS B 36  ? 0.6539 0.1574 0.3330 -0.2040 -0.0640 -0.0265 36  HIS B NE2 
2560 N  N   . THR B 37  ? 0.3847 0.1579 0.1952 -0.1092 0.0588  -0.0516 37  THR B N   
2561 C  CA  . THR B 37  ? 0.3727 0.1722 0.1829 -0.1190 0.0395  -0.0617 37  THR B CA  
2562 C  C   . THR B 37  ? 0.2791 0.2073 0.1620 -0.1142 0.0320  -0.0309 37  THR B C   
2563 O  O   . THR B 37  ? 0.3993 0.2572 0.1796 -0.1193 -0.0315 0.0127  37  THR B O   
2564 C  CB  . THR B 37  ? 0.4250 0.2311 0.3819 -0.1559 0.0909  -0.0606 37  THR B CB  
2565 O  OG1 . THR B 37  ? 0.6118 0.3677 0.4068 -0.1796 0.1384  -0.0939 37  THR B OG1 
2566 C  CG2 . THR B 37  ? 0.3600 0.1737 0.5288 -0.0522 0.0838  -0.1102 37  THR B CG2 
2567 N  N   . ALA B 38  ? 0.3007 0.1848 0.1313 -0.0668 0.0461  -0.0502 38  ALA B N   
2568 C  CA  . ALA B 38  ? 0.2714 0.2044 0.1187 -0.0773 0.0428  -0.0340 38  ALA B CA  
2569 C  C   . ALA B 38  ? 0.2822 0.1406 0.2254 -0.0803 0.0590  -0.0746 38  ALA B C   
2570 O  O   . ALA B 38  ? 0.4438 0.1762 0.3177 -0.0615 0.1712  -0.0658 38  ALA B O   
2571 C  CB  . ALA B 38  ? 0.2608 0.1572 0.1652 -0.0337 -0.0148 -0.0190 38  ALA B CB  
2572 N  N   . LYS B 39  ? 0.2365 0.2121 0.1679 -0.0974 0.0030  -0.0076 39  LYS B N   
2573 C  CA  . LYS B 39  ? 0.2784 0.3898 0.1300 -0.1577 -0.0236 0.0207  39  LYS B CA  
2574 C  C   . LYS B 39  ? 0.2136 0.2302 0.1023 -0.0861 0.0159  -0.0076 39  LYS B C   
2575 O  O   . LYS B 39  ? 0.1929 0.2209 0.1280 -0.0458 -0.0003 -0.0204 39  LYS B O   
2576 C  CB  . LYS B 39  ? 0.3032 0.4131 0.2385 -0.1832 -0.1464 0.0476  39  LYS B CB  
2577 C  CG  . LYS B 39  ? 0.3088 0.3828 0.2366 -0.0703 -0.0183 -0.0216 39  LYS B CG  
2578 C  CD  . LYS B 39  ? 0.3481 0.4607 0.3163 -0.2243 0.0692  -0.1380 39  LYS B CD  
2579 C  CE  . LYS B 39  ? 0.3416 0.4255 0.2417 -0.0059 0.0478  -0.0680 39  LYS B CE  
2580 N  NZ  . LYS B 39  ? 0.2682 0.6384 0.4372 -0.1345 0.1145  -0.2942 39  LYS B NZ  
2581 N  N   . TYR B 40  ? 0.3016 0.2646 0.1324 -0.0414 0.0465  -0.0500 40  TYR B N   
2582 C  CA  . TYR B 40  ? 0.2517 0.2130 0.1563 -0.0078 0.0425  -0.0060 40  TYR B CA  
2583 C  C   . TYR B 40  ? 0.1717 0.2285 0.1446 0.0164  0.0217  -0.0166 40  TYR B C   
2584 O  O   . TYR B 40  ? 0.2284 0.2764 0.1281 -0.0615 0.0280  -0.0035 40  TYR B O   
2585 C  CB  . TYR B 40  ? 0.3084 0.2551 0.1879 0.0619  0.0964  -0.0142 40  TYR B CB  
2586 C  CG  . TYR B 40  ? 0.2872 0.3499 0.2295 0.0592  0.0948  -0.0438 40  TYR B CG  
2587 C  CD1 . TYR B 40  ? 0.2400 0.3107 0.2157 0.0822  0.0197  -0.0311 40  TYR B CD1 
2588 C  CD2 . TYR B 40  ? 0.2597 0.4147 0.2337 0.0710  0.0777  0.0412  40  TYR B CD2 
2589 C  CE1 . TYR B 40  ? 0.2804 0.4072 0.2671 0.0229  0.0789  0.0096  40  TYR B CE1 
2590 C  CE2 . TYR B 40  ? 0.2498 0.5205 0.2484 0.0683  0.0929  -0.0463 40  TYR B CE2 
2591 C  CZ  . TYR B 40  ? 0.1839 0.6054 0.2500 0.0750  0.0340  0.0083  40  TYR B CZ  
2592 O  OH  . TYR B 40  ? 0.2096 0.7303 0.4176 -0.0186 0.0513  0.1354  40  TYR B OH  
2593 N  N   . ASP B 41  ? 0.1597 0.1981 0.1717 -0.0244 0.0227  0.0032  41  ASP B N   
2594 C  CA  . ASP B 41  ? 0.1647 0.1936 0.1861 0.0060  -0.0080 0.0019  41  ASP B CA  
2595 C  C   . ASP B 41  ? 0.1696 0.2615 0.1663 -0.0027 0.0215  0.0229  41  ASP B C   
2596 O  O   . ASP B 41  ? 0.1719 0.2356 0.1751 -0.0260 0.0007  -0.0026 41  ASP B O   
2597 C  CB  . ASP B 41  ? 0.1817 0.1879 0.2493 0.0284  -0.0062 0.0102  41  ASP B CB  
2598 C  CG  . ASP B 41  ? 0.2211 0.2200 0.2660 0.0631  0.0133  0.0258  41  ASP B CG  
2599 O  OD1 . ASP B 41  ? 0.2263 0.2675 0.2736 -0.0003 -0.0259 0.0659  41  ASP B OD1 
2600 O  OD2 . ASP B 41  ? 0.2985 0.2718 0.2626 0.1204  -0.0590 -0.0109 41  ASP B OD2 
2601 N  N   . PRO B 42  ? 0.1688 0.3556 0.1918 -0.0379 0.0283  0.0348  42  PRO B N   
2602 C  CA  . PRO B 42  ? 0.1814 0.3935 0.2883 -0.0443 0.0817  -0.0630 42  PRO B CA  
2603 C  C   . PRO B 42  ? 0.2134 0.3840 0.2960 -0.0846 0.0500  -0.0432 42  PRO B C   
2604 O  O   . PRO B 42  ? 0.2858 0.5582 0.2838 -0.1950 0.0687  -0.0808 42  PRO B O   
2605 C  CB  . PRO B 42  ? 0.3068 0.4646 0.2831 -0.0813 0.1298  -0.0653 42  PRO B CB  
2606 C  CG  . PRO B 42  ? 0.3519 0.4541 0.2491 -0.0745 0.0876  0.0489  42  PRO B CG  
2607 C  CD  . PRO B 42  ? 0.3113 0.3928 0.1999 -0.0917 0.1066  -0.0394 42  PRO B CD  
2608 N  N   . SER B 43  ? 0.2281 0.3222 0.2055 -0.0961 0.0186  0.0152  43  SER B N   
2609 C  CA  . SER B 43  ? 0.3192 0.2922 0.2442 -0.0527 -0.0077 0.0430  43  SER B CA  
2610 C  C   . SER B 43  ? 0.2876 0.2720 0.2302 -0.0927 0.0060  0.0181  43  SER B C   
2611 O  O   . SER B 43  ? 0.4684 0.2743 0.3120 -0.1676 -0.0287 0.0153  43  SER B O   
2612 C  CB  . SER B 43  ? 0.3244 0.2405 0.3474 0.0000  0.0526  0.0654  43  SER B CB  
2613 O  OG  . SER B 43  ? 0.3808 0.2455 0.3208 0.0214  -0.0505 0.0666  43  SER B OG  
2614 N  N   . LEU B 44  ? 0.3269 0.3055 0.1884 -0.0782 -0.0065 0.0590  44  LEU B N   
2615 C  CA  . LEU B 44  ? 0.2694 0.2996 0.1963 -0.0775 -0.0348 -0.0148 44  LEU B CA  
2616 C  C   . LEU B 44  ? 0.1863 0.2939 0.2526 -0.0381 -0.0028 -0.0277 44  LEU B C   
2617 O  O   . LEU B 44  ? 0.1689 0.4932 0.3472 0.0133  -0.0113 -0.1369 44  LEU B O   
2618 C  CB  . LEU B 44  ? 0.2073 0.2655 0.1853 0.0049  -0.0102 0.0183  44  LEU B CB  
2619 C  CG  . LEU B 44  ? 0.1900 0.2175 0.1377 -0.0087 -0.0219 -0.0249 44  LEU B CG  
2620 C  CD1 . LEU B 44  ? 0.2723 0.2346 0.1914 0.0015  0.0403  0.0328  44  LEU B CD1 
2621 C  CD2 . LEU B 44  ? 0.3283 0.2242 0.1627 0.0204  -0.0005 -0.0304 44  LEU B CD2 
2622 N  N   . LYS B 45  ? 0.2100 0.2493 0.2644 -0.0377 -0.0425 -0.0399 45  LYS B N   
2623 C  CA  . LYS B 45  ? 0.1808 0.2487 0.2601 -0.0381 -0.0443 0.0274  45  LYS B CA  
2624 C  C   . LYS B 45  ? 0.1514 0.2109 0.2623 -0.0494 0.0027  -0.0348 45  LYS B C   
2625 O  O   . LYS B 45  ? 0.1457 0.2570 0.2712 -0.0127 0.0000  0.0131  45  LYS B O   
2626 C  CB  . LYS B 45  ? 0.2486 0.2421 0.2371 -0.1053 -0.0390 0.0089  45  LYS B CB  
2627 C  CG  . LYS B 45  ? 0.2955 0.3689 0.3068 -0.0688 -0.0595 0.0623  45  LYS B CG  
2628 C  CD  . LYS B 45  ? 0.3644 0.4532 0.3989 -0.0091 -0.0675 -0.0421 45  LYS B CD  
2629 C  CE  . LYS B 45  ? 0.4384 0.5792 0.8194 -0.0522 -0.1441 0.0007  45  LYS B CE  
2630 N  NZ  . LYS B 45  ? 0.8149 0.5717 0.7480 -0.1441 0.1464  -0.0043 45  LYS B NZ  
2631 N  N   . PRO B 46  ? 0.1203 0.2658 0.2858 -0.0006 0.0030  -0.0248 46  PRO B N   
2632 C  CA  . PRO B 46  ? 0.1625 0.2996 0.2460 0.0493  0.0074  -0.0353 46  PRO B CA  
2633 C  C   . PRO B 46  ? 0.1440 0.1697 0.2173 0.0121  0.0166  -0.0108 46  PRO B C   
2634 O  O   . PRO B 46  ? 0.0945 0.2242 0.2524 0.0272  -0.0044 0.0059  46  PRO B O   
2635 C  CB  . PRO B 46  ? 0.1387 0.3348 0.2552 0.0337  0.0267  -0.0500 46  PRO B CB  
2636 C  CG  . PRO B 46  ? 0.1428 0.4397 0.3036 0.0533  0.0201  0.0472  46  PRO B CG  
2637 C  CD  . PRO B 46  ? 0.1654 0.3120 0.2788 -0.0132 0.0267  0.0548  46  PRO B CD  
2638 N  N   . LEU B 47  ? 0.1228 0.2186 0.2425 -0.0097 0.0104  -0.0272 47  LEU B N   
2639 C  CA  . LEU B 47  ? 0.0688 0.2114 0.2484 0.0249  -0.0006 -0.0211 47  LEU B CA  
2640 C  C   . LEU B 47  ? 0.0586 0.2524 0.3267 0.0227  -0.0076 -0.0645 47  LEU B C   
2641 O  O   . LEU B 47  ? 0.1185 0.2646 0.4147 0.0680  -0.0848 -0.1460 47  LEU B O   
2642 C  CB  . LEU B 47  ? 0.1669 0.2610 0.3244 -0.0326 0.0412  -0.0190 47  LEU B CB  
2643 C  CG  . LEU B 47  ? 0.1403 0.2606 0.3034 0.0187  0.0043  0.0531  47  LEU B CG  
2644 C  CD1 . LEU B 47  ? 0.1072 0.3107 0.3673 0.0447  0.0313  0.0676  47  LEU B CD1 
2645 C  CD2 . LEU B 47  ? 0.1676 0.2491 0.3693 -0.0203 0.0384  0.0379  47  LEU B CD2 
2646 N  N   . SER B 48  ? 0.1126 0.2066 0.2324 0.0483  -0.0142 -0.0533 48  SER B N   
2647 C  CA  . SER B 48  ? 0.1284 0.2139 0.2157 0.0155  -0.0120 -0.0443 48  SER B CA  
2648 C  C   . SER B 48  ? 0.0959 0.2278 0.2223 0.0267  -0.0306 -0.0295 48  SER B C   
2649 O  O   . SER B 48  ? 0.1212 0.1843 0.2184 0.0303  -0.0010 0.0037  48  SER B O   
2650 C  CB  . SER B 48  ? 0.1223 0.2204 0.2973 0.0359  -0.0436 -0.0318 48  SER B CB  
2651 O  OG  . SER B 48  ? 0.1847 0.3267 0.2944 -0.0405 0.0258  -0.0980 48  SER B OG  
2652 N  N   . VAL B 49  ? 0.1701 0.1865 0.2130 0.0432  -0.0315 -0.0218 49  VAL B N   
2653 C  CA  . VAL B 49  ? 0.1958 0.2229 0.2143 0.0674  -0.0228 -0.0008 49  VAL B CA  
2654 C  C   . VAL B 49  ? 0.2177 0.2615 0.2486 0.0944  -0.0766 0.0154  49  VAL B C   
2655 O  O   . VAL B 49  ? 0.2242 0.3601 0.2594 0.1492  -0.0816 -0.0276 49  VAL B O   
2656 C  CB  . VAL B 49  ? 0.2784 0.2078 0.2366 0.0790  0.0260  0.0126  49  VAL B CB  
2657 C  CG1 . VAL B 49  ? 0.4040 0.2572 0.2436 0.1079  0.0384  0.0060  49  VAL B CG1 
2658 C  CG2 . VAL B 49  ? 0.2906 0.1881 0.3391 0.0930  0.0183  -0.0109 49  VAL B CG2 
2659 N  N   . SER B 50  ? 0.1539 0.2763 0.2215 0.0577  -0.0282 -0.0159 50  SER B N   
2660 C  CA  . SER B 50  ? 0.1419 0.3181 0.2975 0.0623  -0.0346 -0.0342 50  SER B CA  
2661 C  C   . SER B 50  ? 0.1328 0.3512 0.2885 0.0608  -0.0631 0.0254  50  SER B C   
2662 O  O   . SER B 50  ? 0.1961 0.2820 0.2904 0.0414  -0.0967 -0.0368 50  SER B O   
2663 C  CB  . SER B 50  ? 0.2554 0.3556 0.3750 0.0322  0.0233  -0.0653 50  SER B CB  
2664 O  OG  . SER B 50  ? 0.2080 0.4205 0.4264 0.0190  -0.0132 0.0063  50  SER B OG  
2665 N  N   . TYR B 51  ? 0.1728 0.2786 0.2538 0.0698  -0.0551 -0.0148 51  TYR B N   
2666 C  CA  . TYR B 51  ? 0.1519 0.2457 0.2626 0.0621  -0.0772 -0.0187 51  TYR B CA  
2667 C  C   . TYR B 51  ? 0.1423 0.3310 0.3271 0.0226  -0.0656 -0.1147 51  TYR B C   
2668 O  O   . TYR B 51  ? 0.2040 0.3005 0.2921 0.0483  -0.1178 -0.0740 51  TYR B O   
2669 C  CB  . TYR B 51  ? 0.1466 0.2098 0.2238 0.0560  -0.0777 -0.0226 51  TYR B CB  
2670 C  CG  . TYR B 51  ? 0.1425 0.2094 0.1760 0.0498  -0.0505 -0.0054 51  TYR B CG  
2671 C  CD1 . TYR B 51  ? 0.1731 0.1453 0.2635 0.0482  -0.0989 -0.0377 51  TYR B CD1 
2672 C  CD2 . TYR B 51  ? 0.1724 0.1747 0.1720 0.0403  -0.0401 -0.0171 51  TYR B CD2 
2673 C  CE1 . TYR B 51  ? 0.1597 0.1555 0.1805 0.0324  -0.0379 -0.0263 51  TYR B CE1 
2674 C  CE2 . TYR B 51  ? 0.1631 0.1485 0.1609 0.0309  -0.0493 0.0000  51  TYR B CE2 
2675 C  CZ  . TYR B 51  ? 0.1300 0.1588 0.1629 0.0438  -0.0256 -0.0068 51  TYR B CZ  
2676 O  OH  . TYR B 51  ? 0.1385 0.1448 0.1808 0.0153  -0.0498 -0.0049 51  TYR B OH  
2677 N  N   . ASP B 52  ? 0.1149 0.4314 0.3124 0.0791  -0.0762 -0.0870 52  ASP B N   
2678 C  CA  . ASP B 52  ? 0.1539 0.3544 0.3519 -0.0322 -0.0914 -0.1244 52  ASP B CA  
2679 C  C   . ASP B 52  ? 0.2457 0.3700 0.3370 0.0240  -0.1617 -0.1013 52  ASP B C   
2680 O  O   . ASP B 52  ? 0.3847 0.3623 0.3679 0.0873  -0.2091 -0.1234 52  ASP B O   
2681 C  CB  . ASP B 52  ? 0.1862 0.4260 0.3594 0.0007  -0.0848 -0.1416 52  ASP B CB  
2682 C  CG  . ASP B 52  ? 0.2646 0.5486 0.7332 0.0507  0.0754  -0.0467 52  ASP B CG  
2683 O  OD1 . ASP B 52  ? 0.3795 0.5314 0.6919 0.0121  0.1598  -0.0104 52  ASP B OD1 
2684 O  OD2 . ASP B 52  ? 0.7415 1.0470 0.9172 -0.2289 -0.0516 -0.5371 52  ASP B OD2 
2685 N  N   . GLN B 53  ? 0.2017 0.3479 0.3639 0.0186  -0.1134 -0.0954 53  GLN B N   
2686 C  CA  . GLN B 53  ? 0.2459 0.2754 0.3867 -0.0524 -0.1039 -0.1005 53  GLN B CA  
2687 C  C   . GLN B 53  ? 0.2772 0.1922 0.2094 0.0040  -0.0403 -0.0087 53  GLN B C   
2688 O  O   . GLN B 53  ? 0.2017 0.2583 0.3043 0.0105  -0.0737 -0.0573 53  GLN B O   
2689 C  CB  . GLN B 53  ? 0.2967 0.3077 0.5454 -0.0666 -0.0408 -0.0954 53  GLN B CB  
2690 C  CG  . GLN B 53  ? 0.2957 0.5945 0.4426 -0.0920 -0.0546 -0.1177 53  GLN B CG  
2691 C  CD  . GLN B 53  ? 0.2633 0.7153 0.3411 -0.0560 0.0351  -0.1713 53  GLN B CD  
2692 O  OE1 . GLN B 53  ? 0.5220 1.0715 0.4404 -0.3072 0.1536  -0.2393 53  GLN B OE1 
2693 N  NE2 . GLN B 53  ? 0.2944 1.1433 0.3862 0.0010  -0.0799 -0.2201 53  GLN B NE2 
2694 N  N   . ALA B 54  ? 0.2188 0.1672 0.2800 0.0274  -0.0538 -0.0066 54  ALA B N   
2695 C  CA  . ALA B 54  ? 0.2358 0.1731 0.2293 0.0000  -0.0771 0.0094  54  ALA B CA  
2696 C  C   . ALA B 54  ? 0.3273 0.1956 0.2310 0.0361  -0.0733 0.0399  54  ALA B C   
2697 O  O   . ALA B 54  ? 0.3429 0.3036 0.2985 0.1244  -0.0992 0.0575  54  ALA B O   
2698 C  CB  . ALA B 54  ? 0.2709 0.1448 0.3472 0.0057  -0.0221 0.0133  54  ALA B CB  
2699 N  N   . THR B 55  ? 0.2637 0.1509 0.1703 -0.0104 -0.0586 -0.0121 55  THR B N   
2700 C  CA  . THR B 55  ? 0.2917 0.1634 0.2022 -0.0851 -0.0749 -0.0038 55  THR B CA  
2701 C  C   . THR B 55  ? 0.2716 0.1158 0.1464 -0.0003 -0.0904 -0.0141 55  THR B C   
2702 O  O   . THR B 55  ? 0.2682 0.1110 0.1775 -0.0027 -0.0606 -0.0177 55  THR B O   
2703 C  CB  . THR B 55  ? 0.3896 0.2459 0.2409 -0.0846 0.0120  -0.0799 55  THR B CB  
2704 O  OG1 . THR B 55  ? 0.4088 0.1839 0.4890 -0.0693 -0.1788 0.0227  55  THR B OG1 
2705 C  CG2 . THR B 55  ? 0.5604 0.2031 0.1999 -0.1521 -0.0160 -0.0640 55  THR B CG2 
2706 N  N   . SER B 56  ? 0.3332 0.1047 0.1848 -0.0474 -0.1306 -0.0081 56  SER B N   
2707 C  CA  . SER B 56  ? 0.3436 0.1065 0.1421 -0.0119 -0.0798 -0.0178 56  SER B CA  
2708 C  C   . SER B 56  ? 0.3438 0.1397 0.1861 -0.0720 -0.0361 -0.0293 56  SER B C   
2709 O  O   . SER B 56  ? 0.4713 0.1208 0.1793 -0.0925 -0.1221 -0.0091 56  SER B O   
2710 C  CB  . SER B 56  ? 0.4092 0.1099 0.1705 -0.0073 -0.1181 -0.0226 56  SER B CB  
2711 O  OG  . SER B 56  ? 0.4273 0.0968 0.2019 -0.0216 -0.1599 -0.0049 56  SER B OG  
2712 N  N   . LEU B 57  ? 0.3411 0.0986 0.1083 -0.0513 -0.0329 -0.0089 57  LEU B N   
2713 C  CA  . LEU B 57  ? 0.4119 0.1083 0.1697 -0.0741 -0.0140 -0.0138 57  LEU B CA  
2714 C  C   . LEU B 57  ? 0.4142 0.1187 0.1324 -0.0658 -0.0212 -0.0412 57  LEU B C   
2715 O  O   . LEU B 57  ? 0.4352 0.1230 0.1196 -0.0529 -0.0255 -0.0355 57  LEU B O   
2716 C  CB  . LEU B 57  ? 0.4275 0.1733 0.1872 -0.0115 0.0221  -0.0436 57  LEU B CB  
2717 C  CG  . LEU B 57  ? 0.5849 0.1056 0.2293 -0.0702 -0.0401 0.0207  57  LEU B CG  
2718 C  CD1 . LEU B 57  ? 0.5794 0.1589 0.3190 0.0401  0.0617  -0.0507 57  LEU B CD1 
2719 C  CD2 . LEU B 57  ? 0.7680 0.1651 0.2745 -0.1629 -0.1341 -0.0041 57  LEU B CD2 
2720 N  N   A ARG B 58  ? 0.3961 0.1383 0.1453 -0.1033 -0.0127 -0.0366 58  ARG B N   
2721 N  N   B ARG B 58  ? 0.4262 0.1416 0.1390 -0.1172 -0.0131 -0.0196 58  ARG B N   
2722 C  CA  A ARG B 58  ? 0.2723 0.1516 0.1592 -0.0275 -0.0214 -0.0502 58  ARG B CA  
2723 C  CA  B ARG B 58  ? 0.3095 0.1476 0.1536 -0.0286 -0.0068 -0.0683 58  ARG B CA  
2724 C  C   A ARG B 58  ? 0.3109 0.1058 0.1232 -0.0057 -0.0234 -0.0170 58  ARG B C   
2725 C  C   B ARG B 58  ? 0.3235 0.0996 0.1282 -0.0068 -0.0194 -0.0230 58  ARG B C   
2726 O  O   A ARG B 58  ? 0.4092 0.1238 0.1135 -0.0593 0.0051  -0.0276 58  ARG B O   
2727 O  O   B ARG B 58  ? 0.4005 0.1254 0.1229 -0.0557 0.0066  -0.0292 58  ARG B O   
2728 C  CB  A ARG B 58  ? 0.1491 0.2912 0.1103 0.0057  0.0054  0.0133  58  ARG B CB  
2729 C  CB  B ARG B 58  ? 0.2739 0.2085 0.1917 -0.0527 -0.0164 -0.0474 58  ARG B CB  
2730 C  CG  A ARG B 58  ? 0.0782 0.1959 0.2836 -0.0154 0.0719  -0.1773 58  ARG B CG  
2731 C  CG  B ARG B 58  ? 0.2084 0.1845 0.3330 0.0601  0.0615  -0.0807 58  ARG B CG  
2732 C  CD  A ARG B 58  ? 0.1780 0.2752 0.1247 0.0835  0.0153  -0.0617 58  ARG B CD  
2733 C  CD  B ARG B 58  ? 0.3086 0.2773 0.2657 0.0144  0.0665  -0.1299 58  ARG B CD  
2734 N  NE  A ARG B 58  ? 0.1101 0.1890 0.1316 0.0006  0.0035  -0.0522 58  ARG B NE  
2735 N  NE  B ARG B 58  ? 0.4061 0.4271 0.3494 0.0010  0.0080  -0.0736 58  ARG B NE  
2736 C  CZ  A ARG B 58  ? 0.0898 0.2869 0.1216 0.0551  -0.0171 -0.0806 58  ARG B CZ  
2737 C  CZ  B ARG B 58  ? 0.2437 0.3571 0.2849 0.0529  0.0390  -0.1272 58  ARG B CZ  
2738 N  NH1 A ARG B 58  ? 0.2265 0.1748 0.1406 0.0421  0.0233  -0.0524 58  ARG B NH1 
2739 N  NH1 B ARG B 58  ? 0.2141 0.2761 0.2994 0.1112  -0.1335 -0.1606 58  ARG B NH1 
2740 N  NH2 A ARG B 58  ? 0.1428 0.1564 0.1098 0.0793  0.0060  -0.0225 58  ARG B NH2 
2741 N  NH2 B ARG B 58  ? 0.5062 0.4771 0.3472 0.0392  -0.0245 -0.0921 58  ARG B NH2 
2742 N  N   . ILE B 59  ? 0.2960 0.1277 0.1105 -0.0300 -0.0178 -0.0136 59  ILE B N   
2743 C  CA  . ILE B 59  ? 0.2139 0.1270 0.1386 -0.0013 -0.0306 -0.0278 59  ILE B CA  
2744 C  C   . ILE B 59  ? 0.2408 0.0850 0.1380 -0.0012 -0.0518 -0.0326 59  ILE B C   
2745 O  O   . ILE B 59  ? 0.3725 0.1710 0.1010 -0.0494 -0.0166 -0.0240 59  ILE B O   
2746 C  CB  . ILE B 59  ? 0.3149 0.0966 0.1221 -0.0098 -0.0383 -0.0089 59  ILE B CB  
2747 C  CG1 . ILE B 59  ? 0.2861 0.0970 0.1174 -0.0093 -0.0450 -0.0024 59  ILE B CG1 
2748 C  CG2 . ILE B 59  ? 0.3677 0.1187 0.1108 -0.0315 -0.0763 0.0068  59  ILE B CG2 
2749 C  CD1 . ILE B 59  ? 0.3535 0.0979 0.1160 0.0071  -0.0331 -0.0032 59  ILE B CD1 
2750 N  N   . LEU B 60  ? 0.1599 0.1304 0.2150 0.0093  -0.0573 -0.0038 60  LEU B N   
2751 C  CA  . LEU B 60  ? 0.2558 0.1084 0.1229 0.0166  -0.0649 -0.0298 60  LEU B CA  
2752 C  C   . LEU B 60  ? 0.2463 0.1151 0.1168 0.0186  -0.0252 -0.0133 60  LEU B C   
2753 O  O   . LEU B 60  ? 0.2256 0.1403 0.1056 0.0178  0.0038  -0.0296 60  LEU B O   
2754 C  CB  . LEU B 60  ? 0.2120 0.1298 0.1990 0.0562  -0.0260 -0.0137 60  LEU B CB  
2755 C  CG  . LEU B 60  ? 0.2511 0.1158 0.1741 0.0320  -0.0350 -0.0417 60  LEU B CG  
2756 C  CD1 . LEU B 60  ? 0.2439 0.1672 0.2005 0.0478  0.0092  -0.0274 60  LEU B CD1 
2757 C  CD2 . LEU B 60  ? 0.3140 0.1254 0.2389 0.0654  -0.0342 -0.0078 60  LEU B CD2 
2758 N  N   . ASN B 61  ? 0.3100 0.1212 0.1221 0.0397  0.0162  -0.0215 61  ASN B N   
2759 C  CA  . ASN B 61  ? 0.2924 0.1665 0.1254 0.0644  0.0410  0.0307  61  ASN B CA  
2760 C  C   . ASN B 61  ? 0.2696 0.1426 0.1367 0.0524  0.0125  -0.0184 61  ASN B C   
2761 O  O   . ASN B 61  ? 0.3680 0.1252 0.1491 0.0705  0.0410  -0.0273 61  ASN B O   
2762 C  CB  . ASN B 61  ? 0.3540 0.1106 0.1459 0.0485  0.0379  -0.0176 61  ASN B CB  
2763 C  CG  . ASN B 61  ? 0.2725 0.1570 0.1156 0.0909  0.0419  0.0220  61  ASN B CG  
2764 O  OD1 . ASN B 61  ? 0.2804 0.1379 0.1591 0.0719  0.0538  0.0255  61  ASN B OD1 
2765 N  ND2 . ASN B 61  ? 0.3165 0.1304 0.1392 0.0851  0.0610  0.0339  61  ASN B ND2 
2766 N  N   . ASN B 62  ? 0.3470 0.1144 0.1333 0.0812  0.0223  0.0006  62  ASN B N   
2767 C  CA  . ASN B 62  ? 0.2946 0.1764 0.1385 0.0582  -0.0046 -0.0062 62  ASN B CA  
2768 C  C   . ASN B 62  ? 0.2815 0.1922 0.1512 0.1410  0.0281  -0.0170 62  ASN B C   
2769 O  O   . ASN B 62  ? 0.3483 0.2470 0.2120 0.1623  0.0416  0.0115  62  ASN B O   
2770 C  CB  . ASN B 62  ? 0.4582 0.1212 0.1976 0.0838  0.0031  0.0010  62  ASN B CB  
2771 C  CG  . ASN B 62  ? 0.3301 0.1354 0.1471 0.0795  0.0024  0.0201  62  ASN B CG  
2772 O  OD1 . ASN B 62  ? 0.3142 0.1176 0.1622 0.0615  0.0320  0.0013  62  ASN B OD1 
2773 N  ND2 . ASN B 62  ? 0.5157 0.1512 0.1875 0.0737  0.0559  0.0153  62  ASN B ND2 
2774 N  N   . GLY B 63  ? 0.2585 0.1787 0.1729 0.0841  0.0392  -0.0074 63  GLY B N   
2775 C  CA  . GLY B 63  ? 0.2660 0.1972 0.1492 0.1340  0.0513  0.0049  63  GLY B CA  
2776 C  C   . GLY B 63  ? 0.2599 0.1561 0.1958 0.0707  0.0662  0.0284  63  GLY B C   
2777 O  O   . GLY B 63  ? 0.2240 0.2360 0.2355 0.0918  0.0487  0.0555  63  GLY B O   
2778 N  N   . HIS B 64  ? 0.2177 0.1602 0.1584 0.0952  0.0645  0.0179  64  HIS B N   
2779 C  CA  . HIS B 64  ? 0.2101 0.1846 0.1740 0.0865  0.0215  -0.0097 64  HIS B CA  
2780 C  C   . HIS B 64  ? 0.1766 0.1670 0.1678 0.0628  0.0315  -0.0163 64  HIS B C   
2781 O  O   . HIS B 64  ? 0.1922 0.2347 0.3801 0.0474  0.0384  -0.1471 64  HIS B O   
2782 C  CB  . HIS B 64  ? 0.1987 0.2053 0.1701 0.0781  0.0370  0.0027  64  HIS B CB  
2783 C  CG  . HIS B 64  ? 0.2333 0.2089 0.1927 0.0445  0.0362  -0.0205 64  HIS B CG  
2784 N  ND1 . HIS B 64  ? 0.2191 0.2599 0.2333 0.0762  0.0505  0.0888  64  HIS B ND1 
2785 C  CD2 . HIS B 64  ? 0.3059 0.1988 0.1950 0.0744  0.0456  0.0193  64  HIS B CD2 
2786 C  CE1 . HIS B 64  ? 0.1990 0.3264 0.2524 0.0988  0.0333  0.0155  64  HIS B CE1 
2787 N  NE2 . HIS B 64  ? 0.2933 0.2858 0.2991 0.0702  0.0913  0.0366  64  HIS B NE2 
2788 N  N   . ALA B 65  ? 0.1884 0.1474 0.1295 0.0627  0.0131  -0.0041 65  ALA B N   
2789 C  CA  . ALA B 65  ? 0.1791 0.1117 0.1354 0.0511  0.0241  0.0013  65  ALA B CA  
2790 C  C   . ALA B 65  ? 0.2383 0.0988 0.1004 0.0449  0.0357  -0.0044 65  ALA B C   
2791 O  O   . ALA B 65  ? 0.2314 0.1498 0.1354 0.0399  0.0392  -0.0318 65  ALA B O   
2792 C  CB  . ALA B 65  ? 0.2161 0.1810 0.1228 0.0285  0.0208  -0.0126 65  ALA B CB  
2793 N  N   . PHE B 66  ? 0.2187 0.1065 0.1169 0.0383  0.0167  -0.0184 66  PHE B N   
2794 C  CA  . PHE B 66  ? 0.2597 0.1040 0.1063 0.0241  -0.0031 -0.0241 66  PHE B CA  
2795 C  C   . PHE B 66  ? 0.2143 0.0996 0.0910 0.0258  -0.0110 -0.0153 66  PHE B C   
2796 O  O   . PHE B 66  ? 0.2743 0.1058 0.0961 0.0249  0.0083  -0.0190 66  PHE B O   
2797 C  CB  . PHE B 66  ? 0.2635 0.1589 0.1045 0.0346  -0.0049 -0.0126 66  PHE B CB  
2798 C  CG  . PHE B 66  ? 0.2425 0.1383 0.0953 0.0196  -0.0197 -0.0010 66  PHE B CG  
2799 C  CD1 . PHE B 66  ? 0.2364 0.1771 0.1004 0.0183  -0.0232 -0.0052 66  PHE B CD1 
2800 C  CD2 . PHE B 66  ? 0.2633 0.1324 0.1153 0.0131  0.0070  0.0164  66  PHE B CD2 
2801 C  CE1 . PHE B 66  ? 0.2317 0.1410 0.1149 0.0250  -0.0381 -0.0121 66  PHE B CE1 
2802 C  CE2 . PHE B 66  ? 0.2360 0.1272 0.1230 0.0489  -0.0081 0.0195  66  PHE B CE2 
2803 C  CZ  . PHE B 66  ? 0.2256 0.1358 0.1229 0.0340  -0.0204 0.0055  66  PHE B CZ  
2804 N  N   . ASN B 67  ? 0.2310 0.1045 0.1108 0.0219  -0.0107 -0.0230 67  ASN B N   
2805 C  CA  . ASN B 67  ? 0.2409 0.0988 0.1138 0.0296  -0.0046 -0.0076 67  ASN B CA  
2806 C  C   . ASN B 67  ? 0.2606 0.0834 0.0968 -0.0054 -0.0432 -0.0198 67  ASN B C   
2807 O  O   . ASN B 67  ? 0.2967 0.1313 0.1089 0.0107  -0.0220 -0.0252 67  ASN B O   
2808 C  CB  . ASN B 67  ? 0.2542 0.1182 0.1360 0.0608  -0.0138 -0.0096 67  ASN B CB  
2809 C  CG  . ASN B 67  ? 0.2646 0.1571 0.1836 0.0907  0.0221  0.0052  67  ASN B CG  
2810 O  OD1 . ASN B 67  ? 0.2576 0.2155 0.1608 0.0942  -0.0288 -0.0331 67  ASN B OD1 
2811 N  ND2 . ASN B 67  ? 0.2083 0.2269 0.3048 0.0942  -0.0452 0.0114  67  ASN B ND2 
2812 N  N   . VAL B 68  ? 0.2412 0.1072 0.1135 0.0019  -0.0012 -0.0017 68  VAL B N   
2813 C  CA  . VAL B 68  ? 0.3199 0.0959 0.0900 -0.0794 -0.0487 -0.0126 68  VAL B CA  
2814 C  C   . VAL B 68  ? 0.3195 0.1065 0.1108 -0.0421 -0.0353 -0.0111 68  VAL B C   
2815 O  O   . VAL B 68  ? 0.3066 0.0938 0.1072 -0.0324 -0.0300 -0.0066 68  VAL B O   
2816 C  CB  . VAL B 68  ? 0.3043 0.0807 0.1523 -0.0298 -0.0277 -0.0170 68  VAL B CB  
2817 C  CG1 . VAL B 68  ? 0.3265 0.1615 0.1289 -0.0719 -0.0751 0.0109  68  VAL B CG1 
2818 C  CG2 . VAL B 68  ? 0.3079 0.1268 0.1467 -0.0109 -0.0504 0.0399  68  VAL B CG2 
2819 N  N   . GLU B 69  ? 0.3896 0.1250 0.0869 -0.0489 0.0135  -0.0131 69  GLU B N   
2820 C  CA  . GLU B 69  ? 0.2517 0.1415 0.1168 0.0008  0.0126  -0.0100 69  GLU B CA  
2821 C  C   . GLU B 69  ? 0.3492 0.0977 0.1784 -0.0601 -0.0628 -0.0156 69  GLU B C   
2822 O  O   . GLU B 69  ? 0.2570 0.1413 0.1744 -0.0483 -0.0292 -0.0083 69  GLU B O   
2823 C  CB  . GLU B 69  ? 0.1354 0.2096 0.2119 -0.0195 0.0307  -0.0172 69  GLU B CB  
2824 C  CG  . GLU B 69  ? 0.1291 0.2190 0.2284 0.0240  0.0305  -0.0394 69  GLU B CG  
2825 C  CD  . GLU B 69  ? 0.1864 0.1739 0.2242 -0.0021 0.0377  -0.0423 69  GLU B CD  
2826 O  OE1 . GLU B 69  ? 0.2522 0.2150 0.2448 0.0093  0.0126  -0.0665 69  GLU B OE1 
2827 O  OE2 . GLU B 69  ? 0.1783 0.2579 0.2969 0.0261  0.0443  -0.0650 69  GLU B OE2 
2828 N  N   . PHE B 70  ? 0.2732 0.1027 0.1275 -0.0127 -0.0181 -0.0166 70  PHE B N   
2829 C  CA  . PHE B 70  ? 0.2381 0.0825 0.1632 -0.0322 -0.0608 -0.0151 70  PHE B CA  
2830 C  C   . PHE B 70  ? 0.2664 0.0930 0.1559 -0.0469 -0.0511 0.0000  70  PHE B C   
2831 O  O   . PHE B 70  ? 0.2775 0.0898 0.1981 -0.0167 -0.0689 -0.0200 70  PHE B O   
2832 C  CB  . PHE B 70  ? 0.2389 0.1088 0.1257 -0.0041 -0.0621 -0.0041 70  PHE B CB  
2833 C  CG  . PHE B 70  ? 0.2806 0.0675 0.1450 -0.0328 -0.0778 -0.0175 70  PHE B CG  
2834 C  CD1 . PHE B 70  ? 0.2644 0.0971 0.1270 -0.0436 -0.0310 -0.0275 70  PHE B CD1 
2835 C  CD2 . PHE B 70  ? 0.2793 0.1023 0.1362 -0.0262 -0.0571 -0.0035 70  PHE B CD2 
2836 C  CE1 . PHE B 70  ? 0.2623 0.1169 0.1645 -0.0361 -0.0428 -0.0322 70  PHE B CE1 
2837 C  CE2 . PHE B 70  ? 0.2976 0.0991 0.1437 -0.0129 -0.0383 -0.0249 70  PHE B CE2 
2838 C  CZ  . PHE B 70  ? 0.2820 0.1174 0.1360 -0.0280 -0.0303 -0.0019 70  PHE B CZ  
2839 N  N   . ASP B 71  ? 0.3019 0.0908 0.2008 -0.0491 -0.1062 -0.0214 71  ASP B N   
2840 C  CA  . ASP B 71  ? 0.2800 0.1013 0.2148 -0.0500 -0.0646 -0.0461 71  ASP B CA  
2841 C  C   . ASP B 71  ? 0.2445 0.0799 0.2824 0.0333  -0.0328 -0.0245 71  ASP B C   
2842 O  O   . ASP B 71  ? 0.2608 0.1678 0.3856 0.0394  -0.0082 0.0383  71  ASP B O   
2843 C  CB  . ASP B 71  ? 0.3404 0.1047 0.3944 -0.0105 -0.1916 -0.0791 71  ASP B CB  
2844 C  CG  . ASP B 71  ? 0.4000 0.1468 0.4343 -0.0428 -0.2078 -0.0447 71  ASP B CG  
2845 O  OD1 . ASP B 71  ? 0.3569 0.1221 0.4600 -0.0582 -0.1520 -0.0353 71  ASP B OD1 
2846 O  OD2 . ASP B 71  ? 0.5056 0.1399 0.8750 -0.0309 -0.4413 -0.0644 71  ASP B OD2 
2847 N  N   . ASP B 72  ? 0.1723 0.0785 0.2304 0.0035  -0.0073 -0.0196 72  ASP B N   
2848 C  CA  . ASP B 72  ? 0.2089 0.0872 0.2326 0.0054  0.0000  -0.0024 72  ASP B CA  
2849 C  C   . ASP B 72  ? 0.3005 0.1035 0.2908 0.0096  -0.0024 -0.0109 72  ASP B C   
2850 O  O   . ASP B 72  ? 0.3169 0.1004 0.2707 0.0266  0.0364  0.0046  72  ASP B O   
2851 C  CB  . ASP B 72  ? 0.2138 0.1254 0.2041 0.0030  0.0381  0.0003  72  ASP B CB  
2852 C  CG  . ASP B 72  ? 0.2114 0.1455 0.1615 -0.0255 0.0006  -0.0049 72  ASP B CG  
2853 O  OD1 . ASP B 72  ? 0.2434 0.1985 0.1978 0.0434  -0.0216 -0.0430 72  ASP B OD1 
2854 O  OD2 . ASP B 72  ? 0.2353 0.1961 0.1708 0.0280  -0.0300 -0.0280 72  ASP B OD2 
2855 N  N   . SER B 73  ? 0.2583 0.0959 0.3224 0.0015  0.0046  -0.0275 73  SER B N   
2856 C  CA  . SER B 73  ? 0.2552 0.1040 0.3535 -0.0048 0.0322  -0.0286 73  SER B CA  
2857 C  C   . SER B 73  ? 0.2204 0.0984 0.3871 0.0120  0.0375  0.0388  73  SER B C   
2858 O  O   . SER B 73  ? 0.2806 0.0982 0.3332 -0.0060 0.0054  -0.0168 73  SER B O   
2859 C  CB  . SER B 73  ? 0.4203 0.1494 0.4293 0.0300  -0.0157 -0.1248 73  SER B CB  
2860 O  OG  . SER B 73  ? 0.3822 0.1238 0.3497 -0.0482 0.0485  -0.0632 73  SER B OG  
2861 N  N   . GLN B 74  ? 0.2170 0.1360 0.4681 -0.0027 0.0373  -0.0059 74  GLN B N   
2862 C  CA  . GLN B 74  ? 0.2845 0.1787 0.4458 -0.0272 0.0663  -0.0502 74  GLN B CA  
2863 C  C   . GLN B 74  ? 0.2001 0.2558 0.3016 -0.0989 -0.0217 -0.0379 74  GLN B C   
2864 O  O   . GLN B 74  ? 0.1703 0.1832 0.2542 -0.0035 -0.0653 -0.0171 74  GLN B O   
2865 C  CB  . GLN B 74  ? 0.2707 0.1909 0.5378 -0.0449 0.0715  -0.0502 74  GLN B CB  
2866 C  CG  . GLN B 74  ? 0.2750 0.1719 0.7968 0.0286  0.0408  -0.1536 74  GLN B CG  
2867 C  CD  . GLN B 74  ? 0.2711 0.5612 0.8902 -0.0177 -0.0006 -0.1938 74  GLN B CD  
2868 O  OE1 . GLN B 74  ? 0.5157 0.7069 1.0298 -0.0603 0.3515  -0.1555 74  GLN B OE1 
2869 N  NE2 . GLN B 74  ? 0.7889 0.3567 0.9140 0.0597  -0.0003 0.2425  74  GLN B NE2 
2870 N  N   . ASP B 75  ? 0.2504 0.2531 0.3375 0.0628  0.0208  0.0274  75  ASP B N   
2871 C  CA  . ASP B 75  ? 0.2592 0.1660 0.2619 -0.0181 -0.0483 0.0162  75  ASP B CA  
2872 C  C   . ASP B 75  ? 0.2037 0.3016 0.3125 0.0077  -0.0688 0.0582  75  ASP B C   
2873 O  O   . ASP B 75  ? 0.1836 0.5345 0.4961 0.0082  -0.0337 0.0718  75  ASP B O   
2874 C  CB  . ASP B 75  ? 0.3794 0.4800 0.3971 0.0661  0.0566  0.1941  75  ASP B CB  
2875 C  CG  . ASP B 75  ? 0.5116 0.6690 0.7082 0.1562  0.1658  -0.1891 75  ASP B CG  
2876 O  OD1 . ASP B 75  ? 0.4815 1.0048 0.2091 0.3713  0.0967  0.0974  75  ASP B OD1 
2877 O  OD2 . ASP B 75  ? 0.2008 0.5382 0.7659 0.1124  -0.0192 -0.0522 75  ASP B OD2 
2878 N  N   . LYS B 76  ? 0.2675 0.1807 0.2468 0.0179  -0.0483 -0.0498 76  LYS B N   
2879 C  CA  . LYS B 76  ? 0.4004 0.1575 0.3413 0.0351  -0.0388 -0.0186 76  LYS B CA  
2880 C  C   . LYS B 76  ? 0.6708 0.1465 0.6413 -0.0480 -0.0718 -0.1165 76  LYS B C   
2881 O  O   . LYS B 76  ? 0.4492 0.7233 1.0189 0.0126  -0.1230 -0.1899 76  LYS B O   
2882 C  CB  . LYS B 76  ? 0.4088 0.1337 0.2843 0.0443  -0.1429 -0.0219 76  LYS B CB  
2883 C  CG  . LYS B 76  ? 0.6140 0.2263 0.4322 0.0882  -0.2603 -0.1081 76  LYS B CG  
2884 C  CD  . LYS B 76  ? 1.1418 0.1868 0.3034 0.0993  -0.3240 -0.0126 76  LYS B CD  
2885 C  CE  . LYS B 76  ? 1.2078 0.2605 0.3883 -0.0835 -0.3756 -0.0021 76  LYS B CE  
2886 N  NZ  . LYS B 76  ? 0.5953 0.3515 0.4237 -0.0189 -0.1978 0.0187  76  LYS B NZ  
