data_8ZA3
# 
_entry.id   8ZA3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8ZA3         pdb_00008za3 10.2210/pdb8za3/pdb 
WWPDB D_1300046687 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZA3 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yixincen@shutcm.edu.cn 
_pdbx_contact_author.name_first         Yixin 
_pdbx_contact_author.name_last          Cen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5851-3170 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, W.H.'  1 ? 
'Cen, Y.X.' 2 ? 
'Wu, Q.'    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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'lbADH mutant A144F with NADP' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, W.H.'  1 ? 
primary 'Cen, Y.X.' 2 ? 
primary 'Wu, Q.'    3 ? 
# 
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 'R-specific alcohol dehydrogenase'                 26674.121 1   ? E144F ? ? 
2 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   1   ? ?     ? ? 
3 non-polymer syn 'TETRAETHYLENE GLYCOL'                             194.226   1   ? ?     ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                    24.305    2   ? ?     ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                     62.068    1   ? ?     ? ? 
6 water       nat water                                              18.015    199 ? ?     ? ? 
# 
_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       
;SNRLDGKVAIITGGTLGIGLAIATKFVEEGAKVMITGRHSDVGEKAAKSVGTPDQIQFFQHDSSDEDGWTKLFDATEKAF
GPVSTLVNNAGIAVNKSVEETTTAEWRKLLAVNLDGVFFGTRLGIQRMKNKGLGASIINMSSIFGFVGDPSLGAYNASKG
AVRIMSKSAALDCALKDYDVRVNTVHPGYIKTPLVDDLPGAEEAMSQRTKTPMGHIGEPNDIAYICVYLASNESKFATGS
EFVVDGGYTAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNRLDGKVAIITGGTLGIGLAIATKFVEEGAKVMITGRHSDVGEKAAKSVGTPDQIQFFQHDSSDEDGWTKLFDATEKAF
GPVSTLVNNAGIAVNKSVEETTTAEWRKLLAVNLDGVFFGTRLGIQRMKNKGLGASIINMSSIFGFVGDPSLGAYNASKG
AVRIMSKSAALDCALKDYDVRVNTVHPGYIKTPLVDDLPGAEEAMSQRTKTPMGHIGEPNDIAYICVYLASNESKFATGS
EFVVDGGYTAQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP 
3 'TETRAETHYLENE GLYCOL'                             PG4 
4 'MAGNESIUM ION'                                    MG  
5 1,2-ETHANEDIOL                                     EDO 
6 water                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ARG n 
1 4   LEU n 
1 5   ASP n 
1 6   GLY n 
1 7   LYS n 
1 8   VAL n 
1 9   ALA n 
1 10  ILE n 
1 11  ILE n 
1 12  THR n 
1 13  GLY n 
1 14  GLY n 
1 15  THR n 
1 16  LEU n 
1 17  GLY n 
1 18  ILE n 
1 19  GLY n 
1 20  LEU n 
1 21  ALA n 
1 22  ILE n 
1 23  ALA n 
1 24  THR n 
1 25  LYS n 
1 26  PHE n 
1 27  VAL n 
1 28  GLU n 
1 29  GLU n 
1 30  GLY n 
1 31  ALA n 
1 32  LYS n 
1 33  VAL n 
1 34  MET n 
1 35  ILE n 
1 36  THR n 
1 37  GLY n 
1 38  ARG n 
1 39  HIS n 
1 40  SER n 
1 41  ASP n 
1 42  VAL n 
1 43  GLY n 
1 44  GLU n 
1 45  LYS n 
1 46  ALA n 
1 47  ALA n 
1 48  LYS n 
1 49  SER n 
1 50  VAL n 
1 51  GLY n 
1 52  THR n 
1 53  PRO n 
1 54  ASP n 
1 55  GLN n 
1 56  ILE n 
1 57  GLN n 
1 58  PHE n 
1 59  PHE n 
1 60  GLN n 
1 61  HIS n 
1 62  ASP n 
1 63  SER n 
1 64  SER n 
1 65  ASP n 
1 66  GLU n 
1 67  ASP n 
1 68  GLY n 
1 69  TRP n 
1 70  THR n 
1 71  LYS n 
1 72  LEU n 
1 73  PHE n 
1 74  ASP n 
1 75  ALA n 
1 76  THR n 
1 77  GLU n 
1 78  LYS n 
1 79  ALA n 
1 80  PHE n 
1 81  GLY n 
1 82  PRO n 
1 83  VAL n 
1 84  SER n 
1 85  THR n 
1 86  LEU n 
1 87  VAL n 
1 88  ASN n 
1 89  ASN n 
1 90  ALA n 
1 91  GLY n 
1 92  ILE n 
1 93  ALA n 
1 94  VAL n 
1 95  ASN n 
1 96  LYS n 
1 97  SER n 
1 98  VAL n 
1 99  GLU n 
1 100 GLU n 
1 101 THR n 
1 102 THR n 
1 103 THR n 
1 104 ALA n 
1 105 GLU n 
1 106 TRP n 
1 107 ARG n 
1 108 LYS n 
1 109 LEU n 
1 110 LEU n 
1 111 ALA n 
1 112 VAL n 
1 113 ASN n 
1 114 LEU n 
1 115 ASP n 
1 116 GLY n 
1 117 VAL n 
1 118 PHE n 
1 119 PHE n 
1 120 GLY n 
1 121 THR n 
1 122 ARG n 
1 123 LEU n 
1 124 GLY n 
1 125 ILE n 
1 126 GLN n 
1 127 ARG n 
1 128 MET n 
1 129 LYS n 
1 130 ASN n 
1 131 LYS n 
1 132 GLY n 
1 133 LEU n 
1 134 GLY n 
1 135 ALA n 
1 136 SER n 
1 137 ILE n 
1 138 ILE n 
1 139 ASN n 
1 140 MET n 
1 141 SER n 
1 142 SER n 
1 143 ILE n 
1 144 PHE n 
1 145 GLY n 
1 146 PHE n 
1 147 VAL n 
1 148 GLY n 
1 149 ASP n 
1 150 PRO n 
1 151 SER n 
1 152 LEU n 
1 153 GLY n 
1 154 ALA n 
1 155 TYR n 
1 156 ASN n 
1 157 ALA n 
1 158 SER n 
1 159 LYS n 
1 160 GLY n 
1 161 ALA n 
1 162 VAL n 
1 163 ARG n 
1 164 ILE n 
1 165 MET n 
1 166 SER n 
1 167 LYS n 
1 168 SER n 
1 169 ALA n 
1 170 ALA n 
1 171 LEU n 
1 172 ASP n 
1 173 CYS n 
1 174 ALA n 
1 175 LEU n 
1 176 LYS n 
1 177 ASP n 
1 178 TYR n 
1 179 ASP n 
1 180 VAL n 
1 181 ARG n 
1 182 VAL n 
1 183 ASN n 
1 184 THR n 
1 185 VAL n 
1 186 HIS n 
1 187 PRO n 
1 188 GLY n 
1 189 TYR n 
1 190 ILE n 
1 191 LYS n 
1 192 THR n 
1 193 PRO n 
1 194 LEU n 
1 195 VAL n 
1 196 ASP n 
1 197 ASP n 
1 198 LEU n 
1 199 PRO n 
1 200 GLY n 
1 201 ALA n 
1 202 GLU n 
1 203 GLU n 
1 204 ALA n 
1 205 MET n 
1 206 SER n 
1 207 GLN n 
1 208 ARG n 
1 209 THR n 
1 210 LYS n 
1 211 THR n 
1 212 PRO n 
1 213 MET n 
1 214 GLY n 
1 215 HIS n 
1 216 ILE n 
1 217 GLY n 
1 218 GLU n 
1 219 PRO n 
1 220 ASN n 
1 221 ASP n 
1 222 ILE n 
1 223 ALA n 
1 224 TYR n 
1 225 ILE n 
1 226 CYS n 
1 227 VAL n 
1 228 TYR n 
1 229 LEU n 
1 230 ALA n 
1 231 SER n 
1 232 ASN n 
1 233 GLU n 
1 234 SER n 
1 235 LYS n 
1 236 PHE n 
1 237 ALA n 
1 238 THR n 
1 239 GLY n 
1 240 SER n 
1 241 GLU n 
1 242 PHE n 
1 243 VAL n 
1 244 VAL n 
1 245 ASP n 
1 246 GLY n 
1 247 GLY n 
1 248 TYR n 
1 249 THR n 
1 250 ALA n 
1 251 GLN 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                   251 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 radh 
_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      'Levilactobacillus brevis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1580 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                            ?                                            
'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                           ?                                            
'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                         ?                                            
'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                    ?                                            
'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                           ?                                            
'C3 H7 N O2 S'      121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                     'ETHYLENE GLYCOL'                            
'C2 H6 O2'          62.068  
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 
MG  non-polymer         . 'MAGNESIUM ION'                                    ?                                            'Mg 2' 
24.305  
NAP non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'                             ?                                            
'C8 H18 O5'         194.226 
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 
# 
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   SER 1   1   1   SER SER A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   ARG 3   3   3   ARG ARG A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  THR 12  12  12  THR THR A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ALA 21  21  21  ALA ALA 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  THR 24  24  24  THR THR A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  LYS 32  32  32  LYS LYS A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  MET 34  34  34  MET MET A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  HIS 39  39  39  HIS HIS A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  HIS 61  61  61  HIS HIS A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  TRP 69  69  69  TRP TRP A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PHE 73  73  73  PHE PHE A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 TRP 106 106 106 TRP TRP A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 MET 128 128 128 MET MET A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 ASN 130 130 130 ASN ASN A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 MET 140 140 140 MET MET A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 CYS 173 173 173 CYS CYS A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 TYR 189 189 189 TYR TYR A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 GLU 203 203 203 GLU GLU A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 MET 205 205 205 MET MET A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 GLN 207 207 207 GLN GLN A . n 
A 1 208 ARG 208 208 208 ARG ARG A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 MET 213 213 213 MET MET A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 HIS 215 215 215 HIS HIS A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 ASN 220 220 220 ASN ASN A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 ILE 225 225 225 ILE ILE A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 TYR 248 248 248 TYR TYR A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAP 1   301 301 NAP NAP A . 
C 3 PG4 1   302 302 PG4 PG4 A . 
D 4 MG  1   303 1   MG  MG  A . 
E 4 MG  1   304 2   MG  MG  A . 
F 5 EDO 1   305 226 EDO EDO A . 
G 6 HOH 1   401 180 HOH HOH A . 
G 6 HOH 2   402 144 HOH HOH A . 
G 6 HOH 3   403 154 HOH HOH A . 
G 6 HOH 4   404 219 HOH HOH A . 
G 6 HOH 5   405 179 HOH HOH A . 
G 6 HOH 6   406 140 HOH HOH A . 
G 6 HOH 7   407 101 HOH HOH A . 
G 6 HOH 8   408 3   HOH HOH A . 
G 6 HOH 9   409 49  HOH HOH A . 
G 6 HOH 10  410 108 HOH HOH A . 
G 6 HOH 11  411 124 HOH HOH A . 
G 6 HOH 12  412 57  HOH HOH A . 
G 6 HOH 13  413 32  HOH HOH A . 
G 6 HOH 14  414 83  HOH HOH A . 
G 6 HOH 15  415 109 HOH HOH A . 
G 6 HOH 16  416 15  HOH HOH A . 
G 6 HOH 17  417 25  HOH HOH A . 
G 6 HOH 18  418 2   HOH HOH A . 
G 6 HOH 19  419 66  HOH HOH A . 
G 6 HOH 20  420 196 HOH HOH A . 
G 6 HOH 21  421 79  HOH HOH A . 
G 6 HOH 22  422 29  HOH HOH A . 
G 6 HOH 23  423 174 HOH HOH A . 
G 6 HOH 24  424 102 HOH HOH A . 
G 6 HOH 25  425 145 HOH HOH A . 
G 6 HOH 26  426 204 HOH HOH A . 
G 6 HOH 27  427 70  HOH HOH A . 
G 6 HOH 28  428 146 HOH HOH A . 
G 6 HOH 29  429 103 HOH HOH A . 
G 6 HOH 30  430 96  HOH HOH A . 
G 6 HOH 31  431 21  HOH HOH A . 
G 6 HOH 32  432 171 HOH HOH A . 
G 6 HOH 33  433 30  HOH HOH A . 
G 6 HOH 34  434 40  HOH HOH A . 
G 6 HOH 35  435 169 HOH HOH A . 
G 6 HOH 36  436 8   HOH HOH A . 
G 6 HOH 37  437 27  HOH HOH A . 
G 6 HOH 38  438 82  HOH HOH A . 
G 6 HOH 39  439 141 HOH HOH A . 
G 6 HOH 40  440 14  HOH HOH A . 
G 6 HOH 41  441 9   HOH HOH A . 
G 6 HOH 42  442 19  HOH HOH A . 
G 6 HOH 43  443 92  HOH HOH A . 
G 6 HOH 44  444 74  HOH HOH A . 
G 6 HOH 45  445 13  HOH HOH A . 
G 6 HOH 46  446 26  HOH HOH A . 
G 6 HOH 47  447 62  HOH HOH A . 
G 6 HOH 48  448 53  HOH HOH A . 
G 6 HOH 49  449 189 HOH HOH A . 
G 6 HOH 50  450 35  HOH HOH A . 
G 6 HOH 51  451 107 HOH HOH A . 
G 6 HOH 52  452 6   HOH HOH A . 
G 6 HOH 53  453 167 HOH HOH A . 
G 6 HOH 54  454 16  HOH HOH A . 
G 6 HOH 55  455 97  HOH HOH A . 
G 6 HOH 56  456 1   HOH HOH A . 
G 6 HOH 57  457 110 HOH HOH A . 
G 6 HOH 58  458 209 HOH HOH A . 
G 6 HOH 59  459 225 HOH HOH A . 
G 6 HOH 60  460 64  HOH HOH A . 
G 6 HOH 61  461 181 HOH HOH A . 
G 6 HOH 62  462 48  HOH HOH A . 
G 6 HOH 63  463 63  HOH HOH A . 
G 6 HOH 64  464 41  HOH HOH A . 
G 6 HOH 65  465 18  HOH HOH A . 
G 6 HOH 66  466 77  HOH HOH A . 
G 6 HOH 67  467 224 HOH HOH A . 
G 6 HOH 68  468 142 HOH HOH A . 
G 6 HOH 69  469 20  HOH HOH A . 
G 6 HOH 70  470 117 HOH HOH A . 
G 6 HOH 71  471 65  HOH HOH A . 
G 6 HOH 72  472 52  HOH HOH A . 
G 6 HOH 73  473 51  HOH HOH A . 
G 6 HOH 74  474 4   HOH HOH A . 
G 6 HOH 75  475 38  HOH HOH A . 
G 6 HOH 76  476 221 HOH HOH A . 
G 6 HOH 77  477 81  HOH HOH A . 
G 6 HOH 78  478 61  HOH HOH A . 
G 6 HOH 79  479 113 HOH HOH A . 
G 6 HOH 80  480 23  HOH HOH A . 
G 6 HOH 81  481 106 HOH HOH A . 
G 6 HOH 82  482 131 HOH HOH A . 
G 6 HOH 83  483 56  HOH HOH A . 
G 6 HOH 84  484 118 HOH HOH A . 
G 6 HOH 85  485 133 HOH HOH A . 
G 6 HOH 86  486 188 HOH HOH A . 
G 6 HOH 87  487 39  HOH HOH A . 
G 6 HOH 88  488 80  HOH HOH A . 
G 6 HOH 89  489 132 HOH HOH A . 
G 6 HOH 90  490 183 HOH HOH A . 
G 6 HOH 91  491 54  HOH HOH A . 
G 6 HOH 92  492 137 HOH HOH A . 
G 6 HOH 93  493 147 HOH HOH A . 
G 6 HOH 94  494 55  HOH HOH A . 
G 6 HOH 95  495 127 HOH HOH A . 
G 6 HOH 96  496 192 HOH HOH A . 
G 6 HOH 97  497 73  HOH HOH A . 
G 6 HOH 98  498 50  HOH HOH A . 
G 6 HOH 99  499 84  HOH HOH A . 
G 6 HOH 100 500 210 HOH HOH A . 
G 6 HOH 101 501 71  HOH HOH A . 
G 6 HOH 102 502 112 HOH HOH A . 
G 6 HOH 103 503 59  HOH HOH A . 
G 6 HOH 104 504 91  HOH HOH A . 
G 6 HOH 105 505 212 HOH HOH A . 
G 6 HOH 106 506 85  HOH HOH A . 
G 6 HOH 107 507 205 HOH HOH A . 
G 6 HOH 108 508 47  HOH HOH A . 
G 6 HOH 109 509 11  HOH HOH A . 
G 6 HOH 110 510 17  HOH HOH A . 
G 6 HOH 111 511 130 HOH HOH A . 
G 6 HOH 112 512 22  HOH HOH A . 
G 6 HOH 113 513 193 HOH HOH A . 
G 6 HOH 114 514 31  HOH HOH A . 
G 6 HOH 115 515 34  HOH HOH A . 
G 6 HOH 116 516 67  HOH HOH A . 
G 6 HOH 117 517 222 HOH HOH A . 
G 6 HOH 118 518 76  HOH HOH A . 
G 6 HOH 119 519 10  HOH HOH A . 
G 6 HOH 120 520 138 HOH HOH A . 
G 6 HOH 121 521 78  HOH HOH A . 
G 6 HOH 122 522 69  HOH HOH A . 
G 6 HOH 123 523 42  HOH HOH A . 
G 6 HOH 124 524 88  HOH HOH A . 
G 6 HOH 125 525 75  HOH HOH A . 
G 6 HOH 126 526 89  HOH HOH A . 
G 6 HOH 127 527 157 HOH HOH A . 
G 6 HOH 128 528 12  HOH HOH A . 
G 6 HOH 129 529 104 HOH HOH A . 
G 6 HOH 130 530 116 HOH HOH A . 
G 6 HOH 131 531 105 HOH HOH A . 
G 6 HOH 132 532 46  HOH HOH A . 
G 6 HOH 133 533 148 HOH HOH A . 
G 6 HOH 134 534 43  HOH HOH A . 
G 6 HOH 135 535 139 HOH HOH A . 
G 6 HOH 136 536 143 HOH HOH A . 
G 6 HOH 137 537 7   HOH HOH A . 
G 6 HOH 138 538 72  HOH HOH A . 
G 6 HOH 139 539 36  HOH HOH A . 
G 6 HOH 140 540 214 HOH HOH A . 
G 6 HOH 141 541 213 HOH HOH A . 
G 6 HOH 142 542 220 HOH HOH A . 
G 6 HOH 143 543 2   HOH HOH A . 
G 6 HOH 144 544 152 HOH HOH A . 
G 6 HOH 145 545 44  HOH HOH A . 
G 6 HOH 146 546 170 HOH HOH A . 
G 6 HOH 147 547 115 HOH HOH A . 
G 6 HOH 148 548 126 HOH HOH A . 
G 6 HOH 149 549 200 HOH HOH A . 
G 6 HOH 150 550 28  HOH HOH A . 
G 6 HOH 151 551 149 HOH HOH A . 
G 6 HOH 152 552 5   HOH HOH A . 
G 6 HOH 153 553 218 HOH HOH A . 
G 6 HOH 154 554 176 HOH HOH A . 
G 6 HOH 155 555 94  HOH HOH A . 
G 6 HOH 156 556 121 HOH HOH A . 
G 6 HOH 157 557 195 HOH HOH A . 
G 6 HOH 158 558 98  HOH HOH A . 
G 6 HOH 159 559 68  HOH HOH A . 
G 6 HOH 160 560 223 HOH HOH A . 
G 6 HOH 161 561 37  HOH HOH A . 
G 6 HOH 162 562 58  HOH HOH A . 
G 6 HOH 163 563 33  HOH HOH A . 
G 6 HOH 164 564 203 HOH HOH A . 
G 6 HOH 165 565 198 HOH HOH A . 
G 6 HOH 166 566 185 HOH HOH A . 
G 6 HOH 167 567 24  HOH HOH A . 
G 6 HOH 168 568 111 HOH HOH A . 
G 6 HOH 169 569 86  HOH HOH A . 
G 6 HOH 170 570 1   HOH HOH A . 
G 6 HOH 171 571 194 HOH HOH A . 
G 6 HOH 172 572 190 HOH HOH A . 
G 6 HOH 173 573 114 HOH HOH A . 
G 6 HOH 174 574 202 HOH HOH A . 
G 6 HOH 175 575 182 HOH HOH A . 
G 6 HOH 176 576 150 HOH HOH A . 
G 6 HOH 177 577 215 HOH HOH A . 
G 6 HOH 178 578 129 HOH HOH A . 
G 6 HOH 179 579 208 HOH HOH A . 
G 6 HOH 180 580 165 HOH HOH A . 
G 6 HOH 181 581 156 HOH HOH A . 
G 6 HOH 182 582 93  HOH HOH A . 
G 6 HOH 183 583 197 HOH HOH A . 
G 6 HOH 184 584 201 HOH HOH A . 
G 6 HOH 185 585 87  HOH HOH A . 
G 6 HOH 186 586 119 HOH HOH A . 
G 6 HOH 187 587 155 HOH HOH A . 
G 6 HOH 188 588 207 HOH HOH A . 
G 6 HOH 189 589 164 HOH HOH A . 
G 6 HOH 190 590 161 HOH HOH A . 
G 6 HOH 191 591 163 HOH HOH A . 
G 6 HOH 192 592 95  HOH HOH A . 
G 6 HOH 193 593 178 HOH HOH A . 
G 6 HOH 194 594 162 HOH HOH A . 
G 6 HOH 195 595 120 HOH HOH A . 
G 6 HOH 196 596 199 HOH HOH A . 
G 6 HOH 197 597 206 HOH HOH A . 
G 6 HOH 198 598 172 HOH HOH A . 
G 6 HOH 199 599 177 HOH HOH A . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.17.1_3660 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZA3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.900 
_cell.length_a_esd                 ? 
_cell.length_b                     82.360 
_cell.length_b_esd                 ? 
_cell.length_c                     112.640 
_cell.length_c_esd                 ? 
_cell.volume                       518585.999 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZA3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   8ZA3 
_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             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.39 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;30% PEG1000
0.1 M Tris pH 8.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 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         2023-04-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_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   0.97852 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97852 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          16.72 
_reflns.entry_id                                       8ZA3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.56 
_reflns.d_resolution_low                               46.25 
_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                                     36446 
_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                           97.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          27.7 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.56 
_reflns_shell.d_res_low                                     1.59 
_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                             1464 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_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_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.882 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               21.30 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8ZA3 
_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                            1.56 
_refine.ls_d_res_low                             26.67 
_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                     36405 
_refine.ls_number_reflns_R_free                  1831 
_refine.ls_number_reflns_R_work                  34574 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.38 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1639 
_refine.ls_R_factor_R_free                       0.1879 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1627 
_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                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 17.9995 
_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                            0.1359 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.56 
_refine_hist.d_res_low                        26.67 
_refine_hist.number_atoms_solvent             199 
_refine_hist.number_atoms_total               2139 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1873 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0084  ? 1994 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9390  ? 2701 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0599  ? 306  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 344  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.2987 ? 746  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.56 1.60  . . 105 2240 82.89  . . . . 0.2213 . . . . . . . . . . . 0.2516 
'X-RAY DIFFRACTION' 1.60 1.65  . . 127 2464 91.72  . . . . 0.1869 . . . . . . . . . . . 0.2098 
'X-RAY DIFFRACTION' 1.65 1.70  . . 150 2621 96.96  . . . . 0.1562 . . . . . . . . . . . 0.2055 
'X-RAY DIFFRACTION' 1.70 1.76  . . 133 2684 99.82  . . . . 0.1550 . . . . . . . . . . . 0.1802 
'X-RAY DIFFRACTION' 1.76 1.83  . . 142 2717 99.97  . . . . 0.1581 . . . . . . . . . . . 0.1635 
'X-RAY DIFFRACTION' 1.83 1.92  . . 149 2656 98.32  . . . . 0.2021 . . . . . . . . . . . 0.2449 
'X-RAY DIFFRACTION' 1.92 2.02  . . 140 2663 98.42  . . . . 0.1804 . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 2.02 2.14  . . 156 2711 99.34  . . . . 0.1761 . . . . . . . . . . . 0.2237 
'X-RAY DIFFRACTION' 2.14 2.31  . . 136 2661 98.31  . . . . 0.1689 . . . . . . . . . . . 0.1991 
'X-RAY DIFFRACTION' 2.31 2.54  . . 159 2721 100.00 . . . . 0.1526 . . . . . . . . . . . 0.1627 
'X-RAY DIFFRACTION' 2.54 2.91  . . 164 2733 99.93  . . . . 0.1552 . . . . . . . . . . . 0.1855 
'X-RAY DIFFRACTION' 2.91 3.67  . . 146 2776 99.93  . . . . 0.1541 . . . . . . . . . . . 0.1874 
'X-RAY DIFFRACTION' 3.67 26.67 . . 124 2927 99.93  . . . . 0.1538 . . . . . . . . . . . 0.1518 
# 
_struct.entry_id                     8ZA3 
_struct.title                        'lbADH mutant A144F with NADP' 
_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        8ZA3 
_struct_keywords.text            'alcohol dehydrogenase, rational design, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q84EX5_LEVBR 
_struct_ref.pdbx_db_accession          Q84EX5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SNRLDGKVAIITGGTLGIGLAIATKFVEEGAKVMITGRHSDVGEKAAKSVGTPDQIQFFQHDSSDEDGWTKLFDATEKAF
GPVSTLVNNAGIAVNKSVEETTTAEWRKLLAVNLDGVFFGTRLGIQRMKNKGLGASIINMSSIEGFVGDPSLGAYNASKG
AVRIMSKSAALDCALKDYDVRVNTVHPGYIKTPLVDDLPGAEEAMSQRTKTPMGHIGEPNDIAYICVYLASNESKFATGS
EFVVDGGYTAQ
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZA3 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 251 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q84EX5 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  252 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       251 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8ZA3 
_struct_ref_seq_dif.mon_id                       PHE 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      144 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q84EX5 
_struct_ref_seq_dif.db_mon_id                    GLU 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          145 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            144 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
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_and_software_defined_assembly PISA tetrameric 4 
2 author_and_software_defined_assembly PISA dimeric    2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 20980 ? 
1 MORE         -126  ? 
1 'SSA (A^2)'  31580 ? 
2 'ABSA (A^2)' 6450  ? 
2 MORE         -36   ? 
2 'SSA (A^2)'  19730 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2,3,4 A,B,C,D,E,F,G 
2 1,2     A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_455 -x-1,-y,z -1.0000000000 0.0000000000 0.0000000000 -55.9000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_455 -x-1,y,-z -1.0000000000 0.0000000000 0.0000000000 -55.9000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 LEU A 16  ? GLU A 29  ? LEU A 16  GLU A 29  1 ? 14 
HELX_P HELX_P2  AA2 HIS A 39  ? GLY A 51  ? HIS A 39  GLY A 51  1 ? 13 
HELX_P HELX_P3  AA3 ASP A 65  ? GLY A 81  ? ASP A 65  GLY A 81  1 ? 17 
HELX_P HELX_P4  AA4 THR A 102 ? LEU A 114 ? THR A 102 LEU A 114 1 ? 13 
HELX_P HELX_P5  AA5 LEU A 114 ? LYS A 129 ? LEU A 114 LYS A 129 1 ? 16 
HELX_P HELX_P6  AA6 SER A 142 ? PHE A 146 ? SER A 142 PHE A 146 5 ? 5  
HELX_P HELX_P7  AA7 LEU A 152 ? LYS A 176 ? LEU A 152 LYS A 176 1 ? 25 
HELX_P HELX_P8  AA8 THR A 192 ? ASP A 197 ? THR A 192 ASP A 197 1 ? 6  
HELX_P HELX_P9  AA9 GLY A 200 ? SER A 206 ? GLY A 200 SER A 206 1 ? 7  
HELX_P HELX_P10 AB1 GLU A 218 ? SER A 231 ? GLU A 218 SER A 231 1 ? 14 
HELX_P HELX_P11 AB2 ASN A 232 ? LYS A 235 ? ASN A 232 LYS A 235 5 ? 4  
HELX_P HELX_P12 AB3 GLY A 247 ? GLN A 251 ? GLY A 247 GLN A 251 5 ? 5  
# 
_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 GLN 251 O   ? ? ? 1_555 D MG  . MG ? ? A GLN 251 A MG  303 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc2  metalc ? ? A GLN 251 O   ? ? ? 1_555 D MG  . MG ? ? A GLN 251 A MG  303 4_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc3  metalc ? ? B NAP .   O2A ? ? ? 1_555 E MG  . MG ? ? A NAP 301 A MG  304 1_555 ? ? ? ? ? ? ? 2.487 ? ? 
metalc4  metalc ? ? B NAP .   O2N ? ? ? 1_555 E MG  . MG ? ? A NAP 301 A MG  304 1_555 ? ? ? ? ? ? ? 1.805 ? ? 
metalc5  metalc ? ? B NAP .   O1X ? ? ? 1_555 E MG  . MG ? ? A NAP 301 A MG  304 1_555 ? ? ? ? ? ? ? 2.180 ? ? 
metalc6  metalc ? ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  303 A HOH 474 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc7  metalc ? ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  303 A HOH 474 4_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc8  metalc ? ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  303 A HOH 537 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc9  metalc ? ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  303 A HOH 537 4_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc10 metalc ? ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  303 A HOH 567 1_555 ? ? ? ? ? ? ? 2.161 ? ? 
metalc11 metalc ? ? D MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  303 A HOH 567 4_555 ? ? ? ? ? ? ? 2.161 ? ? 
metalc12 metalc ? ? E MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  304 A HOH 517 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc13 metalc ? ? E MG  .   MG  ? ? ? 1_555 G HOH . O  ? ? A MG  304 A HOH 524 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
# 
_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  O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? A GLN 251 ? A GLN 251 ? 1_555 0.0   ? 
2  O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 474 ? 1_555 92.0  ? 
3  O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 474 ? 1_555 92.0  ? 
4  O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 474 ? 4_555 88.0  ? 
5  O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 474 ? 4_555 88.0  ? 
6  O   ? G HOH .   ? A HOH 474 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 474 ? 4_555 178.4 ? 
7  O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 1_555 90.0  ? 
8  O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 1_555 90.0  ? 
9  O   ? G HOH .   ? A HOH 474 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 1_555 94.6  ? 
10 O   ? G HOH .   ? A HOH 474 ? 4_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 1_555 83.9  ? 
11 O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 4_555 90.0  ? 
12 O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 4_555 90.0  ? 
13 O   ? G HOH .   ? A HOH 474 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 4_555 83.9  ? 
14 O   ? G HOH .   ? A HOH 474 ? 4_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 4_555 94.6  ? 
15 O   ? G HOH .   ? A HOH 537 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 537 ? 4_555 10.7  ? 
16 O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 1_555 99.0  ? 
17 O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 1_555 99.0  ? 
18 O   ? G HOH .   ? A HOH 474 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 1_555 100.6 ? 
19 O   ? G HOH .   ? A HOH 474 ? 4_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 1_555 80.9  ? 
20 O   ? G HOH .   ? A HOH 537 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 1_555 162.0 ? 
21 O   ? G HOH .   ? A HOH 537 ? 4_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 1_555 169.7 ? 
22 O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 4_555 81.0  ? 
23 O   ? A GLN 251 ? A GLN 251 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 4_555 81.0  ? 
24 O   ? G HOH .   ? A HOH 474 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 4_555 80.9  ? 
25 O   ? G HOH .   ? A HOH 474 ? 4_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 4_555 100.6 ? 
26 O   ? G HOH .   ? A HOH 537 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 4_555 169.7 ? 
27 O   ? G HOH .   ? A HOH 537 ? 4_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 4_555 162.0 ? 
28 O   ? G HOH .   ? A HOH 567 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? G HOH .   ? A HOH 567 ? 4_555 27.3  ? 
29 O2A ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O2N ? B NAP .   ? A NAP 301 ? 1_555 80.2  ? 
30 O2A ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O1X ? B NAP .   ? A NAP 301 ? 1_555 97.7  ? 
31 O2N ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O1X ? B NAP .   ? A NAP 301 ? 1_555 97.3  ? 
32 O2A ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O   ? G HOH .   ? A HOH 517 ? 1_555 158.3 ? 
33 O2N ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O   ? G HOH .   ? A HOH 517 ? 1_555 94.5  ? 
34 O1X ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O   ? G HOH .   ? A HOH 517 ? 1_555 103.8 ? 
35 O2A ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O   ? G HOH .   ? A HOH 524 ? 1_555 79.0  ? 
36 O2N ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O   ? G HOH .   ? A HOH 524 ? 1_555 87.5  ? 
37 O1X ? B NAP .   ? A NAP 301 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O   ? G HOH .   ? A HOH 524 ? 1_555 173.7 ? 
38 O   ? G HOH .   ? A HOH 517 ? 1_555 MG ? E MG . ? A MG 304 ? 1_555 O   ? G HOH .   ? A HOH 524 ? 1_555 79.8  ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   7 
_struct_sheet.details          ? 
# 
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 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? 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 ILE A 56  ? GLN A 60  ? ILE A 56  GLN A 60  
AA1 2 LYS A 32  ? GLY A 37  ? LYS A 32  GLY A 37  
AA1 3 VAL A 8   ? ILE A 11  ? VAL A 8   ILE A 11  
AA1 4 THR A 85  ? ASN A 88  ? THR A 85  ASN A 88  
AA1 5 ALA A 135 ? MET A 140 ? ALA A 135 MET A 140 
AA1 6 VAL A 180 ? PRO A 187 ? VAL A 180 PRO A 187 
AA1 7 GLU A 241 ? VAL A 244 ? GLU A 241 VAL A 244 
# 
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 O GLN A 57  ? O GLN A 57  N ILE A 35  ? N ILE A 35  
AA1 2 3 O LYS A 32  ? O LYS A 32  N ALA A 9   ? N ALA A 9   
AA1 3 4 N ILE A 10  ? N ILE A 10  O VAL A 87  ? O VAL A 87  
AA1 4 5 N LEU A 86  ? N LEU A 86  O ILE A 138 ? O ILE A 138 
AA1 5 6 N ILE A 137 ? N ILE A 137 O ARG A 181 ? O ARG A 181 
AA1 6 7 N HIS A 186 ? N HIS A 186 O PHE A 242 ? O PHE A 242 
# 
_pdbx_entry_details.entry_id                   8ZA3 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   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 141 ? ? -108.38 -128.31 
2 1 LYS A 210 ? ? -109.26 -66.58  
3 1 ASP A 245 ? ? -141.87 14.91   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A MG  303 ? D MG  . 
2 1 A HOH 537 ? G HOH . 
3 1 A HOH 575 ? G HOH . 
4 1 A HOH 581 ? G HOH . 
5 1 A HOH 582 ? G HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -25.1154674252 
_pdbx_refine_tls.origin_y         -15.6228146679 
_pdbx_refine_tls.origin_z         -14.6881414064 
_pdbx_refine_tls.T[1][1]          0.161190668022 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.00930849720202 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.00396274351043 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.160267512125 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0214989516235 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.152855978295 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.65552137895 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0179814620635 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0795531118758 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.523818831783 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.056886922702 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.542711606898 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0204563634493 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0845346519545 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.119093808676 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0833064009984 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0138834576232 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0283809095664 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0755514692968 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.031957379823 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0113383762203 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
MG  MG   MG N N 260 
NAP PA   P  N R 261 
NAP O1A  O  N N 262 
NAP O2A  O  N N 263 
NAP O5B  O  N N 264 
NAP C5B  C  N N 265 
NAP C4B  C  N R 266 
NAP O4B  O  N N 267 
NAP C3B  C  N R 268 
NAP O3B  O  N N 269 
NAP C2B  C  N R 270 
NAP O2B  O  N N 271 
NAP C1B  C  N R 272 
NAP N9A  N  Y N 273 
NAP C8A  C  Y N 274 
NAP N7A  N  Y N 275 
NAP C5A  C  Y N 276 
NAP C6A  C  Y N 277 
NAP N6A  N  N N 278 
NAP N1A  N  Y N 279 
NAP C2A  C  Y N 280 
NAP N3A  N  Y N 281 
NAP C4A  C  Y N 282 
NAP O3   O  N N 283 
NAP PN   P  N N 284 
NAP O1N  O  N N 285 
NAP O2N  O  N N 286 
NAP O5D  O  N N 287 
NAP C5D  C  N N 288 
NAP C4D  C  N R 289 
NAP O4D  O  N N 290 
NAP C3D  C  N S 291 
NAP O3D  O  N N 292 
NAP C2D  C  N R 293 
NAP O2D  O  N N 294 
NAP C1D  C  N R 295 
NAP N1N  N  Y N 296 
NAP C2N  C  Y N 297 
NAP C3N  C  Y N 298 
NAP C7N  C  N N 299 
NAP O7N  O  N N 300 
NAP N7N  N  N N 301 
NAP C4N  C  Y N 302 
NAP C5N  C  Y N 303 
NAP C6N  C  Y N 304 
NAP P2B  P  N N 305 
NAP O1X  O  N N 306 
NAP O2X  O  N N 307 
NAP O3X  O  N N 308 
NAP HOA2 H  N N 309 
NAP H51A H  N N 310 
NAP H52A H  N N 311 
NAP H4B  H  N N 312 
NAP H3B  H  N N 313 
NAP HO3A H  N N 314 
NAP H2B  H  N N 315 
NAP H1B  H  N N 316 
NAP H8A  H  N N 317 
NAP H61A H  N N 318 
NAP H62A H  N N 319 
NAP H2A  H  N N 320 
NAP H51N H  N N 321 
NAP H52N H  N N 322 
NAP H4D  H  N N 323 
NAP H3D  H  N N 324 
NAP HO3N H  N N 325 
NAP H2D  H  N N 326 
NAP HO2N H  N N 327 
NAP H1D  H  N N 328 
NAP H2N  H  N N 329 
NAP H71N H  N N 330 
NAP H72N H  N N 331 
NAP H4N  H  N N 332 
NAP H5N  H  N N 333 
NAP H6N  H  N N 334 
NAP HOP2 H  N N 335 
NAP HOP3 H  N N 336 
PG4 O1   O  N N 337 
PG4 C1   C  N N 338 
PG4 C2   C  N N 339 
PG4 O2   O  N N 340 
PG4 C3   C  N N 341 
PG4 C4   C  N N 342 
PG4 O3   O  N N 343 
PG4 C5   C  N N 344 
PG4 C6   C  N N 345 
PG4 O4   O  N N 346 
PG4 C7   C  N N 347 
PG4 C8   C  N N 348 
PG4 O5   O  N N 349 
PG4 HO1  H  N N 350 
PG4 H11  H  N N 351 
PG4 H12  H  N N 352 
PG4 H21  H  N N 353 
PG4 H22  H  N N 354 
PG4 H31  H  N N 355 
PG4 H32  H  N N 356 
PG4 H41  H  N N 357 
PG4 H42  H  N N 358 
PG4 H51  H  N N 359 
PG4 H52  H  N N 360 
PG4 H61  H  N N 361 
PG4 H62  H  N N 362 
PG4 H71  H  N N 363 
PG4 H72  H  N N 364 
PG4 H81  H  N N 365 
PG4 H82  H  N N 366 
PG4 HO5  H  N N 367 
PHE N    N  N N 368 
PHE CA   C  N S 369 
PHE C    C  N N 370 
PHE O    O  N N 371 
PHE CB   C  N N 372 
PHE CG   C  Y N 373 
PHE CD1  C  Y N 374 
PHE CD2  C  Y N 375 
PHE CE1  C  Y N 376 
PHE CE2  C  Y N 377 
PHE CZ   C  Y N 378 
PHE OXT  O  N N 379 
PHE H    H  N N 380 
PHE H2   H  N N 381 
PHE HA   H  N N 382 
PHE HB2  H  N N 383 
PHE HB3  H  N N 384 
PHE HD1  H  N N 385 
PHE HD2  H  N N 386 
PHE HE1  H  N N 387 
PHE HE2  H  N N 388 
PHE HZ   H  N N 389 
PHE HXT  H  N N 390 
PRO N    N  N N 391 
PRO CA   C  N S 392 
PRO C    C  N N 393 
PRO O    O  N N 394 
PRO CB   C  N N 395 
PRO CG   C  N N 396 
PRO CD   C  N N 397 
PRO OXT  O  N N 398 
PRO H    H  N N 399 
PRO HA   H  N N 400 
PRO HB2  H  N N 401 
PRO HB3  H  N N 402 
PRO HG2  H  N N 403 
PRO HG3  H  N N 404 
PRO HD2  H  N N 405 
PRO HD3  H  N N 406 
PRO HXT  H  N N 407 
SER N    N  N N 408 
SER CA   C  N S 409 
SER C    C  N N 410 
SER O    O  N N 411 
SER CB   C  N N 412 
SER OG   O  N N 413 
SER OXT  O  N N 414 
SER H    H  N N 415 
SER H2   H  N N 416 
SER HA   H  N N 417 
SER HB2  H  N N 418 
SER HB3  H  N N 419 
SER HG   H  N N 420 
SER HXT  H  N N 421 
THR N    N  N N 422 
THR CA   C  N S 423 
THR C    C  N N 424 
THR O    O  N N 425 
THR CB   C  N R 426 
THR OG1  O  N N 427 
THR CG2  C  N N 428 
THR OXT  O  N N 429 
THR H    H  N N 430 
THR H2   H  N N 431 
THR HA   H  N N 432 
THR HB   H  N N 433 
THR HG1  H  N N 434 
THR HG21 H  N N 435 
THR HG22 H  N N 436 
THR HG23 H  N N 437 
THR HXT  H  N N 438 
TRP N    N  N N 439 
TRP CA   C  N S 440 
TRP C    C  N N 441 
TRP O    O  N N 442 
TRP CB   C  N N 443 
TRP CG   C  Y N 444 
TRP CD1  C  Y N 445 
TRP CD2  C  Y N 446 
TRP NE1  N  Y N 447 
TRP CE2  C  Y N 448 
TRP CE3  C  Y N 449 
TRP CZ2  C  Y N 450 
TRP CZ3  C  Y N 451 
TRP CH2  C  Y N 452 
TRP OXT  O  N N 453 
TRP H    H  N N 454 
TRP H2   H  N N 455 
TRP HA   H  N N 456 
TRP HB2  H  N N 457 
TRP HB3  H  N N 458 
TRP HD1  H  N N 459 
TRP HE1  H  N N 460 
TRP HE3  H  N N 461 
TRP HZ2  H  N N 462 
TRP HZ3  H  N N 463 
TRP HH2  H  N N 464 
TRP HXT  H  N N 465 
TYR N    N  N N 466 
TYR CA   C  N S 467 
TYR C    C  N N 468 
TYR O    O  N N 469 
TYR CB   C  N N 470 
TYR CG   C  Y N 471 
TYR CD1  C  Y N 472 
TYR CD2  C  Y N 473 
TYR CE1  C  Y N 474 
TYR CE2  C  Y N 475 
TYR CZ   C  Y N 476 
TYR OH   O  N N 477 
TYR OXT  O  N N 478 
TYR H    H  N N 479 
TYR H2   H  N N 480 
TYR HA   H  N N 481 
TYR HB2  H  N N 482 
TYR HB3  H  N N 483 
TYR HD1  H  N N 484 
TYR HD2  H  N N 485 
TYR HE1  H  N N 486 
TYR HE2  H  N N 487 
TYR HH   H  N N 488 
TYR HXT  H  N N 489 
VAL N    N  N N 490 
VAL CA   C  N S 491 
VAL C    C  N N 492 
VAL O    O  N N 493 
VAL CB   C  N N 494 
VAL CG1  C  N N 495 
VAL CG2  C  N N 496 
VAL OXT  O  N N 497 
VAL H    H  N N 498 
VAL H2   H  N N 499 
VAL HA   H  N N 500 
VAL HB   H  N N 501 
VAL HG11 H  N N 502 
VAL HG12 H  N N 503 
VAL HG13 H  N N 504 
VAL HG21 H  N N 505 
VAL HG22 H  N N 506 
VAL HG23 H  N N 507 
VAL HXT  H  N N 508 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
NAP PA  O1A  doub N N 246 
NAP PA  O2A  sing N N 247 
NAP PA  O5B  sing N N 248 
NAP PA  O3   sing N N 249 
NAP O2A HOA2 sing N N 250 
NAP O5B C5B  sing N N 251 
NAP C5B C4B  sing N N 252 
NAP C5B H51A sing N N 253 
NAP C5B H52A sing N N 254 
NAP C4B O4B  sing N N 255 
NAP C4B C3B  sing N N 256 
NAP C4B H4B  sing N N 257 
NAP O4B C1B  sing N N 258 
NAP C3B O3B  sing N N 259 
NAP C3B C2B  sing N N 260 
NAP C3B H3B  sing N N 261 
NAP O3B HO3A sing N N 262 
NAP C2B O2B  sing N N 263 
NAP C2B C1B  sing N N 264 
NAP C2B H2B  sing N N 265 
NAP O2B P2B  sing N N 266 
NAP C1B N9A  sing N N 267 
NAP C1B H1B  sing N N 268 
NAP N9A C8A  sing Y N 269 
NAP N9A C4A  sing Y N 270 
NAP C8A N7A  doub Y N 271 
NAP C8A H8A  sing N N 272 
NAP N7A C5A  sing Y N 273 
NAP C5A C6A  sing Y N 274 
NAP C5A C4A  doub Y N 275 
NAP C6A N6A  sing N N 276 
NAP C6A N1A  doub Y N 277 
NAP N6A H61A sing N N 278 
NAP N6A H62A sing N N 279 
NAP N1A C2A  sing Y N 280 
NAP C2A N3A  doub Y N 281 
NAP C2A H2A  sing N N 282 
NAP N3A C4A  sing Y N 283 
NAP O3  PN   sing N N 284 
NAP PN  O1N  doub N N 285 
NAP PN  O2N  sing N N 286 
NAP PN  O5D  sing N N 287 
NAP O5D C5D  sing N N 288 
NAP C5D C4D  sing N N 289 
NAP C5D H51N sing N N 290 
NAP C5D H52N sing N N 291 
NAP C4D O4D  sing N N 292 
NAP C4D C3D  sing N N 293 
NAP C4D H4D  sing N N 294 
NAP O4D C1D  sing N N 295 
NAP C3D O3D  sing N N 296 
NAP C3D C2D  sing N N 297 
NAP C3D H3D  sing N N 298 
NAP O3D HO3N sing N N 299 
NAP C2D O2D  sing N N 300 
NAP C2D C1D  sing N N 301 
NAP C2D H2D  sing N N 302 
NAP O2D HO2N sing N N 303 
NAP C1D N1N  sing N N 304 
NAP C1D H1D  sing N N 305 
NAP N1N C2N  sing Y N 306 
NAP N1N C6N  doub Y N 307 
NAP C2N C3N  doub Y N 308 
NAP C2N H2N  sing N N 309 
NAP C3N C7N  sing N N 310 
NAP C3N C4N  sing Y N 311 
NAP C7N O7N  doub N N 312 
NAP C7N N7N  sing N N 313 
NAP N7N H71N sing N N 314 
NAP N7N H72N sing N N 315 
NAP C4N C5N  doub Y N 316 
NAP C4N H4N  sing N N 317 
NAP C5N C6N  sing Y N 318 
NAP C5N H5N  sing N N 319 
NAP C6N H6N  sing N N 320 
NAP P2B O1X  doub N N 321 
NAP P2B O2X  sing N N 322 
NAP P2B O3X  sing N N 323 
NAP O2X HOP2 sing N N 324 
NAP O3X HOP3 sing N N 325 
PG4 O1  C1   sing N N 326 
PG4 O1  HO1  sing N N 327 
PG4 C1  C2   sing N N 328 
PG4 C1  H11  sing N N 329 
PG4 C1  H12  sing N N 330 
PG4 C2  O2   sing N N 331 
PG4 C2  H21  sing N N 332 
PG4 C2  H22  sing N N 333 
PG4 O2  C3   sing N N 334 
PG4 C3  C4   sing N N 335 
PG4 C3  H31  sing N N 336 
PG4 C3  H32  sing N N 337 
PG4 C4  O3   sing N N 338 
PG4 C4  H41  sing N N 339 
PG4 C4  H42  sing N N 340 
PG4 O3  C5   sing N N 341 
PG4 C5  C6   sing N N 342 
PG4 C5  H51  sing N N 343 
PG4 C5  H52  sing N N 344 
PG4 C6  O4   sing N N 345 
PG4 C6  H61  sing N N 346 
PG4 C6  H62  sing N N 347 
PG4 O4  C7   sing N N 348 
PG4 C7  C8   sing N N 349 
PG4 C7  H71  sing N N 350 
PG4 C7  H72  sing N N 351 
PG4 C8  O5   sing N N 352 
PG4 C8  H81  sing N N 353 
PG4 C8  H82  sing N N 354 
PG4 O5  HO5  sing N N 355 
PHE N   CA   sing N N 356 
PHE N   H    sing N N 357 
PHE N   H2   sing N N 358 
PHE CA  C    sing N N 359 
PHE CA  CB   sing N N 360 
PHE CA  HA   sing N N 361 
PHE C   O    doub N N 362 
PHE C   OXT  sing N N 363 
PHE CB  CG   sing N N 364 
PHE CB  HB2  sing N N 365 
PHE CB  HB3  sing N N 366 
PHE CG  CD1  doub Y N 367 
PHE CG  CD2  sing Y N 368 
PHE CD1 CE1  sing Y N 369 
PHE CD1 HD1  sing N N 370 
PHE CD2 CE2  doub Y N 371 
PHE CD2 HD2  sing N N 372 
PHE CE1 CZ   doub Y N 373 
PHE CE1 HE1  sing N N 374 
PHE CE2 CZ   sing Y N 375 
PHE CE2 HE2  sing N N 376 
PHE CZ  HZ   sing N N 377 
PHE OXT HXT  sing N N 378 
PRO N   CA   sing N N 379 
PRO N   CD   sing N N 380 
PRO N   H    sing N N 381 
PRO CA  C    sing N N 382 
PRO CA  CB   sing N N 383 
PRO CA  HA   sing N N 384 
PRO C   O    doub N N 385 
PRO C   OXT  sing N N 386 
PRO CB  CG   sing N N 387 
PRO CB  HB2  sing N N 388 
PRO CB  HB3  sing N N 389 