2887 N  N   . ALA B 77  ? 0.3050 0.2865 0.3567 -0.0185 -0.1817 -0.0658 77  ALA B N   
2888 C  CA  . ALA B 77  ? 0.2157 0.2098 0.1981 0.0379  -0.0724 -0.0195 77  ALA B CA  
2889 C  C   . ALA B 77  ? 0.1273 0.1911 0.2381 0.0403  -0.0763 0.0165  77  ALA B C   
2890 O  O   . ALA B 77  ? 0.1200 0.3652 0.3070 0.0254  -0.0604 0.1123  77  ALA B O   
2891 C  CB  . ALA B 77  ? 0.2119 0.2526 0.1861 0.0143  -0.0736 -0.0034 77  ALA B CB  
2892 N  N   . VAL B 78  ? 0.1872 0.1555 0.2060 0.0379  -0.0684 -0.0225 78  VAL B N   
2893 C  CA  . VAL B 78  ? 0.1765 0.1254 0.2190 -0.0088 -0.0942 -0.0207 78  VAL B CA  
2894 C  C   . VAL B 78  ? 0.1061 0.1421 0.2367 -0.0060 -0.0353 -0.0065 78  VAL B C   
2895 O  O   . VAL B 78  ? 0.1552 0.1611 0.2685 0.0333  -0.0712 -0.0205 78  VAL B O   
2896 C  CB  . VAL B 78  ? 0.3813 0.1489 0.2644 -0.0346 -0.0562 0.0062  78  VAL B CB  
2897 C  CG1 . VAL B 78  ? 0.4729 0.1340 0.3652 -0.0223 -0.1207 -0.0449 78  VAL B CG1 
2898 C  CG2 . VAL B 78  ? 0.3314 0.2366 0.3309 0.0085  -0.0395 -0.0178 78  VAL B CG2 
2899 N  N   . LEU B 79  ? 0.1209 0.1234 0.1963 0.0093  -0.0205 -0.0198 79  LEU B N   
2900 C  CA  . LEU B 79  ? 0.1322 0.1252 0.1713 0.0059  -0.0250 -0.0251 79  LEU B CA  
2901 C  C   . LEU B 79  ? 0.1396 0.1562 0.1805 0.0384  0.0074  -0.0102 79  LEU B C   
2902 O  O   . LEU B 79  ? 0.1683 0.1705 0.1802 0.0375  0.0183  0.0232  79  LEU B O   
2903 C  CB  . LEU B 79  ? 0.1534 0.1460 0.2071 -0.0020 -0.0348 -0.0227 79  LEU B CB  
2904 C  CG  . LEU B 79  ? 0.1459 0.1342 0.2071 -0.0183 -0.0229 -0.0211 79  LEU B CG  
2905 C  CD1 . LEU B 79  ? 0.1572 0.1457 0.4259 0.0390  0.0351  -0.0723 79  LEU B CD1 
2906 C  CD2 . LEU B 79  ? 0.1459 0.1509 0.1778 -0.0110 0.0013  -0.0115 79  LEU B CD2 
2907 N  N   . LYS B 80  ? 0.1507 0.1768 0.1755 0.0254  0.0063  0.0124  80  LYS B N   
2908 C  CA  . LYS B 80  ? 0.1435 0.1653 0.2075 -0.0082 0.0019  -0.0187 80  LYS B CA  
2909 C  C   . LYS B 80  ? 0.1086 0.1751 0.2257 -0.0038 0.0286  0.0013  80  LYS B C   
2910 O  O   . LYS B 80  ? 0.1306 0.1602 0.2214 0.0126  -0.0049 -0.0107 80  LYS B O   
2911 C  CB  . LYS B 80  ? 0.2112 0.1847 0.2405 -0.0208 -0.0060 -0.0159 80  LYS B CB  
2912 C  CG  . LYS B 80  ? 0.1643 0.1741 0.3116 -0.0137 -0.0125 -0.0153 80  LYS B CG  
2913 C  CD  . LYS B 80  ? 0.1841 0.1783 0.4950 -0.0142 0.0286  -0.1096 80  LYS B CD  
2914 C  CE  . LYS B 80  ? 0.3731 0.3619 0.5809 0.1949  0.1053  -0.0225 80  LYS B CE  
2915 N  NZ  . LYS B 80  ? 0.8198 0.8177 1.1322 -0.2849 -0.1059 0.2373  80  LYS B NZ  
2916 N  N   . GLY B 81  ? 0.1641 0.2026 0.1895 -0.0031 0.0485  -0.0065 81  GLY B N   
2917 C  CA  . GLY B 81  ? 0.1408 0.2274 0.2294 -0.0368 0.0734  -0.0421 81  GLY B CA  
2918 C  C   . GLY B 81  ? 0.1347 0.1880 0.2414 -0.0333 0.0670  -0.0439 81  GLY B C   
2919 O  O   . GLY B 81  ? 0.1520 0.1554 0.2116 0.0063  0.0392  0.0063  81  GLY B O   
2920 N  N   . GLY B 82  ? 0.1367 0.1958 0.3476 0.0121  0.0485  -0.0590 82  GLY B N   
2921 C  CA  . GLY B 82  ? 0.1857 0.1543 0.3589 0.0251  -0.0013 -0.0485 82  GLY B CA  
2922 C  C   . GLY B 82  ? 0.1606 0.1659 0.2967 -0.0186 0.0372  -0.0252 82  GLY B C   
2923 O  O   . GLY B 82  ? 0.1888 0.3691 0.2953 -0.0790 0.0810  -0.0491 82  GLY B O   
2924 N  N   . PRO B 83  ? 0.1557 0.1545 0.2360 -0.0253 0.0136  -0.0394 83  PRO B N   
2925 C  CA  . PRO B 83  ? 0.1777 0.1843 0.1916 -0.0557 -0.0010 -0.0063 83  PRO B CA  
2926 C  C   . PRO B 83  ? 0.1636 0.2412 0.1990 -0.0461 -0.0188 0.0280  83  PRO B C   
2927 O  O   . PRO B 83  ? 0.2050 0.2268 0.2033 -0.0467 -0.0524 -0.0135 83  PRO B O   
2928 C  CB  . PRO B 83  ? 0.1879 0.2302 0.2081 -0.0593 -0.0357 0.0041  83  PRO B CB  
2929 C  CG  . PRO B 83  ? 0.1562 0.1543 0.1920 -0.0121 0.0015  -0.0306 83  PRO B CG  
2930 C  CD  . PRO B 83  ? 0.1507 0.1374 0.2520 -0.0081 0.0306  0.0175  83  PRO B CD  
2931 N  N   . LEU B 84  ? 0.1509 0.1478 0.1961 -0.0258 0.0087  0.0006  84  LEU B N   
2932 C  CA  . LEU B 84  ? 0.1464 0.1243 0.1826 -0.0188 0.0071  0.0297  84  LEU B CA  
2933 C  C   . LEU B 84  ? 0.1548 0.1642 0.2168 -0.0379 -0.0005 0.0432  84  LEU B C   
2934 O  O   . LEU B 84  ? 0.1945 0.1798 0.2773 -0.0436 0.0463  0.0636  84  LEU B O   
2935 C  CB  . LEU B 84  ? 0.1419 0.1184 0.1947 -0.0241 0.0241  0.0046  84  LEU B CB  
2936 C  CG  . LEU B 84  ? 0.1246 0.1017 0.1719 -0.0164 0.0241  0.0124  84  LEU B CG  
2937 C  CD1 . LEU B 84  ? 0.1435 0.1647 0.1961 0.0057  0.0054  0.0221  84  LEU B CD1 
2938 C  CD2 . LEU B 84  ? 0.1270 0.1207 0.1744 -0.0207 0.0225  0.0063  84  LEU B CD2 
2939 N  N   A ASP B 85  ? 0.2349 0.1395 0.2313 -0.0355 -0.0463 0.0772  85  ASP B N   
2940 N  N   B ASP B 85  ? 0.2278 0.1462 0.2251 -0.0296 -0.0485 0.0852  85  ASP B N   
2941 C  CA  A ASP B 85  ? 0.3149 0.1349 0.2962 -0.0315 0.0046  0.0778  85  ASP B CA  
2942 C  CA  B ASP B 85  ? 0.2766 0.1194 0.2698 0.0068  0.0057  0.0728  85  ASP B CA  
2943 C  C   A ASP B 85  ? 0.3467 0.1992 0.3506 0.0208  -0.0842 0.0273  85  ASP B C   
2944 C  C   B ASP B 85  ? 0.2292 0.0889 0.3068 0.0109  0.0586  0.0300  85  ASP B C   
2945 O  O   A ASP B 85  ? 0.2781 0.2250 0.3375 -0.0080 -0.0183 0.0527  85  ASP B O   
2946 O  O   B ASP B 85  ? 0.2049 0.1742 0.3018 -0.0159 0.0560  0.0732  85  ASP B O   
2947 C  CB  A ASP B 85  ? 0.4611 0.1112 0.3271 -0.0714 -0.1307 0.0559  85  ASP B CB  
2948 C  CB  B ASP B 85  ? 0.3262 0.2238 0.3212 -0.0368 -0.0155 0.1484  85  ASP B CB  
2949 C  CG  A ASP B 85  ? 0.4973 0.3508 0.4034 -0.2852 0.0368  0.0502  85  ASP B CG  
2950 C  CG  B ASP B 85  ? 0.5360 0.4429 0.4165 -0.0895 0.0035  0.0093  85  ASP B CG  
2951 O  OD1 A ASP B 85  ? 0.4793 0.5550 0.4548 0.0401  -0.0228 -0.3036 85  ASP B OD1 
2952 O  OD1 B ASP B 85  ? 0.5924 0.7652 0.1625 0.0666  -0.0129 0.0666  85  ASP B OD1 
2953 O  OD2 A ASP B 85  ? 0.4397 0.7057 0.7429 -0.2088 0.0035  -0.1158 85  ASP B OD2 
2954 O  OD2 B ASP B 85  ? 0.5074 0.5928 0.6700 0.1872  0.0049  -0.0282 85  ASP B OD2 
2955 N  N   A GLY B 86  ? 0.3244 0.2495 0.3203 0.0628  -0.0238 -0.0146 86  GLY B N   
2956 N  N   B GLY B 86  ? 0.2795 0.1316 0.3097 0.0597  -0.0910 -0.0472 86  GLY B N   
2957 C  CA  A GLY B 86  ? 0.4483 0.3145 0.1814 0.1280  -0.0143 -0.0288 86  GLY B CA  
2958 C  CA  B GLY B 86  ? 0.3145 0.1625 0.2168 0.0681  0.0373  0.0178  86  GLY B CA  
2959 C  C   A GLY B 86  ? 0.2170 0.2903 0.2425 0.1362  -0.0159 -0.0241 86  GLY B C   
2960 C  C   B GLY B 86  ? 0.2703 0.2475 0.2137 0.0857  -0.0408 0.0175  86  GLY B C   
2961 O  O   A GLY B 86  ? 0.3840 0.3398 0.2709 0.2292  0.0102  0.0130  86  GLY B O   
2962 O  O   B GLY B 86  ? 0.3422 0.3880 0.2933 0.2299  -0.0137 -0.0559 86  GLY B O   
2963 N  N   A THR B 87  ? 0.1817 0.1338 0.2175 -0.0035 0.0038  0.0353  87  THR B N   
2964 N  N   B THR B 87  ? 0.1839 0.1360 0.2226 -0.0060 0.0021  0.0384  87  THR B N   
2965 C  CA  A THR B 87  ? 0.1333 0.1645 0.2231 -0.0441 -0.0132 0.0322  87  THR B CA  
2966 C  CA  B THR B 87  ? 0.1468 0.2047 0.2317 -0.0293 -0.0174 0.0322  87  THR B CA  
2967 C  C   A THR B 87  ? 0.1207 0.1146 0.2044 -0.0015 -0.0162 0.0203  87  THR B C   
2968 C  C   B THR B 87  ? 0.1301 0.1097 0.2110 0.0000  -0.0189 0.0192  87  THR B C   
2969 O  O   A THR B 87  ? 0.1588 0.1005 0.2257 0.0130  0.0144  0.0359  87  THR B O   
2970 O  O   B THR B 87  ? 0.1602 0.1004 0.2256 0.0131  0.0116  0.0335  87  THR B O   
2971 C  CB  A THR B 87  ? 0.1326 0.1624 0.2306 -0.0417 -0.0031 0.0293  87  THR B CB  
2972 C  CB  B THR B 87  ? 0.2277 0.2876 0.2527 -0.1014 -0.0263 0.0425  87  THR B CB  
2973 O  OG1 A THR B 87  ? 0.1898 0.1316 0.1940 -0.0259 0.0293  -0.0137 87  THR B OG1 
2974 O  OG1 B THR B 87  ? 0.2811 0.2976 0.3409 -0.0692 0.0359  0.0904  87  THR B OG1 
2975 C  CG2 A THR B 87  ? 0.0968 0.2958 0.2689 -0.1283 -0.0542 0.0643  87  THR B CG2 
2976 C  CG2 B THR B 87  ? 0.1994 0.3192 0.2870 0.0076  -0.0646 0.0705  87  THR B CG2 
2977 N  N   . TYR B 88  ? 0.1067 0.1011 0.1777 -0.0057 -0.0105 0.0043  88  TYR B N   
2978 C  CA  . TYR B 88  ? 0.1153 0.1150 0.1507 -0.0010 -0.0030 0.0156  88  TYR B CA  
2979 C  C   . TYR B 88  ? 0.0984 0.1207 0.1715 0.0185  -0.0232 0.0038  88  TYR B C   
2980 O  O   . TYR B 88  ? 0.1442 0.1995 0.2006 0.0703  -0.0340 -0.0052 88  TYR B O   
2981 C  CB  . TYR B 88  ? 0.1270 0.0943 0.1579 -0.0086 -0.0041 0.0082  88  TYR B CB  
2982 C  CG  . TYR B 88  ? 0.1189 0.0785 0.1511 0.0102  0.0049  0.0046  88  TYR B CG  
2983 C  CD1 . TYR B 88  ? 0.1641 0.1150 0.1493 -0.0005 0.0040  0.0125  88  TYR B CD1 
2984 C  CD2 . TYR B 88  ? 0.1194 0.0707 0.1416 -0.0107 -0.0071 -0.0035 88  TYR B CD2 
2985 C  CE1 . TYR B 88  ? 0.1132 0.1185 0.1525 -0.0133 0.0161  0.0007  88  TYR B CE1 
2986 C  CE2 . TYR B 88  ? 0.1004 0.0881 0.1426 -0.0082 0.0007  0.0005  88  TYR B CE2 
2987 C  CZ  . TYR B 88  ? 0.1138 0.0854 0.1347 0.0041  0.0024  0.0093  88  TYR B CZ  
2988 O  OH  . TYR B 88  ? 0.1208 0.1110 0.1410 0.0015  -0.0077 0.0251  88  TYR B OH  
2989 N  N   . ARG B 89  ? 0.1160 0.0868 0.1453 -0.0013 -0.0126 0.0198  89  ARG B N   
2990 C  CA  . ARG B 89  ? 0.1279 0.0868 0.1415 -0.0111 -0.0250 -0.0057 89  ARG B CA  
2991 C  C   . ARG B 89  ? 0.1070 0.0697 0.1205 0.0038  -0.0270 -0.0200 89  ARG B C   
2992 O  O   . ARG B 89  ? 0.1074 0.0728 0.1274 0.0000  -0.0241 -0.0040 89  ARG B O   
2993 C  CB  . ARG B 89  ? 0.2157 0.0641 0.2028 -0.0144 -0.0697 -0.0175 89  ARG B CB  
2994 C  CG  . ARG B 89  ? 0.2310 0.1509 0.2002 0.0324  -0.0395 -0.0370 89  ARG B CG  
2995 C  CD  . ARG B 89  ? 0.2743 0.1369 0.1820 -0.0286 0.0057  -0.0146 89  ARG B CD  
2996 N  NE  . ARG B 89  ? 0.2809 0.1437 0.1925 -0.0001 -0.0015 -0.0425 89  ARG B NE  
2997 C  CZ  . ARG B 89  ? 0.2276 0.1229 0.2089 0.0172  -0.0093 0.0148  89  ARG B CZ  
2998 N  NH1 . ARG B 89  ? 0.2454 0.1565 0.3041 -0.0107 0.0513  -0.0718 89  ARG B NH1 
2999 N  NH2 . ARG B 89  ? 0.2806 0.1336 0.2328 -0.0222 -0.0163 -0.0241 89  ARG B NH2 
3000 N  N   . LEU B 90  ? 0.1117 0.0932 0.1178 0.0199  -0.0273 -0.0087 90  LEU B N   
3001 C  CA  . LEU B 90  ? 0.1318 0.0825 0.1174 0.0168  -0.0223 -0.0006 90  LEU B CA  
3002 C  C   . LEU B 90  ? 0.1406 0.0873 0.1065 0.0073  -0.0364 -0.0115 90  LEU B C   
3003 O  O   . LEU B 90  ? 0.1455 0.1174 0.1381 -0.0048 -0.0232 -0.0428 90  LEU B O   
3004 C  CB  . LEU B 90  ? 0.1279 0.1056 0.1299 0.0168  -0.0258 -0.0098 90  LEU B CB  
3005 C  CG  . LEU B 90  ? 0.1426 0.0961 0.1405 0.0176  -0.0355 -0.0037 90  LEU B CG  
3006 C  CD1 . LEU B 90  ? 0.2028 0.0852 0.1467 0.0024  -0.0388 -0.0020 90  LEU B CD1 
3007 C  CD2 . LEU B 90  ? 0.1837 0.1555 0.1809 0.0434  -0.0454 0.0275  90  LEU B CD2 
3008 N  N   . ILE B 91  ? 0.1430 0.0718 0.1194 -0.0078 -0.0102 -0.0177 91  ILE B N   
3009 C  CA  . ILE B 91  ? 0.1449 0.0772 0.1141 0.0127  -0.0015 -0.0046 91  ILE B CA  
3010 C  C   . ILE B 91  ? 0.1530 0.0698 0.1135 0.0063  -0.0104 -0.0148 91  ILE B C   
3011 O  O   . ILE B 91  ? 0.1652 0.0797 0.1027 0.0216  -0.0118 -0.0097 91  ILE B O   
3012 C  CB  . ILE B 91  ? 0.1589 0.0878 0.1159 0.0186  -0.0054 -0.0160 91  ILE B CB  
3013 C  CG1 . ILE B 91  ? 0.2073 0.1483 0.1389 0.0781  -0.0010 0.0019  91  ILE B CG1 
3014 C  CG2 . ILE B 91  ? 0.1924 0.0837 0.1308 0.0217  -0.0136 -0.0238 91  ILE B CG2 
3015 C  CD1 . ILE B 91  ? 0.2213 0.1810 0.1665 0.0917  -0.0055 0.0132  91  ILE B CD1 
3016 N  N   . GLN B 92  ? 0.1369 0.0742 0.1047 0.0091  -0.0175 -0.0155 92  GLN B N   
3017 C  CA  . GLN B 92  ? 0.1758 0.0579 0.1097 -0.0049 -0.0066 -0.0146 92  GLN B CA  
3018 C  C   . GLN B 92  ? 0.1523 0.0649 0.1001 0.0098  -0.0060 -0.0092 92  GLN B C   
3019 O  O   . GLN B 92  ? 0.1608 0.0745 0.0965 0.0108  -0.0083 -0.0074 92  GLN B O   
3020 C  CB  . GLN B 92  ? 0.1880 0.0950 0.1230 -0.0007 -0.0019 -0.0208 92  GLN B CB  
3021 C  CG  . GLN B 92  ? 0.1897 0.0777 0.1584 0.0251  -0.0129 -0.0252 92  GLN B CG  
3022 C  CD  . GLN B 92  ? 0.1739 0.0956 0.1439 0.0087  0.0038  -0.0296 92  GLN B CD  
3023 O  OE1 . GLN B 92  ? 0.1965 0.0962 0.1344 0.0038  -0.0152 -0.0172 92  GLN B OE1 
3024 N  NE2 . GLN B 92  ? 0.1814 0.1431 0.2046 0.0168  0.0220  -0.0194 92  GLN B NE2 
3025 N  N   . PHE B 93  ? 0.1758 0.0543 0.0916 0.0070  -0.0143 -0.0110 93  PHE B N   
3026 C  CA  . PHE B 93  ? 0.1660 0.0553 0.1029 0.0125  -0.0092 -0.0035 93  PHE B CA  
3027 C  C   . PHE B 93  ? 0.1399 0.0653 0.0980 0.0066  -0.0208 -0.0175 93  PHE B C   
3028 O  O   . PHE B 93  ? 0.2195 0.0825 0.0948 0.0041  -0.0197 -0.0113 93  PHE B O   
3029 C  CB  . PHE B 93  ? 0.1588 0.0798 0.1027 0.0189  -0.0368 -0.0131 93  PHE B CB  
3030 C  CG  . PHE B 93  ? 0.1566 0.0804 0.1092 0.0099  -0.0559 -0.0100 93  PHE B CG  
3031 C  CD1 . PHE B 93  ? 0.2175 0.0935 0.1092 0.0219  -0.0362 0.0023  93  PHE B CD1 
3032 C  CD2 . PHE B 93  ? 0.1760 0.1086 0.1441 -0.0060 -0.0841 -0.0318 93  PHE B CD2 
3033 C  CE1 . PHE B 93  ? 0.2296 0.0777 0.1239 -0.0080 -0.0661 -0.0032 93  PHE B CE1 
3034 C  CE2 . PHE B 93  ? 0.2605 0.1006 0.1460 -0.0060 -0.0734 0.0138  93  PHE B CE2 
3035 C  CZ  . PHE B 93  ? 0.2671 0.0826 0.1482 -0.0240 -0.0910 -0.0076 93  PHE B CZ  
3036 N  N   . HIS B 94  ? 0.1477 0.0648 0.0964 0.0027  -0.0293 -0.0115 94  HIS B N   
3037 C  CA  . HIS B 94  ? 0.1297 0.0847 0.0860 0.0013  -0.0120 -0.0127 94  HIS B CA  
3038 C  C   . HIS B 94  ? 0.1106 0.0777 0.0746 0.0098  -0.0315 -0.0065 94  HIS B C   
3039 O  O   . HIS B 94  ? 0.1458 0.0772 0.0837 0.0013  -0.0062 -0.0132 94  HIS B O   
3040 C  CB  . HIS B 94  ? 0.1246 0.0879 0.0995 0.0013  -0.0092 -0.0109 94  HIS B CB  
3041 C  CG  . HIS B 94  ? 0.1523 0.0848 0.0749 0.0115  0.0068  -0.0028 94  HIS B CG  
3042 N  ND1 . HIS B 94  ? 0.1410 0.0874 0.0872 0.0163  -0.0049 0.0043  94  HIS B ND1 
3043 C  CD2 . HIS B 94  ? 0.1072 0.0886 0.0834 0.0244  -0.0153 -0.0030 94  HIS B CD2 
3044 C  CE1 . HIS B 94  ? 0.1106 0.0781 0.1070 0.0098  -0.0074 -0.0066 94  HIS B CE1 
3045 N  NE2 . HIS B 94  ? 0.1067 0.0771 0.0975 0.0120  -0.0120 -0.0032 94  HIS B NE2 
3046 N  N   . PHE B 95  ? 0.1388 0.0644 0.1035 0.0206  -0.0001 -0.0028 95  PHE B N   
3047 C  CA  . PHE B 95  ? 0.1020 0.0636 0.1119 0.0082  -0.0006 -0.0049 95  PHE B CA  
3048 C  C   . PHE B 95  ? 0.1228 0.0658 0.0959 0.0248  0.0077  0.0147  95  PHE B C   
3049 O  O   . PHE B 95  ? 0.1169 0.0935 0.1093 0.0199  0.0000  -0.0006 95  PHE B O   
3050 C  CB  . PHE B 95  ? 0.1327 0.0870 0.0954 0.0070  -0.0253 0.0001  95  PHE B CB  
3051 C  CG  . PHE B 95  ? 0.1410 0.0716 0.0989 0.0142  -0.0275 0.0043  95  PHE B CG  
3052 C  CD1 . PHE B 95  ? 0.1665 0.0771 0.1013 0.0049  -0.0296 0.0059  95  PHE B CD1 
3053 C  CD2 . PHE B 95  ? 0.1386 0.0909 0.1160 0.0247  -0.0259 0.0115  95  PHE B CD2 
3054 C  CE1 . PHE B 95  ? 0.1489 0.0979 0.1004 0.0125  -0.0286 0.0035  95  PHE B CE1 
3055 C  CE2 . PHE B 95  ? 0.1553 0.0864 0.1191 0.0107  -0.0249 0.0217  95  PHE B CE2 
3056 C  CZ  . PHE B 95  ? 0.1349 0.0993 0.1214 0.0081  -0.0258 0.0190  95  PHE B CZ  
3057 N  N   . HIS B 96  ? 0.1322 0.0690 0.0859 0.0137  -0.0108 0.0052  96  HIS B N   
3058 C  CA  . HIS B 96  ? 0.1102 0.0706 0.1011 0.0046  -0.0110 0.0057  96  HIS B CA  
3059 C  C   . HIS B 96  ? 0.1054 0.0799 0.0883 0.0098  0.0074  0.0068  96  HIS B C   
3060 O  O   . HIS B 96  ? 0.1074 0.0762 0.1029 0.0046  0.0110  0.0021  96  HIS B O   
3061 C  CB  . HIS B 96  ? 0.1184 0.0762 0.1047 0.0052  -0.0189 0.0141  96  HIS B CB  
3062 C  CG  . HIS B 96  ? 0.1228 0.0954 0.0986 0.0165  -0.0024 0.0193  96  HIS B CG  
3063 N  ND1 . HIS B 96  ? 0.1045 0.0715 0.1484 -0.0027 -0.0116 0.0068  96  HIS B ND1 
3064 C  CD2 . HIS B 96  ? 0.1151 0.0643 0.1004 0.0097  -0.0065 0.0043  96  HIS B CD2 
3065 C  CE1 . HIS B 96  ? 0.1182 0.0759 0.1340 0.0028  -0.0013 0.0197  96  HIS B CE1 
3066 N  NE2 . HIS B 96  ? 0.1017 0.0864 0.1040 0.0168  -0.0040 -0.0074 96  HIS B NE2 
3067 N  N   . TRP B 97  ? 0.1074 0.0688 0.0870 0.0097  -0.0030 0.0041  97  TRP B N   
3068 C  CA  . TRP B 97  ? 0.1168 0.0707 0.1101 0.0085  0.0015  0.0097  97  TRP B CA  
3069 C  C   . TRP B 97  ? 0.1058 0.0820 0.1022 0.0113  0.0096  0.0215  97  TRP B C   
3070 O  O   . TRP B 97  ? 0.1063 0.0851 0.1264 0.0164  0.0142  0.0113  97  TRP B O   
3071 C  CB  . TRP B 97  ? 0.1376 0.0800 0.0935 0.0157  0.0030  0.0177  97  TRP B CB  
3072 C  CG  . TRP B 97  ? 0.1239 0.0837 0.0926 0.0087  0.0020  0.0023  97  TRP B CG  
3073 C  CD1 . TRP B 97  ? 0.1501 0.1097 0.0984 0.0226  0.0167  0.0190  97  TRP B CD1 
3074 C  CD2 . TRP B 97  ? 0.1552 0.0772 0.0950 0.0205  0.0104  -0.0031 97  TRP B CD2 
3075 N  NE1 . TRP B 97  ? 0.1933 0.0877 0.1004 0.0275  0.0344  0.0149  97  TRP B NE1 
3076 C  CE2 . TRP B 97  ? 0.1590 0.0916 0.0959 0.0166  0.0013  0.0141  97  TRP B CE2 
3077 C  CE3 . TRP B 97  ? 0.1433 0.0861 0.0970 0.0057  -0.0109 0.0070  97  TRP B CE3 
3078 C  CZ2 . TRP B 97  ? 0.1873 0.1068 0.1011 0.0412  0.0222  0.0153  97  TRP B CZ2 
3079 C  CZ3 . TRP B 97  ? 0.1809 0.0856 0.1022 0.0236  -0.0015 -0.0017 97  TRP B CZ3 
3080 C  CH2 . TRP B 97  ? 0.2046 0.0822 0.1022 0.0253  0.0021  0.0078  97  TRP B CH2 
3081 N  N   . GLY B 98  ? 0.1331 0.0634 0.1119 0.0020  -0.0003 0.0127  98  GLY B N   
3082 C  CA  . GLY B 98  ? 0.1344 0.0804 0.1146 -0.0078 0.0097  0.0065  98  GLY B CA  
3083 C  C   . GLY B 98  ? 0.1347 0.0873 0.1398 0.0197  -0.0065 0.0186  98  GLY B C   
3084 O  O   . GLY B 98  ? 0.1446 0.0930 0.1347 0.0129  0.0035  0.0217  98  GLY B O   
3085 N  N   . SER B 99  ? 0.1466 0.1061 0.1512 -0.0006 0.0102  0.0430  99  SER B N   
3086 C  CA  . SER B 99  ? 0.1638 0.0945 0.1755 0.0168  0.0348  0.0425  99  SER B CA  
3087 C  C   . SER B 99  ? 0.1805 0.0932 0.1777 -0.0017 0.0052  0.0465  99  SER B C   
3088 O  O   . SER B 99  ? 0.2312 0.1266 0.1801 0.0088  0.0065  0.0500  99  SER B O   
3089 C  CB  . SER B 99  ? 0.1827 0.1340 0.1977 0.0070  0.0277  0.0652  99  SER B CB  
3090 O  OG  . SER B 99  ? 0.1374 0.1263 0.2333 -0.0068 0.0227  0.0421  99  SER B OG  
3091 N  N   . LEU B 100 ? 0.1214 0.1282 0.1854 0.0083  0.0125  0.0438  100 LEU B N   
3092 C  CA  . LEU B 100 ? 0.1586 0.0737 0.2139 -0.0094 0.0286  0.0185  100 LEU B CA  
3093 C  C   . LEU B 100 ? 0.1595 0.0989 0.1617 0.0115  0.0077  0.0165  100 LEU B C   
3094 O  O   . LEU B 100 ? 0.1581 0.0930 0.1769 0.0109  0.0099  0.0284  100 LEU B O   
3095 C  CB  . LEU B 100 ? 0.2092 0.1819 0.3643 -0.0645 0.0449  -0.0584 100 LEU B CB  
3096 C  CG  . LEU B 100 ? 0.2042 0.2378 0.3639 -0.0877 -0.0255 -0.0474 100 LEU B CG  
3097 C  CD1 . LEU B 100 ? 0.2777 0.4771 0.3858 -0.2400 -0.0282 0.0247  100 LEU B CD1 
3098 C  CD2 . LEU B 100 ? 0.4702 0.1803 0.4230 -0.0582 0.2126  0.0527  100 LEU B CD2 
3099 N  N   . ASP B 101 ? 0.1468 0.1063 0.1850 0.0099  0.0099  0.0114  101 ASP B N   
3100 C  CA  . ASP B 101 ? 0.1456 0.1146 0.1895 0.0243  0.0006  -0.0115 101 ASP B CA  
3101 C  C   . ASP B 101 ? 0.1387 0.0961 0.1651 -0.0005 0.0086  -0.0109 101 ASP B C   
3102 O  O   . ASP B 101 ? 0.1798 0.1256 0.1766 -0.0222 0.0054  -0.0144 101 ASP B O   
3103 C  CB  . ASP B 101 ? 0.1496 0.1360 0.2001 0.0397  -0.0348 -0.0298 101 ASP B CB  
3104 C  CG  . ASP B 101 ? 0.1645 0.0993 0.2324 0.0234  -0.0324 -0.0260 101 ASP B CG  
3105 O  OD1 . ASP B 101 ? 0.2001 0.1324 0.1934 0.0227  -0.0041 -0.0175 101 ASP B OD1 
3106 O  OD2 . ASP B 101 ? 0.2342 0.1823 0.2428 0.0798  -0.0623 -0.0174 101 ASP B OD2 
3107 N  N   . GLY B 102 ? 0.1692 0.1022 0.1875 0.0170  -0.0222 -0.0219 102 GLY B N   
3108 C  CA  . GLY B 102 ? 0.1634 0.0781 0.1967 0.0040  -0.0153 -0.0237 102 GLY B CA  
3109 C  C   . GLY B 102 ? 0.1586 0.0903 0.1622 -0.0116 0.0076  -0.0265 102 GLY B C   
3110 O  O   . GLY B 102 ? 0.1717 0.1052 0.1658 -0.0006 0.0074  -0.0303 102 GLY B O   
3111 N  N   . GLN B 103 ? 0.1270 0.0747 0.1577 0.0175  -0.0026 -0.0110 103 GLN B N   
3112 C  CA  . GLN B 103 ? 0.1279 0.0939 0.1173 0.0027  -0.0063 -0.0012 103 GLN B CA  
3113 C  C   . GLN B 103 ? 0.1140 0.0907 0.1153 0.0057  0.0174  0.0080  103 GLN B C   
3114 O  O   . GLN B 103 ? 0.1421 0.0793 0.1268 -0.0024 0.0006  0.0087  103 GLN B O   
3115 C  CB  . GLN B 103 ? 0.1491 0.1058 0.1810 0.0024  0.0168  0.0074  103 GLN B CB  
3116 C  CG  . GLN B 103 ? 0.1255 0.1207 0.1983 -0.0127 0.0298  0.0142  103 GLN B CG  
3117 C  CD  . GLN B 103 ? 0.1613 0.1352 0.2356 -0.0351 0.0476  -0.0414 103 GLN B CD  
3118 O  OE1 . GLN B 103 ? 0.2405 0.3447 0.4120 -0.1730 0.1298  -0.2117 103 GLN B OE1 
3119 N  NE2 . GLN B 103 ? 0.1580 0.1467 0.2478 -0.0264 0.0403  -0.0143 103 GLN B NE2 
3120 N  N   . GLY B 104 ? 0.1080 0.0728 0.1121 -0.0048 0.0065  0.0006  104 GLY B N   
3121 C  CA  . GLY B 104 ? 0.1088 0.0738 0.1185 -0.0070 -0.0073 0.0027  104 GLY B CA  
3122 C  C   . GLY B 104 ? 0.1006 0.0688 0.1217 0.0168  -0.0023 -0.0078 104 GLY B C   
3123 O  O   . GLY B 104 ? 0.1054 0.0917 0.1234 0.0109  0.0051  -0.0136 104 GLY B O   
3124 N  N   . SER B 105 ? 0.0995 0.0837 0.0977 0.0063  0.0024  0.0049  105 SER B N   
3125 C  CA  . SER B 105 ? 0.1035 0.0744 0.1015 0.0167  0.0043  0.0059  105 SER B CA  
3126 C  C   . SER B 105 ? 0.0855 0.0720 0.1014 -0.0043 0.0024  0.0048  105 SER B C   
3127 O  O   . SER B 105 ? 0.1059 0.0794 0.1256 0.0000  -0.0179 0.0105  105 SER B O   
3128 C  CB  . SER B 105 ? 0.0872 0.0732 0.1010 0.0206  -0.0035 -0.0127 105 SER B CB  
3129 O  OG  . SER B 105 ? 0.1022 0.0780 0.1124 0.0071  0.0021  -0.0057 105 SER B OG  
3130 N  N   . GLU B 106 ? 0.0948 0.0767 0.0993 0.0054  -0.0030 0.0120  106 GLU B N   
3131 C  CA  . GLU B 106 ? 0.0974 0.0826 0.1031 0.0173  -0.0063 0.0019  106 GLU B CA  
3132 C  C   . GLU B 106 ? 0.1033 0.0773 0.0991 0.0062  -0.0131 0.0048  106 GLU B C   
3133 O  O   . GLU B 106 ? 0.1018 0.0995 0.1090 -0.0035 -0.0104 0.0098  106 GLU B O   
3134 C  CB  . GLU B 106 ? 0.0776 0.0789 0.1071 0.0137  -0.0065 0.0003  106 GLU B CB  
3135 C  CG  . GLU B 106 ? 0.1476 0.0798 0.1239 0.0231  0.0210  -0.0071 106 GLU B CG  
3136 C  CD  . GLU B 106 ? 0.0850 0.0798 0.1333 0.0000  0.0020  0.0065  106 GLU B CD  
3137 O  OE1 . GLU B 106 ? 0.0824 0.0864 0.1277 0.0153  -0.0003 0.0030  106 GLU B OE1 
3138 O  OE2 . GLU B 106 ? 0.0936 0.1042 0.1453 0.0041  0.0010  0.0131  106 GLU B OE2 
3139 N  N   . HIS B 107 ? 0.1036 0.0644 0.0957 0.0038  -0.0092 -0.0076 107 HIS B N   
3140 C  CA  . HIS B 107 ? 0.0930 0.0718 0.0913 -0.0035 -0.0068 -0.0006 107 HIS B CA  
3141 C  C   . HIS B 107 ? 0.0772 0.0861 0.0941 0.0102  -0.0006 -0.0060 107 HIS B C   
3142 O  O   . HIS B 107 ? 0.0900 0.0885 0.1090 0.0051  -0.0052 0.0001  107 HIS B O   
3143 C  CB  . HIS B 107 ? 0.0961 0.0687 0.1090 0.0003  -0.0102 0.0020  107 HIS B CB  
3144 C  CG  . HIS B 107 ? 0.0838 0.0745 0.1011 -0.0132 -0.0074 0.0000  107 HIS B CG  
3145 N  ND1 . HIS B 107 ? 0.1049 0.0662 0.1004 -0.0003 -0.0116 -0.0015 107 HIS B ND1 
3146 C  CD2 . HIS B 107 ? 0.0627 0.0725 0.1149 -0.0151 -0.0060 -0.0015 107 HIS B CD2 
3147 C  CE1 . HIS B 107 ? 0.0938 0.0773 0.1098 -0.0175 -0.0271 0.0164  107 HIS B CE1 
3148 N  NE2 . HIS B 107 ? 0.0887 0.0838 0.1013 -0.0024 -0.0100 0.0086  107 HIS B NE2 
3149 N  N   . THR B 108 ? 0.0984 0.0746 0.1150 -0.0092 -0.0017 -0.0063 108 THR B N   
3150 C  CA  . THR B 108 ? 0.1212 0.0539 0.1184 -0.0149 -0.0010 -0.0167 108 THR B CA  
3151 C  C   . THR B 108 ? 0.1004 0.0701 0.1026 -0.0148 -0.0135 -0.0122 108 THR B C   
3152 O  O   . THR B 108 ? 0.1151 0.0852 0.1121 -0.0085 -0.0102 -0.0043 108 THR B O   
3153 C  CB  . THR B 108 ? 0.1052 0.1185 0.1205 -0.0244 -0.0182 0.0046  108 THR B CB  
3154 O  OG1 . THR B 108 ? 0.1241 0.1040 0.1273 -0.0094 -0.0259 -0.0013 108 THR B OG1 
3155 C  CG2 . THR B 108 ? 0.1101 0.1428 0.1328 -0.0204 -0.0003 -0.0023 108 THR B CG2 
3156 N  N   . VAL B 109 ? 0.1214 0.0873 0.1123 -0.0017 -0.0074 -0.0171 109 VAL B N   
3157 C  CA  . VAL B 109 ? 0.1425 0.0997 0.1098 0.0160  0.0087  -0.0242 109 VAL B CA  
3158 C  C   . VAL B 109 ? 0.1254 0.0914 0.1146 0.0159  0.0059  -0.0122 109 VAL B C   
3159 O  O   . VAL B 109 ? 0.1205 0.0834 0.1349 0.0000  0.0003  -0.0187 109 VAL B O   
3160 C  CB  . VAL B 109 ? 0.1065 0.1045 0.1507 0.0010  0.0007  -0.0252 109 VAL B CB  
3161 C  CG1 . VAL B 109 ? 0.1218 0.1250 0.1591 0.0167  0.0157  -0.0285 109 VAL B CG1 
3162 C  CG2 . VAL B 109 ? 0.1295 0.1198 0.1404 -0.0071 -0.0214 -0.0340 109 VAL B CG2 
3163 N  N   . ASP B 110 ? 0.1584 0.1038 0.1040 -0.0318 -0.0013 -0.0200 110 ASP B N   
3164 C  CA  . ASP B 110 ? 0.1811 0.0891 0.1272 -0.0291 0.0205  -0.0351 110 ASP B CA  
3165 C  C   . ASP B 110 ? 0.1911 0.0697 0.1235 -0.0209 -0.0027 -0.0177 110 ASP B C   
3166 O  O   . ASP B 110 ? 0.1834 0.0856 0.1493 -0.0162 0.0052  -0.0230 110 ASP B O   
3167 C  CB  . ASP B 110 ? 0.2187 0.1340 0.1566 -0.0237 0.0581  -0.0478 110 ASP B CB  
3168 C  CG  . ASP B 110 ? 0.2260 0.1337 0.1455 -0.0261 0.0441  -0.0549 110 ASP B CG  
3169 O  OD1 . ASP B 110 ? 0.2547 0.1378 0.1923 -0.0320 0.0606  -0.0366 110 ASP B OD1 
3170 O  OD2 . ASP B 110 ? 0.2360 0.2213 0.1981 -0.0401 0.0373  -0.0438 110 ASP B OD2 
3171 N  N   . LYS B 111 ? 0.1500 0.1022 0.1189 -0.0320 -0.0096 -0.0260 111 LYS B N   
3172 C  CA  . LYS B 111 ? 0.1563 0.0929 0.1311 -0.0300 -0.0168 -0.0133 111 LYS B CA  
3173 C  C   . LYS B 111 ? 0.1453 0.0898 0.1207 0.0040  -0.0057 -0.0189 111 LYS B C   
3174 O  O   . LYS B 111 ? 0.1474 0.1365 0.1403 -0.0168 0.0100  0.0091  111 LYS B O   
3175 C  CB  . LYS B 111 ? 0.1699 0.1523 0.1624 -0.0513 -0.0170 -0.0328 111 LYS B CB  
3176 C  CG  . LYS B 111 ? 0.2718 0.1798 0.1782 -0.0772 -0.0557 -0.0071 111 LYS B CG  
3177 C  CD  . LYS B 111 ? 0.2161 0.2527 0.2913 -0.0340 -0.1030 0.0702  111 LYS B CD  
3178 C  CE  . LYS B 111 ? 0.2687 0.2840 0.2462 -0.0603 -0.0982 0.0297  111 LYS B CE  
3179 N  NZ  . LYS B 111 ? 0.2423 0.3395 0.3312 -0.0592 -0.0251 -0.0900 111 LYS B NZ  
3180 N  N   . LYS B 112 ? 0.1417 0.0922 0.1160 -0.0082 -0.0135 -0.0186 112 LYS B N   
3181 C  CA  . LYS B 112 ? 0.1410 0.1164 0.1155 -0.0001 -0.0044 -0.0038 112 LYS B CA  
3182 C  C   . LYS B 112 ? 0.1189 0.0842 0.1237 -0.0094 -0.0041 -0.0082 112 LYS B C   
3183 O  O   . LYS B 112 ? 0.1349 0.0790 0.1149 -0.0082 -0.0071 0.0003  112 LYS B O   
3184 C  CB  . LYS B 112 ? 0.1377 0.1309 0.1412 0.0077  -0.0114 0.0038  112 LYS B CB  
3185 C  CG  . LYS B 112 ? 0.1160 0.1708 0.1547 0.0174  -0.0076 0.0386  112 LYS B CG  
3186 C  CD  . LYS B 112 ? 0.1155 0.2222 0.1861 0.0027  -0.0348 -0.0208 112 LYS B CD  
3187 C  CE  . LYS B 112 ? 0.2163 0.1750 0.2055 0.0226  -0.0597 0.0296  112 LYS B CE  
3188 N  NZ  . LYS B 112 ? 0.1960 0.1446 0.2259 -0.0104 -0.0351 -0.0083 112 LYS B NZ  
3189 N  N   A LYS B 113 ? 0.1255 0.0953 0.1067 -0.0136 -0.0060 -0.0063 113 LYS B N   
3190 N  N   B LYS B 113 ? 0.1248 0.0986 0.1074 -0.0137 -0.0052 -0.0060 113 LYS B N   
3191 C  CA  A LYS B 113 ? 0.1196 0.0961 0.1189 -0.0241 -0.0136 -0.0161 113 LYS B CA  
3192 C  CA  B LYS B 113 ? 0.1223 0.0877 0.1199 -0.0250 -0.0115 -0.0115 113 LYS B CA  
3193 C  C   A LYS B 113 ? 0.1198 0.0636 0.1311 0.0049  -0.0007 -0.0132 113 LYS B C   
3194 C  C   B LYS B 113 ? 0.1212 0.0639 0.1324 0.0049  0.0000  -0.0153 113 LYS B C   
3195 O  O   A LYS B 113 ? 0.1800 0.0555 0.1677 0.0000  -0.0250 -0.0165 113 LYS B O   
3196 O  O   B LYS B 113 ? 0.1832 0.0577 0.1597 -0.0034 -0.0320 -0.0146 113 LYS B O   
3197 C  CB  A LYS B 113 ? 0.1207 0.1151 0.1316 -0.0092 -0.0027 -0.0116 113 LYS B CB  
3198 C  CB  B LYS B 113 ? 0.1226 0.1053 0.1320 -0.0127 -0.0026 -0.0041 113 LYS B CB  
3199 C  CG  A LYS B 113 ? 0.1017 0.1446 0.1430 -0.0159 0.0031  -0.0182 113 LYS B CG  
3200 C  CG  B LYS B 113 ? 0.1092 0.1342 0.1570 -0.0162 -0.0074 -0.0230 113 LYS B CG  
3201 C  CD  A LYS B 113 ? 0.1086 0.1667 0.2087 -0.0307 0.0217  0.0000  113 LYS B CD  
3202 C  CD  B LYS B 113 ? 0.1137 0.1381 0.1911 -0.0443 -0.0212 0.0087  113 LYS B CD  
3203 C  CE  A LYS B 113 ? 0.1295 0.1868 0.2477 -0.0461 -0.0173 0.0013  113 LYS B CE  
3204 C  CE  B LYS B 113 ? 0.1270 0.2373 0.2394 -0.0129 -0.0584 -0.0147 113 LYS B CE  
3205 N  NZ  A LYS B 113 ? 0.0775 0.1791 0.2578 -0.0220 -0.0439 0.0237  113 LYS B NZ  
3206 N  NZ  B LYS B 113 ? 0.1816 0.2177 0.2301 -0.0310 -0.0414 -0.0051 113 LYS B NZ  
3207 N  N   . TYR B 114 ? 0.1056 0.0806 0.1243 0.0082  -0.0071 -0.0087 114 TYR B N   
3208 C  CA  . TYR B 114 ? 0.1094 0.0856 0.1191 -0.0046 -0.0184 -0.0122 114 TYR B CA  
3209 C  C   . TYR B 114 ? 0.0905 0.0599 0.1277 0.0000  -0.0093 -0.0027 114 TYR B C   
3210 O  O   . TYR B 114 ? 0.0926 0.0912 0.1275 0.0052  -0.0012 0.0046  114 TYR B O   
3211 C  CB  . TYR B 114 ? 0.1090 0.0781 0.1221 -0.0038 0.0000  -0.0127 114 TYR B CB  
3212 C  CG  . TYR B 114 ? 0.1101 0.0763 0.1259 -0.0121 -0.0148 -0.0294 114 TYR B CG  
3213 C  CD1 . TYR B 114 ? 0.1448 0.0889 0.1322 -0.0126 0.0037  -0.0250 114 TYR B CD1 
3214 C  CD2 . TYR B 114 ? 0.1011 0.0910 0.1638 0.0060  -0.0027 -0.0170 114 TYR B CD2 
3215 C  CE1 . TYR B 114 ? 0.1895 0.0877 0.1349 -0.0085 0.0044  -0.0359 114 TYR B CE1 
3216 C  CE2 . TYR B 114 ? 0.1275 0.1211 0.1918 0.0013  0.0181  -0.0071 114 TYR B CE2 
3217 C  CZ  . TYR B 114 ? 0.1618 0.1272 0.1730 0.0153  0.0346  -0.0270 114 TYR B CZ  
3218 O  OH  . TYR B 114 ? 0.2116 0.1951 0.2096 -0.0013 0.0822  0.0142  114 TYR B OH  
3219 N  N   . ALA B 115 ? 0.1094 0.0763 0.1105 0.0230  -0.0137 -0.0100 115 ALA B N   
3220 C  CA  . ALA B 115 ? 0.1277 0.0627 0.1196 0.0197  0.0055  0.0008  115 ALA B CA  
3221 C  C   . ALA B 115 ? 0.1124 0.0684 0.1101 0.0138  0.0001  -0.0035 115 ALA B C   
3222 O  O   . ALA B 115 ? 0.1124 0.0772 0.1250 0.0142  0.0114  0.0017  115 ALA B O   
3223 C  CB  . ALA B 115 ? 0.1593 0.0945 0.1270 0.0386  -0.0122 -0.0057 115 ALA B CB  
3224 N  N   . ALA B 116 ? 0.1050 0.0561 0.1132 -0.0035 -0.0066 -0.0076 116 ALA B N   
3225 C  CA  . ALA B 116 ? 0.1120 0.0634 0.1027 0.0074  -0.0023 -0.0031 116 ALA B CA  
3226 C  C   . ALA B 116 ? 0.0905 0.0643 0.1011 0.0054  -0.0054 -0.0102 116 ALA B C   
3227 O  O   . ALA B 116 ? 0.1002 0.0727 0.1027 0.0133  -0.0030 -0.0074 116 ALA B O   
3228 C  CB  . ALA B 116 ? 0.1365 0.0904 0.1027 0.0055  -0.0071 0.0015  116 ALA B CB  
3229 N  N   . GLU B 117 ? 0.1184 0.0520 0.1038 0.0015  -0.0098 -0.0021 117 GLU B N   
3230 C  CA  . GLU B 117 ? 0.0938 0.0573 0.1040 0.0041  -0.0131 -0.0054 117 GLU B CA  
3231 C  C   . GLU B 117 ? 0.1044 0.0772 0.0788 0.0023  -0.0082 -0.0020 117 GLU B C   
3232 O  O   . GLU B 117 ? 0.1098 0.0873 0.1121 0.0019  0.0155  -0.0149 117 GLU B O   
3233 C  CB  . GLU B 117 ? 0.1067 0.0873 0.0966 0.0028  -0.0073 0.0062  117 GLU B CB  
3234 C  CG  . GLU B 117 ? 0.1173 0.0925 0.1006 -0.0017 -0.0182 0.0023  117 GLU B CG  
3235 C  CD  . GLU B 117 ? 0.0952 0.0663 0.0996 0.0065  -0.0035 -0.0048 117 GLU B CD  
3236 O  OE1 . GLU B 117 ? 0.1059 0.0944 0.1108 -0.0060 -0.0126 -0.0034 117 GLU B OE1 
3237 O  OE2 . GLU B 117 ? 0.1035 0.0873 0.1022 0.0003  -0.0228 0.0026  117 GLU B OE2 
3238 N  N   . LEU B 118 ? 0.1031 0.0593 0.0923 0.0015  -0.0187 0.0005  118 LEU B N   
3239 C  CA  . LEU B 118 ? 0.1088 0.0537 0.0932 0.0043  -0.0174 -0.0031 118 LEU B CA  
3240 C  C   . LEU B 118 ? 0.1062 0.0623 0.0887 0.0080  -0.0157 -0.0040 118 LEU B C   
3241 O  O   . LEU B 118 ? 0.0905 0.0672 0.0918 0.0087  -0.0088 -0.0043 118 LEU B O   
3242 C  CB  . LEU B 118 ? 0.1178 0.0666 0.1153 0.0120  -0.0182 -0.0093 118 LEU B CB  
3243 C  CG  . LEU B 118 ? 0.1094 0.0806 0.1189 -0.0015 -0.0294 -0.0166 118 LEU B CG  
3244 C  CD1 . LEU B 118 ? 0.1787 0.0776 0.1067 0.0030  -0.0425 -0.0300 118 LEU B CD1 
3245 C  CD2 . LEU B 118 ? 0.1137 0.1327 0.1444 0.0102  -0.0483 -0.0174 118 LEU B CD2 
3246 N  N   . HIS B 119 ? 0.1189 0.0476 0.0852 0.0046  -0.0166 -0.0065 119 HIS B N   
3247 C  CA  . HIS B 119 ? 0.1020 0.0626 0.0877 0.0012  -0.0126 -0.0024 119 HIS B CA  
3248 C  C   . HIS B 119 ? 0.1004 0.0579 0.0913 0.0137  -0.0147 -0.0186 119 HIS B C   
3249 O  O   . HIS B 119 ? 0.1329 0.0656 0.0898 0.0026  -0.0046 -0.0051 119 HIS B O   
3250 C  CB  . HIS B 119 ? 0.0944 0.0749 0.1020 -0.0140 -0.0196 -0.0057 119 HIS B CB  
3251 C  CG  . HIS B 119 ? 0.0977 0.0676 0.0808 -0.0008 -0.0115 0.0049  119 HIS B CG  
3252 N  ND1 . HIS B 119 ? 0.0802 0.0727 0.0977 0.0015  -0.0031 -0.0103 119 HIS B ND1 
3253 C  CD2 . HIS B 119 ? 0.0850 0.0821 0.0968 0.0035  -0.0248 -0.0003 119 HIS B CD2 
3254 C  CE1 . HIS B 119 ? 0.0943 0.0873 0.0843 0.0046  -0.0086 0.0021  119 HIS B CE1 
3255 N  NE2 . HIS B 119 ? 0.0847 0.0839 0.0950 0.0024  -0.0156 -0.0032 119 HIS B NE2 
3256 N  N   . LEU B 120 ? 0.0820 0.0597 0.0956 0.0017  -0.0124 -0.0041 120 LEU B N   
3257 C  CA  . LEU B 120 ? 0.0979 0.0606 0.1099 0.0059  -0.0311 -0.0174 120 LEU B CA  
3258 C  C   . LEU B 120 ? 0.0754 0.0645 0.0916 -0.0013 -0.0125 -0.0183 120 LEU B C   
3259 O  O   . LEU B 120 ? 0.0950 0.0768 0.0921 0.0143  -0.0071 -0.0071 120 LEU B O   
3260 C  CB  . LEU B 120 ? 0.0891 0.0797 0.1259 0.0109  -0.0231 0.0052  120 LEU B CB  
3261 C  CG  . LEU B 120 ? 0.1374 0.0970 0.1254 0.0209  -0.0395 -0.0037 120 LEU B CG  
3262 C  CD1 . LEU B 120 ? 0.1922 0.1264 0.1615 0.0702  -0.0287 0.0020  120 LEU B CD1 
3263 C  CD2 . LEU B 120 ? 0.1676 0.1424 0.1422 -0.0070 -0.0654 0.0183  120 LEU B CD2 
3264 N  N   . VAL B 121 ? 0.0939 0.0658 0.0961 0.0107  -0.0119 -0.0133 121 VAL B N   
3265 C  CA  . VAL B 121 ? 0.1119 0.0599 0.1089 0.0148  -0.0120 -0.0060 121 VAL B CA  
3266 C  C   . VAL B 121 ? 0.1040 0.0683 0.1024 0.0081  -0.0057 0.0074  121 VAL B C   
3267 O  O   . VAL B 121 ? 0.1326 0.0741 0.0980 0.0052  -0.0103 -0.0046 121 VAL B O   
3268 C  CB  . VAL B 121 ? 0.1047 0.0578 0.1198 0.0083  -0.0099 -0.0012 121 VAL B CB  
3269 C  CG1 . VAL B 121 ? 0.1178 0.0877 0.1361 0.0208  0.0021  0.0027  121 VAL B CG1 
3270 C  CG2 . VAL B 121 ? 0.1207 0.0788 0.1189 -0.0104 -0.0097 0.0063  121 VAL B CG2 
3271 N  N   . HIS B 122 ? 0.1049 0.0559 0.0995 0.0086  -0.0115 0.0060  122 HIS B N   
3272 C  CA  . HIS B 122 ? 0.1029 0.0546 0.1174 0.0057  -0.0046 0.0032  122 HIS B CA  
3273 C  C   . HIS B 122 ? 0.0910 0.0681 0.1092 -0.0035 -0.0111 -0.0085 122 HIS B C   
3274 O  O   . HIS B 122 ? 0.1164 0.0788 0.1193 0.0142  -0.0198 -0.0007 122 HIS B O   
3275 C  CB  . HIS B 122 ? 0.1084 0.0645 0.1380 0.0098  -0.0138 0.0031  122 HIS B CB  
3276 C  CG  . HIS B 122 ? 0.1006 0.0724 0.1020 0.0127  -0.0135 -0.0076 122 HIS B CG  
3277 N  ND1 . HIS B 122 ? 0.1031 0.0632 0.1237 0.0118  -0.0051 -0.0124 122 HIS B ND1 
3278 C  CD2 . HIS B 122 ? 0.1056 0.0859 0.1360 0.0063  -0.0218 -0.0028 122 HIS B CD2 
3279 C  CE1 . HIS B 122 ? 0.0832 0.1180 0.1235 -0.0006 -0.0060 -0.0020 122 HIS B CE1 
3280 N  NE2 . HIS B 122 ? 0.0988 0.0966 0.1385 0.0175  -0.0194 -0.0024 122 HIS B NE2 
3281 N  N   . TRP B 123 ? 0.1079 0.0599 0.1150 0.0153  -0.0104 0.0057  123 TRP B N   
3282 C  CA  . TRP B 123 ? 0.1289 0.0632 0.1071 0.0074  -0.0093 0.0035  123 TRP B CA  
3283 C  C   . TRP B 123 ? 0.0926 0.0772 0.1202 0.0193  -0.0054 -0.0007 123 TRP B C   
3284 O  O   . TRP B 123 ? 0.0998 0.0756 0.1482 0.0041  -0.0178 0.0122  123 TRP B O   
3285 C  CB  . TRP B 123 ? 0.1422 0.1083 0.1246 0.0263  -0.0111 -0.0001 123 TRP B CB  
3286 C  CG  . TRP B 123 ? 0.1518 0.0844 0.1307 0.0249  -0.0015 -0.0060 123 TRP B CG  
3287 C  CD1 . TRP B 123 ? 0.1738 0.1014 0.1180 0.0408  -0.0068 -0.0120 123 TRP B CD1 
3288 C  CD2 . TRP B 123 ? 0.1868 0.0706 0.1453 0.0331  0.0070  0.0024  123 TRP B CD2 
3289 N  NE1 . TRP B 123 ? 0.1963 0.0731 0.1466 0.0311  -0.0122 0.0013  123 TRP B NE1 
3290 C  CE2 . TRP B 123 ? 0.1936 0.0729 0.1704 0.0297  -0.0205 0.0032  123 TRP B CE2 
3291 C  CE3 . TRP B 123 ? 0.1983 0.0675 0.1476 0.0261  0.0164  0.0096  123 TRP B CE3 
3292 C  CZ2 . TRP B 123 ? 0.2746 0.0538 0.1947 0.0087  0.0175  -0.0082 123 TRP B CZ2 
3293 C  CZ3 . TRP B 123 ? 0.2664 0.0650 0.1660 0.0300  0.0259  -0.0003 123 TRP B CZ3 
3294 C  CH2 . TRP B 123 ? 0.3010 0.0627 0.1764 0.0015  0.0043  -0.0195 123 TRP B CH2 
3295 N  N   . ASN B 124 ? 0.1178 0.0754 0.1247 0.0020  -0.0144 0.0164  124 ASN B N   
3296 C  CA  . ASN B 124 ? 0.1283 0.0657 0.1358 -0.0153 -0.0081 0.0133  124 ASN B CA  
3297 C  C   . ASN B 124 ? 0.1234 0.0822 0.1252 -0.0082 -0.0012 0.0122  124 ASN B C   
3298 O  O   . ASN B 124 ? 0.1322 0.0872 0.1286 -0.0071 0.0010  0.0031  124 ASN B O   
3299 C  CB  . ASN B 124 ? 0.1379 0.0957 0.1182 -0.0183 -0.0012 0.0074  124 ASN B CB  
3300 C  CG  . ASN B 124 ? 0.1577 0.0719 0.1389 0.0098  -0.0012 0.0060  124 ASN B CG  
3301 O  OD1 . ASN B 124 ? 0.1744 0.0780 0.1647 -0.0140 0.0006  0.0185  124 ASN B OD1 
3302 N  ND2 . ASN B 124 ? 0.2127 0.0950 0.1333 -0.0034 -0.0054 0.0284  124 ASN B ND2 
3303 N  N   . THR B 125 ? 0.1399 0.0817 0.1442 -0.0272 -0.0163 0.0091  125 THR B N   
3304 C  CA  . THR B 125 ? 0.1474 0.0759 0.1959 -0.0032 -0.0087 0.0000  125 THR B CA  
3305 C  C   . THR B 125 ? 0.1451 0.0803 0.1818 -0.0266 0.0013  -0.0074 125 THR B C   
3306 O  O   . THR B 125 ? 0.1819 0.0975 0.1742 -0.0062 -0.0184 -0.0185 125 THR B O   
3307 C  CB  . THR B 125 ? 0.1398 0.1484 0.2439 0.0085  -0.0236 0.0038  125 THR B CB  
3308 O  OG1 . THR B 125 ? 0.1922 0.1777 0.3445 -0.0549 0.0715  -0.0211 125 THR B OG1 
3309 C  CG2 . THR B 125 ? 0.1701 0.1597 0.2858 0.0104  -0.0811 0.0266  125 THR B CG2 
3310 N  N   . LYS B 126 ? 0.1868 0.0706 0.1529 -0.0034 0.0171  0.0186  127 LYS B N   
3311 C  CA  . LYS B 126 ? 0.1992 0.1020 0.1579 -0.0057 -0.0003 0.0337  127 LYS B CA  
3312 C  C   . LYS B 126 ? 0.2364 0.0543 0.1697 -0.0081 0.0092  0.0120  127 LYS B C   
3313 O  O   . LYS B 126 ? 0.2399 0.0930 0.1899 0.0183  0.0205  0.0298  127 LYS B O   
3314 C  CB  . LYS B 126 ? 0.2428 0.1329 0.1665 0.0124  -0.0222 0.0153  127 LYS B CB  
3315 C  CG  . LYS B 126 ? 0.2213 0.1365 0.1715 0.0175  -0.0219 -0.0130 127 LYS B CG  
3316 C  CD  . LYS B 126 ? 0.3589 0.2134 0.1908 0.0410  0.0193  0.0024  127 LYS B CD  
3317 C  CE  . LYS B 126 ? 0.1981 0.2511 0.5655 -0.0244 -0.0637 0.1180  127 LYS B CE  
3318 N  NZ  . LYS B 126 ? 0.6769 0.4991 0.6366 0.1875  -0.0003 0.3154  127 LYS B NZ  
3319 N  N   . TYR B 127 ? 0.1852 0.0764 0.1395 0.0054  -0.0109 -0.0006 128 TYR B N   
3320 C  CA  . TYR B 127 ? 0.1782 0.0745 0.1313 0.0070  -0.0204 -0.0081 128 TYR B CA  
3321 C  C   . TYR B 127 ? 0.1864 0.0869 0.1483 0.0140  -0.0071 0.0104  128 TYR B C   
3322 O  O   . TYR B 127 ? 0.1890 0.0966 0.1561 0.0132  0.0126  0.0115  128 TYR B O   
3323 C  CB  . TYR B 127 ? 0.1875 0.0917 0.1773 -0.0164 -0.0006 -0.0038 128 TYR B CB  
3324 C  CG  . TYR B 127 ? 0.1509 0.0763 0.1613 0.0000  -0.0151 0.0149  128 TYR B CG  
3325 C  CD1 . TYR B 127 ? 0.2030 0.0922 0.1708 0.0032  -0.0178 0.0199  128 TYR B CD1 
3326 C  CD2 . TYR B 127 ? 0.1419 0.0995 0.1555 -0.0116 -0.0065 0.0017  128 TYR B CD2 
3327 C  CE1 . TYR B 127 ? 0.2081 0.1142 0.1552 0.0019  -0.0281 0.0362  128 TYR B CE1 
3328 C  CE2 . TYR B 127 ? 0.1232 0.1032 0.1509 -0.0027 -0.0177 0.0199  128 TYR B CE2 
3329 C  CZ  . TYR B 127 ? 0.1823 0.1120 0.1503 -0.0245 -0.0269 0.0238  128 TYR B CZ  
3330 O  OH  . TYR B 127 ? 0.2349 0.1367 0.1521 -0.0215 -0.0339 0.0445  128 TYR B OH  
3331 N  N   . GLY B 128 ? 0.1740 0.0870 0.1414 0.0144  -0.0204 -0.0063 129 GLY B N   
3332 C  CA  . GLY B 128 ? 0.2281 0.0781 0.1537 0.0076  0.0151  -0.0098 129 GLY B CA  
3333 C  C   . GLY B 128 ? 0.2193 0.0812 0.1315 -0.0165 -0.0164 -0.0127 129 GLY B C   
3334 O  O   . GLY B 128 ? 0.2576 0.0973 0.1475 -0.0078 -0.0141 -0.0163 129 GLY B O   
3335 N  N   . ASP B 129 ? 0.2017 0.0891 0.1455 -0.0131 -0.0171 -0.0048 130 ASP B N   
3336 C  CA  . ASP B 129 ? 0.2946 0.0864 0.1320 -0.0209 0.0059  -0.0057 130 ASP B CA  
3337 C  C   . ASP B 129 ? 0.2197 0.1286 0.1331 -0.0285 -0.0124 -0.0043 130 ASP B C   
3338 O  O   . ASP B 129 ? 0.2732 0.1092 0.1352 -0.0280 -0.0172 0.0099  130 ASP B O   
3339 C  CB  . ASP B 129 ? 0.2450 0.1780 0.1891 -0.0171 0.0399  -0.0219 130 ASP B CB  
3340 C  CG  . ASP B 129 ? 0.2763 0.1077 0.1626 -0.0560 0.0296  -0.0172 130 ASP B CG  
3341 O  OD1 . ASP B 129 ? 0.3804 0.2046 0.2608 0.0855  -0.1070 0.0149  130 ASP B OD1 
3342 O  OD2 . ASP B 129 ? 0.3386 0.1651 0.2969 -0.0153 0.0918  -0.0524 130 ASP B OD2 
3343 N  N   . PHE B 130 ? 0.2441 0.0922 0.1243 -0.0065 0.0057  0.0020  131 PHE B N   
3344 C  CA  . PHE B 130 ? 0.1737 0.0983 0.1270 -0.0068 -0.0197 -0.0020 131 PHE B CA  
3345 C  C   . PHE B 130 ? 0.1861 0.0970 0.1333 0.0052  0.0278  0.0066  131 PHE B C   
3346 O  O   . PHE B 130 ? 0.1834 0.1176 0.1214 0.0238  0.0088  0.0006  131 PHE B O   
3347 C  CB  . PHE B 130 ? 0.1904 0.0925 0.1448 -0.0065 -0.0203 0.0172  131 PHE B CB  
3348 C  CG  . PHE B 130 ? 0.1674 0.0810 0.1504 0.0017  0.0076  0.0209  131 PHE B CG  
3349 C  CD1 . PHE B 130 ? 0.1913 0.1002 0.1226 0.0346  -0.0200 -0.0021 131 PHE B CD1 
3350 C  CD2 . PHE B 130 ? 0.1908 0.1345 0.1626 0.0074  0.0148  0.0210  131 PHE B CD2 
3351 C  CE1 . PHE B 130 ? 0.2220 0.1081 0.1572 0.0172  -0.0176 -0.0065 131 PHE B CE1 
3352 C  CE2 . PHE B 130 ? 0.2135 0.1615 0.1683 -0.0348 -0.0057 -0.0006 131 PHE B CE2 
3353 C  CZ  . PHE B 130 ? 0.2102 0.1601 0.1720 0.0132  -0.0348 0.0164  131 PHE B CZ  
3354 N  N   . GLY B 131 ? 0.2432 0.1200 0.1484 0.0408  0.0482  0.0087  132 GLY B N   
3355 C  CA  . GLY B 131 ? 0.2187 0.1613 0.1640 0.0502  0.0687  -0.0027 132 GLY B CA  
3356 C  C   . GLY B 131 ? 0.2096 0.1661 0.1757 0.0595  0.0546  -0.0152 132 GLY B C   
3357 O  O   . GLY B 131 ? 0.2019 0.1313 0.2205 0.0410  0.0289  0.0361  132 GLY B O   
3358 N  N   . LYS B 132 ? 0.1967 0.1426 0.1735 0.0439  0.0355  0.0118  133 LYS B N   
3359 C  CA  . LYS B 132 ? 0.2038 0.0859 0.1877 0.0366  0.0186  -0.0060 133 LYS B CA  
3360 C  C   . LYS B 132 ? 0.1523 0.1032 0.1647 0.0283  0.0183  0.0164  133 LYS B C   
3361 O  O   . LYS B 132 ? 0.1609 0.1160 0.1644 0.0406  -0.0052 0.0206  133 LYS B O   
3362 C  CB  . LYS B 132 ? 0.1996 0.0989 0.2236 0.0244  0.0153  0.0083  133 LYS B CB  
3363 C  CG  . LYS B 132 ? 0.1941 0.1218 0.3643 0.0274  -0.0388 -0.0758 133 LYS B CG  
3364 C  CD  . LYS B 132 ? 0.1559 0.1974 0.5605 0.0482  -0.0344 -0.1414 133 LYS B CD  
3365 C  CE  . LYS B 132 ? 0.4393 0.1943 0.6521 0.0986  -0.2377 -0.1062 133 LYS B CE  
3366 N  NZ  . LYS B 132 ? 0.4822 0.5360 0.5062 0.0015  -0.2115 0.1229  133 LYS B NZ  
3367 N  N   . ALA B 133 ? 0.1432 0.1111 0.1441 0.0395  0.0088  0.0024  134 ALA B N   
3368 C  CA  . ALA B 133 ? 0.1361 0.1265 0.1180 0.0359  -0.0017 -0.0063 134 ALA B CA  
3369 C  C   . ALA B 133 ? 0.1512 0.1214 0.1130 0.0474  -0.0015 0.0190  134 ALA B C   
3370 O  O   . ALA B 133 ? 0.1180 0.1399 0.1207 0.0193  -0.0060 0.0129  134 ALA B O   
3371 C  CB  . ALA B 133 ? 0.1423 0.1311 0.1187 0.0408  -0.0163 0.0068  134 ALA B CB  
3372 N  N   . VAL B 134 ? 0.1353 0.1085 0.1473 0.0153  0.0121  0.0046  135 VAL B N   
3373 C  CA  . VAL B 134 ? 0.1751 0.1272 0.1459 0.0187  0.0173  -0.0060 135 VAL B CA  
3374 C  C   . VAL B 134 ? 0.1324 0.1297 0.1601 0.0212  0.0200  0.0003  135 VAL B C   
3375 O  O   . VAL B 134 ? 0.1538 0.1480 0.1676 -0.0087 0.0216  -0.0157 135 VAL B O   
3376 C  CB  . VAL B 134 ? 0.2099 0.1432 0.1893 0.0590  0.0678  0.0401  135 VAL B CB  
3377 C  CG1 . VAL B 134 ? 0.2155 0.1688 0.1827 0.0434  0.0216  0.0186  135 VAL B CG1 
3378 C  CG2 . VAL B 134 ? 0.1714 0.1423 0.1947 0.0195  0.0412  0.0062  135 VAL B CG2 
3379 N  N   . GLN B 135 ? 0.1259 0.1164 0.1746 0.0313  0.0190  0.0108  136 GLN B N   
3380 C  CA  . GLN B 135 ? 0.1274 0.1308 0.1944 0.0296  0.0120  0.0205  136 GLN B CA  
3381 C  C   . GLN B 135 ? 0.1365 0.1430 0.1732 0.0419  -0.0080 -0.0006 136 GLN B C   
3382 O  O   . GLN B 135 ? 0.1286 0.2274 0.2067 0.0353  -0.0184 0.0277  136 GLN B O   
3383 C  CB  . GLN B 135 ? 0.1342 0.1580 0.2270 0.0688  0.0172  -0.0193 136 GLN B CB  
3384 C  CG  . GLN B 135 ? 0.1791 0.2144 0.2471 0.0296  0.0377  -0.0434 136 GLN B CG  
3385 C  CD  . GLN B 135 ? 0.2329 0.2795 0.2442 0.0918  0.0115  -0.0225 136 GLN B CD  
3386 O  OE1 . GLN B 135 ? 0.2865 0.4499 0.3668 0.1588  -0.0417 0.0283  136 GLN B OE1 
3387 N  NE2 . GLN B 135 ? 0.2143 0.2922 0.2786 0.0472  0.0328  -0.0370 136 GLN B NE2 
3388 N  N   . GLN B 136 ? 0.1180 0.1103 0.1708 0.0140  0.0170  -0.0066 137 GLN B N   
3389 C  CA  . GLN B 136 ? 0.1147 0.1453 0.1577 0.0071  -0.0187 0.0223  137 GLN B CA  
3390 C  C   . GLN B 136 ? 0.1187 0.1561 0.1281 -0.0006 0.0093  0.0286  137 GLN B C   
3391 O  O   . GLN B 136 ? 0.1713 0.1106 0.1101 0.0043  -0.0059 0.0153  137 GLN B O   
3392 C  CB  . GLN B 136 ? 0.1265 0.1029 0.1862 0.0020  -0.0383 0.0189  137 GLN B CB  
3393 C  CG  . GLN B 136 ? 0.2689 0.1322 0.1774 -0.0557 0.0192  -0.0038 137 GLN B CG  
3394 C  CD  . GLN B 136 ? 0.2583 0.1035 0.3953 -0.0081 0.0461  -0.0263 137 GLN B CD  
3395 O  OE1 . GLN B 136 ? 0.2772 0.1879 0.3727 0.0096  0.0052  0.1491  137 GLN B OE1 
3396 N  NE2 . GLN B 136 ? 0.3289 0.2376 0.6283 0.0324  0.0812  -0.1741 137 GLN B NE2 
3397 N  N   . PRO B 137 ? 0.0943 0.1532 0.1237 -0.0060 -0.0212 0.0251  138 PRO B N   
3398 C  CA  . PRO B 137 ? 0.1369 0.1534 0.1274 -0.0153 -0.0220 -0.0074 138 PRO B CA  
3399 C  C   . PRO B 137 ? 0.1237 0.1656 0.1313 -0.0149 -0.0153 -0.0041 138 PRO B C   
3400 O  O   . PRO B 137 ? 0.1886 0.1588 0.1972 -0.0272 -0.0081 -0.0186 138 PRO B O   
3401 C  CB  . PRO B 137 ? 0.2067 0.2200 0.1280 -0.0297 -0.0164 0.0152  138 PRO B CB  
3402 C  CG  . PRO B 137 ? 0.4185 0.2685 0.1313 -0.0109 -0.0820 0.0505  138 PRO B CG  
3403 C  CD  . PRO B 137 ? 0.1395 0.2439 0.1455 0.0428  -0.0254 0.0494  138 PRO B CD  
3404 N  N   . ASP B 138 ? 0.1155 0.1478 0.1153 -0.0137 -0.0160 0.0049  139 ASP B N   
3405 C  CA  . ASP B 138 ? 0.1309 0.1288 0.1181 -0.0088 -0.0060 0.0173  139 ASP B CA  
3406 C  C   . ASP B 138 ? 0.1164 0.1018 0.1151 0.0164  -0.0130 0.0093  139 ASP B C   
3407 O  O   . ASP B 138 ? 0.1313 0.1176 0.1395 0.0104  -0.0121 0.0103  139 ASP B O   
3408 C  CB  . ASP B 138 ? 0.1793 0.1263 0.1337 -0.0252 0.0082  0.0001  139 ASP B CB  
3409 C  CG  . ASP B 138 ? 0.1480 0.1765 0.1354 -0.0241 0.0000  0.0346  139 ASP B CG  
3410 O  OD1 . ASP B 138 ? 0.1950 0.1261 0.1512 -0.0225 0.0027  0.0397  139 ASP B OD1 
3411 O  OD2 . ASP B 138 ? 0.1983 0.1940 0.1929 -0.0267 0.0217  0.0524  139 ASP B OD2 
3412 N  N   . GLY B 139 ? 0.1182 0.0988 0.1045 0.0086  -0.0087 0.0121  140 GLY B N   
3413 C  CA  . GLY B 139 ? 0.1207 0.0920 0.1110 0.0151  -0.0168 0.0054  140 GLY B CA  
3414 C  C   . GLY B 139 ? 0.1029 0.0627 0.1146 0.0007  -0.0041 0.0105  140 GLY B C   
3415 O  O   . GLY B 139 ? 0.1158 0.0807 0.1198 -0.0038 -0.0248 0.0044  140 GLY B O   
3416 N  N   . LEU B 140 ? 0.0936 0.0808 0.1221 0.0164  -0.0059 0.0160  141 LEU B N   
3417 C  CA  . LEU B 140 ? 0.1092 0.0635 0.1083 0.0151  -0.0082 0.0086  141 LEU B CA  
3418 C  C   . LEU B 140 ? 0.0989 0.0759 0.1002 0.0000  -0.0196 0.0006  141 LEU B C   
3419 O  O   . LEU B 140 ? 0.1083 0.0725 0.1101 0.0094  -0.0076 0.0035  141 LEU B O   
3420 C  CB  . LEU B 140 ? 0.1123 0.0889 0.1020 0.0017  -0.0024 0.0130  141 LEU B CB  
3421 C  CG  . LEU B 140 ? 0.1383 0.1036 0.1492 -0.0205 0.0231  -0.0091 141 LEU B CG  
3422 C  CD1 . LEU B 140 ? 0.1302 0.1102 0.1374 -0.0074 0.0132  0.0065  141 LEU B CD1 
3423 C  CD2 . LEU B 140 ? 0.2366 0.1040 0.1949 -0.0483 0.0551  -0.0423 141 LEU B CD2 
3424 N  N   . ALA B 141 ? 0.0841 0.0742 0.1083 0.0000  -0.0160 0.0000  142 ALA B N   
3425 C  CA  . ALA B 141 ? 0.1084 0.0502 0.1135 0.0131  -0.0093 -0.0038 142 ALA B CA  
3426 C  C   . ALA B 141 ? 0.0892 0.0692 0.1079 0.0043  -0.0125 -0.0057 142 ALA B C   
3427 O  O   . ALA B 141 ? 0.1176 0.0710 0.1108 0.0076  -0.0232 -0.0038 142 ALA B O   
3428 C  CB  . ALA B 141 ? 0.0954 0.1058 0.1340 0.0031  0.0071  0.0019  142 ALA B CB  
3429 N  N   . VAL B 142 ? 0.0820 0.0631 0.1031 0.0138  -0.0153 -0.0071 143 VAL B N   
3430 C  CA  . VAL B 142 ? 0.0894 0.0676 0.0995 0.0137  -0.0130 0.0035  143 VAL B CA  
3431 C  C   . VAL B 142 ? 0.0790 0.0751 0.0848 0.0131  -0.0020 0.0074  143 VAL B C   
3432 O  O   . VAL B 142 ? 0.0892 0.0894 0.0921 0.0063  -0.0121 -0.0028 143 VAL B O   
3433 C  CB  . VAL B 142 ? 0.0657 0.1042 0.0997 -0.0015 -0.0115 -0.0080 143 VAL B CB  
3434 C  CG1 . VAL B 142 ? 0.1097 0.1035 0.0927 -0.0218 -0.0151 0.0063  143 VAL B CG1 
3435 C  CG2 . VAL B 142 ? 0.0841 0.1234 0.1207 0.0041  -0.0086 -0.0204 143 VAL B CG2 
3436 N  N   . LEU B 143 ? 0.0941 0.0613 0.1089 0.0125  -0.0188 -0.0015 144 LEU B N   
3437 C  CA  . LEU B 143 ? 0.0724 0.0738 0.1108 0.0181  -0.0225 -0.0015 144 LEU B CA  
3438 C  C   . LEU B 143 ? 0.0766 0.0843 0.0895 0.0239  -0.0088 -0.0124 144 LEU B C   
3439 O  O   . LEU B 143 ? 0.1178 0.0882 0.0941 0.0096  -0.0052 -0.0104 144 LEU B O   
3440 C  CB  . LEU B 143 ? 0.0868 0.0980 0.1423 0.0028  -0.0241 -0.0131 144 LEU B CB  
3441 C  CG  . LEU B 143 ? 0.0848 0.1180 0.1553 -0.0027 -0.0193 -0.0015 144 LEU B CG  
3442 C  CD1 . LEU B 143 ? 0.1068 0.1507 0.1712 0.0211  -0.0265 -0.0423 144 LEU B CD1 
3443 C  CD2 . LEU B 143 ? 0.0966 0.1480 0.1776 0.0007  -0.0308 -0.0267 144 LEU B CD2 
3444 N  N   . GLY B 144 ? 0.0879 0.0606 0.1033 0.0140  -0.0109 -0.0122 145 GLY B N   
3445 C  CA  . GLY B 144 ? 0.0938 0.0635 0.1108 0.0060  -0.0138 0.0026  145 GLY B CA  
3446 C  C   . GLY B 144 ? 0.0764 0.0722 0.0881 0.0082  -0.0124 -0.0060 145 GLY B C   
3447 O  O   . GLY B 144 ? 0.1001 0.0872 0.0968 0.0104  0.0013  0.0027  145 GLY B O   
3448 N  N   . ILE B 145 ? 0.0864 0.0736 0.0916 0.0038  -0.0175 -0.0019 146 ILE B N   
3449 C  CA  . ILE B 145 ? 0.0715 0.0728 0.1070 0.0125  -0.0227 -0.0017 146 ILE B CA  
3450 C  C   . ILE B 145 ? 0.0832 0.0678 0.1044 0.0109  -0.0185 -0.0015 146 ILE B C   
3451 O  O   . ILE B 145 ? 0.1005 0.0750 0.1099 0.0083  -0.0003 -0.0005 146 ILE B O   
3452 C  CB  . ILE B 145 ? 0.0844 0.0793 0.1318 0.0086  -0.0302 0.0015  146 ILE B CB  
3453 C  CG1 . ILE B 145 ? 0.1172 0.1018 0.1583 -0.0199 -0.0408 0.0015  146 ILE B CG1 
3454 C  CG2 . ILE B 145 ? 0.0930 0.1171 0.1668 0.0115  -0.0498 -0.0013 146 ILE B CG2 
3455 C  CD1 . ILE B 145 ? 0.1008 0.1191 0.1423 0.0073  -0.0359 -0.0170 146 ILE B CD1 
3456 N  N   . PHE B 146 ? 0.0948 0.0722 0.0945 0.0032  -0.0227 -0.0010 147 PHE B N   
3457 C  CA  . PHE B 146 ? 0.1105 0.0544 0.1014 -0.0137 -0.0251 -0.0006 147 PHE B CA  
3458 C  C   . PHE B 146 ? 0.0916 0.0639 0.1120 0.0098  -0.0221 0.0010  147 PHE B C   
3459 O  O   . PHE B 146 ? 0.0970 0.0872 0.1279 -0.0081 -0.0324 0.0093  147 PHE B O   
3460 C  CB  . PHE B 146 ? 0.1009 0.0746 0.1181 0.0093  -0.0274 -0.0114 147 PHE B CB  
3461 C  CG  . PHE B 146 ? 0.0785 0.0702 0.1059 0.0030  -0.0275 -0.0176 147 PHE B CG  
3462 C  CD1 . PHE B 146 ? 0.0869 0.0671 0.1255 0.0034  -0.0240 -0.0070 147 PHE B CD1 
3463 C  CD2 . PHE B 146 ? 0.1171 0.0715 0.1184 0.0100  -0.0250 -0.0261 147 PHE B CD2 
3464 C  CE1 . PHE B 146 ? 0.1023 0.0857 0.1128 -0.0021 -0.0222 -0.0037 147 PHE B CE1 
3465 C  CE2 . PHE B 146 ? 0.0962 0.0781 0.1235 0.0114  -0.0089 -0.0189 147 PHE B CE2 
3466 C  CZ  . PHE B 146 ? 0.0778 0.0835 0.1180 0.0094  -0.0148 -0.0160 147 PHE B CZ  
3467 N  N   . LEU B 147 ? 0.0876 0.0744 0.1160 0.0078  -0.0088 0.0031  148 LEU B N   
3468 C  CA  . LEU B 147 ? 0.1340 0.0636 0.1013 0.0197  -0.0143 0.0065  148 LEU B CA  
3469 C  C   . LEU B 147 ? 0.0914 0.0864 0.1167 0.0113  0.0044  -0.0096 148 LEU B C   
3470 O  O   . LEU B 147 ? 0.0920 0.0754 0.1291 0.0065  0.0003  -0.0060 148 LEU B O   
3471 C  CB  . LEU B 147 ? 0.1291 0.0737 0.1228 0.0177  -0.0151 -0.0001 148 LEU B CB  
3472 C  CG  . LEU B 147 ? 0.1349 0.0685 0.1335 0.0099  -0.0146 0.0006  148 LEU B CG  
3473 C  CD1 . LEU B 147 ? 0.1803 0.0851 0.1263 0.0057  -0.0340 -0.0040 148 LEU B CD1 
3474 C  CD2 . LEU B 147 ? 0.1370 0.1198 0.1368 0.0142  -0.0310 -0.0026 148 LEU B CD2 
3475 N  N   . LYS B 148 ? 0.1022 0.0767 0.1444 0.0135  -0.0133 0.0049  149 LYS B N   
3476 C  CA  . LYS B 148 ? 0.1421 0.0631 0.1298 0.0086  -0.0132 0.0093  149 LYS B CA  
3477 C  C   . LYS B 148 ? 0.1241 0.1029 0.1342 -0.0043 -0.0249 0.0005  149 LYS B C   
3478 O  O   . LYS B 148 ? 0.1577 0.1160 0.1421 -0.0166 -0.0412 0.0108  149 LYS B O   
3479 C  CB  . LYS B 148 ? 0.1676 0.0998 0.1372 0.0250  -0.0236 -0.0318 149 LYS B CB  
3480 C  CG  . LYS B 148 ? 0.1383 0.1394 0.1732 0.0324  -0.0141 -0.0322 149 LYS B CG  
3481 C  CD  . LYS B 148 ? 0.2249 0.2184 0.2606 0.0627  0.0310  -0.0471 149 LYS B CD  
3482 C  CE  . LYS B 148 ? 0.2928 0.4444 0.2825 0.0869  0.0656  -0.1184 149 LYS B CE  
3483 N  NZ  . LYS B 148 ? 0.5816 0.5030 0.3702 0.2833  0.0640  -0.1377 149 LYS B NZ  
3484 N  N   . VAL B 149 ? 0.1537 0.0923 0.1354 0.0168  -0.0261 0.0143  150 VAL B N   
3485 C  CA  . VAL B 149 ? 0.1453 0.0914 0.1556 0.0031  -0.0215 0.0225  150 VAL B CA  
3486 C  C   . VAL B 149 ? 0.1595 0.1105 0.1468 0.0133  -0.0310 0.0017  150 VAL B C   
3487 O  O   . VAL B 149 ? 0.2013 0.1020 0.1713 0.0166  -0.0206 -0.0140 150 VAL B O   
3488 C  CB  . VAL B 149 ? 0.1541 0.0910 0.1491 0.0000  -0.0231 -0.0027 150 VAL B CB  
3489 C  CG1 . VAL B 149 ? 0.2046 0.1358 0.1504 0.0006  -0.0209 0.0107  150 VAL B CG1 
3490 C  CG2 . VAL B 149 ? 0.1534 0.1641 0.2064 0.0315  -0.0132 0.0048  150 VAL B CG2 
3491 N  N   . GLY B 150 ? 0.1719 0.1070 0.1448 0.0320  -0.0471 -0.0008 151 GLY B N   
3492 C  CA  . GLY B 150 ? 0.1796 0.1153 0.1835 0.0513  -0.0427 -0.0131 151 GLY B CA  
3493 C  C   . GLY B 150 ? 0.1659 0.1164 0.1586 0.0357  -0.0395 -0.0091 151 GLY B C   
3494 O  O   . GLY B 150 ? 0.1796 0.1205 0.1854 0.0266  -0.0388 0.0140  151 GLY B O   
3495 N  N   A SER B 151 ? 0.1559 0.1159 0.2029 0.0292  -0.0368 0.0129  152 SER B N   
3496 N  N   B SER B 151 ? 0.1665 0.1182 0.2076 0.0300  -0.0326 0.0142  152 SER B N   
3497 C  CA  A SER B 151 ? 0.1559 0.1536 0.1895 0.0456  -0.0498 0.0006  152 SER B CA  
3498 C  CA  B SER B 151 ? 0.1701 0.1541 0.2091 0.0421  -0.0463 -0.0024 152 SER B CA  
3499 C  C   A SER B 151 ? 0.1843 0.0894 0.1789 0.0063  -0.0606 0.0197  152 SER B C   
3500 C  C   B SER B 151 ? 0.1796 0.0959 0.1783 0.0017  -0.0551 0.0221  152 SER B C   
3501 O  O   A SER B 151 ? 0.2023 0.1237 0.1641 0.0401  -0.0472 0.0141  152 SER B O   
3502 O  O   B SER B 151 ? 0.2073 0.1270 0.1703 0.0388  -0.0450 0.0164  152 SER B O   
3503 C  CB  A SER B 151 ? 0.1428 0.2362 0.3244 0.0306  -0.0230 -0.0560 152 SER B CB  
3504 C  CB  B SER B 151 ? 0.1644 0.2479 0.3635 0.0559  -0.0076 -0.0401 152 SER B CB  
3505 O  OG  A SER B 151 ? 0.1548 0.3012 0.3750 -0.0032 -0.0636 -0.1896 152 SER B OG  
3506 O  OG  B SER B 151 ? 0.2570 0.3388 0.3808 0.0175  -0.0231 0.0000  152 SER B OG  
3507 N  N   . ALA B 152 ? 0.1598 0.1234 0.1888 0.0015  -0.0707 0.0212  153 ALA B N   
3508 C  CA  . ALA B 152 ? 0.2035 0.1024 0.1789 0.0032  -0.0469 0.0151  153 ALA B CA  
3509 C  C   . ALA B 152 ? 0.1938 0.1221 0.1534 -0.0012 -0.0529 0.0263  153 ALA B C   
3510 O  O   . ALA B 152 ? 0.2096 0.1295 0.2125 0.0032  -0.0362 0.0155  153 ALA B O   
3511 C  CB  . ALA B 152 ? 0.2335 0.1289 0.1712 -0.0080 -0.0648 0.0249  153 ALA B CB  
3512 N  N   . LYS B 153 ? 0.2081 0.1020 0.1855 0.0105  -0.0640 0.0132  154 LYS B N   
3513 C  CA  . LYS B 153 ? 0.2297 0.0842 0.1798 0.0116  -0.0513 0.0140  154 LYS B CA  
3514 C  C   . LYS B 153 ? 0.1837 0.1234 0.1915 -0.0309 -0.0326 0.0483  154 LYS B C   
3515 O  O   . LYS B 153 ? 0.1983 0.1419 0.1697 -0.0231 -0.0785 0.0282  154 LYS B O   
3516 C  CB  . LYS B 153 ? 0.2391 0.0977 0.1836 0.0092  -0.0866 0.0092  154 LYS B CB  
3517 C  CG  . LYS B 153 ? 0.3377 0.0941 0.2265 0.0154  -0.0860 0.0373  154 LYS B CG  
3518 C  CD  . LYS B 153 ? 0.3583 0.1077 0.2247 -0.0008 -0.0939 0.0186  154 LYS B CD  
3519 C  CE  . LYS B 153 ? 0.4422 0.1385 0.2303 -0.0746 -0.1057 0.0263  154 LYS B CE  
3520 N  NZ  . LYS B 153 ? 0.2786 0.2209 0.3231 -0.0280 -0.0923 0.0590  154 LYS B NZ  
3521 N  N   . PRO B 154 ? 0.2091 0.1593 0.1976 -0.0467 -0.0693 0.0210  155 PRO B N   
3522 C  CA  . PRO B 154 ? 0.2187 0.1528 0.2315 -0.0083 -0.0890 0.0074  155 PRO B CA  
3523 C  C   . PRO B 154 ? 0.2026 0.1774 0.1825 -0.0304 -0.0908 -0.0085 155 PRO B C   
3524 O  O   . PRO B 154 ? 0.2833 0.1852 0.1927 0.0082  -0.1010 -0.0269 155 PRO B O   
3525 C  CB  . PRO B 154 ? 0.2096 0.1870 0.2712 -0.0269 -0.0879 0.0096  155 PRO B CB  
3526 C  CG  . PRO B 154 ? 0.1861 0.2450 0.2921 -0.0110 -0.0529 -0.0043 155 PRO B CG  
3527 C  CD  . PRO B 154 ? 0.2005 0.2041 0.2259 -0.0012 -0.0417 0.0291  155 PRO B CD  
3528 N  N   . GLY B 155 ? 0.1981 0.1171 0.2208 -0.0270 -0.0886 0.0107  156 GLY B N   
3529 C  CA  . GLY B 155 ? 0.2592 0.1205 0.2236 -0.0203 -0.0604 0.0339  156 GLY B CA  
3530 C  C   . GLY B 155 ? 0.3009 0.0959 0.2186 -0.0010 -0.0654 -0.0292 156 GLY B C   
3531 O  O   . GLY B 155 ? 0.3388 0.1098 0.2906 -0.0129 -0.0707 -0.0331 156 GLY B O   
3532 N  N   . LEU B 156 ? 0.2125 0.1248 0.1906 0.0000  -0.0588 0.0135  157 LEU B N   
3533 C  CA  . LEU B 156 ? 0.2319 0.1068 0.1609 -0.0109 -0.0715 -0.0027 157 LEU B CA  
3534 C  C   . LEU B 156 ? 0.2321 0.1147 0.1789 -0.0154 -0.0581 0.0153  157 LEU B C   
3535 O  O   . LEU B 156 ? 0.2655 0.1144 0.1510 0.0109  -0.0731 0.0215  157 LEU B O   
3536 C  CB  . LEU B 156 ? 0.2084 0.1392 0.1659 0.0250  -0.0778 -0.0151 157 LEU B CB  
3537 C  CG  . LEU B 156 ? 0.2127 0.1310 0.1771 0.0212  -0.0675 -0.0031 157 LEU B CG  
3538 C  CD1 . LEU B 156 ? 0.2784 0.1516 0.1703 0.0329  -0.0930 0.0035  157 LEU B CD1 
3539 C  CD2 . LEU B 156 ? 0.2040 0.1457 0.1780 0.0038  -0.0619 -0.0217 157 LEU B CD2 
3540 N  N   . GLN B 157 ? 0.2658 0.1306 0.1640 0.0331  -0.0839 0.0046  158 GLN B N   
3541 C  CA  . GLN B 157 ? 0.3287 0.1405 0.1358 0.0432  -0.0797 0.0040  158 GLN B CA  