PRO CG  CD   sing N N 390 
PRO CG  HG2  sing N N 391 
PRO CG  HG3  sing N N 392 
PRO CD  HD2  sing N N 393 
PRO CD  HD3  sing N N 394 
PRO OXT HXT  sing N N 395 
SER N   CA   sing N N 396 
SER N   H    sing N N 397 
SER N   H2   sing N N 398 
SER CA  C    sing N N 399 
SER CA  CB   sing N N 400 
SER CA  HA   sing N N 401 
SER C   O    doub N N 402 
SER C   OXT  sing N N 403 
SER CB  OG   sing N N 404 
SER CB  HB2  sing N N 405 
SER CB  HB3  sing N N 406 
SER OG  HG   sing N N 407 
SER OXT HXT  sing N N 408 
THR N   CA   sing N N 409 
THR N   H    sing N N 410 
THR N   H2   sing N N 411 
THR CA  C    sing N N 412 
THR CA  CB   sing N N 413 
THR CA  HA   sing N N 414 
THR C   O    doub N N 415 
THR C   OXT  sing N N 416 
THR CB  OG1  sing N N 417 
THR CB  CG2  sing N N 418 
THR CB  HB   sing N N 419 
THR OG1 HG1  sing N N 420 
THR CG2 HG21 sing N N 421 
THR CG2 HG22 sing N N 422 
THR CG2 HG23 sing N N 423 
THR OXT HXT  sing N N 424 
TRP N   CA   sing N N 425 
TRP N   H    sing N N 426 
TRP N   H2   sing N N 427 
TRP CA  C    sing N N 428 
TRP CA  CB   sing N N 429 
TRP CA  HA   sing N N 430 
TRP C   O    doub N N 431 
TRP C   OXT  sing N N 432 
TRP CB  CG   sing N N 433 
TRP CB  HB2  sing N N 434 
TRP CB  HB3  sing N N 435 
TRP CG  CD1  doub Y N 436 
TRP CG  CD2  sing Y N 437 
TRP CD1 NE1  sing Y N 438 
TRP CD1 HD1  sing N N 439 
TRP CD2 CE2  doub Y N 440 
TRP CD2 CE3  sing Y N 441 
TRP NE1 CE2  sing Y N 442 
TRP NE1 HE1  sing N N 443 
TRP CE2 CZ2  sing Y N 444 
TRP CE3 CZ3  doub Y N 445 
TRP CE3 HE3  sing N N 446 
TRP CZ2 CH2  doub Y N 447 
TRP CZ2 HZ2  sing N N 448 
TRP CZ3 CH2  sing Y N 449 
TRP CZ3 HZ3  sing N N 450 
TRP CH2 HH2  sing N N 451 
TRP OXT HXT  sing N N 452 
TYR N   CA   sing N N 453 
TYR N   H    sing N N 454 
TYR N   H2   sing N N 455 
TYR CA  C    sing N N 456 
TYR CA  CB   sing N N 457 
TYR CA  HA   sing N N 458 
TYR C   O    doub N N 459 
TYR C   OXT  sing N N 460 
TYR CB  CG   sing N N 461 
TYR CB  HB2  sing N N 462 
TYR CB  HB3  sing N N 463 
TYR CG  CD1  doub Y N 464 
TYR CG  CD2  sing Y N 465 
TYR CD1 CE1  sing Y N 466 
TYR CD1 HD1  sing N N 467 
TYR CD2 CE2  doub Y N 468 
TYR CD2 HD2  sing N N 469 
TYR CE1 CZ   doub Y N 470 
TYR CE1 HE1  sing N N 471 
TYR CE2 CZ   sing Y N 472 
TYR CE2 HE2  sing N N 473 
TYR CZ  OH   sing N N 474 
TYR OH  HH   sing N N 475 
TYR OXT HXT  sing N N 476 
VAL N   CA   sing N N 477 
VAL N   H    sing N N 478 
VAL N   H2   sing N N 479 
VAL CA  C    sing N N 480 
VAL CA  CB   sing N N 481 
VAL CA  HA   sing N N 482 
VAL C   O    doub N N 483 
VAL C   OXT  sing N N 484 
VAL CB  CG1  sing N N 485 
VAL CB  CG2  sing N N 486 
VAL CB  HB   sing N N 487 
VAL CG1 HG11 sing N N 488 
VAL CG1 HG12 sing N N 489 
VAL CG1 HG13 sing N N 490 
VAL CG2 HG21 sing N N 491 
VAL CG2 HG22 sing N N 492 
VAL CG2 HG23 sing N N 493 
VAL OXT HXT  sing N N 494 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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   1ZK4 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZA3 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.017889 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012142 
_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]   0.008878 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   A SER A 1 1   ? -28.77900 -33.93900 -1.14700  0.522 35.88190 ? 1   SER A N   1 
ATOM   2    N  N   B SER A 1 1   ? -27.67000 -34.21600 -3.50500  0.478 34.89741 ? 1   SER A N   1 
ATOM   3    C  CA  A SER A 1 1   ? -28.75500 -34.19300 -2.58400  0.522 35.03832 ? 1   SER A CA  1 
ATOM   4    C  CA  B SER A 1 1   ? -28.78000 -34.39000 -2.57000  0.478 35.11745 ? 1   SER A CA  1 
ATOM   5    C  C   A SER A 1 1   ? -30.13600 -33.98000 -3.18900  0.522 34.04142 ? 1   SER A C   1 
ATOM   6    C  C   B SER A 1 1   ? -30.13700 -34.04400 -3.18500  0.478 34.06377 ? 1   SER A C   1 
ATOM   7    O  O   A SER A 1 1   ? -31.10600 -33.71400 -2.46900  0.522 34.45530 ? 1   SER A O   1 
ATOM   8    O  O   B SER A 1 1   ? -31.08900 -33.72700 -2.46400  0.478 34.45776 ? 1   SER A O   1 
ATOM   9    C  CB  A SER A 1 1   ? -28.26300 -35.61200 -2.88100  0.522 35.90452 ? 1   SER A CB  1 
ATOM   10   C  CB  B SER A 1 1   ? -28.55400 -33.53600 -1.32200  0.478 35.60974 ? 1   SER A CB  1 
ATOM   11   O  OG  A SER A 1 1   ? -26.88700 -35.74900 -2.57000  0.522 35.61024 ? 1   SER A OG  1 
ATOM   12   O  OG  B SER A 1 1   ? -28.02100 -32.27100 -1.66500  0.478 34.97880 ? 1   SER A OG  1 
ATOM   13   N  N   . ASN A 1 2   ? -30.21000 -34.08800 -4.51800  1.000 37.12645 ? 2   ASN A N   1 
ATOM   14   C  CA  . ASN A 1 2   ? -31.45300 -33.85100 -5.26000  1.000 32.04680 ? 2   ASN A CA  1 
ATOM   15   C  C   . ASN A 1 2   ? -32.07200 -32.48200 -4.96000  1.000 24.79962 ? 2   ASN A C   1 
ATOM   16   O  O   . ASN A 1 2   ? -33.29200 -32.31200 -5.02500  1.000 24.47829 ? 2   ASN A O   1 
ATOM   17   C  CB  . ASN A 1 2   ? -32.47000 -34.96200 -4.99600  1.000 37.47966 ? 2   ASN A CB  1 
ATOM   18   C  CG  . ASN A 1 2   ? -32.81300 -35.74200 -6.25000  1.000 44.66417 ? 2   ASN A CG  1 
ATOM   19   O  OD1 . ASN A 1 2   ? -33.00800 -35.16200 -7.32600  1.000 46.63649 ? 2   ASN A OD1 1 
ATOM   20   N  ND2 . ASN A 1 2   ? -32.89800 -37.06600 -6.12000  1.000 48.19176 ? 2   ASN A ND2 1 
ATOM   21   N  N   . ARG A 1 3   ? -31.24900 -31.47100 -4.67400  1.000 22.77545 ? 3   ARG A N   1 
ATOM   22   C  CA  . ARG A 1 3   ? -31.81600 -30.17900 -4.32100  1.000 19.16894 ? 3   ARG A CA  1 
ATOM   23   C  C   . ARG A 1 3   ? -32.47100 -29.48400 -5.50900  1.000 19.20683 ? 3   ARG A C   1 
ATOM   24   O  O   . ARG A 1 3   ? -33.24900 -28.54600 -5.29500  1.000 19.28103 ? 3   ARG A O   1 
ATOM   25   C  CB  . ARG A 1 3   ? -30.73300 -29.28100 -3.70500  1.000 19.35904 ? 3   ARG A CB  1 
ATOM   26   C  CG  . ARG A 1 3   ? -30.28200 -29.77500 -2.31900  1.000 19.20769 ? 3   ARG A CG  1 
ATOM   27   C  CD  . ARG A 1 3   ? -29.04000 -29.03600 -1.82700  1.000 19.48635 ? 3   ARG A CD  1 
ATOM   28   N  NE  . ARG A 1 3   ? -29.31500 -27.61900 -1.61200  1.000 18.41117 ? 3   ARG A NE  1 
ATOM   29   C  CZ  . ARG A 1 3   ? -28.40400 -26.65400 -1.69700  1.000 18.23631 ? 3   ARG A CZ  1 
ATOM   30   N  NH1 . ARG A 1 3   ? -27.13600 -26.94900 -1.97900  1.000 20.88048 ? 3   ARG A NH1 1 
ATOM   31   N  NH2 . ARG A 1 3   ? -28.75200 -25.39900 -1.48300  1.000 18.15898 ? 3   ARG A NH2 1 
ATOM   32   N  N   . LEU A 1 4   ? -32.20000 -29.94200 -6.74300  1.000 18.13009 ? 4   LEU A N   1 
ATOM   33   C  CA  . LEU A 1 4   ? -32.80800 -29.37200 -7.94100  1.000 18.93164 ? 4   LEU A CA  1 
ATOM   34   C  C   . LEU A 1 4   ? -33.60600 -30.43000 -8.70200  1.000 20.40665 ? 4   LEU A C   1 
ATOM   35   O  O   . LEU A 1 4   ? -33.69800 -30.39200 -9.93000  1.000 22.29697 ? 4   LEU A O   1 
ATOM   36   C  CB  . LEU A 1 4   ? -31.74300 -28.73400 -8.84100  1.000 18.32200 ? 4   LEU A CB  1 
ATOM   37   C  CG  . LEU A 1 4   ? -30.92500 -27.61800 -8.17200  1.000 18.36554 ? 4   LEU A CG  1 
ATOM   38   C  CD1 . LEU A 1 4   ? -29.88800 -27.10700 -9.13700  1.000 16.53565 ? 4   LEU A CD1 1 
ATOM   39   C  CD2 . LEU A 1 4   ? -31.83300 -26.46600 -7.73000  1.000 17.64426 ? 4   LEU A CD2 1 
ATOM   40   N  N   . ASP A 1 5   ? -34.18700 -31.37700 -7.97500  1.000 20.67884 ? 5   ASP A N   1 
ATOM   41   C  CA  . ASP A 1 5   ? -34.94200 -32.46300 -8.58300  1.000 23.92598 ? 5   ASP A CA  1 
ATOM   42   C  C   . ASP A 1 5   ? -35.98700 -31.94500 -9.57400  1.000 22.81012 ? 5   ASP A C   1 
ATOM   43   O  O   . ASP A 1 5   ? -36.77500 -31.04900 -9.26600  1.000 21.06353 ? 5   ASP A O   1 
ATOM   44   C  CB  . ASP A 1 5   ? -35.60300 -33.28000 -7.47000  1.000 29.05263 ? 5   ASP A CB  1 
ATOM   45   C  CG  . ASP A 1 5   ? -36.37300 -34.47700 -7.99700  1.000 36.09416 ? 5   ASP A CG  1 
ATOM   46   O  OD1 . ASP A 1 5   ? -35.74300 -35.41000 -8.54900  1.000 38.42885 ? 5   ASP A OD1 1 
ATOM   47   O  OD2 . ASP A 1 5   ? -37.60900 -34.48300 -7.83600  1.000 39.95614 ? 5   ASP A OD2 1 
ATOM   48   N  N   . GLY A 1 6   ? -35.95000 -32.48500 -10.79600 1.000 21.94720 ? 6   GLY A N   1 
ATOM   49   C  CA  . GLY A 1 6   ? -36.91500 -32.11800 -11.81600 1.000 20.69139 ? 6   GLY A CA  1 
ATOM   50   C  C   . GLY A 1 6   ? -36.66300 -30.80500 -12.53400 1.000 20.66114 ? 6   GLY A C   1 
ATOM   51   O  O   . GLY A 1 6   ? -37.33400 -30.53700 -13.53700 1.000 20.76293 ? 6   GLY A O   1 
ATOM   52   N  N   . LYS A 1 7   ? -35.70500 -29.98800 -12.08500 1.000 18.35943 ? 7   LYS A N   1 
ATOM   53   C  CA  . LYS A 1 7   ? -35.50300 -28.67500 -12.68400 1.000 17.17886 ? 7   LYS A CA  1 
ATOM   54   C  C   . LYS A 1 7   ? -34.82900 -28.80400 -14.04300 1.000 18.71155 ? 7   LYS A C   1 
ATOM   55   O  O   . LYS A 1 7   ? -34.04800 -29.72700 -14.29100 1.000 20.24480 ? 7   LYS A O   1 
ATOM   56   C  CB  . LYS A 1 7   ? -34.63100 -27.78300 -11.78800 1.000 16.63515 ? 7   LYS A CB  1 
ATOM   57   C  CG  . LYS A 1 7   ? -35.23600 -27.49800 -10.40200 1.000 18.69575 ? 7   LYS A CG  1 
ATOM   58   C  CD  . LYS A 1 7   ? -36.45600 -26.58300 -10.45900 1.000 18.10800 ? 7   LYS A CD  1 
ATOM   59   C  CE  . LYS A 1 7   ? -36.91100 -26.25200 -9.01700  1.000 18.83652 ? 7   LYS A CE  1 
ATOM   60   N  NZ  . LYS A 1 7   ? -38.18000 -25.42600 -8.98700  1.000 18.61853 ? 7   LYS A NZ  1 
ATOM   61   N  N   . VAL A 1 8   ? -35.13500 -27.85300 -14.92300 1.000 18.14930 ? 8   VAL A N   1 
ATOM   62   C  CA  . VAL A 1 8   ? -34.55000 -27.76700 -16.25500 1.000 18.01896 ? 8   VAL A CA  1 
ATOM   63   C  C   . VAL A 1 8   ? -33.95500 -26.37800 -16.37600 1.000 16.55810 ? 8   VAL A C   1 
ATOM   64   O  O   . VAL A 1 8   ? -34.68800 -25.38400 -16.29600 1.000 17.64867 ? 8   VAL A O   1 
ATOM   65   C  CB  . VAL A 1 8   ? -35.60100 -27.99400 -17.35900 1.000 17.37718 ? 8   VAL A CB  1 
ATOM   66   C  CG1 . VAL A 1 8   ? -34.97400 -27.74400 -18.73200 1.000 17.73882 ? 8   VAL A CG1 1 
ATOM   67   C  CG2 . VAL A 1 8   ? -36.19900 -29.39800 -17.26500 1.000 19.10962 ? 8   VAL A CG2 1 
ATOM   68   N  N   . ALA A 1 9   ? -32.63200 -26.28700 -16.55400 1.000 16.28609 ? 9   ALA A N   1 
ATOM   69   C  CA  . ALA A 1 9   ? -31.95000 -25.00700 -16.42400 1.000 15.65581 ? 9   ALA A CA  1 
ATOM   70   C  C   . ALA A 1 9   ? -31.20600 -24.62300 -17.69300 1.000 17.59233 ? 9   ALA A C   1 
ATOM   71   O  O   . ALA A 1 9   ? -30.56100 -25.46600 -18.30600 1.000 20.36403 ? 9   ALA A O   1 
ATOM   72   C  CB  . ALA A 1 9   ? -30.93100 -25.04700 -15.27000 1.000 15.31745 ? 9   ALA A CB  1 
ATOM   73   N  N   . ILE A 1 10  ? -31.26200 -23.34100 -18.05800 1.000 15.22369 ? 10  ILE A N   1 
ATOM   74   C  CA  . ILE A 1 10  ? -30.38200 -22.75200 -19.06600 1.000 15.36067 ? 10  ILE A CA  1 
ATOM   75   C  C   . ILE A 1 10  ? -29.34700 -21.91300 -18.32300 1.000 15.00518 ? 10  ILE A C   1 
ATOM   76   O  O   . ILE A 1 10  ? -29.70300 -21.10200 -17.45500 1.000 16.09941 ? 10  ILE A O   1 
ATOM   77   C  CB  . ILE A 1 10  ? -31.16900 -21.88500 -20.06000 1.000 15.54082 ? 10  ILE A CB  1 
ATOM   78   C  CG1 . ILE A 1 10  ? -32.07700 -22.78000 -20.92700 1.000 17.49112 ? 10  ILE A CG1 1 
ATOM   79   C  CG2 . ILE A 1 10  ? -30.20600 -21.09200 -20.96700 1.000 15.85872 ? 10  ILE A CG2 1 
ATOM   80   C  CD1 . ILE A 1 10  ? -33.08100 -22.00700 -21.80500 1.000 18.84700 ? 10  ILE A CD1 1 
ATOM   81   N  N   . ILE A 1 11  ? -28.06700 -22.10500 -18.64600 1.000 15.25964 ? 11  ILE A N   1 
ATOM   82   C  CA  . ILE A 1 11  ? -26.99300 -21.29600 -18.06900 1.000 14.57623 ? 11  ILE A CA  1 
ATOM   83   C  C   . ILE A 1 11  ? -26.21800 -20.67600 -19.22000 1.000 16.42286 ? 11  ILE A C   1 
ATOM   84   O  O   . ILE A 1 11  ? -25.57800 -21.40200 -19.99000 1.000 17.14684 ? 11  ILE A O   1 
ATOM   85   C  CB  . ILE A 1 11  ? -26.05600 -22.14900 -17.20400 1.000 14.68539 ? 11  ILE A CB  1 
ATOM   86   C  CG1 . ILE A 1 11  ? -26.84300 -22.81300 -16.07200 1.000 16.33158 ? 11  ILE A CG1 1 
ATOM   87   C  CG2 . ILE A 1 11  ? -24.89100 -21.30200 -16.64500 1.000 14.39278 ? 11  ILE A CG2 1 
ATOM   88   C  CD1 . ILE A 1 11  ? -26.06900 -23.94700 -15.37100 1.000 17.91075 ? 11  ILE A CD1 1 
ATOM   89   N  N   . THR A 1 12  ? -26.26900 -19.35100 -19.35200 1.000 16.31715 ? 12  THR A N   1 
ATOM   90   C  CA  . THR A 1 12  ? -25.50900 -18.72500 -20.43400 1.000 17.27415 ? 12  THR A CA  1 
ATOM   91   C  C   . THR A 1 12  ? -24.06200 -18.56200 -20.00800 1.000 17.56229 ? 12  THR A C   1 
ATOM   92   O  O   . THR A 1 12  ? -23.75600 -18.38200 -18.82600 1.000 15.94743 ? 12  THR A O   1 
ATOM   93   C  CB  . THR A 1 12  ? -26.09000 -17.36700 -20.84600 1.000 18.03603 ? 12  THR A CB  1 
ATOM   94   O  OG1 . THR A 1 12  ? -25.99200 -16.42700 -19.75500 1.000 16.62799 ? 12  THR A OG1 1 
ATOM   95   C  CG2 . THR A 1 12  ? -27.54000 -17.50600 -21.31700 1.000 17.74109 ? 12  THR A CG2 1 
ATOM   96   N  N   . GLY A 1 13  ? -23.15600 -18.67300 -20.98000 1.000 17.02464 ? 13  GLY A N   1 
ATOM   97   C  CA  . GLY A 1 13  ? -21.74900 -18.65600 -20.61300 1.000 18.16844 ? 13  GLY A CA  1 
ATOM   98   C  C   . GLY A 1 13  ? -21.41800 -19.77800 -19.65000 1.000 18.82718 ? 13  GLY A C   1 
ATOM   99   O  O   . GLY A 1 13  ? -20.73800 -19.56600 -18.63000 1.000 18.77293 ? 13  GLY A O   1 
ATOM   100  N  N   . GLY A 1 14  ? -21.90300 -20.97600 -19.95000 1.000 17.28908 ? 14  GLY A N   1 
ATOM   101  C  CA  . GLY A 1 14  ? -21.75300 -22.07500 -19.01000 1.000 18.80217 ? 14  GLY A CA  1 
ATOM   102  C  C   . GLY A 1 14  ? -20.65900 -23.04800 -19.38200 1.000 17.08956 ? 14  GLY A C   1 
ATOM   103  O  O   . GLY A 1 14  ? -20.63900 -24.17700 -18.87700 1.000 17.53245 ? 14  GLY A O   1 
ATOM   104  N  N   . THR A 1 15  ? -19.73800 -22.64200 -20.26500 1.000 18.80605 ? 15  THR A N   1 
ATOM   105  C  CA  . THR A 1 15  ? -18.78400 -23.59800 -20.81700 1.000 18.34402 ? 15  THR A CA  1 
ATOM   106  C  C   . THR A 1 15  ? -17.39500 -23.47300 -20.19400 1.000 18.90357 ? 15  THR A C   1 
ATOM   107  O  O   . THR A 1 15  ? -16.54800 -24.35000 -20.42500 1.000 20.71657 ? 15  THR A O   1 
ATOM   108  C  CB  . THR A 1 15  ? -18.69900 -23.47900 -22.35000 1.000 21.09111 ? 15  THR A CB  1 
ATOM   109  O  OG1 . THR A 1 15  ? -18.11900 -22.22800 -22.72200 1.000 20.85430 ? 15  THR A OG1 1 
ATOM   110  C  CG2 . THR A 1 15  ? -20.09500 -23.58700 -22.97800 1.000 19.86241 ? 15  THR A CG2 1 
ATOM   111  N  N   . LEU A 1 16  ? -17.18900 -22.46200 -19.35200 1.000 19.50097 ? 16  LEU A N   1 
ATOM   112  C  CA  . LEU A 1 16  ? -15.93100 -22.21200 -18.66700 1.000 21.32540 ? 16  LEU A CA  1 
ATOM   113  C  C   . LEU A 1 16  ? -16.20700 -21.52400 -17.33600 1.000 21.17650 ? 16  LEU A C   1 
ATOM   114  O  O   . LEU A 1 16  ? -17.24600 -20.87100 -17.14400 1.000 19.75694 ? 16  LEU A O   1 
ATOM   115  C  CB  . LEU A 1 16  ? -14.99500 -21.31200 -19.48300 1.000 25.18097 ? 16  LEU A CB  1 
ATOM   116  C  CG  . LEU A 1 16  ? -14.29000 -21.84800 -20.71600 1.000 32.39352 ? 16  LEU A CG  1 
ATOM   117  C  CD1 . LEU A 1 16  ? -13.63800 -20.67900 -21.42900 1.000 33.50801 ? 16  LEU A CD1 1 
ATOM   118  C  CD2 . LEU A 1 16  ? -13.25400 -22.89000 -20.32700 1.000 33.95686 ? 16  LEU A CD2 1 
ATOM   119  N  N   . GLY A 1 17  ? -15.24600 -21.66800 -16.42500 1.000 21.54610 ? 17  GLY A N   1 
ATOM   120  C  CA  . GLY A 1 17  ? -15.19500 -20.81600 -15.24700 1.000 18.88404 ? 17  GLY A CA  1 
ATOM   121  C  C   . GLY A 1 17  ? -16.43400 -20.95500 -14.37200 1.000 17.42108 ? 17  GLY A C   1 
ATOM   122  O  O   . GLY A 1 17  ? -16.89400 -22.06500 -14.08400 1.000 20.10334 ? 17  GLY A O   1 
ATOM   123  N  N   . ILE A 1 18  ? -16.96600 -19.80100 -13.96300 1.000 17.12223 ? 18  ILE A N   1 
ATOM   124  C  CA  . ILE A 1 18  ? -18.09900 -19.75400 -13.03600 1.000 17.44981 ? 18  ILE A CA  1 
ATOM   125  C  C   . ILE A 1 18  ? -19.30700 -20.48100 -13.61200 1.000 18.34158 ? 18  ILE A C   1 
ATOM   126  O  O   . ILE A 1 18  ? -19.93900 -21.29600 -12.93300 1.000 15.97799 ? 18  ILE A O   1 
ATOM   127  C  CB  . ILE A 1 18  ? -18.43400 -18.29500 -12.67800 1.000 17.79977 ? 18  ILE A CB  1 
ATOM   128  C  CG1 . ILE A 1 18  ? -17.33400 -17.71800 -11.76600 1.000 21.49831 ? 18  ILE A CG1 1 
ATOM   129  C  CG2 . ILE A 1 18  ? -19.83200 -18.17200 -12.04600 1.000 19.16707 ? 18  ILE A CG2 1 
ATOM   130  C  CD1 . ILE A 1 18  ? -17.47200 -16.22400 -11.56700 1.000 22.94019 ? 18  ILE A CD1 1 
ATOM   131  N  N   . GLY A 1 19  ? -19.66100 -20.18200 -14.86800 1.000 17.89780 ? 19  GLY A N   1 
ATOM   132  C  CA  . GLY A 1 19  ? -20.83100 -20.82400 -15.46900 1.000 16.77092 ? 19  GLY A CA  1 
ATOM   133  C  C   . GLY A 1 19  ? -20.71100 -22.33400 -15.53800 1.000 17.21468 ? 19  GLY A C   1 
ATOM   134  O  O   . GLY A 1 19  ? -21.69800 -23.05300 -15.34300 1.000 15.89058 ? 19  GLY A O   1 
ATOM   135  N  N   . LEU A 1 20  ? -19.50600 -22.83800 -15.83700 1.000 16.03826 ? 20  LEU A N   1 
ATOM   136  C  CA  . LEU A 1 20  ? -19.29700 -24.28600 -15.84400 1.000 17.68106 ? 20  LEU A CA  1 
ATOM   137  C  C   . LEU A 1 20  ? -19.45600 -24.89000 -14.44800 1.000 17.39212 ? 20  LEU A C   1 
ATOM   138  O  O   . LEU A 1 20  ? -19.99100 -25.99900 -14.30800 1.000 18.43079 ? 20  LEU A O   1 
ATOM   139  C  CB  . LEU A 1 20  ? -17.91900 -24.60800 -16.42700 1.000 19.41319 ? 20  LEU A CB  1 
ATOM   140  C  CG  . LEU A 1 20  ? -17.60400 -26.09400 -16.53300 1.000 22.23409 ? 20  LEU A CG  1 
ATOM   141  C  CD1 . LEU A 1 20  ? -18.62500 -26.81500 -17.42400 1.000 22.92479 ? 20  LEU A CD1 1 
ATOM   142  C  CD2 . LEU A 1 20  ? -16.19000 -26.26600 -17.06500 1.000 23.35611 ? 20  LEU A CD2 1 
ATOM   143  N  N   . ALA A 1 21  ? -18.94600 -24.21600 -13.40700 1.000 15.47245 ? 21  ALA A N   1 
ATOM   144  C  CA  . ALA A 1 21  ? -19.14900 -24.70800 -12.04700 1.000 15.45457 ? 21  ALA A CA  1 
ATOM   145  C  C   . ALA A 1 21  ? -20.63000 -24.74500 -11.68800 1.000 16.00755 ? 21  ALA A C   1 
ATOM   146  O  O   . ALA A 1 21  ? -21.10000 -25.69600 -11.05000 1.000 18.20053 ? 21  ALA A O   1 
ATOM   147  C  CB  . ALA A 1 21  ? -18.39200 -23.83600 -11.04300 1.000 15.39119 ? 21  ALA A CB  1 
ATOM   148  N  N   . ILE A 1 22  ? -21.36900 -23.70000 -12.05800 1.000 14.79996 ? 22  ILE A N   1 
ATOM   149  C  CA  . ILE A 1 22  ? -22.81000 -23.69800 -11.80800 1.000 15.17780 ? 22  ILE A CA  1 
ATOM   150  C  C   . ILE A 1 22  ? -23.44900 -24.89800 -12.48900 1.000 16.36538 ? 22  ILE A C   1 
ATOM   151  O  O   . ILE A 1 22  ? -24.27300 -25.61500 -11.90100 1.000 16.83284 ? 22  ILE A O   1 
ATOM   152  C  CB  . ILE A 1 22  ? -23.44000 -22.38100 -12.28900 1.000 15.53197 ? 22  ILE A CB  1 
ATOM   153  C  CG1 . ILE A 1 22  ? -22.89100 -21.16300 -11.53500 1.000 16.20467 ? 22  ILE A CG1 1 
ATOM   154  C  CG2 . ILE A 1 22  ? -24.98500 -22.43900 -12.11200 1.000 14.75033 ? 22  ILE A CG2 1 
ATOM   155  C  CD1 . ILE A 1 22  ? -23.30800 -19.83000 -12.18600 1.000 17.47841 ? 22  ILE A CD1 1 
ATOM   156  N  N   . ALA A 1 23  ? -23.09400 -25.12400 -13.75500 1.000 16.50015 ? 23  ALA A N   1 
ATOM   157  C  CA  . ALA A 1 23  ? -23.67900 -26.23800 -14.49300 1.000 17.19151 ? 23  ALA A CA  1 
ATOM   158  C  C   . ALA A 1 23  ? -23.33700 -27.56800 -13.84300 1.000 18.48400 ? 23  ALA A C   1 
ATOM   159  O  O   . ALA A 1 23  ? -24.19000 -28.45900 -13.74600 1.000 18.74779 ? 23  ALA A O   1 
ATOM   160  C  CB  . ALA A 1 23  ? -23.20200 -26.22300 -15.95200 1.000 17.17971 ? 23  ALA A CB  1 
ATOM   161  N  N   . THR A 1 24  ? -22.09300 -27.71300 -13.38000 1.000 17.68808 ? 24  THR A N   1 
ATOM   162  C  CA  . THR A 1 24  ? -21.66600 -28.96000 -12.75800 1.000 19.83989 ? 24  THR A CA  1 
ATOM   163  C  C   . THR A 1 24  ? -22.45600 -29.24800 -11.49200 1.000 19.23055 ? 24  THR A C   1 
ATOM   164  O  O   . THR A 1 24  ? -22.94400 -30.36400 -11.29700 1.000 19.39716 ? 24  THR A O   1 
ATOM   165  C  CB  . THR A 1 24  ? -20.17100 -28.90400 -12.45200 1.000 19.88654 ? 24  THR A CB  1 
ATOM   166  O  OG1 . THR A 1 24  ? -19.46900 -28.62300 -13.67000 1.000 21.21614 ? 24  THR A OG1 1 
ATOM   167  C  CG2 . THR A 1 24  ? -19.71400 -30.25700 -11.91400 1.000 19.51776 ? 24  THR A CG2 1 
ATOM   168  N  N   . LYS A 1 25  ? -22.57100 -28.25500 -10.60700 1.000 19.18806 ? 25  LYS A N   1 
ATOM   169  C  CA  . LYS A 1 25  ? -23.35000 -28.44600 -9.38700  1.000 19.31828 ? 25  LYS A CA  1 
ATOM   170  C  C   . LYS A 1 25  ? -24.83600 -28.61600 -9.68000  1.000 18.36706 ? 25  LYS A C   1 
ATOM   171  O  O   . LYS A 1 25  ? -25.51700 -29.36200 -8.97000  1.000 21.37210 ? 25  LYS A O   1 
ATOM   172  C  CB  . LYS A 1 25  ? -23.13500 -27.28600 -8.41800  1.000 18.47867 ? 25  LYS A CB  1 
ATOM   173  C  CG  . LYS A 1 25  ? -21.71500 -27.19200 -7.85600  1.000 22.98850 ? 25  LYS A CG  1 
ATOM   174  C  CD  . LYS A 1 25  ? -21.31400 -28.47500 -7.14400  1.000 26.57558 ? 25  LYS A CD  1 
ATOM   175  C  CE  . LYS A 1 25  ? -19.92100 -28.35100 -6.51800  1.000 29.58462 ? 25  LYS A CE  1 
ATOM   176  N  NZ  . LYS A 1 25  ? -19.43800 -29.67500 -5.98800  1.000 35.14930 ? 25  LYS A NZ  1 
ATOM   177  N  N   . PHE A 1 26  ? -25.36600 -27.92500 -10.69400 1.000 18.54865 ? 26  PHE A N   1 
ATOM   178  C  CA  . PHE A 1 26  ? -26.77300 -28.12400 -11.04800 1.000 17.44554 ? 26  PHE A CA  1 
ATOM   179  C  C   . PHE A 1 26  ? -27.04500 -29.57600 -11.43100 1.000 18.02049 ? 26  PHE A C   1 
ATOM   180  O  O   . PHE A 1 26  ? -28.03200 -30.17700 -10.98000 1.000 19.12245 ? 26  PHE A O   1 
ATOM   181  C  CB  . PHE A 1 26  ? -27.16000 -27.17300 -12.18300 1.000 17.39680 ? 26  PHE A CB  1 
ATOM   182  C  CG  . PHE A 1 26  ? -27.59900 -25.80400 -11.72100 1.000 16.85280 ? 26  PHE A CG  1 
ATOM   183  C  CD1 . PHE A 1 26  ? -27.13500 -25.25400 -10.51800 1.000 17.15414 ? 26  PHE A CD1 1 
ATOM   184  C  CD2 . PHE A 1 26  ? -28.47100 -25.04600 -12.49600 1.000 17.40173 ? 26  PHE A CD2 1 
ATOM   185  C  CE1 . PHE A 1 26  ? -27.51700 -23.99100 -10.11300 1.000 15.31513 ? 26  PHE A CE1 1 
ATOM   186  C  CE2 . PHE A 1 26  ? -28.88000 -23.78100 -12.08100 1.000 14.85289 ? 26  PHE A CE2 1 
ATOM   187  C  CZ  . PHE A 1 26  ? -28.40700 -23.25200 -10.88700 1.000 14.95323 ? 26  PHE A CZ  1 
ATOM   188  N  N   . VAL A 1 27  ? -26.18000 -30.15700 -12.26400 1.000 17.95983 ? 27  VAL A N   1 
ATOM   189  C  CA  . VAL A 1 27  ? -26.33300 -31.55800 -12.65500 1.000 19.29619 ? 27  VAL A CA  1 
ATOM   190  C  C   . VAL A 1 27  ? -26.19800 -32.46200 -11.43800 1.000 21.19637 ? 27  VAL A C   1 
ATOM   191  O  O   . VAL A 1 27  ? -26.97000 -33.41600 -11.26400 1.000 21.89252 ? 27  VAL A O   1 
ATOM   192  C  CB  . VAL A 1 27  ? -25.31700 -31.93000 -13.76100 1.000 21.21380 ? 27  VAL A CB  1 
ATOM   193  C  CG1 . VAL A 1 27  ? -25.30000 -33.43700 -14.00400 1.000 22.10048 ? 27  VAL A CG1 1 
ATOM   194  C  CG2 . VAL A 1 27  ? -25.63000 -31.19300 -15.07500 1.000 21.86319 ? 27  VAL A CG2 1 
ATOM   195  N  N   . GLU A 1 28  ? -25.21700 -32.17900 -10.57200 1.000 20.50829 ? 28  GLU A N   1 
ATOM   196  C  CA  . GLU A 1 28  ? -25.04600 -32.98100 -9.36400  1.000 21.04633 ? 28  GLU A CA  1 
ATOM   197  C  C   . GLU A 1 28  ? -26.29400 -32.97400 -8.49800  1.000 22.37690 ? 28  GLU A C   1 
ATOM   198  O  O   . GLU A 1 28  ? -26.58000 -33.95900 -7.81200  1.000 23.54809 ? 28  GLU A O   1 
ATOM   199  C  CB  . GLU A 1 28  ? -23.85600 -32.45300 -8.56300  1.000 28.18179 ? 28  GLU A CB  1 
ATOM   200  C  CG  . GLU A 1 28  ? -22.52900 -32.84800 -9.14300  1.000 35.93034 ? 28  GLU A CG  1 
ATOM   201  C  CD  . GLU A 1 28  ? -21.35000 -32.26000 -8.38300  1.000 41.57536 ? 28  GLU A CD  1 
ATOM   202  O  OE1 . GLU A 1 28  ? -20.22400 -32.30600 -8.93400  1.000 44.41782 ? 28  GLU A OE1 1 
ATOM   203  O  OE2 . GLU A 1 28  ? -21.54300 -31.76700 -7.24100  1.000 42.12451 ? 28  GLU A OE2 1 
ATOM   204  N  N   . GLU A 1 29  ? -27.03600 -31.87100 -8.49200  1.000 20.96462 ? 29  GLU A N   1 
ATOM   205  C  CA  . GLU A 1 29  ? -28.25100 -31.77900 -7.69300  1.000 22.24259 ? 29  GLU A CA  1 
ATOM   206  C  C   . GLU A 1 29  ? -29.50200 -32.18300 -8.46400  1.000 22.32308 ? 29  GLU A C   1 
ATOM   207  O  O   . GLU A 1 29  ? -30.61600 -31.92900 -7.99200  1.000 21.75680 ? 29  GLU A O   1 
ATOM   208  C  CB  . GLU A 1 29  ? -28.38600 -30.36300 -7.12800  1.000 21.90865 ? 29  GLU A CB  1 
ATOM   209  C  CG  . GLU A 1 29  ? -27.25600 -29.99200 -6.17600  1.000 23.34981 ? 29  GLU A CG  1 
ATOM   210  C  CD  . GLU A 1 29  ? -27.24800 -30.83500 -4.90400  1.000 24.89518 ? 29  GLU A CD  1 
ATOM   211  O  OE1 . GLU A 1 29  ? -28.30300 -31.39700 -4.53300  1.000 23.41526 ? 29  GLU A OE1 1 
ATOM   212  O  OE2 . GLU A 1 29  ? -26.17900 -30.92600 -4.26200  1.000 26.97711 ? 29  GLU A OE2 1 
ATOM   213  N  N   . GLY A 1 30  ? -29.35200 -32.81300 -9.63400  1.000 20.35154 ? 30  GLY A N   1 
ATOM   214  C  CA  . GLY A 1 30  ? -30.48100 -33.40700 -10.33400 1.000 20.50641 ? 30  GLY A CA  1 
ATOM   215  C  C   . GLY A 1 30  ? -31.12200 -32.56900 -11.42100 1.000 20.65293 ? 30  GLY A C   1 
ATOM   216  O  O   . GLY A 1 30  ? -32.11500 -33.01100 -12.01300 1.000 22.20861 ? 30  GLY A O   1 
ATOM   217  N  N   . ALA A 1 31  ? -30.59900 -31.38800 -11.71300 1.000 17.54927 ? 31  ALA A N   1 
ATOM   218  C  CA  . ALA A 1 31  ? -31.15700 -30.60500 -12.80300 1.000 17.29554 ? 31  ALA A CA  1 
ATOM   219  C  C   . ALA A 1 31  ? -30.69700 -31.12900 -14.16300 1.000 18.19617 ? 31  ALA A C   1 
ATOM   220  O  O   . ALA A 1 31  ? -29.61200 -31.70100 -14.30500 1.000 21.33080 ? 31  ALA A O   1 
ATOM   221  C  CB  . ALA A 1 31  ? -30.75600 -29.14200 -12.64200 1.000 17.57350 ? 31  ALA A CB  1 
ATOM   222  N  N   . LYS A 1 32  ? -31.52500 -30.90500 -15.18000 1.000 17.73709 ? 32  LYS A N   1 
ATOM   223  C  CA  . LYS A 1 32  ? -31.08800 -31.03600 -16.56300 1.000 17.99324 ? 32  LYS A CA  1 
ATOM   224  C  C   . LYS A 1 32  ? -30.65500 -29.65000 -17.02400 1.000 18.69392 ? 32  LYS A C   1 
ATOM   225  O  O   . LYS A 1 32  ? -31.28600 -28.65700 -16.66200 1.000 20.80531 ? 32  LYS A O   1 
ATOM   226  C  CB  . LYS A 1 32  ? -32.21400 -31.58600 -17.43400 1.000 19.93216 ? 32  LYS A CB  1 
ATOM   227  C  CG  . LYS A 1 32  ? -32.51700 -33.07200 -17.13900 1.000 25.19434 ? 32  LYS A CG  1 
ATOM   228  C  CD  . LYS A 1 32  ? -33.76100 -33.56500 -17.89300 1.000 31.65794 ? 32  LYS A CD  1 
ATOM   229  C  CE  . LYS A 1 32  ? -35.05200 -33.15700 -17.17400 1.000 35.14880 ? 32  LYS A CE  1 
ATOM   230  N  NZ  . LYS A 1 32  ? -35.36200 -34.00000 -15.97000 1.000 36.40798 ? 32  LYS A NZ  1 
ATOM   231  N  N   . VAL A 1 33  ? -29.54400 -29.57000 -17.76800 1.000 19.03779 ? 33  VAL A N   1 
ATOM   232  C  CA  . VAL A 1 33  ? -28.87100 -28.29300 -18.00100 1.000 18.13326 ? 33  VAL A CA  1 
ATOM   233  C  C   . VAL A 1 33  ? -28.55600 -28.11800 -19.48000 1.000 18.32274 ? 33  VAL A C   1 
ATOM   234  O  O   . VAL A 1 33  ? -27.98000 -29.01200 -20.10100 1.000 18.72937 ? 33  VAL A O   1 
ATOM   235  C  CB  . VAL A 1 33  ? -27.56200 -28.18300 -17.19100 1.000 17.25980 ? 33  VAL A CB  1 
ATOM   236  C  CG1 . VAL A 1 33  ? -26.80600 -26.89700 -17.56600 1.000 18.92389 ? 33  VAL A CG1 1 
ATOM   237  C  CG2 . VAL A 1 33  ? -27.84600 -28.24700 -15.67500 1.000 17.45423 ? 33  VAL A CG2 1 
ATOM   238  N  N   . MET A 1 34  ? -28.89000 -26.95200 -20.02900 1.000 17.57455 ? 34  MET A N   1 
ATOM   239  C  CA  . MET A 1 34  ? -28.36500 -26.51100 -21.31900 1.000 17.80250 ? 34  MET A CA  1 
ATOM   240  C  C   . MET A 1 34  ? -27.39600 -25.36100 -21.06100 1.000 17.26352 ? 34  MET A C   1 
ATOM   241  O  O   . MET A 1 34  ? -27.80500 -24.31800 -20.55000 1.000 16.61611 ? 34  MET A O   1 
ATOM   242  C  CB  . MET A 1 34  ? -29.49300 -26.06500 -22.26100 1.000 18.91465 ? 34  MET A CB  1 
ATOM   243  C  CG  . MET A 1 34  ? -29.00900 -25.74900 -23.69100 1.000 17.45070 ? 34  MET A CG  1 
ATOM   244  S  SD  . MET A 1 34  ? -28.57500 -27.22500 -24.62400 1.000 18.30910 ? 34  MET A SD  1 
ATOM   245  C  CE  . MET A 1 34  ? -30.21700 -27.90100 -24.92200 1.000 18.67832 ? 34  MET A CE  1 
ATOM   246  N  N   . ILE A 1 35  ? -26.11000 -25.55700 -21.39000 1.000 17.85832 ? 35  ILE A N   1 
ATOM   247  C  CA  . ILE A 1 35  ? -25.10100 -24.50800 -21.26800 1.000 17.62308 ? 35  ILE A CA  1 
ATOM   248  C  C   . ILE A 1 35  ? -24.90000 -23.84400 -22.62200 1.000 17.38149 ? 35  ILE A C   1 
ATOM   249  O  O   . ILE A 1 35  ? -24.99200 -24.49400 -23.66900 1.000 18.04241 ? 35  ILE A O   1 
ATOM   250  C  CB  . ILE A 1 35  ? -23.75600 -25.06200 -20.73600 1.000 16.99260 ? 35  ILE A CB  1 
ATOM   251  C  CG1 . ILE A 1 35  ? -23.17300 -26.15800 -21.62900 1.000 18.80658 ? 35  ILE A CG1 1 
ATOM   252  C  CG2 . ILE A 1 35  ? -23.92300 -25.54900 -19.30700 1.000 16.40811 ? 35  ILE A CG2 1 
ATOM   253  C  CD1 . ILE A 1 35  ? -21.84900 -26.73900 -21.11100 1.000 18.66876 ? 35  ILE A CD1 1 
ATOM   254  N  N   . THR A 1 36  ? -24.59600 -22.54400 -22.61000 1.000 17.68926 ? 36  THR A N   1 
ATOM   255  C  CA  . THR A 1 36  ? -24.28200 -21.81700 -23.84400 1.000 18.10666 ? 36  THR A CA  1 
ATOM   256  C  C   . THR A 1 36  ? -22.90500 -21.16700 -23.80400 1.000 17.64815 ? 36  THR A C   1 
ATOM   257  O  O   . THR A 1 36  ? -22.30800 -20.96200 -22.74300 1.000 17.94151 ? 36  THR A O   1 
ATOM   258  C  CB  . THR A 1 36  ? -25.29100 -20.70000 -24.16500 1.000 19.19629 ? 36  THR A CB  1 
ATOM   259  O  OG1 . THR A 1 36  ? -25.01300 -19.55800 -23.35000 1.000 16.55077 ? 36  THR A OG1 1 
ATOM   260  C  CG2 . THR A 1 36  ? -26.73100 -21.15600 -23.93000 1.000 19.19307 ? 36  THR A CG2 1 
ATOM   261  N  N   . GLY A 1 37  ? -22.44900 -20.82000 -25.00000 1.000 17.74089 ? 37  GLY A N   1 
ATOM   262  C  CA  . GLY A 1 37  ? -21.23000 -20.06000 -25.24400 1.000 16.74862 ? 37  GLY A CA  1 
ATOM   263  C  C   . GLY A 1 37  ? -21.13100 -19.88300 -26.74300 1.000 17.82384 ? 37  GLY A C   1 
ATOM   264  O  O   . GLY A 1 37  ? -21.90000 -20.48100 -27.50600 1.000 18.49229 ? 37  GLY A O   1 
ATOM   265  N  N   . ARG A 1 38  ? -20.14300 -19.07800 -27.16200 1.000 17.78505 ? 38  ARG A N   1 
ATOM   266  C  CA  . ARG A 1 38  ? -20.00200 -18.76800 -28.58500 1.000 20.20794 ? 38  ARG A CA  1 
ATOM   267  C  C   . ARG A 1 38  ? -19.20800 -19.81900 -29.34100 1.000 21.20674 ? 38  ARG A C   1 
ATOM   268  O  O   . ARG A 1 38  ? -19.41900 -19.99000 -30.54900 1.000 22.35984 ? 38  ARG A O   1 
ATOM   269  C  CB  . ARG A 1 38  ? -19.34400 -17.39900 -28.74900 1.000 22.23709 ? 38  ARG A CB  1 
ATOM   270  C  CG  . ARG A 1 38  ? -20.12900 -16.28500 -28.11000 1.000 24.22444 ? 38  ARG A CG  1 
ATOM   271  C  CD  . ARG A 1 38  ? -19.29200 -15.01400 -27.96300 1.000 27.43212 ? 38  ARG A CD  1 
ATOM   272  N  NE  . ARG A 1 38  ? -18.11800 -15.25800 -27.13700 1.000 26.79817 ? 38  ARG A NE  1 
ATOM   273  C  CZ  . ARG A 1 38  ? -16.95200 -14.62800 -27.26600 1.000 30.42411 ? 38  ARG A CZ  1 
ATOM   274  N  NH1 . ARG A 1 38  ? -16.77800 -13.70000 -28.19900 1.000 32.49566 ? 38  ARG A NH1 1 
ATOM   275  N  NH2 . ARG A 1 38  ? -15.94700 -14.93800 -26.46700 1.000 31.93278 ? 38  ARG A NH2 1 
ATOM   276  N  N   . HIS A 1 39  ? -18.30500 -20.52800 -28.67500 1.000 19.90610 ? 39  HIS A N   1 
ATOM   277  C  CA  . HIS A 1 39  ? -17.41000 -21.46200 -29.34500 1.000 20.71121 ? 39  HIS A CA  1 
ATOM   278  C  C   . HIS A 1 39  ? -17.81500 -22.90000 -29.07200 1.000 22.16985 ? 39  HIS A C   1 
ATOM   279  O  O   . HIS A 1 39  ? -17.84200 -23.33200 -27.90800 1.000 23.14330 ? 39  HIS A O   1 
ATOM   280  C  CB  . HIS A 1 39  ? -15.96800 -21.23600 -28.89600 1.000 21.07168 ? 39  HIS A CB  1 
ATOM   281  C  CG  . HIS A 1 39  ? -15.49500 -19.83700 -29.09500 1.000 25.05336 ? 39  HIS A CG  1 
ATOM   282  N  ND1 . HIS A 1 39  ? -15.46200 -18.91600 -28.07200 1.000 27.29688 ? 39  HIS A ND1 1 
ATOM   283  C  CD2 . HIS A 1 39  ? -15.03000 -19.19800 -30.19500 1.000 26.68299 ? 39  HIS A CD2 1 
ATOM   284  C  CE1 . HIS A 1 39  ? -14.98300 -17.77200 -28.52900 1.000 27.46571 ? 39  HIS A CE1 1 
ATOM   285  N  NE2 . HIS A 1 39  ? -14.70600 -17.91800 -29.81200 1.000 27.44342 ? 39  HIS A NE2 1 
ATOM   286  N  N   . SER A 1 40  ? -18.06300 -23.65000 -30.15300 1.000 24.12890 ? 40  SER A N   1 
ATOM   287  C  CA  . SER A 1 40  ? -18.57700 -25.00500 -30.01800 1.000 24.47899 ? 40  SER A CA  1 
ATOM   288  C  C   . SER A 1 40  ? -17.50600 -25.96500 -29.54700 1.000 23.12378 ? 40  SER A C   1 
ATOM   289  O  O   . SER A 1 40  ? -17.82600 -26.95900 -28.88800 1.000 25.07419 ? 40  SER A O   1 
ATOM   290  C  CB  . SER A 1 40  ? -19.17800 -25.48900 -31.34200 1.000 25.55526 ? 40  SER A CB  1 
ATOM   291  O  OG  . SER A 1 40  ? -18.17800 -25.55400 -32.34200 1.000 27.36716 ? 40  SER A OG  1 
ATOM   292  N  N   . ASP A 1 41  ? -16.23500 -25.70000 -29.87000 1.000 24.02253 ? 41  ASP A N   1 
ATOM   293  C  CA  . ASP A 1 41  ? -15.17100 -26.55100 -29.36500 1.000 24.76151 ? 41  ASP A CA  1 
ATOM   294  C  C   . ASP A 1 41  ? -15.18400 -26.58600 -27.84100 1.000 24.76698 ? 41  ASP A C   1 
ATOM   295  O  O   . ASP A 1 41  ? -15.13800 -27.66400 -27.23700 1.000 27.45798 ? 41  ASP A O   1 
ATOM   296  C  CB  . ASP A 1 41  ? -13.81900 -26.06200 -29.88900 1.000 23.00201 ? 41  ASP A CB  1 
ATOM   297  C  CG  . ASP A 1 41  ? -13.61900 -24.57000 -29.65600 1.000 23.58523 ? 41  ASP A CG  1 
ATOM   298  O  OD1 . ASP A 1 41  ? -14.25900 -23.75200 -30.35100 1.000 23.29972 ? 41  ASP A OD1 1 
ATOM   299  O  OD2 . ASP A 1 41  ? -12.80800 -24.20800 -28.78200 1.000 24.25980 ? 41  ASP A OD2 1 
ATOM   300  N  N   . VAL A 1 42  ? -15.26000 -25.41300 -27.20500 1.000 22.45224 ? 42  VAL A N   1 
ATOM   301  C  CA  . VAL A 1 42  ? -15.28000 -25.35500 -25.74800 1.000 22.38607 ? 42  VAL A CA  1 
ATOM   302  C  C   . VAL A 1 42  ? -16.57100 -25.96300 -25.22900 1.000 21.69472 ? 42  VAL A C   1 
ATOM   303  O  O   . VAL A 1 42  ? -16.57600 -26.71900 -24.24600 1.000 22.23015 ? 42  VAL A O   1 
ATOM   304  C  CB  . VAL A 1 42  ? -15.11000 -23.89400 -25.27400 1.000 22.44304 ? 42  VAL A CB  1 
ATOM   305  C  CG1 . VAL A 1 42  ? -15.08000 -23.79200 -23.73800 1.000 24.03429 ? 42  VAL A CG1 1 
ATOM   306  C  CG2 . VAL A 1 42  ? -13.85200 -23.28100 -25.87500 1.000 23.80068 ? 42  VAL A CG2 1 
ATOM   307  N  N   . GLY A 1 43  ? -17.68200 -25.64700 -25.89000 1.000 21.44505 ? 43  GLY A N   1 
ATOM   308  C  CA  . GLY A 1 43  ? -18.97800 -26.00500 -25.34000 1.000 22.03743 ? 43  GLY A CA  1 
ATOM   309  C  C   . GLY A 1 43  ? -19.24600 -27.49400 -25.37400 1.000 22.20606 ? 43  GLY A C   1 
ATOM   310  O  O   . GLY A 1 43  ? -19.77900 -28.05700 -24.41400 1.000 22.61213 ? 43  GLY A O   1 
ATOM   311  N  N   . GLU A 1 44  ? -18.91000 -28.15600 -26.47900 1.000 23.86540 ? 44  GLU A N   1 
ATOM   312  C  CA  . GLU A 1 44  ? -19.19800 -29.58300 -26.52000 1.000 24.97038 ? 44  GLU A CA  1 
ATOM   313  C  C   . GLU A 1 44  ? -18.28700 -30.35000 -25.57100 1.000 25.72259 ? 44  GLU A C   1 
ATOM   314  O  O   . GLU A 1 44  ? -18.71800 -31.31900 -24.94500 1.000 25.49686 ? 44  GLU A O   1 
ATOM   315  C  CB  . GLU A 1 44  ? -19.07600 -30.11000 -27.95100 1.000 27.74700 ? 44  GLU A CB  1 
ATOM   316  C  CG  . GLU A 1 44  ? -20.00500 -29.45100 -28.95600 1.000 29.94197 ? 44  GLU A CG  1 
ATOM   317  C  CD  . GLU A 1 44  ? -21.47900 -29.83900 -28.77900 1.000 33.03074 ? 44  GLU A CD  1 
ATOM   318  O  OE1 . GLU A 1 44  ? -21.80700 -30.57900 -27.82700 1.000 33.47876 ? 44  GLU A OE1 1 
ATOM   319  O  OE2 . GLU A 1 44  ? -22.31100 -29.39800 -29.60500 1.000 34.71600 ? 44  GLU A OE2 1 
ATOM   320  N  N   . LYS A 1 45  ? -17.04200 -29.90700 -25.41200 1.000 24.79226 ? 45  LYS A N   1 
ATOM   321  C  CA  . LYS A 1 45  ? -16.18000 -30.55900 -24.43700 1.000 25.81476 ? 45  LYS A CA  1 
ATOM   322  C  C   . LYS A 1 45  ? -16.68300 -30.33100 -23.01900 1.000 23.99744 ? 45  LYS A C   1 
ATOM   323  O  O   . LYS A 1 45  ? -16.63800 -31.24300 -22.18600 1.000 25.91131 ? 45  LYS A O   1 
ATOM   324  C  CB  . LYS A 1 45  ? -14.74400 -30.06000 -24.58200 1.000 31.19345 ? 45  LYS A CB  1 
ATOM   325  C  CG  . LYS A 1 45  ? -13.72800 -31.06200 -24.07000 1.000 36.95136 ? 45  LYS A CG  1 
ATOM   326  C  CD  . LYS A 1 45  ? -12.30300 -30.55400 -24.21400 1.000 39.11366 ? 45  LYS A CD  1 
ATOM   327  C  CE  . LYS A 1 45  ? -12.05500 -30.05300 -25.62800 1.000 38.80179 ? 45  LYS A CE  1 
ATOM   328  N  NZ  . LYS A 1 45  ? -10.82700 -30.68400 -26.27100 1.000 39.60279 ? 45  LYS A NZ  1 
ATOM   329  N  N   . ALA A 1 46  ? -17.16200 -29.12100 -22.72500 1.000 22.40969 ? 46  ALA A N   1 
ATOM   330  C  CA  . ALA A 1 46  ? -17.64800 -28.83600 -21.37800 1.000 21.80114 ? 46  ALA A CA  1 
ATOM   331  C  C   . ALA A 1 46  ? -18.83700 -29.72600 -21.03400 1.000 22.82658 ? 46  ALA A C   1 
ATOM   332  O  O   . ALA A 1 46  ? -18.86900 -30.34600 -19.96500 1.000 24.75586 ? 46  ALA A O   1 
ATOM   333  C  CB  . ALA A 1 46  ? -18.00600 -27.35800 -21.24600 1.000 20.74043 ? 46  ALA A CB  1 
ATOM   334  N  N   . ALA A 1 47  ? -19.81500 -29.82700 -21.94300 1.000 23.03641 ? 47  ALA A N   1 
ATOM   335  C  CA  . ALA A 1 47  ? -20.98000 -30.66400 -21.66400 1.000 23.41659 ? 47  ALA A CA  1 
ATOM   336  C  C   . ALA A 1 47  ? -20.56600 -32.10200 -21.38500 1.000 26.00553 ? 47  ALA A C   1 
ATOM   337  O  O   . ALA A 1 47  ? -20.96300 -32.68500 -20.37100 1.000 26.05643 ? 47  ALA A O   1 
ATOM   338  C  CB  . ALA A 1 47  ? -21.97200 -30.61100 -22.83000 1.000 23.99050 ? 47  ALA A CB  1 
ATOM   339  N  N   . LYS A 1 48  ? -19.72400 -32.67200 -22.25800 1.000 26.11318 ? 48  LYS A N   1 
ATOM   340  C  CA  . LYS A 1 48  ? -19.28100 -34.05700 -22.10800 1.000 28.03619 ? 48  LYS A CA  1 
ATOM   341  C  C   . LYS A 1 48  ? -18.51300 -34.27400 -20.81600 1.000 27.53840 ? 48  LYS A C   1 
ATOM   342  O  O   . LYS A 1 48  ? -18.54600 -35.37400 -20.25200 1.000 28.98145 ? 48  LYS A O   1 
ATOM   343  C  CB  . LYS A 1 48  ? -18.39100 -34.45100 -23.28600 1.000 31.86931 ? 48  LYS A CB  1 
ATOM   344  C  CG  . LYS A 1 48  ? -19.11300 -34.71800 -24.59500 1.000 35.79034 ? 48  LYS A CG  1 
ATOM   345  C  CD  . LYS A 1 48  ? -18.09100 -35.11800 -25.67600 1.000 39.14482 ? 48  LYS A CD  1 
ATOM   346  C  CE  . LYS A 1 48  ? -18.74000 -35.83300 -26.86000 1.000 41.87162 ? 48  LYS A CE  1 
ATOM   347  N  NZ  . LYS A 1 48  ? -18.24700 -37.23400 -27.01500 1.000 42.73567 ? 48  LYS A NZ  1 
ATOM   348  N  N   . SER A 1 49  ? -17.79200 -33.25600 -20.35400 1.000 26.62226 ? 49  SER A N   1 
ATOM   349  C  CA  . SER A 1 49  ? -17.02200 -33.38100 -19.12500 1.000 28.33130 ? 49  SER A CA  1 
ATOM   350  C  C   . SER A 1 49  ? -17.91100 -33.44600 -17.88700 1.000 28.28514 ? 49  SER A C   1 
ATOM   351  O  O   . SER A 1 49  ? -17.44600 -33.90300 -16.83800 1.000 29.63234 ? 49  SER A O   1 
ATOM   352  C  CB  . SER A 1 49  ? -16.03300 -32.21200 -18.99900 1.000 27.82630 ? 49  SER A CB  1 
ATOM   353  O  OG  . SER A 1 49  ? -16.68400 -31.01900 -18.59400 1.000 28.54475 ? 49  SER A OG  1 
ATOM   354  N  N   . VAL A 1 50  ? -19.16400 -33.00900 -17.98100 1.000 26.14231 ? 50  VAL A N   1 
ATOM   355  C  CA  . VAL A 1 50  ? -20.05700 -32.94400 -16.83100 1.000 24.11604 ? 50  VAL A CA  1 
ATOM   356  C  C   . VAL A 1 50  ? -20.99900 -34.14500 -16.76800 1.000 26.65199 ? 50  VAL A C   1 
ATOM   357  O  O   . VAL A 1 50  ? -21.20500 -34.71200 -15.69500 1.000 29.14915 ? 50  VAL A O   1 
ATOM   358  C  CB  . VAL A 1 50  ? -20.84300 -31.61400 -16.84400 1.000 23.94745 ? 50  VAL A CB  1 
ATOM   359  C  CG1 . VAL A 1 50  ? -21.96000 -31.62700 -15.80900 1.000 22.07356 ? 50  VAL A CG1 1 
ATOM   360  C  CG2 . VAL A 1 50  ? -19.90300 -30.45200 -16.58400 1.000 23.96314 ? 50  VAL A CG2 1 
ATOM   361  N  N   . GLY A 1 51  ? -21.58100 -34.55300 -17.89000 1.000 25.40396 ? 51  GLY A N   1 
ATOM   362  C  CA  . GLY A 1 51  ? -22.52100 -35.65800 -17.86600 1.000 24.84031 ? 51  GLY A CA  1 
ATOM   363  C  C   . GLY A 1 51  ? -22.87800 -36.09000 -19.27000 1.000 26.59512 ? 51  GLY A C   1 
ATOM   364  O  O   . GLY A 1 51  ? -22.27600 -35.63800 -20.24600 1.000 26.77904 ? 51  GLY A O   1 
ATOM   365  N  N   . THR A 1 52  ? -23.86800 -36.97800 -19.36100 1.000 27.12472 ? 52  THR A N   1 
ATOM   366  C  CA  . THR A 1 52  ? -24.36300 -37.46800 -20.64000 1.000 27.62804 ? 52  THR A CA  1 
ATOM   367  C  C   . THR A 1 52  ? -25.34900 -36.47300 -21.24100 1.000 26.14342 ? 52  THR A C   1 
ATOM   368  O  O   . THR A 1 52  ? -25.81600 -35.54900 -20.57200 1.000 24.21813 ? 52  THR A O   1 
ATOM   369  C  CB  . THR A 1 52  ? -25.03700 -38.82900 -20.45700 1.000 31.58026 ? 52  THR A CB  1 
ATOM   370  O  OG1 . THR A 1 52  ? -26.23200 -38.66600 -19.69300 1.000 33.34028 ? 52  THR A OG1 1 
ATOM   371  C  CG2 . THR A 1 52  ? -24.12400 -39.80900 -19.74500 1.000 32.35349 ? 52  THR A CG2 1 
ATOM   372  N  N   . PRO A 1 53  ? -25.69900 -36.63000 -22.51900 1.000 26.09894 ? 53  PRO A N   1 
ATOM   373  C  CA  . PRO A 1 53  ? -26.70700 -35.73800 -23.10900 1.000 24.13773 ? 53  PRO A CA  1 
ATOM   374  C  C   . PRO A 1 53  ? -28.06100 -35.80200 -22.41300 1.000 26.03676 ? 53  PRO A C   1 
ATOM   375  O  O   . PRO A 1 53  ? -28.85000 -34.86600 -22.54900 1.000 25.40064 ? 53  PRO A O   1 
ATOM   376  C  CB  . PRO A 1 53  ? -26.79000 -36.22300 -24.56300 1.000 27.08347 ? 53  PRO A CB  1 
ATOM   377  C  CG  . PRO A 1 53  ? -25.47600 -36.85900 -24.81000 1.000 27.69648 ? 53  PRO A CG  1 
ATOM   378  C  CD  . PRO A 1 53  ? -25.08400 -37.50200 -23.53500 1.000 26.97410 ? 53  PRO A CD  1 
ATOM   379  N  N   . ASP A 1 54  ? -28.35700 -36.87600 -21.67500 1.000 27.21406 ? 54  ASP A N   1 
ATOM   380  C  CA  . ASP A 1 54  ? -29.58500 -36.93500 -20.88700 1.000 31.00961 ? 54  ASP A CA  1 
ATOM   381  C  C   . ASP A 1 54  ? -29.56600 -35.97500 -19.70800 1.000 28.94409 ? 54  ASP A C   1 
ATOM   382  O  O   . ASP A 1 54  ? -30.63200 -35.67400 -19.15100 1.000 28.02765 ? 54  ASP A O   1 
ATOM   383  C  CB  . ASP A 1 54  ? -29.81900 -38.35600 -20.36800 1.000 37.08267 ? 54  ASP A CB  1 
ATOM   384  C  CG  . ASP A 1 54  ? -30.10300 -39.34500 -21.48100 1.000 44.65803 ? 54  ASP A CG  1 