3542 C  C   . GLN B 157 ? 0.3298 0.1328 0.1360 0.0353  -0.0895 0.0237  158 GLN B C   
3543 O  O   . GLN B 157 ? 0.2809 0.1467 0.1606 0.0274  -0.0744 0.0226  158 GLN B O   
3544 C  CB  . GLN B 157 ? 0.3513 0.1361 0.1983 0.0631  -0.0895 0.0131  158 GLN B CB  
3545 C  CG  . GLN B 157 ? 0.3876 0.1266 0.1798 0.0038  -0.0904 0.0228  158 GLN B CG  
3546 C  CD  . GLN B 157 ? 0.3750 0.1327 0.1694 0.0111  -0.1066 0.0179  158 GLN B CD  
3547 O  OE1 . GLN B 157 ? 0.3601 0.1315 0.1649 0.0054  -0.0864 0.0199  158 GLN B OE1 
3548 N  NE2 . GLN B 157 ? 0.3867 0.1579 0.1762 0.1014  -0.0790 0.0057  158 GLN B NE2 
3549 N  N   . LYS B 158 ? 0.3107 0.1365 0.1753 0.0269  -0.1134 -0.0142 159 LYS B N   
3550 C  CA  . LYS B 158 ? 0.2702 0.1133 0.1872 0.0052  -0.0948 -0.0149 159 LYS B CA  
3551 C  C   . LYS B 158 ? 0.2723 0.1228 0.1521 0.0114  -0.0913 0.0434  159 LYS B C   
3552 O  O   . LYS B 158 ? 0.3438 0.2094 0.1397 0.0147  -0.0702 0.0115  159 LYS B O   
3553 C  CB  . LYS B 158 ? 0.3767 0.1237 0.2459 -0.0179 -0.1150 -0.0755 159 LYS B CB  
3554 C  CG  . LYS B 158 ? 0.4767 0.2763 0.2872 0.0166  -0.1695 -0.0724 159 LYS B CG  
3555 C  CD  . LYS B 158 ? 0.5257 0.6241 0.7717 -0.2029 -0.2944 -0.2343 159 LYS B CD  
3556 C  CE  . LYS B 158 ? 0.6219 0.5047 0.5909 -0.1451 -0.3353 -0.0480 159 LYS B CE  
3557 N  NZ  . LYS B 158 ? 0.6807 0.3616 0.4521 -0.0223 -0.2451 -0.0401 159 LYS B NZ  
3558 N  N   . VAL B 159 ? 0.3318 0.1234 0.1453 0.0006  -0.0992 0.0390  160 VAL B N   
3559 C  CA  . VAL B 159 ? 0.3005 0.0995 0.1473 0.0043  -0.0785 0.0138  160 VAL B CA  
3560 C  C   . VAL B 159 ? 0.2881 0.0950 0.1643 0.0015  -0.0718 -0.0023 160 VAL B C   
3561 O  O   . VAL B 159 ? 0.2806 0.1142 0.1757 0.0049  -0.0844 0.0119  160 VAL B O   
3562 C  CB  . VAL B 159 ? 0.3037 0.1160 0.1432 0.0399  -0.0679 0.0118  160 VAL B CB  
3563 C  CG1 . VAL B 159 ? 0.3226 0.1613 0.1604 0.0577  -0.0766 -0.0136 160 VAL B CG1 
3564 C  CG2 . VAL B 159 ? 0.3860 0.1473 0.1634 -0.0428 -0.1165 0.0394  160 VAL B CG2 
3565 N  N   . VAL B 160 ? 0.2799 0.0934 0.1534 0.0124  -0.0637 0.0125  161 VAL B N   
3566 C  CA  . VAL B 160 ? 0.3492 0.0874 0.1537 0.0087  -0.0344 -0.0041 161 VAL B CA  
3567 C  C   . VAL B 160 ? 0.3127 0.1135 0.1561 0.0120  -0.0350 0.0233  161 VAL B C   
3568 O  O   . VAL B 160 ? 0.3287 0.1322 0.1909 0.0395  -0.0182 0.0204  161 VAL B O   
3569 C  CB  . VAL B 160 ? 0.4471 0.1171 0.1780 0.0094  0.0076  0.0186  161 VAL B CB  
3570 C  CG1 . VAL B 160 ? 0.3578 0.1498 0.2524 0.0159  -0.0734 0.0394  161 VAL B CG1 
3571 C  CG2 . VAL B 160 ? 0.3425 0.1469 0.2134 -0.0285 -0.0357 0.0024  161 VAL B CG2 
3572 N  N   . ASP B 161 ? 0.3734 0.1536 0.1467 0.0414  -0.0850 0.0008  162 ASP B N   
3573 C  CA  . ASP B 161 ? 0.3709 0.2468 0.1656 0.0988  -0.0452 0.0414  162 ASP B CA  
3574 C  C   . ASP B 161 ? 0.2405 0.2398 0.1546 0.0476  -0.0834 0.0147  162 ASP B C   
3575 O  O   . ASP B 161 ? 0.5543 0.2951 0.1579 0.1377  -0.0170 0.0278  162 ASP B O   
3576 C  CB  . ASP B 161 ? 0.3955 0.2682 0.1961 0.1001  -0.1058 0.0164  162 ASP B CB  
3577 C  CG  . ASP B 161 ? 0.4609 0.2083 0.1679 0.0346  -0.0590 0.0406  162 ASP B CG  
3578 O  OD1 . ASP B 161 ? 0.3950 0.2978 0.3045 0.1001  -0.0579 0.0665  162 ASP B OD1 
3579 O  OD2 . ASP B 161 ? 0.4839 0.5655 0.2283 0.0381  -0.0921 0.0507  162 ASP B OD2 
3580 N  N   . VAL B 162 ? 0.3903 0.1469 0.1351 0.0527  -0.0899 -0.0098 163 VAL B N   
3581 C  CA  . VAL B 162 ? 0.4207 0.1650 0.1852 0.0511  -0.0873 -0.0335 163 VAL B CA  
3582 C  C   . VAL B 162 ? 0.4133 0.1376 0.1295 0.0209  -0.0288 -0.0161 163 VAL B C   
3583 O  O   . VAL B 162 ? 0.4589 0.1500 0.1301 0.0502  -0.0233 -0.0098 163 VAL B O   
3584 C  CB  . VAL B 162 ? 0.4767 0.1304 0.2266 0.0244  -0.0869 -0.0348 163 VAL B CB  
3585 C  CG1 . VAL B 162 ? 0.4388 0.1282 0.2092 0.0184  -0.0996 0.0051  163 VAL B CG1 
3586 C  CG2 . VAL B 162 ? 0.4370 0.1866 0.2340 0.0171  0.0020  -0.0339 163 VAL B CG2 
3587 N  N   . LEU B 163 ? 0.4530 0.1476 0.1449 0.0698  -0.0549 -0.0306 164 LEU B N   
3588 C  CA  . LEU B 163 ? 0.4011 0.1033 0.1491 0.0223  0.0172  -0.0258 164 LEU B CA  
3589 C  C   . LEU B 163 ? 0.4253 0.1631 0.1559 0.0253  0.0270  0.0046  164 LEU B C   
3590 O  O   . LEU B 163 ? 0.3948 0.1408 0.1510 0.0190  0.0318  -0.0171 164 LEU B O   
3591 C  CB  . LEU B 163 ? 0.3625 0.1081 0.1378 0.0450  -0.0059 -0.0082 164 LEU B CB  
3592 C  CG  . LEU B 163 ? 0.3140 0.1155 0.1243 0.0337  -0.0109 -0.0144 164 LEU B CG  
3593 C  CD1 . LEU B 163 ? 0.3416 0.1146 0.1580 0.0052  0.0181  -0.0359 164 LEU B CD1 
3594 C  CD2 . LEU B 163 ? 0.3285 0.1345 0.1196 0.0212  -0.0296 0.0098  164 LEU B CD2 
3595 N  N   . ASP B 164 ? 0.5056 0.1491 0.1371 0.0399  0.0114  0.0266  165 ASP B N   
3596 C  CA  . ASP B 164 ? 0.5471 0.1487 0.2062 0.0324  0.0493  0.0344  165 ASP B CA  
3597 C  C   . ASP B 164 ? 0.5950 0.2114 0.2014 0.0397  0.0847  0.0315  165 ASP B C   
3598 O  O   . ASP B 164 ? 0.6798 0.2606 0.2815 0.0222  0.1344  0.0160  165 ASP B O   
3599 C  CB  . ASP B 164 ? 0.7099 0.2405 0.2216 0.1010  0.0100  0.0579  165 ASP B CB  
3600 C  CG  . ASP B 164 ? 0.8054 0.3161 0.4056 0.2675  -0.1841 0.1103  165 ASP B CG  
3601 O  OD1 . ASP B 164 ? 0.5575 0.9284 0.3003 0.2083  -0.0562 0.0975  165 ASP B OD1 
3602 O  OD2 . ASP B 164 ? 1.1055 1.5478 0.5486 0.0750  -0.0562 0.5543  165 ASP B OD2 
3603 N  N   . SER B 165 ? 0.4776 0.2119 0.1180 0.0688  -0.0166 -0.0055 166 SER B N   
3604 C  CA  . SER B 165 ? 0.4573 0.2480 0.1277 0.0935  -0.0063 -0.0217 166 SER B CA  
3605 C  C   . SER B 165 ? 0.3944 0.1843 0.1176 0.0294  0.0142  -0.0163 166 SER B C   
3606 O  O   . SER B 165 ? 0.5353 0.1853 0.1392 0.0601  -0.0076 -0.0241 166 SER B O   
3607 C  CB  . SER B 165 ? 0.6266 0.2055 0.2112 0.0133  0.0635  -0.0447 166 SER B CB  
3608 O  OG  . SER B 165 ? 0.6675 0.1994 0.2146 0.0281  0.0494  -0.0298 166 SER B OG  
3609 N  N   . ILE B 166 ? 0.4262 0.1545 0.1229 0.0522  -0.0057 -0.0068 167 ILE B N   
3610 C  CA  . ILE B 166 ? 0.3677 0.1320 0.1525 0.0245  0.0078  -0.0122 167 ILE B CA  
3611 C  C   . ILE B 166 ? 0.2728 0.1595 0.1196 0.0287  0.0046  0.0223  167 ILE B C   
3612 O  O   . ILE B 166 ? 0.3447 0.1279 0.1394 0.0511  0.0397  -0.0118 167 ILE B O   
3613 C  CB  . ILE B 166 ? 0.4016 0.1168 0.1031 0.0529  -0.0097 0.0062  167 ILE B CB  
3614 C  CG1 . ILE B 166 ? 0.3501 0.1244 0.1281 0.0162  0.0080  -0.0043 167 ILE B CG1 
3615 C  CG2 . ILE B 166 ? 0.4815 0.0996 0.1480 0.0372  -0.0375 -0.0230 167 ILE B CG2 
3616 C  CD1 . ILE B 166 ? 0.2867 0.1432 0.1304 0.0368  0.0162  0.0185  167 ILE B CD1 
3617 N  N   . LYS B 167 ? 0.3508 0.1292 0.1645 0.0465  0.0452  -0.0024 168 LYS B N   
3618 C  CA  . LYS B 167 ? 0.2486 0.2064 0.1635 0.0076  0.0083  0.0507  168 LYS B CA  
3619 C  C   . LYS B 167 ? 0.2691 0.1748 0.1164 0.0292  0.0593  -0.0208 168 LYS B C   
3620 O  O   . LYS B 167 ? 0.3070 0.1295 0.1403 0.0597  0.0258  0.0197  168 LYS B O   
3621 C  CB  . LYS B 167 ? 0.3438 0.1541 0.1532 0.0324  -0.0049 0.0542  168 LYS B CB  
3622 C  CG  . LYS B 167 ? 0.3086 0.1703 0.1751 0.0291  0.0304  0.0359  168 LYS B CG  
3623 C  CD  . LYS B 167 ? 0.4882 0.2481 0.2425 -0.0315 -0.0714 0.1020  168 LYS B CD  
3624 C  CE  . LYS B 167 ? 0.4925 0.3418 0.3109 -0.0939 -0.0221 0.0771  168 LYS B CE  
3625 N  NZ  . LYS B 167 ? 0.4733 0.3140 0.4009 0.0866  0.0038  0.1288  168 LYS B NZ  
3626 N  N   . THR B 168 ? 0.3208 0.1498 0.1464 0.0612  0.0640  0.0076  169 THR B N   
3627 C  CA  . THR B 168 ? 0.3283 0.1495 0.1541 0.0472  0.0804  -0.0074 169 THR B CA  
3628 C  C   . THR B 168 ? 0.3160 0.1805 0.1272 0.0201  0.0661  -0.0229 169 THR B C   
3629 O  O   . THR B 168 ? 0.3619 0.1297 0.1848 0.0772  0.0544  -0.0109 169 THR B O   
3630 C  CB  . THR B 168 ? 0.3197 0.1925 0.1620 0.0540  0.0487  0.0412  169 THR B CB  
3631 O  OG1 . THR B 168 ? 0.4079 0.2269 0.1546 0.0666  0.0802  0.0083  169 THR B OG1 
3632 C  CG2 . THR B 168 ? 0.3878 0.1816 0.1932 0.0892  0.0684  0.0540  169 THR B CG2 
3633 N  N   A LYS B 169 ? 0.3700 0.1977 0.1615 0.1059  0.1237  0.0256  170 LYS B N   
3634 N  N   B LYS B 169 ? 0.3648 0.1996 0.1759 0.1070  0.1096  0.0252  170 LYS B N   
3635 C  CA  A LYS B 169 ? 0.3617 0.1683 0.1995 0.0405  0.0935  0.0164  170 LYS B CA  
3636 C  CA  B LYS B 169 ? 0.2949 0.1740 0.1931 0.0359  0.1027  0.0133  170 LYS B CA  
3637 C  C   A LYS B 169 ? 0.3086 0.2102 0.1495 0.0958  0.0665  -0.0241 170 LYS B C   
3638 C  C   B LYS B 169 ? 0.3258 0.2211 0.1532 0.0631  0.0734  -0.0249 170 LYS B C   
3639 O  O   A LYS B 169 ? 0.4925 0.2304 0.1537 0.1405  0.1086  0.0189  170 LYS B O   
3640 O  O   B LYS B 169 ? 0.3835 0.2204 0.1791 0.1277  0.0971  -0.0068 170 LYS B O   
3641 C  CB  A LYS B 169 ? 0.3310 0.1471 0.1573 0.0342  0.1118  0.0373  170 LYS B CB  
3642 C  CB  B LYS B 169 ? 0.3009 0.1543 0.1762 0.0234  0.0812  0.0104  170 LYS B CB  
3643 C  CG  A LYS B 169 ? 0.3079 0.1520 0.1913 0.0263  0.0527  0.0041  170 LYS B CG  
3644 C  CG  B LYS B 169 ? 0.4169 0.1800 0.2493 0.0469  -0.0308 -0.0131 170 LYS B CG  
3645 C  CD  A LYS B 169 ? 0.3574 0.1504 0.1331 0.0623  0.0489  0.0397  170 LYS B CD  
3646 C  CD  B LYS B 169 ? 0.3684 0.2372 0.2360 0.0551  0.0948  -0.0533 170 LYS B CD  
3647 C  CE  A LYS B 169 ? 0.1967 0.3587 0.2583 -0.1633 0.0203  -0.0621 170 LYS B CE  
3648 C  CE  B LYS B 169 ? 0.3163 0.2913 0.4797 -0.0068 -0.0203 0.0148  170 LYS B CE  
3649 N  NZ  A LYS B 169 ? 0.1949 0.4833 0.2391 -0.1915 -0.0142 0.0100  170 LYS B NZ  
3650 N  NZ  B LYS B 169 ? 0.3971 0.3433 0.5584 -0.1991 0.0094  -0.0203 170 LYS B NZ  
3651 N  N   . GLY B 170 ? 0.4083 0.1495 0.1744 0.1234  0.0639  -0.0081 171 GLY B N   
3652 C  CA  . GLY B 170 ? 0.2220 0.1322 0.2831 0.0697  0.0118  -0.0553 171 GLY B CA  
3653 C  C   . GLY B 170 ? 0.4165 0.1478 0.1762 0.0458  -0.0201 -0.0062 171 GLY B C   
3654 O  O   . GLY B 170 ? 0.5109 0.1191 0.3000 0.1072  -0.0104 -0.0604 171 GLY B O   
3655 N  N   . LYS B 171 ? 0.4070 0.0986 0.2186 0.0917  0.0869  -0.0307 172 LYS B N   
3656 C  CA  . LYS B 171 ? 0.4072 0.1501 0.1794 0.0233  0.0500  -0.0247 172 LYS B CA  
3657 C  C   . LYS B 171 ? 0.4257 0.1369 0.1374 0.0175  0.0549  -0.0386 172 LYS B C   
3658 O  O   . LYS B 171 ? 0.3657 0.1568 0.1378 0.0207  0.0439  -0.0434 172 LYS B O   
3659 C  CB  . LYS B 171 ? 0.4104 0.1755 0.1473 0.0670  0.0619  -0.0049 172 LYS B CB  
3660 C  CG  . LYS B 171 ? 0.4343 0.2146 0.2023 0.0802  0.0923  0.0518  172 LYS B CG  
3661 C  CD  . LYS B 171 ? 0.6133 0.2621 0.2949 0.1368  0.0693  0.0813  172 LYS B CD  
3662 C  CE  . LYS B 171 ? 0.6796 0.4392 0.2951 0.0966  0.0766  0.0518  172 LYS B CE  
3663 N  NZ  . LYS B 171 ? 0.6498 0.5034 0.3871 -0.1569 -0.0109 0.0062  172 LYS B NZ  
3664 N  N   . SER B 172 ? 0.4426 0.1520 0.1455 0.0538  0.0049  -0.0645 173 SER B N   
3665 C  CA  . SER B 172 ? 0.4456 0.1460 0.1823 0.0197  0.0608  -0.0154 173 SER B CA  
3666 C  C   . SER B 172 ? 0.3544 0.1656 0.1477 -0.0337 0.0228  -0.0559 173 SER B C   
3667 O  O   . SER B 172 ? 0.5382 0.2229 0.1196 -0.0679 0.0151  -0.0487 173 SER B O   
3668 C  CB  . SER B 172 ? 0.5716 0.1430 0.1870 0.0790  0.0920  -0.0240 173 SER B CB  
3669 O  OG  . SER B 172 ? 0.6503 0.1501 0.2391 -0.0143 0.1086  -0.0658 173 SER B OG  
3670 N  N   . ALA B 173 ? 0.4014 0.1924 0.1757 -0.1466 0.0027  -0.0041 174 ALA B N   
3671 C  CA  . ALA B 173 ? 0.4194 0.3210 0.1268 -0.1597 -0.0326 -0.1032 174 ALA B CA  
3672 C  C   . ALA B 173 ? 0.2384 0.2574 0.1826 -0.0781 -0.0758 -0.0046 174 ALA B C   
3673 O  O   . ALA B 173 ? 0.2908 0.2004 0.1367 -0.0715 -0.0269 -0.0212 174 ALA B O   
3674 C  CB  . ALA B 173 ? 0.5917 0.2696 0.1940 -0.2158 -0.0851 0.0483  174 ALA B CB  
3675 N  N   . ASP B 174 ? 0.4830 0.2976 0.1365 -0.1546 -0.0189 -0.0750 175 ASP B N   
3676 C  CA  . ASP B 174 ? 0.4933 0.2387 0.1353 -0.1300 0.0249  -0.0857 175 ASP B CA  
3677 C  C   . ASP B 174 ? 0.3774 0.1981 0.1608 -0.1000 -0.0487 -0.0260 175 ASP B C   
3678 O  O   . ASP B 174 ? 0.6376 0.2290 0.1613 -0.1430 -0.0176 0.0296  175 ASP B O   
3679 C  CB  . ASP B 174 ? 0.3472 0.4329 0.3052 -0.1062 0.0219  -0.1711 175 ASP B CB  
3680 C  CG  . ASP B 174 ? 0.5286 0.3163 0.4138 0.1644  0.0636  0.0750  175 ASP B CG  
3681 O  OD1 . ASP B 174 ? 0.6969 0.4569 0.3858 0.2727  -0.2129 -0.1331 175 ASP B OD1 
3682 O  OD2 . ASP B 174 ? 0.2596 0.7026 0.3885 0.0702  -0.0509 0.0227  175 ASP B OD2 
3683 N  N   . PHE B 175 ? 0.3865 0.1737 0.1534 -0.0588 -0.0091 0.0073  176 PHE B N   
3684 C  CA  . PHE B 175 ? 0.3989 0.1595 0.1552 -0.0623 -0.0472 -0.0310 176 PHE B CA  
3685 C  C   . PHE B 175 ? 0.4142 0.1096 0.1777 -0.0560 -0.0970 0.0005  176 PHE B C   
3686 O  O   . PHE B 175 ? 0.4560 0.2082 0.1647 -0.0727 -0.1396 0.0188  176 PHE B O   
3687 C  CB  . PHE B 175 ? 0.4729 0.1477 0.1631 -0.0593 -0.0626 -0.0447 176 PHE B CB  
3688 C  CG  . PHE B 175 ? 0.4546 0.1063 0.1686 -0.0595 -0.0645 -0.0028 176 PHE B CG  
3689 C  CD1 . PHE B 175 ? 0.4334 0.1328 0.1945 -0.0255 -0.0326 0.0175  176 PHE B CD1 
3690 C  CD2 . PHE B 175 ? 0.4682 0.1583 0.1656 -0.0562 -0.0992 -0.0310 176 PHE B CD2 
3691 C  CE1 . PHE B 175 ? 0.5346 0.1133 0.2145 -0.0185 -0.0203 0.0324  176 PHE B CE1 
3692 C  CE2 . PHE B 175 ? 0.4282 0.1185 0.1986 -0.0662 -0.1037 -0.0116 176 PHE B CE2 
3693 C  CZ  . PHE B 175 ? 0.4406 0.1225 0.2190 -0.0447 -0.1011 0.0178  176 PHE B CZ  
3694 N  N   . THR B 176 ? 0.3833 0.1720 0.1190 -0.0275 -0.0785 -0.0288 177 THR B N   
3695 C  CA  . THR B 176 ? 0.3941 0.1174 0.1650 -0.0520 -0.0694 -0.0388 177 THR B CA  
3696 C  C   . THR B 176 ? 0.3643 0.1099 0.1289 -0.0120 -0.0905 -0.0496 177 THR B C   
3697 O  O   . THR B 176 ? 0.4122 0.1140 0.1674 0.0098  -0.0895 -0.0273 177 THR B O   
3698 C  CB  . THR B 176 ? 0.4040 0.1412 0.1676 0.0164  -0.1150 -0.0524 177 THR B CB  
3699 O  OG1 . THR B 176 ? 0.5278 0.1906 0.1581 -0.0672 -0.1132 -0.0430 177 THR B OG1 
3700 C  CG2 . THR B 176 ? 0.4023 0.2121 0.3614 -0.0087 -0.1710 -0.1466 177 THR B CG2 
3701 N  N   . ASN B 177 ? 0.3531 0.1534 0.1307 -0.0318 -0.0986 -0.0192 178 ASN B N   
3702 C  CA  . ASN B 177 ? 0.3722 0.1606 0.1656 0.0297  -0.1083 -0.0571 178 ASN B CA  
3703 C  C   . ASN B 177 ? 0.3725 0.1509 0.1509 -0.0189 -0.0841 -0.0419 178 ASN B C   
3704 O  O   . ASN B 177 ? 0.4735 0.1859 0.3161 0.0373  -0.2105 -0.1273 178 ASN B O   
3705 C  CB  . ASN B 177 ? 0.3343 0.1336 0.2297 0.0184  -0.1326 -0.0614 178 ASN B CB  
3706 C  CG  . ASN B 177 ? 0.3185 0.1798 0.1861 -0.0322 -0.0878 -0.0491 178 ASN B CG  
3707 O  OD1 . ASN B 177 ? 0.4871 0.1553 0.2435 -0.0667 -0.0502 -0.0335 178 ASN B OD1 
3708 N  ND2 . ASN B 177 ? 0.3296 0.1401 0.1916 0.0219  -0.1333 -0.0478 178 ASN B ND2 
3709 N  N   . PHE B 178 ? 0.3700 0.1081 0.1403 -0.0251 -0.1046 -0.0253 179 PHE B N   
3710 C  CA  . PHE B 178 ? 0.4113 0.1180 0.1256 0.0469  -0.0697 -0.0430 179 PHE B CA  
3711 C  C   . PHE B 178 ? 0.2610 0.0914 0.1421 -0.0010 -0.0767 -0.0244 179 PHE B C   
3712 O  O   . PHE B 178 ? 0.3307 0.1129 0.1453 0.0241  -0.0834 -0.0163 179 PHE B O   
3713 C  CB  . PHE B 178 ? 0.4099 0.1042 0.1611 -0.0281 -0.0498 -0.0417 179 PHE B CB  
3714 C  CG  . PHE B 178 ? 0.3210 0.1011 0.1428 -0.0144 -0.0294 -0.0399 179 PHE B CG  
3715 C  CD1 . PHE B 178 ? 0.3813 0.1009 0.1654 -0.0362 -0.0741 -0.0221 179 PHE B CD1 
3716 C  CD2 . PHE B 178 ? 0.3075 0.1209 0.1468 0.0038  -0.0452 -0.0370 179 PHE B CD2 
3717 C  CE1 . PHE B 178 ? 0.4383 0.1288 0.1785 -0.0007 -0.0980 -0.0443 179 PHE B CE1 
3718 C  CE2 . PHE B 178 ? 0.2407 0.1172 0.1547 0.0179  -0.0498 -0.0355 179 PHE B CE2 
3719 C  CZ  . PHE B 178 ? 0.3332 0.1018 0.1730 -0.0137 -0.0626 -0.0408 179 PHE B CZ  
3720 N  N   . ASP B 179 ? 0.2680 0.1223 0.1704 0.0000  -0.0925 -0.0320 180 ASP B N   
3721 C  CA  . ASP B 179 ? 0.2509 0.1897 0.1705 -0.0408 -0.0900 -0.0178 180 ASP B CA  
3722 C  C   . ASP B 179 ? 0.2408 0.1101 0.1617 -0.0121 -0.0617 -0.0076 180 ASP B C   
3723 O  O   . ASP B 179 ? 0.2432 0.1077 0.1703 -0.0046 -0.0744 -0.0108 180 ASP B O   
3724 C  CB  . ASP B 179 ? 0.2617 0.1782 0.2304 -0.0261 -0.1341 -0.0320 180 ASP B CB  
3725 C  CG  . ASP B 179 ? 0.2222 0.2342 0.2648 -0.0581 -0.1112 -0.0712 180 ASP B CG  
3726 O  OD1 . ASP B 179 ? 0.2513 0.1553 0.2466 -0.0259 -0.0948 -0.0388 180 ASP B OD1 
3727 O  OD2 . ASP B 179 ? 0.1992 0.4329 0.3889 -0.0043 -0.1406 -0.0885 180 ASP B OD2 
3728 N  N   . PRO B 180 ? 0.2096 0.1058 0.1482 -0.0060 -0.0549 -0.0182 181 PRO B N   
3729 C  CA  . PRO B 180 ? 0.1771 0.1247 0.1638 -0.0001 -0.0644 -0.0335 181 PRO B CA  
3730 C  C   . PRO B 180 ? 0.1977 0.1171 0.1255 -0.0030 -0.0590 -0.0070 181 PRO B C   
3731 O  O   . PRO B 180 ? 0.1739 0.1239 0.1459 -0.0068 -0.0504 -0.0247 181 PRO B O   
3732 C  CB  . PRO B 180 ? 0.1636 0.1580 0.1933 0.0037  -0.0715 -0.0071 181 PRO B CB  
3733 C  CG  . PRO B 180 ? 0.1900 0.1473 0.1756 0.0199  -0.0784 -0.0099 181 PRO B CG  
3734 C  CD  . PRO B 180 ? 0.2365 0.1180 0.1552 0.0107  -0.0807 -0.0238 181 PRO B CD  
3735 N  N   . ARG B 181 ? 0.1592 0.1356 0.1584 -0.0126 -0.0549 -0.0317 182 ARG B N   
3736 C  CA  . ARG B 181 ? 0.1532 0.1344 0.1895 0.0121  -0.0307 -0.0065 182 ARG B CA  
3737 C  C   . ARG B 181 ? 0.1857 0.1491 0.2035 -0.0198 -0.1005 -0.0340 182 ARG B C   
3738 O  O   . ARG B 181 ? 0.1766 0.1498 0.2207 0.0024  -0.0599 -0.0271 182 ARG B O   
3739 C  CB  . ARG B 181 ? 0.1669 0.1474 0.2181 -0.0113 -0.0540 -0.0125 182 ARG B CB  
3740 C  CG  . ARG B 181 ? 0.1794 0.1383 0.2741 -0.0049 -0.0253 0.0055  182 ARG B CG  
3741 C  CD  . ARG B 181 ? 0.1618 0.2195 0.3379 -0.0366 -0.0199 -0.0373 182 ARG B CD  
3742 N  NE  . ARG B 181 ? 0.2143 0.1866 0.3623 0.0082  -0.0518 -0.0851 182 ARG B NE  
3743 C  CZ  . ARG B 181 ? 0.1641 0.3774 0.3625 -0.0458 0.0186  -0.1345 182 ARG B CZ  
3744 N  NH1 . ARG B 181 ? 0.1818 0.3759 0.5070 -0.0432 0.1006  -0.1588 182 ARG B NH1 
3745 N  NH2 . ARG B 181 ? 0.2347 0.4302 0.4147 -0.0555 -0.0421 -0.1621 182 ARG B NH2 
3746 N  N   . GLY B 182 ? 0.2046 0.1471 0.1922 -0.0141 -0.0996 -0.0172 183 GLY B N   
3747 C  CA  . GLY B 182 ? 0.2736 0.1203 0.2119 -0.0027 -0.1133 -0.0261 183 GLY B CA  
3748 C  C   . GLY B 182 ? 0.2842 0.1218 0.1837 -0.0007 -0.1074 -0.0144 183 GLY B C   
3749 O  O   . GLY B 182 ? 0.3452 0.1151 0.2527 0.0000  -0.1369 -0.0015 183 GLY B O   
3750 N  N   . LEU B 183 ? 0.2245 0.1286 0.1468 -0.0076 -0.0700 0.0000  184 LEU B N   
3751 C  CA  . LEU B 183 ? 0.2046 0.1159 0.1632 -0.0173 -0.0873 0.0005  184 LEU B CA  
3752 C  C   . LEU B 183 ? 0.1805 0.1349 0.1570 0.0007  -0.0747 -0.0040 184 LEU B C   
3753 O  O   . LEU B 183 ? 0.1766 0.1518 0.1764 -0.0197 -0.0590 -0.0252 184 LEU B O   
3754 C  CB  . LEU B 183 ? 0.1841 0.1528 0.1557 -0.0164 -0.0423 -0.0143 184 LEU B CB  
3755 C  CG  . LEU B 183 ? 0.2761 0.1401 0.1640 -0.0416 -0.0662 -0.0006 184 LEU B CG  
3756 C  CD1 . LEU B 183 ? 0.2870 0.2768 0.1500 -0.0163 -0.0684 -0.0676 184 LEU B CD1 
3757 C  CD2 . LEU B 183 ? 0.3564 0.1773 0.1801 -0.0586 -0.0361 0.0198  184 LEU B CD2 
3758 N  N   . LEU B 184 ? 0.2168 0.1160 0.1740 -0.0293 -0.0511 -0.0234 185 LEU B N   
3759 C  CA  . LEU B 184 ? 0.1523 0.1235 0.1690 0.0195  -0.0540 -0.0315 185 LEU B CA  
3760 C  C   . LEU B 184 ? 0.2195 0.1440 0.1884 0.0672  -0.0841 -0.0465 185 LEU B C   
3761 O  O   . LEU B 184 ? 0.3120 0.2038 0.3382 0.1370  -0.2320 -0.1229 185 LEU B O   
3762 C  CB  . LEU B 184 ? 0.1067 0.1295 0.1974 0.0175  -0.0546 -0.0263 185 LEU B CB  
3763 C  CG  . LEU B 184 ? 0.1049 0.1352 0.1791 0.0003  -0.0206 -0.0175 185 LEU B CG  
3764 C  CD1 . LEU B 184 ? 0.1918 0.1398 0.1807 -0.0104 -0.0263 -0.0015 185 LEU B CD1 
3765 C  CD2 . LEU B 184 ? 0.1023 0.1631 0.2211 0.0253  -0.0355 -0.0390 185 LEU B CD2 
3766 N  N   . PRO B 185 ? 0.1232 0.1383 0.1759 0.0368  -0.0590 -0.0328 186 PRO B N   
3767 C  CA  . PRO B 185 ? 0.1547 0.1338 0.1949 0.0219  -0.0403 -0.0546 186 PRO B CA  
3768 C  C   . PRO B 185 ? 0.1126 0.1239 0.2489 0.0230  -0.0800 -0.0351 186 PRO B C   
3769 O  O   . PRO B 185 ? 0.1049 0.1345 0.3768 0.0066  -0.0680 -0.0573 186 PRO B O   
3770 C  CB  . PRO B 185 ? 0.1168 0.1378 0.2100 0.0019  -0.0329 -0.0258 186 PRO B CB  
3771 C  CG  . PRO B 185 ? 0.1065 0.1514 0.1600 0.0017  -0.0222 -0.0130 186 PRO B CG  
3772 C  CD  . PRO B 185 ? 0.1008 0.1283 0.1483 -0.0126 -0.0344 -0.0131 186 PRO B CD  
3773 N  N   A GLU B 186 ? 0.1246 0.1383 0.2757 0.0285  -0.0634 -0.0531 187 GLU B N   
3774 N  N   B GLU B 186 ? 0.1371 0.1416 0.2653 0.0436  -0.0667 -0.0273 187 GLU B N   
3775 C  CA  A GLU B 186 ? 0.1038 0.1564 0.2800 0.0627  -0.0649 -0.0454 187 GLU B CA  
3776 C  CA  B GLU B 186 ? 0.1358 0.1416 0.3009 0.0006  -0.0577 -0.0524 187 GLU B CA  
3777 C  C   A GLU B 186 ? 0.0829 0.1478 0.3149 0.0148  -0.0485 -0.0098 187 GLU B C   
3778 C  C   B GLU B 186 ? 0.0816 0.1342 0.3183 0.0082  -0.0239 -0.0381 187 GLU B C   
3779 O  O   A GLU B 186 ? 0.2231 0.2028 0.4004 -0.0737 -0.0454 -0.0081 187 GLU B O   
3780 O  O   B GLU B 186 ? 0.0474 0.1564 0.3395 0.0026  -0.0164 -0.0182 187 GLU B O   
3781 C  CB  A GLU B 186 ? 0.1703 0.1871 0.3118 0.1044  -0.0891 -0.1027 187 GLU B CB  
3782 C  CB  B GLU B 186 ? 0.1622 0.1805 0.3752 0.0701  -0.1251 -0.0452 187 GLU B CB  
3783 C  CG  A GLU B 186 ? 0.1316 0.2279 0.4347 0.0331  -0.0732 -0.0482 187 GLU B CG  
3784 C  CG  B GLU B 186 ? 0.0927 0.1940 0.3774 0.0614  -0.0943 -0.0065 187 GLU B CG  
3785 C  CD  A GLU B 186 ? 0.1835 0.2960 0.4675 0.0952  -0.0465 -0.0601 187 GLU B CD  
3786 C  CD  B GLU B 186 ? 0.1852 0.2389 0.3285 0.1286  -0.0720 -0.0126 187 GLU B CD  
3787 O  OE1 A GLU B 186 ? 0.1450 0.2495 0.5098 0.0222  -0.0595 -0.0631 187 GLU B OE1 
3788 O  OE1 B GLU B 186 ? 0.2703 0.2294 0.3510 0.0564  -0.0140 -0.0375 187 GLU B OE1 
3789 O  OE2 A GLU B 186 ? 0.2434 0.2231 0.5877 -0.0082 0.1121  -0.1233 187 GLU B OE2 
3790 O  OE2 B GLU B 186 ? 0.2466 0.2705 0.4481 0.0834  -0.1337 0.0493  187 GLU B OE2 
3791 N  N   . SER B 187 ? 0.0690 0.1571 0.2815 0.0251  -0.0238 -0.0201 188 SER B N   
3792 C  CA  . SER B 187 ? 0.0939 0.1489 0.2770 0.0104  0.0031  -0.0293 188 SER B CA  
3793 C  C   . SER B 187 ? 0.0776 0.1579 0.2390 0.0131  -0.0138 -0.0263 188 SER B C   
3794 O  O   . SER B 187 ? 0.0907 0.1717 0.2506 0.0175  0.0000  -0.0083 188 SER B O   
3795 C  CB  . SER B 187 ? 0.1408 0.1801 0.2655 0.0421  -0.0103 -0.0322 188 SER B CB  
3796 O  OG  . SER B 187 ? 0.1159 0.1807 0.2624 0.0274  -0.0104 -0.0255 188 SER B OG  
3797 N  N   . LEU B 188 ? 0.0820 0.1486 0.2392 0.0222  -0.0104 -0.0113 189 LEU B N   
3798 C  CA  . LEU B 188 ? 0.0979 0.1493 0.2414 0.0088  -0.0212 -0.0157 189 LEU B CA  
3799 C  C   . LEU B 188 ? 0.0873 0.1292 0.2196 0.0046  -0.0020 0.0182  189 LEU B C   
3800 O  O   . LEU B 188 ? 0.1232 0.1622 0.2047 0.0015  -0.0160 0.0285  189 LEU B O   
3801 C  CB  . LEU B 188 ? 0.1045 0.1750 0.2425 0.0035  -0.0263 -0.0168 189 LEU B CB  
3802 C  CG  . LEU B 188 ? 0.1178 0.2166 0.2865 0.0068  0.0038  -0.0843 189 LEU B CG  
3803 C  CD1 . LEU B 188 ? 0.1726 0.1816 0.3871 0.0478  -0.0137 -0.0797 189 LEU B CD1 
3804 C  CD2 . LEU B 188 ? 0.1172 0.2858 0.2469 -0.0063 -0.0245 -0.0869 189 LEU B CD2 
3805 N  N   . ASP B 189 ? 0.0873 0.1686 0.1877 -0.0087 -0.0007 0.0130  190 ASP B N   
3806 C  CA  . ASP B 189 ? 0.0957 0.1688 0.1827 0.0228  0.0255  -0.0063 190 ASP B CA  
3807 C  C   . ASP B 189 ? 0.1072 0.1193 0.1555 0.0277  0.0183  0.0035  190 ASP B C   
3808 O  O   . ASP B 189 ? 0.0907 0.1349 0.1474 0.0052  0.0003  0.0010  190 ASP B O   
3809 C  CB  . ASP B 189 ? 0.1516 0.2092 0.2177 0.0860  0.0505  -0.0236 190 ASP B CB  
3810 C  CG  . ASP B 189 ? 0.1818 0.3921 0.2222 0.0662  0.0524  -0.0054 190 ASP B CG  
3811 O  OD1 . ASP B 189 ? 0.1696 0.4533 0.3217 0.1124  0.0975  0.0668  190 ASP B OD1 
3812 O  OD2 . ASP B 189 ? 0.1703 0.6098 0.3305 0.1495  0.0030  -0.1447 190 ASP B OD2 
3813 N  N   . TYR B 190 ? 0.0995 0.1424 0.1369 0.0183  0.0153  -0.0195 191 TYR B N   
3814 C  CA  . TYR B 190 ? 0.0878 0.1421 0.1203 0.0212  0.0028  -0.0174 191 TYR B CA  
3815 C  C   . TYR B 190 ? 0.1133 0.1083 0.1076 0.0060  0.0252  -0.0189 191 TYR B C   
3816 O  O   . TYR B 190 ? 0.1226 0.1354 0.1065 0.0020  0.0185  -0.0063 191 TYR B O   
3817 C  CB  . TYR B 190 ? 0.1140 0.1169 0.1220 0.0142  0.0041  -0.0116 191 TYR B CB  
3818 C  CG  . TYR B 190 ? 0.1009 0.1426 0.1203 0.0182  -0.0005 -0.0206 191 TYR B CG  
3819 C  CD1 . TYR B 190 ? 0.1180 0.1319 0.1406 0.0233  0.0102  -0.0144 191 TYR B CD1 
3820 C  CD2 . TYR B 190 ? 0.1205 0.1349 0.1441 -0.0037 0.0241  -0.0181 191 TYR B CD2 
3821 C  CE1 . TYR B 190 ? 0.1318 0.1430 0.1507 0.0003  0.0063  -0.0138 191 TYR B CE1 
3822 C  CE2 . TYR B 190 ? 0.1239 0.1543 0.1747 0.0204  -0.0035 -0.0078 191 TYR B CE2 
3823 C  CZ  . TYR B 190 ? 0.1380 0.1223 0.1500 0.0065  0.0109  0.0010  191 TYR B CZ  
3824 O  OH  . TYR B 190 ? 0.1649 0.1545 0.1756 -0.0087 0.0063  0.0163  191 TYR B OH  
3825 N  N   . TRP B 191 ? 0.1020 0.0953 0.1137 0.0196  -0.0021 -0.0074 192 TRP B N   
3826 C  CA  . TRP B 191 ? 0.1090 0.0882 0.1117 0.0065  -0.0015 -0.0138 192 TRP B CA  
3827 C  C   . TRP B 191 ? 0.0957 0.1011 0.0934 0.0098  0.0065  0.0093  192 TRP B C   
3828 O  O   . TRP B 191 ? 0.1169 0.1241 0.0977 0.0164  0.0066  -0.0003 192 TRP B O   
3829 C  CB  . TRP B 191 ? 0.1045 0.0986 0.1168 0.0076  0.0031  -0.0019 192 TRP B CB  
3830 C  CG  . TRP B 191 ? 0.1298 0.1020 0.1108 0.0023  -0.0044 -0.0148 192 TRP B CG  
3831 C  CD1 . TRP B 191 ? 0.1446 0.1110 0.1212 -0.0205 0.0055  -0.0048 192 TRP B CD1 
3832 C  CD2 . TRP B 191 ? 0.0905 0.1186 0.1378 0.0010  0.0054  -0.0087 192 TRP B CD2 
3833 N  NE1 . TRP B 191 ? 0.1762 0.1151 0.1505 0.0046  0.0187  -0.0164 192 TRP B NE1 
3834 C  CE2 . TRP B 191 ? 0.1298 0.1270 0.1502 0.0031  -0.0068 -0.0114 192 TRP B CE2 
3835 C  CE3 . TRP B 191 ? 0.0926 0.1404 0.1304 -0.0148 -0.0085 0.0031  192 TRP B CE3 
3836 C  CZ2 . TRP B 191 ? 0.1333 0.1041 0.1798 0.0015  -0.0049 -0.0104 192 TRP B CZ2 
3837 C  CZ3 . TRP B 191 ? 0.0776 0.1365 0.1796 0.0012  0.0028  0.0168  192 TRP B CZ3 
3838 C  CH2 . TRP B 191 ? 0.1093 0.1381 0.1882 0.0023  -0.0046 0.0124  192 TRP B CH2 
3839 N  N   . THR B 192 ? 0.0905 0.0968 0.0997 0.0070  -0.0026 -0.0048 193 THR B N   
3840 C  CA  . THR B 192 ? 0.1036 0.0984 0.1047 0.0121  -0.0049 0.0028  193 THR B CA  
3841 C  C   . THR B 192 ? 0.0920 0.1115 0.0974 -0.0133 0.0083  -0.0063 193 THR B C   
3842 O  O   . THR B 192 ? 0.1140 0.1292 0.0883 0.0137  0.0074  -0.0026 193 THR B O   
3843 C  CB  . THR B 192 ? 0.1223 0.0907 0.1068 0.0065  0.0071  -0.0070 193 THR B CB  
3844 O  OG1 . THR B 192 ? 0.1050 0.0973 0.1133 -0.0077 0.0013  -0.0019 193 THR B OG1 
3845 C  CG2 . THR B 192 ? 0.1155 0.1252 0.1133 -0.0198 0.0120  -0.0080 193 THR B CG2 
3846 N  N   . TYR B 193 ? 0.0865 0.0988 0.0920 0.0019  -0.0142 0.0046  194 TYR B N   
3847 C  CA  . TYR B 193 ? 0.1090 0.1090 0.0877 -0.0074 -0.0240 -0.0054 194 TYR B CA  
3848 C  C   . TYR B 193 ? 0.0696 0.1068 0.1018 0.0013  -0.0107 0.0006  194 TYR B C   
3849 O  O   . TYR B 193 ? 0.0907 0.1038 0.0989 -0.0046 -0.0133 -0.0076 194 TYR B O   
3850 C  CB  . TYR B 193 ? 0.1133 0.1083 0.1006 -0.0204 -0.0198 0.0051  194 TYR B CB  
3851 C  CG  . TYR B 193 ? 0.0984 0.0842 0.1074 -0.0167 -0.0239 -0.0071 194 TYR B CG  
3852 C  CD1 . TYR B 193 ? 0.1146 0.0825 0.0970 -0.0130 -0.0183 -0.0027 194 TYR B CD1 
3853 C  CD2 . TYR B 193 ? 0.0991 0.0971 0.1141 -0.0221 -0.0266 0.0127  194 TYR B CD2 
3854 C  CE1 . TYR B 193 ? 0.0847 0.0838 0.1162 0.0031  -0.0214 0.0017  194 TYR B CE1 
3855 C  CE2 . TYR B 193 ? 0.1090 0.0842 0.1198 -0.0216 -0.0302 0.0027  194 TYR B CE2 
3856 C  CZ  . TYR B 193 ? 0.0843 0.0771 0.1058 -0.0263 -0.0231 -0.0030 194 TYR B CZ  
3857 O  OH  . TYR B 193 ? 0.0904 0.0930 0.1074 0.0000  -0.0099 0.0062  194 TYR B OH  
3858 N  N   . PRO B 194 ? 0.0932 0.1081 0.0873 0.0003  -0.0146 0.0102  195 PRO B N   
3859 C  CA  . PRO B 194 ? 0.0991 0.0939 0.1214 -0.0037 0.0024  0.0251  195 PRO B CA  
3860 C  C   . PRO B 194 ? 0.0790 0.0878 0.1022 -0.0068 -0.0241 0.0136  195 PRO B C   
3861 O  O   . PRO B 194 ? 0.1159 0.1171 0.1081 -0.0304 -0.0209 0.0034  195 PRO B O   
3862 C  CB  . PRO B 194 ? 0.1309 0.1379 0.1123 0.0035  -0.0057 0.0228  195 PRO B CB  
3863 C  CG  . PRO B 194 ? 0.1371 0.1473 0.1234 0.0156  -0.0137 0.0129  195 PRO B CG  
3864 C  CD  . PRO B 194 ? 0.1425 0.1495 0.1018 0.0280  -0.0115 0.0057  195 PRO B CD  
3865 N  N   . GLY B 195 ? 0.0889 0.0859 0.0956 -0.0070 -0.0137 0.0194  196 GLY B N   
3866 C  CA  . GLY B 195 ? 0.0920 0.0945 0.1072 -0.0019 -0.0174 0.0027  196 GLY B CA  
3867 C  C   . GLY B 195 ? 0.0834 0.0855 0.1022 -0.0021 -0.0207 0.0114  196 GLY B C   
3868 O  O   . GLY B 195 ? 0.1017 0.0806 0.1110 0.0007  -0.0114 0.0167  196 GLY B O   
3869 N  N   . SER B 196 ? 0.0741 0.0869 0.1009 -0.0001 -0.0179 0.0043  197 SER B N   
3870 C  CA  . SER B 196 ? 0.0729 0.0914 0.1207 0.0028  -0.0071 0.0144  197 SER B CA  
3871 C  C   . SER B 196 ? 0.0729 0.0822 0.1121 0.0111  -0.0141 0.0071  197 SER B C   
3872 O  O   . SER B 196 ? 0.0718 0.0860 0.1211 0.0027  -0.0086 0.0103  197 SER B O   
3873 C  CB  . SER B 196 ? 0.0775 0.0923 0.1381 0.0096  -0.0242 0.0263  197 SER B CB  
3874 O  OG  . SER B 196 ? 0.0710 0.0909 0.1324 -0.0005 -0.0115 0.0076  197 SER B OG  
3875 N  N   . LEU B 197 ? 0.0692 0.0938 0.1076 -0.0046 0.0030  0.0131  198 LEU B N   
3876 C  CA  . LEU B 197 ? 0.0863 0.0798 0.1085 0.0146  0.0063  0.0143  198 LEU B CA  
3877 C  C   . LEU B 197 ? 0.0639 0.0834 0.1280 0.0197  0.0010  0.0211  198 LEU B C   
3878 O  O   . LEU B 197 ? 0.0790 0.1013 0.1328 0.0176  -0.0024 0.0281  198 LEU B O   
3879 C  CB  . LEU B 197 ? 0.0870 0.1054 0.1250 0.0110  -0.0060 -0.0001 198 LEU B CB  
3880 C  CG  . LEU B 197 ? 0.1108 0.0886 0.1315 0.0183  0.0003  0.0015  198 LEU B CG  
3881 C  CD1 . LEU B 197 ? 0.1167 0.1164 0.1766 0.0231  0.0040  0.0010  198 LEU B CD1 
3882 C  CD2 . LEU B 197 ? 0.1103 0.1328 0.1967 0.0074  0.0252  -0.0353 198 LEU B CD2 
3883 N  N   . THR B 198 ? 0.0731 0.0883 0.1114 0.0074  -0.0012 0.0207  199 THR B N   
3884 C  CA  . THR B 198 ? 0.0938 0.0755 0.1532 0.0087  0.0038  0.0188  199 THR B CA  
3885 C  C   . THR B 198 ? 0.0693 0.1031 0.1360 0.0065  -0.0104 0.0066  199 THR B C   
3886 O  O   . THR B 198 ? 0.0724 0.0965 0.1521 0.0003  0.0049  0.0104  199 THR B O   
3887 C  CB  . THR B 198 ? 0.0847 0.0810 0.1351 0.0104  -0.0060 0.0131  199 THR B CB  
3888 O  OG1 . THR B 198 ? 0.0993 0.0896 0.1067 0.0143  -0.0024 0.0080  199 THR B OG1 
3889 C  CG2 . THR B 198 ? 0.0886 0.1225 0.1221 0.0120  0.0074  0.0093  199 THR B CG2 
3890 N  N   . THR B 199 ? 0.1054 0.1108 0.1381 0.0197  0.0179  0.0155  200 THR B N   
3891 C  CA  . THR B 199 ? 0.0898 0.1083 0.1474 0.0216  0.0111  0.0239  200 THR B CA  
3892 C  C   . THR B 199 ? 0.0881 0.1130 0.1622 0.0164  0.0170  0.0242  200 THR B C   
3893 O  O   . THR B 199 ? 0.0900 0.1014 0.1755 0.0201  0.0073  0.0361  200 THR B O   
3894 C  CB  . THR B 199 ? 0.0925 0.1180 0.1543 0.0087  0.0093  0.0103  200 THR B CB  
3895 O  OG1 . THR B 199 ? 0.2080 0.1645 0.1704 -0.0570 -0.0060 0.0229  200 THR B OG1 
3896 C  CG2 . THR B 199 ? 0.1659 0.1583 0.1591 0.0635  0.0046  0.0131  200 THR B CG2 
3897 N  N   . PRO B 200 ? 0.0970 0.1158 0.1780 0.0217  0.0240  0.0249  201 PRO B N   
3898 C  CA  . PRO B 200 ? 0.0977 0.1437 0.1658 0.0423  0.0206  0.0026  201 PRO B CA  
3899 C  C   . PRO B 200 ? 0.1317 0.1394 0.1726 0.0237  0.0221  0.0137  201 PRO B C   
3900 O  O   . PRO B 200 ? 0.1398 0.1564 0.1778 0.0351  0.0118  0.0166  201 PRO B O   
3901 C  CB  . PRO B 200 ? 0.1090 0.1600 0.2238 0.0258  0.0225  0.0168  201 PRO B CB  
3902 C  CG  . PRO B 200 ? 0.0811 0.1704 0.1915 0.0138  0.0153  0.0129  201 PRO B CG  
3903 C  CD  . PRO B 200 ? 0.0861 0.1378 0.1932 0.0164  0.0318  0.0285  201 PRO B CD  
3904 N  N   . PRO B 201 ? 0.1081 0.1444 0.1581 0.0186  0.0153  0.0126  202 PRO B N   
3905 C  CA  . PRO B 201 ? 0.1478 0.1142 0.1589 0.0430  0.0153  0.0098  202 PRO B CA  
3906 C  C   . PRO B 201 ? 0.0838 0.1423 0.1550 0.0234  0.0028  -0.0043 202 PRO B C   
3907 O  O   . PRO B 201 ? 0.1014 0.1223 0.1934 0.0287  0.0071  0.0082  202 PRO B O   
3908 C  CB  . PRO B 201 ? 0.1413 0.1169 0.2426 0.0357  0.0227  -0.0162 202 PRO B CB  
3909 C  CG  . PRO B 201 ? 0.1441 0.1250 0.2213 0.0152  0.0048  0.0074  202 PRO B CG  
3910 C  CD  . PRO B 201 ? 0.1336 0.1265 0.1611 0.0026  0.0089  0.0013  202 PRO B CD  
3911 N  N   . LEU B 202 ? 0.0816 0.1005 0.1464 0.0110  0.0089  0.0017  203 LEU B N   
3912 C  CA  . LEU B 202 ? 0.0865 0.1077 0.1403 0.0153  -0.0078 0.0182  203 LEU B CA  
3913 C  C   . LEU B 202 ? 0.0851 0.0977 0.1410 0.0249  -0.0143 0.0038  203 LEU B C   
3914 O  O   . LEU B 202 ? 0.0850 0.0995 0.1448 0.0035  -0.0199 0.0136  203 LEU B O   
3915 C  CB  . LEU B 202 ? 0.0741 0.1211 0.1852 0.0041  -0.0176 0.0357  203 LEU B CB  
3916 C  CG  . LEU B 202 ? 0.0640 0.1065 0.1886 0.0031  0.0000  0.0266  203 LEU B CG  
3917 C  CD1 . LEU B 202 ? 0.0719 0.1581 0.2504 -0.0030 -0.0087 0.0540  203 LEU B CD1 
3918 C  CD2 . LEU B 202 ? 0.0753 0.1171 0.1897 0.0129  -0.0143 0.0242  203 LEU B CD2 
3919 N  N   . LEU B 203 ? 0.0979 0.0868 0.1692 0.0076  -0.0026 0.0152  204 LEU B N   
3920 C  CA  . LEU B 203 ? 0.0804 0.0872 0.1652 0.0054  -0.0096 0.0207  204 LEU B CA  
3921 C  C   . LEU B 203 ? 0.0834 0.0778 0.1615 0.0107  -0.0115 0.0200  204 LEU B C   
3922 O  O   . LEU B 203 ? 0.0934 0.0989 0.1439 0.0130  -0.0192 0.0275  204 LEU B O   
3923 C  CB  . LEU B 203 ? 0.1076 0.0907 0.1830 0.0023  0.0059  0.0023  204 LEU B CB  
3924 C  CG  . LEU B 203 ? 0.1351 0.1223 0.1805 -0.0070 0.0189  0.0085  204 LEU B CG  
3925 C  CD1 . LEU B 203 ? 0.1389 0.1177 0.2498 0.0043  0.0294  -0.0259 204 LEU B CD1 
3926 C  CD2 . LEU B 203 ? 0.1403 0.1617 0.2824 0.0790  0.0099  -0.0041 204 LEU B CD2 
3927 N  N   . GLU B 204 ? 0.0847 0.1225 0.1563 0.0318  -0.0054 0.0293  205 GLU B N   
3928 C  CA  . GLU B 204 ? 0.0929 0.1187 0.1352 -0.0080 -0.0271 0.0337  205 GLU B CA  
3929 C  C   . GLU B 204 ? 0.1035 0.0910 0.1446 -0.0020 -0.0353 0.0258  205 GLU B C   
3930 O  O   . GLU B 204 ? 0.1308 0.1469 0.1523 -0.0282 -0.0397 0.0524  205 GLU B O   
3931 C  CB  . GLU B 204 ? 0.1279 0.1221 0.1656 -0.0178 -0.0493 0.0241  205 GLU B CB  
3932 C  CG  . GLU B 204 ? 0.1072 0.1194 0.1771 -0.0141 -0.0491 0.0241  205 GLU B CG  
3933 C  CD  . GLU B 204 ? 0.1380 0.1289 0.1595 -0.0094 -0.0511 0.0401  205 GLU B CD  
3934 O  OE1 . GLU B 204 ? 0.1552 0.1719 0.2157 -0.0142 -0.0922 0.0560  205 GLU B OE1 
3935 O  OE2 . GLU B 204 ? 0.1237 0.1446 0.1773 0.0020  -0.0526 0.0120  205 GLU B OE2 
3936 N  N   . CYS B 205 ? 0.0782 0.0941 0.1478 0.0080  -0.0259 0.0131  206 CYS B N   
3937 C  CA  . CYS B 205 ? 0.0841 0.1008 0.1422 0.0059  -0.0277 0.0116  206 CYS B CA  
3938 C  C   . CYS B 205 ? 0.0733 0.0882 0.1315 -0.0043 -0.0144 0.0088  206 CYS B C   
3939 O  O   . CYS B 205 ? 0.1090 0.0927 0.1710 -0.0110 -0.0381 0.0062  206 CYS B O   
3940 C  CB  . CYS B 205 ? 0.1067 0.0961 0.1388 0.0116  -0.0088 0.0110  206 CYS B CB  
3941 S  SG  . CYS B 205 ? 0.1331 0.1054 0.1448 -0.0031 -0.0148 0.0044  206 CYS B SG  
3942 N  N   . VAL B 206 ? 0.0886 0.0793 0.1272 0.0099  -0.0162 0.0055  207 VAL B N   
3943 C  CA  . VAL B 206 ? 0.0742 0.0813 0.1187 0.0118  -0.0197 0.0008  207 VAL B CA  
3944 C  C   . VAL B 206 ? 0.0892 0.0732 0.1200 -0.0060 -0.0284 -0.0081 207 VAL B C   
3945 O  O   . VAL B 206 ? 0.0846 0.1047 0.1380 -0.0087 -0.0181 -0.0127 207 VAL B O   
3946 C  CB  . VAL B 206 ? 0.0803 0.0900 0.1275 0.0054  -0.0020 0.0082  207 VAL B CB  
3947 C  CG1 . VAL B 206 ? 0.0781 0.0922 0.1250 0.0034  -0.0183 0.0132  207 VAL B CG1 
3948 C  CG2 . VAL B 206 ? 0.0895 0.1080 0.1440 -0.0097 0.0088  -0.0010 207 VAL B CG2 
3949 N  N   . THR B 207 ? 0.0816 0.0684 0.1202 -0.0031 -0.0165 -0.0026 208 THR B N   
3950 C  CA  . THR B 207 ? 0.0997 0.0753 0.1086 0.0105  -0.0109 0.0044  208 THR B CA  
3951 C  C   . THR B 207 ? 0.0935 0.0698 0.0943 0.0098  -0.0074 0.0049  208 THR B C   
3952 O  O   . THR B 207 ? 0.0948 0.0882 0.1056 0.0010  -0.0146 0.0003  208 THR B O   
3953 C  CB  . THR B 207 ? 0.1023 0.0886 0.1117 0.0035  -0.0094 0.0087  208 THR B CB  
3954 O  OG1 . THR B 207 ? 0.1237 0.0868 0.1281 -0.0052 -0.0076 0.0186  208 THR B OG1 
3955 C  CG2 . THR B 207 ? 0.1248 0.1153 0.1340 0.0003  0.0148  -0.0027 208 THR B CG2 
3956 N  N   . TRP B 208 ? 0.0822 0.0733 0.0943 -0.0003 -0.0070 0.0035  209 TRP B N   
3957 C  CA  . TRP B 208 ? 0.0712 0.0666 0.1102 0.0003  -0.0086 -0.0001 209 TRP B CA  
3958 C  C   . TRP B 208 ? 0.0826 0.0780 0.0900 -0.0076 -0.0017 0.0000  209 TRP B C   
3959 O  O   . TRP B 208 ? 0.0901 0.0957 0.0952 0.0041  -0.0041 -0.0024 209 TRP B O   
3960 C  CB  . TRP B 208 ? 0.0697 0.0821 0.1106 -0.0085 -0.0063 -0.0076 209 TRP B CB  
3961 C  CG  . TRP B 208 ? 0.0729 0.0693 0.1041 -0.0054 -0.0104 -0.0043 209 TRP B CG  
3962 C  CD1 . TRP B 208 ? 0.0764 0.0953 0.1045 0.0063  -0.0127 0.0131  209 TRP B CD1 
3963 C  CD2 . TRP B 208 ? 0.0604 0.0834 0.1162 0.0003  -0.0103 0.0108  209 TRP B CD2 
3964 N  NE1 . TRP B 208 ? 0.0820 0.0856 0.1146 0.0127  -0.0063 0.0046  209 TRP B NE1 
3965 C  CE2 . TRP B 208 ? 0.0546 0.0850 0.1084 -0.0170 -0.0171 0.0000  209 TRP B CE2 
3966 C  CE3 . TRP B 208 ? 0.0574 0.0777 0.1045 0.0010  -0.0195 -0.0027 209 TRP B CE3 
3967 C  CZ2 . TRP B 208 ? 0.0878 0.0905 0.1232 -0.0308 0.0065  0.0087  209 TRP B CZ2 
3968 C  CZ3 . TRP B 208 ? 0.0860 0.1093 0.0998 -0.0187 -0.0006 -0.0100 209 TRP B CZ3 
3969 C  CH2 . TRP B 208 ? 0.1053 0.0780 0.1217 -0.0181 0.0052  0.0021  209 TRP B CH2 
3970 N  N   . ILE B 209 ? 0.0680 0.0784 0.0935 0.0008  -0.0041 0.0005  210 ILE B N   
3971 C  CA  . ILE B 209 ? 0.0662 0.0780 0.1027 0.0068  -0.0087 0.0017  210 ILE B CA  
3972 C  C   . ILE B 209 ? 0.0634 0.0756 0.1029 0.0023  -0.0057 -0.0057 210 ILE B C   
3973 O  O   . ILE B 209 ? 0.1250 0.0825 0.0964 0.0044  -0.0108 -0.0023 210 ILE B O   
3974 C  CB  . ILE B 209 ? 0.0656 0.0803 0.1491 -0.0008 -0.0086 0.0074  210 ILE B CB  
3975 C  CG1 . ILE B 209 ? 0.0873 0.0869 0.1924 -0.0241 -0.0170 0.0215  210 ILE B CG1 
3976 C  CG2 . ILE B 209 ? 0.0881 0.1239 0.1552 0.0007  0.0030  0.0015  210 ILE B CG2 
3977 C  CD1 . ILE B 209 ? 0.0850 0.0913 0.2243 -0.0181 0.0068  -0.0140 210 ILE B CD1 
3978 N  N   . VAL B 210 ? 0.0747 0.0693 0.1040 0.0074  -0.0031 -0.0109 211 VAL B N   
3979 C  CA  . VAL B 210 ? 0.0688 0.0749 0.0962 0.0097  -0.0030 -0.0052 211 VAL B CA  
3980 C  C   . VAL B 210 ? 0.0838 0.0798 0.0997 -0.0065 0.0055  -0.0003 211 VAL B C   
3981 O  O   . VAL B 210 ? 0.1056 0.0959 0.0993 0.0098  0.0019  -0.0057 211 VAL B O   
3982 C  CB  . VAL B 210 ? 0.0815 0.0957 0.1313 -0.0057 -0.0049 -0.0013 211 VAL B CB  
3983 C  CG1 . VAL B 210 ? 0.1189 0.0772 0.1367 -0.0028 -0.0142 0.0068  211 VAL B CG1 
3984 C  CG2 . VAL B 210 ? 0.0810 0.1205 0.1406 0.0043  -0.0159 -0.0144 211 VAL B CG2 
3985 N  N   . LEU B 211 ? 0.0727 0.0912 0.1234 0.0077  -0.0153 0.0043  212 LEU B N   
3986 C  CA  . LEU B 211 ? 0.0768 0.1040 0.1291 0.0136  -0.0185 -0.0076 212 LEU B CA  
3987 C  C   . LEU B 211 ? 0.0834 0.0988 0.1216 0.0195  -0.0104 -0.0024 212 LEU B C   
3988 O  O   . LEU B 211 ? 0.0945 0.1126 0.1223 0.0035  -0.0125 -0.0027 212 LEU B O   
3989 C  CB  . LEU B 211 ? 0.0793 0.1097 0.1362 0.0046  -0.0161 -0.0086 212 LEU B CB  
3990 C  CG  . LEU B 211 ? 0.0988 0.1130 0.1396 0.0108  -0.0089 -0.0073 212 LEU B CG  
3991 C  CD1 . LEU B 211 ? 0.0870 0.1532 0.1773 0.0164  -0.0427 -0.0227 212 LEU B CD1 
3992 C  CD2 . LEU B 211 ? 0.1002 0.1165 0.1769 -0.0144 -0.0046 0.0049  212 LEU B CD2 
3993 N  N   . LYS B 212 ? 0.0947 0.1205 0.1135 0.0242  -0.0115 -0.0100 213 LYS B N   
3994 C  CA  . LYS B 212 ? 0.1185 0.1044 0.1252 0.0267  -0.0060 -0.0351 213 LYS B CA  
3995 C  C   . LYS B 212 ? 0.0970 0.0923 0.1412 0.0243  -0.0006 -0.0198 213 LYS B C   
3996 O  O   . LYS B 212 ? 0.1165 0.1097 0.1796 0.0126  -0.0259 -0.0243 213 LYS B O   
3997 C  CB  . LYS B 212 ? 0.1460 0.1471 0.1507 0.0463  0.0229  -0.0179 213 LYS B CB  
3998 C  CG  . LYS B 212 ? 0.2750 0.1589 0.1537 0.0248  -0.0121 -0.0417 213 LYS B CG  
3999 C  CD  . LYS B 212 ? 0.4050 0.2477 0.2163 0.1299  0.0322  -0.0109 213 LYS B CD  
4000 C  CE  . LYS B 212 ? 0.4607 0.3476 0.3483 0.0333  0.1216  -0.1318 213 LYS B CE  
4001 N  NZ  . LYS B 212 ? 0.6629 0.6421 0.3600 0.1225  0.1783  -0.0710 213 LYS B NZ  
4002 N  N   . GLU B 213 ? 0.0991 0.1059 0.1229 0.0186  -0.0175 -0.0151 214 GLU B N   
4003 C  CA  . GLU B 213 ? 0.0943 0.1108 0.1482 0.0414  -0.0104 -0.0041 214 GLU B CA  
4004 C  C   . GLU B 213 ? 0.0870 0.0883 0.1425 0.0263  -0.0083 -0.0183 214 GLU B C   
4005 O  O   . GLU B 213 ? 0.0745 0.0943 0.1507 0.0021  -0.0153 -0.0238 214 GLU B O   
4006 C  CB  . GLU B 213 ? 0.0824 0.1414 0.1681 0.0272  -0.0329 -0.0242 214 GLU B CB  
4007 C  CG  . GLU B 213 ? 0.1090 0.1534 0.2152 0.0430  -0.0601 -0.0196 214 GLU B CG  
4008 C  CD  . GLU B 213 ? 0.1160 0.2358 0.2335 0.0500  -0.0339 0.0297  214 GLU B CD  
4009 O  OE1 . GLU B 213 ? 0.1171 0.1777 0.3080 0.0185  -0.0502 -0.0161 214 GLU B OE1 
4010 O  OE2 . GLU B 213 ? 0.1805 0.5659 0.4146 0.0674  -0.0737 0.1847  214 GLU B OE2 
4011 N  N   A PRO B 214 ? 0.1004 0.0816 0.1295 0.0076  -0.0126 -0.0175 215 PRO B N   
4012 N  N   B PRO B 214 ? 0.1056 0.0954 0.1345 0.0074  -0.0120 -0.0073 215 PRO B N   
4013 C  CA  A PRO B 214 ? 0.1068 0.0920 0.1386 -0.0021 -0.0136 -0.0135 215 PRO B CA  
4014 C  CA  B PRO B 214 ? 0.1142 0.0905 0.1428 0.0001  -0.0137 -0.0164 215 PRO B CA  
4015 C  C   A PRO B 214 ? 0.0966 0.0944 0.1457 0.0192  -0.0240 0.0100  215 PRO B C   
4016 C  C   B PRO B 214 ? 0.1092 0.0979 0.1471 0.0154  -0.0233 0.0093  215 PRO B C   
4017 O  O   A PRO B 214 ? 0.1031 0.1509 0.1642 0.0373  -0.0355 -0.0187 215 PRO B O   
4018 O  O   B PRO B 214 ? 0.1138 0.1482 0.1701 0.0297  -0.0297 -0.0197 215 PRO B O   
4019 C  CB  A PRO B 214 ? 0.1184 0.0666 0.1467 0.0129  0.0073  -0.0099 215 PRO B CB  
4020 C  CB  B PRO B 214 ? 0.1325 0.0806 0.1695 0.0030  0.0031  0.0086  215 PRO B CB  
4021 C  CG  A PRO B 214 ? 0.1550 0.0639 0.1229 0.0185  0.0329  -0.0035 215 PRO B CG  
4022 C  CG  B PRO B 214 ? 0.1846 0.1794 0.2033 -0.0119 0.0196  -0.0017 215 PRO B CG  
4023 C  CD  A PRO B 214 ? 0.1058 0.0604 0.1442 0.0103  0.0065  -0.0013 215 PRO B CD  
4024 C  CD  B PRO B 214 ? 0.1913 0.0974 0.2033 -0.0167 0.0234  -0.0344 215 PRO B CD  
4025 N  N   . ILE B 215 ? 0.1059 0.1101 0.1266 -0.0031 -0.0272 -0.0006 216 ILE B N   
4026 C  CA  . ILE B 215 ? 0.1237 0.0995 0.1431 0.0190  -0.0234 0.0207  216 ILE B CA  
4027 C  C   . ILE B 215 ? 0.1144 0.0964 0.1404 -0.0008 -0.0291 0.0142  216 ILE B C   
4028 O  O   . ILE B 215 ? 0.1063 0.1058 0.1787 0.0091  -0.0250 0.0241  216 ILE B O   
4029 C  CB  . ILE B 215 ? 0.1208 0.0819 0.1719 -0.0007 -0.0266 0.0124  216 ILE B CB  
4030 C  CG1 . ILE B 215 ? 0.1622 0.1065 0.1451 0.0188  -0.0258 -0.0126 216 ILE B CG1 
4031 C  CG2 . ILE B 215 ? 0.1588 0.1228 0.1607 -0.0353 -0.0414 0.0130  216 ILE B CG2 
4032 C  CD1 . ILE B 215 ? 0.2029 0.1459 0.1626 -0.0133 -0.0225 -0.0122 216 ILE B CD1 
4033 N  N   A SER B 216 ? 0.1114 0.1102 0.1629 0.0023  -0.0361 0.0211  217 SER B N   
4034 N  N   B SER B 216 ? 0.1241 0.1110 0.1631 0.0074  -0.0359 0.0185  217 SER B N   
4035 C  CA  A SER B 216 ? 0.1174 0.1117 0.1553 0.0081  -0.0318 0.0299  217 SER B CA  
4036 C  CA  B SER B 216 ? 0.1338 0.1185 0.1597 0.0043  -0.0317 0.0261  217 SER B CA  
4037 C  C   A SER B 216 ? 0.1396 0.0864 0.1598 -0.0006 -0.0439 0.0082  217 SER B C   
4038 C  C   B SER B 216 ? 0.1500 0.0896 0.1624 -0.0028 -0.0392 0.0063  217 SER B C   
4039 O  O   A SER B 216 ? 0.1415 0.1194 0.1791 -0.0114 -0.0571 0.0001  217 SER B O   
4040 O  O   B SER B 216 ? 0.1462 0.1184 0.1843 -0.0098 -0.0480 -0.0008 217 SER B O   
4041 C  CB  A SER B 216 ? 0.2628 0.0756 0.1837 0.0516  0.0173  0.0293  217 SER B CB  
4042 C  CB  B SER B 216 ? 0.2775 0.1101 0.2130 0.0631  0.0272  -0.0168 217 SER B CB  
4043 O  OG  A SER B 216 ? 0.1954 0.1419 0.1748 0.0562  -0.0370 0.0013  217 SER B OG  
4044 O  OG  B SER B 216 ? 0.3792 0.1960 0.2655 0.0436  0.0135  0.0432  217 SER B OG  
4045 N  N   . VAL B 217 ? 0.1482 0.0905 0.1509 0.0175  -0.0313 0.0059  218 VAL B N   
4046 C  CA  . VAL B 217 ? 0.1717 0.0780 0.1404 0.0173  -0.0287 0.0006  218 VAL B CA  
4047 C  C   . VAL B 217 ? 0.1678 0.0870 0.1396 0.0185  -0.0423 0.0030  218 VAL B C   
4048 O  O   . VAL B 217 ? 0.1629 0.0898 0.1482 0.0219  -0.0425 0.0021  218 VAL B O   
4049 C  CB  . VAL B 217 ? 0.1328 0.0750 0.2112 0.0249  -0.0570 0.0088  218 VAL B CB  
4050 C  CG1 . VAL B 217 ? 0.1678 0.0789 0.1983 0.0138  -0.0439 0.0121  218 VAL B CG1 
4051 C  CG2 . VAL B 217 ? 0.1413 0.1209 0.2055 0.0142  -0.0350 0.0157  218 VAL B CG2 
4052 N  N   . SER B 218 ? 0.1544 0.0842 0.1466 0.0115  -0.0305 0.0148  219 SER B N   
4053 C  CA  . SER B 218 ? 0.1708 0.0799 0.1654 0.0310  -0.0252 0.0164  219 SER B CA  
4054 C  C   . SER B 218 ? 0.1741 0.0746 0.1559 0.0136  -0.0142 -0.0043 219 SER B C   
4055 O  O   . SER B 218 ? 0.1771 0.0790 0.1543 0.0151  -0.0401 0.0035  219 SER B O   
4056 C  CB  . SER B 218 ? 0.1755 0.0966 0.1449 0.0160  -0.0311 0.0098  219 SER B CB  
4057 O  OG  . SER B 218 ? 0.2002 0.1110 0.1536 0.0199  -0.0375 0.0122  219 SER B OG  
4058 N  N   A SER B 219 ? 0.1714 0.0768 0.1595 0.0178  -0.0199 0.0026  220 SER B N   
4059 N  N   B SER B 219 ? 0.1746 0.0793 0.1590 0.0163  -0.0259 0.0087  220 SER B N   
4060 C  CA  A SER B 219 ? 0.2037 0.0753 0.2096 0.0055  -0.0102 -0.0083 220 SER B CA  
4061 C  CA  B SER B 219 ? 0.2008 0.0816 0.2136 0.0044  -0.0181 -0.0141 220 SER B CA  
4062 C  C   A SER B 219 ? 0.1865 0.0829 0.2041 0.0071  -0.0274 -0.0001 220 SER B C   
4063 C  C   B SER B 219 ? 0.1821 0.0856 0.2050 0.0060  -0.0294 0.0000  220 SER B C   
4064 O  O   A SER B 219 ? 0.2102 0.1001 0.2357 0.0274  -0.0001 0.0046  220 SER B O   
4065 O  O   B SER B 219 ? 0.2047 0.1160 0.2328 0.0259  -0.0015 -0.0063 220 SER B O   
4066 C  CB  A SER B 219 ? 0.2687 0.0834 0.2520 0.0097  -0.0063 0.0054  220 SER B CB  
4067 C  CB  B SER B 219 ? 0.2448 0.0907 0.2448 0.0173  -0.0198 0.0037  220 SER B CB  
4068 O  OG  A SER B 219 ? 0.2966 0.0821 0.2324 -0.0304 -0.0110 0.0339  220 SER B OG  
4069 O  OG  B SER B 219 ? 0.2793 0.1376 0.2698 -0.0228 -0.0043 -0.0361 220 SER B OG  
4070 N  N   . GLU B 220 ? 0.2166 0.0810 0.1694 0.0015  -0.0196 0.0135  221 GLU B N   
4071 C  CA  . GLU B 220 ? 0.2121 0.1153 0.2015 -0.0007 -0.0252 0.0054  221 GLU B CA  
4072 C  C   . GLU B 220 ? 0.2191 0.1090 0.1395 -0.0068 -0.0167 -0.0159 221 GLU B C   
4073 O  O   . GLU B 220 ? 0.2610 0.1181 0.1590 -0.0001 0.0211  0.0043  221 GLU B O   
4074 C  CB  . GLU B 220 ? 0.2994 0.1808 0.1945 0.0529  -0.0568 0.0785  221 GLU B CB  
4075 C  CG  . GLU B 220 ? 0.3946 0.1755 0.2479 0.0317  -0.1466 0.0504  221 GLU B CG  
4076 C  CD  . GLU B 220 ? 0.4336 0.1518 0.3343 0.0329  -0.0269 0.1154  221 GLU B CD  
4077 O  OE1 . GLU B 220 ? 0.2529 0.1807 0.3283 0.0967  0.0070  0.0599  221 GLU B OE1 
4078 O  OE2 . GLU B 220 ? 0.4987 0.3120 0.7174 0.0967  -0.0098 0.2820  221 GLU B OE2 
4079 N  N   . GLN B 221 ? 0.1814 0.0907 0.1712 0.0040  -0.0346 0.0107  222 GLN B N   
4080 C  CA  . GLN B 221 ? 0.2188 0.0813 0.1496 0.0122  -0.0313 -0.0065 222 GLN B CA  
4081 C  C   . GLN B 221 ? 0.1690 0.1018 0.1457 0.0227  -0.0262 -0.0144 222 GLN B C   
4082 O  O   . GLN B 221 ? 0.2046 0.1160 0.1435 0.0250  -0.0052 -0.0126 222 GLN B O   
4083 C  CB  . GLN B 221 ? 0.1902 0.1108 0.1432 0.0190  -0.0461 0.0226  222 GLN B CB  
4084 C  CG  . GLN B 221 ? 0.2050 0.1105 0.1187 0.0366  -0.0397 -0.0001 222 GLN B CG  
4085 C  CD  . GLN B 221 ? 0.2110 0.0873 0.1345 0.0253  -0.0584 0.0007  222 GLN B CD  
4086 O  OE1 . GLN B 221 ? 0.1703 0.1056 0.1516 0.0041  -0.0337 0.0034  222 GLN B OE1 
4087 N  NE2 . GLN B 221 ? 0.2116 0.1053 0.1595 0.0242  -0.0555 -0.0087 222 GLN B NE2 
4088 N  N   . VAL B 222 ? 0.1825 0.1045 0.1482 0.0271  -0.0248 -0.0116 223 VAL B N   
4089 C  CA  . VAL B 222 ? 0.1922 0.1146 0.1615 0.0296  -0.0287 -0.0210 223 VAL B CA  
4090 C  C   . VAL B 222 ? 0.1965 0.1129 0.1814 0.0241  -0.0049 -0.0096 223 VAL B C   
4091 O  O   . VAL B 222 ? 0.1855 0.1182 0.1724 0.0171  -0.0120 -0.0297 223 VAL B O   
4092 C  CB  . VAL B 222 ? 0.1870 0.1590 0.2193 0.0070  -0.0582 -0.0507 223 VAL B CB  
4093 C  CG1 . VAL B 222 ? 0.1931 0.2051 0.2378 0.0283  -0.0417 -0.0838 223 VAL B CG1 
4094 C  CG2 . VAL B 222 ? 0.2028 0.1902 0.2570 0.0183  -0.0636 -0.0408 223 VAL B CG2 
4095 N  N   . LEU B 223 ? 0.1938 0.1383 0.1865 0.0003  0.0049  -0.0060 224 LEU B N   
4096 C  CA  . LEU B 223 ? 0.1897 0.1178 0.2396 0.0388  0.0156  0.0242  224 LEU B CA  
4097 C  C   . LEU B 223 ? 0.2269 0.1468 0.2044 0.0147  0.0280  0.0410  224 LEU B C   
4098 O  O   . LEU B 223 ? 0.2348 0.1738 0.2110 0.0148  0.0219  0.0375  224 LEU B O   
4099 C  CB  . LEU B 223 ? 0.2861 0.1324 0.2579 0.0399  0.0149  0.0518  224 LEU B CB  
4100 C  CG  . LEU B 223 ? 0.3057 0.1577 0.3041 0.0306  0.0120  0.0271  224 LEU B CG  
4101 C  CD1 . LEU B 223 ? 0.3082 0.2105 0.3452 0.0211  -0.0397 0.0449  224 LEU B CD1 
4102 C  CD2 . LEU B 223 ? 0.3339 0.2412 0.4119 -0.0476 0.0115  0.0236  224 LEU B CD2 
4103 N  N   . LYS B 224 ? 0.2522 0.1288 0.1511 0.0174  0.0074  0.0074  225 LYS B N   
4104 C  CA  . LYS B 224 ? 0.2240 0.1870 0.1647 0.0167  0.0175  -0.0024 225 LYS B CA  
4105 C  C   . LYS B 224 ? 0.2585 0.1475 0.1340 0.0126  0.0155  -0.0148 225 LYS B C   
4106 O  O   . LYS B 224 ? 0.2603 0.1453 0.1252 0.0111  0.0230  -0.0118 225 LYS B O   
4107 C  CB  . LYS B 224 ? 0.2644 0.1953 0.1996 -0.0044 -0.0322 -0.0610 225 LYS B CB  
4108 C  CG  . LYS B 224 ? 0.2989 0.3163 0.2448 0.0273  -0.0639 0.0174  225 LYS B CG  
4109 C  CD  . LYS B 224 ? 0.3998 0.2581 0.2662 -0.0160 -0.0918 0.0346  225 LYS B CD  
4110 C  CE  . LYS B 224 ? 0.3621 0.5175 0.4268 0.2187  -0.0212 0.1350  225 LYS B CE  
4111 N  NZ  . LYS B 224 ? 0.5286 0.3623 0.4440 0.0954  -0.0266 0.2034  225 LYS B NZ  
4112 N  N   . PHE B 225 ? 0.2337 0.1211 0.1295 0.0311  0.0186  -0.0155 226 PHE B N   
4113 C  CA  . PHE B 225 ? 0.1832 0.1101 0.1473 0.0331  0.0265  -0.0152 226 PHE B CA  
4114 C  C   . PHE B 225 ? 0.2305 0.1027 0.1329 0.0381  0.0414  -0.0031 226 PHE B C   
4115 O  O   . PHE B 225 ? 0.2261 0.1266 0.1378 0.0362  0.0408  0.0197  226 PHE B O   
4116 C  CB  . PHE B 225 ? 0.2102 0.1036 0.1315 -0.0024 0.0125  -0.0081 226 PHE B CB  
4117 C  CG  . PHE B 225 ? 0.2224 0.0879 0.1489 0.0335  0.0329  0.0088  226 PHE B CG  
4118 C  CD1 . PHE B 225 ? 0.2588 0.1483 0.1856 -0.0309 0.0294  -0.0260 226 PHE B CD1 
4119 C  CD2 . PHE B 225 ? 0.2152 0.1834 0.1719 0.0299  0.0013  0.0537  226 PHE B CD2 
4120 C  CE1 . PHE B 225 ? 0.2707 0.1965 0.1972 -0.0401 0.0388  -0.0326 226 PHE B CE1 
4121 C  CE2 . PHE B 225 ? 0.1791 0.2231 0.1992 0.0226  0.0194  0.0815  226 PHE B CE2 
4122 C  CZ  . PHE B 225 ? 0.2102 0.1412 0.2267 0.0351  -0.0275 0.0494  226 PHE B CZ  
4123 N  N   . ARG B 226 ? 0.2002 0.1001 0.1243 0.0168  -0.0017 0.0023  227 ARG B N   
4124 C  CA  . ARG B 226 ? 0.1959 0.1247 0.1505 0.0178  0.0225  0.0027  227 ARG B CA  
4125 C  C   . ARG B 226 ? 0.2217 0.1239 0.1667 0.0142  0.0302  -0.0091 227 ARG B C   
4126 O  O   . ARG B 226 ? 0.2204 0.1611 0.1886 0.0114  0.0399  0.0164  227 ARG B O   
4127 C  CB  . ARG B 226 ? 0.2236 0.1151 0.1392 0.0188  0.0153  -0.0021 227 ARG B CB  
4128 C  CG  . ARG B 226 ? 0.1902 0.1226 0.1483 0.0027  -0.0013 -0.0303 227 ARG B CG  
4129 C  CD  . ARG B 226 ? 0.2578 0.1153 0.1947 0.0394  0.0280  -0.0193 227 ARG B CD  
4130 N  NE  . ARG B 226 ? 0.1987 0.0966 0.1505 0.0414  -0.0198 -0.0153 227 ARG B NE  
4131 C  CZ  . ARG B 226 ? 0.1981 0.1265 0.1368 0.0511  -0.0197 0.0052  227 ARG B CZ  
4132 N  NH1 . ARG B 226 ? 0.2558 0.1803 0.2168 0.0799  -0.0249 0.0617  227 ARG B NH1 
4133 N  NH2 . ARG B 226 ? 0.2482 0.1376 0.1580 0.0663  0.0126  -0.0071 227 ARG B NH2 
4134 N  N   . LYS B 227 ? 0.2116 0.1133 0.1405 0.0217  0.0194  0.0183  228 LYS B N   
4135 C  CA  . LYS B 227 ? 0.2468 0.1568 0.1556 0.0785  0.0430  0.0289  228 LYS B CA  
4136 C  C   . LYS B 227 ? 0.2942 0.1181 0.1218 0.0430  0.0388  0.0111  228 LYS B C   
4137 O  O   . LYS B 227 ? 0.3314 0.1870 0.1325 0.0819  0.0474  0.0370  228 LYS B O   
4138 C  CB  . LYS B 227 ? 0.2847 0.2227 0.1390 0.0498  0.0000  0.0548  228 LYS B CB  
4139 C  CG  . LYS B 227 ? 0.3693 0.2398 0.1821 0.1044  0.0353  0.0359  228 LYS B CG  
4140 C  CD  . LYS B 227 ? 0.4343 0.4490 0.2394 0.1905  0.0450  0.1422  228 LYS B CD  
4141 C  CE  . LYS B 227 ? 0.4714 0.7300 0.3328 0.2386  -0.0111 -0.0164 228 LYS B CE  
4142 N  NZ  . LYS B 227 ? 0.8634 1.2421 0.6955 -0.0732 -0.3501 0.0966  228 LYS B NZ  
4143 N  N   . LEU B 228 ? 0.2809 0.1194 0.1365 0.0593  0.0188  0.0274  229 LEU B N   
4144 C  CA  . LEU B 228 ? 0.2621 0.1263 0.1625 0.0544  0.0505  0.0305  229 LEU B CA  
4145 C  C   . LEU B 228 ? 0.2777 0.1115 0.1492 0.0579  0.0653  0.0469  229 LEU B C   
4146 O  O   . LEU B 228 ? 0.2369 0.1259 0.1509 0.0450  0.0549  0.0265  229 LEU B O   
4147 C  CB  . LEU B 228 ? 0.2770 0.1315 0.1446 0.0784  0.0491  0.0307  229 LEU B CB  
4148 C  CG  . LEU B 228 ? 0.2500 0.1744 0.1241 0.0509  0.0274  0.0023  229 LEU B CG  
4149 C  CD1 . LEU B 228 ? 0.2872 0.1647 0.1476 0.0504  0.0241  0.0447  229 LEU B CD1 
4150 C  CD2 . LEU B 228 ? 0.3713 0.1541 0.1708 0.0463  0.0650  -0.0241 229 LEU B CD2 
4151 N  N   . ASN B 229 ? 0.2551 0.1564 0.1414 0.0851  0.0653  0.0406  230 ASN B N   
4152 C  CA  . ASN B 229 ? 0.2664 0.1475 0.1432 0.0722  0.0782  0.0379  230 ASN B CA  
4153 C  C   . ASN B 229 ? 0.2804 0.1750 0.1810 0.0970  0.1018  0.0447  230 ASN B C   
4154 O  O   . ASN B 229 ? 0.2858 0.1652 0.1607 0.0734  0.0662  0.0401  230 ASN B O   
4155 C  CB  . ASN B 229 ? 0.2788 0.1753 0.1514 0.0812  0.0856  0.0261  230 ASN B CB  
4156 C  CG  . ASN B 229 ? 0.3461 0.2202 0.1412 0.0983  0.0842  0.0469  230 ASN B CG  
4157 O  OD1 . ASN B 229 ? 0.5080 0.2040 0.1784 0.0916  0.1407  0.0526  230 ASN B OD1 
4158 N  ND2 . ASN B 229 ? 0.3310 0.1602 0.1925 0.0802  0.0873  0.0650  230 ASN B ND2 
4159 N  N   . PHE B 230 ? 0.2799 0.1722 0.1785 0.1181  0.1057  0.0533  231 PHE B N   
4160 C  CA  . PHE B 230 ? 0.2384 0.1502 0.2002 0.0872  0.0733  0.0436  231 PHE B CA  
4161 C  C   . PHE B 230 ? 0.3280 0.1920 0.2396 0.1380  0.1242  0.0746  231 PHE B C   
4162 O  O   . PHE B 230 ? 0.3307 0.1796 0.2083 0.1307  0.0895  0.0606  231 PHE B O   
4163 C  CB  . PHE B 230 ? 0.2797 0.2257 0.1868 0.1393  0.0944  0.0588  231 PHE B CB  
4164 C  CG  . PHE B 230 ? 0.2231 0.1764 0.1825 0.0785  0.0465  0.0307  231 PHE B CG  
4165 C  CD1 . PHE B 230 ? 0.2393 0.2168 0.1609 0.0917  0.0474  0.0494  231 PHE B CD1 
4166 C  CD2 . PHE B 230 ? 0.2639 0.1956 0.1669 0.0357  0.0918  0.0527  231 PHE B CD2 
4167 C  CE1 . PHE B 230 ? 0.2272 0.1839 0.1927 0.1013  0.0494  0.0428  231 PHE B CE1 
4168 C  CE2 . PHE B 230 ? 0.2216 0.1834 0.1703 0.0644  0.0502  0.0414  231 PHE B CE2 
4169 C  CZ  . PHE B 230 ? 0.2006 0.2294 0.1340 0.0910  0.0608  0.0259  231 PHE B CZ  
4170 N  N   . ASN B 231 ? 0.2754 0.2265 0.2014 0.1133  0.1199  0.0662  232 ASN B N   
4171 C  CA  . ASN B 231 ? 0.2851 0.1907 0.2145 0.1079  0.1000  0.0406  232 ASN B CA  
4172 C  C   . ASN B 231 ? 0.2682 0.1960 0.1990 0.0476  0.0817  0.0447  232 ASN B C   
4173 O  O   . ASN B 231 ? 0.3533 0.1949 0.1945 0.0869  0.1032  0.0300  232 ASN B O   
4174 C  CB  . ASN B 231 ? 0.3501 0.2107 0.2583 0.1483  0.1754  0.0680  232 ASN B CB  
4175 C  CG  . ASN B 231 ? 0.2915 0.2051 0.2558 0.1160  0.1228  0.0430  232 ASN B CG  
4176 O  OD1 . ASN B 231 ? 0.4377 0.1947 0.2457 0.1342  0.1724  0.0811  232 ASN B OD1 
4177 N  ND2 . ASN B 231 ? 0.3993 0.2831 0.2306 0.1124  0.1418  0.0754  232 ASN B ND2 
4178 N  N   . GLY B 232 ? 0.3574 0.2044 0.2508 0.1032  0.1317  0.0373  233 GLY B N   
4179 C  CA  . GLY B 232 ? 0.3752 0.2123 0.2044 0.0504  0.1248  0.0111  233 GLY B CA  
4180 C  C   . GLY B 232 ? 0.2114 0.2468 0.2464 0.0667  -0.0074 0.0232  233 GLY B C   
4181 O  O   . GLY B 232 ? 0.3456 0.3222 0.2942 0.0544  0.1829  -0.0461 233 GLY B O   
4182 N  N   . GLU B 233 ? 0.2002 0.2615 0.2168 0.0480  0.0590  0.0162  234 GLU B N   
4183 C  CA  . GLU B 233 ? 0.2329 0.2261 0.1877 -0.0074 0.0410  0.0386  234 GLU B CA  
4184 C  C   . GLU B 233 ? 0.2596 0.2651 0.2020 0.0177  0.0516  -0.0259 234 GLU B C   
4185 O  O   . GLU B 233 ? 0.3673 0.2867 0.2259 0.0746  0.1155  0.0030  234 GLU B O   
4186 C  CB  . GLU B 233 ? 0.3061 0.2425 0.1888 -0.0076 0.0206  -0.0296 234 GLU B CB  
4187 C  CG  . GLU B 233 ? 0.3061 0.3319 0.1785 0.0987  0.0627  -0.0076 234 GLU B CG  
4188 C  CD  . GLU B 233 ? 0.4589 0.5060 0.3332 -0.1155 -0.0103 0.0843  234 GLU B CD  
4189 O  OE1 . GLU B 233 ? 0.4253 0.4079 0.3431 0.0829  0.1040  -0.0046 234 GLU B OE1 
4190 O  OE2 . GLU B 233 ? 0.3474 0.4251 0.4569 0.0403  -0.0582 0.1599  234 GLU B OE2 
4191 N  N   . GLY B 234 ? 0.3844 0.3190 0.2496 0.0197  0.1111  0.0881  235 GLY B N   
4192 C  CA  . GLY B 234 ? 0.3982 0.2617 0.2926 -0.0296 0.0705  0.0724  235 GLY B CA  
4193 C  C   . GLY B 234 ? 0.4029 0.4894 0.2800 -0.0719 0.1143  -0.0441 235 GLY B C   
4194 O  O   . GLY B 234 ? 0.4710 0.6736 0.3327 -0.0718 0.2140  -0.0417 235 GLY B O   
4195 N  N   . GLU B 235 ? 0.3767 0.3188 0.3366 -0.0027 0.1973  0.0111  236 GLU B N   
4196 C  CA  . GLU B 235 ? 0.2806 0.2134 0.2922 0.0366  0.1288  0.0353  236 GLU B CA  