ATOM   385  O  OD1 . ASP A 1 54  ? -30.93500 -39.02700 -22.36400 1.000 47.75304 ? 54  ASP A OD1 1 
ATOM   386  O  OD2 . ASP A 1 54  ? -29.48800 -40.43600 -21.48100 1.000 47.81410 ? 54  ASP A OD2 1 
ATOM   387  N  N   . GLN A 1 55  ? -28.38700 -35.49900 -19.30900 1.000 28.06689 ? 55  GLN A N   1 
ATOM   388  C  CA  . GLN A 1 55  ? -28.22100 -34.58000 -18.19300 1.000 25.47032 ? 55  GLN A CA  1 
ATOM   389  C  C   . GLN A 1 55  ? -27.86900 -33.17200 -18.63200 1.000 22.42322 ? 55  GLN A C   1 
ATOM   390  O  O   . GLN A 1 55  ? -28.31900 -32.20600 -18.01700 1.000 19.57525 ? 55  GLN A O   1 
ATOM   391  C  CB  . GLN A 1 55  ? -27.10900 -35.07500 -17.25700 1.000 25.59553 ? 55  GLN A CB  1 
ATOM   392  C  CG  . GLN A 1 55  ? -27.33000 -36.47000 -16.67700 1.000 29.70107 ? 55  GLN A CG  1 
ATOM   393  C  CD  . GLN A 1 55  ? -26.09600 -36.98700 -15.97800 1.000 32.65572 ? 55  GLN A CD  1 
ATOM   394  O  OE1 . GLN A 1 55  ? -25.03900 -37.11200 -16.58600 1.000 33.11466 ? 55  GLN A OE1 1 
ATOM   395  N  NE2 . GLN A 1 55  ? -26.21500 -37.26000 -14.68300 1.000 35.88051 ? 55  GLN A NE2 1 
ATOM   396  N  N   . ILE A 1 56  ? -27.03500 -33.03300 -19.66200 1.000 23.04260 ? 56  ILE A N   1 
ATOM   397  C  CA  . ILE A 1 56  ? -26.49200 -31.71800 -19.97600 1.000 20.86465 ? 56  ILE A CA  1 
ATOM   398  C  C   . ILE A 1 56  ? -26.12200 -31.67800 -21.45600 1.000 21.22474 ? 56  ILE A C   1 
ATOM   399  O  O   . ILE A 1 56  ? -25.53600 -32.62400 -22.00300 1.000 22.25495 ? 56  ILE A O   1 
ATOM   400  C  CB  . ILE A 1 56  ? -25.29300 -31.37100 -19.06800 1.000 20.91288 ? 56  ILE A CB  1 
ATOM   401  C  CG1 . ILE A 1 56  ? -24.69800 -30.00500 -19.42400 1.000 20.42046 ? 56  ILE A CG1 1 
ATOM   402  C  CG2 . ILE A 1 56  ? -24.24400 -32.45900 -19.12700 1.000 21.49460 ? 56  ILE A CG2 1 
ATOM   403  C  CD1 . ILE A 1 56  ? -23.77500 -29.43200 -18.34000 1.000 20.43091 ? 56  ILE A CD1 1 
ATOM   404  N  N   . GLN A 1 57  ? -26.50200 -30.59200 -22.11900 1.000 19.64708 ? 57  GLN A N   1 
ATOM   405  C  CA  . GLN A 1 57  ? -26.13100 -30.36400 -23.50600 1.000 19.92667 ? 57  GLN A CA  1 
ATOM   406  C  C   . GLN A 1 57  ? -25.63900 -28.93500 -23.68000 1.000 18.81579 ? 57  GLN A C   1 
ATOM   407  O  O   . GLN A 1 57  ? -25.80900 -28.08500 -22.80400 1.000 18.18417 ? 57  GLN A O   1 
ATOM   408  C  CB  . GLN A 1 57  ? -27.30500 -30.63500 -24.44300 1.000 20.74520 ? 57  GLN A CB  1 
ATOM   409  C  CG  . GLN A 1 57  ? -27.59000 -32.11400 -24.56900 1.000 23.50594 ? 57  GLN A CG  1 
ATOM   410  C  CD  . GLN A 1 57  ? -28.80000 -32.39400 -25.41300 1.000 26.95070 ? 57  GLN A CD  1 
ATOM   411  O  OE1 . GLN A 1 57  ? -29.02000 -31.74800 -26.44200 1.000 29.43481 ? 57  GLN A OE1 1 
ATOM   412  N  NE2 . GLN A 1 57  ? -29.61400 -33.34300 -24.97000 1.000 27.14611 ? 57  GLN A NE2 1 
ATOM   413  N  N   . PHE A 1 58  ? -25.02200 -28.68900 -24.83800 1.000 21.31563 ? 58  PHE A N   1 
ATOM   414  C  CA  . PHE A 1 58  ? -24.52000 -27.37900 -25.23000 1.000 19.68730 ? 58  PHE A CA  1 
ATOM   415  C  C   . PHE A 1 58  ? -25.35100 -26.80700 -26.37800 1.000 19.37779 ? 58  PHE A C   1 
ATOM   416  O  O   . PHE A 1 58  ? -25.78300 -27.53700 -27.28100 1.000 21.38976 ? 58  PHE A O   1 
ATOM   417  C  CB  . PHE A 1 58  ? -23.04300 -27.47800 -25.63900 1.000 20.92342 ? 58  PHE A CB  1 
ATOM   418  C  CG  . PHE A 1 58  ? -22.51400 -26.27100 -26.38500 1.000 19.59738 ? 58  PHE A CG  1 
ATOM   419  C  CD1 . PHE A 1 58  ? -22.30600 -25.06200 -25.72900 1.000 20.10209 ? 58  PHE A CD1 1 
ATOM   420  C  CD2 . PHE A 1 58  ? -22.22900 -26.36200 -27.73800 1.000 19.96236 ? 58  PHE A CD2 1 
ATOM   421  C  CE1 . PHE A 1 58  ? -21.80500 -23.96200 -26.41300 1.000 19.26515 ? 58  PHE A CE1 1 
ATOM   422  C  CE2 . PHE A 1 58  ? -21.73200 -25.27000 -28.43600 1.000 21.09424 ? 58  PHE A CE2 1 
ATOM   423  C  CZ  . PHE A 1 58  ? -21.51400 -24.07300 -27.77900 1.000 18.84023 ? 58  PHE A CZ  1 
ATOM   424  N  N   . PHE A 1 59  ? -25.58300 -25.50200 -26.32500 1.000 19.36758 ? 59  PHE A N   1 
ATOM   425  C  CA  . PHE A 1 59  ? -26.23000 -24.75600 -27.39700 1.000 20.27734 ? 59  PHE A CA  1 
ATOM   426  C  C   . PHE A 1 59  ? -25.38000 -23.52700 -27.70800 1.000 19.72519 ? 59  PHE A C   1 
ATOM   427  O  O   . PHE A 1 59  ? -25.15400 -22.67900 -26.83100 1.000 18.18433 ? 59  PHE A O   1 
ATOM   428  C  CB  . PHE A 1 59  ? -27.66300 -24.35000 -26.99600 1.000 19.54670 ? 59  PHE A CB  1 
ATOM   429  C  CG  . PHE A 1 59  ? -28.43800 -23.70600 -28.11900 1.000 20.68008 ? 59  PHE A CG  1 
ATOM   430  C  CD1 . PHE A 1 59  ? -28.42200 -22.33300 -28.28600 1.000 19.39480 ? 59  PHE A CD1 1 
ATOM   431  C  CD2 . PHE A 1 59  ? -29.16100 -24.48500 -29.01500 1.000 22.17969 ? 59  PHE A CD2 1 
ATOM   432  C  CE1 . PHE A 1 59  ? -29.13300 -21.73900 -29.33900 1.000 19.98398 ? 59  PHE A CE1 1 
ATOM   433  C  CE2 . PHE A 1 59  ? -29.85600 -23.90100 -30.07000 1.000 22.48706 ? 59  PHE A CE2 1 
ATOM   434  C  CZ  . PHE A 1 59  ? -29.84300 -22.52600 -30.22600 1.000 21.81983 ? 59  PHE A CZ  1 
ATOM   435  N  N   . GLN A 1 60  ? -24.92800 -23.42100 -28.95300 1.000 20.28070 ? 60  GLN A N   1 
ATOM   436  C  CA  . GLN A 1 60  ? -24.07700 -22.31000 -29.36200 1.000 18.64842 ? 60  GLN A CA  1 
ATOM   437  C  C   . GLN A 1 60  ? -24.90500 -21.04400 -29.52000 1.000 20.36156 ? 60  GLN A C   1 
ATOM   438  O  O   . GLN A 1 60  ? -25.85300 -21.00800 -30.31500 1.000 21.42188 ? 60  GLN A O   1 
ATOM   439  C  CB  . GLN A 1 60  ? -23.37700 -22.65200 -30.67100 1.000 19.39589 ? 60  GLN A CB  1 
ATOM   440  C  CG  . GLN A 1 60  ? -22.45300 -21.56200 -31.16100 1.000 21.48232 ? 60  GLN A CG  1 
ATOM   441  C  CD  . GLN A 1 60  ? -21.77700 -21.95000 -32.45800 1.000 25.99098 ? 60  GLN A CD  1 
ATOM   442  O  OE1 . GLN A 1 60  ? -22.43300 -22.33800 -33.42000 1.000 32.15324 ? 60  GLN A OE1 1 
ATOM   443  N  NE2 . GLN A 1 60  ? -20.46400 -21.88200 -32.48100 1.000 29.20216 ? 60  GLN A NE2 1 
ATOM   444  N  N   . HIS A 1 61  ? -24.55300 -20.00300 -28.76100 1.000 18.46795 ? 61  HIS A N   1 
ATOM   445  C  CA  . HIS A 1 61  ? -25.36900 -18.79500 -28.72900 1.000 20.03070 ? 61  HIS A CA  1 
ATOM   446  C  C   . HIS A 1 61  ? -24.59600 -17.64100 -28.10500 1.000 20.31372 ? 61  HIS A C   1 
ATOM   447  O  O   . HIS A 1 61  ? -24.00400 -17.78100 -27.02500 1.000 20.82728 ? 61  HIS A O   1 
ATOM   448  C  CB  . HIS A 1 61  ? -26.66400 -19.05900 -27.93900 1.000 19.15930 ? 61  HIS A CB  1 
ATOM   449  C  CG  . HIS A 1 61  ? -27.53900 -17.85700 -27.77900 1.000 18.58198 ? 61  HIS A CG  1 
ATOM   450  N  ND1 . HIS A 1 61  ? -27.97300 -17.40300 -26.54800 1.000 18.70598 ? 61  HIS A ND1 1 
ATOM   451  C  CD2 . HIS A 1 61  ? -28.07500 -17.01900 -28.70000 1.000 19.33805 ? 61  HIS A CD2 1 
ATOM   452  C  CE1 . HIS A 1 61  ? -28.73700 -16.33500 -26.71900 1.000 18.02062 ? 61  HIS A CE1 1 
ATOM   453  N  NE2 . HIS A 1 61  ? -28.82000 -16.08500 -28.01500 1.000 18.23100 ? 61  HIS A NE2 1 
ATOM   454  N  N   . ASP A 1 62  ? -24.60000 -16.49300 -28.77300 1.000 19.26266 ? 62  ASP A N   1 
ATOM   455  C  CA  . ASP A 1 62  ? -24.12300 -15.23800 -28.19800 1.000 20.29499 ? 62  ASP A CA  1 
ATOM   456  C  C   . ASP A 1 62  ? -25.29800 -14.58600 -27.47900 1.000 18.42487 ? 62  ASP A C   1 
ATOM   457  O  O   . ASP A 1 62  ? -26.34900 -14.37800 -28.08800 1.000 19.85557 ? 62  ASP A O   1 
ATOM   458  C  CB  . ASP A 1 62  ? -23.59600 -14.34400 -29.31900 1.000 20.46603 ? 62  ASP A CB  1 
ATOM   459  C  CG  . ASP A 1 62  ? -22.94100 -13.08100 -28.82200 1.000 24.18221 ? 62  ASP A CG  1 
ATOM   460  O  OD1 . ASP A 1 62  ? -23.43900 -12.44100 -27.87100 1.000 21.99168 ? 62  ASP A OD1 1 
ATOM   461  O  OD2 . ASP A 1 62  ? -21.90400 -12.71600 -29.42700 1.000 27.75207 ? 62  ASP A OD2 1 
ATOM   462  N  N   . SER A 1 63  ? -25.14100 -14.28700 -26.18300 1.000 18.52941 ? 63  SER A N   1 
ATOM   463  C  CA  . SER A 1 63  ? -26.29600 -13.81700 -25.41200 1.000 17.62595 ? 63  SER A CA  1 
ATOM   464  C  C   . SER A 1 63  ? -26.82300 -12.46500 -25.89500 1.000 20.12286 ? 63  SER A C   1 
ATOM   465  O  O   . SER A 1 63  ? -27.94900 -12.09500 -25.54300 1.000 21.16079 ? 63  SER A O   1 
ATOM   466  C  CB  . SER A 1 63  ? -25.95300 -13.77100 -23.91800 1.000 19.51095 ? 63  SER A CB  1 
ATOM   467  O  OG  . SER A 1 63  ? -25.05900 -12.70000 -23.65800 1.000 20.69429 ? 63  SER A OG  1 
ATOM   468  N  N   . SER A 1 64  ? -26.06700 -11.73300 -26.71300 1.000 19.99640 ? 64  SER A N   1 
ATOM   469  C  CA  . SER A 1 64  ? -26.57700 -10.49900 -27.31600 1.000 21.51784 ? 64  SER A CA  1 
ATOM   470  C  C   . SER A 1 64  ? -27.50600 -10.74800 -28.50000 1.000 22.37521 ? 64  SER A C   1 
ATOM   471  O  O   . SER A 1 64  ? -28.10500 -9.78900  -29.01600 1.000 22.00695 ? 64  SER A O   1 
ATOM   472  C  CB  . SER A 1 64  ? -25.40700 -9.59900  -27.76000 1.000 20.65795 ? 64  SER A CB  1 
ATOM   473  O  OG  . SER A 1 64  ? -24.65400 -10.20700 -28.81000 1.000 21.87661 ? 64  SER A OG  1 
ATOM   474  N  N   . ASP A 1 65  ? -27.63500 -11.99800 -28.94100 1.000 20.67279 ? 65  ASP A N   1 
ATOM   475  C  CA  . ASP A 1 65  ? -28.38700 -12.36500 -30.14300 1.000 21.18001 ? 65  ASP A CA  1 
ATOM   476  C  C   . ASP A 1 65  ? -29.83700 -12.63300 -29.73900 1.000 20.36337 ? 65  ASP A C   1 
ATOM   477  O  O   . ASP A 1 65  ? -30.16100 -13.69900 -29.21100 1.000 19.64712 ? 65  ASP A O   1 
ATOM   478  C  CB  . ASP A 1 65  ? -27.71200 -13.56600 -30.79300 1.000 21.64436 ? 65  ASP A CB  1 
ATOM   479  C  CG  . ASP A 1 65  ? -28.53400 -14.22100 -31.89500 1.000 23.21559 ? 65  ASP A CG  1 
ATOM   480  O  OD1 . ASP A 1 65  ? -29.57300 -13.69000 -32.33100 1.000 22.48339 ? 65  ASP A OD1 1 
ATOM   481  O  OD2 . ASP A 1 65  ? -28.11100 -15.31500 -32.32900 1.000 25.61854 ? 65  ASP A OD2 1 
ATOM   482  N  N   . GLU A 1 66  ? -30.71600 -11.66100 -30.01500 1.000 20.18941 ? 66  GLU A N   1 
ATOM   483  C  CA  . GLU A 1 66  ? -32.11100 -11.74600 -29.57600 1.000 19.56600 ? 66  GLU A CA  1 
ATOM   484  C  C   . GLU A 1 66  ? -32.85000 -12.92700 -30.21100 1.000 20.05062 ? 66  GLU A C   1 
ATOM   485  O  O   . GLU A 1 66  ? -33.56300 -13.67400 -29.52500 1.000 20.52701 ? 66  GLU A O   1 
ATOM   486  C  CB  . GLU A 1 66  ? -32.82100 -10.42700 -29.89700 1.000 19.14969 ? 66  GLU A CB  1 
ATOM   487  C  CG  . GLU A 1 66  ? -34.24500 -10.35700 -29.37300 1.000 19.04047 ? 66  GLU A CG  1 
ATOM   488  C  CD  . GLU A 1 66  ? -34.95200 -9.09100  -29.77100 1.000 20.32504 ? 66  GLU A CD  1 
ATOM   489  O  OE1 . GLU A 1 66  ? -34.38100 -8.26300  -30.50700 1.000 22.96261 ? 66  GLU A OE1 1 
ATOM   490  O  OE2 . GLU A 1 66  ? -36.11300 -8.93200  -29.36200 1.000 22.49822 ? 66  GLU A OE2 1 
ATOM   491  N  N   . ASP A 1 67  ? -32.73400 -13.09400 -31.52800 1.000 20.39979 ? 67  ASP A N   1 
ATOM   492  C  CA  . ASP A 1 67  ? -33.43200 -14.20900 -32.15100 1.000 22.45259 ? 67  ASP A CA  1 
ATOM   493  C  C   . ASP A 1 67  ? -32.89900 -15.54700 -31.66000 1.000 21.01447 ? 67  ASP A C   1 
ATOM   494  O  O   . ASP A 1 67  ? -33.66900 -16.50800 -31.53000 1.000 22.00744 ? 67  ASP A O   1 
ATOM   495  C  CB  . ASP A 1 67  ? -33.32700 -14.12000 -33.67400 1.000 29.11833 ? 67  ASP A CB  1 
ATOM   496  C  CG  . ASP A 1 67  ? -34.14700 -15.19300 -34.37800 1.000 39.49497 ? 67  ASP A CG  1 
ATOM   497  O  OD1 . ASP A 1 67  ? -35.26900 -15.51300 -33.90700 1.000 42.94245 ? 67  ASP A OD1 1 
ATOM   498  O  OD2 . ASP A 1 67  ? -33.67100 -15.71800 -35.41200 1.000 44.04492 ? 67  ASP A OD2 1 
ATOM   499  N  N   . GLY A 1 68  ? -31.59800 -15.63000 -31.36700 1.000 20.36228 ? 68  GLY A N   1 
ATOM   500  C  CA  . GLY A 1 68  ? -31.04300 -16.87800 -30.88100 1.000 20.90354 ? 68  GLY A CA  1 
ATOM   501  C  C   . GLY A 1 68  ? -31.58400 -17.29900 -29.53100 1.000 20.37193 ? 68  GLY A C   1 
ATOM   502  O  O   . GLY A 1 68  ? -31.60900 -18.49700 -29.21900 1.000 21.18303 ? 68  GLY A O   1 
ATOM   503  N  N   . TRP A 1 69  ? -32.03600 -16.33400 -28.71900 1.000 18.43725 ? 69  TRP A N   1 
ATOM   504  C  CA  . TRP A 1 69  ? -32.61800 -16.66800 -27.41700 1.000 16.82920 ? 69  TRP A CA  1 
ATOM   505  C  C   . TRP A 1 69  ? -33.85500 -17.53900 -27.58300 1.000 18.72634 ? 69  TRP A C   1 
ATOM   506  O  O   . TRP A 1 69  ? -34.08000 -18.47400 -26.80800 1.000 19.22640 ? 69  TRP A O   1 
ATOM   507  C  CB  . TRP A 1 69  ? -32.97200 -15.38600 -26.66000 1.000 17.70093 ? 69  TRP A CB  1 
ATOM   508  C  CG  . TRP A 1 69  ? -31.89400 -14.87400 -25.76800 1.000 17.28094 ? 69  TRP A CG  1 
ATOM   509  C  CD1 . TRP A 1 69  ? -31.02600 -13.83800 -26.00600 1.000 18.86710 ? 69  TRP A CD1 1 
ATOM   510  C  CD2 . TRP A 1 69  ? -31.58500 -15.37200 -24.46300 1.000 15.95779 ? 69  TRP A CD2 1 
ATOM   511  N  NE1 . TRP A 1 69  ? -30.18600 -13.67800 -24.91400 1.000 18.20736 ? 69  TRP A NE1 1 
ATOM   512  C  CE2 . TRP A 1 69  ? -30.52200 -14.61000 -23.96300 1.000 17.27211 ? 69  TRP A CE2 1 
ATOM   513  C  CE3 . TRP A 1 69  ? -32.11400 -16.41000 -23.67300 1.000 17.74715 ? 69  TRP A CE3 1 
ATOM   514  C  CZ2 . TRP A 1 69  ? -29.97100 -14.84600 -22.69500 1.000 18.02026 ? 69  TRP A CZ2 1 
ATOM   515  C  CZ3 . TRP A 1 69  ? -31.57500 -16.64000 -22.42800 1.000 16.84377 ? 69  TRP A CZ3 1 
ATOM   516  C  CH2 . TRP A 1 69  ? -30.50600 -15.87400 -21.96100 1.000 18.01599 ? 69  TRP A CH2 1 
ATOM   517  N  N   . THR A 1 70  ? -34.68700 -17.23100 -28.58400 1.000 19.70492 ? 70  THR A N   1 
ATOM   518  C  CA  . THR A 1 70  ? -35.85200 -18.06600 -28.85600 1.000 18.69223 ? 70  THR A CA  1 
ATOM   519  C  C   . THR A 1 70  ? -35.42900 -19.48200 -29.22200 1.000 21.34185 ? 70  THR A C   1 
ATOM   520  O  O   . THR A 1 70  ? -35.98800 -20.46300 -28.71600 1.000 21.85569 ? 70  THR A O   1 
ATOM   521  C  CB  . THR A 1 70  ? -36.68400 -17.43000 -29.97400 1.000 21.81144 ? 70  THR A CB  1 
ATOM   522  O  OG1 . THR A 1 70  ? -36.97100 -16.06800 -29.62400 1.000 24.22486 ? 70  THR A OG1 1 
ATOM   523  C  CG2 . THR A 1 70  ? -37.98800 -18.19500 -30.19500 1.000 23.53756 ? 70  THR A CG2 1 
ATOM   524  N  N   . LYS A 1 71  ? -34.43100 -19.60600 -30.10700 1.000 20.28599 ? 71  LYS A N   1 
ATOM   525  C  CA  . LYS A 1 71  ? -33.94700 -20.92100 -30.51300 1.000 21.34111 ? 71  LYS A CA  1 
ATOM   526  C  C   . LYS A 1 71  ? -33.33900 -21.67000 -29.33600 1.000 20.26891 ? 71  LYS A C   1 
ATOM   527  O  O   . LYS A 1 71  ? -33.47400 -22.89300 -29.23800 1.000 20.95571 ? 71  LYS A O   1 
ATOM   528  C  CB  . LYS A 1 71  ? -32.92700 -20.77600 -31.64000 1.000 25.33942 ? 71  LYS A CB  1 
ATOM   529  C  CG  . LYS A 1 71  ? -33.52500 -20.21100 -32.93600 1.000 30.79588 ? 71  LYS A CG  1 
ATOM   530  C  CD  . LYS A 1 71  ? -32.45800 -19.61800 -33.85300 1.000 35.53389 ? 71  LYS A CD  1 
ATOM   531  C  CE  . LYS A 1 71  ? -32.72900 -19.91900 -35.30900 1.000 39.29396 ? 71  LYS A CE  1 
ATOM   532  N  NZ  . LYS A 1 71  ? -34.12600 -19.59500 -35.67400 1.000 41.66732 ? 71  LYS A NZ  1 
ATOM   533  N  N   . LEU A 1 72  ? -32.69600 -20.94500 -28.42000 1.000 19.01366 ? 72  LEU A N   1 
ATOM   534  C  CA  . LEU A 1 72  ? -32.11500 -21.57200 -27.23400 1.000 19.52826 ? 72  LEU A CA  1 
ATOM   535  C  C   . LEU A 1 72  ? -33.19400 -22.17300 -26.32900 1.000 19.71188 ? 72  LEU A C   1 
ATOM   536  O  O   . LEU A 1 72  ? -33.09500 -23.33600 -25.91400 1.000 20.74336 ? 72  LEU A O   1 
ATOM   537  C  CB  . LEU A 1 72  ? -31.29100 -20.53200 -26.48000 1.000 16.84284 ? 72  LEU A CB  1 
ATOM   538  C  CG  . LEU A 1 72  ? -30.91200 -20.85000 -25.03900 1.000 16.91591 ? 72  LEU A CG  1 
ATOM   539  C  CD1 . LEU A 1 72  ? -30.01000 -22.06700 -24.99200 1.000 17.96747 ? 72  LEU A CD1 1 
ATOM   540  C  CD2 . LEU A 1 72  ? -30.23100 -19.64500 -24.41700 1.000 17.82730 ? 72  LEU A CD2 1 
ATOM   541  N  N   . PHE A 1 73  ? -34.24900 -21.40700 -26.02500 1.000 21.08722 ? 73  PHE A N   1 
ATOM   542  C  CA  . PHE A 1 73  ? -35.34300 -21.97100 -25.23300 1.000 18.81150 ? 73  PHE A CA  1 
ATOM   543  C  C   . PHE A 1 73  ? -36.03400 -23.12500 -25.96500 1.000 20.43557 ? 73  PHE A C   1 
ATOM   544  O  O   . PHE A 1 73  ? -36.38600 -24.14200 -25.34500 1.000 21.41610 ? 73  PHE A O   1 
ATOM   545  C  CB  . PHE A 1 73  ? -36.35200 -20.87800 -24.85600 1.000 18.69077 ? 73  PHE A CB  1 
ATOM   546  C  CG  . PHE A 1 73  ? -36.09100 -20.25600 -23.52500 1.000 17.27460 ? 73  PHE A CG  1 
ATOM   547  C  CD1 . PHE A 1 73  ? -35.14300 -19.26900 -23.40300 1.000 16.42744 ? 73  PHE A CD1 1 
ATOM   548  C  CD2 . PHE A 1 73  ? -36.79300 -20.65900 -22.39700 1.000 17.47436 ? 73  PHE A CD2 1 
ATOM   549  C  CE1 . PHE A 1 73  ? -34.88100 -18.66000 -22.17300 1.000 18.21356 ? 73  PHE A CE1 1 
ATOM   550  C  CE2 . PHE A 1 73  ? -36.54500 -20.05200 -21.14400 1.000 17.22961 ? 73  PHE A CE2 1 
ATOM   551  C  CZ  . PHE A 1 73  ? -35.57700 -19.05500 -21.04500 1.000 18.28825 ? 73  PHE A CZ  1 
ATOM   552  N  N   . ASP A 1 74  ? -36.23800 -22.98900 -27.28100 1.000 20.23840 ? 74  ASP A N   1 
ATOM   553  C  CA  . ASP A 1 74  ? -36.83700 -24.06800 -28.06200 1.000 21.92646 ? 74  ASP A CA  1 
ATOM   554  C  C   . ASP A 1 74  ? -36.01700 -25.34400 -27.94500 1.000 21.60203 ? 74  ASP A C   1 
ATOM   555  O  O   . ASP A 1 74  ? -36.55800 -26.43100 -27.72800 1.000 22.37052 ? 74  ASP A O   1 
ATOM   556  C  CB  . ASP A 1 74  ? -36.92800 -23.67400 -29.53600 1.000 21.94749 ? 74  ASP A CB  1 
ATOM   557  C  CG  . ASP A 1 74  ? -38.03700 -22.68100 -29.83700 1.000 26.09930 ? 74  ASP A CG  1 
ATOM   558  O  OD1 . ASP A 1 74  ? -38.93600 -22.46600 -29.00100 1.000 26.20614 ? 74  ASP A OD1 1 
ATOM   559  O  OD2 . ASP A 1 74  ? -38.00500 -22.11900 -30.95800 1.000 27.91060 ? 74  ASP A OD2 1 
ATOM   560  N  N   . ALA A 1 75  ? -34.70500 -25.23400 -28.12800 1.000 20.96605 ? 75  ALA A N   1 
ATOM   561  C  CA  . ALA A 1 75  ? -33.87000 -26.42500 -28.09400 1.000 21.33660 ? 75  ALA A CA  1 
ATOM   562  C  C   . ALA A 1 75  ? -33.84300 -27.03600 -26.70000 1.000 21.08569 ? 75  ALA A C   1 
ATOM   563  O  O   . ALA A 1 75  ? -33.79900 -28.26200 -26.55500 1.000 23.63124 ? 75  ALA A O   1 
ATOM   564  C  CB  . ALA A 1 75  ? -32.45300 -26.07800 -28.54800 1.000 21.28194 ? 75  ALA A CB  1 
ATOM   565  N  N   . THR A 1 76  ? -33.85300 -26.20200 -25.66300 1.000 20.46571 ? 76  THR A N   1 
ATOM   566  C  CA  . THR A 1 76  ? -33.84600 -26.75700 -24.31900 1.000 19.00128 ? 76  THR A CA  1 
ATOM   567  C  C   . THR A 1 76  ? -35.14900 -27.49500 -24.02400 1.000 21.53993 ? 76  THR A C   1 
ATOM   568  O  O   . THR A 1 76  ? -35.12400 -28.59300 -23.45700 1.000 21.34560 ? 76  THR A O   1 
ATOM   569  C  CB  . THR A 1 76  ? -33.57500 -25.65200 -23.29900 1.000 18.36115 ? 76  THR A CB  1 
ATOM   570  O  OG1 . THR A 1 76  ? -32.35700 -24.98200 -23.65600 1.000 18.38764 ? 76  THR A OG1 1 
ATOM   571  C  CG2 . THR A 1 76  ? -33.41300 -26.24500 -21.89600 1.000 19.72152 ? 76  THR A CG2 1 
ATOM   572  N  N   . GLU A 1 77  ? -36.29000 -26.92000 -24.42500 1.000 21.22942 ? 77  GLU A N   1 
ATOM   573  C  CA  . GLU A 1 77  ? -37.57000 -27.60300 -24.25500 1.000 23.16192 ? 77  GLU A CA  1 
ATOM   574  C  C   . GLU A 1 77  ? -37.57900 -28.94900 -24.96300 1.000 23.40978 ? 77  GLU A C   1 
ATOM   575  O  O   . GLU A 1 77  ? -38.07400 -29.94400 -24.42100 1.000 25.85219 ? 77  GLU A O   1 
ATOM   576  C  CB  . GLU A 1 77  ? -38.70800 -26.75600 -24.81500 1.000 25.19197 ? 77  GLU A CB  1 
ATOM   577  C  CG  . GLU A 1 77  ? -39.04100 -25.57300 -23.99500 1.000 26.69292 ? 77  GLU A CG  1 
ATOM   578  C  CD  . GLU A 1 77  ? -40.08700 -24.69200 -24.64400 1.000 30.05826 ? 77  GLU A CD  1 
ATOM   579  O  OE1 . GLU A 1 77  ? -40.09400 -23.48500 -24.31000 1.000 30.14674 ? 77  GLU A OE1 1 
ATOM   580  O  OE2 . GLU A 1 77  ? -40.88400 -25.20400 -25.48500 1.000 32.22606 ? 77  GLU A OE2 1 
ATOM   581  N  N   . LYS A 1 78  ? -37.05200 -28.98800 -26.19000 1.000 23.44985 ? 78  LYS A N   1 
ATOM   582  C  CA  . LYS A 1 78  ? -37.04200 -30.21800 -26.97100 1.000 26.00508 ? 78  LYS A CA  1 
ATOM   583  C  C   . LYS A 1 78  ? -36.20400 -31.29700 -26.31200 1.000 24.96311 ? 78  LYS A C   1 
ATOM   584  O  O   . LYS A 1 78  ? -36.55000 -32.48200 -26.37200 1.000 25.82589 ? 78  LYS A O   1 
ATOM   585  C  CB  . LYS A 1 78  ? -36.52000 -29.91900 -28.36700 1.000 29.92096 ? 78  LYS A CB  1 
ATOM   586  C  CG  . LYS A 1 78  ? -37.45900 -29.00700 -29.10600 1.000 36.44930 ? 78  LYS A CG  1 
ATOM   587  C  CD  . LYS A 1 78  ? -37.58700 -29.40600 -30.53800 1.000 42.78951 ? 78  LYS A CD  1 
ATOM   588  C  CE  . LYS A 1 78  ? -37.41200 -28.20900 -31.43800 1.000 45.72567 ? 78  LYS A CE  1 
ATOM   589  N  NZ  . LYS A 1 78  ? -38.23000 -27.04800 -30.97300 1.000 46.03190 ? 78  LYS A NZ  1 
ATOM   590  N  N   . ALA A 1 79  ? -35.09300 -30.90800 -25.68500 1.000 22.83545 ? 79  ALA A N   1 
ATOM   591  C  CA  . ALA A 1 79  ? -34.20900 -31.89200 -25.08100 1.000 24.49810 ? 79  ALA A CA  1 
ATOM   592  C  C   . ALA A 1 79  ? -34.73400 -32.37500 -23.74000 1.000 24.84060 ? 79  ALA A C   1 
ATOM   593  O  O   . ALA A 1 79  ? -34.64300 -33.56900 -23.42700 1.000 26.06053 ? 79  ALA A O   1 
ATOM   594  C  CB  . ALA A 1 79  ? -32.81100 -31.29700 -24.89500 1.000 23.43597 ? 79  ALA A CB  1 
ATOM   595  N  N   . PHE A 1 80  ? -35.25900 -31.45700 -22.92500 1.000 23.17710 ? 80  PHE A N   1 
ATOM   596  C  CA  . PHE A 1 80  ? -35.43500 -31.70800 -21.50900 1.000 22.78493 ? 80  PHE A CA  1 
ATOM   597  C  C   . PHE A 1 80  ? -36.83100 -31.42800 -20.98600 1.000 22.22291 ? 80  PHE A C   1 
ATOM   598  O  O   . PHE A 1 80  ? -37.09600 -31.73200 -19.81500 1.000 24.97600 ? 80  PHE A O   1 
ATOM   599  C  CB  . PHE A 1 80  ? -34.46000 -30.84700 -20.69200 1.000 21.24306 ? 80  PHE A CB  1 
ATOM   600  C  CG  . PHE A 1 80  ? -33.00700 -31.10100 -20.98600 1.000 21.91107 ? 80  PHE A CG  1 
ATOM   601  C  CD1 . PHE A 1 80  ? -32.49900 -32.39600 -21.03800 1.000 23.65258 ? 80  PHE A CD1 1 
ATOM   602  C  CD2 . PHE A 1 80  ? -32.14300 -30.03100 -21.17700 1.000 21.80190 ? 80  PHE A CD2 1 
ATOM   603  C  CE1 . PHE A 1 80  ? -31.13800 -32.61700 -21.28500 1.000 22.22115 ? 80  PHE A CE1 1 
ATOM   604  C  CE2 . PHE A 1 80  ? -30.77800 -30.24200 -21.42300 1.000 20.51651 ? 80  PHE A CE2 1 
ATOM   605  C  CZ  . PHE A 1 80  ? -30.28200 -31.53200 -21.47800 1.000 21.01716 ? 80  PHE A CZ  1 
ATOM   606  N  N   . GLY A 1 81  ? -37.69000 -30.78600 -21.76900 1.000 22.52243 ? 81  GLY A N   1 
ATOM   607  C  CA  . GLY A 1 81  ? -38.98300 -30.34300 -21.30500 1.000 22.68041 ? 81  GLY A CA  1 
ATOM   608  C  C   . GLY A 1 81  ? -38.96300 -28.88300 -20.90200 1.000 21.36795 ? 81  GLY A C   1 
ATOM   609  O  O   . GLY A 1 81  ? -37.94300 -28.18600 -21.01000 1.000 21.44987 ? 81  GLY A O   1 
ATOM   610  N  N   . PRO A 1 82  ? -40.09100 -28.39300 -20.39700 1.000 19.24765 ? 82  PRO A N   1 
ATOM   611  C  CA  . PRO A 1 82  ? -40.19600 -26.96400 -20.07200 1.000 18.58093 ? 82  PRO A CA  1 
ATOM   612  C  C   . PRO A 1 82  ? -39.09800 -26.46900 -19.14600 1.000 20.03145 ? 82  PRO A C   1 
ATOM   613  O  O   . PRO A 1 82  ? -38.78100 -27.08800 -18.11900 1.000 20.34510 ? 82  PRO A O   1 
ATOM   614  C  CB  . PRO A 1 82  ? -41.57000 -26.85600 -19.40700 1.000 20.08650 ? 82  PRO A CB  1 
ATOM   615  C  CG  . PRO A 1 82  ? -42.35600 -27.98800 -20.03900 1.000 22.32248 ? 82  PRO A CG  1 
ATOM   616  C  CD  . PRO A 1 82  ? -41.36300 -29.10900 -20.19500 1.000 22.78811 ? 82  PRO A CD  1 
ATOM   617  N  N   . VAL A 1 83  ? -38.54700 -25.31200 -19.51000 1.000 18.35196 ? 83  VAL A N   1 
ATOM   618  C  CA  . VAL A 1 83  ? -37.47400 -24.70000 -18.73800 1.000 18.82082 ? 83  VAL A CA  1 
ATOM   619  C  C   . VAL A 1 83  ? -38.04600 -24.12200 -17.45500 1.000 18.47015 ? 83  VAL A C   1 
ATOM   620  O  O   . VAL A 1 83  ? -39.04100 -23.38800 -17.47500 1.000 20.25551 ? 83  VAL A O   1 
ATOM   621  C  CB  . VAL A 1 83  ? -36.78200 -23.62000 -19.57800 1.000 18.16875 ? 83  VAL A CB  1 
ATOM   622  C  CG1 . VAL A 1 83  ? -35.63900 -22.96300 -18.80200 1.000 17.84158 ? 83  VAL A CG1 1 
ATOM   623  C  CG2 . VAL A 1 83  ? -36.29300 -24.24300 -20.88100 1.000 19.31138 ? 83  VAL A CG2 1 
ATOM   624  N  N   . SER A 1 84  ? -37.39900 -24.42900 -16.33500 1.000 16.37925 ? 84  SER A N   1 
ATOM   625  C  CA  . SER A 1 84  ? -37.77700 -23.86700 -15.04800 1.000 16.38099 ? 84  SER A CA  1 
ATOM   626  C  C   . SER A 1 84  ? -36.78700 -22.84900 -14.51700 1.000 16.65550 ? 84  SER A C   1 
ATOM   627  O  O   . SER A 1 84  ? -37.12800 -22.10600 -13.59700 1.000 16.31683 ? 84  SER A O   1 
ATOM   628  C  CB  . SER A 1 84  ? -37.89800 -24.99400 -14.01600 1.000 16.49932 ? 84  SER A CB  1 
ATOM   629  O  OG  . SER A 1 84  ? -36.59500 -25.51500 -13.76000 1.000 19.40311 ? 84  SER A OG  1 
ATOM   630  N  N   . THR A 1 85  ? -35.55800 -22.81900 -15.03600 1.000 15.72539 ? 85  THR A N   1 
ATOM   631  C  CA  . THR A 1 85  ? -34.47400 -22.10400 -14.36800 1.000 15.45040 ? 85  THR A CA  1 
ATOM   632  C  C   . THR A 1 85  ? -33.57900 -21.45000 -15.41400 1.000 15.75870 ? 85  THR A C   1 
ATOM   633  O  O   . THR A 1 85  ? -33.22500 -22.09500 -16.40200 1.000 17.86475 ? 85  THR A O   1 
ATOM   634  C  CB  . THR A 1 85  ? -33.65500 -23.09300 -13.50900 1.000 16.29117 ? 85  THR A CB  1 
ATOM   635  O  OG1 . THR A 1 85  ? -34.54500 -23.87800 -12.69600 1.000 17.27529 ? 85  THR A OG1 1 
ATOM   636  C  CG2 . THR A 1 85  ? -32.67100 -22.37300 -12.62300 1.000 15.55173 ? 85  THR A CG2 1 
ATOM   637  N  N   . LEU A 1 86  ? -33.25100 -20.16800 -15.22500 1.000 15.50442 ? 86  LEU A N   1 
ATOM   638  C  CA  . LEU A 1 86  ? -32.37300 -19.46100 -16.15000 1.000 14.86472 ? 86  LEU A CA  1 
ATOM   639  C  C   . LEU A 1 86  ? -31.31100 -18.73900 -15.34900 1.000 14.95653 ? 86  LEU A C   1 
ATOM   640  O  O   . LEU A 1 86  ? -31.63900 -17.95600 -14.45800 1.000 16.15953 ? 86  LEU A O   1 
ATOM   641  C  CB  . LEU A 1 86  ? -33.13500 -18.45800 -17.01800 1.000 15.25346 ? 86  LEU A CB  1 
ATOM   642  C  CG  . LEU A 1 86  ? -32.26300 -17.52500 -17.87100 1.000 17.35598 ? 86  LEU A CG  1 
ATOM   643  C  CD1 . LEU A 1 86  ? -31.43600 -18.29000 -18.90400 1.000 17.89726 ? 86  LEU A CD1 1 
ATOM   644  C  CD2 . LEU A 1 86  ? -33.09400 -16.45200 -18.56200 1.000 14.91558 ? 86  LEU A CD2 1 
ATOM   645  N  N   . VAL A 1 87  ? -30.03800 -19.00700 -15.65000 1.000 15.04114 ? 87  VAL A N   1 
ATOM   646  C  CA  . VAL A 1 87  ? -28.93200 -18.26300 -15.06500 1.000 15.29946 ? 87  VAL A CA  1 
ATOM   647  C  C   . VAL A 1 87  ? -28.33100 -17.40300 -16.16800 1.000 16.79647 ? 87  VAL A C   1 
ATOM   648  O  O   . VAL A 1 87  ? -27.73700 -17.92600 -17.12400 1.000 17.51263 ? 87  VAL A O   1 
ATOM   649  C  CB  . VAL A 1 87  ? -27.88300 -19.19900 -14.44400 1.000 14.87768 ? 87  VAL A CB  1 
ATOM   650  C  CG1 . VAL A 1 87  ? -26.80800 -18.39100 -13.73200 1.000 16.35072 ? 87  VAL A CG1 1 
ATOM   651  C  CG2 . VAL A 1 87  ? -28.54600 -20.18000 -13.45400 1.000 16.01680 ? 87  VAL A CG2 1 
ATOM   652  N  N   . ASN A 1 88  ? -28.51900 -16.08200 -16.07100 1.000 15.31607 ? 88  ASN A N   1 
ATOM   653  C  CA  . ASN A 1 88  ? -27.97300 -15.14400 -17.06500 1.000 15.30675 ? 88  ASN A CA  1 
ATOM   654  C  C   . ASN A 1 88  ? -26.56700 -14.79500 -16.60500 1.000 15.55895 ? 88  ASN A C   1 
ATOM   655  O  O   . ASN A 1 88  ? -26.36400 -13.81800 -15.88400 1.000 16.60619 ? 88  ASN A O   1 
ATOM   656  C  CB  . ASN A 1 88  ? -28.82100 -13.87900 -17.16300 1.000 15.15630 ? 88  ASN A CB  1 
ATOM   657  C  CG  . ASN A 1 88  ? -29.97200 -14.00700 -18.12200 1.000 16.77161 ? 88  ASN A CG  1 
ATOM   658  O  OD1 . ASN A 1 88  ? -29.78600 -14.36200 -19.29100 1.000 17.47475 ? 88  ASN A OD1 1 
ATOM   659  N  ND2 . ASN A 1 88  ? -31.18000 -13.70900 -17.64300 1.000 16.67678 ? 88  ASN A ND2 1 
ATOM   660  N  N   . ASN A 1 89  ? -25.58200 -15.59300 -17.02500 1.000 16.10934 ? 89  ASN A N   1 
ATOM   661  C  CA  . ASN A 1 89  ? -24.21900 -15.49100 -16.51100 1.000 14.77745 ? 89  ASN A CA  1 
ATOM   662  C  C   . ASN A 1 89  ? -23.23300 -14.90000 -17.50900 1.000 15.66283 ? 89  ASN A C   1 
ATOM   663  O  O   . ASN A 1 89  ? -22.24100 -14.29400 -17.08500 1.000 18.78294 ? 89  ASN A O   1 
ATOM   664  C  CB  . ASN A 1 89  ? -23.73900 -16.88100 -16.06200 1.000 16.89136 ? 89  ASN A CB  1 
ATOM   665  C  CG  . ASN A 1 89  ? -22.24600 -16.93200 -15.73400 1.000 17.00524 ? 89  ASN A CG  1 
ATOM   666  O  OD1 . ASN A 1 89  ? -21.81000 -16.48100 -14.66300 1.000 18.42192 ? 89  ASN A OD1 1 
ATOM   667  N  ND2 . ASN A 1 89  ? -21.45500 -17.53800 -16.63600 1.000 18.12176 ? 89  ASN A ND2 1 
ATOM   668  N  N   . ALA A 1 90  ? -23.49300 -15.02300 -18.81500 1.000 15.61249 ? 90  ALA A N   1 
ATOM   669  C  CA  . ALA A 1 90  ? -22.55100 -14.52500 -19.81600 1.000 18.01826 ? 90  ALA A CA  1 
ATOM   670  C  C   . ALA A 1 90  ? -22.35900 -13.02100 -19.67200 1.000 17.88351 ? 90  ALA A C   1 
ATOM   671  O  O   . ALA A 1 90  ? -23.32300 -12.26100 -19.50700 1.000 18.79816 ? 90  ALA A O   1 
ATOM   672  C  CB  . ALA A 1 90  ? -23.04500 -14.85500 -21.23000 1.000 18.45006 ? 90  ALA A CB  1 
ATOM   673  N  N   . GLY A 1 91  ? -21.10700 -12.58100 -19.74600 1.000 18.82123 ? 91  GLY A N   1 
ATOM   674  C  CA  . GLY A 1 91  ? -20.82100 -11.17500 -19.58600 1.000 19.42114 ? 91  GLY A CA  1 
ATOM   675  C  C   . GLY A 1 91  ? -19.40300 -10.90600 -20.02000 1.000 21.31374 ? 91  GLY A C   1 
ATOM   676  O  O   . GLY A 1 91  ? -18.55600 -11.81000 -20.03200 1.000 24.47432 ? 91  GLY A O   1 
ATOM   677  N  N   . ILE A 1 92  ? -19.14800 -9.65000  -20.38000 1.000 18.57649 ? 92  ILE A N   1 
ATOM   678  C  CA  . ILE A 1 92  ? -17.79800 -9.23800  -20.75000 1.000 18.29677 ? 92  ILE A CA  1 
ATOM   679  C  C   . ILE A 1 92  ? -17.42700 -7.97100  -19.99600 1.000 18.40566 ? 92  ILE A C   1 
ATOM   680  O  O   . ILE A 1 92  ? -18.26900 -7.28000  -19.42800 1.000 18.51639 ? 92  ILE A O   1 
ATOM   681  C  CB  . ILE A 1 92  ? -17.64000 -9.02600  -22.27300 1.000 22.03470 ? 92  ILE A CB  1 
ATOM   682  C  CG1 . ILE A 1 92  ? -18.54200 -7.89200  -22.76000 1.000 22.95819 ? 92  ILE A CG1 1 
ATOM   683  C  CG2 . ILE A 1 92  ? -17.93000 -10.31000 -22.99600 1.000 23.89337 ? 92  ILE A CG2 1 
ATOM   684  C  CD1 . ILE A 1 92  ? -18.37700 -7.59200  -24.26600 1.000 23.62508 ? 92  ILE A CD1 1 
ATOM   685  N  N   . ALA A 1 93  ? -16.12900 -7.67000  -19.98400 1.000 20.41276 ? 93  ALA A N   1 
ATOM   686  C  CA  . ALA A 1 93  ? -15.64300 -6.47600  -19.31800 1.000 21.74972 ? 93  ALA A CA  1 
ATOM   687  C  C   . ALA A 1 93  ? -14.71200 -5.72800  -20.25600 1.000 23.41516 ? 93  ALA A C   1 
ATOM   688  O  O   . ALA A 1 93  ? -14.02100 -6.32600  -21.08000 1.000 26.60737 ? 93  ALA A O   1 
ATOM   689  C  CB  . ALA A 1 93  ? -14.91700 -6.80600  -17.99600 1.000 23.48626 ? 93  ALA A CB  1 
ATOM   690  N  N   . VAL A 1 94  ? -14.75400 -4.40500  -20.15100 1.000 19.07428 ? 94  VAL A N   1 
ATOM   691  C  CA  . VAL A 1 94  ? -13.82000 -3.50600  -20.81300 1.000 21.40053 ? 94  VAL A CA  1 
ATOM   692  C  C   . VAL A 1 94  ? -13.01700 -2.81500  -19.71100 1.000 20.37959 ? 94  VAL A C   1 
ATOM   693  O  O   . VAL A 1 94  ? -13.58700 -2.33300  -18.72200 1.000 21.50813 ? 94  VAL A O   1 
ATOM   694  C  CB  . VAL A 1 94  ? -14.58100 -2.50900  -21.70900 1.000 23.45070 ? 94  VAL A CB  1 
ATOM   695  C  CG1 . VAL A 1 94  ? -13.69200 -1.38600  -22.17400 1.000 25.47006 ? 94  VAL A CG1 1 
ATOM   696  C  CG2 . VAL A 1 94  ? -15.21000 -3.24800  -22.90100 1.000 24.50545 ? 94  VAL A CG2 1 
ATOM   697  N  N   . ASN A 1 95  ? -11.69600 -2.80600  -19.85100 1.000 23.81528 ? 95  ASN A N   1 
ATOM   698  C  CA  . ASN A 1 95  ? -10.83100 -2.16100  -18.86500 1.000 24.29759 ? 95  ASN A CA  1 
ATOM   699  C  C   . ASN A 1 95  ? -10.65600 -0.70300  -19.28300 1.000 23.63677 ? 95  ASN A C   1 
ATOM   700  O  O   . ASN A 1 95  ? -9.64500  -0.30000  -19.85800 1.000 27.19764 ? 95  ASN A O   1 
ATOM   701  C  CB  . ASN A 1 95  ? -9.49900  -2.90100  -18.77200 1.000 32.02831 ? 95  ASN A CB  1 
ATOM   702  C  CG  . ASN A 1 95  ? -8.43100  -2.12000  -18.00600 1.000 39.05672 ? 95  ASN A CG  1 
ATOM   703  O  OD1 . ASN A 1 95  ? -8.70000  -1.51500  -16.97300 1.000 38.73479 ? 95  ASN A OD1 1 
ATOM   704  N  ND2 . ASN A 1 95  ? -7.20700  -2.11400  -18.54000 1.000 43.19534 ? 95  ASN A ND2 1 
ATOM   705  N  N   . LYS A 1 96  ? -11.72900 0.06800   -19.08600 1.000 19.51686 ? 96  LYS A N   1 
ATOM   706  C  CA  . LYS A 1 96  ? -11.69400 1.48100   -19.42000 1.000 18.61158 ? 96  LYS A CA  1 
ATOM   707  C  C   . LYS A 1 96  ? -12.51900 2.26300   -18.40900 1.000 16.34849 ? 96  LYS A C   1 
ATOM   708  O  O   . LYS A 1 96  ? -13.61100 1.83000   -17.99700 1.000 17.34898 ? 96  LYS A O   1 
ATOM   709  C  CB  . LYS A 1 96  ? -12.25400 1.77000   -20.82000 1.000 19.93692 ? 96  LYS A CB  1 
ATOM   710  C  CG  . LYS A 1 96  ? -11.45500 1.20400   -21.99400 1.000 20.85377 ? 96  LYS A CG  1 
ATOM   711  C  CD  . LYS A 1 96  ? -10.24200 2.04700   -22.29600 1.000 20.91658 ? 96  LYS A CD  1 
ATOM   712  C  CE  . LYS A 1 96  ? -9.71100  1.75700   -23.72200 1.000 23.55224 ? 96  LYS A CE  1 
ATOM   713  N  NZ  . LYS A 1 96  ? -10.54900 2.35400   -24.82900 1.000 28.10065 ? 96  LYS A NZ  1 
ATOM   714  N  N   . SER A 1 97  ? -11.99800 3.43200   -18.05000 1.000 17.83770 ? 97  SER A N   1 
ATOM   715  C  CA  . SER A 1 97  ? -12.77300 4.43100   -17.34100 1.000 16.41662 ? 97  SER A CA  1 
ATOM   716  C  C   . SER A 1 97  ? -13.91000 4.91400   -18.23100 1.000 17.03366 ? 97  SER A C   1 
ATOM   717  O  O   . SER A 1 97  ? -13.87100 4.77500   -19.45400 1.000 17.19637 ? 97  SER A O   1 
ATOM   718  C  CB  . SER A 1 97  ? -11.87900 5.61800   -16.96500 1.000 16.15462 ? 97  SER A CB  1 
ATOM   719  O  OG  . SER A 1 97  ? -11.42900 6.27600   -18.14600 1.000 16.76842 ? 97  SER A OG  1 
ATOM   720  N  N   . VAL A 1 98  ? -14.93600 5.49300   -17.60200 1.000 15.89615 ? 98  VAL A N   1 
ATOM   721  C  CA  . VAL A 1 98  ? -15.98300 6.16400   -18.37600 1.000 17.01405 ? 98  VAL A CA  1 
ATOM   722  C  C   . VAL A 1 98  ? -15.36400 7.14100   -19.37100 1.000 16.00765 ? 98  VAL A C   1 
ATOM   723  O  O   . VAL A 1 98  ? -15.73000 7.16900   -20.55900 1.000 16.27563 ? 98  VAL A O   1 
ATOM   724  C  CB  . VAL A 1 98  ? -16.96100 6.87400   -17.43100 1.000 15.82585 ? 98  VAL A CB  1 
ATOM   725  C  CG1 . VAL A 1 98  ? -17.99300 7.67100   -18.25600 1.000 15.68102 ? 98  VAL A CG1 1 
ATOM   726  C  CG2 . VAL A 1 98  ? -17.67100 5.83700   -16.55300 1.000 14.52744 ? 98  VAL A CG2 1 
ATOM   727  N  N   . GLU A 1 99  ? -14.39600 7.94500   -18.90200 1.000 17.50897 ? 99  GLU A N   1 
ATOM   728  C  CA  . GLU A 1 99  ? -13.76300 8.96700   -19.73800 1.000 18.44071 ? 99  GLU A CA  1 
ATOM   729  C  C   . GLU A 1 99  ? -13.16400 8.37300   -21.01500 1.000 18.69184 ? 99  GLU A C   1 
ATOM   730  O  O   . GLU A 1 99  ? -13.23900 8.98200   -22.09000 1.000 19.61088 ? 99  GLU A O   1 
ATOM   731  C  CB  . GLU A 1 99  ? -12.67100 9.68300   -18.93600 1.000 19.93900 ? 99  GLU A CB  1 
ATOM   732  C  CG  . GLU A 1 99  ? -12.10000 10.86900  -19.66600 1.000 22.00919 ? 99  GLU A CG  1 
ATOM   733  C  CD  . GLU A 1 99  ? -10.77300 11.34900  -19.11500 1.000 22.12872 ? 99  GLU A CD  1 
ATOM   734  O  OE1 . GLU A 1 99  ? -10.07400 10.61200  -18.36700 1.000 21.10524 ? 99  GLU A OE1 1 
ATOM   735  O  OE2 . GLU A 1 99  ? -10.41000 12.48200  -19.46800 1.000 23.66138 ? 99  GLU A OE2 1 
ATOM   736  N  N   . GLU A 1 100 ? -12.57800 7.18200   -20.91600 1.000 17.71746 ? 100 GLU A N   1 
ATOM   737  C  CA  . GLU A 1 100 ? -11.83000 6.57300   -22.00400 1.000 18.24505 ? 100 GLU A CA  1 
ATOM   738  C  C   . GLU A 1 100 ? -12.59300 5.47300   -22.71800 1.000 18.72621 ? 100 GLU A C   1 
ATOM   739  O  O   . GLU A 1 100 ? -12.02200 4.79400   -23.56800 1.000 21.19175 ? 100 GLU A O   1 
ATOM   740  C  CB  . GLU A 1 100 ? -10.49300 6.03300   -21.47600 1.000 20.83030 ? 100 GLU A CB  1 
ATOM   741  C  CG  . GLU A 1 100 ? -9.65700  7.14600   -20.85300 1.000 24.75379 ? 100 GLU A CG  1 
ATOM   742  C  CD  . GLU A 1 100 ? -8.25600  6.71500   -20.47700 1.000 32.29867 ? 100 GLU A CD  1 
ATOM   743  O  OE1 . GLU A 1 100 ? -8.01300  5.50100   -20.30400 1.000 34.29183 ? 100 GLU A OE1 1 
ATOM   744  O  OE2 . GLU A 1 100 ? -7.38900  7.61100   -20.35400 1.000 34.92346 ? 100 GLU A OE2 1 
ATOM   745  N  N   . THR A 1 101 ? -13.88500 5.31800   -22.44800 1.000 16.85214 ? 101 THR A N   1 
ATOM   746  C  CA  . THR A 1 101 ? -14.67100 4.29300   -23.12000 1.000 16.66435 ? 101 THR A CA  1 
ATOM   747  C  C   . THR A 1 101 ? -15.09100 4.78900   -24.50300 1.000 18.52729 ? 101 THR A C   1 
ATOM   748  O  O   . THR A 1 101 ? -15.71400 5.85100   -24.61800 1.000 19.07260 ? 101 THR A O   1 
ATOM   749  C  CB  . THR A 1 101 ? -15.90300 3.96500   -22.27200 1.000 16.03105 ? 101 THR A CB  1 
ATOM   750  O  OG1 . THR A 1 101 ? -15.50300 3.47100   -20.97500 1.000 15.97069 ? 101 THR A OG1 1 
ATOM   751  C  CG2 . THR A 1 101 ? -16.76000 2.91400   -22.94300 1.000 16.32612 ? 101 THR A CG2 1 
ATOM   752  N  N   . THR A 1 102 ? -14.76300 4.03600   -25.55200 1.000 18.88201 ? 102 THR A N   1 
ATOM   753  C  CA  . THR A 1 102 ? -15.28700 4.40900   -26.85800 1.000 17.96434 ? 102 THR A CA  1 
ATOM   754  C  C   . THR A 1 102 ? -16.74600 3.98600   -26.95300 1.000 17.59241 ? 102 THR A C   1 
ATOM   755  O  O   . THR A 1 102 ? -17.20300 3.09300   -26.24000 1.000 17.03198 ? 102 THR A O   1 
ATOM   756  C  CB  . THR A 1 102 ? -14.50100 3.76500   -28.00700 1.000 20.76400 ? 102 THR A CB  1 
ATOM   757  O  OG1 . THR A 1 102 ? -14.79100 2.36200   -28.06800 1.000 20.94224 ? 102 THR A OG1 1 
ATOM   758  C  CG2 . THR A 1 102 ? -13.01000 3.96900   -27.82000 1.000 21.67091 ? 102 THR A CG2 1 
ATOM   759  N  N   . THR A 1 103 ? -17.48000 4.63800   -27.86000 1.000 17.96652 ? 103 THR A N   1 
ATOM   760  C  CA  . THR A 1 103 ? -18.87900 4.26200   -28.00300 1.000 17.97683 ? 103 THR A CA  1 
ATOM   761  C  C   . THR A 1 103 ? -19.02200 2.83400   -28.51000 1.000 17.59835 ? 103 THR A C   1 
ATOM   762  O  O   . THR A 1 103 ? -19.95500 2.13300   -28.10300 1.000 17.28185 ? 103 THR A O   1 
ATOM   763  C  CB  . THR A 1 103 ? -19.57700 5.26700   -28.90300 1.000 19.04876 ? 103 THR A CB  1 
ATOM   764  O  OG1 . THR A 1 103 ? -19.46000 6.55500   -28.29300 1.000 19.85828 ? 103 THR A OG1 1 
ATOM   765  C  CG2 . THR A 1 103 ? -21.05800 4.93400   -29.06200 1.000 21.06415 ? 103 THR A CG2 1 
ATOM   766  N  N   . ALA A 1 104 ? -18.09300 2.37300   -29.36100 1.000 19.06996 ? 104 ALA A N   1 
ATOM   767  C  CA  . ALA A 1 104 ? -18.14700 0.98500   -29.80800 1.000 19.67383 ? 104 ALA A CA  1 
ATOM   768  C  C   . ALA A 1 104 ? -17.97700 0.02500   -28.64200 1.000 20.07852 ? 104 ALA A C   1 
ATOM   769  O  O   . ALA A 1 104 ? -18.67200 -0.99300  -28.57100 1.000 20.13215 ? 104 ALA A O   1 
ATOM   770  C  CB  . ALA A 1 104 ? -17.07500 0.72100   -30.87400 1.000 20.94132 ? 104 ALA A CB  1 
ATOM   771  N  N   . GLU A 1 105 ? -17.06400 0.34100   -27.71000 1.000 20.03681 ? 105 GLU A N   1 
ATOM   772  C  CA  . GLU A 1 105 ? -16.88300 -0.48700  -26.52100 1.000 18.19775 ? 105 GLU A CA  1 
ATOM   773  C  C   . GLU A 1 105 ? -18.13200 -0.47400  -25.66100 1.000 17.41208 ? 105 GLU A C   1 
ATOM   774  O  O   . GLU A 1 105 ? -18.56700 -1.51100  -25.15600 1.000 19.47528 ? 105 GLU A O   1 
ATOM   775  C  CB  . GLU A 1 105 ? -15.69400 0.01500   -25.68600 1.000 19.85309 ? 105 GLU A CB  1 
ATOM   776  C  CG  . GLU A 1 105 ? -14.34900 -0.36700  -26.25600 1.000 20.53885 ? 105 GLU A CG  1 
ATOM   777  C  CD  . GLU A 1 105 ? -13.20600 0.43200   -25.66200 1.000 24.23808 ? 105 GLU A CD  1 
ATOM   778  O  OE1 . GLU A 1 105 ? -13.42400 1.54000   -25.10700 1.000 23.42103 ? 105 GLU A OE1 1 
ATOM   779  O  OE2 . GLU A 1 105 ? -12.06500 -0.05700  -25.77200 1.000 24.84005 ? 105 GLU A OE2 1 
ATOM   780  N  N   . TRP A 1 106 ? -18.69300 0.71300   -25.46300 1.000 17.69395 ? 106 TRP A N   1 
ATOM   781  C  CA  . TRP A 1 106 ? -19.92300 0.87300   -24.69500 1.000 17.98753 ? 106 TRP A CA  1 
ATOM   782  C  C   . TRP A 1 106 ? -21.04400 -0.00000  -25.26400 1.000 17.22393 ? 106 TRP A C   1 
ATOM   783  O  O   . TRP A 1 106 ? -21.69500 -0.76100  -24.53500 1.000 17.17376 ? 106 TRP A O   1 
ATOM   784  C  CB  . TRP A 1 106 ? -20.29300 2.36000   -24.72700 1.000 17.82401 ? 106 TRP A CB  1 
ATOM   785  C  CG  . TRP A 1 106 ? -21.58500 2.74700   -24.06800 1.000 18.12029 ? 106 TRP A CG  1 
ATOM   786  C  CD1 . TRP A 1 106 ? -22.76000 3.03700   -24.69600 1.000 19.06058 ? 106 TRP A CD1 1 
ATOM   787  C  CD2 . TRP A 1 106 ? -21.80800 2.96400   -22.66600 1.000 18.37286 ? 106 TRP A CD2 1 
ATOM   788  N  NE1 . TRP A 1 106 ? -23.70800 3.39700   -23.77300 1.000 18.10648 ? 106 TRP A NE1 1 
ATOM   789  C  CE2 . TRP A 1 106 ? -23.15600 3.34800   -22.51800 1.000 16.90497 ? 106 TRP A CE2 1 
ATOM   790  C  CE3 . TRP A 1 106 ? -20.99900 2.86600   -21.52000 1.000 18.30814 ? 106 TRP A CE3 1 
ATOM   791  C  CZ2 . TRP A 1 106 ? -23.71600 3.64000   -21.26700 1.000 15.72402 ? 106 TRP A CZ2 1 
ATOM   792  C  CZ3 . TRP A 1 106 ? -21.55800 3.14600   -20.27300 1.000 17.20618 ? 106 TRP A CZ3 1 
ATOM   793  C  CH2 . TRP A 1 106 ? -22.91800 3.52400   -20.16200 1.000 17.08386 ? 106 TRP A CH2 1 
ATOM   794  N  N   . ARG A 1 107 ? -21.27500 0.09200   -26.57500 1.000 18.41567 ? 107 ARG A N   1 
ATOM   795  C  CA  . ARG A 1 107 ? -22.38200 -0.64800  -27.16600 1.000 18.08471 ? 107 ARG A CA  1 
ATOM   796  C  C   . ARG A 1 107 ? -22.13100 -2.14800  -27.16100 1.000 19.02680 ? 107 ARG A C   1 
ATOM   797  O  O   . ARG A 1 107 ? -23.07000 -2.93400  -26.97300 1.000 19.75723 ? 107 ARG A O   1 
ATOM   798  C  CB  . ARG A 1 107 ? -22.63000 -0.15200  -28.58800 1.000 19.78922 ? 107 ARG A CB  1 
ATOM   799  C  CG  . ARG A 1 107 ? -23.09100 1.28400   -28.63700 1.000 23.29958 ? 107 ARG A CG  1 
ATOM   800  C  CD  . ARG A 1 107 ? -23.96300 1.52300   -29.87100 1.000 28.14327 ? 107 ARG A CD  1 
ATOM   801  N  NE  . ARG A 1 107 ? -24.09500 2.93500   -30.23200 1.000 31.89068 ? 107 ARG A NE  1 
ATOM   802  C  CZ  . ARG A 1 107 ? -24.98600 3.76800   -29.71200 1.000 35.23991 ? 107 ARG A CZ  1 
ATOM   803  N  NH1 . ARG A 1 107 ? -25.84300 3.33700   -28.79600 1.000 36.35823 ? 107 ARG A NH1 1 
ATOM   804  N  NH2 . ARG A 1 107 ? -25.02100 5.03400   -30.11100 1.000 35.79640 ? 107 ARG A NH2 1 
ATOM   805  N  N   . LYS A 1 108 ? -20.87900 -2.56800  -27.39300 1.000 18.56286 ? 108 LYS A N   1 
ATOM   806  C  CA  . LYS A 1 108 ? -20.57000 -3.99500  -27.37000 1.000 19.24476 ? 108 LYS A CA  1 
ATOM   807  C  C   . LYS A 1 108 ? -20.80900 -4.59300  -25.98600 1.000 18.07180 ? 108 LYS A C   1 
ATOM   808  O  O   . LYS A 1 108 ? -21.47500 -5.62900  -25.84700 1.000 19.09867 ? 108 LYS A O   1 
ATOM   809  C  CB  . LYS A 1 108 ? -19.12400 -4.22300  -27.80300 1.000 22.74186 ? 108 LYS A CB  1 
ATOM   810  C  CG  . LYS A 1 108 ? -18.71700 -5.67200  -27.86900 1.000 29.69965 ? 108 LYS A CG  1 
ATOM   811  C  CD  . LYS A 1 108 ? -17.32200 -5.78800  -28.49000 1.000 35.84415 ? 108 LYS A CD  1 
ATOM   812  C  CE  . LYS A 1 108 ? -16.24700 -5.04600  -27.65500 1.000 39.46502 ? 108 LYS A CE  1 
ATOM   813  N  NZ  . LYS A 1 108 ? -15.26100 -4.22300  -28.44300 1.000 41.58363 ? 108 LYS A NZ  1 
ATOM   814  N  N   . LEU A 1 109 ? -20.29300 -3.94200  -24.94300 1.000 17.21547 ? 109 LEU A N   1 
ATOM   815  C  CA  . LEU A 1 109 ? -20.47200 -4.46400  -23.59600 1.000 15.56339 ? 109 LEU A CA  1 
ATOM   816  C  C   . LEU A 1 109 ? -21.94900 -4.49300  -23.21700 1.000 17.42845 ? 109 LEU A C   1 
ATOM   817  O  O   . LEU A 1 109 ? -22.43000 -5.48200  -22.66100 1.000 17.87299 ? 109 LEU A O   1 
ATOM   818  C  CB  . LEU A 1 109 ? -19.65500 -3.63700  -22.59500 1.000 16.56387 ? 109 LEU A CB  1 
ATOM   819  C  CG  . LEU A 1 109 ? -19.72300 -4.16800  -21.14900 1.000 16.42196 ? 109 LEU A CG  1 
ATOM   820  C  CD1 . LEU A 1 109 ? -18.37500 -3.97600  -20.43700 1.000 16.39187 ? 109 LEU A CD1 1 
ATOM   821  C  CD2 . LEU A 1 109 ? -20.84100 -3.49600  -20.34200 1.000 17.16605 ? 109 LEU A CD2 1 
ATOM   822  N  N   . LEU A 1 110 ? -22.67800 -3.41100  -23.50500 1.000 15.53469 ? 110 LEU A N   1 
ATOM   823  C  CA  . LEU A 1 110 ? -24.08400 -3.36700  -23.11400 1.000 17.98856 ? 110 LEU A CA  1 
ATOM   824  C  C   . LEU A 1 110 ? -24.90100 -4.38600  -23.89300 1.000 17.47950 ? 110 LEU A C   1 
ATOM   825  O  O   . LEU A 1 110 ? -25.88600 -4.92300  -23.36100 1.000 17.31750 ? 110 LEU A O   1 
ATOM   826  C  CB  . LEU A 1 110 ? -24.64100 -1.95500  -23.30100 1.000 18.45859 ? 110 LEU A CB  1 
ATOM   827  C  CG  . LEU A 1 110 ? -24.16300 -0.88200  -22.30200 1.000 20.38515 ? 110 LEU A CG  1 
ATOM   828  C  CD1 . LEU A 1 110 ? -24.81100 0.44800   -22.65000 1.000 23.16749 ? 110 LEU A CD1 1 
ATOM   829  C  CD2 . LEU A 1 110 ? -24.43200 -1.27300  -20.85800 1.000 20.02139 ? 110 LEU A CD2 1 
ATOM   830  N  N   . ALA A 1 111 ? -24.50100 -4.69000  -25.13400 1.000 16.09973 ? 111 ALA A N   1 
ATOM   831  C  CA  . ALA A 1 111 ? -25.24200 -5.69100  -25.90100 1.000 15.85887 ? 111 ALA A CA  1 
ATOM   832  C  C   . ALA A 1 111 ? -25.21600 -7.04800  -25.20100 1.000 17.12913 ? 111 ALA A C   1 
ATOM   833  O  O   . ALA A 1 111 ? -26.23300 -7.74200  -25.13300 1.000 18.20400 ? 111 ALA A O   1 
ATOM   834  C  CB  . ALA A 1 111 ? -24.68900 -5.78700  -27.32800 1.000 17.49833 ? 111 ALA A CB  1 
ATOM   835  N  N   . VAL A 1 112 ? -24.06300 -7.43700  -24.66100 1.000 16.89178 ? 112 VAL A N   1 
ATOM   836  C  CA  . VAL A 1 112 ? -23.96900 -8.71400  -23.96600 1.000 16.93447 ? 112 VAL A CA  1 
ATOM   837  C  C   . VAL A 1 112 ? -24.52800 -8.62000  -22.55300 1.000 15.85230 ? 112 VAL A C   1 
ATOM   838  O  O   . VAL A 1 112 ? -25.38800 -9.41700  -22.15500 1.000 17.55130 ? 112 VAL A O   1 
ATOM   839  C  CB  . VAL A 1 112 ? -22.50600 -9.18600  -23.94200 1.000 17.01293 ? 112 VAL A CB  1 
ATOM   840  C  CG1 . VAL A 1 112 ? -22.40400 -10.47800 -23.14900 1.000 18.03641 ? 112 VAL A CG1 1 
ATOM   841  C  CG2 . VAL A 1 112 ? -21.97800 -9.34100  -25.36800 1.000 19.70638 ? 112 VAL A CG2 1 
ATOM   842  N  N   . ASN A 1 113 ? -24.04000 -7.65300  -21.76900 1.000 15.80949 ? 113 ASN A N   1 
ATOM   843  C  CA  . ASN A 1 113 ? -24.26100 -7.63300  -20.32300 1.000 13.90513 ? 113 ASN A CA  1 
ATOM   844  C  C   . ASN A 1 113 ? -25.63100 -7.10100  -19.94600 1.000 16.59363 ? 113 ASN A C   1 
ATOM   845  O  O   . ASN A 1 113 ? -26.12800 -7.42100  -18.86300 1.000 17.94735 ? 113 ASN A O   1 
ATOM   846  C  CB  . ASN A 1 113 ? -23.22400 -6.73700  -19.63300 1.000 14.33189 ? 113 ASN A CB  1 
ATOM   847  C  CG  . ASN A 1 113 ? -21.82300 -7.30700  -19.64000 1.000 16.64113 ? 113 ASN A CG  1 
ATOM   848  O  OD1 . ASN A 1 113 ? -21.48100 -8.21300  -20.40200 1.000 16.75857 ? 113 ASN A OD1 1 
ATOM   849  N  ND2 . ASN A 1 113 ? -20.98900 -6.76000  -18.77000 1.000 16.78822 ? 113 ASN A ND2 1 
ATOM   850  N  N   . LEU A 1 114 ? -26.20300 -6.22300  -20.76600 1.000 16.88651 ? 114 LEU A N   1 
ATOM   851  C  CA  . LEU A 1 114 ? -27.48700 -5.61700  -20.44700 1.000 15.27178 ? 114 LEU A CA  1 
ATOM   852  C  C   . LEU A 1 114 ? -28.57600 -6.10500  -21.39000 1.000 15.48364 ? 114 LEU A C   1 
ATOM   853  O  O   . LEU A 1 114 ? -29.55700 -6.69500  -20.92100 1.000 15.67143 ? 114 LEU A O   1 
ATOM   854  C  CB  . LEU A 1 114 ? -27.38000 -4.08900  -20.47400 1.000 15.90583 ? 114 LEU A CB  1 
ATOM   855  C  CG  . LEU A 1 114 ? -28.68900 -3.33100  -20.21000 1.000 18.00208 ? 114 LEU A CG  1 
ATOM   856  C  CD1 . LEU A 1 114 ? -29.36100 -3.86200  -18.96600 1.000 15.85504 ? 114 LEU A CD1 1 
ATOM   857  C  CD2 . LEU A 1 114 ? -28.40700 -1.84000  -20.09500 1.000 18.46973 ? 114 LEU A CD2 1 
ATOM   858  N  N   . ASP A 1 115 ? -28.41700 -5.91100  -22.70900 1.000 15.00206 ? 115 ASP A N   1 
ATOM   859  C  CA  . ASP A 1 115 ? -29.42800 -6.41400  -23.64300 1.000 14.56859 ? 115 ASP A CA  1 
ATOM   860  C  C   . ASP A 1 115 ? -29.59900 -7.91900  -23.47800 1.000 15.93606 ? 115 ASP A C   1 
ATOM   861  O  O   . ASP A 1 115 ? -30.72600 -8.43500  -23.44200 1.000 17.65139 ? 115 ASP A O   1 
ATOM   862  C  CB  . ASP A 1 115 ? -29.06200 -6.11000  -25.10100 1.000 16.19730 ? 115 ASP A CB  1 
ATOM   863  C  CG  . ASP A 1 115 ? -29.05100 -4.64100  -25.43300 1.000 19.70131 ? 115 ASP A CG  1 
ATOM   864  O  OD1 . ASP A 1 115 ? -29.54200 -3.81100  -24.64100 1.000 21.13659 ? 115 ASP A OD1 1 
ATOM   865  O  OD2 . ASP A 1 115 ? -28.50000 -4.31500  -26.51800 1.000 23.59380 ? 115 ASP A OD2 1 
ATOM   866  N  N   . GLY A 1 116 ? -28.49000 -8.64700  -23.37300 1.000 17.48232 ? 116 GLY A N   1 
ATOM   867  C  CA  . GLY A 1 116 ? -28.59900 -10.09100 -23.27000 1.000 18.27488 ? 116 GLY A CA  1 
ATOM   868  C  C   . GLY A 1 116 ? -29.37500 -10.54500 -22.04500 1.000 17.30673 ? 116 GLY A C   1 
ATOM   869  O  O   . GLY A 1 116 ? -30.16300 -11.49500 -22.12100 1.000 16.72933 ? 116 GLY A O   1 
ATOM   870  N  N   . VAL A 1 117 ? -29.14100 -9.89400  -20.89600 1.000 15.82355 ? 117 VAL A N   1 
ATOM   871  C  CA  . VAL A 1 117 ? -29.83600 -10.26500 -19.66700 1.000 15.41058 ? 117 VAL A CA  1 
ATOM   872  C  C   . VAL A 1 117 ? -31.30600 -9.86500  -19.75600 1.000 15.43337 ? 117 VAL A C   1 
ATOM   873  O  O   . VAL A 1 117 ? -32.19100 -10.59100 -19.29200 1.000 16.12225 ? 117 VAL A O   1 
ATOM   874  C  CB  . VAL A 1 117 ? -29.14400 -9.63700  -18.45100 1.000 16.12414 ? 117 VAL A CB  1 
ATOM   875  C  CG1 . VAL A 1 117 ? -29.92200 -9.96100  -17.19400 1.000 15.41093 ? 117 VAL A CG1 1 
ATOM   876  C  CG2 . VAL A 1 117 ? -27.72000 -10.19000 -18.33800 1.000 18.20340 ? 117 VAL A CG2 1 
ATOM   877  N  N   . PHE A 1 118 ? -31.58800 -8.71800  -20.38200 1.000 14.62802 ? 118 PHE A N   1 
ATOM   878  C  CA  . PHE A 1 118 ? -32.97300 -8.33200  -20.64600 1.000 14.94792 ? 118 PHE A CA  1 
ATOM   879  C  C   . PHE A 1 118 ? -33.66100 -9.35100  -21.55500 1.000 15.58703 ? 118 PHE A C   1 
ATOM   880  O  O   . PHE A 1 118 ? -34.77400 -9.80000  -21.25000 1.000 15.59187 ? 118 PHE A O   1 
ATOM   881  C  CB  . PHE A 1 118 ? -33.01200 -6.91900  -21.24800 1.000 14.68443 ? 118 PHE A CB  1 
ATOM   882  C  CG  . PHE A 1 118 ? -34.32900 -6.56700  -21.93900 1.000 16.23220 ? 118 PHE A CG  1 
ATOM   883  C  CD1 . PHE A 1 118 ? -35.49100 -6.40900  -21.19000 1.000 16.42859 ? 118 PHE A CD1 1 
ATOM   884  C  CD2 . PHE A 1 118 ? -34.38800 -6.40300  -23.32200 1.000 15.26271 ? 118 PHE A CD2 1 
ATOM   885  C  CE1 . PHE A 1 118 ? -36.68700 -6.09300  -21.79400 1.000 16.42628 ? 118 PHE A CE1 1 
ATOM   886  C  CE2 . PHE A 1 118 ? -35.57900 -6.08200  -23.94000 1.000 16.61411 ? 118 PHE A CE2 1 
ATOM   887  C  CZ  . PHE A 1 118 ? -36.74100 -5.93300  -23.16800 1.000 17.00625 ? 118 PHE A CZ  1 
ATOM   888  N  N   . PHE A 1 119 ? -33.01800 -9.73600  -22.67300 1.000 15.94901 ? 119 PHE A N   1 
ATOM   889  C  CA  . PHE A 1 119 ? -33.64200 -10.71400 -23.57200 1.000 16.99474 ? 119 PHE A CA  1 
ATOM   890  C  C   . PHE A 1 119 ? -33.93900 -12.02800 -22.85100 1.000 16.95463 ? 119 PHE A C   1 
ATOM   891  O  O   . PHE A 1 119 ? -34.99700 -12.63800 -23.05700 1.000 17.79065 ? 119 PHE A O   1 
ATOM   892  C  CB  . PHE A 1 119 ? -32.75300 -11.02800 -24.79100 1.000 16.28867 ? 119 PHE A CB  1 
ATOM   893  C  CG  . PHE A 1 119 ? -32.52800 -9.86600  -25.73300 1.000 16.92902 ? 119 PHE A CG  1 
ATOM   894  C  CD1 . PHE A 1 119 ? -33.50500 -8.89500  -25.94500 1.000 17.38139 ? 119 PHE A CD1 1 
ATOM   895  C  CD2 . PHE A 1 119 ? -31.29200 -9.74500  -26.40000 1.000 17.38486 ? 119 PHE A CD2 1 
ATOM   896  C  CE1 . PHE A 1 119 ? -33.26700 -7.82400  -26.82200 1.000 17.90735 ? 119 PHE A CE1 1 
ATOM   897  C  CE2 . PHE A 1 119 ? -31.05100 -8.66800  -27.26800 1.000 18.12572 ? 119 PHE A CE2 1 
ATOM   898  C  CZ  . PHE A 1 119 ? -32.03600 -7.71400  -27.47300 1.000 18.29121 ? 119 PHE A CZ  1 
ATOM   899  N  N   . GLY A 1 120 ? -32.99500 -12.51000 -22.05100 1.000 16.32690 ? 120 GLY A N   1 
ATOM   900  C  CA  . GLY A 1 120 ? -33.21400 -13.76100 -21.35000 1.000 15.21604 ? 120 GLY A CA  1 
ATOM   901  C  C   . GLY A 1 120 ? -34.26000 -13.63800 -20.25600 1.000 15.74933 ? 120 GLY A C   1 
ATOM   902  O  O   . GLY A 1 120 ? -35.08000 -14.54000 -20.06700 1.000 16.80342 ? 120 GLY A O   1 
ATOM   903  N  N   . THR A 1 121 ? -34.22100 -12.53800 -19.49400 1.000 14.55448 ? 121 THR A N   1 
ATOM   904  C  CA  . THR A 1 121 ? -35.22600 -12.34000 -18.44900 1.000 15.05697 ? 121 THR A CA  1 
ATOM   905  C  C   . THR A 1 121 ? -36.62300 -12.20900 -19.04100 1.000 15.36562 ? 121 THR A C   1 
ATOM   906  O  O   . THR A 1 121 ? -37.56600 -12.85900 -18.57500 1.000 17.52917 ? 121 THR A O   1 
ATOM   907  C  CB  . THR A 1 121 ? -34.88700 -11.10900 -17.61100 1.000 14.20372 ? 121 THR A CB  1 
ATOM   908  O  OG1 . THR A 1 121 ? -33.56600 -11.27800 -17.03700 1.000 16.03384 ? 121 THR A OG1 1 
ATOM   909  C  CG2 . THR A 1 121 ? -35.88800 -10.94700 -16.45900 1.000 12.79523 ? 121 THR A CG2 1 
ATOM   910  N  N   . ARG A 1 122 ? -36.77600 -11.36400 -20.06800 1.000 14.90526 ? 122 ARG A N   1 
ATOM   911  C  CA  . ARG A 1 122 ? -38.08400 -11.18300 -20.69300 1.000 16.15325 ? 122 ARG A CA  1 
ATOM   912  C  C   . ARG A 1 122 ? -38.62600 -12.50200 -21.23500 1.000 16.40562 ? 122 ARG A C   1 
ATOM   913  O  O   . ARG A 1 122 ? -39.77600 -12.87600 -20.95900 1.000 17.57239 ? 122 ARG A O   1 
ATOM   914  C  CB  . ARG A 1 122 ? -37.98600 -10.14300 -21.80900 1.000 15.91404 ? 122 ARG A CB  1 
ATOM   915  C  CG  . ARG A 1 122 ? -39.31000 -9.86700  -22.50900 1.000 16.31885 ? 122 ARG A CG  1 
ATOM   916  C  CD  . ARG A 1 122 ? -39.12100 -8.89600  -23.67700 1.000 16.96704 ? 122 ARG A CD  1 
ATOM   917  N  NE  . ARG A 1 122 ? -38.27000 -9.48700  -24.70800 1.000 17.36674 ? 122 ARG A NE  1 
ATOM   918  C  CZ  . ARG A 1 122 ? -37.82800 -8.84600  -25.78000 1.000 20.01304 ? 122 ARG A CZ  1 
ATOM   919  N  NH1 . ARG A 1 122 ? -38.14500 -7.57700  -25.99400 1.000 17.66268 ? 122 ARG A NH1 1 
ATOM   920  N  NH2 . ARG A 1 122 ? -37.05700 -9.50000  -26.64200 1.000 19.09959 ? 122 ARG A NH2 1 
ATOM   921  N  N   . LEU A 1 123 ? -37.82000 -13.21300 -22.03000 1.000 16.24333 ? 123 LEU A N   1 
ATOM   922  C  CA  . LEU A 1 123 ? -38.26000 -14.49500 -22.58000 1.000 17.21500 ? 123 LEU A CA  1 
ATOM   923  C  C   . LEU A 1 123 ? -38.51500 -15.52000 -21.47400 1.000 17.97870 ? 123 LEU A C   1 
ATOM   924  O  O   . LEU A 1 123 ? -39.46700 -16.30200 -21.55000 1.000 17.29940 ? 123 LEU A O   1 
ATOM   925  C  CB  . LEU A 1 123 ? -37.20900 -15.02500 -23.55000 1.000 17.44794 ? 123 LEU A CB  1 
ATOM   926  C  CG  . LEU A 1 123 ? -37.46400 -16.36600 -24.23500 1.000 17.59746 ? 123 LEU A CG  1 
ATOM   927  C  CD1 . LEU A 1 123 ? -38.81300 -16.41400 -24.95300 1.000 19.96388 ? 123 LEU A CD1 1 
ATOM   928  C  CD2 . LEU A 1 123 ? -36.36000 -16.64700 -25.22500 1.000 19.23433 ? 123 LEU A CD2 1 
ATOM   929  N  N   . GLY A 1 124 ? -37.63700 -15.56300 -20.46800 1.000 17.44024 ? 124 GLY A N   1 
ATOM   930  C  CA  . GLY A 1 124 ? -37.82600 -16.49300 -19.36100 1.000 14.98337 ? 124 GLY A CA  1 
ATOM   931  C  C   . GLY A 1 124 ? -39.16900 -16.32100 -18.67800 1.000 16.31696 ? 124 GLY A C   1 
ATOM   932  O  O   . GLY A 1 124 ? -39.85300 -17.30100 -18.38500 1.000 18.56471 ? 124 GLY A O   1 
ATOM   933  N  N   . ILE A 1 125 ? -39.54400 -15.07400 -18.37300 1.000 15.09476 ? 125 ILE A N   1 
ATOM   934  C  CA  . ILE A 1 125 ? -40.85700 -14.84000 -17.77000 1.000 14.35415 ? 125 ILE A CA  1 
ATOM   935  C  C   . ILE A 1 125 ? -41.94200 -15.37400 -18.67500 1.000 14.85166 ? 125 ILE A C   1 
ATOM   936  O  O   . ILE A 1 125 ? -42.87700 -16.04100 -18.21600 1.000 17.17692 ? 125 ILE A O   1 
ATOM   937  C  CB  . ILE A 1 125 ? -41.07500 -13.34500 -17.46800 1.000 16.35327 ? 125 ILE A CB  1 
ATOM   938  C  CG1 . ILE A 1 125 ? -40.05600 -12.86000 -16.42700 1.000 17.67639 ? 125 ILE A CG1 1 
ATOM   939  C  CG2 . ILE A 1 125 ? -42.52800 -13.11000 -17.00400 1.000 15.60130 ? 125 ILE A CG2 1 
ATOM   940  C  CD1 . ILE A 1 125 ? -39.95300 -11.36000 -16.33200 1.000 18.38655 ? 125 ILE A CD1 1 
ATOM   941  N  N   . GLN A 1 126 ? -41.85300 -15.07400 -19.97800 1.000 15.84259 ? 126 GLN A N   1 
ATOM   942  C  CA  . GLN A 1 126 ? -42.92700 -15.46500 -20.88900 1.000 17.19173 ? 126 GLN A CA  1 
ATOM   943  C  C   . GLN A 1 126 ? -43.03600 -16.97500 -21.00900 1.000 18.21447 ? 126 GLN A C   1 
ATOM   944  O  O   . GLN A 1 126 ? -44.14400 -17.50500 -21.13400 1.000 21.31604 ? 126 GLN A O   1 
ATOM   945  C  CB  . GLN A 1 126 ? -42.71500 -14.82500 -22.26700 1.000 18.91540 ? 126 GLN A CB  1 
ATOM   946  C  CG  . GLN A 1 126 ? -42.79000 -13.29800 -22.18900 1.000 22.00226 ? 126 GLN A CG  1 
ATOM   947  C  CD  . GLN A 1 126 ? -42.37200 -12.58300 -23.44800 1.000 29.02408 ? 126 GLN A CD  1 
ATOM   948  O  OE1 . GLN A 1 126 ? -41.42800 -12.97500 -24.12700 1.000 30.25396 ? 126 GLN A OE1 1 
ATOM   949  N  NE2 . GLN A 1 126 ? -43.07200 -11.50300 -23.75900 1.000 34.32503 ? 126 GLN A NE2 1 
ATOM   950  N  N   . ARG A 1 127 ? -41.91300 -17.68600 -20.92700 1.000 18.60787 ? 127 ARG A N   1 
ATOM   951  C  CA  . ARG A 1 127 ? -41.90400 -19.13700 -21.08700 1.000 20.52772 ? 127 ARG A CA  1 
ATOM   952  C  C   . ARG A 1 127 ? -42.12400 -19.88800 -19.77900 1.000 18.47044 ? 127 ARG A C   1 
ATOM   953  O  O   . ARG A 1 127 ? -42.62200 -21.02200 -19.80200 1.000 20.04084 ? 127 ARG A O   1 
ATOM   954  C  CB  . ARG A 1 127 ? -40.57100 -19.59400 -21.69000 1.000 21.65295 ? 127 ARG A CB  1 
ATOM   955  C  CG  . ARG A 1 127 ? -40.30900 -19.11400 -23.12400 1.000 24.47336 ? 127 ARG A CG  1 
ATOM   956  C  CD  . ARG A 1 127 ? -40.62000 -20.21300 -24.12400 1.000 23.74114 ? 127 ARG A CD  1 
ATOM   957  N  NE  . ARG A 1 127 ? -40.57500 -19.70700 -25.49200 1.000 21.39021 ? 127 ARG A NE  1 
ATOM   958  C  CZ  . ARG A 1 127 ? -40.07500 -20.37400 -26.52500 1.000 19.78374 ? 127 ARG A CZ  1 
ATOM   959  N  NH1 . ARG A 1 127 ? -39.58800 -21.60700 -26.36800 1.000 20.49764 ? 127 ARG A NH1 1 
ATOM   960  N  NH2 . ARG A 1 127 ? -40.08100 -19.80700 -27.72600 1.000 20.45309 ? 127 ARG A NH2 1 
ATOM   961  N  N   . MET A 1 128 ? -41.74700 -19.31500 -18.64300 1.000 16.33207 ? 128 MET A N   1 
ATOM   962  C  CA  . MET A 1 128 ? -41.81300 -20.07500 -17.40800 1.000 16.29771 ? 128 MET A CA  1 
ATOM   963  C  C   . MET A 1 128 ? -43.03300 -19.73800 -16.54600 1.000 17.00550 ? 128 MET A C   1 
ATOM   964  O  O   . MET A 1 128 ? -43.36500 -20.51900 -15.64600 1.000 20.72496 ? 128 MET A O   1 
ATOM   965  C  CB  . MET A 1 128 ? -40.49800 -19.89500 -16.63200 1.000 21.24731 ? 128 MET A CB  1 
ATOM   966  C  CG  . MET A 1 128 ? -39.31100 -20.32000 -17.53000 1.000 25.55798 ? 128 MET A CG  1 
ATOM   967  S  SD  . MET A 1 128 ? -37.72700 -20.37800 -16.68900 1.000 33.48839 ? 128 MET A SD  1 
ATOM   968  C  CE  . MET A 1 128 ? -37.97100 -18.78000 -15.94100 1.000 14.25876 ? 128 MET A CE  1 
ATOM   969  N  N   . LYS A 1 129 ? -43.72700 -18.63600 -16.81300 1.000 17.39391 ? 129 LYS A N   1 
ATOM   970  C  CA  . LYS A 1 129 ? -44.82600 -18.23700 -15.94000 1.000 19.13419 ? 129 LYS A CA  1 
ATOM   971  C  C   . LYS A 1 129 ? -45.98800 -19.22900 -16.00200 1.000 20.03613 ? 129 LYS A C   1 
ATOM   972  O  O   . LYS A 1 129 ? -46.26100 -19.84100 -17.03400 1.000 20.40163 ? 129 LYS A O   1 
ATOM   973  C  CB  . LYS A 1 129 ? -45.33100 -16.84400 -16.31700 1.000 20.01476 ? 129 LYS A CB  1 
ATOM   974  C  CG  . LYS A 1 129 ? -45.92100 -16.76500 -17.72500 1.000 21.55220 ? 129 LYS A CG  1 
ATOM   975  C  CD  . LYS A 1 129 ? -46.48700 -15.38900 -17.95500 1.000 25.02490 ? 129 LYS A CD  1 
ATOM   976  C  CE  . LYS A 1 129 ? -47.06700 -15.23000 -19.33000 1.000 28.08306 ? 129 LYS A CE  1 
ATOM   977  N  NZ  . LYS A 1 129 ? -47.73100 -13.89400 -19.38600 1.000 29.70506 ? 129 LYS A NZ  1 
ATOM   978  N  N   . ASN A 1 130 ? -46.65700 -19.39400 -14.85800 1.000 20.32214 ? 130 ASN A N   1 
ATOM   979  C  CA  . ASN A 1 130 ? -47.94600 -20.08200 -14.77400 1.000 20.98937 ? 130 ASN A CA  1 
ATOM   980  C  C   . ASN A 1 130 ? -47.85700 -21.56800 -15.11900 1.000 21.93968 ? 130 ASN A C   1 
ATOM   981  O  O   . ASN A 1 130 ? -48.84500 -22.17300 -15.55200 1.000 25.12528 ? 130 ASN A O   1 
ATOM   982  C  CB  . ASN A 1 130 ? -48.98300 -19.38900 -15.66200 1.000 22.79078 ? 130 ASN A CB  1 
ATOM   983  C  CG  . ASN A 1 130 ? -49.21300 -17.95400 -15.25200 1.000 24.75415 ? 130 ASN A CG  1 
ATOM   984  O  OD1 . ASN A 1 130 ? -49.15000 -17.62500 -14.05800 1.000 26.47053 ? 130 ASN A OD1 1 
ATOM   985  N  ND2 . ASN A 1 130 ? -49.49000 -17.09000 -16.22700 1.000 25.71975 ? 130 ASN A ND2 1 
ATOM   986  N  N   . LYS A 1 131 ? -46.69800 -22.18900 -14.91800 1.000 21.70429 ? 131 LYS A N   1 
ATOM   987  C  CA  . LYS A 1 131 ? -46.53300 -23.60000 -15.22300 1.000 22.78927 ? 131 LYS A CA  1 
ATOM   988  C  C   . LYS A 1 131 ? -46.27100 -24.44900 -13.98700 1.000 22.96098 ? 131 LYS A C   1 
ATOM   989  O  O   . LYS A 1 131 ? -46.01600 -25.65200 -14.12100 1.000 25.19356 ? 131 LYS A O   1 
ATOM   990  C  CB  . LYS A 1 131 ? -45.41700 -23.78600 -16.25400 1.000 23.48796 ? 131 LYS A CB  1 
ATOM   991  C  CG  . LYS A 1 131 ? -45.85200 -23.27200 -17.62300 1.000 25.95714 ? 131 LYS A CG  1 
ATOM   992  C  CD  . LYS A 1 131 ? -44.83800 -23.54500 -18.71800 1.000 28.98066 ? 131 LYS A CD  1 
ATOM   993  C  CE  . LYS A 1 131 ? -45.40000 -23.05700 -20.04200 1.000 33.41427 ? 131 LYS A CE  1 
ATOM   994  N  NZ  . LYS A 1 131 ? -44.35800 -22.96700 -21.10300 1.000 35.78148 ? 131 LYS A NZ  1 
ATOM   995  N  N   . GLY A 1 132 ? -46.31500 -23.85600 -12.79800 1.000 22.67059 ? 132 GLY A N   1 
ATOM   996  C  CA  . GLY A 1 132 ? -46.09200 -24.62300 -11.59000 1.000 22.61283 ? 132 GLY A CA  1 
ATOM   997  C  C   . GLY A 1 132 ? -44.70500 -25.21700 -11.50100 1.000 22.53380 ? 132 GLY A C   1 
ATOM   998  O  O   . GLY A 1 132 ? -44.52200 -26.25600 -10.85800 1.000 22.80276 ? 132 GLY A O   1 
ATOM   999  N  N   . LEU A 1 133 ? -43.71800 -24.57800 -12.12100 1.000 21.97435 ? 133 LEU A N   1 
ATOM   1000 C  CA  . LEU A 1 133 ? -42.36300 -25.12400 -12.14500 1.000 19.74938 ? 133 LEU A CA  1 
ATOM   1001 C  C   . LEU A 1 133 ? -41.48600 -24.67800 -10.98000 1.000 17.92831 ? 133 LEU A C   1 
ATOM   1002 O  O   . LEU A 1 133 ? -40.37200 -25.18900 -10.83300 1.000 18.17941 ? 133 LEU A O   1 
ATOM   1003 C  CB  . LEU A 1 133 ? -41.66700 -24.72900 -13.45100 1.000 19.36334 ? 133 LEU A CB  1 
ATOM   1004 C  CG  . LEU A 1 133 ? -42.37900 -25.17700 -14.72700 1.000 22.11418 ? 133 LEU A CG  1 
ATOM   1005 C  CD1 . LEU A 1 133 ? -41.76800 -24.43300 -15.90000 1.000 22.45255 ? 133 LEU A CD1 1 
ATOM   1006 C  CD2 . LEU A 1 133 ? -42.23300 -26.67300 -14.91600 1.000 24.90319 ? 133 LEU A CD2 1 
ATOM   1007 N  N   . GLY A 1 134 ? -41.93900 -23.73500 -10.16900 1.000 16.66321 ? 134 GLY A N   1 
ATOM   1008 C  CA  . GLY A 1 134 ? -41.07600 -23.16300 -9.16100  1.000 16.19208 ? 134 GLY A CA  1 
ATOM   1009 C  C   . GLY A 1 134 ? -39.92900 -22.47500 -9.87000  1.000 17.28509 ? 134 GLY A C   1 
ATOM   1010 O  O   . GLY A 1 134 ? -38.73900 -22.72200 -9.60000  1.000 16.85167 ? 134 GLY A O   1 
ATOM   1011 N  N   . ALA A 1 135 ? -40.27800 -21.60800 -10.81100 1.000 15.19254 ? 135 ALA A N   1 
ATOM   1012 C  CA  . ALA A 1 135 ? -39.27400 -21.08300 -11.72900 1.000 14.59020 ? 135 ALA A CA  1 
ATOM   1013 C  C   . ALA A 1 135 ? -38.41000 -20.00400 -11.07200 1.000 14.81308 ? 135 ALA A C   1 
ATOM   1014 O  O   . ALA A 1 135 ? -38.84800 -19.27100 -10.17600 1.000 16.33545 ? 135 ALA A O   1 
ATOM   1015 C  CB  . ALA A 1 135 ? -39.94000 -20.54300 -13.00200 1.000 15.13818 ? 135 ALA A CB  1 
ATOM   1016 N  N   . SER A 1 136 ? -37.16000 -19.91100 -11.53300 1.000 13.89555 ? 136 SER A N   1 
ATOM   1017 C  CA  . SER A 1 136 ? -36.20000 -19.01600 -10.92400 1.000 13.48686 ? 136 SER A CA  1 
ATOM   1018 C  C   . SER A 1 136 ? -35.28100 -18.46000 -12.00400 1.000 14.98422 ? 136 SER A C   1 
ATOM   1019 O  O   . SER A 1 136 ? -34.70500 -19.23200 -12.77700 1.000 16.03259 ? 136 SER A O   1 
ATOM   1020 C  CB  . SER A 1 136 ? -35.41300 -19.78500 -9.85900  1.000 13.67897 ? 136 SER A CB  1 
ATOM   1021 O  OG  . SER A 1 136 ? -34.50100 -18.93200 -9.19900  1.000 14.94150 ? 136 SER A OG  1 
ATOM   1022 N  N   . ILE A 1 137 ? -35.17400 -17.13100 -12.06500 1.000 13.01831 ? 137 ILE A N   1 
ATOM   1023 C  CA  . ILE A 1 137 ? -34.22700 -16.43700 -12.93900 1.000 13.61846 ? 137 ILE A CA  1 
ATOM   1024 C  C   . ILE A 1 137 ? -33.15500 -15.83300 -12.05100 1.000 13.02131 ? 137 ILE A C   1 
ATOM   1025 O  O   . ILE A 1 137 ? -33.46100 -15.06800 -11.12600 1.000 13.73476 ? 137 ILE A O   1 
ATOM   1026 C  CB  . ILE A 1 137 ? -34.92200 -15.36500 -13.78600 1.000 14.01218 ? 137 ILE A CB  1 
ATOM   1027 C  CG1 . ILE A 1 137 ? -35.95700 -16.03900 -14.70600 1.000 13.20711 ? 137 ILE A CG1 1 
ATOM   1028 C  CG2 . ILE A 1 137 ? -33.90600 -14.58700 -14.62000 1.000 17.26811 ? 137 ILE A CG2 1 
ATOM   1029 C  CD1 . ILE A 1 137 ? -36.86900 -15.04300 -15.47600 1.000 15.34121 ? 137 ILE A CD1 1 
ATOM   1030 N  N   . ILE A 1 138 ? -31.90700 -16.22000 -12.29500 1.000 13.73223 ? 138 ILE A N   1 
ATOM   1031 C  CA  . ILE A 1 138 ? -30.75700 -15.81100 -11.49800 1.000 13.32393 ? 138 ILE A CA  1 
ATOM   1032 C  C   . ILE A 1 138 ? -29.89000 -14.94300 -12.39500 1.000 12.70637 ? 138 ILE A C   1 
ATOM   1033 O  O   . ILE A 1 138 ? -29.28600 -15.45000 -13.35100 1.000 14.36060 ? 138 ILE A O   1 
ATOM   1034 C  CB  . ILE A 1 138 ? -29.99100 -17.03200 -10.97700 1.000 12.51367 ? 138 ILE A CB  1 
ATOM   1035 C  CG1 . ILE A 1 138 ? -30.92700 -17.89700 -10.11800 1.000 16.39916 ? 138 ILE A CG1 1 
ATOM   1036 C  CG2 . ILE A 1 138 ? -28.77200 -16.57200 -10.21100 1.000 13.83523 ? 138 ILE A CG2 1 
ATOM   1037 C  CD1 . ILE A 1 138 ? -30.41800 -19.34000 -9.93700  1.000 18.48339 ? 138 ILE A CD1 1 
ATOM   1038 N  N   . ASN A 1 139 ? -29.86900 -13.63600 -12.14700 1.000 13.41830 ? 139 ASN A N   1 
ATOM   1039 C  CA  . ASN A 1 139 ? -29.11800 -12.73000 -13.00500 1.000 12.65348 ? 139 ASN A CA  1 
ATOM   1040 C  C   . ASN A 1 139 ? -27.78800 -12.42300 -12.35200 1.000 13.55850 ? 139 ASN A C   1 
ATOM   1041 O  O   . ASN A 1 139 ? -27.73500 -11.95700 -11.20600 1.000 13.50480 ? 139 ASN A O   1 
ATOM   1042 C  CB  . ASN A 1 139 ? -29.91400 -11.46500 -13.30500 1.000 15.03050 ? 139 ASN A CB  1 
ATOM   1043 C  CG  . ASN A 1 139 ? -31.04000 -11.75300 -14.27300 1.000 15.46496 ? 139 ASN A CG  1 
ATOM   1044 O  OD1 . ASN A 1 139 ? -30.98200 -12.75000 -14.99500 1.000 14.86043 ? 139 ASN A OD1 1 
ATOM   1045 N  ND2 . ASN A 1 139 ? -32.08500 -10.92900 -14.26100 1.000 14.79583 ? 139 ASN A ND2 1 
ATOM   1046 N  N   . MET A 1 140 ? -26.72600 -12.76400 -13.05100 1.000 14.30072 ? 140 MET A N   1 
ATOM   1047 C  CA  . MET A 1 140 ? -25.39700 -12.52000 -12.53300 1.000 14.86154 ? 140 MET A CA  1 
ATOM   1048 C  C   . MET A 1 140 ? -25.11100 -11.03800 -12.61500 1.000 15.45363 ? 140 MET A C   1 
ATOM   1049 O  O   . MET A 1 140 ? -25.07200 -10.44400 -13.69500 1.000 16.92718 ? 140 MET A O   1 
ATOM   1050 C  CB  . MET A 1 140 ? -24.36700 -13.32500 -13.32700 1.000 17.26260 ? 140 MET A CB  1 
ATOM   1051 C  CG  . MET A 1 140 ? -23.06300 -13.51000 -12.61200 1.000 21.20827 ? 140 MET A CG  1 
ATOM   1052 S  SD  . MET A 1 140 ? -23.21800 -14.51600 -11.10900 1.000 21.14158 ? 140 MET A SD  1 
ATOM   1053 C  CE  . MET A 1 140 ? -23.97600 -16.03700 -11.66500 1.000 22.95709 ? 140 MET A CE  1 
ATOM   1054 N  N   . SER A 1 141 ? -24.90300 -10.42100 -11.47000 1.000 17.45136 ? 141 SER A N   1 
ATOM   1055 C  CA  . SER A 1 141 ? -24.40900 -9.05900  -11.41700 1.000 18.76491 ? 141 SER A CA  1 
ATOM   1056 C  C   . SER A 1 141 ? -22.96500 -9.13800  -10.92100 1.000 20.48905 ? 141 SER A C   1 
ATOM   1057 O  O   . SER A 1 141 ? -22.21100 -9.98200  -11.43200 1.000 24.93276 ? 141 SER A O   1 
ATOM   1058 C  CB  . SER A 1 141 ? -25.35200 -8.19000  -10.59500 1.000 22.47818 ? 141 SER A CB  1 
ATOM   1059 O  OG  . SER A 1 141 ? -24.80600 -6.89300  -10.37400 1.000 23.44750 ? 141 SER A OG  1 
ATOM   1060 N  N   . SER A 1 142 ? -22.58900 -8.39300  -9.90400  1.000 18.84107 ? 142 SER A N   1 
ATOM   1061 C  CA  . SER A 1 142 ? -21.20000 -8.22300  -9.55000  1.000 15.88242 ? 142 SER A CA  1 
ATOM   1062 C  C   . SER A 1 142 ? -21.17800 -7.36900  -8.29500  1.000 15.30525 ? 142 SER A C   1 
ATOM   1063 O  O   . SER A 1 142 ? -22.11800 -6.61200  -8.02400  1.000 14.93101 ? 142 SER A O   1 
ATOM   1064 C  CB  . SER A 1 142 ? -20.43300 -7.54000  -10.68800 1.000 16.87671 ? 142 SER A CB  1 
ATOM   1065 O  OG  . SER A 1 142 ? -19.11700 -7.24300  -10.31300 1.000 16.20163 ? 142 SER A OG  1 
ATOM   1066 N  N   . ILE A 1 143 ? -20.07800 -7.46300  -7.54600  1.000 15.01953 ? 143 ILE A N   1 
ATOM   1067 C  CA  . ILE A 1 143 ? -19.81600 -6.38300  -6.60100  1.000 13.36309 ? 143 ILE A CA  1 
ATOM   1068 C  C   . ILE A 1 143 ? -19.87300 -5.02900  -7.29700  1.000 12.93169 ? 143 ILE A C   1 
ATOM   1069 O  O   . ILE A 1 143 ? -20.18200 -4.01000  -6.66400  1.000 13.21819 ? 143 ILE A O   1 
ATOM   1070 C  CB  . ILE A 1 143 ? -18.46200 -6.58100  -5.89200  1.000 13.14999 ? 143 ILE A CB  1 
ATOM   1071 C  CG1 . ILE A 1 143 ? -17.32900 -6.81400  -6.90500  1.000 14.53372 ? 143 ILE A CG1 1 
ATOM   1072 C  CG2 . ILE A 1 143 ? -18.57200 -7.73300  -4.91900  1.000 15.58914 ? 143 ILE A CG2 1 
ATOM   1073 C  CD1 . ILE A 1 143 ? -15.91700 -6.77700  -6.27800  1.000 15.23254 ? 143 ILE A CD1 1 
ATOM   1074 N  N   . PHE A 1 144 ? -19.59100 -4.99000  -8.59800  1.000 14.08219 ? 144 PHE A N   1 
ATOM   1075 C  CA  . PHE A 1 144 ? -19.60100 -3.75500  -9.36400  1.000 11.85537 ? 144 PHE A CA  1 
ATOM   1076 C  C   . PHE A 1 144 ? -20.99600 -3.38400  -9.85400  1.000 13.12997 ? 144 PHE A C   1 
ATOM   1077 O  O   . PHE A 1 144 ? -21.15100 -2.44800  -10.64200 1.000 14.75410 ? 144 PHE A O   1 
ATOM   1078 C  CB  . PHE A 1 144 ? -18.56200 -3.88800  -10.49200 1.000 12.50313 ? 144 PHE A CB  1 
ATOM   1079 C  CG  . PHE A 1 144 ? -17.16900 -4.04100  -9.94600  1.000 13.26659 ? 144 PHE A CG  1 
ATOM   1080 C  CD1 . PHE A 1 144 ? -16.73700 -3.17400  -8.95100  1.000 15.60254 ? 144 PHE A CD1 1 
ATOM   1081 C  CD2 . PHE A 1 144 ? -16.36200 -5.11100  -10.31900 1.000 15.66990 ? 144 PHE A CD2 1 
ATOM   1082 C  CE1 . PHE A 1 144 ? -15.47200 -3.31600  -8.37100  1.000 16.03377 ? 144 PHE A CE1 1 
ATOM   1083 C  CE2 . PHE A 1 144 ? -15.07500 -5.25900  -9.73600  1.000 14.74859 ? 144 PHE A CE2 1 
ATOM   1084 C  CZ  . PHE A 1 144 ? -14.64900 -4.36200  -8.76700  1.000 15.29403 ? 144 PHE A CZ  1 
ATOM   1085 N  N   . GLY A 1 145 ? -22.00700 -4.07400  -9.34600  1.000 12.54133 ? 145 GLY A N   1 
ATOM   1086 C  CA  . GLY A 1 145 ? -23.35600 -3.54100  -9.33600  1.000 12.32442 ? 145 GLY A CA  1 
ATOM   1087 C  C   . GLY A 1 145 ? -23.68700 -2.75600  -8.08700  1.000 12.75039 ? 145 GLY A C   1 
ATOM   1088 O  O   . GLY A 1 145 ? -24.77100 -2.15400  -8.01600  1.000 13.26824 ? 145 GLY A O   1 
ATOM   1089 N  N   . PHE A 1 146 ? -22.78200 -2.75700  -7.09800  1.000 12.82291 ? 146 PHE A N   1 
ATOM   1090 C  CA  . PHE A 1 146 ? -22.91600 -2.01800  -5.84100  1.000 13.51843 ? 146 PHE A CA  1 
ATOM   1091 C  C   . PHE A 1 146 ? -21.95100 -0.84600  -5.75300  1.000 14.09437 ? 146 PHE A C   1 
ATOM   1092 O  O   . PHE A 1 146 ? -22.32400 0.24800   -5.30800  1.000 17.18169 ? 146 PHE A O   1 
ATOM   1093 C  CB  . PHE A 1 146 ? -22.65700 -2.94900  -4.63000  1.000 13.77704 ? 146 PHE A CB  1 
ATOM   1094 C  CG  . PHE A 1 146 ? -23.82100 -3.80800  -4.23400  1.000 15.37548 ? 146 PHE A CG  1 
ATOM   1095 C  CD1 . PHE A 1 146 ? -24.74000 -3.35200  -3.30000  1.000 16.93884 ? 146 PHE A CD1 1 
ATOM   1096 C  CD2 . PHE A 1 146 ? -23.96500 -5.08400  -4.74000  1.000 15.93907 ? 146 PHE A CD2 1 
ATOM   1097 C  CE1 . PHE A 1 146 ? -25.80900 -4.14900  -2.89500  1.000 15.89167 ? 146 PHE A CE1 1 
ATOM   1098 C  CE2 . PHE A 1 146 ? -25.04500 -5.88500  -4.34300  1.000 17.32948 ? 146 PHE A CE2 1 
ATOM   1099 C  CZ  . PHE A 1 146 ? -25.95700 -5.40800  -3.41600  1.000 17.27038 ? 146 PHE A CZ  1 
ATOM   1100 N  N   . VAL A 1 147 ? -20.68200 -1.06100  -6.11100  1.000 13.37479 ? 147 VAL A N   1 
ATOM   1101 C  CA  . VAL A 1 147 ? -19.67400 -0.03300  -5.95700  1.000 12.86809 ? 147 VAL A CA  1 
ATOM   1102 C  C   . VAL A 1 147 ? -19.04000 0.22100   -7.31900  1.000 13.65878 ? 147 VAL A C   1 
ATOM   1103 O  O   . VAL A 1 147 ? -18.99700 -0.66000  -8.19400  1.000 14.44377 ? 147 VAL A O   1 
ATOM   1104 C  CB  . VAL A 1 147 ? -18.59500 -0.40900  -4.89500  1.000 12.84668 ? 147 VAL A CB  1 
ATOM   1105 C  CG1 . VAL A 1 147 ? -19.19700 -0.38900  -3.49800  1.000 13.02196 ? 147 VAL A CG1 1 
ATOM   1106 C  CG2 . VAL A 1 147 ? -18.00500 -1.80100  -5.15300  1.000 14.13602 ? 147 VAL A CG2 1 
ATOM   1107 N  N   . GLY A 1 148 ? -18.54000 1.43700   -7.48600  1.000 13.94926 ? 148 GLY A N   1 
ATOM   1108 C  CA  . GLY A 1 148 ? -17.80200 1.76400   -8.68700  1.000 13.41099 ? 148 GLY A CA  1 
ATOM   1109 C  C   . GLY A 1 148 ? -16.40000 1.17100   -8.69600  1.000 15.18704 ? 148 GLY A C   1 
ATOM   1110 O  O   . GLY A 1 148 ? -15.81900 0.80000   -7.67200  1.000 15.96005 ? 148 GLY A O   1 
ATOM   1111 N  N   . ASP A 1 149 ? -15.85300 1.07300   -9.90800  1.000 12.97014 ? 149 ASP A N   1 
ATOM   1112 C  CA  . ASP A 1 149 ? -14.42700 0.86600   -10.09900 1.000 13.64927 ? 149 ASP A CA  1 
ATOM   1113 C  C   . ASP A 1 149 ? -14.03800 1.87200   -11.16900 1.000 14.55742 ? 149 ASP A C   1 
ATOM   1114 O  O   . ASP A 1 149 ? -14.72200 1.95900   -12.21100 1.000 14.70463 ? 149 ASP A O   1 
ATOM   1115 C  CB  . ASP A 1 149 ? -14.08100 -0.55400  -10.54200 1.000 15.21338 ? 149 ASP A CB  1 
ATOM   1116 C  CG  . ASP A 1 149 ? -12.59500 -0.74300  -10.69100 1.000 19.60183 ? 149 ASP A CG  1 
ATOM   1117 O  OD1 . ASP A 1 149 ? -11.97400 -1.29000  -9.75200  1.000 25.54853 ? 149 ASP A OD1 1 
ATOM   1118 O  OD2 . ASP A 1 149 ? -12.02000 -0.27100  -11.68700 1.000 19.64679 ? 149 ASP A OD2 1 
ATOM   1119 N  N   . PRO A 1 150 ? -12.95800 2.63200   -10.97400 1.000 15.36927 ? 150 PRO A N   1 
ATOM   1120 C  CA  . PRO A 1 150 ? -12.64200 3.72000   -11.91000 1.000 15.24158 ? 150 PRO A CA  1 
ATOM   1121 C  C   . PRO A 1 150 ? -12.30600 3.22100   -13.30000 1.000 15.24531 ? 150 PRO A C   1 
ATOM   1122 O  O   . PRO A 1 150 ? -12.40300 3.99300   -14.26500 1.000 16.29315 ? 150 PRO A O   1 
ATOM   1123 C  CB  . PRO A 1 150 ? -11.42900 4.40900   -11.25300 1.000 16.73364 ? 150 PRO A CB  1 
ATOM   1124 C  CG  . PRO A 1 150 ? -10.81800 3.33000   -10.37900 1.000 15.61689 ? 150 PRO A CG  1 
ATOM   1125 C  CD  . PRO A 1 150 ? -11.98800 2.54200   -9.85800  1.000 15.34126 ? 150 PRO A CD  1 
ATOM   1126 N  N   . SER A 1 151 ? -11.91700 1.95200   -13.43400 1.000 15.54099 ? 151 SER A N   1 
ATOM   1127 C  CA  . SER A 1 151 ? -11.53300 1.40700   -14.73000 1.000 16.82073 ? 151 SER A CA  1 
ATOM   1128 C  C   . SER A 1 151 ? -12.55000 0.42700   -15.27800 1.000 16.02574 ? 151 SER A C   1 
ATOM   1129 O  O   . SER A 1 151 ? -12.21500 -0.37400  -16.14500 1.000 16.23844 ? 151 SER A O   1 
ATOM   1130 C  CB  . SER A 1 151 ? -10.16800 0.72700   -14.64100 1.000 21.78727 ? 151 SER A CB  1 
ATOM   1131 O  OG  . SER A 1 151 ? -9.19500  1.69300   -14.33200 1.000 26.08501 ? 151 SER A OG  1 
ATOM   1132 N  N   . LEU A 1 152 ? -13.78600 0.46400   -14.78000 1.000 14.02505 ? 152 LEU A N   1 
ATOM   1133 C  CA  . LEU A 1 152 ? -14.84300 -0.44100  -15.23800 1.000 14.67592 ? 152 LEU A CA  1 
ATOM   1134 C  C   . LEU A 1 152 ? -16.12700 0.32700   -15.51900 1.000 15.12857 ? 152 LEU A C   1 
ATOM   1135 O  O   . LEU A 1 152 ? -17.22400 -0.10000  -15.15300 1.000 14.72812 ? 152 LEU A O   1 
ATOM   1136 C  CB  . LEU A 1 152 ? -15.09900 -1.53300  -14.20400 1.000 15.07643 ? 152 LEU A CB  1 
ATOM   1137 C  CG  . LEU A 1 152 ? -14.02500 -2.60600  -14.04700 1.000 16.71631 ? 152 LEU A CG  1 
ATOM   1138 C  CD1 . LEU A 1 152 ? -14.37000 -3.52900  -12.88000 1.000 17.39772 ? 152 LEU A CD1 1 
ATOM   1139 C  CD2 . LEU A 1 152 ? -13.83800 -3.38400  -15.35700 1.000 17.22567 ? 152 LEU A CD2 1 
ATOM   1140 N  N   . GLY A 1 153 ? -16.02000 1.46000   -16.22000 1.000 16.08104 ? 153 GLY A N   1 
ATOM   1141 C  CA  . GLY A 1 153 ? -17.19100 2.31900   -16.38500 1.000 14.92097 ? 153 GLY A CA  1 
ATOM   1142 C  C   . GLY A 1 153 ? -18.40300 1.66000   -17.02500 1.000 14.61692 ? 153 GLY A C   1 
ATOM   1143 O  O   . GLY A 1 153 ? -19.49200 1.67600   -16.44200 1.000 14.92777 ? 153 GLY A O   1 
ATOM   1144 N  N   . ALA A 1 154 ? -18.23000 1.07600   -18.21600 1.000 13.91873 ? 154 ALA A N   1 
ATOM   1145 C  CA  . ALA A 1 154 ? -19.35100 0.42800   -18.89900 1.000 13.81700 ? 154 ALA A CA  1 
ATOM   1146 C  C   . ALA A 1 154 ? -19.82300 -0.80900  -18.13800 1.000 14.74188 ? 154 ALA A C   1 
ATOM   1147 O  O   . ALA A 1 154 ? -21.02800 -1.05500  -18.01500 1.000 13.21389 ? 154 ALA A O   1 
ATOM   1148 C  CB  . ALA A 1 154 ? -18.94000 0.08800   -20.33100 1.000 15.33775 ? 154 ALA A CB  1 
ATOM   1149 N  N   . TYR A 1 155 ? -18.88300 -1.57600  -17.57700 1.000 14.88356 ? 155 TYR A N   1 
ATOM   1150 C  CA  . TYR A 1 155 ? -19.23200 -2.72400  -16.75400 1.000 13.71141 ? 155 TYR A CA  1 
ATOM   1151 C  C   . TYR A 1 155 ? -20.12800 -2.31000  -15.59500 1.000 14.08872 ? 155 TYR A C   1 
ATOM   1152 O  O   . TYR A 1 155 ? -21.16000 -2.95100  -15.33600 1.000 14.18104 ? 155 TYR A O   1 
ATOM   1153 C  CB  . TYR A 1 155 ? -17.95000 -3.38100  -16.21700 1.000 13.65067 ? 155 TYR A CB  1 
ATOM   1154 C  CG  . TYR A 1 155 ? -18.17200 -4.75800  -15.61900 1.000 14.73018 ? 155 TYR A CG  1 
ATOM   1155 C  CD1 . TYR A 1 155 ? -18.33800 -5.86500  -16.44100 1.000 17.66226 ? 155 TYR A CD1 1 
ATOM   1156 C  CD2 . TYR A 1 155 ? -18.16600 -4.95300  -14.24700 1.000 14.96449 ? 155 TYR A CD2 1 
ATOM   1157 C  CE1 . TYR A 1 155 ? -18.49800 -7.11900  -15.93000 1.000 17.53215 ? 155 TYR A CE1 1 
ATOM   1158 C  CE2 . TYR A 1 155 ? -18.36100 -6.21700  -13.71000 1.000 16.27065 ? 155 TYR A CE2 1 
ATOM   1159 C  CZ  . TYR A 1 155 ? -18.51200 -7.29300  -14.55600 1.000 17.08183 ? 155 TYR A CZ  1 
ATOM   1160 O  OH  . TYR A 1 155 ? -18.69400 -8.56300  -14.03400 1.000 20.65469 ? 155 TYR A OH  1 
ATOM   1161 N  N   . ASN A 1 156 ? -19.71000 -1.26800  -14.86400 1.000 13.49709 ? 156 ASN A N   1 
ATOM   1162 C  CA  . ASN A 1 156 ? -20.51200 -0.72000  -13.76000 1.000 12.54393 ? 156 ASN A CA  1 
ATOM   1163 C  C   . ASN A 1 156 ? -21.91800 -0.37700  -14.22800 1.000 12.77744 ? 156 ASN A C   1 
ATOM   1164 O  O   . ASN A 1 156 ? -22.89600 -0.65900  -13.53100 1.000 13.66549 ? 156 ASN A O   1 
ATOM   1165 C  CB  . ASN A 1 156 ? -19.87400 0.55900   -13.18200 1.000 12.96548 ? 156 ASN A CB  1 
ATOM   1166 C  CG  . ASN A 1 156 ? -18.82500 0.29600   -12.06200 1.000 13.55989 ? 156 ASN A CG  1 
ATOM   1167 O  OD1 . ASN A 1 156 ? -17.78800 0.93800   -12.02700 1.000 14.07037 ? 156 ASN A OD1 1 
ATOM   1168 N  ND2 . ASN A 1 156 ? -19.12300 -0.61600  -11.15200 1.000 13.00302 ? 156 ASN A ND2 1 
ATOM   1169 N  N   . ALA A 1 157 ? -22.02500 0.30400   -15.38100 1.000 13.48957 ? 157 ALA A N   1 
ATOM   1170 C  CA  . ALA A 1 157 ? -23.34200 0.66100   -15.88700 1.000 12.90177 ? 157 ALA A CA  1 
ATOM   1171 C  C   . ALA A 1 157 ? -24.19200 -0.58500  -16.08400 1.000 14.55611 ? 157 ALA A C   1 
ATOM   1172 O  O   . ALA A 1 157 ? -25.34200 -0.63700  -15.63000 1.000 14.02719 ? 157 ALA A O   1 
ATOM   1173 C  CB  . ALA A 1 157 ? -23.20800 1.43300   -17.20600 1.000 13.74517 ? 157 ALA A CB  1 
ATOM   1174 N  N   . SER A 1 158 ? -23.62900 -1.61300  -16.73300 1.000 13.52507 ? 158 SER A N   1 
ATOM   1175 C  CA  . SER A 1 158 ? -24.39800 -2.81400  -17.03900 1.000 14.00789 ? 158 SER A CA  1 
ATOM   1176 C  C   . SER A 1 158 ? -24.80800 -3.55900  -15.77400 1.000 13.88644 ? 158 SER A C   1 
ATOM   1177 O  O   . SER A 1 158 ? -25.91300 -4.10900  -15.71300 1.000 14.29045 ? 158 SER A O   1 
ATOM   1178 C  CB  . SER A 1 158 ? -23.59900 -3.74800  -17.97200 1.000 14.05041 ? 158 SER A CB  1 
ATOM   1179 O  OG  . SER A 1 158 ? -22.53600 -4.39500  -17.25400 1.000 13.79809 ? 158 SER A OG  1 
ATOM   1180 N  N   . LYS A 1 159 ? -23.92400 -3.62300  -14.76400 1.000 14.01512 ? 159 LYS A N   1 
ATOM   1181 C  CA  . LYS A 1 159 ? -24.24600 -4.40900  -13.57300 1.000 13.87097 ? 159 LYS A CA  1 
ATOM   1182 C  C   . LYS A 1 159 ? -25.21600 -3.67100  -12.66200 1.000 15.79757 ? 159 LYS A C   1 
ATOM   1183 O  O   . LYS A 1 159 ? -26.05000 -4.32000  -12.01000 1.000 16.10625 ? 159 LYS A O   1 
ATOM   1184 C  CB  . LYS A 1 159 ? -22.95100 -4.76800  -12.83200 1.000 15.03996 ? 159 LYS A CB  1 
ATOM   1185 C  CG  . LYS A 1 159 ? -22.03800 -5.72700  -13.65900 1.000 17.67313 ? 159 LYS A CG  1 
ATOM   1186 C  CD  . LYS A 1 159 ? -22.79900 -6.98300  -14.12200 1.000 20.12359 ? 159 LYS A CD  1 
ATOM   1187 C  CE  . LYS A 1 159 ? -21.95700 -7.93700  -14.98100 1.000 22.41766 ? 159 LYS A CE  1 
ATOM   1188 N  NZ  . LYS A 1 159 ? -22.66100 -9.21500  -15.28300 1.000 23.65771 ? 159 LYS A NZ  1 
ATOM   1189 N  N   . GLY A 1 160 ? -25.15800 -2.33300  -12.64000 1.000 13.04565 ? 160 GLY A N   1 
ATOM   1190 C  CA  . GLY A 1 160 ? -26.18200 -1.57000  -11.93400 1.000 12.48025 ? 160 GLY A CA  1 
ATOM   1191 C  C   . GLY A 1 160 ? -27.53100 -1.70400  -12.59900 1.000 14.06889 ? 160 GLY A C   1 
ATOM   1192 O  O   . GLY A 1 160 ? -28.55500 -1.82200  -11.91500 1.000 16.02328 ? 160 GLY A O   1 
ATOM   1193 N  N   . ALA A 1 161 ? -27.54800 -1.71500  -13.94200 1.000 13.12009 ? 161 ALA A N   1 
ATOM   1194 C  CA  . ALA A 1 161 ? -28.80800 -1.93700  -14.67000 1.000 13.28803 ? 161 ALA A CA  1 
ATOM   1195 C  C   . ALA A 1 161 ? -29.38400 -3.31500  -14.37300 1.000 13.60663 ? 161 ALA A C   1 
ATOM   1196 O  O   . ALA A 1 161 ? -30.58600 -3.44600  -14.10800 1.000 14.84891 ? 161 ALA A O   1 
ATOM   1197 C  CB  . ALA A 1 161 ? -28.57900 -1.77400  -16.17100 1.000 14.54841 ? 161 ALA A CB  1 
ATOM   1198 N  N   . VAL A 1 162 ? -28.54900 -4.36100  -14.40300 1.000 14.64302 ? 162 VAL A N   1 
ATOM   1199 C  CA  . VAL A 1 162 ? -29.05100 -5.70900  -14.12000 1.000 15.05684 ? 162 VAL A CA  1 
ATOM   1200 C  C   . VAL A 1 162 ? -29.61400 -5.78300  -12.70200 1.000 14.03144 ? 162 VAL A C   1 
ATOM   1201 O  O   . VAL A 1 162 ? -30.68400 -6.35400  -12.46700 1.000 13.64757 ? 162 VAL A O   1 
ATOM   1202 C  CB  . VAL A 1 162 ? -27.95300 -6.76900  -14.34300 1.000 17.65634 ? 162 VAL A CB  1 
ATOM   1203 C  CG1 . VAL A 1 162 ? -28.47200 -8.13500  -13.85800 1.000 15.81373 ? 162 VAL A CG1 1 
ATOM   1204 C  CG2 . VAL A 1 162 ? -27.58100 -6.85000  -15.83200 1.000 19.52927 ? 162 VAL A CG2 1 
ATOM   1205 N  N   . ARG A 1 163 ? -28.92600 -5.16500  -11.74400 1.000 14.30607 ? 163 ARG A N   1 
ATOM   1206 C  CA  . ARG A 1 163 ? -29.37400 -5.18100  -10.35500 1.000 14.01576 ? 163 ARG A CA  1 
ATOM   1207 C  C   . ARG A 1 163 ? -30.80600 -4.64800  -10.18900 1.000 14.27175 ? 163 ARG A C   1 
ATOM   1208 O  O   . ARG A 1 163 ? -31.63900 -5.28300  -9.52100  1.000 14.70290 ? 163 ARG A O   1 
ATOM   1209 C  CB  . ARG A 1 163 ? -28.38400 -4.35600  -9.53700  1.000 13.93842 ? 163 ARG A CB  1 
ATOM   1210 C  CG  . ARG A 1 163 ? -28.72200 -4.23900  -8.05500  1.000 13.29379 ? 163 ARG A CG  1 
ATOM   1211 C  CD  . ARG A 1 163 ? -27.71100 -3.30500  -7.38900  1.000 13.17458 ? 163 ARG A CD  1 
ATOM   1212 N  NE  . ARG A 1 163 ? -28.10000 -3.01700  -6.01700  1.000 13.53907 ? 163 ARG A NE  1 
ATOM   1213 C  CZ  . ARG A 1 163 ? -27.52500 -2.07900  -5.27300  1.000 15.31477 ? 163 ARG A CZ  1 
ATOM   1214 N  NH1 . ARG A 1 163 ? -26.54000 -1.31900  -5.78700  1.000 13.71231 ? 163 ARG A NH1 1 
ATOM   1215 N  NH2 . ARG A 1 163 ? -27.95100 -1.89000  -4.03400  1.000 18.45474 ? 163 ARG A NH2 1 
ATOM   1216 N  N   . ILE A 1 164 ? -31.11500 -3.49400  -10.79300 1.000 12.72307 ? 164 ILE A N   1 