4197 C  C   . GLU B 235 ? 0.5171 0.3183 0.3431 0.1143  0.2266  0.0177  236 GLU B C   
4198 O  O   . GLU B 235 ? 0.6075 0.3264 0.4129 0.1361  0.3321  0.0737  236 GLU B O   
4199 C  CB  . GLU B 235 ? 0.3465 0.2716 0.2948 0.0662  0.1608  0.0228  236 GLU B CB  
4200 C  CG  . GLU B 235 ? 0.4642 0.2899 0.3463 0.1102  0.1861  0.0206  236 GLU B CG  
4201 C  CD  . GLU B 235 ? 0.5841 0.6822 0.3808 0.3912  0.2520  0.1914  236 GLU B CD  
4202 O  OE1 . GLU B 235 ? 0.3625 0.6082 0.4126 0.1798  0.1794  -0.0126 236 GLU B OE1 
4203 O  OE2 . GLU B 235 ? 0.5331 0.4343 0.7838 0.1875  0.3249  -0.1299 236 GLU B OE2 
4204 N  N   . PRO B 236 ? 0.3542 0.3522 0.3628 0.0992  0.2171  -0.0186 237 PRO B N   
4205 C  CA  . PRO B 236 ? 0.4330 0.4146 0.4447 0.1199  0.3111  0.0010  237 PRO B CA  
4206 C  C   . PRO B 236 ? 0.4287 0.3650 0.2782 0.1709  0.2336  0.1008  237 PRO B C   
4207 O  O   . PRO B 236 ? 0.3876 0.2996 0.3102 0.1412  0.2127  0.1004  237 PRO B O   
4208 C  CB  . PRO B 236 ? 0.3485 0.5630 0.6093 0.0178  0.3359  -0.1176 237 PRO B CB  
4209 C  CG  . PRO B 236 ? 0.4947 0.5766 0.5157 0.0732  0.2329  -0.2700 237 PRO B CG  
4210 C  CD  . PRO B 236 ? 0.3740 0.6384 0.3515 0.0478  0.1352  -0.0414 237 PRO B CD  
4211 N  N   . GLU B 237 ? 0.3953 0.2232 0.2610 0.0566  0.1510  0.0621  238 GLU B N   
4212 C  CA  . GLU B 237 ? 0.3914 0.3007 0.1811 0.0816  0.1448  0.0715  238 GLU B CA  
4213 C  C   . GLU B 237 ? 0.3305 0.2725 0.2385 0.0966  0.1146  0.0318  238 GLU B C   
4214 O  O   . GLU B 237 ? 0.2001 0.3368 0.2038 0.0922  0.0542  0.0395  238 GLU B O   
4215 C  CB  . GLU B 237 ? 0.3752 0.2177 0.2066 -0.0219 0.0148  0.0540  238 GLU B CB  
4216 C  CG  . GLU B 237 ? 0.3305 0.2660 0.2696 0.0326  0.0143  0.0644  238 GLU B CG  
4217 C  CD  . GLU B 237 ? 0.3231 0.2098 0.1877 0.0168  0.0165  0.0366  238 GLU B CD  
4218 O  OE1 . GLU B 237 ? 0.4586 0.2462 0.4221 -0.0658 -0.1057 0.1242  238 GLU B OE1 
4219 O  OE2 . GLU B 237 ? 0.3790 0.2123 0.2721 0.0313  0.0575  0.1133  238 GLU B OE2 
4220 N  N   . GLU B 238 ? 0.3237 0.3041 0.1747 0.1794  0.1274  0.1077  239 GLU B N   
4221 C  CA  . GLU B 238 ? 0.1904 0.3867 0.1929 0.1678  0.0706  0.0825  239 GLU B CA  
4222 C  C   . GLU B 238 ? 0.1720 0.2143 0.1407 0.0662  0.0509  0.0395  239 GLU B C   
4223 O  O   . GLU B 238 ? 0.3163 0.1641 0.2198 0.0778  0.0974  0.0527  239 GLU B O   
4224 C  CB  . GLU B 238 ? 0.2544 0.2583 0.2944 0.0811  0.0445  0.0674  239 GLU B CB  
4225 C  CG  . GLU B 238 ? 0.2937 0.3172 0.6197 -0.1503 0.2456  -0.2442 239 GLU B CG  
4226 C  CD  . GLU B 238 ? 0.2137 0.6963 1.1638 0.0087  0.0212  -0.6751 239 GLU B CD  
4227 O  OE1 . GLU B 238 ? 0.7264 0.5066 0.9810 0.4223  -0.1018 -0.0355 239 GLU B OE1 
4228 O  OE2 . GLU B 238 ? 0.2078 0.3452 0.6753 -0.1172 -0.0692 -0.0207 239 GLU B OE2 
4229 N  N   . LEU B 239 ? 0.1773 0.2013 0.1604 0.0438  0.0604  0.0388  240 LEU B N   
4230 C  CA  . LEU B 239 ? 0.1632 0.1555 0.1694 0.0516  0.0645  0.0410  240 LEU B CA  
4231 C  C   . LEU B 239 ? 0.2162 0.1457 0.1395 0.0386  0.0384  0.0081  240 LEU B C   
4232 O  O   . LEU B 239 ? 0.1814 0.1776 0.1561 0.0537  0.0604  0.0331  240 LEU B O   
4233 C  CB  . LEU B 239 ? 0.1280 0.1353 0.1839 0.0038  -0.0035 0.0186  240 LEU B CB  
4234 C  CG  . LEU B 239 ? 0.1374 0.1315 0.2135 0.0207  -0.0031 0.0417  240 LEU B CG  
4235 C  CD1 . LEU B 239 ? 0.2065 0.1000 0.3966 -0.0111 -0.0790 0.0164  240 LEU B CD1 
4236 C  CD2 . LEU B 239 ? 0.2213 0.1516 0.1908 -0.0093 0.0168  0.0333  240 LEU B CD2 
4237 N  N   . MET B 240 ? 0.1911 0.1252 0.1574 0.0245  0.0663  0.0248  241 MET B N   
4238 C  CA  . MET B 240 ? 0.2590 0.1464 0.1347 0.0340  0.0922  0.0096  241 MET B CA  
4239 C  C   . MET B 240 ? 0.1680 0.1451 0.1286 0.0529  0.0496  0.0441  241 MET B C   
4240 O  O   . MET B 240 ? 0.1841 0.1389 0.1383 0.0263  0.0454  0.0153  241 MET B O   
4241 C  CB  . MET B 240 ? 0.2773 0.1117 0.1541 0.0320  0.0540  0.0359  241 MET B CB  
4242 C  CG  . MET B 240 ? 0.2238 0.1383 0.1374 0.0324  0.0657  0.0164  241 MET B CG  
4243 S  SD  . MET B 240 ? 0.2827 0.1159 0.1777 0.0447  0.0746  0.0161  241 MET B SD  
4244 C  CE  . MET B 240 ? 0.2921 0.1439 0.1856 0.0509  0.0996  0.0115  241 MET B CE  
4245 N  N   . VAL B 241 ? 0.1819 0.1135 0.1370 0.0311  0.0408  0.0313  242 VAL B N   
4246 C  CA  . VAL B 241 ? 0.1601 0.1106 0.1221 0.0276  0.0344  0.0263  242 VAL B CA  
4247 C  C   . VAL B 241 ? 0.1545 0.1189 0.1394 0.0305  0.0467  0.0482  242 VAL B C   
4248 O  O   . VAL B 241 ? 0.1349 0.1525 0.1553 0.0379  0.0434  0.0401  242 VAL B O   
4249 C  CB  . VAL B 241 ? 0.1528 0.1132 0.1489 0.0370  0.0335  0.0355  242 VAL B CB  
4250 C  CG1 . VAL B 241 ? 0.1987 0.1250 0.1595 0.0375  0.0175  0.0511  242 VAL B CG1 
4251 C  CG2 . VAL B 241 ? 0.1900 0.1298 0.2024 0.0093  0.0553  0.0434  242 VAL B CG2 
4252 N  N   . ASP B 242 ? 0.1532 0.1049 0.1209 0.0291  0.0388  0.0399  243 ASP B N   
4253 C  CA  . ASP B 242 ? 0.1164 0.1058 0.1465 -0.0065 0.0199  0.0355  243 ASP B CA  
4254 C  C   . ASP B 242 ? 0.1234 0.1103 0.1263 0.0278  0.0308  0.0181  243 ASP B C   
4255 O  O   . ASP B 242 ? 0.1313 0.1310 0.1832 0.0164  0.0175  0.0397  243 ASP B O   
4256 C  CB  . ASP B 242 ? 0.1165 0.1110 0.1624 0.0163  -0.0008 0.0206  243 ASP B CB  
4257 C  CG  . ASP B 242 ? 0.1059 0.1027 0.1914 -0.0027 0.0162  0.0234  243 ASP B CG  
4258 O  OD1 . ASP B 242 ? 0.1178 0.0980 0.1546 0.0122  0.0154  0.0229  243 ASP B OD1 
4259 O  OD2 . ASP B 242 ? 0.1449 0.1291 0.2169 -0.0103 0.0333  0.0368  243 ASP B OD2 
4260 N  N   . ASN B 243 ? 0.1275 0.0804 0.1374 0.0063  0.0383  0.0230  244 ASN B N   
4261 C  CA  . ASN B 243 ? 0.1273 0.0852 0.1310 0.0184  0.0328  0.0241  244 ASN B CA  
4262 C  C   . ASN B 243 ? 0.0914 0.0941 0.1308 0.0167  0.0253  0.0020  244 ASN B C   
4263 O  O   . ASN B 243 ? 0.1369 0.1022 0.1282 -0.0174 0.0245  -0.0012 244 ASN B O   
4264 C  CB  . ASN B 243 ? 0.1144 0.1140 0.1319 0.0390  0.0359  0.0062  244 ASN B CB  
4265 C  CG  . ASN B 243 ? 0.1263 0.0970 0.1342 0.0434  0.0320  0.0149  244 ASN B CG  
4266 O  OD1 . ASN B 243 ? 0.1248 0.1254 0.1489 0.0342  0.0207  -0.0074 244 ASN B OD1 
4267 N  ND2 . ASN B 243 ? 0.1739 0.1600 0.2216 0.0447  -0.0083 -0.0785 244 ASN B ND2 
4268 N  N   . TRP B 244 ? 0.1147 0.0812 0.1111 0.0217  0.0142  0.0173  245 TRP B N   
4269 C  CA  . TRP B 244 ? 0.0777 0.1099 0.1103 0.0164  0.0071  0.0155  245 TRP B CA  
4270 C  C   . TRP B 244 ? 0.1081 0.0977 0.1250 -0.0041 0.0147  0.0052  245 TRP B C   
4271 O  O   . TRP B 244 ? 0.0961 0.1173 0.1688 -0.0035 -0.0035 0.0401  245 TRP B O   
4272 C  CB  . TRP B 244 ? 0.0881 0.0844 0.1333 0.0013  0.0124  0.0164  245 TRP B CB  
4273 C  CG  . TRP B 244 ? 0.0939 0.0894 0.1280 -0.0020 0.0100  0.0000  245 TRP B CG  
4274 C  CD1 . TRP B 244 ? 0.1115 0.0834 0.1270 0.0082  0.0308  0.0081  245 TRP B CD1 
4275 C  CD2 . TRP B 244 ? 0.0860 0.1038 0.1284 0.0052  0.0142  0.0105  245 TRP B CD2 
4276 N  NE1 . TRP B 244 ? 0.0959 0.0932 0.1401 0.0109  0.0044  0.0026  245 TRP B NE1 
4277 C  CE2 . TRP B 244 ? 0.1138 0.0877 0.1486 -0.0087 0.0181  -0.0074 245 TRP B CE2 
4278 C  CE3 . TRP B 244 ? 0.1232 0.1138 0.1349 0.0087  0.0005  -0.0032 245 TRP B CE3 
4279 C  CZ2 . TRP B 244 ? 0.1376 0.0881 0.1591 -0.0124 0.0175  0.0027  245 TRP B CZ2 
4280 C  CZ3 . TRP B 244 ? 0.1372 0.1094 0.1739 -0.0003 0.0142  -0.0115 245 TRP B CZ3 
4281 C  CH2 . TRP B 244 ? 0.1187 0.1360 0.1841 -0.0102 0.0177  -0.0021 245 TRP B CH2 
4282 N  N   . ARG B 245 ? 0.0877 0.1011 0.1158 0.0040  0.0051  0.0154  246 ARG B N   
4283 C  CA  . ARG B 245 ? 0.0936 0.0977 0.1316 -0.0015 0.0110  0.0119  246 ARG B CA  
4284 C  C   . ARG B 245 ? 0.0877 0.0846 0.1234 -0.0098 -0.0107 0.0333  246 ARG B C   
4285 O  O   . ARG B 245 ? 0.0910 0.1137 0.1455 -0.0129 -0.0060 0.0148  246 ARG B O   
4286 C  CB  . ARG B 245 ? 0.0606 0.0989 0.1358 -0.0074 -0.0109 0.0248  246 ARG B CB  
4287 C  CG  . ARG B 245 ? 0.0537 0.1045 0.1582 -0.0038 -0.0054 0.0156  246 ARG B CG  
4288 C  CD  . ARG B 245 ? 0.0535 0.1239 0.1686 0.0175  -0.0017 0.0428  246 ARG B CD  
4289 N  NE  . ARG B 245 ? 0.0842 0.1239 0.1658 0.0078  -0.0059 0.0252  246 ARG B NE  
4290 C  CZ  . ARG B 245 ? 0.0759 0.1246 0.1484 0.0148  0.0041  0.0230  246 ARG B CZ  
4291 N  NH1 . ARG B 245 ? 0.0991 0.1209 0.1530 0.0100  0.0119  0.0214  246 ARG B NH1 
4292 N  NH2 . ARG B 245 ? 0.0957 0.1430 0.1967 0.0256  -0.0149 0.0142  246 ARG B NH2 
4293 N  N   A PRO B 246 ? 0.0869 0.1135 0.1532 -0.0073 -0.0010 0.0032  247 PRO B N   
4294 N  N   B PRO B 246 ? 0.0950 0.0898 0.1541 -0.0013 -0.0059 0.0129  247 PRO B N   
4295 C  CA  A PRO B 246 ? 0.1101 0.1056 0.1299 -0.0209 -0.0210 0.0098  247 PRO B CA  
4296 C  CA  B PRO B 246 ? 0.1450 0.0988 0.1419 -0.0223 -0.0070 0.0078  247 PRO B CA  
4297 C  C   A PRO B 246 ? 0.1101 0.0912 0.1399 -0.0175 -0.0143 0.0065  247 PRO B C   
4298 C  C   B PRO B 246 ? 0.1072 0.0943 0.1317 -0.0063 -0.0227 0.0057  247 PRO B C   
4299 O  O   A PRO B 246 ? 0.0690 0.1155 0.1541 -0.0023 -0.0203 0.0104  247 PRO B O   
4300 O  O   B PRO B 246 ? 0.1250 0.1017 0.1480 -0.0082 -0.0179 0.0155  247 PRO B O   
4301 C  CB  A PRO B 246 ? 0.1577 0.1356 0.1819 -0.0715 0.0044  -0.0214 247 PRO B CB  
4302 C  CB  B PRO B 246 ? 0.1181 0.1647 0.2208 -0.0436 -0.0097 0.0322  247 PRO B CB  
4303 C  CG  A PRO B 246 ? 0.0974 0.1412 0.1805 -0.0397 -0.0012 -0.0153 247 PRO B CG  
4304 C  CG  B PRO B 246 ? 0.1280 0.1615 0.2811 -0.0542 -0.0078 -0.0080 247 PRO B CG  
4305 C  CD  A PRO B 246 ? 0.0810 0.1194 0.2091 -0.0230 -0.0076 -0.0006 247 PRO B CD  
4306 C  CD  B PRO B 246 ? 0.0968 0.1265 0.2502 -0.0205 0.0000  0.0031  247 PRO B CD  
4307 N  N   . ALA B 247 ? 0.1137 0.1196 0.1320 -0.0037 -0.0041 0.0119  248 ALA B N   
4308 C  CA  . ALA B 247 ? 0.1072 0.1320 0.1365 -0.0028 -0.0141 0.0131  248 ALA B CA  
4309 C  C   . ALA B 247 ? 0.0966 0.1189 0.1538 -0.0157 -0.0141 -0.0013 248 ALA B C   
4310 O  O   . ALA B 247 ? 0.1169 0.1297 0.1683 -0.0315 -0.0238 0.0017  248 ALA B O   
4311 C  CB  . ALA B 247 ? 0.1845 0.1299 0.1638 -0.0065 0.0203  -0.0227 248 ALA B CB  
4312 N  N   . GLN B 248 ? 0.0905 0.0998 0.1485 -0.0073 -0.0277 -0.0006 249 GLN B N   
4313 C  CA  . GLN B 248 ? 0.0744 0.1356 0.1485 -0.0068 -0.0265 -0.0048 249 GLN B CA  
4314 C  C   . GLN B 248 ? 0.0856 0.1137 0.1615 -0.0292 -0.0430 -0.0207 249 GLN B C   
4315 O  O   . GLN B 248 ? 0.1248 0.1299 0.1525 -0.0021 -0.0200 -0.0024 249 GLN B O   
4316 C  CB  . GLN B 248 ? 0.1010 0.1228 0.1785 -0.0005 -0.0305 -0.0197 249 GLN B CB  
4317 C  CG  . GLN B 248 ? 0.1119 0.1441 0.1489 -0.0015 -0.0368 0.0000  249 GLN B CG  
4318 C  CD  . GLN B 248 ? 0.0975 0.1753 0.1678 0.0077  -0.0342 -0.0049 249 GLN B CD  
4319 O  OE1 . GLN B 248 ? 0.1088 0.2254 0.2021 0.0414  -0.0179 0.0215  249 GLN B OE1 
4320 N  NE2 . GLN B 248 ? 0.1406 0.1732 0.1679 -0.0087 -0.0094 -0.0007 249 GLN B NE2 
4321 N  N   . PRO B 249 ? 0.1297 0.1723 0.1559 -0.0355 -0.0439 -0.0010 250 PRO B N   
4322 C  CA  . PRO B 249 ? 0.1620 0.2078 0.1747 -0.0450 -0.0568 0.0102  250 PRO B CA  
4323 C  C   . PRO B 249 ? 0.1256 0.1435 0.1532 -0.0143 -0.0502 -0.0087 250 PRO B C   
4324 O  O   . PRO B 249 ? 0.1351 0.1437 0.1564 -0.0303 -0.0417 -0.0040 250 PRO B O   
4325 C  CB  . PRO B 249 ? 0.1365 0.2928 0.2121 -0.0834 -0.0806 0.0553  250 PRO B CB  
4326 C  CG  . PRO B 249 ? 0.2044 0.3068 0.1972 0.0161  -0.0798 0.0156  250 PRO B CG  
4327 C  CD  . PRO B 249 ? 0.0912 0.3086 0.2342 -0.0291 -0.1013 -0.0136 250 PRO B CD  
4328 N  N   . LEU B 250 ? 0.1687 0.1464 0.1448 -0.0399 -0.0355 -0.0137 251 LEU B N   
4329 C  CA  . LEU B 250 ? 0.1518 0.1203 0.1426 -0.0131 -0.0208 0.0062  251 LEU B CA  
4330 C  C   . LEU B 250 ? 0.1746 0.1108 0.1412 -0.0281 -0.0388 -0.0031 251 LEU B C   
4331 O  O   . LEU B 250 ? 0.1412 0.1347 0.1544 -0.0244 -0.0524 0.0037  251 LEU B O   
4332 C  CB  . LEU B 250 ? 0.1996 0.1419 0.1748 -0.0055 0.0244  -0.0208 251 LEU B CB  
4333 C  CG  . LEU B 250 ? 0.1877 0.1694 0.1638 0.0281  0.0236  0.0102  251 LEU B CG  
4334 C  CD1 . LEU B 250 ? 0.1383 0.2360 0.1933 0.0165  -0.0282 0.0313  251 LEU B CD1 
4335 C  CD2 . LEU B 250 ? 0.3057 0.1705 0.2279 0.0693  0.0636  0.0507  251 LEU B CD2 
4336 N  N   . LYS B 251 ? 0.1873 0.1791 0.1473 -0.0452 -0.0720 0.0006  252 LYS B N   
4337 C  CA  . LYS B 251 ? 0.1793 0.2257 0.1503 -0.0250 -0.0432 0.0143  252 LYS B CA  
4338 C  C   . LYS B 251 ? 0.1759 0.1947 0.2191 -0.0335 -0.0727 -0.0020 252 LYS B C   
4339 O  O   . LYS B 251 ? 0.2234 0.2398 0.2101 0.0146  -0.0190 0.0214  252 LYS B O   
4340 C  CB  . LYS B 251 ? 0.2572 0.1938 0.1792 0.0143  -0.0767 0.0209  252 LYS B CB  
4341 C  CG  . LYS B 251 ? 0.2075 0.2739 0.2894 0.0063  -0.0264 0.0366  252 LYS B CG  
4342 C  CD  . LYS B 251 ? 0.1715 0.3204 0.3438 -0.0461 -0.0373 0.0013  252 LYS B CD  
4343 C  CE  . LYS B 251 ? 0.1274 0.3267 0.5587 -0.0439 0.0216  0.0247  252 LYS B CE  
4344 N  NZ  . LYS B 251 ? 0.1875 0.4350 0.5296 0.0430  -0.0868 -0.0738 252 LYS B NZ  
4345 N  N   . ASN B 252 ? 0.2125 0.1829 0.1592 -0.0388 -0.0593 0.0296  253 ASN B N   
4346 C  CA  . ASN B 252 ? 0.2182 0.4623 0.1969 -0.0971 -0.0944 0.0878  253 ASN B CA  
4347 C  C   . ASN B 252 ? 0.2150 0.3280 0.2614 -0.1006 -0.0930 0.0403  253 ASN B C   
4348 O  O   . ASN B 252 ? 0.2711 0.3043 0.3375 -0.0496 -0.0074 0.0535  253 ASN B O   
4349 C  CB  . ASN B 252 ? 0.3010 0.5134 0.3125 -0.0864 -0.1132 0.2003  253 ASN B CB  
4350 C  CG  . ASN B 252 ? 0.3797 0.3774 0.3467 -0.0087 0.0348  0.0808  253 ASN B CG  
4351 O  OD1 . ASN B 252 ? 0.8256 0.6578 0.3610 0.1669  0.0715  -0.0872 253 ASN B OD1 
4352 N  ND2 . ASN B 252 ? 0.4203 0.4729 0.7257 -0.1451 -0.1474 0.3573  253 ASN B ND2 
4353 N  N   . ARG B 253 ? 0.1859 0.3107 0.1309 -0.0623 -0.0388 -0.0171 254 ARG B N   
4354 C  CA  . ARG B 253 ? 0.1645 0.1659 0.1160 -0.0339 -0.0223 -0.0027 254 ARG B CA  
4355 C  C   . ARG B 253 ? 0.2196 0.1520 0.1212 -0.0267 0.0206  -0.0034 254 ARG B C   
4356 O  O   . ARG B 253 ? 0.3400 0.1767 0.3106 -0.0690 0.1306  -0.0702 254 ARG B O   
4357 C  CB  . ARG B 253 ? 0.1819 0.1462 0.1151 -0.0144 -0.0173 0.0054  254 ARG B CB  
4358 C  CG  . ARG B 253 ? 0.1777 0.1460 0.1268 -0.0081 -0.0091 0.0186  254 ARG B CG  
4359 C  CD  . ARG B 253 ? 0.1471 0.1243 0.1153 -0.0021 -0.0192 0.0238  254 ARG B CD  
4360 N  NE  . ARG B 253 ? 0.1437 0.1153 0.1259 0.0017  -0.0192 0.0186  254 ARG B NE  
4361 C  CZ  . ARG B 253 ? 0.1059 0.1067 0.1207 -0.0040 -0.0054 0.0057  254 ARG B CZ  
4362 N  NH1 . ARG B 253 ? 0.0869 0.1160 0.1328 -0.0024 -0.0394 0.0001  254 ARG B NH1 
4363 N  NH2 . ARG B 253 ? 0.0988 0.1209 0.1238 -0.0232 -0.0392 -0.0034 254 ARG B NH2 
4364 N  N   . GLN B 254 ? 0.1746 0.1672 0.1510 -0.0198 -0.0283 0.0463  255 GLN B N   
4365 C  CA  . GLN B 254 ? 0.2010 0.1969 0.1394 -0.0008 -0.0292 0.0395  255 GLN B CA  
4366 C  C   . GLN B 254 ? 0.1592 0.1279 0.1597 -0.0031 -0.0375 -0.0013 255 GLN B C   
4367 O  O   . GLN B 254 ? 0.2721 0.1173 0.2231 0.0086  -0.0685 -0.0083 255 GLN B O   
4368 C  CB  . GLN B 254 ? 0.2394 0.3447 0.1816 -0.0086 -0.0284 0.1240  255 GLN B CB  
4369 C  CG  . GLN B 254 ? 0.3224 0.5091 0.2759 0.0207  -0.0143 0.0768  255 GLN B CG  
4370 C  CD  . GLN B 254 ? 0.5892 0.4350 0.2899 0.1076  0.0397  -0.1295 255 GLN B CD  
4371 O  OE1 . GLN B 254 ? 0.6247 0.2813 0.8062 0.1049  -0.0012 -0.0623 255 GLN B OE1 
4372 N  NE2 . GLN B 254 ? 0.8773 0.3055 0.5961 0.1680  0.1348  -0.0204 255 GLN B NE2 
4373 N  N   A ILE B 255 ? 0.1465 0.1244 0.1275 0.0021  -0.0103 0.0089  256 ILE B N   
4374 N  N   B ILE B 255 ? 0.1473 0.1248 0.1277 0.0020  -0.0104 0.0094  256 ILE B N   
4375 C  CA  A ILE B 255 ? 0.1491 0.1255 0.1081 -0.0172 -0.0129 0.0035  256 ILE B CA  
4376 C  CA  B ILE B 255 ? 0.1492 0.1255 0.1083 -0.0171 -0.0130 0.0035  256 ILE B CA  
4377 C  C   A ILE B 255 ? 0.1528 0.1464 0.1164 -0.0299 0.0017  -0.0285 256 ILE B C   
4378 C  C   B ILE B 255 ? 0.1532 0.1464 0.1162 -0.0300 0.0017  -0.0285 256 ILE B C   
4379 O  O   A ILE B 255 ? 0.1995 0.1457 0.1489 -0.0250 0.0193  -0.0456 256 ILE B O   
4380 O  O   B ILE B 255 ? 0.2001 0.1455 0.1489 -0.0252 0.0190  -0.0461 256 ILE B O   
4381 C  CB  A ILE B 255 ? 0.1841 0.1250 0.1205 -0.0306 -0.0206 0.0026  256 ILE B CB  
4382 C  CB  B ILE B 255 ? 0.1841 0.1250 0.1205 -0.0306 -0.0208 0.0027  256 ILE B CB  
4383 C  CG1 A ILE B 255 ? 0.1539 0.1068 0.1834 -0.0241 -0.0071 0.0166  256 ILE B CG1 
4384 C  CG1 B ILE B 255 ? 0.1543 0.1067 0.1856 -0.0241 -0.0071 0.0176  256 ILE B CG1 
4385 C  CG2 A ILE B 255 ? 0.1190 0.1444 0.1505 -0.0167 -0.0065 0.0006  256 ILE B CG2 
4386 C  CG2 B ILE B 255 ? 0.1205 0.1444 0.1509 -0.0164 -0.0065 0.0006  256 ILE B CG2 
4387 C  CD1 A ILE B 255 ? 0.1362 0.1257 0.1589 -0.0041 0.0357  0.0362  256 ILE B CD1 
4388 C  CD1 B ILE B 255 ? 0.2003 0.1778 0.2137 -0.0028 0.0220  0.0197  256 ILE B CD1 
4389 N  N   . LYS B 256 ? 0.1344 0.1570 0.1054 -0.0184 -0.0105 -0.0181 257 LYS B N   
4390 C  CA  . LYS B 256 ? 0.1392 0.1421 0.1160 -0.0183 0.0114  -0.0126 257 LYS B CA  
4391 C  C   . LYS B 256 ? 0.1536 0.1128 0.1108 0.0000  0.0125  -0.0124 257 LYS B C   
4392 O  O   . LYS B 256 ? 0.1981 0.2075 0.1022 0.0617  0.0063  -0.0052 257 LYS B O   
4393 C  CB  . LYS B 256 ? 0.1622 0.1507 0.1607 -0.0021 0.0104  0.0142  257 LYS B CB  
4394 C  CG  . LYS B 256 ? 0.2297 0.1826 0.2238 0.0375  0.0148  0.0430  257 LYS B CG  
4395 C  CD  . LYS B 256 ? 0.3237 0.2121 0.2517 0.0445  -0.0142 0.0399  257 LYS B CD  
4396 C  CE  . LYS B 256 ? 0.2779 0.3424 0.2944 0.0942  -0.0013 0.0803  257 LYS B CE  
4397 N  NZ  . LYS B 256 ? 0.2597 0.4343 0.4323 0.1308  0.0644  0.1703  257 LYS B NZ  
4398 N  N   . ALA B 257 ? 0.1313 0.1782 0.1092 0.0000  0.0231  -0.0164 258 ALA B N   
4399 C  CA  . ALA B 257 ? 0.1259 0.1376 0.1487 0.0129  0.0021  -0.0086 258 ALA B CA  
4400 C  C   . ALA B 257 ? 0.1326 0.1462 0.1235 0.0252  0.0244  -0.0076 258 ALA B C   
4401 O  O   . ALA B 257 ? 0.1683 0.1870 0.1250 0.0074  0.0296  0.0026  258 ALA B O   
4402 C  CB  . ALA B 257 ? 0.1816 0.1658 0.1771 0.0082  0.0491  -0.0324 258 ALA B CB  
4403 N  N   . SER B 258 ? 0.1234 0.1553 0.1377 0.0023  0.0071  -0.0115 259 SER B N   
4404 C  CA  . SER B 258 ? 0.1360 0.1805 0.1571 -0.0148 0.0285  0.0007  259 SER B CA  
4405 C  C   . SER B 258 ? 0.1054 0.1965 0.1778 0.0148  0.0296  -0.0010 259 SER B C   
4406 O  O   . SER B 258 ? 0.1379 0.3100 0.2064 -0.0189 0.0344  -0.0098 259 SER B O   
4407 C  CB  . SER B 258 ? 0.1924 0.1577 0.1615 0.0081  -0.0059 0.0006  259 SER B CB  
4408 O  OG  . SER B 258 ? 0.1246 0.2019 0.1387 0.0043  0.0219  0.0038  259 SER B OG  
4409 N  N   . PHE B 259 ? 0.1669 0.1871 0.1917 0.0305  0.0463  -0.0093 260 PHE B N   
4410 C  CA  . PHE B 259 ? 0.2202 0.2314 0.2101 0.0582  0.0732  -0.0288 260 PHE B CA  
4411 C  C   . PHE B 259 ? 0.2414 0.2741 0.2268 0.0555  0.0737  -0.0271 260 PHE B C   
4412 O  O   . PHE B 259 ? 0.3145 0.2114 0.2425 0.0621  0.0368  -0.0772 260 PHE B O   
4413 C  CB  . PHE B 259 ? 0.1453 0.2597 0.2360 0.0298  0.0277  0.0295  260 PHE B CB  
4414 C  CG  . PHE B 259 ? 0.1561 0.2109 0.2116 0.0421  0.0038  -0.0372 260 PHE B CG  
4415 C  CD1 . PHE B 259 ? 0.1737 0.1828 0.1658 0.0351  -0.0006 -0.0089 260 PHE B CD1 
4416 C  CD2 . PHE B 259 ? 0.2676 0.1758 0.2845 0.0362  0.0533  -0.0242 260 PHE B CD2 
4417 C  CE1 . PHE B 259 ? 0.1676 0.1976 0.2329 0.0456  -0.0109 0.0427  260 PHE B CE1 
4418 C  CE2 . PHE B 259 ? 0.2396 0.2234 0.2894 0.0188  0.0328  -0.0432 260 PHE B CE2 
4419 C  CZ  . PHE B 259 ? 0.2673 0.2155 0.2481 0.0599  0.0192  0.0366  260 PHE B CZ  
4420 N  N   . LYS B 260 ? 0.4034 0.3932 0.2513 0.1580  0.0961  -0.0710 261 LYS B N   
4421 C  CA  . LYS B 260 ? 0.6492 0.5141 0.2249 0.1142  0.0869  -0.1247 261 LYS B CA  
4422 C  C   . LYS B 260 ? 0.5925 0.6832 0.4653 0.1926  -0.0760 -0.0864 261 LYS B C   
4423 O  O   . LYS B 260 ? 0.5588 0.4431 0.3474 0.1133  0.0509  -0.0741 261 LYS B O   
4424 C  CB  . LYS B 260 ? 0.7404 0.4832 0.5371 0.1389  0.0661  0.0097  261 LYS B CB  
4425 C  CG  . LYS B 260 ? 0.8288 0.3704 0.6593 0.3745  0.1288  -0.0013 261 LYS B CG  
4426 C  CD  . LYS B 260 ? 0.7203 0.5834 0.8123 0.1976  0.2642  0.1111  261 LYS B CD  
4427 C  CE  . LYS B 260 ? 0.7215 0.4533 0.4548 -0.1168 0.1664  -0.2463 261 LYS B CE  
4428 N  NZ  . LYS B 260 ? 0.7034 0.4939 0.9348 0.0727  0.0922  0.0026  261 LYS B NZ  
4429 O  OXT . LYS B 260 ? 1.0142 0.7592 0.7536 0.3878  0.2718  -0.0983 261 LYS B OXT 
4430 ZN ZN  . ZN  C .   ? 0.0887 0.0623 0.0977 -0.0060 -0.0049 -0.0066 301 ZN  A ZN  
4431 S  S   . DMS D .   ? 0.2238 0.2533 0.3373 -0.0156 0.0458  -0.0542 302 DMS A S   
4432 O  O   . DMS D .   ? 0.3887 0.3129 0.3194 0.1018  0.0494  -0.0842 302 DMS A O   
4433 C  C1  . DMS D .   ? 0.2209 0.2204 0.2633 0.0397  0.0172  -0.0776 302 DMS A C1  
4434 C  C2  . DMS D .   ? 0.1791 0.2135 0.4767 -0.0052 0.0273  -0.0208 302 DMS A C2  
4435 N  N1  . BCN E .   ? 0.2949 0.3328 0.3398 0.0001  -0.0031 -0.0155 303 BCN A N1  
4436 C  C1  . BCN E .   ? 0.2757 0.3847 0.2500 -0.0636 0.0163  0.0172  303 BCN A C1  
4437 C  C2  . BCN E .   ? 0.2603 0.2840 0.3325 -0.0842 0.0403  0.0436  303 BCN A C2  
4438 O  O21 . BCN E .   ? 0.3582 0.2908 0.4614 -0.1002 -0.0630 0.0895  303 BCN A O21 
4439 O  O22 . BCN E .   ? 0.3294 0.3039 0.3402 -0.0504 0.0340  0.0288  303 BCN A O22 
4440 C  C3  . BCN E .   ? 0.2205 0.1498 0.2766 -0.0263 -0.0068 0.0324  303 BCN A C3  
4441 C  C4  . BCN E .   ? 0.4176 0.4666 0.3564 -0.0537 -0.0346 0.0610  303 BCN A C4  
4442 O  O4  . BCN E .   ? 0.5544 0.4727 0.8519 -0.2484 -0.3131 -0.0542 303 BCN A O4  
4443 C  C5  . BCN E .   ? 0.1909 0.1572 0.2363 -0.0307 0.0129  0.0164  303 BCN A C5  
4444 C  C6  . BCN E .   ? 0.4521 0.3950 0.3980 -0.1185 -0.0877 -0.0595 303 BCN A C6  
4445 O  O6  . BCN E .   ? 0.4890 0.2860 0.4763 -0.1726 0.0364  0.0205  303 BCN A O6  
4446 C  C1  . PEG F .   ? 0.5159 0.5238 0.5264 -0.0280 -0.0828 -0.1076 304 PEG A C1  
4447 O  O1  . PEG F .   ? 0.5012 0.5649 0.5924 0.1762  0.0178  -0.0555 304 PEG A O1  
4448 C  C2  . PEG F .   ? 0.4797 0.3217 0.4244 0.0500  -0.1537 -0.0146 304 PEG A C2  
4449 O  O2  . PEG F .   ? 0.3533 0.3768 0.4499 0.0458  0.0156  -0.0219 304 PEG A O2  
4450 C  C3  . PEG F .   ? 0.4323 0.3086 0.4807 0.0357  -0.0405 -0.0603 304 PEG A C3  
4451 C  C4  . PEG F .   ? 0.4086 0.3452 0.3982 0.0329  -0.0697 -0.0313 304 PEG A C4  
4452 O  O4  . PEG F .   ? 0.3393 0.3289 0.5338 0.0480  -0.0397 -0.0353 304 PEG A O4  
4453 C  C1  . MLA G .   ? 0.4625 0.6434 0.5037 -0.1861 0.0027  0.0217  305 MLA A C1  
4454 O  O1A . MLA G .   ? 0.6699 0.7002 0.4266 0.0044  0.0142  0.0452  305 MLA A O1A 
4455 O  O1B . MLA G .   ? 0.7071 0.7366 0.5070 -0.1386 0.0697  0.0568  305 MLA A O1B 
4456 C  C2  . MLA G .   ? 0.3982 0.5284 0.5428 0.0043  -0.0239 -0.0151 305 MLA A C2  
4457 C  C3  . MLA G .   ? 0.6297 0.5332 0.3689 0.0012  0.0666  -0.0454 305 MLA A C3  
4458 O  O3A . MLA G .   ? 0.4962 0.2506 0.4189 -0.0883 0.0657  -0.0003 305 MLA A O3A 
4459 O  O3B . MLA G .   ? 0.4753 0.5011 0.3820 -0.0834 -0.0838 0.0052  305 MLA A O3B 
4460 O  O12 . 6YH H .   ? 0.2400 0.1410 0.2777 0.0178  0.0308  0.0640  306 6YH A O12 
4461 C  C11 . 6YH H .   ? 0.1586 0.1410 0.2096 0.0071  0.0232  0.0230  306 6YH A C11 
4462 C  C4  . 6YH H .   ? 0.1683 0.1020 0.1627 0.0008  0.0232  0.0286  306 6YH A C4  
4463 C  C3  . 6YH H .   ? 0.1328 0.0950 0.1570 -0.0003 -0.0119 0.0087  306 6YH A C3  
4464 C  C2  . 6YH H .   ? 0.1261 0.0768 0.1460 -0.0094 -0.0187 -0.0083 306 6YH A C2  
4465 C  C5  . 6YH H .   ? 0.1611 0.1280 0.1805 0.0012  0.0186  0.0329  306 6YH A C5  
4466 C  C6  . 6YH H .   ? 0.1244 0.1160 0.1681 0.0136  0.0104  0.0274  306 6YH A C6  
4467 C  C1  . 6YH H .   ? 0.1099 0.0842 0.1410 0.0010  -0.0017 0.0028  306 6YH A C1  
4468 S  S7  . 6YH H .   ? 0.0856 0.0706 0.1111 -0.0028 -0.0086 -0.0110 306 6YH A S7  
4469 O  O9  . 6YH H .   ? 0.0816 0.0804 0.1184 0.0035  -0.0020 -0.0126 306 6YH A O9  
4470 N  N10 . 6YH H .   ? 0.0923 0.0562 0.1137 -0.0186 -0.0118 -0.0269 306 6YH A N10 
4471 O  O8  . 6YH H .   ? 0.0794 0.0802 0.1140 -0.0023 -0.0151 -0.0148 306 6YH A O8  
4472 C  C13 . 6YH H .   ? 0.1933 0.1705 0.2500 -0.0579 0.0285  0.0405  306 6YH A C13 
4473 N  N14 . 6YH H .   ? 0.2304 0.1805 0.2222 -0.0399 0.0364  0.0230  306 6YH A N14 
4474 C  C18 . 6YH H .   ? 0.2287 0.1852 0.2057 -0.0225 0.0218  0.0137  306 6YH A C18 
4475 C  C20 . 6YH H .   ? 0.1855 0.2150 0.2105 0.0162  0.0283  -0.0013 306 6YH A C20 
4476 C  C21 . 6YH H .   ? 0.2202 0.2347 0.2189 0.0412  0.0109  -0.0307 306 6YH A C21 
4477 C  C22 . 6YH H .   ? 0.2712 0.2292 0.2569 -0.0015 0.0186  -0.0571 306 6YH A C22 
4478 C  C23 . 6YH H .   ? 0.3477 0.2290 0.2489 -0.0511 -0.0183 0.0052  306 6YH A C23 
4479 C  C19 . 6YH H .   ? 0.2854 0.2029 0.2108 -0.0524 0.0315  0.0132  306 6YH A C19 
4480 N  N17 . 6YH H .   ? 0.2851 0.2220 0.2478 -0.0732 0.0483  0.0388  306 6YH A N17 
4481 C  C16 . 6YH H .   ? 0.3104 0.2107 0.2579 -0.0445 0.0216  0.0092  306 6YH A C16 
4482 ZN ZN  . ZN  I .   ? 0.0975 0.0754 0.0952 0.0111  -0.0068 0.0031  301 ZN  B ZN  
4483 S  S   . DMS J .   ? 0.2362 0.2757 0.3102 0.0012  0.0219  0.0295  302 DMS B S   
4484 O  O   . DMS J .   ? 0.3973 0.4964 1.7142 -0.0280 0.0868  -0.2982 302 DMS B O   
4485 C  C1  . DMS J .   ? 0.2831 0.2682 0.2994 -0.0471 0.0864  0.0772  302 DMS B C1  
4486 C  C2  . DMS J .   ? 0.1791 0.2639 0.2509 -0.0511 0.0078  0.0522  302 DMS B C2  
4487 N  N1  . BCN K .   ? 0.2958 0.3330 0.3964 0.0277  0.0240  0.0590  303 BCN B N1  
4488 C  C1  . BCN K .   ? 0.1953 0.1615 0.2608 0.0076  0.0230  -0.0405 303 BCN B C1  
4489 C  C2  . BCN K .   ? 1.0864 0.7336 0.4101 0.2802  -0.3077 0.1473  303 BCN B C2  
4490 O  O21 . BCN K .   ? 1.8751 1.0487 1.4699 0.2097  0.5465  -0.1254 303 BCN B O21 
4491 O  O22 . BCN K .   ? 0.7156 0.4634 0.4503 0.4041  -0.1136 -0.1331 303 BCN B O22 
4492 C  C3  . BCN K .   ? 0.1875 0.5000 0.3030 0.1026  -0.0364 -0.0615 303 BCN B C3  
4493 C  C4  . BCN K .   ? 0.4013 0.5964 0.2319 -0.1652 0.0215  -0.1094 303 BCN B C4  
4494 O  O4  . BCN K .   ? 0.3517 0.3398 0.3345 0.0491  0.0129  -0.1086 303 BCN B O4  
4495 C  C5  . BCN K .   ? 0.2123 0.1947 0.3152 0.0135  0.0489  -0.0527 303 BCN B C5  
4496 C  C6  . BCN K .   ? 0.3808 0.3838 0.4174 0.0441  0.0068  0.0392  303 BCN B C6  
4497 O  O6  . BCN K .   ? 0.4415 0.3267 0.6696 -0.0454 0.2707  -0.1551 303 BCN B O6  
4498 C  C1  . MLA L .   ? 0.6517 0.4702 0.3914 -0.0529 -0.0120 0.0000  304 MLA B C1  
4499 O  O1A . MLA L .   ? 0.4998 0.3140 0.4519 0.0342  0.0562  0.0175  304 MLA B O1A 
4500 O  O1B . MLA L .   ? 0.5990 0.4718 0.4291 0.1165  -0.0817 -0.0251 304 MLA B O1B 
4501 C  C2  . MLA L .   ? 0.3503 0.3991 0.5091 0.0263  -0.0030 -0.0199 304 MLA B C2  
4502 C  C3  . MLA L .   ? 0.3734 0.2896 0.6369 0.0476  -0.0564 -0.0362 304 MLA B C3  
4503 O  O3A . MLA L .   ? 0.4785 0.5616 0.5424 -0.1233 -0.0381 -0.0619 304 MLA B O3A 
4504 O  O3B . MLA L .   ? 0.7560 0.5209 0.7781 -0.0724 0.0348  -0.1709 304 MLA B O3B 
4505 O  O12 . 6YH M .   ? 0.2412 0.1483 0.2728 -0.0092 0.0308  -0.0560 305 6YH B O12 
4506 C  C11 . 6YH M .   ? 0.1902 0.1532 0.2250 0.0021  0.0223  -0.0504 305 6YH B C11 
4507 C  C4  . 6YH M .   ? 0.1667 0.1106 0.1742 -0.0091 0.0207  -0.0264 305 6YH B C4  
4508 C  C3  . 6YH M .   ? 0.1498 0.1383 0.1899 -0.0104 0.0328  -0.0331 305 6YH B C3  
4509 C  C2  . 6YH M .   ? 0.1279 0.1246 0.1645 0.0013  0.0115  -0.0179 305 6YH B C2  
4510 C  C5  . 6YH M .   ? 0.1410 0.1008 0.1647 0.0034  -0.0125 -0.0168 305 6YH B C5  
4511 C  C6  . 6YH M .   ? 0.1360 0.0861 0.1518 0.0107  -0.0206 -0.0051 305 6YH B C6  
4512 C  C1  . 6YH M .   ? 0.1121 0.1038 0.1395 0.0082  -0.0074 0.0005  305 6YH B C1  
4513 S  S7  . 6YH M .   ? 0.0922 0.0804 0.1128 0.0096  -0.0108 0.0092  305 6YH B S7  
4514 O  O9  . 6YH M .   ? 0.0905 0.0916 0.1162 0.0081  -0.0093 0.0148  305 6YH B O9  
4515 N  N10 . 6YH M .   ? 0.1027 0.0597 0.1093 0.0177  -0.0046 0.0153  305 6YH B N10 
4516 O  O8  . 6YH M .   ? 0.0916 0.0939 0.1184 0.0086  -0.0132 0.0125  305 6YH B O8  
4517 C  C13 . 6YH M .   ? 0.2245 0.1929 0.2827 0.0750  0.0300  -0.0546 305 6YH B C13 
4518 N  N14 . 6YH M .   ? 0.2148 0.1947 0.2372 0.0452  0.0447  -0.0339 305 6YH B N14 
4519 C  C18 . 6YH M .   ? 0.2646 0.1803 0.1997 0.0054  0.0142  -0.0170 305 6YH B C18 
4520 C  C20 . 6YH M .   ? 0.1814 0.2089 0.2143 -0.0273 0.0129  -0.0274 305 6YH B C20 
4521 C  C21 . 6YH M .   ? 0.2364 0.2299 0.2141 -0.0511 0.0028  0.0211  305 6YH B C21 
4522 C  C22 . 6YH M .   ? 0.2563 0.2143 0.2365 -0.0070 0.0278  0.0126  305 6YH B C22 
4523 C  C23 . 6YH M .   ? 0.3303 0.2093 0.2432 -0.0024 0.0031  -0.0122 305 6YH B C23 