ATOM   1217 C  CA  . ILE A 1 164 ? -32.41700 -2.88000  -10.53900 1.000 12.03324 ? 164 ILE A CA  1 
ATOM   1218 C  C   . ILE A 1 164 ? -33.47800 -3.39500  -11.50600 1.000 13.58864 ? 164 ILE A C   1 
ATOM   1219 O  O   . ILE A 1 164 ? -34.64500 -3.55200  -11.11500 1.000 13.84412 ? 164 ILE A O   1 
ATOM   1220 C  CB  . ILE A 1 164 ? -32.29900 -1.34000  -10.56000 1.000 12.19787 ? 164 ILE A CB  1 
ATOM   1221 C  CG1 . ILE A 1 164 ? -31.20200 -0.85400  -9.61200  1.000 13.90096 ? 164 ILE A CG1 1 
ATOM   1222 C  CG2 . ILE A 1 164 ? -33.61500 -0.69800  -10.14200 1.000 14.41846 ? 164 ILE A CG2 1 
ATOM   1223 C  CD1 . ILE A 1 164 ? -31.34300 -1.34400  -8.16800  1.000 13.94366 ? 164 ILE A CD1 1 
ATOM   1224 N  N   A MET A 1 165 ? -33.10600 -3.67600  -12.76500 0.717 13.81216 ? 165 MET A N   1 
ATOM   1225 N  N   B MET A 1 165 ? -33.10800 -3.68300  -12.75900 0.283 13.51892 ? 165 MET A N   1 
ATOM   1226 C  CA  A MET A 1 165 ? -34.06400 -4.30300  -13.67900 0.717 12.89156 ? 165 MET A CA  1 
ATOM   1227 C  CA  B MET A 1 165 ? -34.07000 -4.29500  -13.67300 0.283 13.20767 ? 165 MET A CA  1 
ATOM   1228 C  C   A MET A 1 165 ? -34.59100 -5.61300  -13.10600 0.717 13.98624 ? 165 MET A C   1 
ATOM   1229 C  C   B MET A 1 165 ? -34.59000 -5.61600  -13.11600 0.283 13.65710 ? 165 MET A C   1 
ATOM   1230 O  O   A MET A 1 165 ? -35.78500 -5.92900  -13.24000 0.717 14.02742 ? 165 MET A O   1 
ATOM   1231 O  O   B MET A 1 165 ? -35.77300 -5.94900  -13.28300 0.283 13.94921 ? 165 MET A O   1 
ATOM   1232 C  CB  A MET A 1 165 ? -33.41700 -4.54200  -15.04600 0.717 12.96195 ? 165 MET A CB  1 
ATOM   1233 C  CB  B MET A 1 165 ? -33.43400 -4.50400  -15.04900 0.283 13.32069 ? 165 MET A CB  1 
ATOM   1234 C  CG  A MET A 1 165 ? -34.43800 -5.07000  -16.06000 0.717 13.68495 ? 165 MET A CG  1 
ATOM   1235 C  CG  B MET A 1 165 ? -34.41700 -5.06900  -16.06800 0.283 14.37211 ? 165 MET A CG  1 
ATOM   1236 S  SD  A MET A 1 165 ? -33.66000 -5.88400  -17.45900 0.717 16.71143 ? 165 MET A SD  1 
ATOM   1237 S  SD  B MET A 1 165 ? -34.33500 -6.86600  -16.14300 0.283 16.65663 ? 165 MET A SD  1 
ATOM   1238 C  CE  A MET A 1 165 ? -33.12900 -7.44400  -16.73100 0.717 18.61347 ? 165 MET A CE  1 
ATOM   1239 C  CE  B MET A 1 165 ? -32.79900 -7.07600  -17.05800 0.283 17.38136 ? 165 MET A CE  1 
ATOM   1240 N  N   . SER A 1 166 ? -33.72800 -6.37100  -12.43100 1.000 13.35425 ? 166 SER A N   1 
ATOM   1241 C  CA  . SER A 1 166 ? -34.15100 -7.64700  -11.85900 1.000 13.30797 ? 166 SER A CA  1 
ATOM   1242 C  C   . SER A 1 166 ? -35.20300 -7.45600  -10.76200 1.000 13.34799 ? 166 SER A C   1 
ATOM   1243 O  O   . SER A 1 166 ? -36.10000 -8.30700  -10.62400 1.000 14.57562 ? 166 SER A O   1 
ATOM   1244 C  CB  . SER A 1 166 ? -32.93500 -8.39800  -11.31100 1.000 14.41712 ? 166 SER A CB  1 
ATOM   1245 O  OG  . SER A 1 166 ? -32.04700 -8.69200  -12.38100 1.000 14.07751 ? 166 SER A OG  1 
ATOM   1246 N  N   . LYS A 1 167 ? -35.11100 -6.35900  -9.99100  1.000 13.81767 ? 167 LYS A N   1 
ATOM   1247 C  CA  . LYS A 1 167 ? -36.13900 -6.06800  -8.98800  1.000 12.48316 ? 167 LYS A CA  1 
ATOM   1248 C  C   . LYS A 1 167 ? -37.47600 -5.78000  -9.64700  1.000 13.32739 ? 167 LYS A C   1 
ATOM   1249 O  O   . LYS A 1 167 ? -38.51600 -6.22400  -9.15200  1.000 14.25310 ? 167 LYS A O   1 
ATOM   1250 C  CB  . LYS A 1 167 ? -35.71900 -4.88900  -8.09800  1.000 12.32900 ? 167 LYS A CB  1 
ATOM   1251 C  CG  . LYS A 1 167 ? -34.47000 -5.19100  -7.22800  1.000 13.37227 ? 167 LYS A CG  1 
ATOM   1252 C  CD  . LYS A 1 167 ? -34.10600 -4.00400  -6.35800  1.000 14.41691 ? 167 LYS A CD  1 
ATOM   1253 C  CE  . LYS A 1 167 ? -32.77700 -4.28400  -5.60800  1.000 17.34838 ? 167 LYS A CE  1 
ATOM   1254 N  NZ  . LYS A 1 167 ? -33.06700 -5.21100  -4.44800  1.000 25.96469 ? 167 LYS A NZ  1 
ATOM   1255 N  N   . SER A 1 168 ? -37.47100 -5.06400  -10.78500 1.000 13.57105 ? 168 SER A N   1 
ATOM   1256 C  CA  . SER A 1 168 ? -38.71900 -4.80300  -11.49100 1.000 12.77870 ? 168 SER A CA  1 
ATOM   1257 C  C   . SER A 1 168 ? -39.39600 -6.10800  -11.88900 1.000 13.72740 ? 168 SER A C   1 
ATOM   1258 O  O   . SER A 1 168 ? -40.60600 -6.31000  -11.64900 1.000 14.42141 ? 168 SER A O   1 
ATOM   1259 C  CB  . SER A 1 168 ? -38.44200 -3.94400  -12.73900 1.000 14.49038 ? 168 SER A CB  1 
ATOM   1260 O  OG  . SER A 1 168 ? -39.66100 -3.74400  -13.48100 1.000 15.24417 ? 168 SER A OG  1 
ATOM   1261 N  N   . ALA A 1 169 ? -38.61800 -7.00700  -12.50300 1.000 14.02611 ? 169 ALA A N   1 
ATOM   1262 C  CA  . ALA A 1 169 ? -39.12500 -8.28900  -12.95000 1.000 14.14198 ? 169 ALA A CA  1 
ATOM   1263 C  C   . ALA A 1 169 ? -39.59500 -9.12800  -11.77300 1.000 13.72658 ? 169 ALA A C   1 
ATOM   1264 O  O   . ALA A 1 169 ? -40.66500 -9.74000  -11.83500 1.000 14.35674 ? 169 ALA A O   1 
ATOM   1265 C  CB  . ALA A 1 169 ? -38.03000 -9.02000  -13.74500 1.000 15.01191 ? 169 ALA A CB  1 
ATOM   1266 N  N   . ALA A 1 170 ? -38.83300 -9.13600  -10.67500 1.000 13.45187 ? 170 ALA A N   1 
ATOM   1267 C  CA  . ALA A 1 170 ? -39.25500 -9.85400  -9.47500  1.000 13.44066 ? 170 ALA A CA  1 
ATOM   1268 C  C   . ALA A 1 170 ? -40.61600 -9.37100  -8.99600  1.000 14.29664 ? 170 ALA A C   1 
ATOM   1269 O  O   . ALA A 1 170 ? -41.49500 -10.17900 -8.66500  1.000 13.87977 ? 170 ALA A O   1 
ATOM   1270 C  CB  . ALA A 1 170 ? -38.22300 -9.67300  -8.35200  1.000 12.55729 ? 170 ALA A CB  1 
ATOM   1271 N  N   . LEU A 1 171 ? -40.80000 -8.05100  -8.92300  1.000 13.60410 ? 171 LEU A N   1 
ATOM   1272 C  CA  . LEU A 1 171 ? -42.06500 -7.52400  -8.41900  1.000 12.95826 ? 171 LEU A CA  1 
ATOM   1273 C  C   . LEU A 1 171 ? -43.21400 -7.90100  -9.33600  1.000 13.28701 ? 171 LEU A C   1 
ATOM   1274 O  O   . LEU A 1 171 ? -44.26600 -8.35000  -8.87200  1.000 14.43252 ? 171 LEU A O   1 
ATOM   1275 C  CB  . LEU A 1 171 ? -41.99900 -6.00700  -8.25800  1.000 13.91571 ? 171 LEU A CB  1 
ATOM   1276 C  CG  . LEU A 1 171 ? -41.01500 -5.50300  -7.19200  1.000 15.07113 ? 171 LEU A CG  1 
ATOM   1277 C  CD1 . LEU A 1 171 ? -40.82500 -4.00600  -7.34300  1.000 15.84011 ? 171 LEU A CD1 1 
ATOM   1278 C  CD2 . LEU A 1 171 ? -41.56900 -5.84500  -5.80500  1.000 15.17590 ? 171 LEU A CD2 1 
ATOM   1279 N  N   . ASP A 1 172 ? -43.02600 -7.74100  -10.64900 1.000 13.32342 ? 172 ASP A N   1 
ATOM   1280 C  CA  . ASP A 1 172 ? -44.13200 -8.02000  -11.55300 1.000 13.66500 ? 172 ASP A CA  1 
ATOM   1281 C  C   . ASP A 1 172 ? -44.51600 -9.48800  -11.47200 1.000 15.09112 ? 172 ASP A C   1 
ATOM   1282 O  O   . ASP A 1 172 ? -45.69900 -9.82300  -11.40200 1.000 15.25342 ? 172 ASP A O   1 
ATOM   1283 C  CB  . ASP A 1 172 ? -43.75100 -7.62500  -12.98600 1.000 15.71694 ? 172 ASP A CB  1 
ATOM   1284 C  CG  . ASP A 1 172 ? -44.94300 -7.64000  -13.93800 1.000 18.68628 ? 172 ASP A CG  1 
ATOM   1285 O  OD1 . ASP A 1 172 ? -45.93300 -6.90600  -13.70700 1.000 20.01337 ? 172 ASP A OD1 1 
ATOM   1286 O  OD2 . ASP A 1 172 ? -44.86100 -8.37900  -14.93500 1.000 20.94074 ? 172 ASP A OD2 1 
ATOM   1287 N  N   . CYS A 1 173 ? -43.52100 -10.37000 -11.44600 1.000 16.43958 ? 173 CYS A N   1 
ATOM   1288 C  CA  . CYS A 1 173 ? -43.78100 -11.80000 -11.35000 1.000 13.80596 ? 173 CYS A CA  1 
ATOM   1289 C  C   . CYS A 1 173 ? -44.47300 -12.15800 -10.04100 1.000 17.42498 ? 173 CYS A C   1 
ATOM   1290 O  O   . CYS A 1 173 ? -45.33500 -13.04800 -10.01900 1.000 16.83788 ? 173 CYS A O   1 
ATOM   1291 C  CB  . CYS A 1 173 ? -42.47200 -12.56900 -11.46600 1.000 13.56197 ? 173 CYS A CB  1 
ATOM   1292 S  SG  . CYS A 1 173 ? -41.80700 -12.59700 -13.16300 1.000 15.60849 ? 173 CYS A SG  1 
ATOM   1293 N  N   . ALA A 1 174 ? -44.08200 -11.50200 -8.93600  1.000 16.43417 ? 174 ALA A N   1 
ATOM   1294 C  CA  . ALA A 1 174 ? -44.70200 -11.77800 -7.63700  1.000 14.89537 ? 174 ALA A CA  1 
ATOM   1295 C  C   . ALA A 1 174 ? -46.13500 -11.27900 -7.60800  1.000 15.50183 ? 174 ALA A C   1 
ATOM   1296 O  O   . ALA A 1 174 ? -47.03500 -12.00200 -7.17600  1.000 16.67903 ? 174 ALA A O   1 
ATOM   1297 C  CB  . ALA A 1 174 ? -43.89200 -11.12900 -6.50600  1.000 15.31541 ? 174 ALA A CB  1 
ATOM   1298 N  N   . LEU A 1 175 ? -46.36100 -10.04700 -8.07600  1.000 14.84709 ? 175 LEU A N   1 
ATOM   1299 C  CA  . LEU A 1 175 ? -47.69800 -9.44900  -8.00800  1.000 15.88511 ? 175 LEU A CA  1 
ATOM   1300 C  C   . LEU A 1 175 ? -48.68400 -10.18300 -8.89400  1.000 17.11300 ? 175 LEU A C   1 
ATOM   1301 O  O   . LEU A 1 175 ? -49.89800 -10.16900 -8.62500  1.000 19.57885 ? 175 LEU A O   1 
ATOM   1302 C  CB  . LEU A 1 175 ? -47.63300 -7.97500  -8.41500  1.000 16.26663 ? 175 LEU A CB  1 
ATOM   1303 C  CG  . LEU A 1 175 ? -46.79600 -7.11500  -7.47000  1.000 18.29643 ? 175 LEU A CG  1 
ATOM   1304 C  CD1 . LEU A 1 175 ? -46.48300 -5.75700  -8.07600  1.000 18.53441 ? 175 LEU A CD1 1 
ATOM   1305 C  CD2 . LEU A 1 175 ? -47.52400 -6.97300  -6.12600  1.000 18.44670 ? 175 LEU A CD2 1 
ATOM   1306 N  N   . LYS A 1 176 ? -48.20400 -10.80400 -9.96700  1.000 15.69213 ? 176 LYS A N   1 
ATOM   1307 C  CA  . LYS A 1 176 ? -49.07900 -11.48200 -10.90500 1.000 16.96666 ? 176 LYS A CA  1 
ATOM   1308 C  C   . LYS A 1 176 ? -49.14700 -12.98400 -10.65600 1.000 17.82288 ? 176 LYS A C   1 
ATOM   1309 O  O   . LYS A 1 176 ? -49.77400 -13.70300 -11.45100 1.000 19.78201 ? 176 LYS A O   1 
ATOM   1310 C  CB  . LYS A 1 176 ? -48.65500 -11.18400 -12.34300 1.000 18.22924 ? 176 LYS A CB  1 
ATOM   1311 C  CG  . LYS A 1 176 ? -48.83700 -9.73000  -12.73000 1.000 18.84733 ? 176 LYS A CG  1 
ATOM   1312 C  CD  . LYS A 1 176 ? -48.46200 -9.51000  -14.19800 1.000 22.33158 ? 176 LYS A CD  1 
ATOM   1313 C  CE  . LYS A 1 176 ? -48.82100 -8.09600  -14.64200 1.000 27.40420 ? 176 LYS A CE  1 
ATOM   1314 N  NZ  . LYS A 1 176 ? -48.53100 -7.91800  -16.09500 1.000 32.69150 ? 176 LYS A NZ  1 
ATOM   1315 N  N   . ASP A 1 177 ? -48.52100 -13.46400 -9.57300  1.000 16.85826 ? 177 ASP A N   1 
ATOM   1316 C  CA  . ASP A 1 177 ? -48.58300 -14.86800 -9.17100  1.000 16.76268 ? 177 ASP A CA  1 
ATOM   1317 C  C   . ASP A 1 177 ? -48.09500 -15.78700 -10.28300 1.000 17.30289 ? 177 ASP A C   1 
ATOM   1318 O  O   . ASP A 1 177 ? -48.66300 -16.85700 -10.51800 1.000 19.38412 ? 177 ASP A O   1 
ATOM   1319 C  CB  . ASP A 1 177 ? -50.01200 -15.23700 -8.74700  1.000 18.81612 ? 177 ASP A CB  1 
ATOM   1320 C  CG  . ASP A 1 177 ? -50.47200 -14.43700 -7.53300  1.000 24.08824 ? 177 ASP A CG  1 
ATOM   1321 O  OD1 . ASP A 1 177 ? -49.65300 -14.22000 -6.62700  1.000 26.14234 ? 177 ASP A OD1 1 
ATOM   1322 O  OD2 . ASP A 1 177 ? -51.67100 -14.07400 -7.49400  1.000 31.59738 ? 177 ASP A OD2 1 
ATOM   1323 N  N   . TYR A 1 178 ? -47.01400 -15.36900 -10.95400 1.000 17.83340 ? 178 TYR A N   1 
ATOM   1324 C  CA  . TYR A 1 178 ? -46.46900 -16.10200 -12.09200 1.000 18.82432 ? 178 TYR A CA  1 
ATOM   1325 C  C   . TYR A 1 178 ? -45.69900 -17.35400 -11.68700 1.000 18.64069 ? 178 TYR A C   1 
ATOM   1326 O  O   . TYR A 1 178 ? -45.39100 -18.17500 -12.56000 1.000 18.39587 ? 178 TYR A O   1 
ATOM   1327 C  CB  . TYR A 1 178 ? -45.52500 -15.19000 -12.88600 1.000 17.21331 ? 178 TYR A CB  1 
ATOM   1328 C  CG  . TYR A 1 178 ? -46.14400 -14.24800 -13.89200 1.000 18.08567 ? 178 TYR A CG  1 
ATOM   1329 C  CD1 . TYR A 1 178 ? -47.51500 -14.27300 -14.18300 1.000 18.47795 ? 178 TYR A CD1 1 
ATOM   1330 C  CD2 . TYR A 1 178 ? -45.33800 -13.36100 -14.60100 1.000 18.61148 ? 178 TYR A CD2 1 
ATOM   1331 C  CE1 . TYR A 1 178 ? -48.03500 -13.42300 -15.13000 1.000 19.82840 ? 178 TYR A CE1 1 
ATOM   1332 C  CE2 . TYR A 1 178 ? -45.85700 -12.50800 -15.54700 1.000 17.60868 ? 178 TYR A CE2 1 
ATOM   1333 C  CZ  . TYR A 1 178 ? -47.21000 -12.54400 -15.81300 1.000 21.38451 ? 178 TYR A CZ  1 
ATOM   1334 O  OH  . TYR A 1 178 ? -47.74100 -11.70300 -16.78400 1.000 22.93077 ? 178 TYR A OH  1 
ATOM   1335 N  N   . ASP A 1 179 ? -45.35600 -17.51400 -10.40600 1.000 17.22230 ? 179 ASP A N   1 
ATOM   1336 C  CA  . ASP A 1 179 ? -44.46300 -18.59100 -9.95900  1.000 18.30439 ? 179 ASP A CA  1 
ATOM   1337 C  C   . ASP A 1 179 ? -43.10000 -18.48200 -10.64900 1.000 16.48608 ? 179 ASP A C   1 
ATOM   1338 O  O   . ASP A 1 179 ? -42.53300 -19.46500 -11.13900 1.000 16.38215 ? 179 ASP A O   1 
ATOM   1339 C  CB  . ASP A 1 179 ? -45.09500 -19.96900 -10.17600 1.000 20.85125 ? 179 ASP A CB  1 
ATOM   1340 C  CG  . ASP A 1 179 ? -44.26400 -21.10500 -9.60200  1.000 24.16214 ? 179 ASP A CG  1 
ATOM   1341 O  OD1 . ASP A 1 179 ? -43.60200 -20.90800 -8.55400  1.000 25.14538 ? 179 ASP A OD1 1 
ATOM   1342 O  OD2 . ASP A 1 179 ? -44.25400 -22.18100 -10.24100 1.000 27.13369 ? 179 ASP A OD2 1 
ATOM   1343 N  N   . VAL A 1 180 ? -42.59000 -17.25600 -10.73000 1.000 14.77672 ? 180 VAL A N   1 
ATOM   1344 C  CA  . VAL A 1 180 ? -41.24400 -16.97700 -11.22500 1.000 14.12036 ? 180 VAL A CA  1 
ATOM   1345 C  C   . VAL A 1 180 ? -40.59800 -16.04100 -10.22200 1.000 16.23250 ? 180 VAL A C   1 
ATOM   1346 O  O   . VAL A 1 180 ? -41.15900 -14.99100 -9.91300  1.000 17.07333 ? 180 VAL A O   1 
ATOM   1347 C  CB  . VAL A 1 180 ? -41.24700 -16.31300 -12.61700 1.000 14.70225 ? 180 VAL A CB  1 
ATOM   1348 C  CG1 . VAL A 1 180 ? -39.80700 -16.10800 -13.12000 1.000 14.83700 ? 180 VAL A CG1 1 
ATOM   1349 C  CG2 . VAL A 1 180 ? -42.06700 -17.13500 -13.63700 1.000 17.52794 ? 180 VAL A CG2 1 
ATOM   1350 N  N   . ARG A 1 181 ? -39.42900 -16.41800 -9.70300  1.000 13.49303 ? 181 ARG A N   1 
ATOM   1351 C  CA  . ARG A 1 181 ? -38.63800 -15.51700 -8.88200  1.000 15.44794 ? 181 ARG A CA  1 
ATOM   1352 C  C   . ARG A 1 181 ? -37.47800 -14.97600 -9.70100  1.000 16.09882 ? 181 ARG A C   1 
ATOM   1353 O  O   . ARG A 1 181 ? -37.02600 -15.61900 -10.65500 1.000 14.85255 ? 181 ARG A O   1 
ATOM   1354 C  CB  . ARG A 1 181 ? -38.11000 -16.23500 -7.64800  1.000 15.25261 ? 181 ARG A CB  1 
ATOM   1355 C  CG  . ARG A 1 181 ? -39.26600 -16.71300 -6.79200  1.000 13.98852 ? 181 ARG A CG  1 
ATOM   1356 C  CD  . ARG A 1 181 ? -38.79600 -17.54100 -5.59500  1.000 14.68603 ? 181 ARG A CD  1 
ATOM   1357 N  NE  . ARG A 1 181 ? -38.20900 -18.84500 -5.94200  1.000 15.69236 ? 181 ARG A NE  1 
ATOM   1358 C  CZ  . ARG A 1 181 ? -36.90500 -19.11400 -5.93700  1.000 15.96969 ? 181 ARG A CZ  1 
ATOM   1359 N  NH1 . ARG A 1 181 ? -36.01200 -18.16500 -5.62200  1.000 15.64261 ? 181 ARG A NH1 1 
ATOM   1360 N  NH2 . ARG A 1 181 ? -36.48600 -20.35300 -6.24400  1.000 16.22285 ? 181 ARG A NH2 1 
ATOM   1361 N  N   . VAL A 1 182 ? -37.01000 -13.78200 -9.33600  1.000 12.75388 ? 182 VAL A N   1 
ATOM   1362 C  CA  . VAL A 1 182 ? -35.87100 -13.14400 -10.00800 1.000 13.65429 ? 182 VAL A CA  1 
ATOM   1363 C  C   . VAL A 1 182 ? -34.95800 -12.57200 -8.92800  1.000 13.19381 ? 182 VAL A C   1 
ATOM   1364 O  O   . VAL A 1 182 ? -35.40500 -11.76000 -8.11400  1.000 14.42534 ? 182 VAL A O   1 
ATOM   1365 C  CB  . VAL A 1 182 ? -36.31200 -12.03300 -10.98200 1.000 13.78900 ? 182 VAL A CB  1 
ATOM   1366 C  CG1 . VAL A 1 182 ? -35.11900 -11.55900 -11.84200 1.000 12.64617 ? 182 VAL A CG1 1 
ATOM   1367 C  CG2 . VAL A 1 182 ? -37.44400 -12.52000 -11.89800 1.000 14.21705 ? 182 VAL A CG2 1 
ATOM   1368 N  N   . ASN A 1 183 ? -33.68500 -12.98100 -8.92400  1.000 12.20524 ? 183 ASN A N   1 
ATOM   1369 C  CA  . ASN A 1 183 ? -32.73500 -12.49700 -7.92700  1.000 12.30834 ? 183 ASN A CA  1 
ATOM   1370 C  C   . ASN A 1 183 ? -31.39800 -12.28000 -8.60900  1.000 11.67286 ? 183 ASN A C   1 
ATOM   1371 O  O   . ASN A 1 183 ? -31.16300 -12.78800 -9.71200  1.000 13.87261 ? 183 ASN A O   1 
ATOM   1372 C  CB  . ASN A 1 183 ? -32.54900 -13.50500 -6.77600  1.000 14.19869 ? 183 ASN A CB  1 
ATOM   1373 C  CG  . ASN A 1 183 ? -33.79700 -13.67500 -5.95000  1.000 14.51325 ? 183 ASN A CG  1 
ATOM   1374 O  OD1 . ASN A 1 183 ? -34.12200 -12.82900 -5.10600  1.000 14.23007 ? 183 ASN A OD1 1 
ATOM   1375 N  ND2 . ASN A 1 183 ? -34.52400 -14.77700 -6.18700  1.000 14.67266 ? 183 ASN A ND2 1 
ATOM   1376 N  N   . THR A 1 184 ? -30.53000 -11.50300 -7.97500  1.000 13.26749 ? 184 THR A N   1 
ATOM   1377 C  CA  . THR A 1 184 ? -29.20500 -11.26700 -8.52700  1.000 13.72258 ? 184 THR A CA  1 
ATOM   1378 C  C   . THR A 1 184 ? -28.12700 -11.83000 -7.60400  1.000 12.49411 ? 184 THR A C   1 
ATOM   1379 O  O   . THR A 1 184 ? -28.27800 -11.84300 -6.37200  1.000 14.23090 ? 184 THR A O   1 
ATOM   1380 C  CB  . THR A 1 184 ? -28.94500 -9.77800  -8.79500  1.000 13.80862 ? 184 THR A CB  1 
ATOM   1381 O  OG1 . THR A 1 184 ? -29.21400 -9.00700  -7.62900  1.000 14.93277 ? 184 THR A OG1 1 
ATOM   1382 C  CG2 . THR A 1 184 ? -29.83500 -9.24700  -9.91800  1.000 13.79737 ? 184 THR A CG2 1 
ATOM   1383 N  N   . VAL A 1 185 ? -27.07100 -12.33900 -8.23000  1.000 12.98234 ? 185 VAL A N   1 
ATOM   1384 C  CA  . VAL A 1 185 ? -25.88400 -12.83900 -7.54100  1.000 12.88792 ? 185 VAL A CA  1 
ATOM   1385 C  C   . VAL A 1 185 ? -24.73100 -11.89700 -7.86200  1.000 13.34078 ? 185 VAL A C   1 
ATOM   1386 O  O   . VAL A 1 185 ? -24.55900 -11.47600 -9.01400  1.000 14.91992 ? 185 VAL A O   1 
ATOM   1387 C  CB  . VAL A 1 185 ? -25.56500 -14.28200 -7.96100  1.000 14.21327 ? 185 VAL A CB  1 
ATOM   1388 C  CG1 . VAL A 1 185 ? -24.18700 -14.73100 -7.43900  1.000 14.56323 ? 185 VAL A CG1 1 
ATOM   1389 C  CG2 . VAL A 1 185 ? -26.65400 -15.21400 -7.45300  1.000 16.20328 ? 185 VAL A CG2 1 
ATOM   1390 N  N   . HIS A 1 186 ? -23.95600 -11.53500 -6.83100  1.000 13.04013 ? 186 HIS A N   1 
ATOM   1391 C  CA  . HIS A 1 186 ? -22.91400 -10.52100 -6.97100  1.000 12.21446 ? 186 HIS A CA  1 
ATOM   1392 C  C   . HIS A 1 186 ? -21.58800 -11.10500 -6.52100  1.000 12.98570 ? 186 HIS A C   1 
ATOM   1393 O  O   . HIS A 1 186 ? -21.21000 -10.97500 -5.34700  1.000 12.75606 ? 186 HIS A O   1 
ATOM   1394 C  CB  . HIS A 1 186 ? -23.26400 -9.28800  -6.14400  1.000 12.17883 ? 186 HIS A CB  1 
ATOM   1395 C  CG  . HIS A 1 186 ? -24.57500 -8.68100  -6.53300  1.000 13.34829 ? 186 HIS A CG  1 
ATOM   1396 N  ND1 . HIS A 1 186 ? -24.65200 -7.51300  -7.25700  1.000 14.73552 ? 186 HIS A ND1 1 
ATOM   1397 C  CD2 . HIS A 1 186 ? -25.85600 -9.07700  -6.31300  1.000 13.84630 ? 186 HIS A CD2 1 
ATOM   1398 C  CE1 . HIS A 1 186 ? -25.92600 -7.20600  -7.45800  1.000 14.32081 ? 186 HIS A CE1 1 
ATOM   1399 N  NE2 . HIS A 1 186 ? -26.67000 -8.15400  -6.91700  1.000 13.00942 ? 186 HIS A NE2 1 
ATOM   1400 N  N   . PRO A 1 187 ? -20.86000 -11.75800 -7.41300  1.000 13.10981 ? 187 PRO A N   1 
ATOM   1401 C  CA  . PRO A 1 187 ? -19.53100 -12.25000 -7.04800  1.000 12.93666 ? 187 PRO A CA  1 
ATOM   1402 C  C   . PRO A 1 187 ? -18.56600 -11.10700 -6.82400  1.000 13.64658 ? 187 PRO A C   1 
ATOM   1403 O  O   . PRO A 1 187 ? -18.60500 -10.07900 -7.51700  1.000 14.64580 ? 187 PRO A O   1 
ATOM   1404 C  CB  . PRO A 1 187 ? -19.11400 -13.09500 -8.26700  1.000 14.67949 ? 187 PRO A CB  1 
ATOM   1405 C  CG  . PRO A 1 187 ? -20.37900 -13.33900 -9.02400  1.000 16.37637 ? 187 PRO A CG  1 
ATOM   1406 C  CD  . PRO A 1 187 ? -21.24400 -12.13500 -8.78900  1.000 13.98405 ? 187 PRO A CD  1 
ATOM   1407 N  N   . GLY A 1 188 ? -17.67300 -11.31500 -5.85600  1.000 14.20435 ? 188 GLY A N   1 
ATOM   1408 C  CA  . GLY A 1 188 ? -16.42500 -10.58300 -5.79800  1.000 14.29634 ? 188 GLY A CA  1 
ATOM   1409 C  C   . GLY A 1 188 ? -15.42900 -11.16500 -6.77900  1.000 14.65567 ? 188 GLY A C   1 
ATOM   1410 O  O   . GLY A 1 188 ? -15.79100 -11.75300 -7.79800  1.000 16.30981 ? 188 GLY A O   1 
ATOM   1411 N  N   . TYR A 1 189 ? -14.15100 -11.03700 -6.46100  1.000 15.38755 ? 189 TYR A N   1 
ATOM   1412 C  CA  . TYR A 1 189 ? -13.13100 -11.58100 -7.35300  1.000 14.14621 ? 189 TYR A CA  1 
ATOM   1413 C  C   . TYR A 1 189 ? -13.05200 -13.09700 -7.21000  1.000 15.95899 ? 189 TYR A C   1 
ATOM   1414 O  O   . TYR A 1 189 ? -12.98200 -13.61800 -6.09400  1.000 16.35967 ? 189 TYR A O   1 
ATOM   1415 C  CB  . TYR A 1 189 ? -11.77100 -10.97000 -7.03500  1.000 16.96298 ? 189 TYR A CB  1 
ATOM   1416 C  CG  . TYR A 1 189 ? -11.65900 -9.51300  -7.37300  1.000 17.17785 ? 189 TYR A CG  1 
ATOM   1417 C  CD1 . TYR A 1 189 ? -12.01300 -9.03200  -8.62700  1.000 19.34994 ? 189 TYR A CD1 1 
ATOM   1418 C  CD2 . TYR A 1 189 ? -11.16500 -8.61900  -6.43400  1.000 19.64875 ? 189 TYR A CD2 1 
ATOM   1419 C  CE1 . TYR A 1 189 ? -11.87500 -7.68700  -8.92900  1.000 20.94783 ? 189 TYR A CE1 1 
ATOM   1420 C  CE2 . TYR A 1 189 ? -11.01100 -7.28700  -6.73500  1.000 22.26762 ? 189 TYR A CE2 1 
ATOM   1421 C  CZ  . TYR A 1 189 ? -11.37900 -6.83000  -7.96600  1.000 22.68947 ? 189 TYR A CZ  1 
ATOM   1422 O  OH  . TYR A 1 189 ? -11.22900 -5.49700  -8.24900  1.000 28.48136 ? 189 TYR A OH  1 
ATOM   1423 N  N   . ILE A 1 190 ? -13.07100 -13.80900 -8.34000  1.000 16.62778 ? 190 ILE A N   1 
ATOM   1424 C  CA  . ILE A 1 190 ? -13.10600 -15.27300 -8.37400  1.000 17.36837 ? 190 ILE A CA  1 
ATOM   1425 C  C   . ILE A 1 190 ? -11.98900 -15.74800 -9.29600  1.000 17.93595 ? 190 ILE A C   1 
ATOM   1426 O  O   . ILE A 1 190 ? -11.80000 -15.18400 -10.37900 1.000 19.19504 ? 190 ILE A O   1 
ATOM   1427 C  CB  . ILE A 1 190 ? -14.47000 -15.79700 -8.90000  1.000 18.33470 ? 190 ILE A CB  1 
ATOM   1428 C  CG1 . ILE A 1 190 ? -15.65200 -15.25700 -8.07300  1.000 17.69232 ? 190 ILE A CG1 1 
ATOM   1429 C  CG2 . ILE A 1 190 ? -14.47000 -17.33000 -8.97000  1.000 17.82198 ? 190 ILE A CG2 1 
ATOM   1430 C  CD1 . ILE A 1 190 ? -15.69700 -15.77400 -6.61400  1.000 19.02474 ? 190 ILE A CD1 1 
ATOM   1431 N  N   . LYS A 1 191 ? -11.26300 -16.78900 -8.88000  1.000 17.24625 ? 191 LYS A N   1 
ATOM   1432 C  CA  . LYS A 1 191 ? -10.18300 -17.34900 -9.70500  1.000 19.36227 ? 191 LYS A CA  1 
ATOM   1433 C  C   . LYS A 1 191 ? -10.79400 -18.06800 -10.90300 1.000 26.13508 ? 191 LYS A C   1 
ATOM   1434 O  O   . LYS A 1 191 ? -11.42200 -19.12100 -10.75300 1.000 27.02440 ? 191 LYS A O   1 
ATOM   1435 C  CB  . LYS A 1 191 ? -9.31700  -18.28800 -8.86900  1.000 20.98990 ? 191 LYS A CB  1 
ATOM   1436 C  CG  . LYS A 1 191 ? -7.99900  -18.74900 -9.57200  1.000 23.48294 ? 191 LYS A CG  1 
ATOM   1437 C  CD  . LYS A 1 191 ? -7.12500  -19.53000 -8.58700  1.000 28.55755 ? 191 LYS A CD  1 
ATOM   1438 C  CE  . LYS A 1 191 ? -5.88000  -20.14400 -9.24400  1.000 34.11806 ? 191 LYS A CE  1 
ATOM   1439 N  NZ  . LYS A 1 191 ? -4.78700  -19.14900 -9.40800  1.000 35.00644 ? 191 LYS A NZ  1 
ATOM   1440 N  N   . THR A 1 192 ? -10.63500 -17.47800 -12.08500 1.000 27.29050 ? 192 THR A N   1 
ATOM   1441 C  CA  . THR A 1 192 ? -11.16600 -17.98100 -13.35000 1.000 32.54209 ? 192 THR A CA  1 
ATOM   1442 C  C   . THR A 1 192 ? -10.00800 -18.10500 -14.32500 1.000 35.89061 ? 192 THR A C   1 
ATOM   1443 O  O   . THR A 1 192 ? -8.89700  -17.64700 -14.02200 1.000 34.07075 ? 192 THR A O   1 
ATOM   1444 C  CB  . THR A 1 192 ? -12.22900 -17.04400 -13.92300 1.000 34.45799 ? 192 THR A CB  1 
ATOM   1445 O  OG1 . THR A 1 192 ? -11.65500 -15.75400 -14.17100 1.000 35.77071 ? 192 THR A OG1 1 
ATOM   1446 C  CG2 . THR A 1 192 ? -13.41700 -16.91700 -12.97500 1.000 33.50300 ? 192 THR A CG2 1 
ATOM   1447 N  N   . PRO A 1 193 ? -10.21700 -18.72200 -15.49500 1.000 37.94711 ? 193 PRO A N   1 
ATOM   1448 C  CA  . PRO A 1 193 ? -9.13800  -18.74900 -16.49500 1.000 39.28163 ? 193 PRO A CA  1 
ATOM   1449 C  C   . PRO A 1 193 ? -8.69500  -17.36500 -16.93800 1.000 38.98560 ? 193 PRO A C   1 
ATOM   1450 O  O   . PRO A 1 193 ? -7.49700  -17.14600 -17.13400 1.000 39.35667 ? 193 PRO A O   1 
ATOM   1451 C  CB  . PRO A 1 193 ? -9.76200  -19.54800 -17.65000 1.000 40.81491 ? 193 PRO A CB  1 
ATOM   1452 C  CG  . PRO A 1 193 ? -11.24200 -19.52800 -17.39300 1.000 40.16468 ? 193 PRO A CG  1 
ATOM   1453 C  CD  . PRO A 1 193 ? -11.37500 -19.53200 -15.91800 1.000 39.80466 ? 193 PRO A CD  1 
ATOM   1454 N  N   . LEU A 1 194 ? -9.62600  -16.41800 -17.09900 1.000 39.20119 ? 194 LEU A N   1 
ATOM   1455 C  CA  . LEU A 1 194 ? -9.22900  -15.05900 -17.45900 1.000 41.72230 ? 194 LEU A CA  1 
ATOM   1456 C  C   . LEU A 1 194 ? -8.28800  -14.46500 -16.41700 1.000 39.91119 ? 194 LEU A C   1 
ATOM   1457 O  O   . LEU A 1 194 ? -7.28700  -13.82600 -16.76700 1.000 41.90537 ? 194 LEU A O   1 
ATOM   1458 C  CB  . LEU A 1 194 ? -10.45700 -14.16700 -17.62000 1.000 45.68758 ? 194 LEU A CB  1 
ATOM   1459 C  CG  . LEU A 1 194 ? -11.37300 -14.42200 -18.81500 1.000 49.72292 ? 194 LEU A CG  1 
ATOM   1460 C  CD1 . LEU A 1 194 ? -12.49000 -13.38900 -18.83700 1.000 50.13524 ? 194 LEU A CD1 1 
ATOM   1461 C  CD2 . LEU A 1 194 ? -10.59000 -14.41100 -20.13500 1.000 51.72168 ? 194 LEU A CD2 1 
ATOM   1462 N  N   . VAL A 1 195 ? -8.59400  -14.66800 -15.13000 1.000 39.54131 ? 195 VAL A N   1 
ATOM   1463 C  CA  . VAL A 1 195 ? -7.73500  -14.15000 -14.06500 1.000 34.90480 ? 195 VAL A CA  1 
ATOM   1464 C  C   . VAL A 1 195 ? -6.34900  -14.77600 -14.15000 1.000 34.91838 ? 195 VAL A C   1 
ATOM   1465 O  O   . VAL A 1 195 ? -5.32300  -14.08800 -14.05200 1.000 35.08164 ? 195 VAL A O   1 
ATOM   1466 C  CB  . VAL A 1 195 ? -8.37600  -14.39700 -12.68500 1.000 30.41713 ? 195 VAL A CB  1 
ATOM   1467 C  CG1 . VAL A 1 195 ? -7.38200  -14.05200 -11.57200 1.000 30.21440 ? 195 VAL A CG1 1 
ATOM   1468 C  CG2 . VAL A 1 195 ? -9.67700  -13.60300 -12.55200 1.000 31.42585 ? 195 VAL A CG2 1 
ATOM   1469 N  N   . ASP A 1 196 ? -6.29300  -16.09300 -14.34200 1.000 34.88746 ? 196 ASP A N   1 
ATOM   1470 C  CA  . ASP A 1 196 ? -4.99200  -16.74800 -14.37100 1.000 37.77225 ? 196 ASP A CA  1 
ATOM   1471 C  C   . ASP A 1 196 ? -4.17600  -16.36000 -15.59500 1.000 39.77037 ? 196 ASP A C   1 
ATOM   1472 O  O   . ASP A 1 196 ? -2.95900  -16.56800 -15.59400 1.000 40.18466 ? 196 ASP A O   1 
ATOM   1473 C  CB  . ASP A 1 196 ? -5.14700  -18.26500 -14.32700 1.000 40.82483 ? 196 ASP A CB  1 
ATOM   1474 C  CG  . ASP A 1 196 ? -5.68100  -18.75700 -12.99500 1.000 43.61865 ? 196 ASP A CG  1 
ATOM   1475 O  OD1 . ASP A 1 196 ? -5.52900  -18.04000 -11.97800 1.000 43.63091 ? 196 ASP A OD1 1 
ATOM   1476 O  OD2 . ASP A 1 196 ? -6.25700  -19.86700 -12.97100 1.000 44.49908 ? 196 ASP A OD2 1 
ATOM   1477 N  N   . ASP A 1 197 ? -4.81200  -15.80500 -16.62900 0.747 39.44580 ? 197 ASP A N   1 
ATOM   1478 C  CA  . ASP A 1 197 ? -4.10900  -15.36400 -17.82800 0.747 40.84880 ? 197 ASP A CA  1 
ATOM   1479 C  C   . ASP A 1 197 ? -3.58800  -13.93500 -17.71600 0.747 39.92750 ? 197 ASP A C   1 
ATOM   1480 O  O   . ASP A 1 197 ? -2.89900  -13.47100 -18.63000 0.747 39.55334 ? 197 ASP A O   1 
ATOM   1481 C  CB  . ASP A 1 197 ? -5.02100  -15.49900 -19.06400 0.747 41.11198 ? 197 ASP A CB  1 
ATOM   1482 C  CG  . ASP A 1 197 ? -5.10000  -16.94500 -19.59700 0.747 42.11916 ? 197 ASP A CG  1 
ATOM   1483 O  OD1 . ASP A 1 197 ? -4.11000  -17.70300 -19.44300 0.747 42.62202 ? 197 ASP A OD1 1 
ATOM   1484 O  OD2 . ASP A 1 197 ? -6.15400  -17.32300 -20.17000 0.747 40.98602 ? 197 ASP A OD2 1 
ATOM   1485 N  N   . LEU A 1 198 ? -3.88100  -13.23200 -16.62200 1.000 39.20757 ? 198 LEU A N   1 
ATOM   1486 C  CA  . LEU A 1 198 ? -3.40300  -11.86500 -16.43600 1.000 38.32137 ? 198 LEU A CA  1 
ATOM   1487 C  C   . LEU A 1 198 ? -2.34400  -11.82500 -15.34500 1.000 34.77221 ? 198 LEU A C   1 
ATOM   1488 O  O   . LEU A 1 198 ? -2.68700  -11.90000 -14.15600 1.000 30.25258 ? 198 LEU A O   1 
ATOM   1489 C  CB  . LEU A 1 198 ? -4.55500  -10.92900 -16.07900 1.000 39.49320 ? 198 LEU A CB  1 
ATOM   1490 C  CG  . LEU A 1 198 ? -5.54200  -10.60200 -17.18900 1.000 42.25821 ? 198 LEU A CG  1 
ATOM   1491 C  CD1 . LEU A 1 198 ? -6.86200  -10.15500 -16.59100 1.000 41.28960 ? 198 LEU A CD1 1 
ATOM   1492 C  CD2 . LEU A 1 198 ? -4.95300  -9.53200  -18.10900 1.000 44.21970 ? 198 LEU A CD2 1 
ATOM   1493 N  N   . PRO A 1 199 ? -1.06600  -11.69000 -15.68000 1.000 35.89053 ? 199 PRO A N   1 
ATOM   1494 C  CA  . PRO A 1 199 ? -0.03200  -11.72900 -14.64100 1.000 34.06947 ? 199 PRO A CA  1 
ATOM   1495 C  C   . PRO A 1 199 ? -0.25500  -10.63600 -13.60700 1.000 30.58676 ? 199 PRO A C   1 
ATOM   1496 O  O   . PRO A 1 199 ? -0.49400  -9.47500  -13.94800 1.000 31.64180 ? 199 PRO A O   1 
ATOM   1497 C  CB  . PRO A 1 199 ? 1.26700   -11.51800 -15.42800 1.000 37.01153 ? 199 PRO A CB  1 
ATOM   1498 C  CG  . PRO A 1 199 ? 0.93900   -11.96600 -16.81900 1.000 37.47980 ? 199 PRO A CG  1 
ATOM   1499 C  CD  . PRO A 1 199 ? -0.48600  -11.57000 -17.03200 1.000 36.57511 ? 199 PRO A CD  1 
ATOM   1500 N  N   . GLY A 1 200 ? -0.20500  -11.02500 -12.32600 1.000 27.95004 ? 200 GLY A N   1 
ATOM   1501 C  CA  . GLY A 1 200 ? -0.37300  -10.07700 -11.24800 1.000 24.04669 ? 200 GLY A CA  1 
ATOM   1502 C  C   . GLY A 1 200 ? -1.80800  -9.78900  -10.84800 1.000 22.43736 ? 200 GLY A C   1 
ATOM   1503 O  O   . GLY A 1 200 ? -2.01800  -9.12900  -9.82600  1.000 22.40032 ? 200 GLY A O   1 
ATOM   1504 N  N   . ALA A 1 201 ? -2.79000  -10.23700 -11.63500 1.000 22.03645 ? 201 ALA A N   1 
ATOM   1505 C  CA  . ALA A 1 201 ? -4.18500  -9.92200  -11.35000 1.000 21.33288 ? 201 ALA A CA  1 
ATOM   1506 C  C   . ALA A 1 201 ? -4.61500  -10.47800 -10.00200 1.000 20.08540 ? 201 ALA A C   1 
ATOM   1507 O  O   . ALA A 1 201 ? -5.19600  -9.75800  -9.17800  1.000 18.90421 ? 201 ALA A O   1 
ATOM   1508 C  CB  . ALA A 1 201 ? -5.08000  -10.47200 -12.46000 1.000 23.05955 ? 201 ALA A CB  1 
ATOM   1509 N  N   . GLU A 1 202 ? -4.34400  -11.76100 -9.75700  1.000 21.07042 ? 202 GLU A N   1 
ATOM   1510 C  CA  . GLU A 1 202 ? -4.82300  -12.37500 -8.52000  1.000 18.70343 ? 202 GLU A CA  1 
ATOM   1511 C  C   . GLU A 1 202 ? -4.20900  -11.70300 -7.29500  1.000 18.09818 ? 202 GLU A C   1 
ATOM   1512 O  O   . GLU A 1 202 ? -4.89900  -11.45500 -6.29600  1.000 18.08711 ? 202 GLU A O   1 
ATOM   1513 C  CB  . GLU A 1 202 ? -4.50200  -13.86800 -8.52600  1.000 19.20638 ? 202 GLU A CB  1 
ATOM   1514 C  CG  . GLU A 1 202 ? -4.87800  -14.56400 -7.22900  1.000 21.75651 ? 202 GLU A CG  1 
ATOM   1515 C  CD  . GLU A 1 202 ? -4.79600  -16.07600 -7.29600  1.000 27.43815 ? 202 GLU A CD  1 
ATOM   1516 O  OE1 . GLU A 1 202 ? -4.44300  -16.62900 -8.37300  1.000 29.06096 ? 202 GLU A OE1 1 
ATOM   1517 O  OE2 . GLU A 1 202 ? -5.07200  -16.71800 -6.26000  1.000 28.17685 ? 202 GLU A OE2 1 
ATOM   1518 N  N   . GLU A 1 203 ? -2.92000  -11.37100 -7.36500  1.000 18.80671 ? 203 GLU A N   1 
ATOM   1519 C  CA  . GLU A 1 203 ? -2.28300  -10.70100 -6.23000  1.000 18.36058 ? 203 GLU A CA  1 
ATOM   1520 C  C   . GLU A 1 203 ? -2.93200  -9.35300  -5.97900  1.000 17.84362 ? 203 GLU A C   1 
ATOM   1521 O  O   . GLU A 1 203 ? -3.19600  -8.98500  -4.82500  1.000 18.42427 ? 203 GLU A O   1 
ATOM   1522 C  CB  . GLU A 1 203 ? -0.77700  -10.54100 -6.47800  1.000 19.12392 ? 203 GLU A CB  1 
ATOM   1523 C  CG  . GLU A 1 203 ? -0.05000  -9.75800  -5.35300  1.000 19.75418 ? 203 GLU A CG  1 
ATOM   1524 C  CD  . GLU A 1 203 ? 1.44600   -9.82200  -5.47100  1.000 23.49868 ? 203 GLU A CD  1 
ATOM   1525 O  OE1 . GLU A 1 203 ? 2.13700   -9.34400  -4.54600  1.000 22.33867 ? 203 GLU A OE1 1 
ATOM   1526 O  OE2 . GLU A 1 203 ? 1.94300   -10.34500 -6.49200  1.000 26.44177 ? 203 GLU A OE2 1 
ATOM   1527 N  N   . ALA A 1 204 ? -3.22700  -8.60900  -7.05400  1.000 18.46893 ? 204 ALA A N   1 
ATOM   1528 C  CA  . ALA A 1 204 ? -3.87700  -7.31100  -6.88900  1.000 17.86741 ? 204 ALA A CA  1 
ATOM   1529 C  C   . ALA A 1 204 ? -5.26600  -7.46700  -6.28900  1.000 16.70365 ? 204 ALA A C   1 
ATOM   1530 O  O   . ALA A 1 204 ? -5.66400  -6.69700  -5.40600  1.000 19.13098 ? 204 ALA A O   1 
ATOM   1531 C  CB  . ALA A 1 204 ? -3.98000  -6.58900  -8.23400  1.000 18.71081 ? 204 ALA A CB  1 
ATOM   1532 N  N   . MET A 1 205 ? -6.01000  -8.45700  -6.75600  1.000 15.20501 ? 205 MET A N   1 
ATOM   1533 C  CA  . MET A 1 205 ? -7.35200  -8.68900  -6.24600  1.000 14.72237 ? 205 MET A CA  1 
ATOM   1534 C  C   . MET A 1 205 ? -7.34800  -9.15900  -4.79300  1.000 16.17803 ? 205 MET A C   1 
ATOM   1535 O  O   . MET A 1 205 ? -8.36000  -8.98500  -4.10400  1.000 17.93171 ? 205 MET A O   1 
ATOM   1536 C  CB  . MET A 1 205 ? -8.04800  -9.71600  -7.12800  1.000 16.91757 ? 205 MET A CB  1 
ATOM   1537 C  CG  . MET A 1 205 ? -8.30700  -9.22600  -8.53800  1.000 18.56185 ? 205 MET A CG  1 
ATOM   1538 S  SD  . MET A 1 205 ? -8.71000  -10.65300 -9.54400  1.000 24.25199 ? 205 MET A SD  1 
ATOM   1539 C  CE  . MET A 1 205 ? -9.11400  -9.85000  -11.11000 1.000 27.47339 ? 205 MET A CE  1 
ATOM   1540 N  N   . SER A 1 206 ? -6.25000  -9.76900  -4.34000  1.000 16.87971 ? 206 SER A N   1 
ATOM   1541 C  CA  . SER A 1 206 ? -6.14000  -10.33200 -3.00100  1.000 16.79429 ? 206 SER A CA  1 
ATOM   1542 C  C   . SER A 1 206 ? -5.61900  -9.35000  -1.96100  1.000 16.54547 ? 206 SER A C   1 
ATOM   1543 O  O   . SER A 1 206 ? -5.53700  -9.71900  -0.78200  1.000 17.64949 ? 206 SER A O   1 
ATOM   1544 C  CB  . SER A 1 206 ? -5.21400  -11.55600 -3.03000  1.000 18.57751 ? 206 SER A CB  1 
ATOM   1545 O  OG  . SER A 1 206 ? -5.61700  -12.48500 -4.02100  1.000 19.15579 ? 206 SER A OG  1 
ATOM   1546 N  N   . GLN A 1 207 ? -5.21400  -8.14100  -2.35400  1.000 16.78642 ? 207 GLN A N   1 
ATOM   1547 C  CA  . GLN A 1 207 ? -4.78400  -7.16800  -1.35500  1.000 19.40484 ? 207 GLN A CA  1 
ATOM   1548 C  C   . GLN A 1 207 ? -5.92800  -6.91700  -0.37800  1.000 17.62537 ? 207 GLN A C   1 
ATOM   1549 O  O   . GLN A 1 207 ? -7.09300  -6.86300  -0.77400  1.000 16.23770 ? 207 GLN A O   1 
ATOM   1550 C  CB  . GLN A 1 207 ? -4.37100  -5.85300  -2.01500  1.000 22.05322 ? 207 GLN A CB  1 
ATOM   1551 C  CG  . GLN A 1 207 ? -3.22900  -5.98700  -3.01400  1.000 22.65205 ? 207 GLN A CG  1 
ATOM   1552 C  CD  . GLN A 1 207 ? -1.98800  -6.56300  -2.37700  1.000 28.63874 ? 207 GLN A CD  1 
ATOM   1553 O  OE1 . GLN A 1 207 ? -1.36400  -7.47800  -2.92000  1.000 34.17384 ? 207 GLN A OE1 1 
ATOM   1554 N  NE2 . GLN A 1 207 ? -1.60400  -6.02400  -1.22900  1.000 28.38200 ? 207 GLN A NE2 1 
ATOM   1555 N  N   . ARG A 1 208 ? -5.59000  -6.74500  0.90400   1.000 17.96383 ? 208 ARG A N   1 
ATOM   1556 C  CA  . ARG A 1 208 ? -6.63400  -6.59800  1.92500   1.000 15.31079 ? 208 ARG A CA  1 
ATOM   1557 C  C   . ARG A 1 208 ? -7.50800  -5.37800  1.67500   1.000 16.41102 ? 208 ARG A C   1 
ATOM   1558 O  O   . ARG A 1 208 ? -8.68400  -5.37600  2.05300   1.000 17.28561 ? 208 ARG A O   1 
ATOM   1559 C  CB  . ARG A 1 208 ? -5.99900  -6.48000  3.31600   1.000 16.00226 ? 208 ARG A CB  1 
ATOM   1560 C  CG  . ARG A 1 208 ? -5.08500  -7.61900  3.70300   1.000 18.63338 ? 208 ARG A CG  1 
ATOM   1561 C  CD  . ARG A 1 208 ? -5.83700  -8.92100  3.96500   1.000 18.18600 ? 208 ARG A CD  1 
ATOM   1562 N  NE  . ARG A 1 208 ? -4.94300  -9.88200  4.61400   1.000 17.92497 ? 208 ARG A NE  1 
ATOM   1563 C  CZ  . ARG A 1 208 ? -5.32300  -11.01500 5.18900   1.000 17.31573 ? 208 ARG A CZ  1 
ATOM   1564 N  NH1 . ARG A 1 208 ? -6.61100  -11.36700 5.19700   1.000 16.42577 ? 208 ARG A NH1 1 
ATOM   1565 N  NH2 . ARG A 1 208 ? -4.41600  -11.79500 5.75800   1.000 20.09683 ? 208 ARG A NH2 1 
ATOM   1566 N  N   . THR A 1 209 ? -6.95100  -4.32900  1.05600   1.000 17.42758 ? 209 THR A N   1 
ATOM   1567 C  CA  . THR A 1 209 ? -7.70300  -3.13600  0.67600   1.000 16.92623 ? 209 THR A CA  1 
ATOM   1568 C  C   . THR A 1 209 ? -8.72500  -3.40300  -0.41800  1.000 18.54126 ? 209 THR A C   1 
ATOM   1569 O  O   . THR A 1 209 ? -9.56300  -2.53100  -0.67400  1.000 18.69393 ? 209 THR A O   1 
ATOM   1570 C  CB  . THR A 1 209 ? -6.76400  -2.02800  0.20500   1.000 20.92841 ? 209 THR A CB  1 
ATOM   1571 O  OG1 . THR A 1 209 ? -5.81600  -2.58600  -0.70900  1.000 22.85547 ? 209 THR A OG1 1 
ATOM   1572 C  CG2 . THR A 1 209 ? -6.01600  -1.42500  1.40200   1.000 22.27754 ? 209 THR A CG2 1 
ATOM   1573 N  N   . LYS A 1 210 ? -8.67100  -4.57000  -1.05600  1.000 16.53017 ? 210 LYS A N   1 
ATOM   1574 C  CA  . LYS A 1 210 ? -9.67000  -4.99600  -2.03600  1.000 16.52572 ? 210 LYS A CA  1 
ATOM   1575 C  C   . LYS A 1 210 ? -10.50400 -6.12500  -1.44300  1.000 15.24722 ? 210 LYS A C   1 
ATOM   1576 O  O   . LYS A 1 210 ? -11.70000 -5.93600  -1.17200  1.000 14.72972 ? 210 LYS A O   1 
ATOM   1577 C  CB  . LYS A 1 210 ? -9.00900  -5.43500  -3.35400  1.000 18.32843 ? 210 LYS A CB  1 
ATOM   1578 C  CG  . LYS A 1 210 ? -8.28400  -4.30500  -4.08300  1.000 22.25137 ? 210 LYS A CG  1 
ATOM   1579 C  CD  . LYS A 1 210 ? -9.30500  -3.25100  -4.57000  1.000 27.24494 ? 210 LYS A CD  1 
ATOM   1580 C  CE  . LYS A 1 210 ? -8.60500  -2.10000  -5.28500  1.000 32.04259 ? 210 LYS A CE  1 
ATOM   1581 N  NZ  . LYS A 1 210 ? -9.60200  -1.18600  -5.91700  1.000 34.94725 ? 210 LYS A NZ  1 
ATOM   1582 N  N   . THR A 1 211 ? -9.89900  -7.30000  -1.19700  1.000 14.85893 ? 211 THR A N   1 
ATOM   1583 C  CA  . THR A 1 211 ? -10.61400 -8.42900  -0.61100  1.000 13.85866 ? 211 THR A CA  1 
ATOM   1584 C  C   . THR A 1 211 ? -10.10300 -8.66900  0.80100   1.000 14.16113 ? 211 THR A C   1 
ATOM   1585 O  O   . THR A 1 211 ? -8.98000  -9.16600  0.96200   1.000 15.08147 ? 211 THR A O   1 
ATOM   1586 C  CB  . THR A 1 211 ? -10.42800 -9.69800  -1.45700  1.000 15.82959 ? 211 THR A CB  1 
ATOM   1587 O  OG1 . THR A 1 211 ? -10.79200 -9.41600  -2.82000  1.000 15.25401 ? 211 THR A OG1 1 
ATOM   1588 C  CG2 . THR A 1 211 ? -11.32800 -10.82600 -0.93800  1.000 16.94299 ? 211 THR A CG2 1 
ATOM   1589 N  N   . PRO A 1 212 ? -10.87500 -8.34700  1.84400   1.000 14.05169 ? 212 PRO A N   1 
ATOM   1590 C  CA  . PRO A 1 212 ? -10.35100 -8.47500  3.21700   1.000 14.40671 ? 212 PRO A CA  1 
ATOM   1591 C  C   . PRO A 1 212 ? -9.91100  -9.88400  3.59100   1.000 14.70069 ? 212 PRO A C   1 
ATOM   1592 O  O   . PRO A 1 212 ? -9.01700  -10.02300 4.43200   1.000 15.12603 ? 212 PRO A O   1 
ATOM   1593 C  CB  . PRO A 1 212 ? -11.54000 -8.01000  4.07400   1.000 15.41782 ? 212 PRO A CB  1 
ATOM   1594 C  CG  . PRO A 1 212 ? -12.26300 -7.05600  3.19000   1.000 15.19440 ? 212 PRO A CG  1 
ATOM   1595 C  CD  . PRO A 1 212 ? -12.14500 -7.61100  1.78100   1.000 13.66943 ? 212 PRO A CD  1 
ATOM   1596 N  N   . MET A 1 213 ? -10.48900 -10.92700 2.97600   1.000 14.63787 ? 213 MET A N   1 
ATOM   1597 C  CA  . MET A 1 213 ? -10.04300 -12.28900 3.26800   1.000 15.80638 ? 213 MET A CA  1 
ATOM   1598 C  C   . MET A 1 213 ? -8.62600  -12.55700 2.78400   1.000 16.35609 ? 213 MET A C   1 
ATOM   1599 O  O   . MET A 1 213 ? -8.04800  -13.57200 3.18200   1.000 16.64901 ? 213 MET A O   1 
ATOM   1600 C  CB  . MET A 1 213 ? -11.00100 -13.30800 2.64300   1.000 15.62573 ? 213 MET A CB  1 
ATOM   1601 C  CG  . MET A 1 213 ? -12.25100 -13.50700 3.43000   1.000 15.82545 ? 213 MET A CG  1 
ATOM   1602 S  SD  . MET A 1 213 ? -13.17300 -14.91000 2.75700   1.000 17.68188 ? 213 MET A SD  1 
ATOM   1603 C  CE  . MET A 1 213 ? -14.51100 -15.03600 3.90900   1.000 20.32343 ? 213 MET A CE  1 
ATOM   1604 N  N   . GLY A 1 214 ? -8.07100  -11.69200 1.92900   1.000 15.68138 ? 214 GLY A N   1 
ATOM   1605 C  CA  . GLY A 1 214 ? -6.67000  -11.84000 1.55000   1.000 15.64949 ? 214 GLY A CA  1 
ATOM   1606 C  C   . GLY A 1 214 ? -6.42100  -12.82800 0.43000   1.000 15.74135 ? 214 GLY A C   1 
ATOM   1607 O  O   . GLY A 1 214 ? -5.27100  -13.21300 0.20300   1.000 16.74063 ? 214 GLY A O   1 
ATOM   1608 N  N   . HIS A 1 215 ? -7.47600  -13.28800 -0.22400  1.000 18.03659 ? 215 HIS A N   1 
ATOM   1609 C  CA  . HIS A 1 215 ? -7.40000  -14.21200 -1.34000  1.000 16.45330 ? 215 HIS A CA  1 
ATOM   1610 C  C   . HIS A 1 215 ? -8.70700  -14.05000 -2.08700  1.000 18.09636 ? 215 HIS A C   1 
ATOM   1611 O  O   . HIS A 1 215 ? -9.65200  -13.46400 -1.56300  1.000 17.81421 ? 215 HIS A O   1 
ATOM   1612 C  CB  . HIS A 1 215 ? -7.20200  -15.65800 -0.86900  1.000 16.85585 ? 215 HIS A CB  1 
ATOM   1613 C  CG  . HIS A 1 215 ? -8.34100  -16.19300 -0.06000  1.000 18.04812 ? 215 HIS A CG  1 
ATOM   1614 N  ND1 . HIS A 1 215 ? -9.51200  -16.63600 -0.63500  1.000 19.56389 ? 215 HIS A ND1 1 
ATOM   1615 C  CD2 . HIS A 1 215 ? -8.48700  -16.36000 1.27500   1.000 19.49724 ? 215 HIS A CD2 1 
ATOM   1616 C  CE1 . HIS A 1 215 ? -10.34200 -17.04100 0.31200   1.000 19.74510 ? 215 HIS A CE1 1 
ATOM   1617 N  NE2 . HIS A 1 215 ? -9.74700  -16.87900 1.48000   1.000 20.28157 ? 215 HIS A NE2 1 
ATOM   1618 N  N   . ILE A 1 216 ? -8.75000  -14.56000 -3.31000  1.000 16.94979 ? 216 ILE A N   1 
ATOM   1619 C  CA  . ILE A 1 216 ? -9.96500  -14.52400 -4.10200  1.000 16.76067 ? 216 ILE A CA  1 
ATOM   1620 C  C   . ILE A 1 216 ? -10.69000 -15.86100 -3.99100  1.000 16.51902 ? 216 ILE A C   1 
ATOM   1621 O  O   . ILE A 1 216 ? -10.18600 -16.82500 -3.41700  1.000 17.04262 ? 216 ILE A O   1 
ATOM   1622 C  CB  . ILE A 1 216 ? -9.67800  -14.12200 -5.57400  1.000 18.22708 ? 216 ILE A CB  1 
ATOM   1623 C  CG1 . ILE A 1 216 ? -8.82200  -15.16300 -6.29500  1.000 19.23072 ? 216 ILE A CG1 1 
ATOM   1624 C  CG2 . ILE A 1 216 ? -8.99400  -12.76600 -5.59600  1.000 20.54114 ? 216 ILE A CG2 1 
ATOM   1625 C  CD1 . ILE A 1 216 ? -8.52300  -14.79300 -7.75600  1.000 21.44626 ? 216 ILE A CD1 1 
ATOM   1626 N  N   . GLY A 1 217 ? -11.91700 -15.90200 -4.52100  1.000 14.73016 ? 217 GLY A N   1 
ATOM   1627 C  CA  . GLY A 1 217 ? -12.77400 -17.05900 -4.40000  1.000 16.60928 ? 217 GLY A CA  1 
ATOM   1628 C  C   . GLY A 1 217 ? -12.53100 -18.03500 -5.53400  1.000 18.05804 ? 217 GLY A C   1 
ATOM   1629 O  O   . GLY A 1 217 ? -11.59500 -17.89500 -6.32400  1.000 18.42994 ? 217 GLY A O   1 
ATOM   1630 N  N   . GLU A 1 218 ? -13.37500 -19.05400 -5.59100  1.000 16.24050 ? 218 GLU A N   1 
ATOM   1631 C  CA  . GLU A 1 218 ? -13.30100 -20.04800 -6.65200  1.000 18.30614 ? 218 GLU A CA  1 
ATOM   1632 C  C   . GLU A 1 218 ? -14.68400 -20.22800 -7.26700  1.000 17.04867 ? 218 GLU A C   1 
ATOM   1633 O  O   . GLU A 1 218 ? -15.69400 -19.83100 -6.67800  1.000 16.26058 ? 218 GLU A O   1 