4524 C  C19 . 6YH M .   ? 0.3048 0.2144 0.2324 0.0507  0.0225  -0.0346 305 6YH B C19 
4525 N  N17 . 6YH M .   ? 0.2942 0.2354 0.2621 0.0689  0.0303  -0.0303 305 6YH B N17 
4526 C  C16 . 6YH M .   ? 0.3219 0.2462 0.2748 0.0679  0.0428  -0.0493 305 6YH B C16 
4527 O  O   . HOH N .   ? 0.3007 0.3813 0.3700 0.0527  -0.0908 0.0689  401 HOH A O   
4528 O  O   . HOH N .   ? 0.3070 0.6216 0.5960 -0.0763 -0.1129 0.0020  402 HOH A O   
4529 O  O   . HOH N .   ? 0.3138 0.5838 0.8001 0.1077  0.0282  0.1704  403 HOH A O   
4530 O  O   . HOH N .   ? 0.1789 0.3420 0.7736 -0.0217 0.0683  -0.1284 404 HOH A O   
4531 O  O   . HOH N .   ? 0.3174 0.1081 0.2558 -0.0013 -0.0035 -0.0155 405 HOH A O   
4532 O  O   . HOH N .   ? 0.2662 0.7196 0.5712 -0.0649 -0.0280 -0.3037 406 HOH A O   
4533 O  O   . HOH N .   ? 0.4377 0.5788 0.6431 0.1040  0.2662  0.0066  407 HOH A O   
4534 O  O   . HOH N .   ? 0.3959 0.6353 0.6179 0.0087  -0.2135 0.0882  408 HOH A O   
4535 O  O   . HOH N .   ? 0.2714 0.1351 0.3776 -0.0006 -0.0593 -0.0263 409 HOH A O   
4536 O  O   . HOH N .   ? 0.2730 0.6036 0.2822 0.0397  -0.0584 0.0694  410 HOH A O   
4537 O  O   . HOH N .   ? 0.5938 0.2766 0.4893 -0.1419 -0.0454 0.0199  411 HOH A O   
4538 O  O   . HOH N .   ? 0.6144 0.3407 0.3874 -0.0225 -0.0361 0.0869  412 HOH A O   
4539 O  O   . HOH N .   ? 0.5084 0.2170 0.5322 -0.0291 0.0794  0.0899  413 HOH A O   
4540 O  O   . HOH N .   ? 0.1295 0.8305 1.1208 -0.1937 0.1955  -0.5241 414 HOH A O   
4541 O  O   . HOH N .   ? 0.4384 0.3255 0.2935 -0.0200 0.0052  0.0285  415 HOH A O   
4542 O  O   . HOH N .   ? 0.2547 0.2340 0.7056 0.0315  0.1569  0.1577  416 HOH A O   
4543 O  O   . HOH N .   ? 0.1155 0.5662 0.4747 0.0870  0.0019  -0.1729 417 HOH A O   
4544 O  O   . HOH N .   ? 0.2610 0.2301 0.4745 -0.0364 -0.0529 0.0120  418 HOH A O   
4545 O  O   . HOH N .   ? 0.4496 0.5051 0.2496 0.0469  0.0227  -0.1268 419 HOH A O   
4546 O  O   . HOH N .   ? 0.5295 0.1132 0.2215 0.0098  -0.1888 0.0172  420 HOH A O   
4547 O  O   . HOH N .   ? 0.2976 0.5350 0.6291 0.0020  -0.0931 -0.0405 421 HOH A O   
4548 O  O   . HOH N .   ? 0.1072 0.0988 0.1439 -0.0098 0.0127  -0.0264 422 HOH A O   
4549 O  O   . HOH N .   ? 0.3524 0.4009 0.4372 -0.0272 0.1615  -0.0254 423 HOH A O   
4550 O  O   . HOH N .   ? 1.1546 0.8989 0.3488 0.1661  0.0375  -0.0684 424 HOH A O   
4551 O  O   . HOH N .   ? 0.4095 0.3727 0.3382 -0.0750 -0.0507 0.0754  425 HOH A O   
4552 O  O   . HOH N .   ? 0.6219 0.1756 0.5659 -0.0904 -0.1119 -0.0502 426 HOH A O   
4553 O  O   . HOH N .   ? 0.3294 0.6341 0.6388 0.1503  0.1657  -0.0754 427 HOH A O   
4554 O  O   . HOH N .   ? 0.6301 0.2353 0.4582 0.0242  0.1456  -0.0659 428 HOH A O   
4555 O  O   . HOH N .   ? 0.3348 0.7649 0.2041 0.0038  0.0527  -0.0463 429 HOH A O   
4556 O  O   . HOH N .   ? 0.4050 0.4244 0.6560 0.2202  0.1303  0.1070  430 HOH A O   
4557 O  O   . HOH N .   ? 0.2987 0.3352 0.3479 -0.1228 0.1379  -0.1586 431 HOH A O   
4558 O  O   . HOH N .   ? 0.5490 0.3066 0.4104 -0.0240 -0.2240 0.0767  432 HOH A O   
4559 O  O   . HOH N .   ? 0.5465 0.5356 0.2623 -0.0273 0.1194  -0.0527 433 HOH A O   
4560 O  O   . HOH N .   ? 0.1473 0.5572 0.2168 -0.0357 -0.0074 -0.0271 434 HOH A O   
4561 O  O   . HOH N .   ? 0.2030 0.1738 0.2565 0.0131  0.0168  0.0390  435 HOH A O   
4562 O  O   . HOH N .   ? 0.2786 0.3761 0.6294 -0.0991 -0.1759 0.2973  436 HOH A O   
4563 O  O   . HOH N .   ? 0.2134 0.6380 0.6308 0.0231  -0.1089 -0.0733 437 HOH A O   
4564 O  O   . HOH N .   ? 0.7401 0.4510 0.3371 0.0962  0.0030  -0.0718 438 HOH A O   
4565 O  O   . HOH N .   ? 0.5379 0.4147 0.2928 -0.0837 -0.0154 -0.0623 439 HOH A O   
4566 O  O   . HOH N .   ? 0.3614 0.3063 0.6423 0.1500  -0.2563 -0.1547 440 HOH A O   
4567 O  O   . HOH N .   ? 0.1674 0.3116 0.4708 0.0636  0.0480  0.0601  441 HOH A O   
4568 O  O   . HOH N .   ? 0.2080 0.0912 0.0864 -0.0208 -0.0006 -0.0037 442 HOH A O   
4569 O  O   . HOH N .   ? 0.2198 0.1873 0.3379 0.0252  -0.1638 -0.0546 443 HOH A O   
4570 O  O   . HOH N .   ? 0.3564 0.4702 0.4803 0.0195  -0.0322 -0.1914 444 HOH A O   
4571 O  O   . HOH N .   ? 0.5566 0.3079 0.5885 0.0500  -0.3650 -0.1455 445 HOH A O   
4572 O  O   . HOH N .   ? 0.3161 0.5539 0.1782 -0.1424 -0.1076 0.0886  446 HOH A O   
4573 O  O   . HOH N .   ? 1.5630 0.7134 0.6111 0.3894  -0.0795 0.1256  447 HOH A O   
4574 O  O   . HOH N .   ? 0.1780 0.2144 0.2998 0.0121  0.0032  0.0309  448 HOH A O   
4575 O  O   . HOH N .   ? 0.3440 0.3289 0.4135 0.0848  -0.1617 -0.2246 449 HOH A O   
4576 O  O   . HOH N .   ? 0.3521 0.1990 0.3481 -0.0597 0.0714  -0.0760 450 HOH A O   
4577 O  O   . HOH N .   ? 0.1288 0.0894 0.1297 -0.0073 -0.0024 -0.0143 451 HOH A O   
4578 O  O   . HOH N .   ? 0.3102 0.3424 0.2554 -0.0860 -0.0351 -0.0718 452 HOH A O   
4579 O  O   . HOH N .   ? 0.2006 0.5508 0.3039 -0.0412 -0.0776 -0.0054 453 HOH A O   
4580 O  O   . HOH N .   ? 0.4221 0.4072 0.4061 -0.0207 0.0074  -0.0017 454 HOH A O   
4581 O  O   . HOH N .   ? 0.3073 0.2405 0.1674 -0.0225 -0.0702 0.0167  455 HOH A O   
4582 O  O   . HOH N .   ? 0.4365 0.2781 0.2524 -0.0263 -0.1477 -0.0204 456 HOH A O   
4583 O  O   . HOH N .   ? 0.8420 0.2897 0.2358 0.0151  -0.1163 -0.0921 457 HOH A O   
4584 O  O   . HOH N .   ? 0.2816 0.1906 0.2421 -0.0760 -0.0401 -0.0249 458 HOH A O   
4585 O  O   . HOH N .   ? 0.1699 0.2050 0.2800 0.0138  0.0421  0.0469  459 HOH A O   
4586 O  O   . HOH N .   ? 0.2320 0.4268 0.3761 -0.0568 -0.0309 -0.0340 460 HOH A O   
4587 O  O   . HOH N .   ? 0.2083 0.2286 0.3332 -0.0456 -0.0566 0.0806  461 HOH A O   
4588 O  O   . HOH N .   ? 0.5842 0.2574 0.1778 -0.0445 -0.0406 -0.0511 462 HOH A O   
4589 O  O   . HOH N .   ? 0.4778 0.3526 0.5332 0.0586  0.1168  0.0205  463 HOH A O   
4590 O  O   . HOH N .   ? 0.5159 0.2628 0.5246 -0.0317 -0.0263 0.1111  464 HOH A O   
4591 O  O   . HOH N .   ? 0.2060 0.1681 0.2912 0.0283  0.0476  0.0126  465 HOH A O   
4592 O  O   . HOH N .   ? 0.2154 0.2218 0.2270 -0.0054 -0.0366 0.0232  466 HOH A O   
4593 O  O   . HOH N .   ? 0.6140 0.1768 0.2105 -0.1136 -0.0560 0.0597  467 HOH A O   
4594 O  O   . HOH N .   ? 0.1478 0.0986 0.1360 0.0006  0.0097  -0.0120 468 HOH A O   
4595 O  O   . HOH N .   ? 0.2739 0.3837 0.8550 -0.0551 -0.2337 -0.0204 469 HOH A O   
4596 O  O   . HOH N .   ? 0.4507 0.3249 0.3531 -0.1093 0.0260  -0.0256 470 HOH A O   
4597 O  O   . HOH N .   ? 0.2646 0.1796 0.2849 0.0315  0.0052  0.0529  471 HOH A O   
4598 O  O   . HOH N .   ? 0.3136 0.6272 0.6103 0.0627  0.1791  0.1652  472 HOH A O   
4599 O  O   . HOH N .   ? 0.4914 0.4025 0.3352 -0.1657 0.1876  -0.1776 473 HOH A O   
4600 O  O   . HOH N .   ? 0.2851 0.1735 0.2637 -0.0366 0.0105  -0.0250 474 HOH A O   
4601 O  O   . HOH N .   ? 0.5465 0.1941 0.2506 -0.0181 -0.0731 0.1039  475 HOH A O   
4602 O  O   . HOH N .   ? 0.3107 0.3188 0.2351 -0.0989 0.0643  0.0057  476 HOH A O   
4603 O  O   . HOH N .   ? 0.2994 0.1647 0.4557 0.0394  -0.0430 0.0052  477 HOH A O   
4604 O  O   . HOH N .   ? 0.4167 0.2154 0.1926 -0.0903 0.1005  -0.0028 478 HOH A O   
4605 O  O   . HOH N .   ? 0.4422 0.1741 0.3109 -0.0010 -0.0847 0.0034  479 HOH A O   
4606 O  O   . HOH N .   ? 0.2189 0.1967 0.2019 0.0322  0.0496  -0.0273 480 HOH A O   
4607 O  O   . HOH N .   ? 0.2208 0.3258 0.2991 0.0166  0.0666  -0.0333 481 HOH A O   
4608 O  O   . HOH N .   ? 0.4921 0.2675 0.7519 -0.0636 0.1137  -0.2347 482 HOH A O   
4609 O  O   . HOH N .   ? 0.5968 0.4230 0.3856 -0.1363 -0.0299 0.0500  483 HOH A O   
4610 O  O   . HOH N .   ? 0.2626 0.3652 0.3143 0.0527  0.0160  0.0057  484 HOH A O   
4611 O  O   . HOH N .   ? 0.1704 0.1313 0.1920 -0.0065 -0.0197 0.0216  485 HOH A O   
4612 O  O   . HOH N .   ? 0.3643 0.2403 0.2337 0.0057  0.0209  -0.0454 486 HOH A O   
4613 O  O   . HOH N .   ? 0.2321 0.4146 0.2782 -0.0841 0.0000  0.0744  487 HOH A O   
4614 O  O   . HOH N .   ? 0.2913 0.2538 0.5001 -0.1539 -0.0634 0.0240  488 HOH A O   
4615 O  O   . HOH N .   ? 0.6409 0.4756 0.3811 -0.1332 0.1864  -0.0952 489 HOH A O   
4616 O  O   . HOH N .   ? 0.3298 0.3524 0.4399 0.0668  0.1638  -0.0353 490 HOH A O   
4617 O  O   . HOH N .   ? 0.2912 0.2448 0.4836 -0.0207 0.1645  0.0582  491 HOH A O   
4618 O  O   . HOH N .   ? 0.5375 0.4072 0.6405 -0.1719 0.0882  0.0340  492 HOH A O   
4619 O  O   . HOH N .   ? 0.1591 0.0707 0.1726 -0.0060 -0.0031 -0.0049 493 HOH A O   
4620 O  O   . HOH N .   ? 0.1785 0.1160 0.1893 -0.0109 -0.0296 -0.0013 494 HOH A O   
4621 O  O   . HOH N .   ? 0.2243 0.3219 0.4291 0.0866  -0.0098 0.0568  495 HOH A O   
4622 O  O   . HOH N .   ? 0.0869 0.0927 0.1334 -0.0098 0.0037  0.0005  496 HOH A O   
4623 O  O   . HOH N .   ? 0.0992 0.0847 0.1444 0.0013  -0.0153 -0.0152 497 HOH A O   
4624 O  O   . HOH N .   ? 0.4000 0.4327 0.3790 -0.0172 0.0126  0.0131  498 HOH A O   
4625 O  O   . HOH N .   ? 0.5953 0.2982 0.2563 -0.1208 0.0397  -0.1146 499 HOH A O   
4626 O  O   . HOH N .   ? 1.0117 0.3594 0.5805 -0.2662 0.4146  -0.0727 500 HOH A O   
4627 O  O   . HOH N .   ? 0.0712 0.1424 0.2238 0.0003  -0.0031 -0.0377 501 HOH A O   
4628 O  O   . HOH N .   ? 0.4357 0.3429 0.4782 -0.1129 -0.0685 -0.0520 502 HOH A O   
4629 O  O   . HOH N .   ? 0.2448 0.1868 0.3849 -0.0326 0.0747  -0.0789 503 HOH A O   
4630 O  O   . HOH N .   ? 0.5848 0.6704 0.3583 0.0895  0.0026  -0.0406 504 HOH A O   
4631 O  O   . HOH N .   ? 0.1697 0.1667 0.2423 -0.0094 -0.0108 -0.0361 505 HOH A O   
4632 O  O   . HOH N .   ? 0.2664 0.4914 0.5722 -0.0882 0.1538  -0.0815 506 HOH A O   
4633 O  O   . HOH N .   ? 0.3801 0.3404 0.3637 -0.0439 0.0324  -0.0927 507 HOH A O   
4634 O  O   . HOH N .   ? 0.1031 0.1146 0.1347 0.0344  -0.0113 -0.0074 508 HOH A O   
4635 O  O   . HOH N .   ? 0.4867 0.2497 0.2293 -0.0920 0.1155  -0.1121 509 HOH A O   
4636 O  O   . HOH N .   ? 0.6262 0.2487 0.3844 -0.0489 0.1086  -0.0610 510 HOH A O   
4637 O  O   . HOH N .   ? 0.2238 0.1371 0.2019 -0.0038 -0.0483 -0.0189 511 HOH A O   
4638 O  O   . HOH N .   ? 0.2487 0.2608 0.1868 -0.0107 -0.0242 -0.0688 512 HOH A O   
4639 O  O   . HOH N .   ? 0.1126 0.1378 0.1656 0.0038  -0.0412 0.0192  513 HOH A O   
4640 O  O   . HOH N .   ? 0.3064 0.7950 0.4760 -0.0182 0.0021  0.3795  514 HOH A O   
4641 O  O   . HOH N .   ? 0.4514 0.1550 0.3350 0.1062  -0.0861 -0.0144 515 HOH A O   
4642 O  O   . HOH N .   ? 0.2971 0.2518 0.9944 -0.0317 -0.0181 0.0671  516 HOH A O   
4643 O  O   . HOH N .   ? 0.2344 0.2531 0.1970 0.0296  -0.0136 0.0270  517 HOH A O   
4644 O  O   . HOH N .   ? 0.3456 0.6292 0.1990 0.1330  -0.1327 -0.0754 518 HOH A O   
4645 O  O   . HOH N .   ? 0.4499 0.4325 0.4079 0.0524  -0.0982 -0.0241 519 HOH A O   
4646 O  O   . HOH N .   ? 0.2547 0.4702 0.4117 0.0183  0.0200  -0.0654 520 HOH A O   
4647 O  O   . HOH N .   ? 0.2583 0.2992 0.3194 -0.0003 0.0049  0.0346  521 HOH A O   
4648 O  O   . HOH N .   ? 0.4210 0.2998 0.4711 0.0086  -0.0271 0.2240  522 HOH A O   
4649 O  O   . HOH N .   ? 0.5246 0.4426 0.3558 0.0329  -0.0197 0.0346  523 HOH A O   
4650 O  O   . HOH N .   ? 0.1959 0.1803 0.1927 0.0175  -0.0631 0.0171  524 HOH A O   
4651 O  O   . HOH N .   ? 0.5698 0.4607 0.5993 0.2392  0.2646  0.1507  525 HOH A O   
4652 O  O   . HOH N .   ? 0.4072 0.4004 0.3474 0.0074  -0.0529 -0.0093 526 HOH A O   
4653 O  O   . HOH N .   ? 0.1027 0.1164 0.1780 0.0164  -0.0328 0.0160  527 HOH A O   
4654 O  O   . HOH N .   ? 0.1958 0.1379 0.2669 0.0504  -0.0085 -0.0434 528 HOH A O   
4655 O  O   . HOH N .   ? 0.3258 0.1704 0.2197 0.0930  -0.0983 -0.0185 529 HOH A O   
4656 O  O   . HOH N .   ? 0.1525 0.1032 0.1583 -0.0030 -0.0104 0.0006  530 HOH A O   
4657 O  O   . HOH N .   ? 0.2261 0.3657 0.4113 0.0152  0.0608  0.0802  531 HOH A O   
4658 O  O   . HOH N .   ? 0.8407 0.1922 0.1884 0.0193  0.0297  0.0024  532 HOH A O   
4659 O  O   . HOH N .   ? 0.3652 0.5485 0.2372 -0.1015 -0.1482 0.1465  533 HOH A O   
4660 O  O   . HOH N .   ? 0.4918 0.5906 0.3783 -0.2162 -0.0714 0.2243  534 HOH A O   
4661 O  O   . HOH N .   ? 0.3186 0.2340 0.3208 0.0109  -0.0767 0.0856  535 HOH A O   
4662 O  O   . HOH N .   ? 0.2236 0.5942 0.6682 0.0238  0.0304  -0.0773 536 HOH A O   
4663 O  O   . HOH N .   ? 0.6234 0.2540 0.4634 0.0690  -0.0377 -0.0537 537 HOH A O   
4664 O  O   . HOH N .   ? 0.2917 0.3826 0.2694 -0.1116 0.0406  -0.0722 538 HOH A O   
4665 O  O   . HOH N .   ? 0.4713 0.7024 0.2028 0.0027  0.0416  0.1370  539 HOH A O   
4666 O  O   . HOH N .   ? 0.2297 0.3630 0.3287 -0.0375 -0.1045 0.0199  540 HOH A O   
4667 O  O   . HOH N .   ? 0.3779 0.2621 0.2035 -0.1097 0.1014  -0.0793 541 HOH A O   
4668 O  O   . HOH N .   ? 0.1313 0.2462 0.3885 -0.0337 -0.0425 0.0562  542 HOH A O   
4669 O  O   . HOH N .   ? 0.1187 0.1608 0.2044 0.0292  -0.0295 0.0146  543 HOH A O   
4670 O  O   . HOH N .   ? 0.1112 0.1309 0.3546 -0.0104 -0.0035 0.0099  544 HOH A O   
4671 O  O   . HOH N .   ? 0.4357 0.2435 0.3772 -0.0239 0.2123  -0.0366 545 HOH A O   
4672 O  O   . HOH N .   ? 0.1462 0.0989 0.2114 0.0355  -0.0065 -0.0003 546 HOH A O   
4673 O  O   . HOH N .   ? 0.2675 0.0982 0.2017 0.0175  -0.0756 -0.0040 547 HOH A O   
4674 O  O   . HOH N .   ? 0.2642 0.5548 0.2980 -0.0104 -0.0432 0.1172  548 HOH A O   
4675 O  O   . HOH N .   ? 0.2200 0.1002 0.2064 -0.0063 -0.0041 0.0199  549 HOH A O   
4676 O  O   . HOH N .   ? 0.3082 0.1492 0.3402 -0.0274 -0.1237 -0.0173 550 HOH A O   
4677 O  O   . HOH N .   ? 0.4253 0.1216 0.2110 0.0161  -0.1509 0.0137  551 HOH A O   
4678 O  O   . HOH N .   ? 0.4876 0.1710 0.2119 0.0384  -0.0073 -0.0041 552 HOH A O   
4679 O  O   . HOH N .   ? 0.1882 0.1013 0.1762 0.0147  -0.0452 0.0032  553 HOH A O   
4680 O  O   . HOH N .   ? 0.1778 0.5357 0.4137 -0.0962 -0.0505 -0.0460 554 HOH A O   
4681 O  O   . HOH N .   ? 0.3923 0.1160 0.2047 -0.0450 -0.0274 -0.0296 555 HOH A O   
4682 O  O   . HOH N .   ? 0.3179 0.1808 0.3598 0.0171  -0.0310 -0.0707 556 HOH A O   
4683 O  O   . HOH N .   ? 0.1893 0.1444 0.1949 0.0071  -0.0731 -0.0015 557 HOH A O   
4684 O  O   . HOH N .   ? 0.2705 0.2405 0.9294 0.0612  0.0491  -0.0161 558 HOH A O   
4685 O  O   . HOH N .   ? 0.1561 0.1474 0.1808 -0.0082 -0.0195 -0.0092 559 HOH A O   
4686 O  O   . HOH N .   ? 0.2567 0.1726 0.1972 0.0285  -0.0186 0.0193  560 HOH A O   
4687 O  O   . HOH N .   ? 0.2640 0.2329 0.1708 0.0005  -0.0300 -0.0331 561 HOH A O   
4688 O  O   . HOH N .   ? 0.4900 0.2820 0.4029 0.0299  -0.0252 0.0405  562 HOH A O   
4689 O  O   . HOH N .   ? 0.1283 0.1534 0.3734 -0.0230 -0.0758 0.0020  563 HOH A O   
4690 O  O   . HOH N .   ? 0.3014 0.2217 0.5278 -0.0032 0.0306  -0.1439 564 HOH A O   
4691 O  O   . HOH N .   ? 0.3230 0.3458 0.4129 -0.0987 0.0120  -0.0644 565 HOH A O   
4692 O  O   . HOH N .   ? 0.0851 0.1890 0.2716 0.0264  0.0179  -0.0441 566 HOH A O   
4693 O  O   . HOH N .   ? 0.3258 0.2469 0.2752 0.0212  0.0952  -0.0222 567 HOH A O   
4694 O  O   . HOH N .   ? 0.2481 0.2216 0.2736 -0.0233 -0.0122 0.0052  568 HOH A O   
4695 O  O   . HOH N .   ? 0.1417 0.1295 0.2256 0.0077  0.0207  -0.0130 569 HOH A O   
4696 O  O   . HOH N .   ? 0.2890 0.1841 0.2509 0.0570  0.0671  0.1142  570 HOH A O   
4697 O  O   . HOH N .   ? 0.2193 0.3055 0.3871 -0.0005 0.0542  -0.0120 571 HOH A O   
4698 O  O   . HOH N .   ? 0.7878 0.2416 0.4251 -0.1124 -0.2436 0.0551  572 HOH A O   
4699 O  O   . HOH N .   ? 0.2752 0.2833 0.5763 -0.1638 -0.0318 0.0381  573 HOH A O   
4700 O  O   . HOH N .   ? 0.1169 0.2955 0.3837 0.0032  -0.0500 0.0861  574 HOH A O   
4701 O  O   . HOH N .   ? 0.3267 0.3862 0.3519 -0.0258 -0.0229 0.0350  575 HOH A O   
4702 O  O   . HOH N .   ? 0.2937 0.2303 0.2730 -0.0384 -0.0680 -0.0175 576 HOH A O   
4703 O  O   . HOH N .   ? 0.2511 0.2002 0.2157 -0.0038 -0.0231 -0.0604 577 HOH A O   
4704 O  O   . HOH N .   ? 0.5655 0.2554 0.2303 0.0350  -0.0017 0.0675  578 HOH A O   
4705 O  O   . HOH N .   ? 0.2199 0.3152 0.2592 -0.0221 -0.0599 -0.0366 579 HOH A O   
4706 O  O   . HOH N .   ? 0.1196 0.2684 0.3285 0.0298  -0.0200 0.0938  580 HOH A O   
4707 O  O   . HOH N .   ? 0.2718 0.1559 0.1972 0.0198  -0.0251 -0.0262 581 HOH A O   
4708 O  O   . HOH N .   ? 0.4465 0.2344 0.4090 0.0144  -0.0762 -0.0474 582 HOH A O   
4709 O  O   . HOH N .   ? 0.3093 0.1277 0.2714 0.0710  -0.0465 -0.0483 583 HOH A O   
4710 O  O   . HOH N .   ? 0.4007 0.3896 0.4426 0.1244  0.1495  0.0151  584 HOH A O   
4711 O  O   . HOH N .   ? 0.1629 0.2098 0.4183 0.0649  0.0631  0.0115  585 HOH A O   
4712 O  O   . HOH N .   ? 0.1683 0.1969 0.2930 0.0000  0.0239  -0.0171 586 HOH A O   
4713 O  O   . HOH N .   ? 0.4126 0.2107 0.4821 0.0854  -0.0724 -0.0857 587 HOH A O   
4714 O  O   . HOH N .   ? 0.2570 0.1460 0.2786 -0.0782 -0.0447 -0.0353 588 HOH A O   
4715 O  O   . HOH N .   ? 0.5300 0.2711 0.6553 -0.0260 -0.1068 -0.2005 589 HOH A O   
4716 O  O   . HOH N .   ? 0.1783 0.1916 0.3813 0.0835  -0.0186 -0.0423 590 HOH A O   
4717 O  O   . HOH N .   ? 0.2425 0.1435 0.2829 0.0071  -0.0575 -0.0205 591 HOH A O   
4718 O  O   . HOH N .   ? 0.4090 0.4629 0.5144 0.0551  0.0092  -0.0057 592 HOH A O   
4719 O  O   . HOH N .   ? 0.4862 0.5751 0.3274 0.1064  -0.1255 0.2358  593 HOH A O   
4720 O  O   . HOH N .   ? 0.6266 0.2040 0.2469 -0.1040 -0.1939 0.0086  594 HOH A O   
4721 O  O   . HOH N .   ? 0.3285 0.3580 0.2442 0.1660  -0.0399 0.0467  595 HOH A O   
4722 O  O   . HOH N .   ? 0.3332 0.2642 0.2700 -0.0019 -0.0627 -0.0467 596 HOH A O   
4723 O  O   . HOH N .   ? 1.8641 0.2630 0.2709 0.0229  -0.1488 -0.2372 597 HOH A O   
4724 O  O   . HOH N .   ? 0.4431 0.1852 0.5073 -0.0742 0.0555  -0.0737 598 HOH A O   
4725 O  O   . HOH N .   ? 0.3319 0.2858 0.4995 -0.0282 0.0098  0.1664  599 HOH A O   
4726 O  O   . HOH N .   ? 0.6980 0.3847 0.4800 -0.2175 -0.2843 0.0469  600 HOH A O   
4727 O  O   . HOH N .   ? 0.4955 0.4926 0.5478 -0.0993 -0.0065 -0.1158 601 HOH A O   
4728 O  O   . HOH N .   ? 0.2339 0.2648 0.3609 0.0557  0.0373  0.0627  602 HOH A O   
4729 O  O   . HOH N .   ? 0.5515 0.1735 0.4562 -0.0588 0.0388  -0.0055 603 HOH A O   
4730 O  O   . HOH N .   ? 0.2761 0.5291 0.7815 0.1525  0.0908  -0.0348 604 HOH A O   
4731 O  O   . HOH N .   ? 0.1137 0.2166 0.1735 0.0132  -0.0476 0.0346  605 HOH A O   
4732 O  O   . HOH N .   ? 0.2217 0.4013 0.4544 0.0373  -0.0771 0.0821  606 HOH A O   
4733 O  O   . HOH N .   ? 0.1611 0.2854 0.4611 0.0037  0.0454  0.0181  607 HOH A O   
4734 O  O   . HOH N .   ? 0.5009 0.5758 0.3867 -0.1099 0.0803  -0.2644 608 HOH A O   
4735 O  O   . HOH N .   ? 0.4336 0.1717 0.3427 0.0962  0.0579  0.1032  609 HOH A O   
4736 O  O   . HOH N .   ? 0.3704 0.4519 0.6786 -0.0142 0.1622  -0.0441 610 HOH A O   
4737 O  O   . HOH N .   ? 0.1193 0.0863 0.1791 0.0083  -0.0263 -0.0125 611 HOH A O   
4738 O  O   . HOH N .   ? 0.2824 0.1907 0.2254 0.0516  -0.0544 0.0344  612 HOH A O   
4739 O  O   . HOH N .   ? 0.3244 1.3255 0.3928 0.0140  -0.0716 0.3095  613 HOH A O   
4740 O  O   . HOH N .   ? 0.3357 0.1814 0.2876 -0.0087 -0.0438 -0.0035 614 HOH A O   
4741 O  O   . HOH N .   ? 0.5115 0.6093 0.2976 0.1502  -0.0209 -0.0041 615 HOH A O   
4742 O  O   . HOH N .   ? 0.3770 0.4226 0.3276 0.1089  0.0449  0.0688  616 HOH A O   
4743 O  O   . HOH N .   ? 0.4894 0.4138 0.1978 -0.0381 0.0187  0.0839  617 HOH A O   
4744 O  O   . HOH N .   ? 0.5357 0.2250 0.5392 -0.0957 -0.0715 -0.0052 618 HOH A O   
4745 O  O   . HOH N .   ? 0.1710 0.0855 0.1956 0.0170  -0.0280 -0.0263 619 HOH A O   
4746 O  O   . HOH N .   ? 0.2772 0.2096 0.4198 0.0584  0.0194  0.0443  620 HOH A O   
4747 O  O   . HOH N .   ? 0.7135 0.4237 0.3621 -0.3118 0.1667  -0.1041 621 HOH A O   
4748 O  O   . HOH N .   ? 0.1784 0.2976 0.3332 0.1023  -0.0975 -0.0716 622 HOH A O   
4749 O  O   . HOH N .   ? 0.5231 0.4088 0.2428 -0.1140 0.0125  0.0439  623 HOH A O   
4750 O  O   . HOH N .   ? 0.3127 0.1715 0.5069 0.0001  0.0782  0.0904  624 HOH A O   
4751 O  O   . HOH N .   ? 0.1128 0.1421 0.3598 -0.0141 -0.0076 -0.0046 625 HOH A O   
4752 O  O   . HOH N .   ? 0.3817 0.3680 0.4494 0.1777  0.1246  0.1233  626 HOH A O   
4753 O  O   . HOH N .   ? 0.3671 0.3968 0.4124 0.0046  -0.0151 -0.0015 627 HOH A O   
4754 O  O   . HOH N .   ? 0.3973 0.3973 0.4907 0.0482  0.0284  0.0300  628 HOH A O   
4755 O  O   . HOH N .   ? 0.2493 0.2006 0.5572 0.0559  0.0954  0.0914  629 HOH A O   
4756 O  O   . HOH N .   ? 0.4248 0.3346 0.2815 0.1465  0.0829  -0.0322 630 HOH A O   
4757 O  O   . HOH N .   ? 0.3855 0.5360 0.3336 -0.1218 0.0267  0.0762  631 HOH A O   
4758 O  O   . HOH N .   ? 0.4257 0.4896 0.4108 -0.0094 0.0741  0.1342  632 HOH A O   
4759 O  O   . HOH N .   ? 2.3029 1.1239 0.4551 0.5769  0.2286  0.3212  633 HOH A O   
4760 O  O   . HOH N .   ? 0.3359 0.3280 1.1963 0.0772  0.0610  0.0957  634 HOH A O   
4761 O  O   . HOH N .   ? 0.2899 0.1735 0.2858 0.0480  0.0359  0.0083  635 HOH A O   
4762 O  O   . HOH N .   ? 0.6028 0.7565 0.4239 0.1881  0.1190  0.0851  636 HOH A O   
4763 O  O   . HOH N .   ? 0.5128 0.2442 0.4844 0.1280  0.0204  0.0803  637 HOH A O   
4764 O  O   . HOH N .   ? 0.2732 0.4016 0.5138 -0.0348 -0.0403 0.0974  638 HOH A O   
4765 O  O   . HOH N .   ? 0.3298 0.9254 0.5605 -0.1460 -0.1448 0.2282  639 HOH A O   
4766 O  O   . HOH N .   ? 0.7060 0.3971 0.7085 -0.1932 -0.0723 -0.0445 640 HOH A O   
4767 O  O   . HOH N .   ? 0.3892 0.3831 0.5472 -0.0593 0.1560  -0.1172 641 HOH A O   
4768 O  O   . HOH N .   ? 0.5059 0.5406 0.3621 -0.1298 -0.1174 -0.0648 642 HOH A O   
4769 O  O   . HOH N .   ? 0.5874 0.4801 2.1624 -0.0196 0.6389  0.2319  643 HOH A O   
4770 O  O   . HOH N .   ? 0.3946 0.4704 0.3643 -0.1048 0.1341  -0.0797 644 HOH A O   
4771 O  O   . HOH N .   ? 1.4290 0.8320 0.1789 -0.2136 0.1536  0.1752  645 HOH A O   
4772 O  O   . HOH N .   ? 0.3411 0.2450 0.4031 0.0395  0.1767  0.0905  646 HOH A O   
4773 O  O   . HOH N .   ? 0.2084 0.3285 0.4462 -0.0298 0.0839  -0.0071 647 HOH A O   
4774 O  O   . HOH N .   ? 0.2213 0.4731 0.2896 0.0824  0.0115  0.0405  648 HOH A O   
4775 O  O   . HOH N .   ? 0.5486 0.6510 0.6412 0.0087  -0.2676 0.2651  649 HOH A O   
4776 O  O   . HOH N .   ? 0.4828 0.2331 0.2148 -0.0399 -0.0518 -0.0093 650 HOH A O   
4777 O  O   . HOH N .   ? 0.1938 0.3122 0.3328 0.0238  0.0252  0.0764  651 HOH A O   
4778 O  O   . HOH N .   ? 0.5181 0.3418 0.5540 -0.0046 0.2992  -0.0826 652 HOH A O   
4779 O  O   . HOH N .   ? 0.4374 0.2815 0.3023 0.0549  -0.0326 -0.0274 653 HOH A O   
4780 O  O   . HOH N .   ? 0.4217 0.5066 0.6209 -0.1042 0.1111  0.0093  654 HOH A O   
4781 O  O   . HOH N .   ? 0.3995 0.2852 0.2944 0.0516  -0.1127 0.0434  655 HOH A O   
4782 O  O   . HOH N .   ? 0.1421 0.0930 0.1730 -0.0038 -0.0274 -0.0163 656 HOH A O   
4783 O  O   . HOH N .   ? 0.4377 0.7975 0.3555 -0.3066 0.0764  -0.1868 657 HOH A O   
4784 O  O   . HOH N .   ? 0.5289 0.2809 0.4314 0.1613  0.2226  0.1006  658 HOH A O   
4785 O  O   . HOH N .   ? 0.5289 0.2869 0.3598 -0.1118 0.0631  0.1261  659 HOH A O   
4786 O  O   . HOH N .   ? 0.4235 0.3995 0.4120 0.0176  0.0140  -0.0115 660 HOH A O   
4787 O  O   . HOH N .   ? 0.4940 0.2247 0.5331 -0.0597 0.1448  0.0842  661 HOH A O   
4788 O  O   . HOH N .   ? 0.3616 0.2684 0.4314 0.0098  -0.0392 0.0199  662 HOH A O   
4789 O  O   . HOH N .   ? 0.1394 2.0971 0.7038 0.2412  -0.0124 -0.4025 663 HOH A O   
4790 O  O   . HOH N .   ? 0.4377 0.4670 0.3894 0.0428  -0.0518 -0.0825 664 HOH A O   
4791 O  O   . HOH N .   ? 0.3030 0.3535 0.3689 0.0930  -0.0913 -0.0854 665 HOH A O   
4792 O  O   . HOH N .   ? 0.4334 0.4589 0.8478 0.2745  -0.2466 -0.2576 666 HOH A O   
4793 O  O   . HOH N .   ? 0.4785 0.4481 1.2173 0.0024  0.3244  -0.2721 667 HOH A O   
4794 O  O   . HOH N .   ? 0.4607 0.5339 0.4095 0.0996  -0.0249 0.0749  668 HOH A O   
4795 O  O   . HOH N .   ? 0.4501 0.3783 0.4332 -0.0430 -0.0982 -0.0776 669 HOH A O   
4796 O  O   . HOH N .   ? 0.3743 0.4471 0.6078 0.2230  -0.1729 -0.2229 670 HOH A O   
4797 O  O   . HOH N .   ? 0.4659 0.4183 0.5011 0.0520  0.1380  0.2034  671 HOH A O   
4798 O  O   . HOH N .   ? 0.3504 0.2809 0.4347 -0.0469 0.1138  0.0063  672 HOH A O   
4799 O  O   . HOH N .   ? 0.6269 0.3355 0.5842 0.1172  -0.2035 -0.1101 673 HOH A O   
4800 O  O   . HOH N .   ? 0.3289 0.2163 0.6632 0.0361  -0.1485 -0.0944 674 HOH A O   
4801 O  O   . HOH N .   ? 0.4189 0.6201 0.3296 -0.0661 0.0668  0.2406  675 HOH A O   
4802 O  O   . HOH N .   ? 0.5336 0.4201 0.6729 0.0760  0.0430  0.0819  676 HOH A O   
4803 O  O   . HOH N .   ? 0.6276 0.4009 0.5626 0.0324  0.0131  -0.0315 677 HOH A O   
4804 O  O   . HOH N .   ? 0.6534 0.5307 0.3734 0.0724  0.1083  0.0452  678 HOH A O   
4805 O  O   . HOH N .   ? 0.3747 0.3623 0.3646 -0.1059 -0.0208 0.0855  679 HOH A O   
4806 O  O   . HOH N .   ? 0.4336 0.4169 0.4291 0.0006  -0.0023 0.0142  680 HOH A O   
4807 O  O   . HOH N .   ? 0.2596 0.2549 0.3005 0.0113  -0.0337 -0.0028 681 HOH A O   
4808 O  O   . HOH N .   ? 0.4207 0.3233 0.4512 0.0205  0.1666  -0.0886 682 HOH A O   
4809 O  O   . HOH N .   ? 0.5673 0.3788 0.3436 0.2048  -0.0439 -0.0859 683 HOH A O   
4810 O  O   . HOH N .   ? 0.3251 0.1941 0.4104 0.0895  -0.2400 -0.0640 684 HOH A O   
4811 O  O   . HOH N .   ? 0.4210 0.4000 0.4794 0.0217  -0.0200 0.0866  685 HOH A O   
4812 O  O   . HOH N .   ? 0.3641 0.7336 0.3770 0.2337  -0.0394 0.0948  686 HOH A O   
4813 O  O   . HOH N .   ? 0.3736 0.2145 0.7531 -0.0529 0.0175  0.0860  687 HOH A O   
4814 O  O   . HOH N .   ? 0.3271 0.7824 0.3887 -0.2134 -0.0643 0.1221  688 HOH A O   
4815 O  O   . HOH N .   ? 0.2349 0.2649 0.2730 -0.0241 0.0456  -0.0350 689 HOH A O   
4816 O  O   . HOH N .   ? 0.1943 0.1728 0.2804 0.0383  -0.0615 -0.0288 690 HOH A O   
4817 O  O   . HOH N .   ? 0.2556 0.2885 0.3831 0.0138  -0.0725 0.0524  691 HOH A O   
4818 O  O   . HOH N .   ? 0.2799 0.3169 0.3655 0.1403  -0.1278 -0.1005 692 HOH A O   
4819 O  O   . HOH N .   ? 0.4140 0.2915 0.2709 0.0957  -0.0013 -0.0813 693 HOH A O   
4820 O  O   . HOH N .   ? 0.9032 0.2150 0.4632 0.0856  -0.1972 -0.0869 694 HOH A O   
4821 O  O   . HOH N .   ? 0.3671 0.3508 0.2657 0.0515  0.0362  -0.0756 695 HOH A O   
4822 O  O   . HOH N .   ? 0.6050 0.3810 0.3551 -0.1181 0.0860  -0.1187 696 HOH A O   
4823 O  O   . HOH N .   ? 0.2216 0.2942 0.4879 -0.0688 0.0307  -0.0549 697 HOH A O   
4824 O  O   . HOH N .   ? 0.3853 0.3149 0.5060 -0.0412 0.0063  0.1393  698 HOH A O   
4825 O  O   . HOH N .   ? 0.5191 0.4059 0.5146 0.0055  -0.0746 0.0107  699 HOH A O   
4826 O  O   . HOH N .   ? 0.5238 0.3628 0.5205 0.1002  0.0560  -0.0007 700 HOH A O   
4827 O  O   . HOH N .   ? 0.6042 0.7419 0.3693 0.0223  0.1377  -0.1413 701 HOH A O   
4828 O  O   . HOH N .   ? 0.1958 0.2635 0.3571 0.0405  0.0013  -0.0136 702 HOH A O   
4829 O  O   . HOH N .   ? 0.7204 0.3332 0.3592 -0.0781 -0.0773 0.0322  703 HOH A O   
4830 O  O   . HOH N .   ? 0.3463 0.5149 0.2632 0.0522  -0.0511 0.0414  704 HOH A O   
4831 O  O   . HOH N .   ? 0.5360 0.6751 0.3470 -0.2251 -0.2159 0.1959  705 HOH A O   
4832 O  O   . HOH N .   ? 0.1444 0.3574 0.4785 0.0164  -0.0419 0.0230  706 HOH A O   
4833 O  O   . HOH N .   ? 0.4016 0.3269 0.2080 -0.0952 -0.0192 -0.0041 707 HOH A O   
4834 O  O   . HOH N .   ? 0.4914 0.1776 0.3273 0.0281  -0.0794 0.0173  708 HOH A O   
4835 O  O   . HOH N .   ? 0.8192 0.3648 0.4390 0.0264  0.2372  0.0710  709 HOH A O   
4836 O  O   . HOH N .   ? 0.5680 0.4311 0.3371 0.0342  -0.1238 0.1080  710 HOH A O   
4837 O  O   . HOH N .   ? 0.4629 0.3844 0.3427 -0.0873 -0.1204 -0.1052 711 HOH A O   
4838 O  O   . HOH N .   ? 0.5569 0.4618 0.4241 -0.0244 0.0300  -0.1222 712 HOH A O   
4839 O  O   . HOH N .   ? 0.7574 0.4183 0.6621 0.2746  -0.3510 -0.2204 713 HOH A O   
4840 O  O   . HOH N .   ? 0.4149 0.3810 0.3616 0.0252  0.0273  0.0274  714 HOH A O   
4841 O  O   . HOH N .   ? 0.4442 0.2662 0.8568 -0.0925 -0.3215 0.1767  715 HOH A O   
4842 O  O   . HOH N .   ? 0.5979 0.2506 0.4350 -0.0863 0.0641  -0.0886 716 HOH A O   
4843 O  O   . HOH N .   ? 0.6611 0.2982 0.7271 -0.1933 0.1018  -0.0035 717 HOH A O   
4844 O  O   . HOH N .   ? 0.5127 0.4241 0.4546 0.0233  0.0167  -0.0080 718 HOH A O   
4845 O  O   . HOH N .   ? 0.2813 0.1765 0.4264 -0.0120 0.0015  0.0447  719 HOH A O   
4846 O  O   . HOH N .   ? 0.5910 0.3100 0.4219 -0.1203 0.0362  -0.0837 720 HOH A O   
4847 O  O   . HOH N .   ? 0.6470 0.6366 0.3409 -0.1564 0.0253  -0.1086 721 HOH A O   
4848 O  O   . HOH N .   ? 0.2155 0.1953 0.2389 0.0476  -0.0505 0.0211  722 HOH A O   
4849 O  O   . HOH N .   ? 0.2712 0.1310 0.3824 -0.0055 0.1260  -0.0231 723 HOH A O   
4850 O  O   . HOH N .   ? 0.4875 0.3465 0.3213 0.0697  -0.0498 0.0116  724 HOH A O   
4851 O  O   . HOH N .   ? 0.5550 0.3522 0.3391 0.0119  0.0313  0.1090  725 HOH A O   