ATOM   1634 C  CB  . GLU A 1 218 ? -12.77600 -21.38300 -6.10700  1.000 21.13084 ? 218 GLU A CB  1 
ATOM   1635 C  CG  . GLU A 1 218 ? -13.63000 -21.88100 -4.98500  1.000 26.38027 ? 218 GLU A CG  1 
ATOM   1636 C  CD  . GLU A 1 218 ? -13.60500 -23.36100 -4.82000  1.000 33.18063 ? 218 GLU A CD  1 
ATOM   1637 O  OE1 . GLU A 1 218 ? -12.92000 -24.04800 -5.60400  1.000 35.71661 ? 218 GLU A OE1 1 
ATOM   1638 O  OE2 . GLU A 1 218 ? -14.28800 -23.84500 -3.89800  1.000 34.91890 ? 218 GLU A OE2 1 
ATOM   1639 N  N   . PRO A 1 219 ? -14.76100 -20.79000 -8.47800  1.000 17.20020 ? 219 PRO A N   1 
ATOM   1640 C  CA  . PRO A 1 219 ? -16.06800 -20.88600 -9.15000  1.000 18.05646 ? 219 PRO A CA  1 
ATOM   1641 C  C   . PRO A 1 219 ? -17.15100 -21.58700 -8.34800  1.000 17.06576 ? 219 PRO A C   1 
ATOM   1642 O  O   . PRO A 1 219 ? -18.31600 -21.17700 -8.44500  1.000 17.16380 ? 219 PRO A O   1 
ATOM   1643 C  CB  . PRO A 1 219 ? -15.74100 -21.64400 -10.44000 1.000 17.01785 ? 219 PRO A CB  1 
ATOM   1644 C  CG  . PRO A 1 219 ? -14.30900 -21.22300 -10.74300 1.000 18.54903 ? 219 PRO A CG  1 
ATOM   1645 C  CD  . PRO A 1 219 ? -13.63300 -21.10900 -9.38100  1.000 18.22700 ? 219 PRO A CD  1 
ATOM   1646 N  N   . ASN A 1 220 ? -16.81600 -22.62100 -7.56900  1.000 17.04574 ? 220 ASN A N   1 
ATOM   1647 C  CA  . ASN A 1 220 ? -17.85200 -23.29000 -6.77600  1.000 17.46049 ? 220 ASN A CA  1 
ATOM   1648 C  C   . ASN A 1 220 ? -18.46400 -22.37300 -5.72800  1.000 16.84929 ? 220 ASN A C   1 
ATOM   1649 O  O   . ASN A 1 220 ? -19.61200 -22.61300 -5.32400  1.000 17.28038 ? 220 ASN A O   1 
ATOM   1650 C  CB  . ASN A 1 220 ? -17.28200 -24.53100 -6.08900  1.000 20.51498 ? 220 ASN A CB  1 
ATOM   1651 C  CG  . ASN A 1 220 ? -17.19000 -25.71500 -7.03200  1.000 23.35661 ? 220 ASN A CG  1 
ATOM   1652 O  OD1 . ASN A 1 220 ? -17.86800 -25.75100 -8.06400  1.000 25.03883 ? 220 ASN A OD1 1 
ATOM   1653 N  ND2 . ASN A 1 220 ? -16.33100 -26.67300 -6.69900  1.000 25.53007 ? 220 ASN A ND2 1 
ATOM   1654 N  N   . ASP A 1 221 ? -17.76400 -21.29900 -5.32600  1.000 14.27776 ? 221 ASP A N   1 
ATOM   1655 C  CA  . ASP A 1 221 ? -18.39000 -20.33300 -4.41600  1.000 16.11098 ? 221 ASP A CA  1 
ATOM   1656 C  C   . ASP A 1 221 ? -19.62700 -19.71600 -5.04900  1.000 16.56037 ? 221 ASP A C   1 
ATOM   1657 O  O   . ASP A 1 221 ? -20.64100 -19.49300 -4.37300  1.000 17.78009 ? 221 ASP A O   1 
ATOM   1658 C  CB  . ASP A 1 221 ? -17.40100 -19.22200 -4.04100  1.000 15.53266 ? 221 ASP A CB  1 
ATOM   1659 C  CG  . ASP A 1 221 ? -16.25800 -19.71300 -3.17000  1.000 17.01323 ? 221 ASP A CG  1 
ATOM   1660 O  OD1 . ASP A 1 221 ? -16.49700 -20.56000 -2.27300  1.000 19.15241 ? 221 ASP A OD1 1 
ATOM   1661 O  OD2 . ASP A 1 221 ? -15.10500 -19.24700 -3.38200  1.000 16.22332 ? 221 ASP A OD2 1 
ATOM   1662 N  N   . ILE A 1 222 ? -19.58000 -19.46100 -6.35800  1.000 14.55546 ? 222 ILE A N   1 
ATOM   1663 C  CA  . ILE A 1 222 ? -20.77100 -18.91900 -6.99100  1.000 14.11377 ? 222 ILE A CA  1 
ATOM   1664 C  C   . ILE A 1 222 ? -21.76200 -20.03400 -7.33400  1.000 16.57660 ? 222 ILE A C   1 
ATOM   1665 O  O   . ILE A 1 222 ? -22.97600 -19.82400 -7.24400  1.000 16.46939 ? 222 ILE A O   1 
ATOM   1666 C  CB  . ILE A 1 222 ? -20.36500 -18.08100 -8.21700  1.000 15.10797 ? 222 ILE A CB  1 
ATOM   1667 C  CG1 . ILE A 1 222 ? -19.33400 -17.00000 -7.81400  1.000 14.97903 ? 222 ILE A CG1 1 
ATOM   1668 C  CG2 . ILE A 1 222 ? -21.61000 -17.45700 -8.88000  1.000 16.52320 ? 222 ILE A CG2 1 
ATOM   1669 C  CD1 . ILE A 1 222 ? -19.73100 -16.13500 -6.59300  1.000 15.53088 ? 222 ILE A CD1 1 
ATOM   1670 N  N   . ALA A 1 223 ? -21.28300 -21.23800 -7.67400  1.000 15.60671 ? 223 ALA A N   1 
ATOM   1671 C  CA  . ALA A 1 223 ? -22.19800 -22.34600 -7.94300  1.000 14.93779 ? 223 ALA A CA  1 
ATOM   1672 C  C   . ALA A 1 223 ? -23.13000 -22.60900 -6.75900  1.000 15.50478 ? 223 ALA A C   1 
ATOM   1673 O  O   . ALA A 1 223 ? -24.33100 -22.79700 -6.94700  1.000 14.79278 ? 223 ALA A O   1 
ATOM   1674 C  CB  . ALA A 1 223 ? -21.42100 -23.61300 -8.30500  1.000 16.10310 ? 223 ALA A CB  1 
ATOM   1675 N  N   . TYR A 1 224 ? -22.60600 -22.58800 -5.52600  1.000 14.50753 ? 224 TYR A N   1 
ATOM   1676 C  CA  . TYR A 1 224 ? -23.43900 -22.99700 -4.38900  1.000 15.40335 ? 224 TYR A CA  1 
ATOM   1677 C  C   . TYR A 1 224 ? -24.56400 -22.00400 -4.11000  1.000 15.12751 ? 224 TYR A C   1 
ATOM   1678 O  O   . TYR A 1 224 ? -25.68100 -22.41800 -3.75500  1.000 15.12040 ? 224 TYR A O   1 
ATOM   1679 C  CB  . TYR A 1 224 ? -22.57100 -23.18300 -3.14400  1.000 16.11202 ? 224 TYR A CB  1 
ATOM   1680 C  CG  . TYR A 1 224 ? -21.80500 -24.48900 -3.12400  1.000 18.04541 ? 224 TYR A CG  1 
ATOM   1681 C  CD1 . TYR A 1 224 ? -22.45500 -25.70600 -3.25900  1.000 20.99367 ? 224 TYR A CD1 1 
ATOM   1682 C  CD2 . TYR A 1 224 ? -20.42200 -24.49200 -2.96500  1.000 19.35864 ? 224 TYR A CD2 1 
ATOM   1683 C  CE1 . TYR A 1 224 ? -21.74100 -26.90000 -3.23000  1.000 24.95769 ? 224 TYR A CE1 1 
ATOM   1684 C  CE2 . TYR A 1 224 ? -19.71500 -25.66500 -2.93700  1.000 22.50161 ? 224 TYR A CE2 1 
ATOM   1685 C  CZ  . TYR A 1 224 ? -20.37200 -26.86400 -3.07100  1.000 25.07269 ? 224 TYR A CZ  1 
ATOM   1686 O  OH  . TYR A 1 224 ? -19.63400 -28.02900 -3.03900  1.000 30.54816 ? 224 TYR A OH  1 
ATOM   1687 N  N   . ILE A 1 225 ? -24.31100 -20.69700 -4.25300  1.000 15.33756 ? 225 ILE A N   1 
ATOM   1688 C  CA  . ILE A 1 225 ? -25.40700 -19.76000 -4.03100  1.000 15.37449 ? 225 ILE A CA  1 
ATOM   1689 C  C   . ILE A 1 225 ? -26.41700 -19.88300 -5.16800  1.000 14.23671 ? 225 ILE A C   1 
ATOM   1690 O  O   . ILE A 1 225 ? -27.62900 -19.74100 -4.95300  1.000 15.28462 ? 225 ILE A O   1 
ATOM   1691 C  CB  . ILE A 1 225 ? -24.89500 -18.31400 -3.82600  1.000 14.97200 ? 225 ILE A CB  1 
ATOM   1692 C  CG1 . ILE A 1 225 ? -26.04000 -17.37900 -3.38900  1.000 17.72811 ? 225 ILE A CG1 1 
ATOM   1693 C  CG2 . ILE A 1 225 ? -24.17700 -17.77400 -5.07000  1.000 15.28450 ? 225 ILE A CG2 1 
ATOM   1694 C  CD1 . ILE A 1 225 ? -26.70000 -17.79200 -2.11200  1.000 19.20498 ? 225 ILE A CD1 1 
ATOM   1695 N  N   . CYS A 1 226 ? -25.95800 -20.21700 -6.37400  1.000 14.10821 ? 226 CYS A N   1 
ATOM   1696 C  CA  . CYS A 1 226 ? -26.92000 -20.41900 -7.45800  1.000 13.15740 ? 226 CYS A CA  1 
ATOM   1697 C  C   . CYS A 1 226 ? -27.77400 -21.66300 -7.24900  1.000 15.24734 ? 226 CYS A C   1 
ATOM   1698 O  O   . CYS A 1 226 ? -28.95300 -21.66400 -7.62900  1.000 15.58314 ? 226 CYS A O   1 
ATOM   1699 C  CB  . CYS A 1 226 ? -26.19000 -20.50100 -8.80200  1.000 14.40956 ? 226 CYS A CB  1 
ATOM   1700 S  SG  . CYS A 1 226 ? -25.54200 -18.91200 -9.35600  1.000 15.54609 ? 226 CYS A SG  1 
ATOM   1701 N  N   . VAL A 1 227 ? -27.22300 -22.73000 -6.65000  1.000 14.44853 ? 227 VAL A N   1 
ATOM   1702 C  CA  . VAL A 1 227 ? -28.05700 -23.89400 -6.35700  1.000 15.29209 ? 227 VAL A CA  1 
ATOM   1703 C  C   . VAL A 1 227 ? -29.17400 -23.51300 -5.39100  1.000 15.85106 ? 227 VAL A C   1 
ATOM   1704 O  O   . VAL A 1 227 ? -30.34300 -23.86600 -5.59100  1.000 15.82877 ? 227 VAL A O   1 
ATOM   1705 C  CB  . VAL A 1 227 ? -27.20700 -25.04900 -5.79600  1.000 15.94498 ? 227 VAL A CB  1 
ATOM   1706 C  CG1 . VAL A 1 227 ? -28.11900 -26.18700 -5.25900  1.000 16.74460 ? 227 VAL A CG1 1 
ATOM   1707 C  CG2 . VAL A 1 227 ? -26.22200 -25.55100 -6.85700  1.000 16.27764 ? 227 VAL A CG2 1 
ATOM   1708 N  N   . TYR A 1 228 ? -28.82900 -22.77900 -4.33100  1.000 14.09074 ? 228 TYR A N   1 
ATOM   1709 C  CA  . TYR A 1 228 ? -29.83700 -22.33200 -3.37600  1.000 15.11598 ? 228 TYR A CA  1 
ATOM   1710 C  C   . TYR A 1 228 ? -30.93800 -21.52400 -4.08100  1.000 13.89376 ? 228 TYR A C   1 
ATOM   1711 O  O   . TYR A 1 228 ? -32.13700 -21.76200 -3.87400  1.000 15.03581 ? 228 TYR A O   1 
ATOM   1712 C  CB  . TYR A 1 228 ? -29.15100 -21.51500 -2.27000  1.000 14.32433 ? 228 TYR A CB  1 
ATOM   1713 C  CG  . TYR A 1 228 ? -30.13600 -20.69300 -1.47200  1.000 14.80349 ? 228 TYR A CG  1 
ATOM   1714 C  CD1 . TYR A 1 228 ? -30.95500 -21.29700 -0.51600  1.000 14.23650 ? 228 TYR A CD1 1 
ATOM   1715 C  CD2 . TYR A 1 228 ? -30.25300 -19.32300 -1.69300  1.000 13.17631 ? 228 TYR A CD2 1 
ATOM   1716 C  CE1 . TYR A 1 228 ? -31.89100 -20.53800 0.21100   1.000 15.21217 ? 228 TYR A CE1 1 
ATOM   1717 C  CE2 . TYR A 1 228 ? -31.16000 -18.56100 -0.97000  1.000 15.75212 ? 228 TYR A CE2 1 
ATOM   1718 C  CZ  . TYR A 1 228 ? -31.95300 -19.17200 -0.02200  1.000 14.79799 ? 228 TYR A CZ  1 
ATOM   1719 O  OH  . TYR A 1 228 ? -32.86500 -18.38800 0.67000   1.000 16.69624 ? 228 TYR A OH  1 
ATOM   1720 N  N   . LEU A 1 229 ? -30.55100 -20.58100 -4.94200  1.000 13.95748 ? 229 LEU A N   1 
ATOM   1721 C  CA  . LEU A 1 229 ? -31.54500 -19.72100 -5.59300  1.000 14.90786 ? 229 LEU A CA  1 
ATOM   1722 C  C   . LEU A 1 229 ? -32.37900 -20.45800 -6.63800  1.000 15.18310 ? 229 LEU A C   1 
ATOM   1723 O  O   . LEU A 1 229 ? -33.52600 -20.06000 -6.89100  1.000 16.23123 ? 229 LEU A O   1 
ATOM   1724 C  CB  . LEU A 1 229 ? -30.88000 -18.51600 -6.25400  1.000 13.48639 ? 229 LEU A CB  1 
ATOM   1725 C  CG  . LEU A 1 229 ? -30.31000 -17.47600 -5.27700  1.000 15.53281 ? 229 LEU A CG  1 
ATOM   1726 C  CD1 . LEU A 1 229 ? -29.49300 -16.42900 -6.03900  1.000 14.91547 ? 229 LEU A CD1 1 
ATOM   1727 C  CD2 . LEU A 1 229 ? -31.41800 -16.83200 -4.46500  1.000 16.00031 ? 229 LEU A CD2 1 
ATOM   1728 N  N   . ALA A 1 230 ? -31.82700 -21.49900 -7.28100  1.000 14.64114 ? 230 ALA A N   1 
ATOM   1729 C  CA  . ALA A 1 230 ? -32.60000 -22.29000 -8.24600  1.000 15.62736 ? 230 ALA A CA  1 
ATOM   1730 C  C   . ALA A 1 230 ? -33.55400 -23.24800 -7.56200  1.000 16.55102 ? 230 ALA A C   1 
ATOM   1731 O  O   . ALA A 1 230 ? -34.58200 -23.63400 -8.15000  1.000 16.35012 ? 230 ALA A O   1 
ATOM   1732 C  CB  . ALA A 1 230 ? -31.66700 -23.08000 -9.18100  1.000 14.98634 ? 230 ALA A CB  1 
ATOM   1733 N  N   A SER A 1 231 ? -33.26000 -23.60000 -6.31500  0.522 16.80242 ? 231 SER A N   1 
ATOM   1734 N  N   B SER A 1 231 ? -33.24700 -23.63900 -6.33100  0.478 16.76028 ? 231 SER A N   1 
ATOM   1735 C  CA  A SER A 1 231 ? -33.98900 -24.62100 -5.59300  0.522 15.92220 ? 231 SER A CA  1 
ATOM   1736 C  CA  B SER A 1 231 ? -34.02700 -24.65300 -5.65600  0.478 15.97307 ? 231 SER A CA  1 
ATOM   1737 C  C   A SER A 1 231 ? -35.23800 -24.03700 -4.94100  0.522 16.53164 ? 231 SER A C   1 
ATOM   1738 C  C   B SER A 1 231 ? -35.25900 -24.03900 -5.00300  0.478 16.49897 ? 231 SER A C   1 
ATOM   1739 O  O   A SER A 1 231 ? -35.31400 -22.83800 -4.65600  0.522 16.15696 ? 231 SER A O   1 
ATOM   1740 O  O   B SER A 1 231 ? -35.33900 -22.83100 -4.76100  0.478 16.17318 ? 231 SER A O   1 
ATOM   1741 C  CB  A SER A 1 231 ? -33.07200 -25.25300 -4.54000  0.522 15.54440 ? 231 SER A CB  1 
ATOM   1742 C  CB  B SER A 1 231 ? -33.18300 -25.36100 -4.59800  0.478 15.81076 ? 231 SER A CB  1 
ATOM   1743 O  OG  A SER A 1 231 ? -33.80200 -26.06300 -3.65000  0.522 15.80464 ? 231 SER A OG  1 
ATOM   1744 O  OG  B SER A 1 231 ? -33.10700 -24.55200 -3.44900  0.478 14.83836 ? 231 SER A OG  1 
ATOM   1745 N  N   . ASN A 1 232 ? -36.22900 -24.90400 -4.71700  1.000 16.83687 ? 232 ASN A N   1 
ATOM   1746 C  CA  . ASN A 1 232 ? -37.41100 -24.49200 -3.96500  1.000 17.41557 ? 232 ASN A CA  1 
ATOM   1747 C  C   . ASN A 1 232 ? -37.07700 -24.11900 -2.52100  1.000 17.79891 ? 232 ASN A C   1 
ATOM   1748 O  O   . ASN A 1 232 ? -37.93300 -23.54300 -1.83400  1.000 15.51027 ? 232 ASN A O   1 
ATOM   1749 C  CB  . ASN A 1 232 ? -38.46100 -25.59800 -4.02900  1.000 16.71227 ? 232 ASN A CB  1 
ATOM   1750 C  CG  . ASN A 1 232 ? -38.89500 -25.87500 -5.45300  1.000 18.30889 ? 232 ASN A CG  1 
ATOM   1751 O  OD1 . ASN A 1 232 ? -38.87000 -24.97400 -6.30400  1.000 18.92214 ? 232 ASN A OD1 1 
ATOM   1752 N  ND2 . ASN A 1 232 ? -39.27200 -27.11500 -5.72700  1.000 18.01346 ? 232 ASN A ND2 1 
ATOM   1753 N  N   . GLU A 1 233 ? -35.84300 -24.38800 -2.05800  1.000 16.29024 ? 233 GLU A N   1 
ATOM   1754 C  CA  . GLU A 1 233 ? -35.41700 -23.87800 -0.75500  1.000 15.66594 ? 233 GLU A CA  1 
ATOM   1755 C  C   . GLU A 1 233 ? -35.57300 -22.37700 -0.65400  1.000 16.60715 ? 233 GLU A C   1 
ATOM   1756 O  O   . GLU A 1 233 ? -35.76800 -21.85700 0.45400   1.000 18.90782 ? 233 GLU A O   1 
ATOM   1757 C  CB  . GLU A 1 233 ? -33.94300 -24.21100 -0.47100  1.000 15.43424 ? 233 GLU A CB  1 
ATOM   1758 C  CG  . GLU A 1 233 ? -33.66600 -25.68100 -0.35700  1.000 16.17423 ? 233 GLU A CG  1 
ATOM   1759 C  CD  . GLU A 1 233 ? -32.16900 -25.99100 -0.35400  1.000 20.17071 ? 233 GLU A CD  1 
ATOM   1760 O  OE1 . GLU A 1 233 ? -31.34500 -25.04900 -0.24500  1.000 21.20138 ? 233 GLU A OE1 1 
ATOM   1761 O  OE2 . GLU A 1 233 ? -31.84300 -27.19200 -0.46600  1.000 22.95010 ? 233 GLU A OE2 1 
ATOM   1762 N  N   . SER A 1 234 ? -35.45600 -21.65600 -1.77700  1.000 14.30402 ? 234 SER A N   1 
ATOM   1763 C  CA  . SER A 1 234 ? -35.47700 -20.19400 -1.79300  1.000 13.88195 ? 234 SER A CA  1 
ATOM   1764 C  C   . SER A 1 234 ? -36.78900 -19.62500 -2.33100  1.000 14.11718 ? 234 SER A C   1 
ATOM   1765 O  O   . SER A 1 234 ? -36.81400 -18.49700 -2.82300  1.000 14.64771 ? 234 SER A O   1 
ATOM   1766 C  CB  . SER A 1 234 ? -34.30000 -19.64100 -2.59900  1.000 15.15558 ? 234 SER A CB  1 
ATOM   1767 O  OG  . SER A 1 234 ? -34.40300 -20.04600 -3.96000  1.000 15.97470 ? 234 SER A OG  1 
ATOM   1768 N  N   . LYS A 1 235 ? -37.88200 -20.36900 -2.16500  1.000 14.71832 ? 235 LYS A N   1 
ATOM   1769 C  CA  . LYS A 1 235 ? -39.20200 -20.03000 -2.70900  1.000 14.55670 ? 235 LYS A CA  1 
ATOM   1770 C  C   . LYS A 1 235 ? -39.78800 -18.73100 -2.17200  1.000 16.56925 ? 235 LYS A C   1 
ATOM   1771 O  O   . LYS A 1 235 ? -40.78000 -18.25300 -2.74100  1.000 16.62992 ? 235 LYS A O   1 
ATOM   1772 C  CB  . LYS A 1 235 ? -40.19100 -21.17700 -2.44800  1.000 14.92538 ? 235 LYS A CB  1 
ATOM   1773 C  CG  . LYS A 1 235 ? -40.48700 -21.45300 -0.95500  1.000 17.58125 ? 235 LYS A CG  1 
ATOM   1774 C  CD  . LYS A 1 235 ? -41.33400 -22.71700 -0.84100  1.000 20.54083 ? 235 LYS A CD  1 
ATOM   1775 C  CE  . LYS A 1 235 ? -42.13500 -22.77500 0.44500   1.000 27.11447 ? 235 LYS A CE  1 
ATOM   1776 N  NZ  . LYS A 1 235 ? -41.33100 -22.60000 1.64100   1.000 27.49651 ? 235 LYS A NZ  1 
ATOM   1777 N  N   . PHE A 1 236 ? -39.25400 -18.16600 -1.08900  1.000 14.81484 ? 236 PHE A N   1 
ATOM   1778 C  CA  . PHE A 1 236 ? -39.68500 -16.86200 -0.59900  1.000 14.40588 ? 236 PHE A CA  1 
ATOM   1779 C  C   . PHE A 1 236 ? -38.68900 -15.75400 -0.90400  1.000 15.18098 ? 236 PHE A C   1 
ATOM   1780 O  O   . PHE A 1 236 ? -38.88300 -14.61700 -0.45700  1.000 16.41795 ? 236 PHE A O   1 
ATOM   1781 C  CB  . PHE A 1 236 ? -39.93800 -16.94300 0.92400   1.000 14.24113 ? 236 PHE A CB  1 
ATOM   1782 C  CG  . PHE A 1 236 ? -40.78800 -15.81100 1.49900   1.000 14.29823 ? 236 PHE A CG  1 
ATOM   1783 C  CD1 . PHE A 1 236 ? -42.05900 -15.51700 0.98200   1.000 14.55528 ? 236 PHE A CD1 1 
ATOM   1784 C  CD2 . PHE A 1 236 ? -40.32300 -15.07500 2.59200   1.000 15.12695 ? 236 PHE A CD2 1 
ATOM   1785 C  CE1 . PHE A 1 236 ? -42.82100 -14.48000 1.53000   1.000 16.23813 ? 236 PHE A CE1 1 
ATOM   1786 C  CE2 . PHE A 1 236 ? -41.07800 -14.04400 3.15300   1.000 14.51379 ? 236 PHE A CE2 1 
ATOM   1787 C  CZ  . PHE A 1 236 ? -42.35800 -13.75700 2.63500   1.000 15.61143 ? 236 PHE A CZ  1 
ATOM   1788 N  N   . ALA A 1 237 ? -37.61900 -16.04400 -1.63700  1.000 13.43016 ? 237 ALA A N   1 
ATOM   1789 C  CA  . ALA A 1 237 ? -36.61200 -15.03900 -1.95800  1.000 13.47179 ? 237 ALA A CA  1 
ATOM   1790 C  C   . ALA A 1 237 ? -36.86000 -14.52400 -3.36700  1.000 14.31309 ? 237 ALA A C   1 
ATOM   1791 O  O   . ALA A 1 237 ? -36.79300 -15.29600 -4.32800  1.000 14.21753 ? 237 ALA A O   1 
ATOM   1792 C  CB  . ALA A 1 237 ? -35.20100 -15.60800 -1.87500  1.000 13.96897 ? 237 ALA A CB  1 
ATOM   1793 N  N   . THR A 1 238 ? -37.16300 -13.23200 -3.48500  1.000 12.54164 ? 238 THR A N   1 
ATOM   1794 C  CA  . THR A 1 238 ? -37.28400 -12.63300 -4.80500  1.000 12.40511 ? 238 THR A CA  1 
ATOM   1795 C  C   . THR A 1 238 ? -36.96600 -11.15100 -4.70100  1.000 14.82492 ? 238 THR A C   1 
ATOM   1796 O  O   . THR A 1 238 ? -37.25400 -10.49900 -3.69300  1.000 14.53308 ? 238 THR A O   1 
ATOM   1797 C  CB  . THR A 1 238 ? -38.67000 -12.87000 -5.42600  1.000 13.37654 ? 238 THR A CB  1 
ATOM   1798 O  OG1 . THR A 1 238 ? -38.59300 -12.69300 -6.85000  1.000 14.61965 ? 238 THR A OG1 1 
ATOM   1799 C  CG2 . THR A 1 238 ? -39.73100 -11.90300 -4.87300  1.000 14.08966 ? 238 THR A CG2 1 
ATOM   1800 N  N   . GLY A 1 239 ? -36.35800 -10.62500 -5.75800  1.000 13.49757 ? 239 GLY A N   1 
ATOM   1801 C  CA  . GLY A 1 239 ? -36.01200 -9.22100  -5.75500  1.000 13.93135 ? 239 GLY A CA  1 
ATOM   1802 C  C   . GLY A 1 239 ? -34.79200 -8.86800  -4.94600  1.000 16.25978 ? 239 GLY A C   1 
ATOM   1803 O  O   . GLY A 1 239 ? -34.55700 -7.67700  -4.72000  1.000 15.71740 ? 239 GLY A O   1 
ATOM   1804 N  N   . SER A 1 240 ? -34.01600 -9.85900  -4.51300  1.000 15.82148 ? 240 SER A N   1 
ATOM   1805 C  CA  . SER A 1 240 ? -32.89400 -9.67100  -3.59400  1.000 15.42512 ? 240 SER A CA  1 
ATOM   1806 C  C   . SER A 1 240 ? -31.55000 -9.86500  -4.26800  1.000 14.12568 ? 240 SER A C   1 
ATOM   1807 O  O   . SER A 1 240 ? -31.43200 -10.52700 -5.29900  1.000 14.82670 ? 240 SER A O   1 
ATOM   1808 C  CB  . SER A 1 240 ? -32.99300 -10.64100 -2.41700  1.000 19.07251 ? 240 SER A CB  1 
ATOM   1809 O  OG  . SER A 1 240 ? -34.08700 -10.28900 -1.61200  1.000 24.73765 ? 240 SER A OG  1 
ATOM   1810 N  N   . GLU A 1 241 ? -30.53800 -9.27300  -3.64300  1.000 14.25059 ? 241 GLU A N   1 
ATOM   1811 C  CA  . GLU A 1 241 ? -29.14300 -9.33400  -4.07800  1.000 12.77799 ? 241 GLU A CA  1 
ATOM   1812 C  C   . GLU A 1 241 ? -28.33100 -10.22700 -3.15800  1.000 11.42537 ? 241 GLU A C   1 
ATOM   1813 O  O   . GLU A 1 241 ? -28.32200 -10.00500 -1.94800  1.000 13.83448 ? 241 GLU A O   1 
ATOM   1814 C  CB  . GLU A 1 241 ? -28.49900 -7.94900  -4.05100  1.000 17.39375 ? 241 GLU A CB  1 
ATOM   1815 C  CG  . GLU A 1 241 ? -29.05200 -6.93500  -4.96300  1.000 20.76850 ? 241 GLU A CG  1 
ATOM   1816 C  CD  . GLU A 1 241 ? -29.82400 -5.88900  -4.21700  1.000 22.25108 ? 241 GLU A CD  1 
ATOM   1817 O  OE1 . GLU A 1 241 ? -30.50900 -6.27300  -3.24300  1.000 25.13104 ? 241 GLU A OE1 1 
ATOM   1818 O  OE2 . GLU A 1 241 ? -29.81000 -4.71300  -4.62600  1.000 18.60270 ? 241 GLU A OE2 1 
ATOM   1819 N  N   . PHE A 1 242 ? -27.59900 -11.18800 -3.72000  1.000 12.97198 ? 242 PHE A N   1 
ATOM   1820 C  CA  . PHE A 1 242 ? -26.84600 -12.15600 -2.92000  1.000 12.79450 ? 242 PHE A CA  1 
ATOM   1821 C  C   . PHE A 1 242 ? -25.36300 -11.97800 -3.23300  1.000 13.17563 ? 242 PHE A C   1 
ATOM   1822 O  O   . PHE A 1 242 ? -24.92300 -12.20300 -4.37300  1.000 15.02839 ? 242 PHE A O   1 
ATOM   1823 C  CB  . PHE A 1 242 ? -27.33700 -13.58200 -3.17700  1.000 13.98941 ? 242 PHE A CB  1 
ATOM   1824 C  CG  . PHE A 1 242 ? -28.75500 -13.81400 -2.70600  1.000 15.91793 ? 242 PHE A CG  1 
ATOM   1825 C  CD1 . PHE A 1 242 ? -29.83600 -13.44100 -3.48000  1.000 15.08771 ? 242 PHE A CD1 1 
ATOM   1826 C  CD2 . PHE A 1 242 ? -28.98900 -14.36300 -1.46200  1.000 18.24345 ? 242 PHE A CD2 1 
ATOM   1827 C  CE1 . PHE A 1 242 ? -31.13300 -13.61500 -2.99300  1.000 16.04984 ? 242 PHE A CE1 1 
ATOM   1828 C  CE2 . PHE A 1 242 ? -30.30100 -14.53500 -0.99000  1.000 18.21510 ? 242 PHE A CE2 1 
ATOM   1829 C  CZ  . PHE A 1 242 ? -31.34500 -14.15500 -1.75000  1.000 15.67679 ? 242 PHE A CZ  1 
ATOM   1830 N  N   . VAL A 1 243 ? -24.60700 -11.51300 -2.23200  1.000 12.82889 ? 243 VAL A N   1 
ATOM   1831 C  CA  . VAL A 1 243 ? -23.20400 -11.09900 -2.40700  1.000 13.24595 ? 243 VAL A CA  1 
ATOM   1832 C  C   . VAL A 1 243 ? -22.28300 -12.16600 -1.83800  1.000 13.82848 ? 243 VAL A C   1 
ATOM   1833 O  O   . VAL A 1 243 ? -22.42800 -12.56500 -0.68100  1.000 14.18047 ? 243 VAL A O   1 
ATOM   1834 C  CB  . VAL A 1 243 ? -22.94900 -9.75500  -1.70800  1.000 15.05045 ? 243 VAL A CB  1 
ATOM   1835 C  CG1 . VAL A 1 243 ? -21.46700 -9.34100  -1.84500  1.000 16.09330 ? 243 VAL A CG1 1 
ATOM   1836 C  CG2 . VAL A 1 243 ? -23.90400 -8.67600  -2.25000  1.000 16.23110 ? 243 VAL A CG2 1 
ATOM   1837 N  N   . VAL A 1 244 ? -21.29300 -12.58200 -2.63100  1.000 13.59006 ? 244 VAL A N   1 
ATOM   1838 C  CA  . VAL A 1 244 ? -20.30600 -13.57300 -2.21500  1.000 13.69456 ? 244 VAL A CA  1 
ATOM   1839 C  C   . VAL A 1 244 ? -18.94800 -13.02100 -2.64500  1.000 13.67658 ? 244 VAL A C   1 
ATOM   1840 O  O   . VAL A 1 244 ? -18.52800 -13.21500 -3.79300  1.000 14.69835 ? 244 VAL A O   1 
ATOM   1841 C  CB  . VAL A 1 244 ? -20.59500 -14.95500 -2.83800  1.000 13.47869 ? 244 VAL A CB  1 
ATOM   1842 C  CG1 . VAL A 1 244 ? -19.59700 -15.99400 -2.36900  1.000 13.99441 ? 244 VAL A CG1 1 
ATOM   1843 C  CG2 . VAL A 1 244 ? -22.05000 -15.41600 -2.51600  1.000 15.40922 ? 244 VAL A CG2 1 
ATOM   1844 N  N   . ASP A 1 245 ? -18.29100 -12.25700 -1.75600  1.000 12.84505 ? 245 ASP A N   1 
ATOM   1845 C  CA  . ASP A 1 245 ? -17.20200 -11.40200 -2.22500  1.000 13.70390 ? 245 ASP A CA  1 
ATOM   1846 C  C   . ASP A 1 245 ? -16.01100 -11.30600 -1.28300  1.000 13.43327 ? 245 ASP A C   1 
ATOM   1847 O  O   . ASP A 1 245 ? -15.18000 -10.41200 -1.46100  1.000 14.42107 ? 245 ASP A O   1 
ATOM   1848 C  CB  . ASP A 1 245 ? -17.72800 -9.97000  -2.51900  1.000 14.38939 ? 245 ASP A CB  1 
ATOM   1849 C  CG  . ASP A 1 245 ? -18.08300 -9.17000  -1.25500  1.000 15.38517 ? 245 ASP A CG  1 
ATOM   1850 O  OD1 . ASP A 1 245 ? -18.08900 -9.71000  -0.12600  1.000 13.53297 ? 245 ASP A OD1 1 
ATOM   1851 O  OD2 . ASP A 1 245 ? -18.39100 -7.96000  -1.40200  1.000 14.83233 ? 245 ASP A OD2 1 
ATOM   1852 N  N   . GLY A 1 246 ? -15.89500 -12.19200 -0.29900  1.000 12.97890 ? 246 GLY A N   1 
ATOM   1853 C  CA  . GLY A 1 246 ? -14.73200 -12.15800 0.57300   1.000 13.30714 ? 246 GLY A CA  1 
ATOM   1854 C  C   . GLY A 1 246 ? -14.61800 -10.92000 1.44000   1.000 14.44411 ? 246 GLY A C   1 
ATOM   1855 O  O   . GLY A 1 246 ? -13.54900 -10.66700 2.01400   1.000 14.25080 ? 246 GLY A O   1 
ATOM   1856 N  N   . GLY A 1 247 ? -15.71100 -10.15500 1.57100   1.000 14.42650 ? 247 GLY A N   1 
ATOM   1857 C  CA  . GLY A 1 247 ? -15.74700 -8.92700  2.33800   1.000 14.72744 ? 247 GLY A CA  1 
ATOM   1858 C  C   . GLY A 1 247 ? -15.55600 -7.65400  1.53700   1.000 13.92532 ? 247 GLY A C   1 
ATOM   1859 O  O   . GLY A 1 247 ? -15.50900 -6.57800  2.13600   1.000 13.68029 ? 247 GLY A O   1 
ATOM   1860 N  N   . TYR A 1 248 ? -15.39600 -7.74500  0.21100   1.000 13.58015 ? 248 TYR A N   1 
ATOM   1861 C  CA  . TYR A 1 248 ? -15.05800 -6.56700  -0.59300  1.000 12.69815 ? 248 TYR A CA  1 
ATOM   1862 C  C   . TYR A 1 248 ? -15.97900 -5.37400  -0.31700  1.000 13.73708 ? 248 TYR A C   1 
ATOM   1863 O  O   . TYR A 1 248 ? -15.51300 -4.24000  -0.11000  1.000 14.70852 ? 248 TYR A O   1 
ATOM   1864 C  CB  . TYR A 1 248 ? -15.11400 -6.93800  -2.08400  1.000 13.29928 ? 248 TYR A CB  1 
ATOM   1865 C  CG  . TYR A 1 248 ? -14.58200 -5.86600  -3.03400  1.000 13.18765 ? 248 TYR A CG  1 
ATOM   1866 C  CD1 . TYR A 1 248 ? -15.27600 -4.69400  -3.26700  1.000 12.60060 ? 248 TYR A CD1 1 
ATOM   1867 C  CD2 . TYR A 1 248 ? -13.37200 -6.03800  -3.70900  1.000 12.87839 ? 248 TYR A CD2 1 
ATOM   1868 C  CE1 . TYR A 1 248 ? -14.78600 -3.70200  -4.15500  1.000 13.03470 ? 248 TYR A CE1 1 
ATOM   1869 C  CE2 . TYR A 1 248 ? -12.87300 -5.05200  -4.58300  1.000 12.98387 ? 248 TYR A CE2 1 
ATOM   1870 C  CZ  . TYR A 1 248 ? -13.57600 -3.89200  -4.78400  1.000 13.66575 ? 248 TYR A CZ  1 
ATOM   1871 O  OH  . TYR A 1 248 ? -13.11000 -2.92700  -5.64000  1.000 16.78010 ? 248 TYR A OH  1 
ATOM   1872 N  N   . THR A 1 249 ? -17.29000 -5.60200  -0.33600  1.000 14.19422 ? 249 THR A N   1 
ATOM   1873 C  CA  . THR A 1 249 ? -18.24000 -4.49500  -0.21800  1.000 14.32060 ? 249 THR A CA  1 
ATOM   1874 C  C   . THR A 1 249 ? -18.58400 -4.15500  1.22700   1.000 14.21416 ? 249 THR A C   1 
ATOM   1875 O  O   . THR A 1 249 ? -19.27000 -3.15400  1.46100   1.000 18.10320 ? 249 THR A O   1 
ATOM   1876 C  CB  . THR A 1 249 ? -19.53700 -4.77700  -0.99600  1.000 15.21859 ? 249 THR A CB  1 
ATOM   1877 O  OG1 . THR A 1 249 ? -20.12800 -6.01500  -0.58600  1.000 15.09875 ? 249 THR A OG1 1 
ATOM   1878 C  CG2 . THR A 1 249 ? -19.28600 -4.81500  -2.51500  1.000 14.27906 ? 249 THR A CG2 1 
ATOM   1879 N  N   . ALA A 1 250 ? -18.10700 -4.93400  2.19600   1.000 12.47517 ? 250 ALA A N   1 
ATOM   1880 C  CA  . ALA A 1 250 ? -18.38500 -4.65200  3.59800   1.000 13.67794 ? 250 ALA A CA  1 
ATOM   1881 C  C   . ALA A 1 250 ? -17.51500 -3.53600  4.16000   1.000 15.65424 ? 250 ALA A C   1 
ATOM   1882 O  O   . ALA A 1 250 ? -17.81300 -3.01900  5.23700   1.000 14.10813 ? 250 ALA A O   1 
ATOM   1883 C  CB  . ALA A 1 250 ? -18.18300 -5.91500  4.44600   1.000 14.27964 ? 250 ALA A CB  1 
ATOM   1884 N  N   . GLN A 1 251 ? -16.41500 -3.19400  3.49700   1.000 14.59646 ? 251 GLN A N   1 
ATOM   1885 C  CA  . GLN A 1 251 ? -15.59000 -2.05900  3.91000   1.000 13.28081 ? 251 GLN A CA  1 
ATOM   1886 C  C   . GLN A 1 251 ? -15.72800 -0.88600  2.94000   1.000 14.36117 ? 251 GLN A C   1 
ATOM   1887 O  O   . GLN A 1 251 ? -16.18900 -1.07300  1.79600   1.000 16.01299 ? 251 GLN A O   1 
ATOM   1888 C  CB  . GLN A 1 251 ? -14.11700 -2.49000  4.02200   1.000 13.57480 ? 251 GLN A CB  1 
ATOM   1889 C  CG  . GLN A 1 251 ? -13.50300 -3.04300  2.71500   1.000 14.97626 ? 251 GLN A CG  1 
ATOM   1890 C  CD  . GLN A 1 251 ? -12.05900 -3.51400  2.90100   1.000 16.41899 ? 251 GLN A CD  1 
ATOM   1891 O  OE1 . GLN A 1 251 ? -11.56900 -3.62200  4.01900   1.000 18.95090 ? 251 GLN A OE1 1 
ATOM   1892 N  NE2 . GLN A 1 251 ? -11.38000 -3.80600  1.79300   1.000 17.21360 ? 251 GLN A NE2 1 
ATOM   1893 O  OXT . GLN A 1 251 ? -15.33900 0.24100   3.27300   1.000 14.55521 ? 251 GLN A OXT 1 
HETATM 1894 P  PA  . NAP B 2 .   ? -14.47500 -16.38500 -20.85200 0.803 40.62445 ? 301 NAP A PA  1 
HETATM 1895 O  O1A . NAP B 2 .   ? -13.76600 -16.54800 -19.55600 0.803 42.61395 ? 301 NAP A O1A 1 
HETATM 1896 O  O2A . NAP B 2 .   ? -14.29500 -17.44700 -21.88000 0.803 41.05871 ? 301 NAP A O2A 1 
HETATM 1897 O  O5B . NAP B 2 .   ? -16.04000 -16.17400 -20.56300 0.803 31.79491 ? 301 NAP A O5B 1 
HETATM 1898 C  C5B . NAP B 2 .   ? -16.71100 -17.03800 -19.60700 0.803 25.14379 ? 301 NAP A C5B 1 
HETATM 1899 C  C4B . NAP B 2 .   ? -17.84300 -17.80600 -20.25700 0.803 21.37299 ? 301 NAP A C4B 1 
HETATM 1900 O  O4B . NAP B 2 .   ? -18.77500 -16.90700 -20.91100 0.803 20.80957 ? 301 NAP A O4B 1 
HETATM 1901 C  C3B . NAP B 2 .   ? -17.45400 -18.82000 -21.33900 0.803 21.58521 ? 301 NAP A C3B 1 
HETATM 1902 O  O3B . NAP B 2 .   ? -18.33500 -19.92800 -21.25100 0.803 21.92985 ? 301 NAP A O3B 1 
HETATM 1903 C  C2B . NAP B 2 .   ? -17.65100 -18.01600 -22.61500 0.803 20.92769 ? 301 NAP A C2B 1 
HETATM 1904 O  O2B . NAP B 2 .   ? -17.78900 -18.92000 -23.69700 0.803 20.16615 ? 301 NAP A O2B 1 
HETATM 1905 C  C1B . NAP B 2 .   ? -18.94500 -17.30400 -22.25100 0.803 19.36826 ? 301 NAP A C1B 1 
HETATM 1906 N  N9A . NAP B 2 .   ? -19.27200 -16.13200 -23.05200 0.803 17.33202 ? 301 NAP A N9A 1 
HETATM 1907 C  C8A . NAP B 2 .   ? -18.49600 -15.03000 -23.30000 0.803 18.95076 ? 301 NAP A C8A 1 
HETATM 1908 N  N7A . NAP B 2 .   ? -19.08700 -14.13700 -24.05000 0.803 19.45982 ? 301 NAP A N7A 1 
HETATM 1909 C  C5A . NAP B 2 .   ? -20.33400 -14.68200 -24.31200 0.803 17.48834 ? 301 NAP A C5A 1 
HETATM 1910 C  C6A . NAP B 2 .   ? -21.43500 -14.22400 -25.05900 0.803 18.47216 ? 301 NAP A C6A 1 
HETATM 1911 N  N6A . NAP B 2 .   ? -21.46300 -13.06700 -25.70400 0.803 17.58030 ? 301 NAP A N6A 1 
HETATM 1912 N  N1A . NAP B 2 .   ? -22.52300 -15.02300 -25.11700 0.803 17.10130 ? 301 NAP A N1A 1 
HETATM 1913 C  C2A . NAP B 2 .   ? -22.49600 -16.19400 -24.47500 0.803 17.12780 ? 301 NAP A C2A 1 
HETATM 1914 N  N3A . NAP B 2 .   ? -21.52300 -16.72600 -23.74800 0.803 15.46500 ? 301 NAP A N3A 1 
HETATM 1915 C  C4A . NAP B 2 .   ? -20.45800 -15.91200 -23.70200 0.803 16.54027 ? 301 NAP A C4A 1 
HETATM 1916 O  O3  . NAP B 2 .   ? -14.08000 -14.99300 -21.52400 0.803 41.45174 ? 301 NAP A O3  1 
HETATM 1917 P  PN  . NAP B 2 .   ? -14.03900 -14.48500 -23.04100 0.803 44.73067 ? 301 NAP A PN  1 
HETATM 1918 O  O1N . NAP B 2 .   ? -15.19500 -13.57200 -23.26700 0.803 43.94811 ? 301 NAP A O1N 1 
HETATM 1919 O  O2N . NAP B 2 .   ? -13.87500 -15.62500 -23.98300 0.803 40.31946 ? 301 NAP A O2N 1 
HETATM 1920 O  O5D . NAP B 2 .   ? -12.67900 -13.65000 -23.00600 0.803 47.15590 ? 301 NAP A O5D 1 
HETATM 1921 C  C5D . NAP B 2 .   ? -12.60800 -12.36000 -23.65300 0.803 50.07767 ? 301 NAP A C5D 1 
HETATM 1922 C  C4D . NAP B 2 .   ? -11.98400 -11.38000 -22.69200 0.803 52.15057 ? 301 NAP A C4D 1 
HETATM 1923 O  O4D . NAP B 2 .   ? -10.65400 -11.80100 -22.35500 0.803 53.47648 ? 301 NAP A O4D 1 
HETATM 1924 C  C3D . NAP B 2 .   ? -11.76100 -9.95200  -23.20300 0.803 53.38210 ? 301 NAP A C3D 1 
HETATM 1925 O  O3D . NAP B 2 .   ? -12.98200 -9.22400  -23.12000 0.803 53.90468 ? 301 NAP A O3D 1 
HETATM 1926 C  C2D . NAP B 2 .   ? -10.62900 -9.43100  -22.29500 0.803 53.69306 ? 301 NAP A C2D 1 
HETATM 1927 O  O2D . NAP B 2 .   ? -11.06100 -8.59300  -21.23200 0.803 53.43123 ? 301 NAP A O2D 1 
HETATM 1928 C  C1D . NAP B 2 .   ? -10.04200 -10.71400 -21.68100 0.803 53.91304 ? 301 NAP A C1D 1 
HETATM 1929 N  N1N . NAP B 2 .   ? -8.58100  -10.86900 -21.82800 0.803 54.79413 ? 301 NAP A N1N 1 
HETATM 1930 C  C2N . NAP B 2 .   ? -7.89200  -10.07400 -22.71100 0.803 55.22291 ? 301 NAP A C2N 1 
HETATM 1931 C  C3N . NAP B 2 .   ? -6.51800  -10.22900 -22.84900 0.803 55.17664 ? 301 NAP A C3N 1 
HETATM 1932 C  C7N . NAP B 2 .   ? -5.80500  -9.34400  -23.82100 0.803 55.44720 ? 301 NAP A C7N 1 
HETATM 1933 O  O7N . NAP B 2 .   ? -6.35700  -9.04100  -24.88900 0.803 56.14978 ? 301 NAP A O7N 1 
HETATM 1934 N  N7N . NAP B 2 .   ? -4.60200  -8.89600  -23.49300 0.803 54.88453 ? 301 NAP A N7N 1 
HETATM 1935 C  C4N . NAP B 2 .   ? -5.84700  -11.18600 -22.10500 0.803 55.06100 ? 301 NAP A C4N 1 
HETATM 1936 C  C5N . NAP B 2 .   ? -6.55200  -11.98000 -21.22400 0.803 54.63642 ? 301 NAP A C5N 1 
HETATM 1937 C  C6N . NAP B 2 .   ? -7.91400  -11.81600 -21.08900 0.803 54.61245 ? 301 NAP A C6N 1 
HETATM 1938 P  P2B . NAP B 2 .   ? -17.28400 -18.31200 -25.09100 0.803 21.48394 ? 301 NAP A P2B 1 
HETATM 1939 O  O1X . NAP B 2 .   ? -16.07500 -17.44100 -24.91600 0.803 24.75392 ? 301 NAP A O1X 1 
HETATM 1940 O  O2X . NAP B 2 .   ? -16.98500 -19.55900 -25.85500 0.803 23.14179 ? 301 NAP A O2X 1 
HETATM 1941 O  O3X . NAP B 2 .   ? -18.44200 -17.57300 -25.62700 0.803 19.89079 ? 301 NAP A O3X 1 
HETATM 1942 O  O1  . PG4 C 3 .   ? -36.67800 -31.35600 -3.85400  1.000 36.37026 ? 302 PG4 A O1  1 
HETATM 1943 C  C1  . PG4 C 3 .   ? -36.01500 -30.18800 -3.37900  1.000 34.46878 ? 302 PG4 A C1  1 
HETATM 1944 C  C2  . PG4 C 3 .   ? -36.71000 -29.60500 -2.18500  1.000 34.58987 ? 302 PG4 A C2  1 
HETATM 1945 O  O2  . PG4 C 3 .   ? -36.14500 -28.34500 -1.83400  1.000 33.90392 ? 302 PG4 A O2  1 
HETATM 1946 C  C3  . PG4 C 3 .   ? -36.75400 -27.77400 -0.67900  1.000 33.96691 ? 302 PG4 A C3  1 
HETATM 1947 C  C4  . PG4 C 3 .   ? -38.09600 -27.24700 -1.04000  1.000 35.31083 ? 302 PG4 A C4  1 
HETATM 1948 O  O3  . PG4 C 3 .   ? -38.95500 -27.34000 0.08600   1.000 38.54757 ? 302 PG4 A O3  1 
HETATM 1949 C  C5  . PG4 C 3 .   ? -40.28500 -27.70000 -0.27300  1.000 40.52763 ? 302 PG4 A C5  1 
HETATM 1950 C  C6  . PG4 C 3 .   ? -41.03100 -26.50500 -0.75400  1.000 40.91676 ? 302 PG4 A C6  1 
HETATM 1951 O  O4  . PG4 C 3 .   ? -41.45700 -26.69900 -2.09800  1.000 42.57804 ? 302 PG4 A O4  1 
HETATM 1952 C  C7  . PG4 C 3 .   ? -42.66200 -25.99800 -2.39100  1.000 43.03626 ? 302 PG4 A C7  1 
HETATM 1953 C  C8  . PG4 C 3 .   ? -42.72900 -25.63900 -3.84400  1.000 43.05443 ? 302 PG4 A C8  1 
HETATM 1954 O  O5  . PG4 C 3 .   ? -41.97100 -24.48400 -4.13900  1.000 43.20652 ? 302 PG4 A O5  1 
HETATM 1955 MG MG  . MG  D 4 .   ? -16.18900 0.00000   0.00000   0.50  14.10163 ? 303 MG  A MG  1 
HETATM 1956 MG MG  . MG  E 4 .   ? -13.97200 -17.39100 -24.34500 1.000 35.44470 ? 304 MG  A MG  1 
HETATM 1957 C  C1  . EDO F 5 .   ? -41.53400 -31.47000 -12.62600 1.000 42.94931 ? 305 EDO A C1  1 
HETATM 1958 O  O1  . EDO F 5 .   ? -40.94400 -32.19600 -13.71100 1.000 44.27304 ? 305 EDO A O1  1 
HETATM 1959 C  C2  . EDO F 5 .   ? -42.11500 -30.16200 -13.14400 1.000 41.81988 ? 305 EDO A C2  1 
HETATM 1960 O  O2  . EDO F 5 .   ? -43.22200 -29.79100 -12.31200 1.000 41.79698 ? 305 EDO A O2  1 
HETATM 1961 O  O   . HOH G 6 .   ? -1.87900  -9.67000  -2.34000  1.000 30.50345 ? 401 HOH A O   1 
HETATM 1962 O  O   . HOH G 6 .   ? -18.61000 -38.59100 -28.95400 1.000 44.03688 ? 402 HOH A O   1 
HETATM 1963 O  O   . HOH G 6 .   ? -43.25300 -10.12200 -15.32100 1.000 24.99129 ? 403 HOH A O   1 
HETATM 1964 O  O   . HOH G 6 .   ? -11.49200 -4.56000  -10.45500 1.000 31.51961 ? 404 HOH A O   1 
HETATM 1965 O  O   . HOH G 6 .   ? -26.06200 1.43400   -27.32300 1.000 38.74502 ? 405 HOH A O   1 
HETATM 1966 O  O   . HOH G 6 .   ? -28.61200 -35.04500 -6.09600  1.000 39.50598 ? 406 HOH A O   1 
HETATM 1967 O  O   . HOH G 6 .   ? -11.14900 -3.10100  -7.78000  1.000 31.36470 ? 407 HOH A O   1 
HETATM 1968 O  O   . HOH G 6 .   ? -15.90200 -1.58400  -18.42700 1.000 15.21048 ? 408 HOH A O   1 
HETATM 1969 O  O   . HOH G 6 .   ? -9.15000  3.78600   -18.85700 1.000 24.61640 ? 409 HOH A O   1 
HETATM 1970 O  O   . HOH G 6 .   ? -4.17400  -16.16200 -10.93100 1.000 36.64769 ? 410 HOH A O   1 
HETATM 1971 O  O   . HOH G 6 .   ? 1.68800   -6.81200  -4.25100  1.000 33.57933 ? 411 HOH A O   1 
HETATM 1972 O  O   . HOH G 6 .   ? -24.46700 -8.91200  -17.12000 1.000 24.33502 ? 412 HOH A O   1 
HETATM 1973 O  O   . HOH G 6 .   ? -18.27300 -21.77400 -25.44800 1.000 20.56890 ? 413 HOH A O   1 
HETATM 1974 O  O   . HOH G 6 .   ? -18.96500 -14.50600 -19.91500 1.000 25.75965 ? 414 HOH A O   1 
HETATM 1975 O  O   . HOH G 6 .   ? -33.97200 -34.60800 -11.11300 1.000 30.53256 ? 415 HOH A O   1 
HETATM 1976 O  O   . HOH G 6 .   ? -34.81200 -19.68700 1.83200   1.000 19.97549 ? 416 HOH A O   1 
HETATM 1977 O  O   . HOH G 6 .   ? -39.92500 -29.07300 -16.85600 1.000 21.57934 ? 417 HOH A O   1 
HETATM 1978 O  O   . HOH G 6 .   ? -14.46800 -0.68700  -5.79500  1.000 15.86044 ? 418 HOH A O   1 
HETATM 1979 O  O   . HOH G 6 .   ? -20.94900 -32.39000 -26.12700 1.000 35.94854 ? 419 HOH A O   1 
HETATM 1980 O  O   . HOH G 6 .   ? -25.31200 -34.72600 -4.55700  1.000 43.92909 ? 420 HOH A O   1 
HETATM 1981 O  O   . HOH G 6 .   ? -20.39300 -1.06700  0.31100   1.000 23.29725 ? 421 HOH A O   1 
HETATM 1982 O  O   . HOH G 6 .   ? -25.83900 -17.44400 -24.70500 1.000 20.61863 ? 422 HOH A O   1 
HETATM 1983 O  O   . HOH G 6 .   ? -7.67500  10.23400  -20.16900 1.000 35.94415 ? 423 HOH A O   1 
HETATM 1984 O  O   . HOH G 6 .   ? -39.26700 -12.27900 -25.49300 1.000 28.53655 ? 424 HOH A O   1 
HETATM 1985 O  O   . HOH G 6 .   ? -28.09900 -28.01000 -28.49300 1.000 32.75693 ? 425 HOH A O   1 
HETATM 1986 O  O   . HOH G 6 .   ? -43.60200 -24.61900 -23.04200 1.000 41.92082 ? 426 HOH A O   1 
HETATM 1987 O  O   . HOH G 6 .   ? -11.51300 -25.92400 -27.20500 1.000 29.72039 ? 427 HOH A O   1 
HETATM 1988 O  O   . HOH G 6 .   ? -15.53900 -26.17900 -3.58500  1.000 38.09662 ? 428 HOH A O   1 
HETATM 1989 O  O   . HOH G 6 .   ? 1.58100   -11.55000 -8.84400  1.000 31.92557 ? 429 HOH A O   1 
HETATM 1990 O  O   . HOH G 6 .   ? -28.36300 -5.83300  -28.70800 1.000 33.32569 ? 430 HOH A O   1 
HETATM 1991 O  O   . HOH G 6 .   ? -29.74600 -24.18900 1.71500   1.000 21.24979 ? 431 HOH A O   1 
HETATM 1992 O  O   . HOH G 6 .   ? -14.33400 -25.84500 -20.46900 1.000 33.42123 ? 432 HOH A O   1 
HETATM 1993 O  O   . HOH G 6 .   ? -6.03500  -15.46000 -4.10200  1.000 22.65695 ? 433 HOH A O   1 
HETATM 1994 O  O   . HOH G 6 .   ? -11.34700 -2.82400  6.57000   1.000 23.88591 ? 434 HOH A O   1 
HETATM 1995 O  O   . HOH G 6 .   ? -17.34000 -27.24300 -10.23400 1.000 33.92093 ? 435 HOH A O   1 
HETATM 1996 O  O   . HOH G 6 .   ? -9.72900  8.14200   -17.21700 1.000 20.50144 ? 436 HOH A O   1 
HETATM 1997 O  O   . HOH G 6 .   ? -25.82800 -16.43900 -31.45200 1.000 22.81861 ? 437 HOH A O   1 
HETATM 1998 O  O   . HOH G 6 .   ? -42.61900 -18.79300 -4.63300  1.000 28.91888 ? 438 HOH A O   1 
HETATM 1999 O  O   . HOH G 6 .   ? -5.64100  -14.67100 3.69800   1.000 34.57402 ? 439 HOH A O   1 
HETATM 2000 O  O   . HOH G 6 .   ? -35.89500 -23.09100 -10.49800 1.000 17.48978 ? 440 HOH A O   1 
HETATM 2001 O  O   . HOH G 6 .   ? -15.66800 1.13600   -19.59800 1.000 17.02475 ? 441 HOH A O   1 
HETATM 2002 O  O   . HOH G 6 .   ? -12.87500 -3.53900  -0.77300  1.000 16.81983 ? 442 HOH A O   1 
HETATM 2003 O  O   . HOH G 6 .   ? -50.80400 -15.68100 -12.97400 1.000 28.30765 ? 443 HOH A O   1 
HETATM 2004 O  O   . HOH G 6 .   ? -16.15200 -12.78300 -20.80600 1.000 37.24173 ? 444 HOH A O   1 
HETATM 2005 O  O   . HOH G 6 .   ? -14.53000 5.61700   -14.71600 1.000 16.60734 ? 445 HOH A O   1 
HETATM 2006 O  O   . HOH G 6 .   ? -27.24100 -14.09300 -20.37700 1.000 18.98519 ? 446 HOH A O   1 
HETATM 2007 O  O   . HOH G 6 .   ? -13.27400 0.93000   -29.81300 1.000 29.14616 ? 447 HOH A O   1 
HETATM 2008 O  O   . HOH G 6 .   ? -40.30900 -19.92300 -7.97300  1.000 25.35436 ? 448 HOH A O   1 
HETATM 2009 O  O   . HOH G 6 .   ? -20.40500 -13.93200 -31.35000 1.000 37.85355 ? 449 HOH A O   1 
HETATM 2010 O  O   . HOH G 6 .   ? -45.74600 -19.74700 -19.70800 1.000 23.73252 ? 450 HOH A O   1 
HETATM 2011 O  O   . HOH G 6 .   ? -51.59800 -8.37300  -7.48100  1.000 28.70686 ? 451 HOH A O   1 
HETATM 2012 O  O   . HOH G 6 .   ? -41.01600 -12.91700 -8.07700  1.000 14.91409 ? 452 HOH A O   1 
HETATM 2013 O  O   . HOH G 6 .   ? -36.22700 -22.96200 -32.84400 1.000 37.39320 ? 453 HOH A O   1 
HETATM 2014 O  O   . HOH G 6 .   ? -18.40600 -19.18400 -0.89000  1.000 15.97710 ? 454 HOH A O   1 
HETATM 2015 O  O   . HOH G 6 .   ? -28.99400 -34.19200 -13.36100 1.000 30.09767 ? 455 HOH A O   1 
HETATM 2016 O  O   . HOH G 6 .   ? -36.22000 -11.84200 -0.88800  1.000 15.67943 ? 456 HOH A O   1 
HETATM 2017 O  O   . HOH G 6 .   ? -10.51800 -17.49000 4.03400   1.000 31.69046 ? 457 HOH A O   1 
HETATM 2018 O  O   . HOH G 6 .   ? -22.81600 -36.60200 -14.54400 1.000 38.28756 ? 458 HOH A O   1 
HETATM 2019 O  O   . HOH G 6 .   ? 1.05900   -8.84500  -2.08000  1.000 31.77958 ? 459 HOH A O   1 
HETATM 2020 O  O   . HOH G 6 .   ? -15.12700 -24.01700 -13.32400 1.000 25.83096 ? 460 HOH A O   1 
HETATM 2021 O  O   . HOH G 6 .   ? -16.90400 -28.00900 -3.37000  1.000 42.05136 ? 461 HOH A O   1 
HETATM 2022 O  O   . HOH G 6 .   ? -39.74500 -27.61300 -11.97200 1.000 22.76584 ? 462 HOH A O   1 
HETATM 2023 O  O   . HOH G 6 .   ? -37.93700 -32.46200 -15.41300 1.000 27.26502 ? 463 HOH A O   1 
HETATM 2024 O  O   . HOH G 6 .   ? -39.54700 -23.43300 -21.60900 1.000 25.02452 ? 464 HOH A O   1 
HETATM 2025 O  O   . HOH G 6 .   ? -33.96400 -16.29400 -8.59600  1.000 16.91787 ? 465 HOH A O   1 
HETATM 2026 O  O   . HOH G 6 .   ? -21.77800 -3.14200  2.61100   1.000 30.11764 ? 466 HOH A O   1 
HETATM 2027 O  O   . HOH G 6 .   ? -32.80200 -29.92500 -28.51900 1.000 29.55521 ? 467 HOH A O   1 
HETATM 2028 O  O   . HOH G 6 .   ? -31.09800 -11.60200 -33.30000 1.000 31.23726 ? 468 HOH A O   1 
HETATM 2029 O  O   . HOH G 6 .   ? -25.65100 -11.90600 -20.95300 1.000 19.06189 ? 469 HOH A O   1 
HETATM 2030 O  O   . HOH G 6 .   ? -17.56800 -9.52100  -10.01900 1.000 29.14370 ? 470 HOH A O   1 
HETATM 2031 O  O   . HOH G 6 .   ? -31.95300 -7.21300  -31.31700 1.000 27.63779 ? 471 HOH A O   1 
HETATM 2032 O  O   . HOH G 6 .   ? -41.08300 -23.30300 -19.49100 1.000 22.30671 ? 472 HOH A O   1 
HETATM 2033 O  O   . HOH G 6 .   ? -4.88900  -4.03900  -5.28800  1.000 27.03125 ? 473 HOH A O   1 
HETATM 2034 O  O   . HOH G 6 .   ? -16.16100 -1.73600  -1.12200  1.000 15.88935 ? 474 HOH A O   1 
HETATM 2035 O  O   . HOH G 6 .   ? -13.07100 -19.57100 -1.51800  1.000 20.84395 ? 475 HOH A O   1 
HETATM 2036 O  O   . HOH G 6 .   ? -19.59000 -14.85500 -14.26700 1.000 33.17634 ? 476 HOH A O   1 
HETATM 2037 O  O   . HOH G 6 .   ? -21.39300 -11.93800 -15.87700 1.000 26.72583 ? 477 HOH A O   1 
HETATM 2038 O  O   . HOH G 6 .   ? -38.94500 -31.54600 -17.74700 1.000 24.33461 ? 478 HOH A O   1 
HETATM 2039 O  O   . HOH G 6 .   ? -9.35500  -0.11200  -10.90700 1.000 36.39856 ? 479 HOH A O   1 
HETATM 2040 O  O   . HOH G 6 .   ? -24.95100 0.57000   -4.44400  1.000 20.00285 ? 480 HOH A O   1 
HETATM 2041 O  O   . HOH G 6 .   ? -29.63500 -16.78100 -34.14300 1.000 34.44324 ? 481 HOH A O   1 
HETATM 2042 O  O   . HOH G 6 .   ? -19.44800 -10.66000 -15.70800 1.000 34.34971 ? 482 HOH A O   1 
HETATM 2043 O  O   . HOH G 6 .   ? -23.31300 -34.24500 -22.45500 1.000 26.92673 ? 483 HOH A O   1 
HETATM 2044 O  O   . HOH G 6 .   ? -0.17200  -7.40500  -8.64200  1.000 31.07398 ? 484 HOH A O   1 
HETATM 2045 O  O   . HOH G 6 .   ? -10.44300 -1.90000  -24.44100 1.000 39.96822 ? 485 HOH A O   1 
HETATM 2046 O  O   . HOH G 6 .   ? -4.16800  -19.35700 -6.11900  1.000 41.09780 ? 486 HOH A O   1 
HETATM 2047 O  O   . HOH G 6 .   ? -36.18000 -12.05000 -25.51800 1.000 22.86751 ? 487 HOH A O   1 
HETATM 2048 O  O   . HOH G 6 .   ? -19.83600 -2.00900  -30.90200 1.000 31.09495 ? 488 HOH A O   1 
HETATM 2049 O  O   . HOH G 6 .   ? -25.08300 -22.59900 -34.27500 1.000 34.83325 ? 489 HOH A O   1 
HETATM 2050 O  O   . HOH G 6 .   ? -14.12400 -27.04100 -22.93200 1.000 34.80255 ? 490 HOH A O   1 
HETATM 2051 O  O   . HOH G 6 .   ? -34.28000 -32.46500 -13.75000 1.000 25.08569 ? 491 HOH A O   1 
HETATM 2052 O  O   . HOH G 6 .   ? -27.35400 -19.10600 -31.72100 1.000 35.49550 ? 492 HOH A O   1 
HETATM 2053 O  O   . HOH G 6 .   ? -20.00300 -34.02700 -13.25500 1.000 35.66752 ? 493 HOH A O   1 
HETATM 2054 O  O   . HOH G 6 .   ? -25.72300 -11.10800 0.31000   1.000 18.88738 ? 494 HOH A O   1 
HETATM 2055 O  O   . HOH G 6 .   ? -48.91000 -19.45500 -11.55300 1.000 33.99655 ? 495 HOH A O   1 
HETATM 2056 O  O   . HOH G 6 .   ? -15.03400 -33.53400 -22.45100 1.000 39.01816 ? 496 HOH A O   1 
HETATM 2057 O  O   . HOH G 6 .   ? -14.43000 -24.09300 -7.97400  1.000 26.53285 ? 497 HOH A O   1 
HETATM 2058 O  O   . HOH G 6 .   ? -43.89200 -21.83100 -13.21600 1.000 24.59302 ? 498 HOH A O   1 
HETATM 2059 O  O   . HOH G 6 .   ? -37.30100 -29.59500 -6.91700  1.000 25.45374 ? 499 HOH A O   1 
HETATM 2060 O  O   . HOH G 6 .   ? -40.63600 -26.11700 -28.13600 1.000 35.92547 ? 500 HOH A O   1 
HETATM 2061 O  O   . HOH G 6 .   ? -24.36800 -30.90700 -26.69900 1.000 28.45980 ? 501 HOH A O   1 
HETATM 2062 O  O   . HOH G 6 .   ? -5.57500  -2.04500  -3.46400  1.000 30.14689 ? 502 HOH A O   1 
HETATM 2063 O  O   . HOH G 6 .   ? -39.14600 -29.75900 -10.08800 1.000 24.29584 ? 503 HOH A O   1 
HETATM 2064 O  O   . HOH G 6 .   ? -42.76000 -27.38600 -8.96300  1.000 31.30462 ? 504 HOH A O   1 
HETATM 2065 O  O   . HOH G 6 .   ? -39.78400 -20.25700 -32.11800 1.000 40.99392 ? 505 HOH A O   1 
HETATM 2066 O  O   . HOH G 6 .   ? -47.69800 -21.66800 -11.66700 1.000 31.10369 ? 506 HOH A O   1 
HETATM 2067 O  O   . HOH G 6 .   ? -7.73000  1.44500   -11.92500 1.000 38.90970 ? 507 HOH A O   1 
HETATM 2068 O  O   . HOH G 6 .   ? -24.51100 -11.66400 -17.01000 1.000 22.80770 ? 508 HOH A O   1 
HETATM 2069 O  O   . HOH G 6 .   ? -31.56800 -7.44000  -7.53300  1.000 15.50993 ? 509 HOH A O   1 
HETATM 2070 O  O   . HOH G 6 .   ? -43.00800 -18.64000 -1.03800  1.000 19.13204 ? 510 HOH A O   1 
HETATM 2071 O  O   . HOH G 6 .   ? -49.93100 -17.85400 -18.91800 1.000 36.49981 ? 511 HOH A O   1 
HETATM 2072 O  O   . HOH G 6 .   ? -36.80800 -8.22300  -2.04900  1.000 16.52595 ? 512 HOH A O   1 
HETATM 2073 O  O   . HOH G 6 .   ? -15.71200 -30.10700 -16.08000 1.000 37.80912 ? 513 HOH A O   1 
HETATM 2074 O  O   . HOH G 6 .   ? -35.83100 -27.53400 -5.93600  1.000 19.44145 ? 514 HOH A O   1 
HETATM 2075 O  O   . HOH G 6 .   ? -26.91700 -0.90600  -1.57000  1.000 20.38569 ? 515 HOH A O   1 
HETATM 2076 O  O   . HOH G 6 .   ? -26.89100 -22.88400 -32.19400 1.000 28.22672 ? 516 HOH A O   1 
HETATM 2077 O  O   . HOH G 6 .   ? -12.97200 -17.24200 -26.15100 1.000 31.65744 ? 517 HOH A O   1 
HETATM 2078 O  O   . HOH G 6 .   ? -30.00800 -9.21400  -31.29900 1.000 29.13689 ? 518 HOH A O   1 
HETATM 2079 O  O   . HOH G 6 .   ? -13.50300 -10.01800 -3.73900  1.000 15.23361 ? 519 HOH A O   1 
HETATM 2080 O  O   . HOH G 6 .   ? -17.76700 -23.11200 -2.06500  1.000 29.03990 ? 520 HOH A O   1 
HETATM 2081 O  O   . HOH G 6 .   ? -25.79200 -2.25900  -27.53300 1.000 31.88574 ? 521 HOH A O   1 
HETATM 2082 O  O   . HOH G 6 .   ? -38.90200 -22.11700 -6.16100  1.000 22.39560 ? 522 HOH A O   1 
HETATM 2083 O  O   . HOH G 6 .   ? -38.80200 -28.23300 -14.39600 1.000 21.08808 ? 523 HOH A O   1 
HETATM 2084 O  O   . HOH G 6 .   ? -11.78100 -17.55700 -23.61600 1.000 34.94108 ? 524 HOH A O   1 
HETATM 2085 O  O   . HOH G 6 .   ? -33.89300 -24.37300 -31.66600 1.000 29.94786 ? 525 HOH A O   1 
HETATM 2086 O  O   . HOH G 6 .   ? -21.40900 -6.49900  1.95100   1.000 26.56153 ? 526 HOH A O   1 
HETATM 2087 O  O   . HOH G 6 .   ? -25.57300 -29.35300 -1.65900  1.000 32.24491 ? 527 HOH A O   1 
HETATM 2088 O  O   . HOH G 6 .   ? -18.57600 -18.25600 -16.72400 1.000 19.63065 ? 528 HOH A O   1 
HETATM 2089 O  O   . HOH G 6 .   ? -35.92600 -13.57300 -27.85600 1.000 27.29665 ? 529 HOH A O   1 
HETATM 2090 O  O   . HOH G 6 .   ? -16.70400 -29.25500 -14.26000 1.000 35.23952 ? 530 HOH A O   1 
HETATM 2091 O  O   . HOH G 6 .   ? -9.09500  4.56500   -14.70100 1.000 32.47405 ? 531 HOH A O   1 
HETATM 2092 O  O   . HOH G 6 .   ? -30.55100 -2.73000  -2.64400  1.000 21.38801 ? 532 HOH A O   1 
HETATM 2093 O  O   . HOH G 6 .   ? -11.19800 0.27500   -28.52000 1.000 42.76049 ? 533 HOH A O   1 
HETATM 2094 O  O   . HOH G 6 .   ? -40.08000 -27.57200 -8.53700  1.000 21.83970 ? 534 HOH A O   1 
HETATM 2095 O  O   . HOH G 6 .   ? -16.62900 -22.51200 -32.41600 1.000 31.78588 ? 535 HOH A O   1 
HETATM 2096 O  O   . HOH G 6 .   ? -44.72100 -15.61100 -8.29500  1.000 29.95985 ? 536 HOH A O   1 
HETATM 2097 O  O   . HOH G 6 .   ? -14.16100 0.16300   0.09900   0.5   15.73390 ? 537 HOH A O   1 
HETATM 2098 O  O   . HOH G 6 .   ? -3.22100  -13.53700 -11.79800 1.000 30.35378 ? 538 HOH A O   1 
HETATM 2099 O  O   . HOH G 6 .   ? -1.03200  -12.54000 -9.27600  1.000 22.81446 ? 539 HOH A O   1 
HETATM 2100 O  O   . HOH G 6 .   ? -26.74000 -31.31400 -28.23000 1.000 39.97578 ? 540 HOH A O   1 
HETATM 2101 O  O   . HOH G 6 .   ? -8.17200  -1.36600  -22.16200 1.000 43.49822 ? 541 HOH A O   1 
HETATM 2102 O  O   . HOH G 6 .   ? -25.51700 -10.71800 -31.57300 1.000 32.95956 ? 542 HOH A O   1 
HETATM 2103 O  O   . HOH G 6 .   ? -8.69500  -3.04900  4.24800   1.000 30.95427 ? 543 HOH A O   1 
HETATM 2104 O  O   . HOH G 6 .   ? -12.90700 -12.39600 -10.92200 1.000 37.38535 ? 544 HOH A O   1 
HETATM 2105 O  O   . HOH G 6 .   ? -2.72700  -6.34600  1.50100   1.000 22.48181 ? 545 HOH A O   1 
HETATM 2106 O  O   . HOH G 6 .   ? -50.25500 -14.15600 -17.87700 1.000 37.08652 ? 546 HOH A O   1 
HETATM 2107 O  O   . HOH G 6 .   ? -10.54100 -3.91600  -22.33100 1.000 36.32547 ? 547 HOH A O   1 
HETATM 2108 O  O   . HOH G 6 .   ? -12.77400 -23.28500 -16.74500 1.000 32.83264 ? 548 HOH A O   1 
HETATM 2109 O  O   . HOH G 6 .   ? -21.60500 -30.20200 -2.56000  1.000 43.79910 ? 549 HOH A O   1 
HETATM 2110 O  O   . HOH G 6 .   ? -16.42300 4.09000   -31.12600 1.000 22.96397 ? 550 HOH A O   1 
HETATM 2111 O  O   . HOH G 6 .   ? -10.70900 -19.69500 -2.75800  1.000 30.26748 ? 551 HOH A O   1 
HETATM 2112 O  O   . HOH G 6 .   ? -14.22000 8.23300   -15.92900 1.000 15.72111 ? 552 HOH A O   1 
HETATM 2113 O  O   . HOH G 6 .   ? -14.44300 -10.08200 -20.53500 1.000 38.40192 ? 553 HOH A O   1 
HETATM 2114 O  O   . HOH G 6 .   ? -21.73000 -33.00400 -12.07100 1.000 36.35722 ? 554 HOH A O   1 
HETATM 2115 O  O   . HOH G 6 .   ? -39.40300 -29.03400 -3.40000  1.000 29.79156 ? 555 HOH A O   1 
HETATM 2116 O  O   . HOH G 6 .   ? -46.32700 -14.62600 -5.84600  1.000 29.46023 ? 556 HOH A O   1 
HETATM 2117 O  O   . HOH G 6 .   ? -11.40200 -17.80700 -21.05400 1.000 45.70601 ? 557 HOH A O   1 
HETATM 2118 O  O   . HOH G 6 .   ? -25.70800 -25.53500 -30.98200 1.000 30.36303 ? 558 HOH A O   1 
HETATM 2119 O  O   . HOH G 6 .   ? -12.11800 0.19600   -7.02800  1.000 21.99432 ? 559 HOH A O   1 
HETATM 2120 O  O   . HOH G 6 .   ? -10.51000 -28.32900 -28.25200 1.000 31.74847 ? 560 HOH A O   1 
HETATM 2121 O  O   . HOH G 6 .   ? -12.60800 1.01700   1.98700   1.000 21.78656 ? 561 HOH A O   1 
HETATM 2122 O  O   . HOH G 6 .   ? -33.90000 -8.98500  -8.26700  1.000 22.41352 ? 562 HOH A O   1 
HETATM 2123 O  O   . HOH G 6 .   ? -15.89900 6.88200   -29.44000 1.000 22.82728 ? 563 HOH A O   1 
HETATM 2124 O  O   . HOH G 6 .   ? -3.77100  -3.88000  1.36800   1.000 34.76231 ? 564 HOH A O   1 
HETATM 2125 O  O   . HOH G 6 .   ? -32.31500 -34.75200 -25.92600 1.000 39.03287 ? 565 HOH A O   1 
HETATM 2126 O  O   . HOH G 6 .   ? -14.00900 -12.25600 -27.46200 1.000 40.04461 ? 566 HOH A O   1 
HETATM 2127 O  O   . HOH G 6 .   ? -18.28900 0.50100   -0.09500  0.575 15.43373 ? 567 HOH A O   1 
HETATM 2128 O  O   . HOH G 6 .   ? -18.27900 -11.57400 -25.99000 1.000 34.84971 ? 568 HOH A O   1 
HETATM 2129 O  O   . HOH G 6 .   ? -27.64800 -1.16200  -25.61500 1.000 35.71921 ? 569 HOH A O   1 
HETATM 2130 O  O   . HOH G 6 .   ? -10.24600 -2.98600  -12.71400 1.000 35.38066 ? 570 HOH A O   1 
HETATM 2131 O  O   . HOH G 6 .   ? -34.84900 -26.66200 -31.58900 1.000 40.61414 ? 571 HOH A O   1 
HETATM 2132 O  O   . HOH G 6 .   ? -17.05700 -20.17100 -33.15900 1.000 36.46635 ? 572 HOH A O   1 
HETATM 2133 O  O   . HOH G 6 .   ? -0.73800  -5.90000  -6.07800  1.000 32.52787 ? 573 HOH A O   1 
HETATM 2134 O  O   . HOH G 6 .   ? -51.71600 -14.63900 -14.83700 1.000 41.08733 ? 574 HOH A O   1 
HETATM 2135 O  O   . HOH G 6 .   ? -27.95000 -41.18000 -17.58600 0.50  41.95742 ? 575 HOH A O   1 
HETATM 2136 O  O   . HOH G 6 .   ? -12.70800 -22.74600 -13.86600 1.000 33.26175 ? 576 HOH A O   1 
HETATM 2137 O  O   . HOH G 6 .   ? -25.30900 -36.88000 -10.93000 1.000 44.89750 ? 577 HOH A O   1 
HETATM 2138 O  O   . HOH G 6 .   ? -16.30800 -10.08100 -26.72700 1.000 43.36639 ? 578 HOH A O   1 
HETATM 2139 O  O   . HOH G 6 .   ? -48.20200 -19.18900 -20.44300 1.000 37.57217 ? 579 HOH A O   1 
HETATM 2140 O  O   . HOH G 6 .   ? -26.69400 -3.47300  -30.11000 1.000 37.72898 ? 580 HOH A O   1 
HETATM 2141 O  O   . HOH G 6 .   ? -27.95000 -2.91700  0.00000   0.50  33.32554 ? 581 HOH A O   1 
HETATM 2142 O  O   . HOH G 6 .   ? -27.95000 -5.43700  0.00000   0.50  28.37090 ? 582 HOH A O   1 
HETATM 2143 O  O   . HOH G 6 .   ? -29.27000 -19.34900 -33.00400 1.000 40.73313 ? 583 HOH A O   1 
HETATM 2144 O  O   . HOH G 6 .   ? -6.89900  4.08800   -11.63900 1.000 43.93380 ? 584 HOH A O   1 
HETATM 2145 O  O   . HOH G 6 .   ? -42.66200 -29.63600 -16.76200 1.000 29.63099 ? 585 HOH A O   1 
HETATM 2146 O  O   . HOH G 6 .   ? -12.01500 -26.16800 -24.39300 1.000 33.89846 ? 586 HOH A O   1 
HETATM 2147 O  O   . HOH G 6 .   ? -25.08700 -33.63800 -26.31200 1.000 39.70069 ? 587 HOH A O   1 
HETATM 2148 O  O   . HOH G 6 .   ? -52.28800 -7.83600  -11.47400 1.000 46.45052 ? 588 HOH A O   1 
HETATM 2149 O  O   . HOH G 6 .   ? -22.80800 -34.19600 -25.09700 1.000 36.05909 ? 589 HOH A O   1 
HETATM 2150 O  O   . HOH G 6 .   ? -32.19400 -3.19300  -0.55600  1.000 30.60387 ? 590 HOH A O   1 
HETATM 2151 O  O   . HOH G 6 .   ? -8.69200  -2.27100  7.22000   1.000 31.60122 ? 591 HOH A O   1 
HETATM 2152 O  O   . HOH G 6 .   ? -24.34500 -0.48500  -1.25900  1.000 28.72918 ? 592 HOH A O   1 
HETATM 2153 O  O   . HOH G 6 .   ? -44.65600 -20.66900 -1.99000  1.000 35.30190 ? 593 HOH A O   1 
HETATM 2154 O  O   . HOH G 6 .   ? -50.20700 -6.33800  -11.23700 1.000 39.75539 ? 594 HOH A O   1 
HETATM 2155 O  O   . HOH G 6 .   ? -31.56600 -23.77400 -33.43200 1.000 35.77523 ? 595 HOH A O   1 
HETATM 2156 O  O   . HOH G 6 .   ? -33.08600 -5.05500  0.72000   1.000 33.04865 ? 596 HOH A O   1 
HETATM 2157 O  O   . HOH G 6 .   ? -51.05900 -5.71700  -6.97300  1.000 36.31591 ? 597 HOH A O   1 
HETATM 2158 O  O   . HOH G 6 .   ? -29.49200 -22.10400 -33.51600 1.000 35.70391 ? 598 HOH A O   1 
HETATM 2159 O  O   . HOH G 6 .   ? -13.15500 6.85700   -30.73000 1.000 39.96210 ? 599 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A SER A 1   ? 0.47966 0.37369 0.51000 -0.01239 -0.01712 0.02980  1   SER A N   
2    N  N   B SER A 1   ? 0.46698 0.35682 0.50214 -0.00446 -0.01820 0.01639  1   SER A N   
3    C  CA  A SER A 1   ? 0.46894 0.35987 0.50248 -0.01057 -0.01747 0.02185  1   SER A CA  
4    C  CA  B SER A 1   ? 0.47040 0.35953 0.50438 -0.01077 -0.01772 0.02214  1   SER A CA  
5    C  C   A SER A 1   ? 0.45513 0.34895 0.48934 -0.01604 -0.01621 0.01831  1   SER A C   
6    C  C   B SER A 1   ? 0.45556 0.34879 0.48991 -0.01609 -0.01629 0.01839  1   SER A C   
7    O  O   A SER A 1   ? 0.45941 0.35727 0.49247 -0.02118 -0.01492 0.02219  1   SER A O   
8    O  O   B SER A 1   ? 0.45948 0.35720 0.49255 -0.02112 -0.01495 0.02223  1   SER A O   
9    C  CB  A SER A 1   ? 0.48320 0.36034 0.52066 -0.00830 -0.01985 0.02143  1   SER A CB  
10   C  CB  B SER A 1   ? 0.47526 0.37269 0.50505 -0.01101 -0.01679 0.02826  1   SER A CB  
11   O  OG  A SER A 1   ? 0.47987 0.35541 0.51775 -0.00205 -0.02122 0.02316  1   SER A OG  
12   O  OG  B SER A 1   ? 0.46441 0.37248 0.49214 -0.00788 -0.01559 0.02475  1   SER A OG  
13   N  N   . ASN A 2   ? 0.49408 0.38641 0.53015 -0.01477 -0.01659 0.01079  2   ASN A N   
14   C  CA  . ASN A 2   ? 0.42832 0.32407 0.46525 -0.01932 -0.01598 0.00649  2   ASN A CA  
15   C  C   . ASN A 2   ? 0.33311 0.24195 0.36721 -0.02135 -0.01388 0.00734  2   ASN A C   
16   O  O   . ASN A 2   ? 0.32742 0.23994 0.36271 -0.02630 -0.01325 0.00684  2   ASN A O   
17   C  CB  . ASN A 2   ? 0.49879 0.38608 0.53919 -0.02522 -0.01691 0.00872  2   ASN A CB  
18   C  CG  . ASN A 2   ? 0.59113 0.47120 0.63471 -0.02591 -0.01859 0.00164  2   ASN A CG  
19   O  OD1 . ASN A 2   ? 0.61456 0.50017 0.65725 -0.02490 -0.01847 -0.00497 2   ASN A OD1 
20   N  ND2 . ASN A 2   ? 0.63892 0.50621 0.68594 -0.02773 -0.02033 0.00300  2   ASN A ND2 
21   N  N   . ARG A 3   ? 0.30610 0.22230 0.33696 -0.01747 -0.01286 0.00821  3   ARG A N   
22   C  CA  . ARG A 3   ? 0.25747 0.18509 0.28577 -0.01920 -0.01097 0.00906  3   ARG A CA  
23   C  C   . ARG A 3   ? 0.25601 0.18935 0.28441 -0.01973 -0.01063 0.00276  3   ARG A C   
24   O  O   . ARG A 3   ? 0.25443 0.19631 0.28185 -0.02196 -0.00931 0.00314  3   ARG A O   
25   C  CB  . ARG A 3   ? 0.25909 0.19242 0.28405 -0.01511 -0.01026 0.01139  3   ARG A CB  
26   C  CG  . ARG A 3   ? 0.25866 0.18859 0.28255 -0.01530 -0.01070 0.01859  3   ARG A CG  
27   C  CD  . ARG A 3   ? 0.26149 0.19617 0.28274 -0.01076 -0.01078 0.02012  3   ARG A CD  
28   N  NE  . ARG A 3   ? 0.24530 0.19070 0.26355 -0.01139 -0.00899 0.01938  3   ARG A NE  
29   C  CZ  . ARG A 3   ? 0.24168 0.19298 0.25824 -0.00780 -0.00875 0.01788  3   ARG A CZ  
30   N  NH1 . ARG A 3   ? 0.27562 0.22423 0.29351 -0.00326 -0.01002 0.01704  3   ARG A NH1 
31   N  NH2 . ARG A 3   ? 0.23867 0.19858 0.25270 -0.00874 -0.00722 0.01721  3   ARG A NH2 
32   N  N   . LEU A 4   ? 0.24354 0.17233 0.27299 -0.01766 -0.01188 -0.00302 4   LEU A N   
33   C  CA  . LEU A 4   ? 0.25228 0.18589 0.28115 -0.01809 -0.01202 -0.00896 4   LEU A CA  
34   C  C   . LEU A 4   ? 0.27217 0.19897 0.30421 -0.02123 -0.01384 -0.01277 4   LEU A C   
35   O  O   . LEU A 4   ? 0.29634 0.22325 0.32760 -0.02011 -0.01480 -0.01889 4   LEU A O   
36   C  CB  . LEU A 4   ? 0.24466 0.18095 0.27054 -0.01270 -0.01165 -0.01309 4   LEU A CB  
37   C  CG  . LEU A 4   ? 0.24378 0.18708 0.26695 -0.00987 -0.01004 -0.00989 4   LEU A CG  
38   C  CD1 . LEU A 4   ? 0.22060 0.16610 0.24158 -0.00514 -0.00951 -0.01400 4   LEU A CD1 
39   C  CD2 . LEU A 4   ? 0.23209 0.18439 0.25392 -0.01262 -0.00891 -0.00810 4   LEU A CD2 
40   N  N   . ASP A 5   ? 0.27651 0.19730 0.31189 -0.02538 -0.01438 -0.00912 5   ASP A N   
41   C  CA  . ASP A 5   ? 0.31887 0.23223 0.35798 -0.02901 -0.01629 -0.01237 5   ASP A CA  
42   C  C   . ASP A 5   ? 0.30236 0.22239 0.34194 -0.03145 -0.01704 -0.01772 5   ASP A C   
43   O  O   . ASP A 5   ? 0.27702 0.20665 0.31665 -0.03373 -0.01597 -0.01612 5   ASP A O   
44   C  CB  . ASP A 5   ? 0.38426 0.29274 0.42687 -0.03430 -0.01616 -0.00627 5   ASP A CB  
45   C  CG  . ASP A 5   ? 0.47481 0.37457 0.52203 -0.03873 -0.01822 -0.00912 5   ASP A CG  
46   O  OD1 . ASP A 5   ? 0.50764 0.39682 0.55565 -0.03639 -0.01996 -0.01225 5   ASP A OD1 
47   O  OD2 . ASP A 5   ? 0.52134 0.42500 0.57180 -0.04458 -0.01808 -0.00833 5   ASP A OD2 
48   N  N   . GLY A 6   ? 0.29302 0.20816 0.33271 -0.03051 -0.01903 -0.02440 6   GLY A N   
49   C  CA  . GLY A 6   ? 0.27522 0.19587 0.31509 -0.03273 -0.02047 -0.02979 6   GLY A CA  
50   C  C   . GLY A 6   ? 0.27327 0.20353 0.30824 -0.02897 -0.01981 -0.03256 6   GLY A C   
51   O  O   . GLY A 6   ? 0.27351 0.20763 0.30775 -0.02997 -0.02149 -0.03749 6   GLY A O   
52   N  N   . LYS A 7   ? 0.24402 0.17802 0.27554 -0.02477 -0.01767 -0.02957 7   LYS A N   
53   C  CA  . LYS A 7   ? 0.22757 0.17049 0.25465 -0.02174 -0.01689 -0.03139 7   LYS A CA  
54   C  C   . LYS A 7   ? 0.24913 0.18948 0.27234 -0.01802 -0.01774 -0.03771 7   LYS A C   
55   O  O   . LYS A 7   ? 0.27122 0.20340 0.29459 -0.01587 -0.01798 -0.03985 7   LYS A O   
56   C  CB  . LYS A 7   ? 0.21999 0.16723 0.24484 -0.01870 -0.01441 -0.02650 7   LYS A CB  
57   C  CG  . LYS A 7   ? 0.24401 0.19499 0.27134 -0.02194 -0.01317 -0.02034 7   LYS A CG  
58   C  CD  . LYS A 7   ? 0.23321 0.19339 0.26142 -0.02467 -0.01315 -0.02055 7   LYS A CD  
59   C  CE  . LYS A 7   ? 0.24039 0.20480 0.27051 -0.02724 -0.01123 -0.01460 7   LYS A CE  
60   N  NZ  . LYS A 7   ? 0.23383 0.20754 0.26604 -0.02986 -0.01101 -0.01488 7   LYS A NZ  
61   N  N   . VAL A 8   ? 0.24084 0.18835 0.26039 -0.01709 -0.01812 -0.04064 8   VAL A N   
62   C  CA  . VAL A 8   ? 0.24106 0.18802 0.25556 -0.01366 -0.01855 -0.04636 8   VAL A CA  
63   C  C   . VAL A 8   ? 0.22149 0.17623 0.23141 -0.01037 -0.01656 -0.04460 8   VAL A C   
64   O  O   . VAL A 8   ? 0.23307 0.19509 0.24241 -0.01172 -0.01682 -0.04284 8   VAL A O   
65   C  CB  . VAL A 8   ? 0.23291 0.18073 0.24661 -0.01622 -0.02154 -0.05185 8   VAL A CB  
66   C  CG1 . VAL A 8   ? 0.23954 0.18802 0.24644 -0.01247 -0.02167 -0.05740 8   VAL A CG1 
67   C  CG2 . VAL A 8   ? 0.25593 0.19547 0.27468 -0.02000 -0.02369 -0.05395 8   VAL A CG2 
68   N  N   . ALA A 9   ? 0.21943 0.17276 0.22661 -0.00608 -0.01457 -0.04500 9   ALA A N   
69   C  CA  . ALA A 9   ? 0.21028 0.17033 0.21425 -0.00345 -0.01237 -0.04227 9   ALA A CA  
70   C  C   . ALA A 9   ? 0.23614 0.19797 0.23431 -0.00004 -0.01144 -0.04642 9   ALA A C   
71   O  O   . ALA A 9   ? 0.27317 0.23006 0.27050 0.00206  -0.01117 -0.05045 9   ALA A O   
72   C  CB  . ALA A 9   ? 0.20559 0.16430 0.21211 -0.00163 -0.01036 -0.03769 9   ALA A CB  
73   N  N   . ILE A 10  ? 0.20517 0.17393 0.19933 0.00061  -0.01073 -0.04526 10  ILE A N   
74   C  CA  . ILE A 10  ? 0.20793 0.17944 0.19627 0.00381  -0.00898 -0.04747 10  ILE A CA  
75   C  C   . ILE A 10  ? 0.20205 0.17696 0.19112 0.00576  -0.00618 -0.04302 10  ILE A C   
76   O  O   . ILE A 10  ? 0.21417 0.19254 0.20499 0.00436  -0.00616 -0.03863 10  ILE A O   
77   C  CB  . ILE A 10  ? 0.21040 0.18677 0.19331 0.00299  -0.01043 -0.04893 10  ILE A CB  
78   C  CG1 . ILE A 10  ? 0.23651 0.20977 0.21830 0.00124  -0.01351 -0.05423 10  ILE A CG1 
79   C  CG2 . ILE A 10  ? 0.21544 0.19525 0.19187 0.00598  -0.00806 -0.04973 10  ILE A CG2 
80   C  CD1 . ILE A 10  ? 0.25353 0.23180 0.23077 0.00003  -0.01601 -0.05536 10  ILE A CD1 
81   N  N   . ILE A 11  ? 0.20580 0.18010 0.19390 0.00898  -0.00384 -0.04441 11  ILE A N   
82   C  CA  . ILE A 11  ? 0.19553 0.17378 0.18452 0.01077  -0.00127 -0.04073 11  ILE A CA  
83   C  C   . ILE A 11  ? 0.21944 0.20151 0.20304 0.01300  0.00103  -0.04295 11  ILE A C   
84   O  O   . ILE A 11  ? 0.22969 0.20982 0.21199 0.01529  0.00220  -0.04715 11  ILE A O   
85   C  CB  . ILE A 11  ? 0.19627 0.17101 0.19070 0.01261  -0.00045 -0.03961 11  ILE A CB  
86   C  CG1 . ILE A 11  ? 0.21700 0.18750 0.21602 0.01009  -0.00262 -0.03693 11  ILE A CG1 
87   C  CG2 . ILE A 11  ? 0.19049 0.17016 0.18622 0.01440  0.00191  -0.03617 11  ILE A CG2 
88   C  CD1 . ILE A 11  ? 0.23720 0.20217 0.24115 0.01194  -0.00263 -0.03628 11  ILE A CD1 
89   N  N   . THR A 12  ? 0.21743 0.20472 0.19783 0.01235  0.00181  -0.04020 12  THR A N   
90   C  CA  . THR A 12  ? 0.23013 0.22110 0.20511 0.01405  0.00430  -0.04159 12  THR A CA  
91   C  C   . THR A 12  ? 0.23187 0.22530 0.21011 0.01616  0.00746  -0.04001 12  THR A C   
92   O  O   . THR A 12  ? 0.20953 0.20343 0.19297 0.01583  0.00740  -0.03643 12  THR A O   
93   C  CB  . THR A 12  ? 0.24012 0.23504 0.21013 0.01256  0.00383  -0.03908 12  THR A CB  
94   O  OG1 . THR A 12  ? 0.22038 0.21755 0.19385 0.01156  0.00413  -0.03411 12  THR A OG1 
95   C  CG2 . THR A 12  ? 0.23777 0.23126 0.20505 0.01072  0.00033  -0.04076 12  THR A CG2 
96   N  N   . GLY A 13  ? 0.22538 0.22081 0.20067 0.01839  0.01023  -0.04294 13  GLY A N   
97   C  CA  . GLY A 13  ? 0.23741 0.23585 0.21705 0.02058  0.01324  -0.04200 13  GLY A CA  
98   C  C   . GLY A 13  ? 0.24465 0.23910 0.23159 0.02206  0.01219  -0.04230 13  GLY A C   
99   O  O   . GLY A 13  ? 0.24153 0.23785 0.23390 0.02249  0.01258  -0.03890 13  GLY A O   
100  N  N   . GLY A 14  ? 0.22707 0.21571 0.21413 0.02276  0.01057  -0.04624 14  GLY A N   
101  C  CA  . GLY A 14  ? 0.24577 0.22917 0.23946 0.02384  0.00904  -0.04594 14  GLY A CA  
102  C  C   . GLY A 14  ? 0.22352 0.20546 0.22035 0.02797  0.01088  -0.04986 14  GLY A C   
103  O  O   . GLY A 14  ? 0.22963 0.20539 0.23113 0.02927  0.00926  -0.05079 14  GLY A O   
104  N  N   . THR A 15  ? 0.24416 0.23166 0.23872 0.03016  0.01438  -0.05216 15  THR A N   
105  C  CA  . THR A 15  ? 0.23778 0.22435 0.23486 0.03443  0.01649  -0.05709 15  THR A CA  
106  C  C   . THR A 15  ? 0.24080 0.23246 0.24499 0.03733  0.01869  -0.05491 15  THR A C   
107  O  O   . THR A 15  ? 0.26264 0.25349 0.27101 0.04145  0.02012  -0.05856 15  THR A O   
108  C  CB  . THR A 15  ? 0.27415 0.26342 0.26379 0.03536  0.01919  -0.06242 15  THR A CB  
109  O  OG1 . THR A 15  ? 0.26930 0.26714 0.25593 0.03463  0.02240  -0.05992 15  THR A OG1 
110  C  CG2 . THR A 15  ? 0.26244 0.24721 0.24504 0.03245  0.01638  -0.06466 15  THR A CG2 
111  N  N   . LEU A 16  ? 0.24608 0.24258 0.25229 0.03535  0.01857  -0.04925 16  LEU A N   
112  C  CA  . LEU A 16  ? 0.26495 0.26715 0.27816 0.03740  0.02005  -0.04668 16  LEU A CA  
113  C  C   . LEU A 16  ? 0.26203 0.26493 0.27765 0.03456  0.01754  -0.04047 16  LEU A C   
114  O  O   . LEU A 16  ? 0.24606 0.24749 0.25712 0.03086  0.01592  -0.03810 16  LEU A O   
115  C  CB  . LEU A 16  ? 0.31121 0.32258 0.32297 0.03791  0.02448  -0.04745 16  LEU A CB  
116  C  CG  . LEU A 16  ? 0.40211 0.41599 0.41270 0.04139  0.02826  -0.05335 16  LEU A CG  
117  C  CD1 . LEU A 16  ? 0.41414 0.43728 0.42173 0.04013  0.03251  -0.05242 16  LEU A CD1 
118  C  CD2 . LEU A 16  ? 0.41891 0.43276 0.43853 0.04629  0.02870  -0.05550 16  LEU A CD2 
119  N  N   . GLY A 17  ? 0.26338 0.26898 0.28630 0.03654  0.01719  -0.03809 17  GLY A N   
120  C  CA  . GLY A 17  ? 0.22795 0.23661 0.25295 0.03411  0.01557  -0.03262 17  GLY A CA  
121  C  C   . GLY A 17  ? 0.21231 0.21457 0.23504 0.03120  0.01197  -0.02968 17  GLY A C   
122  O  O   . GLY A 17  ? 0.24823 0.24342 0.27219 0.03213  0.00984  -0.03035 17  GLY A O   
123  N  N   . ILE A 18  ? 0.20872 0.21356 0.22829 0.02761  0.01151  -0.02646 18  ILE A N   
124  C  CA  . ILE A 18  ? 0.21489 0.21545 0.23267 0.02469  0.00859  -0.02339 18  ILE A CA  
125  C  C   . ILE A 18  ? 0.22963 0.22357 0.24370 0.02367  0.00750  -0.02588 18  ILE A C   
126  O  O   . ILE A 18  ? 0.20115 0.18941 0.21653 0.02300  0.00515  -0.02470 18  ILE A O   
127  C  CB  . ILE A 18  ? 0.21882 0.22374 0.23375 0.02144  0.00877  -0.02047 18  ILE A CB  
128  C  CG1 . ILE A 18  ? 0.26232 0.27273 0.28179 0.02188  0.00879  -0.01762 18  ILE A CG1 
129  C  CG2 . ILE A 18  ? 0.23843 0.23947 0.25036 0.01838  0.00648  -0.01848 18  ILE A CG2 
130  C  CD1 . ILE A 18  ? 0.27999 0.29464 0.29699 0.01893  0.00934  -0.01554 18  ILE A CD1 
131  N  N   . GLY A 19  ? 0.22537 0.22007 0.23460 0.02327  0.00906  -0.02919 19  GLY A N   
132  C  CA  . GLY A 19  ? 0.21415 0.20322 0.21985 0.02205  0.00764  -0.03194 19  GLY A CA  
133  C  C   . GLY A 19  ? 0.22093 0.20342 0.22973 0.02433  0.00665  -0.03482 19  GLY A C   
134  O  O   . GLY A 19  ? 0.20626 0.18268 0.21484 0.02263  0.00436  -0.03519 19  GLY A O   
135  N  N   . LEU A 20  ? 0.20453 0.18814 0.21671 0.02819  0.00839  -0.03703 20  LEU A N   
136  C  CA  . LEU A 20  ? 0.22640 0.20309 0.24231 0.03096  0.00734  -0.03979 20  LEU A CA  
137  C  C   . LEU A 20  ? 0.22277 0.19467 0.24338 0.03044  0.00448  -0.03532 20  LEU A C   
138  O  O   . LEU A 20  ? 0.23821 0.20194 0.26014 0.03035  0.00247  -0.03631 20  LEU A O   
139  C  CB  . LEU A 20  ? 0.24615 0.22612 0.26535 0.03569  0.01005  -0.04310 20  LEU A CB  
140  C  CG  . LEU A 20  ? 0.28293 0.25553 0.30634 0.03937  0.00916  -0.04664 20  LEU A CG  
141  C  CD1 . LEU A 20  ? 0.29560 0.26100 0.31444 0.03815  0.00818  -0.05157 20  LEU A CD1 
142  C  CD2 . LEU A 20  ? 0.29413 0.27177 0.32152 0.04436  0.01223  -0.04985 20  LEU A CD2 
143  N  N   . ALA A 21  ? 0.19605 0.17268 0.21916 0.03009  0.00421  -0.03043 21  ALA A N   
144  C  CA  . ALA A 21  ? 0.19613 0.16871 0.22236 0.02928  0.00146  -0.02570 21  ALA A CA  
145  C  C   . ALA A 21  ? 0.20572 0.17394 0.22855 0.02480  -0.00033 -0.02395 21  ALA A C   
146  O  O   . ALA A 21  ? 0.23520 0.19648 0.25986 0.02402  -0.00244 -0.02215 21  ALA A O   
147  C  CB  . ALA A 21  ? 0.19234 0.17173 0.22073 0.02933  0.00139  -0.02119 21  ALA A CB  
148  N  N   . ILE A 22  ? 0.19054 0.16298 0.20881 0.02180  0.00050  -0.02415 22  ILE A N   
149  C  CA  . ILE A 22  ? 0.19713 0.16666 0.21289 0.01771  -0.00101 -0.02300 22  ILE A CA  
150  C  C   . ILE A 22  ? 0.21466 0.17659 0.23056 0.01746  -0.00213 -0.02673 22  ILE A C   
151  O  O   . ILE A 22  ? 0.22199 0.17838 0.23921 0.01504  -0.00400 -0.02498 22  ILE A O   
152  C  CB  . ILE A 22  ? 0.20117 0.17657 0.21240 0.01537  -0.00001 -0.02333 22  ILE A CB  
153  C  CG1 . ILE A 22  ? 0.20748 0.18949 0.21873 0.01512  0.00085  -0.01969 22  ILE A CG1 
154  C  CG2 . ILE A 22  ? 0.19259 0.16569 0.20217 0.01143  -0.00163 -0.02270 22  ILE A CG2 
155  C  CD1 . ILE A 22  ? 0.22332 0.21049 0.23029 0.01358  0.00203  -0.02039 22  ILE A CD1 
156  N  N   . ALA A 23  ? 0.21699 0.17861 0.23133 0.01970  -0.00091 -0.03208 23  ALA A N   
157  C  CA  . ALA A 23  ? 0.22827 0.18258 0.24235 0.01948  -0.00210 -0.03656 23  ALA A CA  
158  C  C   . ALA A 23  ? 0.24568 0.19174 0.26489 0.02110  -0.00363 -0.03568 23  ALA A C   
159  O  O   . ALA A 23  ? 0.25115 0.18984 0.27135 0.01880  -0.00562 -0.03624 23  ALA A O   
160  C  CB  . ALA A 23  ? 0.22863 0.18462 0.23950 0.02213  -0.00024 -0.04276 23  ALA A CB  
161  N  N   . THR A 24  ? 0.23400 0.18118 0.25689 0.02497  -0.00289 -0.03410 24  THR A N   
162  C  CA  . THR A 24  ? 0.26222 0.20139 0.29022 0.02722  -0.00458 -0.03287 24  THR A CA  
163  C  C   . THR A 24  ? 0.25555 0.19050 0.28462 0.02353  -0.00690 -0.02688 24  THR A C   
164  O  O   . THR A 24  ? 0.26007 0.18578 0.29116 0.02251  -0.00878 -0.02676 24  THR A O   
165  C  CB  . THR A 24  ? 0.26017 0.20316 0.29227 0.03220  -0.00356 -0.03184 24  THR A CB  
166  O  OG1 . THR A 24  ? 0.27579 0.22348 0.30685 0.03530  -0.00082 -0.03750 24  THR A OG1 
167  C  CG2 . THR A 24  ? 0.25668 0.19066 0.29425 0.03523  -0.00563 -0.03087 24  THR A CG2 
168  N  N   . LYS A 25  ? 0.25330 0.19479 0.28097 0.02142  -0.00668 -0.02187 25  LYS A N   
169  C  CA  . LYS A 25  ? 0.25583 0.19448 0.28370 0.01772  -0.00839 -0.01615 25  LYS A CA  
170  C  C   . LYS A 25  ? 0.24544 0.18113 0.27129 0.01283  -0.00897 -0.01731 25  LYS A C   
171  O  O   . LYS A 25  ? 0.28503 0.21470 0.31232 0.00998  -0.01048 -0.01413 25  LYS A O   
172  C  CB  . LYS A 25  ? 0.24297 0.18983 0.26930 0.01671  -0.00784 -0.01138 25  LYS A CB  
173  C  CG  . LYS A 25  ? 0.29814 0.24800 0.32732 0.02089  -0.00800 -0.00918 25  LYS A CG  
174  C  CD  . LYS A 25  ? 0.34502 0.28673 0.37800 0.02288  -0.01027 -0.00621 25  LYS A CD  
175  C  CE  . LYS A 25  ? 0.38072 0.32637 0.41698 0.02714  -0.01095 -0.00371 25  LYS A CE  
176  N  NZ  . LYS A 25  ? 0.45267 0.38974 0.49311 0.03009  -0.01344 -0.00123 25  LYS A NZ  
177  N  N   . PHE A 26  ? 0.24732 0.18747 0.26997 0.01164  -0.00791 -0.02150 26  PHE A N   
178  C  CA  . PHE A 26  ? 0.23446 0.17243 0.25596 0.00721  -0.00886 -0.02308 26  PHE A CA  
179  C  C   . PHE A 26  ? 0.24432 0.17189 0.26848 0.00688  -0.01054 -0.02593 26  PHE A C   
180  O  O   . PHE A 26  ? 0.25930 0.18218 0.28509 0.00277  -0.01195 -0.02404 26  PHE A O   
181  C  CB  . PHE A 26  ? 0.23306 0.17742 0.25052 0.00683  -0.00786 -0.02734 26  PHE A CB  
182  C  CG  . PHE A 26  ? 0.22411 0.17699 0.23923 0.00485  -0.00698 -0.02417 26  PHE A CG  
183  C  CD1 . PHE A 26  ? 0.22653 0.18283 0.24242 0.00509  -0.00637 -0.01892 26  PHE A CD1 
184  C  CD2 . PHE A 26  ? 0.23058 0.18798 0.24263 0.00294  -0.00699 -0.02662 26  PHE A CD2 
185  C  CE1 . PHE A 26  ? 0.20153 0.16509 0.21528 0.00351  -0.00555 -0.01667 26  PHE A CE1 
186  C  CE2 . PHE A 26  ? 0.19648 0.16108 0.20679 0.00153  -0.00628 -0.02390 26  PHE A CE2 
187  C  CZ  . PHE A 26  ? 0.19650 0.16397 0.20769 0.00180  -0.00544 -0.01913 26  PHE A CZ  
188  N  N   . VAL A 27  ? 0.24456 0.16842 0.26942 0.01107  -0.01027 -0.03066 27  VAL A N   
189  C  CA  . VAL A 27  ? 0.26419 0.17723 0.29175 0.01131  -0.01193 -0.03404 27  VAL A CA  
190  C  C   . VAL A 27  ? 0.28941 0.19475 0.32120 0.01087  -0.01346 -0.02840 27  VAL A C   
191  O  O   . VAL A 27  ? 0.30036 0.19719 0.33427 0.00763  -0.01524 -0.02800 27  VAL A O   
192  C  CB  . VAL A 27  ? 0.28909 0.20046 0.31648 0.01666  -0.01092 -0.04056 27  VAL A CB  
193  C  CG1 . VAL A 27  ? 0.30326 0.20227 0.33419 0.01775  -0.01273 -0.04387 27  VAL A CG1 
194  C  CG2 . VAL A 27  ? 0.29697 0.21460 0.31914 0.01637  -0.00967 -0.04635 27  VAL A CG2 
195  N  N   . GLU A 28  ? 0.27935 0.18749 0.31238 0.01391  -0.01295 -0.02374 28  GLU A N   
196  C  CA  . GLU A 28  ? 0.28739 0.18864 0.32363 0.01370  -0.01465 -0.01761 28  GLU A CA  
197  C  C   . GLU A 28  ? 0.30483 0.20519 0.34020 0.00740  -0.01537 -0.01250 28  GLU A C   
198  O  O   . GLU A 28  ? 0.32179 0.21337 0.35956 0.00556  -0.01699 -0.00871 28  GLU A O   
199  C  CB  . GLU A 28  ? 0.37566 0.28249 0.41263 0.01762  -0.01421 -0.01335 28  GLU A CB  
200  C  CG  . GLU A 28  ? 0.47318 0.37876 0.51325 0.02413  -0.01392 -0.01710 28  GLU A CG  
201  C  CD  . GLU A 28  ? 0.54188 0.45441 0.58338 0.02778  -0.01369 -0.01315 28  GLU A CD  
202  O  OE1 . GLU A 28  ? 0.57618 0.49105 0.62045 0.03309  -0.01282 -0.01660 28  GLU A OE1 
203  O  OE2 . GLU A 28  ? 0.54819 0.46415 0.58820 0.02534  -0.01437 -0.00685 28  GLU A OE2 
204  N  N   . GLU A 29  ? 0.28499 0.19440 0.31717 0.00411  -0.01407 -0.01211 29  GLU A N   
205  C  CA  . GLU A 29  ? 0.30105 0.21130 0.33276 -0.00177 -0.01425 -0.00769 29  GLU A CA  
206  C  C   . GLU A 29  ? 0.30275 0.21014 0.33528 -0.00616 -0.01491 -0.01170 29  GLU A C   
207  O  O   . GLU A 29  ? 0.29455 0.20504 0.32707 -0.01122 -0.01465 -0.00909 29  GLU A O   
208  C  CB  . GLU A 29  ? 0.29408 0.21579 0.32256 -0.00273 -0.01259 -0.00485 29  GLU A CB  
209  C  CG  . GLU A 29  ? 0.31159 0.23619 0.33941 0.00064  -0.01238 -0.00029 29  GLU A CG  
210  C  CD  . GLU A 29  ? 0.33285 0.25120 0.36186 -0.00074 -0.01369 0.00644  29  GLU A CD  
211  O  OE1 . GLU A 29  ? 0.31529 0.22947 0.34491 -0.00550 -0.01401 0.00878  29  GLU A OE1 
212  O  OE2 . GLU A 29  ? 0.35924 0.27716 0.38860 0.00285  -0.01447 0.00963  29  GLU A OE2 
213  N  N   . GLY A 30  ? 0.27929 0.18126 0.31272 -0.00438 -0.01577 -0.01821 30  GLY A N   
214  C  CA  . GLY A 30  ? 0.28224 0.17992 0.31699 -0.00862 -0.01709 -0.02222 30  GLY A CA  
215  C  C   . GLY A 30  ? 0.28245 0.18795 0.31431 -0.00969 -0.01675 -0.02769 30  GLY A C   
216  O  O   . GLY A 30  ? 0.30259 0.20559 0.33565 -0.01344 -0.01823 -0.03120 30  GLY A O   
217  N  N   . ALA A 31  ? 0.24131 0.15597 0.26951 -0.00667 -0.01510 -0.02842 31  ALA A N   
218  C  CA  . ALA A 31  ? 0.23694 0.15833 0.26188 -0.00730 -0.01503 -0.03332 31  ALA A CA  
219  C  C   . ALA A 31  ? 0.25033 0.16753 0.27352 -0.00428 -0.01563 -0.04083 31  ALA A C   
220  O  O   . ALA A 31  ? 0.29150 0.20363 0.31534 -0.00001 -0.01512 -0.04238 31  ALA A O   
221  C  CB  . ALA A 31  ? 0.23813 0.16999 0.25960 -0.00531 -0.01305 -0.03115 31  ALA A CB  
222  N  N   . LYS A 32  ? 0.24438 0.16433 0.26522 -0.00628 -0.01675 -0.04571 32  LYS A N   
223  C  CA  . LYS A 32  ? 0.24919 0.16826 0.26620 -0.00319 -0.01685 -0.05300 32  LYS A CA  
224  C  C   . LYS A 32  ? 0.25641 0.18569 0.26819 -0.00063 -0.01486 -0.05288 32  LYS A C   
225  O  O   . LYS A 32  ? 0.28100 0.21757 0.29193 -0.00286 -0.01471 -0.04940 32  LYS A O   
226  C  CB  . LYS A 32  ? 0.27476 0.19102 0.29155 -0.00688 -0.01961 -0.05844 32  LYS A CB  
227  C  CG  . LYS A 32  ? 0.34359 0.24806 0.36563 -0.00928 -0.02162 -0.05954 32  LYS A CG  
228  C  CD  . LYS A 32  ? 0.42590 0.32835 0.44860 -0.01399 -0.02470 -0.06460 32  LYS A CD  
229  C  CE  . LYS A 32  ? 0.46713 0.37505 0.49331 -0.01988 -0.02566 -0.05986 32  LYS A CE  
230  N  NZ  . LYS A 32  ? 0.48325 0.38426 0.51582 -0.02353 -0.02586 -0.05447 32  LYS A NZ  
231  N  N   . VAL A 33  ? 0.26165 0.19142 0.27028 0.00411  -0.01311 -0.05639 33  VAL A N   
232  C  CA  . VAL A 33  ? 0.24859 0.18729 0.25311 0.00672  -0.01065 -0.05496 33  VAL A CA  
233  C  C   . VAL A 33  ? 0.25228 0.19311 0.25079 0.00912  -0.00990 -0.06136 33  VAL A C   
234  O  O   . VAL A 33  ? 0.25928 0.19474 0.25761 0.01177  -0.00959 -0.06647 33  VAL A O   
235  C  CB  . VAL A 33  ? 0.23644 0.17573 0.24363 0.01034  -0.00838 -0.05115 33  VAL A CB  
236  C  CG1 . VAL A 33  ? 0.25586 0.20412 0.25904 0.01277  -0.00574 -0.05037 33  VAL A CG1 
237  C  CG2 . VAL A 33  ? 0.23778 0.17578 0.24962 0.00799  -0.00910 -0.04429 33  VAL A CG2 
238  N  N   . MET A 34  ? 0.24192 0.19054 0.23530 0.00844  -0.00948 -0.06098 34  MET A N   
239  C  CA  . MET A 34  ? 0.24582 0.19821 0.23239 0.01110  -0.00792 -0.06539 34  MET A CA  
240  C  C   . MET A 34  ? 0.23712 0.19650 0.22231 0.01341  -0.00468 -0.06127 34  MET A C   
241  O  O   . MET A 34  ? 0.22730 0.19178 0.21225 0.01158  -0.00481 -0.05651 34  MET A O   
242  C  CB  . MET A 34  ? 0.26068 0.21624 0.24175 0.00852  -0.01028 -0.06804 34  MET A CB  
243  C  CG  . MET A 34  ? 0.24387 0.20255 0.21663 0.01107  -0.00891 -0.07297 34  MET A CG  
244  S  SD  . MET A 34  ? 0.25776 0.20882 0.22908 0.01339  -0.00904 -0.08178 34  MET A SD  
245  C  CE  . MET A 34  ? 0.26368 0.21053 0.23548 0.00858  -0.01439 -0.08528 34  MET A CE  
246  N  N   . ILE A 35  ? 0.24466 0.20435 0.22953 0.01740  -0.00177 -0.06325 35  ILE A N   
247  C  CA  . ILE A 35  ? 0.23968 0.20634 0.22357 0.01943  0.00147  -0.05996 35  ILE A CA  
248  C  C   . ILE A 35  ? 0.23762 0.20930 0.21349 0.02043  0.00329  -0.06317 35  ILE A C   
249  O  O   . ILE A 35  ? 0.24817 0.21742 0.21994 0.02145  0.00309  -0.06918 35  ILE A O   
250  C  CB  . ILE A 35  ? 0.23028 0.19566 0.21969 0.02315  0.00373  -0.05961 35  ILE A CB  
251  C  CG1 . ILE A 35  ? 0.25484 0.21599 0.24374 0.02656  0.00476  -0.06646 35  ILE A CG1 
252  C  CG2 . ILE A 35  ? 0.22197 0.18306 0.21840 0.02204  0.00184  -0.05509 35  ILE A CG2 
253  C  CD1 . ILE A 35  ? 0.25127 0.21143 0.24663 0.03081  0.00676  -0.06627 35  ILE A CD1 
254  N  N   . THR A 36  ? 0.24012 0.21860 0.21339 0.02011  0.00511  -0.05917 36  THR A N   
255  C  CA  . THR A 36  ? 0.24636 0.22989 0.21172 0.02099  0.00730  -0.06107 36  THR A CA  
256  C  C   . THR A 36  ? 0.23840 0.22750 0.20464 0.02323  0.01161  -0.05893 36  THR A C   
257  O  O   . THR A 36  ? 0.23959 0.22984 0.21227 0.02359  0.01241  -0.05497 36  THR A O   
258  C  CB  . THR A 36  ? 0.26089 0.24772 0.22076 0.01814  0.00540  -0.05829 36  THR A CB  
259  O  OG1 . THR A 36  ? 0.22523 0.21609 0.18754 0.01730  0.00649  -0.05212 36  THR A OG1 
260  C  CG2 . THR A 36  ? 0.26174 0.24466 0.22285 0.01536  0.00089  -0.05904 36  THR A CG2 
261  N  N   . GLY A 37  ? 0.24060 0.23355 0.19992 0.02443  0.01428  -0.06157 37  GLY A N   
262  C  CA  . GLY A 37  ? 0.22607 0.22555 0.18475 0.02590  0.01877  -0.05975 37  GLY A CA  
263  C  C   . GLY A 37  ? 0.24196 0.24433 0.19093 0.02659  0.02093  -0.06354 37  GLY A C   
264  O  O   . GLY A 37  ? 0.25338 0.25233 0.19691 0.02642  0.01877  -0.06812 37  GLY A O   
265  N  N   . ARG A 38  ? 0.24002 0.24893 0.18680 0.02723  0.02529  -0.06168 38  ARG A N   
266  C  CA  . ARG A 38  ? 0.27295 0.28542 0.20944 0.02756  0.02786  -0.06433 38  ARG A CA  
267  C  C   . ARG A 38  ? 0.28571 0.29874 0.22131 0.03113  0.03112  -0.07135 38  ARG A C   
268  O  O   . ARG A 38  ? 0.30324 0.31691 0.22942 0.03161  0.03194  -0.07568 38  ARG A O   
269  C  CB  . ARG A 38  ? 0.29724 0.31639 0.23129 0.02615  0.03131  -0.05887 38  ARG A CB  
270  C  CG  . ARG A 38  ? 0.32266 0.34094 0.25682 0.02291  0.02821  -0.05239 38  ARG A CG  
271  C  CD  . ARG A 38  ? 0.36119 0.38502 0.29608 0.02152  0.03164  -0.04676 38  ARG A CD  
272  N  NE  . ARG A 38  ? 0.34891 0.37564 0.29366 0.02290  0.03439  -0.04630 38  ARG A NE  
273  C  CZ  . ARG A 38  ? 0.39211 0.42520 0.33867 0.02276  0.03896  -0.04416 38  ARG A CZ  
274  N  NH1 . ARG A 38  ? 0.41972 0.45651 0.35845 0.02110  0.04170  -0.04193 38  ARG A NH1 
275  N  NH2 . ARG A 38  ? 0.40698 0.44294 0.36338 0.02421  0.04074  -0.04409 38  ARG A NH2 
276  N  N   . HIS A 39  ? 0.26617 0.27904 0.21112 0.03387  0.03289  -0.07277 39  HIS A N   
277  C  CA  . HIS A 39  ? 0.27580 0.28994 0.22118 0.03789  0.03656  -0.07942 39  HIS A CA  
278  C  C   . HIS A 39  ? 0.29566 0.30138 0.24531 0.03998  0.03339  -0.08489 39  HIS A C   
279  O  O   . HIS A 39  ? 0.30630 0.30785 0.26519 0.04024  0.03094  -0.08258 39  HIS A O   
280  C  CB  . HIS A 39  ? 0.27542 0.29629 0.22891 0.04008  0.04117  -0.07748 39  HIS A CB  
281  C  CG  . HIS A 39  ? 0.32419 0.35302 0.27471 0.03761  0.04441  -0.07190 39  HIS A CG  
282  N  ND1 . HIS A 39  ? 0.35033 0.38065 0.30618 0.03500  0.04312  -0.06484 39  HIS A ND1 
283  C  CD2 . HIS A 39  ? 0.34527 0.38068 0.28788 0.03717  0.04895  -0.07228 39  HIS A CD2 
284  C  CE1 . HIS A 39  ? 0.35153 0.38855 0.30349 0.03300  0.04659  -0.06116 39  HIS A CE1 
285  N  NE2 . HIS A 39  ? 0.35282 0.39316 0.29675 0.03419  0.05028  -0.06524 39  HIS A NE2 
286  N  N   . SER A 40  ? 0.32360 0.32679 0.26639 0.04152  0.03363  -0.09221 40  SER A N   
287  C  CA  . SER A 40  ? 0.33006 0.32413 0.27589 0.04295  0.03022  -0.09787 40  SER A CA  
288  C  C   . SER A 40  ? 0.31018 0.30266 0.26576 0.04758  0.03244  -0.10089 40  SER A C   
289  O  O   . SER A 40  ? 0.33551 0.31966 0.29754 0.04842  0.02910  -0.10244 40  SER A O   
290  C  CB  . SER A 40  ? 0.34802 0.33977 0.28319 0.04306  0.02949  -0.10530 40  SER A CB  
291  O  OG  . SER A 40  ? 0.37060 0.36815 0.30107 0.04639  0.03503  -0.11014 40  SER A OG  
292  N  N   . ASP A 41  ? 0.31838 0.31877 0.27559 0.05064  0.03798  -0.10161 41  ASP A N   
293  C  CA  . ASP A 41  ? 0.32442 0.32428 0.29213 0.05546  0.03993  -0.10403 41  ASP A CA  
294  C  C   . ASP A 41  ? 0.32205 0.31856 0.30042 0.05469  0.03658  -0.09760 41  ASP A C   
295  O  O   . ASP A 41  ? 0.35618 0.34528 0.34183 0.05719  0.03422  -0.09957 41  ASP A O   
296  C  CB  . ASP A 41  ? 0.29815 0.30912 0.26670 0.05824  0.04658  -0.10475 41  ASP A CB  
297  C  CG  . ASP A 41  ? 0.30320 0.32274 0.27019 0.05447  0.04834  -0.09681 41  ASP A CG  
298  O  OD1 . ASP A 41  ? 0.30242 0.32390 0.25896 0.05093  0.04837  -0.09520 41  ASP A OD1 
299  O  OD2 . ASP A 41  ? 0.30710 0.33129 0.28338 0.05508  0.04951  -0.09219 41  ASP A OD2 
300  N  N   . VAL A 42  ? 0.29085 0.29237 0.26986 0.05119  0.03623  -0.08987 42  VAL A N   
301  C  CA  . VAL A 42  ? 0.28783 0.28693 0.27582 0.05021  0.03314  -0.08368 42  VAL A CA  
302  C  C   . VAL A 42  ? 0.28266 0.27145 0.27019 0.04774  0.02758  -0.08324 42  VAL A C   
303  O  O   . VAL A 42  ? 0.28890 0.27165 0.28410 0.04881  0.02486  -0.08183 42  VAL A O   
304  C  CB  . VAL A 42  ? 0.28607 0.29285 0.27382 0.04681  0.03414  -0.07623 42  VAL A CB  
305  C  CG1 . VAL A 42  ? 0.30392 0.30890 0.30038 0.04584  0.03104  -0.07007 42  VAL A CG1 
306  C  CG2 . VAL A 42  ? 0.29963 0.31693 0.28776 0.04860  0.03993  -0.07670 42  VAL A CG2 
307  N  N   . GLY A 43  ? 0.28309 0.26999 0.26174 0.04432  0.02577  -0.08427 43  GLY A N   
308  C  CA  . GLY A 43  ? 0.29322 0.27218 0.27191 0.04104  0.02059  -0.08281 43  GLY A CA  
309  C  C   . GLY A 43  ? 0.29760 0.26679 0.27933 0.04295  0.01827  -0.08844 43  GLY A C   
310  O  O   . GLY A 43  ? 0.30320 0.26551 0.29045 0.04159  0.01472  -0.08591 43  GLY A O   
311  N  N   . GLU A 44  ? 0.32026 0.28835 0.29817 0.04596  0.02024  -0.09617 44  GLU A N   
312  C  CA  . GLU A 44  ? 0.33672 0.29440 0.31764 0.04767  0.01776  -0.10191 44  GLU A CA  
313  C  C   . GLU A 44  ? 0.34381 0.29790 0.33563 0.05162  0.01807  -0.10063 44  GLU A C   
314  O  O   . GLU A 44  ? 0.34252 0.28680 0.33945 0.05144  0.01458  -0.10081 44  GLU A O   
315  C  CB  . GLU A 44  ? 0.37449 0.33160 0.34817 0.05007  0.01971  -0.11123 44  GLU A CB  
316  C  CG  . GLU A 44  ? 0.40512 0.36529 0.36725 0.04640  0.01879  -0.11287 44  GLU A CG  
317  C  CD  . GLU A 44  ? 0.44727 0.39969 0.40806 0.04190  0.01300  -0.11306 44  GLU A CD  
318  O  OE1 . GLU A 44  ? 0.45292 0.39748 0.42163 0.04113  0.00996  -0.11132 44  GLU A OE1 
319  O  OE2 . GLU A 44  ? 0.47090 0.42543 0.42272 0.03905  0.01146  -0.11480 44  GLU A OE2 
320  N  N   . LYS A 45  ? 0.32804 0.29008 0.32387 0.05500  0.02199  -0.09882 45  LYS A N   
321  C  CA  . LYS A 45  ? 0.33825 0.29772 0.34487 0.05883  0.02172  -0.09683 45  LYS A CA  
322  C  C   . LYS A 45  ? 0.31462 0.27110 0.32608 0.05550  0.01790  -0.08853 45  LYS A C   
323  O  O   . LYS A 45  ? 0.33917 0.28777 0.35757 0.05701  0.01521  -0.08724 45  LYS A O   
324  C  CB  . LYS A 45  ? 0.40154 0.37171 0.41195 0.06287  0.02664  -0.09662 45  LYS A CB  
325  C  CG  . LYS A 45  ? 0.47195 0.43917 0.49286 0.06880  0.02690  -0.09834 45  LYS A CG  
326  C  CD  . LYS A 45  ? 0.49374 0.47291 0.51949 0.07270  0.03180  -0.09824 45  LYS A CD  
327  C  CE  . LYS A 45  ? 0.48991 0.47694 0.50744 0.07299  0.03692  -0.10369 45  LYS A CE  
328  N  NZ  . LYS A 45  ? 0.49694 0.48844 0.51934 0.07969  0.04151  -0.11047 45  LYS A NZ  
329  N  N   . ALA A 46  ? 0.29377 0.25625 0.30144 0.05106  0.01766  -0.08281 46  ALA A N   
330  C  CA  . ALA A 46  ? 0.28542 0.24591 0.29702 0.04788  0.01442  -0.07523 46  ALA A CA  