4852 O  O   . HOH N .   ? 0.6342 0.4183 0.5764 0.1520  -0.1641 -0.3485 726 HOH A O   
4853 O  O   . HOH N .   ? 0.2509 0.5587 0.5260 -0.0909 0.0414  0.0813  727 HOH A O   
4854 O  O   . HOH N .   ? 0.1315 0.3916 0.5257 -0.0236 0.0088  0.0315  728 HOH A O   
4855 O  O   . HOH N .   ? 0.5763 0.3673 0.4318 0.0795  0.1966  0.0285  729 HOH A O   
4856 O  O   . HOH N .   ? 0.9304 0.2759 0.3257 0.0659  -0.0930 0.0035  730 HOH A O   
4857 O  O   . HOH N .   ? 0.4273 0.3109 0.5450 -0.1827 -0.0259 0.1061  731 HOH A O   
4858 O  O   . HOH N .   ? 0.5414 0.5145 0.3930 0.0452  0.0940  -0.0657 732 HOH A O   
4859 O  O   . HOH N .   ? 0.4537 0.4059 0.6807 -0.0046 -0.1849 -0.0894 733 HOH A O   
4860 O  O   . HOH N .   ? 0.5302 0.3998 0.4422 0.0094  -0.0258 0.0308  734 HOH A O   
4861 O  O   . HOH N .   ? 0.3255 0.3477 0.4180 0.1280  0.0573  0.1172  735 HOH A O   
4862 O  O   . HOH N .   ? 0.4805 0.4153 0.4566 0.1222  -0.0408 -0.0116 736 HOH A O   
4863 O  O   . HOH N .   ? 0.3091 0.4562 0.5116 0.1401  -0.0263 0.1103  737 HOH A O   
4864 O  O   . HOH N .   ? 0.3614 0.4275 0.6047 0.1553  -0.1770 -0.1218 738 HOH A O   
4865 O  O   . HOH N .   ? 0.3115 0.5691 0.5573 0.0015  -0.1817 -0.0498 739 HOH A O   
4866 O  O   . HOH N .   ? 0.2732 0.3549 0.5521 -0.1136 -0.0340 -0.2111 740 HOH A O   
4867 O  O   . HOH N .   ? 0.2317 0.4117 0.4839 -0.0423 0.0904  -0.0300 741 HOH A O   
4868 O  O   . HOH N .   ? 0.5595 0.5631 0.4275 0.2547  -0.1305 -0.0599 742 HOH A O   
4869 O  O   . HOH N .   ? 0.2257 0.3695 0.6514 -0.1468 -0.0908 -0.1684 743 HOH A O   
4870 O  O   . HOH N .   ? 0.3416 0.4714 0.5909 -0.0749 0.0355  0.0124  744 HOH A O   
4871 O  O   . HOH N .   ? 0.0834 0.3761 0.7706 -0.0905 -0.1534 0.1515  745 HOH A O   
4872 O  O   . HOH O .   ? 0.2921 0.4334 0.3903 0.0206  -0.1080 0.0125  601 HOH B O   
4873 O  O   . HOH O .   ? 0.2955 0.2071 0.3303 0.0408  -0.0571 -0.0043 602 HOH B O   
4874 O  O   . HOH O .   ? 0.3287 0.4219 0.2480 -0.0824 -0.0751 -0.0485 603 HOH B O   
4875 O  O   . HOH O .   ? 0.4174 0.3224 0.3084 -0.0649 -0.0684 -0.0798 604 HOH B O   
4876 O  O   . HOH O .   ? 0.1647 0.5428 0.5580 0.0370  -0.0573 -0.1172 605 HOH B O   
4877 O  O   . HOH O .   ? 0.3233 0.1230 0.2624 0.0500  0.0041  0.0060  606 HOH B O   
4878 O  O   . HOH O .   ? 0.5065 0.3434 0.3919 0.0020  -0.0364 0.0436  607 HOH B O   
4879 O  O   . HOH O .   ? 0.4088 0.2269 0.4192 -0.0092 0.0737  -0.1015 608 HOH B O   
4880 O  O   . HOH O .   ? 0.4088 0.4854 1.0714 -0.1858 -0.1580 0.1846  609 HOH B O   
4881 O  O   . HOH O .   ? 0.3179 0.2854 0.6844 -0.0212 0.1973  -0.2576 610 HOH B O   
4882 O  O   . HOH O .   ? 0.5202 0.4503 0.6029 0.0599  0.1427  0.0366  611 HOH B O   
4883 O  O   . HOH O .   ? 0.2403 0.4492 0.3549 -0.0131 -0.0419 -0.0458 612 HOH B O   
4884 O  O   . HOH O .   ? 0.2804 0.5253 0.4814 -0.0441 -0.1143 -0.0643 613 HOH B O   
4885 O  O   . HOH O .   ? 0.5655 0.2630 0.2038 0.0793  -0.0412 0.0403  614 HOH B O   
4886 O  O   . HOH O .   ? 0.3271 0.2490 0.6263 0.0474  0.0768  -0.0098 615 HOH B O   
4887 O  O   . HOH O .   ? 0.2531 0.2152 0.4969 0.0331  -0.1460 -0.0103 616 HOH B O   
4888 O  O   . HOH O .   ? 0.4749 0.3885 0.4216 -0.0851 -0.1515 -0.0296 617 HOH B O   
4889 O  O   . HOH O .   ? 0.6086 0.7268 0.4774 0.0944  -0.2788 -0.0196 618 HOH B O   
4890 O  O   . HOH O .   ? 1.3844 0.5162 0.9319 -0.2298 -0.4395 -0.0397 619 HOH B O   
4891 O  O   . HOH O .   ? 0.1172 0.1211 0.1401 0.0149  0.0063  0.0186  620 HOH B O   
4892 O  O   . HOH O .   ? 0.3433 0.3276 0.2815 0.0697  0.0711  0.1076  621 HOH B O   
4893 O  O   . HOH O .   ? 0.5540 0.3215 0.6053 -0.0221 0.1846  -0.1761 622 HOH B O   
4894 O  O   . HOH O .   ? 0.4140 0.3944 0.2779 -0.0207 0.0153  0.0252  623 HOH B O   
4895 O  O   . HOH O .   ? 0.4519 0.3000 0.7911 -0.1814 -0.3758 0.1933  624 HOH B O   
4896 O  O   . HOH O .   ? 0.5695 0.1158 0.2114 -0.0436 -0.1985 -0.0038 625 HOH B O   
4897 O  O   . HOH O .   ? 0.7605 0.2457 0.1652 0.0421  -0.0055 -0.0124 626 HOH B O   
4898 O  O   . HOH O .   ? 0.4526 0.3908 0.4415 -0.0013 -0.0864 0.1617  627 HOH B O   
4899 O  O   . HOH O .   ? 1.0605 0.3844 0.4350 0.2777  0.2567  0.1268  628 HOH B O   
4900 O  O   . HOH O .   ? 0.1931 0.5562 0.1830 0.0450  -0.0031 0.0076  629 HOH B O   
4901 O  O   . HOH O .   ? 0.1022 1.1376 0.6057 -0.2922 -0.0026 0.0296  630 HOH B O   
4902 O  O   . HOH O .   ? 0.7105 0.6974 0.2578 0.1837  0.1261  0.0593  631 HOH B O   
4903 O  O   . HOH O .   ? 0.3406 0.2432 0.3170 0.0283  0.0723  0.0706  632 HOH B O   
4904 O  O   . HOH O .   ? 0.3709 0.5813 0.2669 -0.0763 -0.0227 0.1446  633 HOH B O   
4905 O  O   . HOH O .   ? 0.4485 0.3880 0.3531 0.1983  0.1466  0.1741  634 HOH B O   
4906 O  O   . HOH O .   ? 0.5422 0.4603 0.3785 0.0322  0.0643  -0.1483 635 HOH B O   
4907 O  O   . HOH O .   ? 0.1935 0.1011 0.0920 0.0265  -0.0098 -0.0031 636 HOH B O   
4908 O  O   . HOH O .   ? 0.3172 0.2178 0.3134 0.0329  0.0491  0.0230  637 HOH B O   
4909 O  O   . HOH O .   ? 1.4449 0.9553 0.5881 -0.4462 0.0377  -0.1292 638 HOH B O   
4910 O  O   . HOH O .   ? 0.3318 0.4474 0.3655 -0.0802 0.1209  0.0166  639 HOH B O   
4911 O  O   . HOH O .   ? 0.5022 0.6312 0.6714 0.3226  0.0878  -0.0793 640 HOH B O   
4912 O  O   . HOH O .   ? 0.3876 0.1902 0.4535 0.0220  0.0727  0.0509  641 HOH B O   
4913 O  O   . HOH O .   ? 0.4575 0.3752 0.3851 0.0215  0.0216  -0.0546 642 HOH B O   
4914 O  O   . HOH O .   ? 0.1787 0.2085 0.2565 -0.0041 0.0138  0.0127  643 HOH B O   
4915 O  O   . HOH O .   ? 0.4503 0.2033 0.3698 0.0087  -0.0876 -0.0054 644 HOH B O   
4916 O  O   . HOH O .   ? 0.4268 0.6431 0.3743 -0.1673 -0.0408 -0.2073 645 HOH B O   
4917 O  O   . HOH O .   ? 0.1386 0.1132 0.1272 0.0163  0.0055  0.0038  646 HOH B O   
4918 O  O   . HOH O .   ? 0.3585 0.3400 0.8668 -0.0070 -0.2129 0.0350  647 HOH B O   
4919 O  O   . HOH O .   ? 0.6603 0.3003 0.1834 0.0662  -0.0395 0.0335  648 HOH B O   
4920 O  O   . HOH O .   ? 0.5691 0.2930 0.2815 0.0926  0.0684  0.1053  649 HOH B O   
4921 O  O   . HOH O .   ? 0.2874 0.1986 0.2457 0.0755  -0.0538 0.0100  650 HOH B O   
4922 O  O   . HOH O .   ? 0.7337 0.4278 0.3996 0.1569  0.1419  0.0952  651 HOH B O   
4923 O  O   . HOH O .   ? 0.2001 0.2283 0.2225 -0.0141 -0.0198 -0.0195 652 HOH B O   
4924 O  O   . HOH O .   ? 0.4165 0.1891 0.2078 0.0916  0.1062  -0.0046 653 HOH B O   
4925 O  O   . HOH O .   ? 0.2087 0.2319 0.2739 -0.0179 0.0097  -0.0007 654 HOH B O   
4926 O  O   . HOH O .   ? 0.3300 0.1859 0.2727 -0.0249 0.0071  -0.0516 655 HOH B O   
4927 O  O   . HOH O .   ? 0.3612 0.3549 0.2265 0.1275  0.1207  0.0408  656 HOH B O   
4928 O  O   . HOH O .   ? 0.2418 0.1861 0.3377 -0.0308 -0.1727 0.0412  657 HOH B O   
4929 O  O   . HOH O .   ? 0.1884 0.3097 0.4309 -0.0586 -0.0379 0.0032  658 HOH B O   
4930 O  O   . HOH O .   ? 0.3470 0.2410 0.1791 0.0088  -0.0701 -0.0221 659 HOH B O   
4931 O  O   . HOH O .   ? 0.4246 0.3711 0.2942 0.1386  0.0494  0.0289  660 HOH B O   
4932 O  O   . HOH O .   ? 0.2910 0.3510 0.4054 -0.0308 -0.1362 0.2029  661 HOH B O   
4933 O  O   . HOH O .   ? 0.3542 0.3404 0.4582 0.1432  -0.1090 -0.0225 662 HOH B O   
4934 O  O   . HOH O .   ? 0.4772 0.3138 0.5347 -0.1076 0.0280  0.1002  663 HOH B O   
4935 O  O   . HOH O .   ? 0.3151 0.2504 0.2980 0.0961  -0.0222 -0.0666 664 HOH B O   
4936 O  O   . HOH O .   ? 0.1931 0.2259 0.3079 -0.0103 0.0414  -0.0710 665 HOH B O   
4937 O  O   . HOH O .   ? 0.7117 0.2462 0.1985 0.1451  -0.0656 -0.0913 666 HOH B O   
4938 O  O   . HOH O .   ? 0.2083 0.2930 0.4828 -0.0834 0.0416  -0.0782 667 HOH B O   
4939 O  O   . HOH O .   ? 0.2315 0.5018 0.4140 0.0839  -0.0861 0.0439  668 HOH B O   
4940 O  O   . HOH O .   ? 0.2171 0.2085 0.2790 -0.0329 0.0166  -0.0693 669 HOH B O   
4941 O  O   . HOH O .   ? 0.5899 0.4332 0.3127 -0.0714 -0.0051 -0.0103 670 HOH B O   
4942 O  O   . HOH O .   ? 0.3576 0.3039 0.2197 -0.0922 0.0065  0.0020  671 HOH B O   
4943 O  O   . HOH O .   ? 0.5228 0.2247 0.2565 0.0612  -0.1041 -0.1255 672 HOH B O   
4944 O  O   . HOH O .   ? 0.1404 0.1119 0.1432 0.0088  0.0147  0.0143  673 HOH B O   
4945 O  O   . HOH O .   ? 0.2337 0.4120 0.5568 -0.1626 0.0289  -0.1666 674 HOH B O   
4946 O  O   . HOH O .   ? 0.3621 0.3853 0.5109 -0.1793 0.0412  -0.0399 675 HOH B O   
4947 O  O   . HOH O .   ? 0.2639 0.2750 0.2028 0.0189  -0.0366 0.0825  676 HOH B O   
4948 O  O   . HOH O .   ? 0.9785 1.7745 0.2480 -0.5396 0.1557  -0.2712 677 HOH B O   
4949 O  O   . HOH O .   ? 0.1798 0.0866 0.1728 0.0146  -0.0105 -0.0028 678 HOH B O   
4950 O  O   . HOH O .   ? 0.2353 0.2484 0.3300 0.0080  0.0065  0.0698  679 HOH B O   
4951 O  O   . HOH O .   ? 0.2234 0.4237 0.2874 -0.0164 0.0935  -0.0038 680 HOH B O   
4952 O  O   . HOH O .   ? 0.2655 0.4911 0.3635 -0.0324 0.0898  -0.0006 681 HOH B O   
4953 O  O   . HOH O .   ? 0.6130 0.5737 2.2109 -0.0608 0.3558  -0.7885 682 HOH B O   
4954 O  O   . HOH O .   ? 0.2948 0.2673 0.3327 0.0377  0.0043  -0.0465 683 HOH B O   
4955 O  O   . HOH O .   ? 0.3885 0.5347 0.2463 0.0231  0.0621  0.0586  684 HOH B O   
4956 O  O   . HOH O .   ? 0.1071 0.1110 0.1338 0.0126  0.0120  0.0007  685 HOH B O   
4957 O  O   . HOH O .   ? 0.3016 0.1099 0.2058 -0.0003 -0.0866 0.0005  686 HOH B O   
4958 O  O   . HOH O .   ? 0.1315 0.1604 0.1516 -0.0196 -0.0395 -0.0254 687 HOH B O   
4959 O  O   . HOH O .   ? 0.3971 0.4176 0.4476 0.0017  0.0242  -0.0092 688 HOH B O   
4960 O  O   . HOH O .   ? 0.1902 0.2333 0.1817 0.0077  -0.0491 -0.0281 689 HOH B O   
4961 O  O   . HOH O .   ? 0.1958 0.1302 0.2030 0.0300  -0.0120 0.0057  690 HOH B O   
4962 O  O   . HOH O .   ? 0.2619 0.1643 0.2005 -0.0028 -0.0646 0.0130  691 HOH B O   
4963 O  O   . HOH O .   ? 0.2416 0.2109 0.2114 -0.0153 0.0648  0.0250  692 HOH B O   
4964 O  O   . HOH O .   ? 0.1696 0.4939 0.4289 -0.0052 -0.0049 0.0172  693 HOH B O   
4965 O  O   . HOH O .   ? 0.4702 0.3912 0.5056 -0.0289 -0.1423 -0.1086 694 HOH B O   
4966 O  O   . HOH O .   ? 0.0988 0.1363 0.1439 -0.0161 -0.0172 0.0104  695 HOH B O   
4967 O  O   . HOH O .   ? 0.8519 0.3452 0.4743 0.2861  -0.0216 -0.0245 696 HOH B O   
4968 O  O   . HOH O .   ? 0.1144 0.1086 0.1371 -0.0055 -0.0146 0.0063  697 HOH B O   
4969 O  O   . HOH O .   ? 0.4232 0.5993 0.6826 -0.1639 0.2689  -0.0344 698 HOH B O   
4970 O  O   . HOH O .   ? 0.3910 0.1556 0.3404 -0.1088 -0.0688 0.0060  699 HOH B O   
4971 O  O   . HOH O .   ? 0.2806 0.4388 0.2619 0.0568  0.0137  0.0071  700 HOH B O   
4972 O  O   . HOH O .   ? 0.0922 0.1523 0.2243 0.0121  -0.0041 0.0299  701 HOH B O   
4973 O  O   . HOH O .   ? 0.3371 0.5282 0.2109 0.1052  -0.1416 -0.1301 702 HOH B O   
4974 O  O   . HOH O .   ? 0.1809 0.1288 0.1577 0.0000  0.0020  -0.0183 703 HOH B O   
4975 O  O   . HOH O .   ? 0.3528 0.2030 0.3070 -0.0232 -0.0957 -0.0725 704 HOH B O   
4976 O  O   . HOH O .   ? 0.5687 0.3115 0.3901 -0.0775 0.0132  0.0311  705 HOH B O   
4977 O  O   . HOH O .   ? 0.2188 0.1502 0.2940 -0.0175 0.0142  0.0277  706 HOH B O   
4978 O  O   . HOH O .   ? 0.2946 0.4462 0.3111 0.0171  -0.0680 -0.1453 707 HOH B O   
4979 O  O   . HOH O .   ? 0.4185 0.3034 0.2545 0.0945  0.0777  0.1333  708 HOH B O   
4980 O  O   . HOH O .   ? 0.2980 0.2574 0.4653 -0.0157 0.1739  -0.1055 709 HOH B O   
4981 O  O   . HOH O .   ? 0.2709 0.4704 0.6686 -0.0010 0.0362  0.0560  710 HOH B O   
4982 O  O   . HOH O .   ? 0.3720 0.2551 0.4636 -0.0068 -0.0216 0.0274  711 HOH B O   
4983 O  O   . HOH O .   ? 0.2818 0.2293 0.1953 -0.0126 0.0026  -0.0329 712 HOH B O   
4984 O  O   . HOH O .   ? 0.1942 0.2078 0.2421 0.0133  0.0041  0.0401  713 HOH B O   
4985 O  O   . HOH O .   ? 0.3246 0.2017 0.2678 -0.0274 -0.1136 0.0318  714 HOH B O   
4986 O  O   . HOH O .   ? 0.0934 0.3598 0.4214 0.0427  -0.0296 -0.0243 715 HOH B O   
4987 O  O   . HOH O .   ? 0.6276 0.2723 0.5497 -0.0113 -0.0917 0.1089  716 HOH B O   
4988 O  O   . HOH O .   ? 0.2628 0.2223 0.3445 0.0013  -0.0405 0.0767  717 HOH B O   
4989 O  O   . HOH O .   ? 0.3912 0.2619 0.2260 0.1093  0.1011  0.0719  718 HOH B O   
4990 O  O   . HOH O .   ? 0.1194 0.1302 0.1789 -0.0226 -0.0296 -0.0256 719 HOH B O   
4991 O  O   . HOH O .   ? 0.2071 0.2711 0.6029 0.0381  0.0340  0.1652  720 HOH B O   
4992 O  O   . HOH O .   ? 0.7900 0.1988 0.2177 -0.0164 0.0427  -0.0443 721 HOH B O   
4993 O  O   . HOH O .   ? 0.2408 0.1279 0.2026 0.0264  0.0092  -0.0331 722 HOH B O   
4994 O  O   . HOH O .   ? 0.1212 0.1816 0.3524 0.0161  -0.0094 -0.0068 723 HOH B O   
4995 O  O   . HOH O .   ? 0.4196 0.2928 0.4975 0.1851  -0.0038 -0.0344 724 HOH B O   
4996 O  O   . HOH O .   ? 0.1466 0.1929 0.1773 -0.0153 -0.0189 -0.0066 725 HOH B O   
4997 O  O   . HOH O .   ? 0.4494 0.2513 0.3280 -0.0763 -0.0584 -0.0964 726 HOH B O   
4998 O  O   . HOH O .   ? 0.1789 0.5123 0.4330 0.1010  -0.0777 0.0712  727 HOH B O   
4999 O  O   . HOH O .   ? 0.2220 0.1530 0.2073 0.0217  -0.0474 -0.0240 728 HOH B O   
5000 O  O   . HOH O .   ? 0.2637 0.2700 0.3928 0.0313  0.0759  -0.0140 729 HOH B O   
5001 O  O   . HOH O .   ? 0.1757 0.1577 0.1823 0.0071  -0.0046 -0.0057 730 HOH B O   
5002 O  O   . HOH O .   ? 0.3000 0.4286 0.3177 0.0449  -0.1005 -0.0103 731 HOH B O   
5003 O  O   . HOH O .   ? 0.3752 0.1554 0.3889 -0.0254 -0.1125 0.0425  732 HOH B O   
5004 O  O   . HOH O .   ? 0.4885 0.4760 0.3691 -0.0838 -0.0930 -0.0111 733 HOH B O   
5005 O  O   . HOH O .   ? 0.3838 0.1306 0.2058 -0.0096 -0.1211 -0.0131 734 HOH B O   
5006 O  O   . HOH O .   ? 0.1467 0.1599 0.4666 0.0419  -0.0890 -0.0115 735 HOH B O   
5007 O  O   . HOH O .   ? 0.1500 0.1270 0.2168 -0.0304 0.0003  -0.0015 736 HOH B O   
5008 O  O   . HOH O .   ? 0.5407 0.4875 0.3973 0.2493  0.0688  0.1542  737 HOH B O   
5009 O  O   . HOH O .   ? 0.2101 0.1440 0.1654 -0.0206 -0.0174 -0.0054 738 HOH B O   
5010 O  O   . HOH O .   ? 0.2777 0.1923 0.1798 -0.0151 -0.0296 0.0089  739 HOH B O   
5011 O  O   . HOH O .   ? 0.3373 0.2754 0.2450 -0.0562 0.0615  0.0041  740 HOH B O   
5012 O  O   . HOH O .   ? 0.2869 0.1988 0.2202 -0.0242 0.0467  -0.1033 741 HOH B O   
5013 O  O   . HOH O .   ? 0.1756 0.3393 0.2518 0.0269  -0.0603 0.0076  742 HOH B O   
5014 O  O   . HOH O .   ? 0.5329 0.3781 0.3537 0.0024  -0.0935 -0.0989 743 HOH B O   
5015 O  O   . HOH O .   ? 0.6825 0.2075 0.4286 -0.0832 0.0700  0.0368  744 HOH B O   
5016 O  O   . HOH O .   ? 0.2691 0.2782 0.2831 0.0304  -0.0132 0.0167  745 HOH B O   
5017 O  O   . HOH O .   ? 0.4478 0.1977 0.2362 -0.0619 0.0122  -0.0361 746 HOH B O   
5018 O  O   . HOH O .   ? 0.1509 0.2547 0.4104 -0.0368 0.0759  -0.0038 747 HOH B O   
5019 O  O   . HOH O .   ? 0.2250 0.1613 0.1879 -0.0062 -0.0706 0.0038  748 HOH B O   
5020 O  O   . HOH O .   ? 0.2858 0.4726 0.3941 -0.2029 0.0540  -0.1303 749 HOH B O   
5021 O  O   . HOH O .   ? 0.2517 0.2166 0.2128 0.0458  -0.0351 0.0619  750 HOH B O   
5022 O  O   . HOH O .   ? 0.1604 0.3388 0.3274 -0.0353 -0.0020 -0.1324 751 HOH B O   
5023 O  O   . HOH O .   ? 0.3348 0.2727 0.2504 0.0850  -0.0280 0.0068  752 HOH B O   
5024 O  O   . HOH O .   ? 0.0876 0.2161 0.2612 -0.0200 0.0118  0.0417  753 HOH B O   
5025 O  O   . HOH O .   ? 0.3957 0.2711 0.4869 0.0121  -0.0992 -0.2181 754 HOH B O   
5026 O  O   . HOH O .   ? 0.2867 0.2628 0.3165 -0.0588 0.0905  0.0023  755 HOH B O   
5027 O  O   . HOH O .   ? 0.3240 0.1570 0.2743 -0.0608 -0.0731 0.0414  756 HOH B O   
5028 O  O   . HOH O .   ? 0.4185 0.3822 0.4805 0.0155  0.0979  0.0219  757 HOH B O   
5029 O  O   . HOH O .   ? 0.3323 0.5278 0.3540 -0.0157 -0.0634 0.1476  758 HOH B O   
5030 O  O   . HOH O .   ? 0.2831 0.2002 0.1726 0.0006  -0.0076 -0.0131 759 HOH B O   
5031 O  O   . HOH O .   ? 0.2890 1.4644 0.3874 -0.1516 -0.0505 0.2536  760 HOH B O   
5032 O  O   . HOH O .   ? 0.1342 0.3944 0.3961 -0.0144 -0.0348 -0.0794 761 HOH B O   
5033 O  O   . HOH O .   ? 0.1733 0.7171 0.5006 0.0847  -0.0006 0.1173  762 HOH B O   
5034 O  O   . HOH O .   ? 0.5727 0.2475 0.6942 0.1180  0.2838  -0.0255 763 HOH B O   
5035 O  O   . HOH O .   ? 0.3337 0.3795 0.2732 0.1220  -0.0031 0.0706  764 HOH B O   
5036 O  O   . HOH O .   ? 0.2254 0.2831 0.5200 -0.0152 0.0996  -0.0811 765 HOH B O   
5037 O  O   . HOH O .   ? 0.5611 0.5569 0.3522 0.0456  0.0461  0.1633  766 HOH B O   
5038 O  O   . HOH O .   ? 1.7344 0.3698 1.1052 -0.1146 -0.3443 0.2815  767 HOH B O   
5039 O  O   . HOH O .   ? 0.3298 0.3549 0.2535 -0.1746 -0.0306 -0.0480 768 HOH B O   
5040 O  O   . HOH O .   ? 0.1541 0.1449 0.2222 0.0015  0.0285  -0.0103 769 HOH B O   
5041 O  O   . HOH O .   ? 0.5907 0.3878 0.2743 0.0706  -0.0015 0.1450  770 HOH B O   
5042 O  O   . HOH O .   ? 0.4467 0.2468 0.3562 0.0062  0.1872  0.0535  771 HOH B O   
5043 O  O   . HOH O .   ? 0.5188 0.2148 0.2187 0.1130  -0.1648 -0.0174 772 HOH B O   
5044 O  O   . HOH O .   ? 0.5846 0.2694 0.4264 0.0461  -0.0267 -0.0952 773 HOH B O   
5045 O  O   . HOH O .   ? 0.3109 0.1929 0.2162 -0.0379 -0.0595 0.0286  774 HOH B O   
5046 O  O   . HOH O .   ? 0.3682 0.4707 0.4110 0.1031  0.0284  0.0119  775 HOH B O   
5047 O  O   . HOH O .   ? 0.1706 0.1974 0.2702 0.0190  0.0124  0.0019  776 HOH B O   
5048 O  O   . HOH O .   ? 0.4011 0.4481 0.4860 -0.0234 -0.2025 0.0876  777 HOH B O   
5049 O  O   . HOH O .   ? 0.4129 1.8511 1.3207 0.6003  0.5527  0.1824  778 HOH B O   
5050 O  O   . HOH O .   ? 0.2297 0.3120 0.3224 -0.0187 0.0068  -0.0046 779 HOH B O   
5051 O  O   . HOH O .   ? 0.1138 0.2320 0.1791 0.0007  -0.0491 -0.0494 780 HOH B O   
5052 O  O   . HOH O .   ? 0.7426 0.6251 0.5464 0.3828  0.3323  0.2544  781 HOH B O   
5053 O  O   . HOH O .   ? 0.2953 0.1803 0.2764 -0.0131 -0.0395 0.0127  782 HOH B O   
5054 O  O   . HOH O .   ? 1.2339 0.5088 1.6381 0.1720  0.1828  0.2295  783 HOH B O   
5055 O  O   . HOH O .   ? 0.3319 0.4426 0.5925 -0.1397 -0.1430 0.0785  784 HOH B O   
5056 O  O   . HOH O .   ? 0.3998 0.1494 0.2119 0.0313  -0.0531 0.0225  785 HOH B O   
5057 O  O   . HOH O .   ? 0.3045 0.3260 0.3515 -0.0049 -0.0184 -0.0942 786 HOH B O   
5058 O  O   . HOH O .   ? 0.2554 0.1667 0.2755 0.1032  -0.0553 0.0540  787 HOH B O   
5059 O  O   . HOH O .   ? 0.4140 0.1915 0.3064 -0.0983 0.0080  -0.0873 788 HOH B O   
5060 O  O   . HOH O .   ? 0.4169 0.8086 0.5766 0.0873  -0.2073 -0.1568 789 HOH B O   
5061 O  O   . HOH O .   ? 0.4144 0.5577 0.3962 0.0518  0.0549  -0.1002 790 HOH B O   
5062 O  O   . HOH O .   ? 0.3768 0.3339 0.7900 -0.1335 0.0443  -0.0746 791 HOH B O   
5063 O  O   . HOH O .   ? 0.4618 0.3237 0.3822 0.0350  -0.0019 -0.0070 792 HOH B O   
5064 O  O   . HOH O .   ? 0.4916 0.2833 0.5234 -0.1064 0.1493  -0.0881 793 HOH B O   
5065 O  O   . HOH O .   ? 0.2010 0.2642 0.3853 -0.1011 -0.1186 0.0390  794 HOH B O   
5066 O  O   . HOH O .   ? 0.1295 0.0965 0.1893 -0.0104 -0.0129 -0.0046 795 HOH B O   
5067 O  O   . HOH O .   ? 0.5116 0.4253 0.2062 0.1435  0.0443  -0.0666 796 HOH B O   
5068 O  O   . HOH O .   ? 0.4255 0.3813 0.4167 -0.0935 0.1231  -0.0798 797 HOH B O   
5069 O  O   . HOH O .   ? 0.5638 0.4930 0.3267 -0.0271 -0.0551 0.1173  798 HOH B O   
5070 O  O   . HOH O .   ? 0.4185 0.2037 0.4295 0.0030  0.0882  -0.0912 799 HOH B O   
5071 O  O   . HOH O .   ? 0.2786 0.1943 0.2155 -0.0724 -0.0416 -0.0443 800 HOH B O   
5072 O  O   . HOH O .   ? 0.4000 0.2513 0.2693 0.0140  -0.0904 0.0249  801 HOH B O   
5073 O  O   . HOH O .   ? 0.2040 0.2030 0.3998 -0.0763 -0.0102 0.0057  802 HOH B O   
5074 O  O   . HOH O .   ? 1.4460 1.1596 0.6671 -1.0765 -0.4395 0.5792  803 HOH B O   
5075 O  O   . HOH O .   ? 0.3953 0.6812 0.3048 -0.1055 0.0305  0.0253  804 HOH B O   
5076 O  O   . HOH O .   ? 0.6230 0.4160 0.4460 0.0456  0.1657  -0.0059 805 HOH B O   
5077 O  O   . HOH O .   ? 0.1112 0.1940 0.3734 0.0197  -0.0099 0.0082  806 HOH B O   
5078 O  O   . HOH O .   ? 0.5335 0.5206 0.5971 -0.0020 -0.0518 0.0675  807 HOH B O   
5079 O  O   . HOH O .   ? 0.2978 0.2592 0.5940 -0.0728 0.0908  -0.1235 808 HOH B O   
5080 O  O   . HOH O .   ? 0.4779 0.2425 0.3332 -0.0736 0.0888  -0.0538 809 HOH B O   
5081 O  O   . HOH O .   ? 0.3265 0.6128 0.4738 -0.0507 0.1150  0.0373  810 HOH B O   
5082 O  O   . HOH O .   ? 0.6564 0.4248 0.1865 -0.1527 -0.0346 -0.0230 811 HOH B O   
5083 O  O   . HOH O .   ? 0.3574 0.3515 0.2829 -0.1413 0.0489  0.0515  812 HOH B O   
5084 O  O   . HOH O .   ? 0.5024 0.4345 0.4347 -0.0417 -0.2018 -0.0335 813 HOH B O   
5085 O  O   . HOH O .   ? 0.4255 0.1753 0.3052 0.0077  -0.0851 -0.0245 814 HOH B O   
5086 O  O   . HOH O .   ? 0.2148 0.7896 0.5734 -0.0685 -0.0694 -0.0935 815 HOH B O   
5087 O  O   . HOH O .   ? 0.3370 0.2107 0.2967 -0.0522 0.0340  -0.0399 816 HOH B O   
5088 O  O   . HOH O .   ? 0.6808 1.4723 0.5462 -0.2169 0.1023  0.0317  817 HOH B O   
5089 O  O   . HOH O .   ? 0.4943 0.2556 0.2486 0.0522  -0.1055 0.0060  818 HOH B O   
5090 O  O   . HOH O .   ? 0.3614 0.4163 0.4250 0.0026  -0.0122 -0.0215 819 HOH B O   
5091 O  O   . HOH O .   ? 0.5483 0.4119 0.3540 -0.0019 0.0922  -0.1083 820 HOH B O   
5092 O  O   . HOH O .   ? 0.7232 1.3452 0.9682 0.4341  -0.0070 -0.5449 821 HOH B O   
5093 O  O   . HOH O .   ? 0.5511 0.4309 0.4580 0.0071  -0.0093 -0.0873 822 HOH B O   
5094 O  O   . HOH O .   ? 0.3592 0.9280 0.3982 0.3700  0.1744  0.2451  823 HOH B O   
5095 O  O   . HOH O .   ? 0.5720 0.4230 0.5248 0.0164  0.3158  0.0740  824 HOH B O   
5096 O  O   . HOH O .   ? 0.3758 0.6647 0.3876 0.1881  0.0370  0.1041  825 HOH B O   
5097 O  O   . HOH O .   ? 0.4336 0.2858 0.3244 -0.0825 -0.0183 -0.0445 826 HOH B O   
5098 O  O   . HOH O .   ? 0.3720 0.2504 0.4187 -0.0373 0.2102  -0.0737 827 HOH B O   
5099 O  O   . HOH O .   ? 0.2166 0.4072 0.4451 0.0697  0.1018  0.0445  828 HOH B O   
5100 O  O   . HOH O .   ? 0.3747 0.2687 0.3860 0.0671  0.0474  -0.0315 829 HOH B O   
5101 O  O   . HOH O .   ? 0.2100 0.5184 0.3107 -0.0137 0.0303  -0.0496 830 HOH B O   
5102 O  O   . HOH O .   ? 0.9156 1.1815 0.4356 0.2908  -0.1562 0.1596  831 HOH B O   
5103 O  O   . HOH O .   ? 0.7408 0.9258 0.3777 0.3492  0.1669  0.2928  832 HOH B O   
5104 O  O   . HOH O .   ? 0.1548 0.0992 0.1801 0.0157  -0.0277 0.0164  833 HOH B O   
5105 O  O   . HOH O .   ? 0.4774 0.2658 0.4498 -0.1220 0.1726  -0.0795 834 HOH B O   
5106 O  O   . HOH O .   ? 0.4828 0.3192 0.3752 0.1009  0.1208  -0.1451 835 HOH B O   
5107 O  O   . HOH O .   ? 0.2700 0.4436 0.5648 -0.0126 0.1221  0.0980  836 HOH B O   
5108 O  O   . HOH O .   ? 0.9932 0.5102 0.4025 -0.4898 -0.0593 0.0518  837 HOH B O   
5109 O  O   . HOH O .   ? 0.3176 0.3145 0.3388 -0.0729 -0.0944 0.0024  838 HOH B O   
5110 O  O   . HOH O .   ? 0.3802 0.2942 0.3237 -0.0361 -0.1472 0.1027  839 HOH B O   
5111 O  O   . HOH O .   ? 0.5662 0.2763 0.2985 -0.0661 0.1146  -0.0983 840 HOH B O   
5112 O  O   . HOH O .   ? 0.6097 0.6585 0.4824 0.0753  0.1248  -0.1182 841 HOH B O   
5113 O  O   . HOH O .   ? 0.5613 0.4526 0.9703 -0.0020 0.0573  0.2354  842 HOH B O   
5114 O  O   . HOH O .   ? 0.4124 0.5886 0.4898 0.0636  -0.2587 -0.0073 843 HOH B O   
5115 O  O   . HOH O .   ? 0.5710 0.2141 0.7910 -0.0531 -0.1280 -0.0469 844 HOH B O   
5116 O  O   . HOH O .   ? 0.2135 0.0914 0.2064 -0.0087 -0.0324 0.0206  845 HOH B O   
5117 O  O   . HOH O .   ? 0.4611 0.3332 0.5324 0.0869  -0.0313 -0.0044 846 HOH B O   
5118 O  O   . HOH O .   ? 0.6388 0.3445 0.4174 -0.0621 0.0373  -0.0505 847 HOH B O   
5119 O  O   . HOH O .   ? 0.2448 0.4657 0.3804 -0.0423 -0.0988 0.0961  848 HOH B O   
5120 O  O   . HOH O .   ? 0.3707 0.5224 0.3355 0.0070  0.0299  -0.2144 849 HOH B O   
5121 O  O   . HOH O .   ? 0.6560 0.6963 0.4449 0.3152  -0.1106 0.0606  850 HOH B O   
5122 O  O   . HOH O .   ? 0.4210 0.4190 0.4068 -0.0126 -0.0035 -0.0086 851 HOH B O   
5123 O  O   . HOH O .   ? 0.4372 0.5695 0.4672 -0.1151 0.0339  0.2428  852 HOH B O   
5124 O  O   . HOH O .   ? 0.2766 0.2919 0.3269 0.0000  -0.0425 -0.0176 853 HOH B O   
5125 O  O   . HOH O .   ? 0.2375 0.3968 0.7182 0.0197  0.1011  0.0813  854 HOH B O   
5126 O  O   . HOH O .   ? 0.3059 0.3097 0.6276 -0.1616 -0.1967 0.1435  855 HOH B O   
5127 O  O   . HOH O .   ? 0.3269 0.6222 0.5085 -0.1606 -0.0908 0.1019  856 HOH B O   
5128 O  O   . HOH O .   ? 0.5292 0.3343 0.8849 0.0808  0.3529  0.1536  857 HOH B O   
5129 O  O   . HOH O .   ? 0.4113 0.3183 0.3564 -0.0487 -0.0772 0.0732  858 HOH B O   
5130 O  O   . HOH O .   ? 0.4596 0.4363 0.2998 0.2257  -0.0232 -0.0631 859 HOH B O   
5131 O  O   . HOH O .   ? 0.4027 0.4745 0.6990 -0.2703 -0.1674 -0.0738 860 HOH B O   
5132 O  O   . HOH O .   ? 0.3761 0.2398 0.7389 -0.0099 0.0366  -0.0751 861 HOH B O   
5133 O  O   . HOH O .   ? 0.3203 0.1976 0.3736 -0.0737 -0.1850 0.0471  862 HOH B O   
5134 O  O   . HOH O .   ? 0.4736 0.6802 0.2818 -0.0635 0.0722  -0.0276 863 HOH B O   
5135 O  O   . HOH O .   ? 0.2439 0.2414 0.2996 -0.0248 -0.0762 0.0339  864 HOH B O   
5136 O  O   . HOH O .   ? 0.7258 0.3219 0.3774 -0.0984 0.1093  -0.0923 865 HOH B O   
5137 O  O   . HOH O .   ? 0.2234 0.3093 0.2520 0.0296  0.0048  0.0293  866 HOH B O   
5138 O  O   . HOH O .   ? 0.4799 0.3556 0.3783 0.0855  -0.0326 -0.1331 867 HOH B O   
5139 O  O   . HOH O .   ? 0.4383 0.3479 0.3668 -0.0163 -0.0956 -0.0896 868 HOH B O   
5140 O  O   . HOH O .   ? 0.4111 0.6387 0.3388 -0.0619 -0.0197 -0.1164 869 HOH B O   
5141 O  O   . HOH O .   ? 0.3650 0.2973 0.2964 0.1260  0.0054  0.0350  870 HOH B O   
5142 O  O   . HOH O .   ? 0.6377 0.4695 0.5461 -0.2433 0.0340  -0.1638 871 HOH B O   
5143 O  O   . HOH O .   ? 0.2971 0.3603 0.2942 -0.1204 -0.0553 0.0233  872 HOH B O   
5144 O  O   . HOH O .   ? 0.2071 0.4986 0.7558 0.0542  -0.1059 -0.3039 873 HOH B O   
5145 O  O   . HOH O .   ? 0.4947 0.3185 1.0430 -0.0163 -0.1010 -0.0606 874 HOH B O   
5146 O  O   . HOH O .   ? 0.4566 0.2885 0.5385 0.0621  0.0164  -0.1397 875 HOH B O   
5147 O  O   . HOH O .   ? 0.5296 0.3776 0.4038 0.0635  -0.0291 0.0489  876 HOH B O   
5148 O  O   . HOH O .   ? 0.2399 0.2996 0.5048 0.0966  0.0091  0.0582  877 HOH B O   
5149 O  O   . HOH O .   ? 0.3289 0.3603 0.2782 -0.0873 0.0344  0.0143  878 HOH B O   
5150 O  O   . HOH O .   ? 0.4983 0.2637 0.2090 0.0505  -0.0179 -0.0054 879 HOH B O   
5151 O  O   . HOH O .   ? 0.4463 0.5638 0.3149 0.1561  -0.0979 0.1489  880 HOH B O   
5152 O  O   . HOH O .   ? 0.4018 0.3643 0.2662 -0.0575 0.0803  0.0821  881 HOH B O   
5153 O  O   . HOH O .   ? 0.3723 0.2118 0.3704 -0.0610 -0.0513 -0.0483 882 HOH B O   
5154 O  O   . HOH O .   ? 0.4934 0.4217 0.4167 0.1406  -0.2614 -0.1235 883 HOH B O   
5155 O  O   . HOH O .   ? 0.4774 0.4916 0.2105 -0.1448 -0.0211 -0.0837 884 HOH B O   
5156 O  O   . HOH O .   ? 0.5982 0.4232 0.3671 0.1594  0.1816  0.0866  885 HOH B O   
5157 O  O   . HOH O .   ? 0.4614 0.3968 0.3905 -0.0140 -0.0034 0.1348  886 HOH B O   
5158 O  O   . HOH O .   ? 0.4352 0.3483 0.6768 -0.1152 -0.0661 0.0843  887 HOH B O   
5159 O  O   . HOH O .   ? 0.2960 0.6581 0.5503 0.0232  -0.0746 0.0287  888 HOH B O   
5160 O  O   . HOH O .   ? 1.1455 0.2590 0.4041 -0.0900 -0.1529 0.0649  889 HOH B O   
5161 O  O   . HOH O .   ? 0.5547 0.3571 0.3903 0.1825  0.0803  0.0700  890 HOH B O   
5162 O  O   . HOH O .   ? 0.4429 0.3840 0.3481 -0.0427 -0.1156 -0.0819 891 HOH B O   
5163 O  O   . HOH O .   ? 0.6115 0.2951 0.2240 -0.1604 -0.0333 0.0373  892 HOH B O   
5164 O  O   . HOH O .   ? 0.3537 0.3828 0.5661 -0.1548 0.1398  -0.1403 893 HOH B O   
5165 O  O   . HOH O .   ? 0.1925 0.2132 0.2599 -0.0460 -0.0615 -0.0148 894 HOH B O   
5166 O  O   . HOH O .   ? 0.4066 0.2287 0.4739 -0.0331 0.0685  -0.0604 895 HOH B O   
5167 O  O   . HOH O .   ? 0.4379 0.4201 0.4230 0.0170  0.0118  -0.0059 896 HOH B O   
5168 O  O   . HOH O .   ? 0.1789 0.3030 0.3903 -0.0070 -0.0194 0.0273  897 HOH B O   
5169 O  O   . HOH O .   ? 0.9125 0.4765 0.4298 0.1128  0.0666  0.2013  898 HOH B O   
5170 O  O   . HOH O .   ? 0.3846 0.4323 0.6268 0.1582  -0.1168 0.0430  899 HOH B O   
5171 O  O   . HOH O .   ? 0.4314 0.3494 0.4271 0.1474  -0.0255 -0.0603 900 HOH B O   
5172 O  O   . HOH O .   ? 0.9178 0.2281 0.5710 -0.0822 0.3314  0.0034  901 HOH B O   
5173 O  O   . HOH O .   ? 0.2822 0.1389 0.3537 0.0109  0.1103  0.0276  902 HOH B O   
5174 O  O   . HOH O .   ? 0.3603 0.7095 0.5418 -0.2594 -0.0430 -0.0658 903 HOH B O   
5175 O  O   . HOH O .   ? 0.5684 0.2666 0.2328 -0.0776 -0.0971 0.0289  904 HOH B O   
5176 O  O   . HOH O .   ? 0.2657 0.4262 0.5139 0.0992  0.1005  0.0494  905 HOH B O   
5177 O  O   . HOH O .   ? 0.3603 0.6467 0.4187 0.2098  -0.0698 -0.0428 906 HOH B O   
5178 O  O   . HOH O .   ? 0.6147 0.6348 0.5548 -0.0835 -0.3199 -0.0434 907 HOH B O   
# 