331  C  C   . ALA A 46  ? 0.30208 0.25152 0.31371 0.04515  0.01007  -0.07561 46  ALA A C   
332  O  O   . ALA A 46  ? 0.32644 0.26991 0.34426 0.04528  0.00755  -0.07199 46  ALA A O   
333  C  CB  . ALA A 46  ? 0.27082 0.23940 0.27781 0.04377  0.01509  -0.07006 46  ALA A CB  
334  N  N   . ALA A 47  ? 0.30793 0.25460 0.31275 0.04256  0.00907  -0.07996 47  ALA A N   
335  C  CA  . ALA A 47  ? 0.31586 0.25260 0.32126 0.03939  0.00495  -0.08058 47  ALA A CA  
336  C  C   . ALA A 47  ? 0.34987 0.27648 0.36174 0.04281  0.00371  -0.08353 47  ALA A C   
337  O  O   . ALA A 47  ? 0.35121 0.27069 0.36813 0.04118  0.00078  -0.07946 47  ALA A O   
338  C  CB  . ALA A 47  ? 0.32605 0.26208 0.32340 0.03663  0.00399  -0.08596 47  ALA A CB  
339  N  N   . LYS A 48  ? 0.35145 0.27741 0.36332 0.04777  0.00609  -0.09043 48  LYS A N   
340  C  CA  . LYS A 48  ? 0.37711 0.29290 0.39524 0.05177  0.00498  -0.09412 48  LYS A CA  
341  C  C   . LYS A 48  ? 0.36824 0.28289 0.39521 0.05431  0.00432  -0.08770 48  LYS A C   
342  O  O   . LYS A 48  ? 0.38818 0.29220 0.42078 0.05563  0.00169  -0.08740 48  LYS A O   
343  C  CB  . LYS A 48  ? 0.42560 0.34314 0.44214 0.05728  0.00844  -0.10279 48  LYS A CB  
344  C  CG  . LYS A 48  ? 0.47891 0.39380 0.48716 0.05578  0.00829  -0.11100 48  LYS A CG  
345  C  CD  . LYS A 48  ? 0.52104 0.43835 0.52794 0.06186  0.01233  -0.11958 48  LYS A CD  
346  C  CE  . LYS A 48  ? 0.55999 0.47083 0.56011 0.06139  0.01133  -0.12918 48  LYS A CE  
347  N  NZ  . LYS A 48  ? 0.57260 0.47290 0.57826 0.06650  0.01094  -0.13620 48  LYS A NZ  
348  N  N   . SER A 49  ? 0.35269 0.27790 0.38093 0.05507  0.00649  -0.08259 49  SER A N   
349  C  CA  . SER A 49  ? 0.37161 0.29702 0.40783 0.05748  0.00558  -0.07644 49  SER A CA  
350  C  C   . SER A 49  ? 0.37245 0.29227 0.40999 0.05282  0.00168  -0.06905 49  SER A C   
351  O  O   . SER A 49  ? 0.38858 0.30492 0.43240 0.05473  -0.00013 -0.06431 49  SER A O   
352  C  CB  . SER A 49  ? 0.36041 0.29932 0.39754 0.05898  0.00884  -0.07335 49  SER A CB  
353  O  OG  . SER A 49  ? 0.36902 0.31392 0.40164 0.05362  0.00848  -0.06782 49  SER A OG  
354  N  N   . VAL A 50  ? 0.34740 0.26666 0.37924 0.04692  0.00037  -0.06790 50  VAL A N   
355  C  CA  . VAL A 50  ? 0.32262 0.23838 0.35530 0.04210  -0.00265 -0.06090 50  VAL A CA  
356  C  C   . VAL A 50  ? 0.35864 0.26156 0.39246 0.03968  -0.00582 -0.06251 50  VAL A C   
357  O  O   . VAL A 50  ? 0.39110 0.28742 0.42901 0.03845  -0.00825 -0.05719 50  VAL A O   
358  C  CB  . VAL A 50  ? 0.31958 0.24391 0.34641 0.03710  -0.00202 -0.05793 50  VAL A CB  
359  C  CG1 . VAL A 50  ? 0.29696 0.21755 0.32418 0.03178  -0.00486 -0.05204 50  VAL A CG1 
360  C  CG2 . VAL A 50  ? 0.31597 0.25156 0.34296 0.03886  0.00055  -0.05467 50  VAL A CG2 
361  N  N   . GLY A 51  ? 0.34533 0.24444 0.37546 0.03872  -0.00595 -0.06964 51  GLY A N   
362  C  CA  . GLY A 51  ? 0.34177 0.22880 0.37325 0.03575  -0.00911 -0.07147 51  GLY A CA  
363  C  C   . GLY A 51  ? 0.36643 0.25038 0.39369 0.03597  -0.00897 -0.08091 51  GLY A C   
364  O  O   . GLY A 51  ? 0.36783 0.25849 0.39117 0.03920  -0.00616 -0.08604 51  GLY A O   
365  N  N   . THR A 52  ? 0.37628 0.25011 0.40423 0.03227  -0.01202 -0.08319 52  THR A N   
366  C  CA  . THR A 52  ? 0.38534 0.25524 0.40916 0.03165  -0.01272 -0.09240 52  THR A CA  
367  C  C   . THR A 52  ? 0.36595 0.24458 0.38280 0.02685  -0.01291 -0.09307 52  THR A C   
368  O  O   . THR A 52  ? 0.33941 0.22510 0.35567 0.02344  -0.01294 -0.08628 52  THR A O   
369  C  CB  . THR A 52  ? 0.43888 0.29406 0.46697 0.02917  -0.01629 -0.09450 52  THR A CB  
370  O  OG1 . THR A 52  ? 0.46105 0.31548 0.49024 0.02219  -0.01873 -0.08844 52  THR A OG1 
371  C  CG2 . THR A 52  ? 0.44944 0.29502 0.48482 0.03384  -0.01662 -0.09262 52  THR A CG2 
372  N  N   . PRO A 53  ? 0.36733 0.24573 0.37858 0.02665  -0.01323 -0.10138 53  PRO A N   
373  C  CA  . PRO A 53  ? 0.34208 0.22828 0.34676 0.02213  -0.01413 -0.10190 53  PRO A CA  
374  C  C   . PRO A 53  ? 0.36600 0.24972 0.37356 0.01533  -0.01763 -0.09742 53  PRO A C   
375  O  O   . PRO A 53  ? 0.35644 0.24833 0.36034 0.01178  -0.01824 -0.09525 53  PRO A O   
376  C  CB  . PRO A 53  ? 0.38218 0.26595 0.38092 0.02349  -0.01451 -0.11237 53  PRO A CB  
377  C  CG  . PRO A 53  ? 0.39057 0.27052 0.39125 0.03019  -0.01177 -0.11663 53  PRO A CG  
378  C  CD  . PRO A 53  ? 0.38083 0.25334 0.39073 0.03123  -0.01244 -0.11083 53  PRO A CD  
379  N  N   . ASP A 54  ? 0.38233 0.25511 0.39657 0.01341  -0.01987 -0.09583 54  ASP A N   
380  C  CA  . ASP A 54  ? 0.42976 0.30090 0.44756 0.00674  -0.02257 -0.09066 54  ASP A CA  
381  C  C   . ASP A 54  ? 0.40044 0.27936 0.41995 0.00555  -0.02110 -0.08096 54  ASP A C   
382  O  O   . ASP A 54  ? 0.38744 0.26895 0.40853 0.00009  -0.02257 -0.07664 54  ASP A O   
383  C  CB  . ASP A 54  ? 0.50922 0.36604 0.53371 0.00493  -0.02501 -0.09088 54  ASP A CB  
384  C  CG  . ASP A 54  ? 0.60847 0.45659 0.63173 0.00471  -0.02723 -0.10081 54  ASP A CG  
385  O  OD1 . ASP A 54  ? 0.64768 0.50034 0.66639 0.00158  -0.02879 -0.10564 54  ASP A OD1 
386  O  OD2 . ASP A 54  ? 0.65108 0.48776 0.67787 0.00786  -0.02759 -0.10398 54  ASP A OD2 
387  N  N   . GLN A 55  ? 0.38797 0.27094 0.40751 0.01047  -0.01824 -0.07771 55  GLN A N   
388  C  CA  . GLN A 55  ? 0.35225 0.24247 0.37304 0.00989  -0.01682 -0.06910 55  GLN A CA  
389  C  C   . GLN A 55  ? 0.31131 0.21404 0.32663 0.01162  -0.01435 -0.06866 55  GLN A C   
390  O  O   . GLN A 55  ? 0.27304 0.18303 0.28771 0.00901  -0.01401 -0.06315 55  GLN A O   
391  C  CB  . GLN A 55  ? 0.35377 0.23929 0.37945 0.01392  -0.01588 -0.06487 55  GLN A CB  
392  C  CG  . GLN A 55  ? 0.40835 0.28041 0.43974 0.01264  -0.01831 -0.06389 55  GLN A CG  
393  C  CD  . GLN A 55  ? 0.44590 0.31326 0.48161 0.01792  -0.01765 -0.06083 55  GLN A CD  
394  O  OE1 . GLN A 55  ? 0.45160 0.31940 0.48721 0.02377  -0.01610 -0.06532 55  GLN A OE1 
395  N  NE2 . GLN A 55  ? 0.48674 0.35032 0.52623 0.01599  -0.01878 -0.05297 55  GLN A NE2 
396  N  N   . ILE A 56  ? 0.31960 0.22486 0.33105 0.01607  -0.01239 -0.07426 56  ILE A N   
397  C  CA  . ILE A 56  ? 0.28980 0.20633 0.29664 0.01801  -0.00960 -0.07286 56  ILE A CA  
398  C  C   . ILE A 56  ? 0.29567 0.21440 0.29636 0.02082  -0.00818 -0.08067 56  ILE A C   
399  O  O   . ILE A 56  ? 0.31049 0.22313 0.31196 0.02421  -0.00774 -0.08649 56  ILE A O   
400  C  CB  . ILE A 56  ? 0.28814 0.20780 0.29865 0.02160  -0.00726 -0.06756 56  ILE A CB  
401  C  CG1 . ILE A 56  ? 0.27958 0.21058 0.28573 0.02321  -0.00430 -0.06627 56  ILE A CG1 
402  C  CG2 . ILE A 56  ? 0.29645 0.20912 0.31113 0.02657  -0.00661 -0.07077 56  ILE A CG2 
403  C  CD1 . ILE A 56  ? 0.27688 0.21249 0.28691 0.02509  -0.00268 -0.05987 56  ILE A CD1 
404  N  N   . GLN A 57  ? 0.27501 0.20222 0.26927 0.01942  -0.00754 -0.08089 57  GLN A N   
405  C  CA  . GLN A 57  ? 0.27975 0.21063 0.26674 0.02188  -0.00582 -0.08727 57  GLN A CA  
406  C  C   . GLN A 57  ? 0.26356 0.20525 0.24610 0.02282  -0.00289 -0.08361 57  GLN A C   
407  O  O   . GLN A 57  ? 0.25341 0.19947 0.23804 0.02097  -0.00286 -0.07681 57  GLN A O   
408  C  CB  . GLN A 57  ? 0.29246 0.22131 0.27445 0.01860  -0.00897 -0.09262 57  GLN A CB  
409  C  CG  . GLN A 57  ? 0.32998 0.24766 0.31547 0.01826  -0.01141 -0.09821 57  GLN A CG  
410  C  CD  . GLN A 57  ? 0.37559 0.29147 0.35695 0.01443  -0.01506 -0.10344 57  GLN A CD  
411  O  OE1 . GLN A 57  ? 0.40765 0.32977 0.38098 0.01442  -0.01499 -0.10655 57  GLN A OE1 
412  N  NE2 . GLN A 57  ? 0.37903 0.28654 0.36586 0.01088  -0.01845 -0.10414 57  GLN A NE2 
413  N  N   . PHE A 58  ? 0.29601 0.24173 0.27216 0.02564  -0.00032 -0.08838 58  PHE A N   
414  C  CA  . PHE A 58  ? 0.27389 0.22934 0.24480 0.02641  0.00271  -0.08564 58  PHE A CA  
415  C  C   . PHE A 58  ? 0.27193 0.23096 0.23337 0.02427  0.00143  -0.08836 58  PHE A C   
416  O  O   . PHE A 58  ? 0.30008 0.25530 0.25733 0.02422  -0.00021 -0.09507 58  PHE A O   
417  C  CB  . PHE A 58  ? 0.28849 0.24697 0.25953 0.03137  0.00731  -0.08821 58  PHE A CB  
418  C  CG  . PHE A 58  ? 0.27079 0.23885 0.23497 0.03201  0.01083  -0.08702 58  PHE A CG  
419  C  CD1 . PHE A 58  ? 0.27465 0.24902 0.24011 0.03060  0.01197  -0.07978 58  PHE A CD1 
420  C  CD2 . PHE A 58  ? 0.27730 0.24766 0.23352 0.03386  0.01300  -0.09319 58  PHE A CD2 
421  C  CE1 . PHE A 58  ? 0.26340 0.24578 0.22281 0.03086  0.01522  -0.07835 58  PHE A CE1 
422  C  CE2 . PHE A 58  ? 0.29101 0.26995 0.24053 0.03416  0.01647  -0.09160 58  PHE A CE2 
423  C  CZ  . PHE A 58  ? 0.25993 0.24463 0.21128 0.03257  0.01757  -0.08403 58  PHE A CZ  
424  N  N   . PHE A 59  ? 0.27058 0.23663 0.22867 0.02255  0.00186  -0.08314 59  PHE A N   
425  C  CA  . PHE A 59  ? 0.28374 0.25427 0.23243 0.02104  0.00086  -0.08441 59  PHE A CA  
426  C  C   . PHE A 59  ? 0.27563 0.25401 0.21984 0.02245  0.00483  -0.08074 59  PHE A C   
427  O  O   . PHE A 59  ? 0.25372 0.23529 0.20191 0.02170  0.00579  -0.07425 59  PHE A O   
428  C  CB  . PHE A 59  ? 0.27420 0.24471 0.22378 0.01683  -0.00364 -0.08113 59  PHE A CB  
429  C  CG  . PHE A 59  ? 0.29032 0.26481 0.23062 0.01546  -0.00567 -0.08274 59  PHE A CG  
430  C  CD1 . PHE A 59  ? 0.27337 0.25441 0.20913 0.01515  -0.00466 -0.07771 59  PHE A CD1 
431  C  CD2 . PHE A 59  ? 0.31178 0.28313 0.24781 0.01453  -0.00884 -0.08932 59  PHE A CD2 
432  C  CE1 . PHE A 59  ? 0.28268 0.26712 0.20950 0.01416  -0.00689 -0.07874 59  PHE A CE1 
433  C  CE2 . PHE A 59  ? 0.31735 0.29272 0.24434 0.01346  -0.01113 -0.09076 59  PHE A CE2 
434  C  CZ  . PHE A 59  ? 0.30827 0.29019 0.23060 0.01339  -0.01019 -0.08520 59  PHE A CZ  
435  N  N   . GLN A 60  ? 0.28447 0.26591 0.22019 0.02423  0.00716  -0.08489 60  GLN A N   
436  C  CA  . GLN A 60  ? 0.26292 0.25171 0.19393 0.02528  0.01135  -0.08160 60  GLN A CA  
437  C  C   . GLN A 60  ? 0.28513 0.27769 0.21083 0.02238  0.00926  -0.07640 60  GLN A C   
438  O  O   . GLN A 60  ? 0.30103 0.29320 0.21970 0.02095  0.00608  -0.07867 60  GLN A O   
439  C  CB  . GLN A 60  ? 0.27431 0.26529 0.19735 0.02796  0.01473  -0.08780 60  GLN A CB  
440  C  CG  . GLN A 60  ? 0.29979 0.29862 0.21782 0.02874  0.01960  -0.08444 60  GLN A CG  
441  C  CD  . GLN A 60  ? 0.35873 0.36027 0.26854 0.03135  0.02338  -0.09083 60  GLN A CD  
442  O  OE1 . GLN A 60  ? 0.44019 0.43996 0.34152 0.03105  0.02128  -0.09595 60  GLN A OE1 
443  N  NE2 . GLN A 60  ? 0.39695 0.40314 0.30946 0.03394  0.02895  -0.09090 60  GLN A NE2 
444  N  N   . HIS A 61  ? 0.25879 0.25489 0.18802 0.02161  0.01078  -0.06956 61  HIS A N   
445  C  CA  . HIS A 61  ? 0.27886 0.27752 0.20470 0.01909  0.00850  -0.06425 61  HIS A CA  
446  C  C   . HIS A 61  ? 0.28014 0.28291 0.20878 0.01888  0.01156  -0.05777 61  HIS A C   
447  O  O   . HIS A 61  ? 0.28396 0.28624 0.22115 0.01934  0.01285  -0.05566 61  HIS A O   
448  C  CB  . HIS A 61  ? 0.26731 0.26224 0.19842 0.01674  0.00344  -0.06320 61  HIS A CB  
449  C  CG  . HIS A 61  ? 0.25973 0.25727 0.18904 0.01463  0.00094  -0.05795 61  HIS A CG  
450  N  ND1 . HIS A 61  ? 0.25893 0.25619 0.19562 0.01313  -0.00044 -0.05319 61  HIS A ND1 
451  C  CD2 . HIS A 61  ? 0.27117 0.27154 0.19205 0.01402  -0.00054 -0.05679 61  HIS A CD2 
452  C  CE1 . HIS A 61  ? 0.25050 0.25025 0.18396 0.01188  -0.00255 -0.04966 61  HIS A CE1 
453  N  NE2 . HIS A 61  ? 0.25574 0.25722 0.17974 0.01242  -0.00286 -0.05151 61  HIS A NE2 
454  N  N   . ASP A 62  ? 0.26796 0.27458 0.18935 0.01807  0.01248  -0.05450 62  ASP A N   
455  C  CA  . ASP A 62  ? 0.27926 0.28897 0.20289 0.01708  0.01439  -0.04793 62  ASP A CA  
456  C  C   . ASP A 62  ? 0.25530 0.26327 0.18149 0.01501  0.01005  -0.04392 62  ASP A C   
457  O  O   . ASP A 62  ? 0.27546 0.28284 0.19613 0.01417  0.00660  -0.04431 62  ASP A O   
458  C  CB  . ASP A 62  ? 0.28315 0.29705 0.19742 0.01704  0.01746  -0.04621 62  ASP A CB  
459  C  CG  . ASP A 62  ? 0.32846 0.34524 0.24511 0.01582  0.01997  -0.03979 62  ASP A CG  
460  O  OD1 . ASP A 62  ? 0.29953 0.31481 0.22124 0.01441  0.01758  -0.03566 62  ASP A OD1 
461  O  OD2 . ASP A 62  ? 0.37347 0.39426 0.28672 0.01616  0.02458  -0.03909 62  ASP A OD2 
462  N  N   . SER A 63  ? 0.25396 0.26148 0.18859 0.01433  0.01007  -0.04036 63  SER A N   
463  C  CA  . SER A 63  ? 0.24193 0.24794 0.17984 0.01264  0.00617  -0.03742 63  SER A CA  
464  C  C   . SER A 63  ? 0.27490 0.28260 0.20708 0.01169  0.00494  -0.03336 63  SER A C   
465  O  O   . SER A 63  ? 0.28784 0.29471 0.22146 0.01072  0.00129  -0.03178 63  SER A O   
466  C  CB  . SER A 63  ? 0.26289 0.26831 0.21013 0.01221  0.00675  -0.03465 63  SER A CB  
467  O  OG  . SER A 63  ? 0.27679 0.28496 0.22453 0.01202  0.00960  -0.03059 63  SER A OG  
468  N  N   . SER A 64  ? 0.27462 0.28468 0.20047 0.01198  0.00786  -0.03158 64  SER A N   
469  C  CA  . SER A 64  ? 0.29582 0.30659 0.21517 0.01121  0.00644  -0.02757 64  SER A CA  
470  C  C   . SER A 64  ? 0.30959 0.32018 0.22039 0.01154  0.00321  -0.03008 64  SER A C   
471  O  O   . SER A 64  ? 0.30667 0.31752 0.21197 0.01118  0.00105  -0.02671 64  SER A O   
472  C  CB  . SER A 64  ? 0.28542 0.29857 0.20091 0.01091  0.01091  -0.02412 64  SER A CB  
473  O  OG  . SER A 64  ? 0.30217 0.31750 0.21154 0.01189  0.01414  -0.02751 64  SER A OG  
474  N  N   . ASP A 65  ? 0.28866 0.29859 0.19823 0.01227  0.00258  -0.03592 65  ASP A N   
475  C  CA  . ASP A 65  ? 0.29793 0.30802 0.19880 0.01255  -0.00039 -0.03935 65  ASP A CA  
476  C  C   . ASP A 65  ? 0.28670 0.29533 0.19169 0.01167  -0.00608 -0.04033 65  ASP A C   
477  O  O   . ASP A 65  ? 0.27621 0.28289 0.18740 0.01133  -0.00738 -0.04419 65  ASP A O   
478  C  CB  . ASP A 65  ? 0.30486 0.31480 0.20274 0.01377  0.00209  -0.04567 65  ASP A CB  
479  C  CG  . ASP A 65  ? 0.32752 0.33702 0.21754 0.01394  -0.00147 -0.05081 65  ASP A CG  
480  O  OD1 . ASP A 65  ? 0.31953 0.32965 0.20508 0.01318  -0.00584 -0.04920 65  ASP A OD1 
481  O  OD2 . ASP A 65  ? 0.35878 0.36729 0.24731 0.01499  0.00001  -0.05690 65  ASP A OD2 
482  N  N   . GLU A 66  ? 0.28523 0.29492 0.18696 0.01130  -0.00951 -0.03671 66  GLU A N   
483  C  CA  . GLU A 66  ? 0.27568 0.28526 0.18248 0.01052  -0.01477 -0.03703 66  GLU A CA  
484  C  C   . GLU A 66  ? 0.28254 0.29185 0.18743 0.01010  -0.01825 -0.04330 66  GLU A C   
485  O  O   . GLU A 66  ? 0.28627 0.29463 0.19903 0.00896  -0.02059 -0.04572 66  GLU A O   
486  C  CB  . GLU A 66  ? 0.27115 0.28220 0.17425 0.01083  -0.01774 -0.03201 66  GLU A CB  
487  C  CG  . GLU A 66  ? 0.26726 0.27933 0.17686 0.01035  -0.02287 -0.03185 66  GLU A CG  
488  C  CD  . GLU A 66  ? 0.28426 0.29770 0.19029 0.01129  -0.02615 -0.02722 66  GLU A CD  
489  O  OE1 . GLU A 66  ? 0.32062 0.33359 0.21826 0.01209  -0.02472 -0.02379 66  GLU A OE1 
490  O  OE2 . GLU A 66  ? 0.30931 0.32440 0.22112 0.01127  -0.03025 -0.02692 66  GLU A OE2 
491  N  N   . ASP A 67  ? 0.29021 0.30040 0.18448 0.01077  -0.01877 -0.04601 67  ASP A N   
492  C  CA  . ASP A 67  ? 0.31705 0.32677 0.20927 0.01021  -0.02237 -0.05253 67  ASP A CA  
493  C  C   . ASP A 67  ? 0.29795 0.30440 0.19611 0.00995  -0.02001 -0.05774 67  ASP A C   
494  O  O   . ASP A 67  ? 0.30965 0.31445 0.21208 0.00867  -0.02334 -0.06218 67  ASP A O   
495  C  CB  . ASP A 67  ? 0.40549 0.41688 0.28399 0.01110  -0.02316 -0.05471 67  ASP A CB  
496  C  CG  . ASP A 67  ? 0.53795 0.54902 0.41366 0.01036  -0.02771 -0.06179 67  ASP A CG  
497  O  OD1 . ASP A 67  ? 0.57914 0.59033 0.46214 0.00887  -0.03240 -0.06290 67  ASP A OD1 
498  O  OD2 . ASP A 67  ? 0.59875 0.60973 0.46503 0.01113  -0.02652 -0.06648 67  ASP A OD2 
499  N  N   . GLY A 68  ? 0.28973 0.29514 0.18880 0.01111  -0.01446 -0.05716 68  GLY A N   
500  C  CA  . GLY A 68  ? 0.29574 0.29771 0.20079 0.01139  -0.01234 -0.06173 68  GLY A CA  
501  C  C   . GLY A 68  ? 0.28582 0.28540 0.20282 0.00988  -0.01394 -0.06055 68  GLY A C   
502  O  O   . GLY A 68  ? 0.29571 0.29153 0.21762 0.00946  -0.01434 -0.06487 68  GLY A O   
503  N  N   . TRP A 69  ? 0.25915 0.26060 0.18078 0.00902  -0.01485 -0.05477 69  TRP A N   
504  C  CA  . TRP A 69  ? 0.23571 0.23566 0.16806 0.00742  -0.01619 -0.05338 69  TRP A CA  
505  C  C   . TRP A 69  ? 0.25924 0.25815 0.19412 0.00545  -0.02091 -0.05748 69  TRP A C   
506  O  O   . TRP A 69  ? 0.26407 0.25992 0.20653 0.00403  -0.02131 -0.05912 69  TRP A O   
507  C  CB  . TRP A 69  ? 0.24473 0.24747 0.18035 0.00708  -0.01648 -0.04707 69  TRP A CB  
508  C  CG  . TRP A 69  ? 0.23834 0.24080 0.17746 0.00786  -0.01218 -0.04314 69  TRP A CG  
509  C  CD1 . TRP A 69  ? 0.25930 0.26342 0.19414 0.00901  -0.00923 -0.03961 69  TRP A CD1 
510  C  CD2 . TRP A 69  ? 0.21932 0.21986 0.16714 0.00728  -0.01062 -0.04220 69  TRP A CD2 
511  N  NE1 . TRP A 69  ? 0.24909 0.25270 0.19001 0.00914  -0.00607 -0.03696 69  TRP A NE1 
512  C  CE2 . TRP A 69  ? 0.23543 0.23690 0.18393 0.00825  -0.00700 -0.03846 69  TRP A CE2 
513  C  CE3 . TRP A 69  ? 0.24045 0.23846 0.19539 0.00581  -0.01205 -0.04401 69  TRP A CE3 
514  C  CZ2 . TRP A 69  ? 0.24287 0.24319 0.19863 0.00807  -0.00508 -0.03666 69  TRP A CZ2 
515  C  CZ3 . TRP A 69  ? 0.22728 0.22378 0.18892 0.00564  -0.00992 -0.04177 69  TRP A CZ3 
516  C  CH2 . TRP A 69  ? 0.24164 0.23943 0.20345 0.00691  -0.00661 -0.03830 69  TRP A CH2 
517  N  N   . THR A 70  ? 0.27281 0.27436 0.20153 0.00516  -0.02473 -0.05892 70  THR A N   
518  C  CA  . THR A 70  ? 0.25933 0.26054 0.19035 0.00304  -0.02955 -0.06336 70  THR A CA  
519  C  C   . THR A 70  ? 0.29475 0.29105 0.22509 0.00279  -0.02894 -0.06998 70  THR A C   
520  O  O   . THR A 70  ? 0.29987 0.29318 0.23737 0.00059  -0.03080 -0.07268 70  THR A O   
521  C  CB  . THR A 70  ? 0.29997 0.30538 0.22338 0.00322  -0.03392 -0.06377 70  THR A CB  
522  O  OG1 . THR A 70  ? 0.32905 0.33817 0.25322 0.00401  -0.03422 -0.05738 70  THR A OG1 
523  C  CG2 . THR A 70  ? 0.32034 0.32659 0.24739 0.00070  -0.03950 -0.06811 70  THR A CG2 
524  N  N   . LYS A 71  ? 0.28456 0.27983 0.20639 0.00503  -0.02615 -0.07270 71  LYS A N   
525  C  CA  . LYS A 71  ? 0.29990 0.29027 0.22070 0.00545  -0.02525 -0.07953 71  LYS A CA  
526  C  C   . LYS A 71  ? 0.28471 0.27026 0.21516 0.00545  -0.02235 -0.07891 71  LYS A C   
527  O  O   . LYS A 71  ? 0.29388 0.27416 0.22819 0.00453  -0.02347 -0.08373 71  LYS A O   
528  C  CB  . LYS A 71  ? 0.35387 0.34520 0.26371 0.00823  -0.02203 -0.08213 71  LYS A CB  
529  C  CG  . LYS A 71  ? 0.42536 0.42078 0.32396 0.00820  -0.02526 -0.08344 71  LYS A CG  
530  C  CD  . LYS A 71  ? 0.48817 0.48618 0.37578 0.01077  -0.02102 -0.08291 71  LYS A CD  
531  C  CE  . LYS A 71  ? 0.53946 0.53865 0.41489 0.01116  -0.02337 -0.08871 71  LYS A CE  
532  N  NZ  . LYS A 71  ? 0.56935 0.57100 0.44282 0.00919  -0.03010 -0.08828 71  LYS A NZ  
533  N  N   . LEU A 72  ? 0.26698 0.25402 0.20144 0.00638  -0.01896 -0.07290 72  LEU A N   
534  C  CA  . LEU A 72  ? 0.27188 0.25489 0.21522 0.00650  -0.01655 -0.07151 72  LEU A CA  
535  C  C   . LEU A 72  ? 0.27212 0.25263 0.22422 0.00327  -0.01982 -0.07095 72  LEU A C   
536  O  O   . LEU A 72  ? 0.28539 0.26011 0.24265 0.00260  -0.01991 -0.07364 72  LEU A O   
537  C  CB  . LEU A 72  ? 0.23624 0.22236 0.18136 0.00786  -0.01285 -0.06513 72  LEU A CB  
538  C  CG  . LEU A 72  ? 0.23488 0.21845 0.18940 0.00754  -0.01122 -0.06179 72  LEU A CG  
539  C  CD1 . LEU A 72  ? 0.24916 0.22744 0.20608 0.00931  -0.00923 -0.06568 72  LEU A CD1 
540  C  CD2 . LEU A 72  ? 0.24487 0.23244 0.20005 0.00853  -0.00832 -0.05580 72  LEU A CD2 
541  N  N   . PHE A 73  ? 0.28745 0.27224 0.24153 0.00123  -0.02249 -0.06746 73  PHE A N   
542  C  CA  . PHE A 73  ? 0.25624 0.23981 0.21870 -0.00217 -0.02537 -0.06710 73  PHE A CA  
543  C  C   . PHE A 73  ? 0.27808 0.25814 0.24024 -0.00420 -0.02899 -0.07370 73  PHE A C   
544  O  O   . PHE A 73  ? 0.28971 0.26509 0.25891 -0.00663 -0.02993 -0.07500 73  PHE A O   
545  C  CB  . PHE A 73  ? 0.25184 0.24173 0.21660 -0.00354 -0.02740 -0.06262 73  PHE A CB  
546  C  CG  . PHE A 73  ? 0.23155 0.22276 0.20205 -0.00345 -0.02469 -0.05660 73  PHE A CG  
547  C  CD1 . PHE A 73  ? 0.22139 0.21438 0.18840 -0.00083 -0.02148 -0.05300 73  PHE A CD1 
548  C  CD2 . PHE A 73  ? 0.23132 0.22213 0.21050 -0.00621 -0.02532 -0.05464 73  PHE A CD2 
549  C  CE1 . PHE A 73  ? 0.24197 0.23620 0.21387 -0.00078 -0.01921 -0.04786 73  PHE A CE1 
550  C  CE2 . PHE A 73  ? 0.22623 0.21859 0.20983 -0.00605 -0.02276 -0.04925 73  PHE A CE2 
551  C  CZ  . PHE A 73  ? 0.24038 0.23430 0.22019 -0.00324 -0.01987 -0.04613 73  PHE A CZ  
552  N  N   . ASP A 74  ? 0.27769 0.25974 0.23153 -0.00344 -0.03118 -0.07788 74  ASP A N   
553  C  CA  . ASP A 74  ? 0.30057 0.27929 0.25324 -0.00531 -0.03485 -0.08493 74  ASP A CA  
554  C  C   . ASP A 74  ? 0.29861 0.26899 0.25317 -0.00455 -0.03272 -0.08922 74  ASP A C   
555  O  O   . ASP A 74  ? 0.30822 0.27340 0.26836 -0.00731 -0.03504 -0.09261 74  ASP A O   
556  C  CB  . ASP A 74  ? 0.30344 0.28558 0.24488 -0.00387 -0.03691 -0.08877 74  ASP A CB  
557  C  CG  . ASP A 74  ? 0.35406 0.34355 0.29404 -0.00507 -0.04093 -0.08601 74  ASP A CG  
558  O  OD1 . ASP A 74  ? 0.35171 0.34379 0.30022 -0.00748 -0.04279 -0.08260 74  ASP A OD1 
559  O  OD2 . ASP A 74  ? 0.37923 0.37210 0.30915 -0.00341 -0.04224 -0.08735 74  ASP A OD2 
560  N  N   . ALA A 75  ? 0.29247 0.26149 0.24265 -0.00078 -0.02836 -0.08929 75  ALA A N   
561  C  CA  . ALA A 75  ? 0.29913 0.26045 0.25111 0.00075  -0.02634 -0.09373 75  ALA A CA  
562  C  C   . ALA A 75  ? 0.29406 0.25033 0.25676 -0.00075 -0.02557 -0.09013 75  ALA A C   
563  O  O   . ALA A 75  ? 0.32753 0.27601 0.29434 -0.00148 -0.02634 -0.09395 75  ALA A O   
564  C  CB  . ALA A 75  ? 0.30007 0.26261 0.24593 0.00531  -0.02153 -0.09412 75  ALA A CB  
565  N  N   . THR A 76  ? 0.28346 0.24369 0.25045 -0.00120 -0.02407 -0.08278 76  THR A N   
566  C  CA  . THR A 76  ? 0.26330 0.21916 0.23951 -0.00274 -0.02336 -0.07898 76  THR A CA  
567  C  C   . THR A 76  ? 0.29438 0.24750 0.27654 -0.00757 -0.02729 -0.08018 76  THR A C   
568  O  O   . THR A 76  ? 0.29248 0.23809 0.28046 -0.00900 -0.02757 -0.08096 76  THR A O   
569  C  CB  . THR A 76  ? 0.25261 0.21381 0.23121 -0.00217 -0.02092 -0.07130 76  THR A CB  
570  O  OG1 . THR A 76  ? 0.25381 0.21768 0.22716 0.00187  -0.01739 -0.07054 76  THR A OG1 
571  C  CG2 . THR A 76  ? 0.26858 0.22527 0.25548 -0.00335 -0.01987 -0.06723 76  THR A CG2 
572  N  N   . GLU A 77  ? 0.28881 0.24793 0.26988 -0.01013 -0.03046 -0.08031 77  GLU A N   
573  C  CA  . GLU A 77  ? 0.31171 0.26949 0.29884 -0.01502 -0.03434 -0.08195 77  GLU A CA  
574  C  C   . GLU A 77  ? 0.31775 0.26731 0.30441 -0.01603 -0.03647 -0.08941 77  GLU A C   
575  O  O   . GLU A 77  ? 0.34827 0.29191 0.34209 -0.01959 -0.03793 -0.09007 77  GLU A O   
576  C  CB  . GLU A 77  ? 0.33516 0.30155 0.32046 -0.01680 -0.03776 -0.08200 77  GLU A CB  
577  C  CG  . GLU A 77  ? 0.35076 0.32455 0.33890 -0.01682 -0.03654 -0.07509 77  GLU A CG  
578  C  CD  . GLU A 77  ? 0.39126 0.37348 0.37734 -0.01763 -0.04008 -0.07529 77  GLU A CD  
579  O  OE1 . GLU A 77  ? 0.39063 0.37890 0.37591 -0.01594 -0.03880 -0.07036 77  GLU A OE1 
580  O  OE2 . GLU A 77  ? 0.41882 0.40144 0.40419 -0.01983 -0.04434 -0.08046 77  GLU A OE2 
581  N  N   . LYS A 78  ? 0.32131 0.27032 0.29936 -0.01308 -0.03663 -0.09520 78  LYS A N   
582  C  CA  . LYS A 78  ? 0.35675 0.29802 0.33331 -0.01364 -0.03872 -0.10333 78  LYS A CA  
583  C  C   . LYS A 78  ? 0.34527 0.27634 0.32688 -0.01243 -0.03631 -0.10379 78  LYS A C   
584  O  O   . LYS A 78  ? 0.35763 0.28045 0.34318 -0.01489 -0.03861 -0.10831 78  LYS A O   
585  C  CB  . LYS A 78  ? 0.40932 0.35299 0.37455 -0.01009 -0.03854 -0.10898 78  LYS A CB  
586  C  CG  . LYS A 78  ? 0.49076 0.44336 0.45079 -0.01155 -0.04198 -0.10898 78  LYS A CG  
587  C  CD  . LYS A 78  ? 0.57427 0.52614 0.52539 -0.01102 -0.04479 -0.11744 78  LYS A CD  
588  C  CE  . LYS A 78  ? 0.61226 0.57253 0.55258 -0.00829 -0.04442 -0.11629 78  LYS A CE  
589  N  NZ  . LYS A 78  ? 0.61243 0.58104 0.55553 -0.00987 -0.04605 -0.10921 78  LYS A NZ  
590  N  N   . ALA A 79  ? 0.31818 0.24948 0.29999 -0.00863 -0.03191 -0.09917 79  ALA A N   
591  C  CA  . ALA A 79  ? 0.34079 0.26279 0.32724 -0.00669 -0.02979 -0.09936 79  ALA A CA  
592  C  C   . ALA A 79  ? 0.34332 0.26110 0.33942 -0.01051 -0.03051 -0.09376 79  ALA A C   
593  O  O   . ALA A 79  ? 0.36048 0.26820 0.36150 -0.01145 -0.03130 -0.09565 79  ALA A O   
594  C  CB  . ALA A 79  ? 0.32737 0.25205 0.31104 -0.00125 -0.02509 -0.09644 79  ALA A CB  
595  N  N   . PHE A 80  ? 0.31894 0.24405 0.31764 -0.01261 -0.03009 -0.08675 80  PHE A N   
596  C  CA  . PHE A 80  ? 0.31223 0.23476 0.31873 -0.01506 -0.02928 -0.08007 80  PHE A CA  
597  C  C   . PHE A 80  ? 0.30186 0.22931 0.31320 -0.02069 -0.03148 -0.07677 80  PHE A C   
598  O  O   . PHE A 80  ? 0.33534 0.26055 0.35308 -0.02342 -0.03081 -0.07142 80  PHE A O   
599  C  CB  . PHE A 80  ? 0.29151 0.21828 0.29735 -0.01145 -0.02543 -0.07364 80  PHE A CB  
600  C  CG  . PHE A 80  ? 0.30220 0.22518 0.30514 -0.00588 -0.02278 -0.07575 80  PHE A CG  
601  C  CD1 . PHE A 80  ? 0.32688 0.23929 0.33252 -0.00457 -0.02311 -0.07934 80  PHE A CD1 
602  C  CD2 . PHE A 80  ? 0.30004 0.23013 0.29820 -0.00195 -0.01988 -0.07396 80  PHE A CD2 
603  C  CE1 . PHE A 80  ? 0.31021 0.22000 0.31409 0.00105  -0.02049 -0.08137 80  PHE A CE1 
604  C  CE2 . PHE A 80  ? 0.28509 0.21294 0.28151 0.00315  -0.01712 -0.07579 80  PHE A CE2 
605  C  CZ  . PHE A 80  ? 0.29367 0.21178 0.29310 0.00482  -0.01741 -0.07959 80  PHE A CZ  
606  N  N   . GLY A 81  ? 0.30414 0.23905 0.31256 -0.02222 -0.03385 -0.07926 81  GLY A N   
607  C  CA  . GLY A 81  ? 0.30223 0.24395 0.31557 -0.02684 -0.03569 -0.07607 81  GLY A CA  
608  C  C   . GLY A 81  ? 0.28291 0.23470 0.29427 -0.02491 -0.03371 -0.07060 81  GLY A C   
609  O  O   . GLY A 81  ? 0.28520 0.23864 0.29116 -0.02034 -0.03102 -0.06917 81  GLY A O   
610  N  N   . PRO A 82  ? 0.25211 0.21085 0.26836 -0.02844 -0.03489 -0.06746 82  PRO A N   
611  C  CA  . PRO A 82  ? 0.24103 0.20929 0.25567 -0.02657 -0.03342 -0.06289 82  PRO A CA  
612  C  C   . PRO A 82  ? 0.26010 0.22749 0.27352 -0.02334 -0.02918 -0.05758 82  PRO A C   
613  O  O   . PRO A 82  ? 0.26430 0.22675 0.28196 -0.02446 -0.02735 -0.05433 82  PRO A O   
614  C  CB  . PRO A 82  ? 0.25551 0.22967 0.27802 -0.03134 -0.03488 -0.06035 82  PRO A CB  
615  C  CG  . PRO A 82  ? 0.28399 0.25428 0.30988 -0.03552 -0.03866 -0.06576 82  PRO A CG  
616  C  CD  . PRO A 82  ? 0.29448 0.25313 0.31824 -0.03433 -0.03778 -0.06852 82  PRO A CD  
617  N  N   . VAL A 83  ? 0.23909 0.21155 0.24665 -0.01950 -0.02785 -0.05648 83  VAL A N   
618  C  CA  . VAL A 83  ? 0.24546 0.21812 0.25153 -0.01637 -0.02412 -0.05188 83  VAL A CA  
619  C  C   . VAL A 83  ? 0.23769 0.21513 0.24896 -0.01836 -0.02290 -0.04617 83  VAL A C   
620  O  O   . VAL A 83  ? 0.25742 0.24187 0.27033 -0.01977 -0.02423 -0.04537 83  VAL A O   
621  C  CB  . VAL A 83  ? 0.23840 0.21506 0.23687 -0.01230 -0.02317 -0.05254 83  VAL A CB  
622  C  CG1 . VAL A 83  ? 0.23442 0.21160 0.23188 -0.00939 -0.01947 -0.04806 83  VAL A CG1 
623  C  CG2 . VAL A 83  ? 0.25612 0.22866 0.24897 -0.01056 -0.02417 -0.05863 83  VAL A CG2 
624  N  N   . SER A 84  ? 0.21155 0.18552 0.22527 -0.01819 -0.02039 -0.04226 84  SER A N   
625  C  CA  . SER A 84  ? 0.20885 0.18723 0.22631 -0.01968 -0.01871 -0.03684 84  SER A CA  
626  C  C   . SER A 84  ? 0.21258 0.19352 0.22673 -0.01616 -0.01599 -0.03337 84  SER A C   
627  O  O   . SER A 84  ? 0.20604 0.19192 0.22201 -0.01685 -0.01472 -0.02960 84  SER A O   
628  C  CB  . SER A 84  ? 0.21048 0.18326 0.23316 -0.02283 -0.01809 -0.03428 84  SER A CB  
629  O  OG  . SER A 84  ? 0.25018 0.21616 0.27089 -0.02005 -0.01661 -0.03339 84  SER A OG  
630  N  N   . THR A 85  ? 0.20333 0.18117 0.21300 -0.01254 -0.01496 -0.03472 85  THR A N   
631  C  CA  . THR A 85  ? 0.20002 0.17916 0.20786 -0.00974 -0.01236 -0.03124 85  THR A CA  
632  C  C   . THR A 85  ? 0.20541 0.18580 0.20755 -0.00611 -0.01166 -0.03354 85  THR A C   
633  O  O   . THR A 85  ? 0.23407 0.21088 0.23383 -0.00493 -0.01230 -0.03765 85  THR A O   
634  C  CB  . THR A 85  ? 0.21194 0.18480 0.22225 -0.00943 -0.01125 -0.02917 85  THR A CB  
635  O  OG1 . THR A 85  ? 0.22354 0.19417 0.23867 -0.01333 -0.01202 -0.02721 85  THR A OG1 
636  C  CG2 . THR A 85  ? 0.20213 0.17724 0.21153 -0.00719 -0.00904 -0.02518 85  THR A CG2 
637  N  N   . LEU A 86  ? 0.20126 0.18671 0.20112 -0.00454 -0.01029 -0.03107 86  LEU A N   
638  C  CA  . LEU A 86  ? 0.19444 0.18140 0.18896 -0.00154 -0.00921 -0.03243 86  LEU A CA  
639  C  C   . LEU A 86  ? 0.19503 0.18363 0.18962 0.00020  -0.00673 -0.02885 86  LEU A C   
640  O  O   . LEU A 86  ? 0.20865 0.20048 0.20485 -0.00069 -0.00637 -0.02556 86  LEU A O   
641  C  CB  . LEU A 86  ? 0.19902 0.19062 0.18993 -0.00159 -0.01063 -0.03333 86  LEU A CB  
642  C  CG  . LEU A 86  ? 0.22697 0.22056 0.21191 0.00109  -0.00920 -0.03347 86  LEU A CG  
643  C  CD1 . LEU A 86  ? 0.23614 0.22655 0.21732 0.00284  -0.00847 -0.03739 86  LEU A CD1 
644  C  CD2 . LEU A 86  ? 0.19579 0.19357 0.17737 0.00101  -0.01093 -0.03321 86  LEU A CD2 
645  N  N   . VAL A 87  ? 0.19719 0.18393 0.19037 0.00268  -0.00504 -0.02976 87  VAL A N   
646  C  CA  . VAL A 87  ? 0.19965 0.18875 0.19291 0.00436  -0.00286 -0.02686 87  VAL A CA  
647  C  C   . VAL A 87  ? 0.21929 0.21128 0.20761 0.00614  -0.00154 -0.02815 87  VAL A C   
648  O  O   . VAL A 87  ? 0.22963 0.22019 0.21558 0.00781  -0.00074 -0.03135 87  VAL A O   
649  C  CB  . VAL A 87  ? 0.19433 0.18004 0.19091 0.00584  -0.00190 -0.02634 87  VAL A CB  
650  C  CG1 . VAL A 87  ? 0.21159 0.20067 0.20900 0.00718  -0.00014 -0.02323 87  VAL A CG1 
651  C  CG2 . VAL A 87  ? 0.20868 0.19044 0.20944 0.00378  -0.00337 -0.02482 87  VAL A CG2 
652  N  N   . ASN A 88  ? 0.19985 0.19572 0.18637 0.00573  -0.00124 -0.02575 88  ASN A N   
653  C  CA  . ASN A 88  ? 0.20053 0.19895 0.18211 0.00698  0.00009  -0.02601 88  ASN A CA  
654  C  C   . ASN A 88  ? 0.20271 0.20262 0.18584 0.00827  0.00270  -0.02418 88  ASN A C   
655  O  O   . ASN A 88  ? 0.21485 0.21697 0.19914 0.00771  0.00322  -0.02112 88  ASN A O   
656  C  CB  . ASN A 88  ? 0.19847 0.19954 0.17786 0.00602  -0.00105 -0.02403 88  ASN A CB  
657  C  CG  . ASN A 88  ? 0.21999 0.22099 0.19626 0.00545  -0.00353 -0.02627 88  ASN A CG  
658  O  OD1 . ASN A 88  ? 0.23062 0.23096 0.20238 0.00629  -0.00356 -0.02905 88  ASN A OD1 
659  N  ND2 . ASN A 88  ? 0.21757 0.21982 0.19626 0.00406  -0.00567 -0.02528 88  ASN A ND2 
660  N  N   . ASN A 89  ? 0.20987 0.20881 0.19340 0.01007  0.00428  -0.02636 89  ASN A N   
661  C  CA  . ASN A 89  ? 0.19133 0.19217 0.17797 0.01144  0.00649  -0.02495 89  ASN A CA  
662  C  C   . ASN A 89  ? 0.20248 0.20669 0.18594 0.01267  0.00929  -0.02571 89  ASN A C   
663  O  O   . ASN A 89  ? 0.24014 0.24756 0.22597 0.01293  0.01106  -0.02361 89  ASN A O   
664  C  CB  . ASN A 89  ? 0.21769 0.21533 0.20877 0.01293  0.00629  -0.02647 89  ASN A CB  
665  C  CG  . ASN A 89  ? 0.21706 0.21725 0.21181 0.01505  0.00842  -0.02576 89  ASN A CG  
666  O  OD1 . ASN A 89  ? 0.23322 0.23540 0.23133 0.01460  0.00827  -0.02254 89  ASN A OD1 
667  N  ND2 . ASN A 89  ? 0.23124 0.23167 0.22564 0.01748  0.01029  -0.02909 89  ASN A ND2 
668  N  N   . ALA A 90  ? 0.20376 0.20770 0.18174 0.01316  0.00971  -0.02855 90  ALA A N   
669  C  CA  . ALA A 90  ? 0.23429 0.24173 0.20859 0.01418  0.01284  -0.02920 90  ALA A CA  
670  C  C   . ALA A 90  ? 0.23200 0.24258 0.20491 0.01261  0.01375  -0.02511 90  ALA A C   
671  O  O   . ALA A 90  ? 0.24459 0.25419 0.21547 0.01102  0.01166  -0.02305 90  ALA A O   
672  C  CB  . ALA A 90  ? 0.24244 0.24894 0.20965 0.01468  0.01272  -0.03281 90  ALA A CB  
673  N  N   . GLY A 91  ? 0.24210 0.25649 0.21654 0.01305  0.01687  -0.02403 91  GLY A N   
674  C  CA  . GLY A 91  ? 0.24912 0.26593 0.22287 0.01124  0.01782  -0.02019 91  GLY A CA  
675  C  C   . GLY A 91  ? 0.27111 0.29269 0.24603 0.01166  0.02178  -0.01995 91  GLY A C   
676  O  O   . GLY A 91  ? 0.30924 0.33277 0.28790 0.01364  0.02351  -0.02241 91  GLY A O   
677  N  N   . ILE A 92  ? 0.23674 0.26023 0.20886 0.00978  0.02326  -0.01691 92  ILE A N   
678  C  CA  . ILE A 92  ? 0.23088 0.25962 0.20469 0.00940  0.02730  -0.01606 92  ILE A CA  
679  C  C   . ILE A 92  ? 0.23079 0.26064 0.20790 0.00679  0.02727  -0.01197 92  ILE A C   
680  O  O   . ILE A 92  ? 0.23367 0.25993 0.20994 0.00544  0.02447  -0.00988 92  ILE A O   
681  C  CB  . ILE A 92  ? 0.28026 0.31076 0.24620 0.00937  0.03027  -0.01667 92  ILE A CB  
682  C  CG1 . ILE A 92  ? 0.29536 0.32279 0.25415 0.00731  0.02872  -0.01338 92  ILE A CG1 
683  C  CG2 . ILE A 92  ? 0.30519 0.33466 0.26799 0.01201  0.03029  -0.02150 92  ILE A CG2 
684  C  CD1 . ILE A 92  ? 0.30621 0.33538 0.25606 0.00702  0.03154  -0.01317 92  ILE A CD1 
685  N  N   . ALA A 93  ? 0.25300 0.28817 0.23442 0.00608  0.03047  -0.01114 93  ALA A N   
686  C  CA  . ALA A 93  ? 0.26829 0.30477 0.25333 0.00324  0.03058  -0.00766 93  ALA A CA  
687  C  C   . ALA A 93  ? 0.28847 0.32934 0.27186 0.00132  0.03487  -0.00584 93  ALA A C   
688  O  O   . ALA A 93  ? 0.32760 0.37292 0.31044 0.00264  0.03833  -0.00781 93  ALA A O   
689  C  CB  . ALA A 93  ? 0.28628 0.32553 0.28056 0.00360  0.02949  -0.00805 93  ALA A CB  
690  N  N   . VAL A 94  ? 0.23441 0.27363 0.21670 -0.00186 0.03469  -0.00210 94  VAL A N   
691  C  CA  . VAL A 94  ? 0.26272 0.30572 0.24469 -0.00471 0.03858  0.00063  94  VAL A CA  
692  C  C   . VAL A 94  ? 0.24611 0.29149 0.23673 -0.00724 0.03814  0.00223  94  VAL A C   
693  O  O   . VAL A 94  ? 0.26131 0.30229 0.25361 -0.00801 0.03449  0.00306  94  VAL A O   
694  C  CB  . VAL A 94  ? 0.29341 0.33141 0.26621 -0.00653 0.03847  0.00400  94  VAL A CB  
695  C  CG1 . VAL A 94  ? 0.31812 0.35857 0.29106 -0.01034 0.04196  0.00790  94  VAL A CG1 
696  C  CG2 . VAL A 94  ? 0.30996 0.34710 0.27404 -0.00412 0.03911  0.00207  94  VAL A CG2 
697  N  N   . ASN A 95  ? 0.28521 0.33803 0.28163 -0.00843 0.04177  0.00227  95  ASN A N   
698  C  CA  . ASN A 95  ? 0.28731 0.34342 0.29247 -0.01114 0.04130  0.00353  95  ASN A CA  
699  C  C   . ASN A 95  ? 0.28034 0.33455 0.28320 -0.01579 0.04287  0.00774  95  ASN A C   
700  O  O   . ASN A 95  ? 0.32272 0.38264 0.32803 -0.01838 0.04699  0.00931  95  ASN A O   
701  C  CB  . ASN A 95  ? 0.37914 0.44489 0.39290 -0.01005 0.04411  0.00139  95  ASN A CB  
702  C  CG  . ASN A 95  ? 0.46339 0.53428 0.48631 -0.01358 0.04431  0.00293  95  ASN A CG  
703  O  OD1 . ASN A 95  ? 0.45977 0.52702 0.48496 -0.01529 0.04062  0.00383  95  ASN A OD1 
704  N  ND2 . ASN A 95  ? 0.51103 0.59086 0.53933 -0.01484 0.04877  0.00303  95  ASN A ND2 
705  N  N   . LYS A 96  ? 0.23275 0.27849 0.23031 -0.01668 0.03970  0.00966  96  LYS A N   
706  C  CA  . LYS A 96  ? 0.22337 0.26531 0.21848 -0.02083 0.04047  0.01387  96  LYS A CA  
707  C  C   . LYS A 96  ? 0.19713 0.23145 0.19259 -0.02157 0.03582  0.01451  96  LYS A C   
708  O  O   . LYS A 96  ? 0.21225 0.24213 0.20480 -0.01859 0.03242  0.01274  96  LYS A O   
709  C  CB  . LYS A 96  ? 0.24473 0.28326 0.22952 -0.02090 0.04245  0.01648  96  LYS A CB  
710  C  CG  . LYS A 96  ? 0.25467 0.30043 0.23725 -0.02069 0.04775  0.01622  96  LYS A CG  
711  C  CD  . LYS A 96  ? 0.25245 0.30315 0.23913 -0.02536 0.05200  0.01941  96  LYS A CD  
712  C  CE  . LYS A 96  ? 0.28581 0.34217 0.26690 -0.02558 0.05770  0.02030  96  LYS A CE  
713  N  NZ  . LYS A 96  ? 0.34975 0.39954 0.31840 -0.02626 0.05792  0.02407  96  LYS A NZ  
714  N  N   . SER A 97  ? 0.21525 0.24815 0.21435 -0.02571 0.03591  0.01693  97  SER A N   
715  C  CA  . SER A 97  ? 0.20035 0.22492 0.19849 -0.02683 0.03216  0.01795  97  SER A CA  
716  C  C   . SER A 97  ? 0.21388 0.23071 0.20261 -0.02581 0.03140  0.02058  97  SER A C   
717  O  O   . SER A 97  ? 0.21753 0.23541 0.20044 -0.02571 0.03421  0.02261  97  SER A O   
718  C  CB  . SER A 97  ? 0.19524 0.21957 0.19899 -0.03192 0.03284  0.02007  97  SER A CB  
719  O  OG  . SER A 97  ? 0.20420 0.22828 0.20464 -0.03506 0.03662  0.02425  97  SER A OG  
720  N  N   . VAL A 98  ? 0.20249 0.21180 0.18969 -0.02489 0.02748  0.02043  98  VAL A N   
721  C  CA  . VAL A 98  ? 0.22184 0.22343 0.20120 -0.02409 0.02622  0.02338  98  VAL A CA  
722  C  C   . VAL A 98  ? 0.21070 0.21035 0.18717 -0.02792 0.02919  0.02837  98  VAL A C   
723  O  O   . VAL A 98  ? 0.21724 0.21525 0.18591 -0.02726 0.03045  0.03120  98  VAL A O   
724  C  CB  . VAL A 98  ? 0.20896 0.20316 0.18919 -0.02309 0.02194  0.02252  98  VAL A CB  
725  C  CG1 . VAL A 98  ? 0.21223 0.19839 0.18519 -0.02211 0.02040  0.02596  98  VAL A CG1 
726  C  CG2 . VAL A 98  ? 0.19116 0.18767 0.17314 -0.01937 0.01944  0.01806  98  VAL A CG2 
727  N  N   . GLU A 99  ? 0.22756 0.22756 0.21015 -0.03223 0.03034  0.02960  99  GLU A N   
728  C  CA  . GLU A 99  ? 0.24075 0.23840 0.22151 -0.03670 0.03322  0.03475  99  GLU A CA  
729  C  C   . GLU A 99  ? 0.24313 0.24752 0.21955 -0.03714 0.03804  0.03665  99  GLU A C   
730  O  O   . GLU A 99  ? 0.25822 0.25913 0.22778 -0.03886 0.03993  0.04146  99  GLU A O   
731  C  CB  . GLU A 99  ? 0.25619 0.25537 0.24603 -0.04153 0.03388  0.03472  99  GLU A CB  
732  C  CG  . GLU A 99  ? 0.28412 0.27934 0.27279 -0.04678 0.03643  0.04030  99  GLU A CG  
733  C  CD  . GLU A 99  ? 0.28087 0.28073 0.27919 -0.05222 0.03828  0.04023  99  GLU A CD  
734  O  OE1 . GLU A 99  ? 0.26243 0.27113 0.26835 -0.05189 0.03849  0.03609  99  GLU A OE1 
735  O  OE2 . GLU A 99  ? 0.30198 0.29662 0.30042 -0.05704 0.03947  0.04462  99  GLU A OE2 
736  N  N   . GLU A 100 ? 0.22642 0.24032 0.20644 -0.03542 0.04007  0.03294  100 GLU A N   
737  C  CA  . GLU A 100 ? 0.23134 0.25305 0.20885 -0.03583 0.04516  0.03372  100 GLU A CA  
738  C  C   . GLU A 100 ? 0.23954 0.26251 0.20946 -0.03101 0.04501  0.03149  100 GLU A C   
739  O  O   . GLU A 100 ? 0.26922 0.29908 0.23689 -0.03053 0.04912  0.03091  100 GLU A O   
740  C  CB  . GLU A 100 ? 0.25716 0.28933 0.24497 -0.03731 0.04796  0.03099  100 GLU A CB  
741  C  CG  . GLU A 100 ? 0.30440 0.33612 0.30001 -0.04276 0.04821  0.03315  100 GLU A CG  
742  C  CD  . GLU A 100 ? 0.39265 0.43578 0.39878 -0.04472 0.05118  0.03106  100 GLU A CD  
743  O  OE1 . GLU A 100 ? 0.41445 0.46495 0.42353 -0.04099 0.05170  0.02702  100 GLU A OE1 
744  O  OE2 . GLU A 100 ? 0.42344 0.46811 0.43538 -0.05007 0.05286  0.03354  100 GLU A OE2 
745  N  N   . THR A 101 ? 0.21933 0.23586 0.18511 -0.02757 0.04048  0.03018  101 THR A N   
746  C  CA  . THR A 101 ? 0.21899 0.23637 0.17781 -0.02335 0.03985  0.02789  101 THR A CA  
747  C  C   . THR A 101 ? 0.24740 0.26133 0.19522 -0.02389 0.04108  0.03218  101 THR A C   
748  O  O   . THR A 101 ? 0.25817 0.26426 0.20225 -0.02502 0.03873  0.03617  101 THR A O   
749  C  CB  . THR A 101 ? 0.21241 0.22489 0.17180 -0.01988 0.03452  0.02500  101 THR A CB  
750  O  OG1 . THR A 101 ? 0.20745 0.22323 0.17613 -0.01941 0.03339  0.02132  101 THR A OG1 
751  C  CG2 . THR A 101 ? 0.21811 0.23126 0.17095 -0.01595 0.03347  0.02248  101 THR A CG2 
752  N  N   . THR A 102 ? 0.25184 0.27139 0.19421 -0.02291 0.04461  0.03135  102 THR A N   
753  C  CA  . THR A 102 ? 0.24524 0.26155 0.17577 -0.02295 0.04517  0.03514  102 THR A CA  
754  C  C   . THR A 102 ? 0.24412 0.25546 0.16886 -0.01880 0.04005  0.03323  102 THR A C   
755  O  O   . THR A 102 ? 0.23519 0.24768 0.16427 -0.01581 0.03750  0.02829  102 THR A O   
756  C  CB  . THR A 102 ? 0.27982 0.30394 0.20518 -0.02323 0.05074  0.03460  102 THR A CB  
757  O  OG1 . THR A 102 ? 0.28086 0.30915 0.20570 -0.01899 0.05019  0.02849  102 THR A OG1 
758  C  CG2 . THR A 102 ? 0.28629 0.31758 0.21953 -0.02693 0.05608  0.03537  102 THR A CG2 
759  N  N   . THR A 103 ? 0.25393 0.25988 0.16884 -0.01876 0.03847  0.03747  103 THR A N   
760  C  CA  . THR A 103 ? 0.25703 0.25910 0.16690 -0.01491 0.03337  0.03570  103 THR A CA  
761  C  C   . THR A 103 ? 0.25142 0.25929 0.15795 -0.01195 0.03411  0.03034  103 THR A C   
762  O  O   . THR A 103 ? 0.24730 0.25414 0.15519 -0.00886 0.03018  0.02642  103 THR A O   
763  C  CB  . THR A 103 ? 0.27603 0.27155 0.17619 -0.01531 0.03128  0.04162  103 THR A CB  
764  O  OG1 . THR A 103 ? 0.28692 0.27605 0.19156 -0.01784 0.03027  0.04598  103 THR A OG1 
765  C  CG2 . THR A 103 ? 0.30417 0.29634 0.19984 -0.01128 0.02557  0.03989  103 THR A CG2 
766  N  N   . ALA A 104 ? 0.26926 0.28335 0.17197 -0.01293 0.03927  0.02982  104 ALA A N   
767  C  CA  . ALA A 104 ? 0.27603 0.29533 0.17616 -0.01000 0.04018  0.02399  104 ALA A CA  
768  C  C   . ALA A 104 ? 0.27664 0.29856 0.18770 -0.00819 0.03934  0.01837  104 ALA A C   
769  O  O   . ALA A 104 ? 0.27746 0.29941 0.18806 -0.00515 0.03672  0.01368  104 ALA A O   
770  C  CB  . ALA A 104 ? 0.29162 0.31764 0.18642 -0.01133 0.04650  0.02417  104 ALA A CB  
771  N  N   . GLU A 105 ? 0.27213 0.29611 0.19307 -0.01021 0.04129  0.01894  105 GLU A N   
772  C  CA  . GLU A 105 ? 0.24470 0.27085 0.17588 -0.00858 0.04010  0.01436  105 GLU A CA  
773  C  C   . GLU A 105 ? 0.23607 0.25626 0.16925 -0.00686 0.03429  0.01343  105 GLU A C   
774  O  O   . GLU A 105 ? 0.26094 0.28175 0.19728 -0.00430 0.03223  0.00902  105 GLU A O   
775  C  CB  . GLU A 105 ? 0.26131 0.29077 0.20225 -0.01138 0.04270  0.01572  105 GLU A CB  
776  C  CG  . GLU A 105 ? 0.26662 0.30441 0.20935 -0.01239 0.04866  0.01487  105 GLU A CG  
777  C  CD  . GLU A 105 ? 0.30955 0.35062 0.26077 -0.01617 0.05124  0.01754  105 GLU A CD  
778  O  OE1 . GLU A 105 ? 0.30034 0.33613 0.25342 -0.01881 0.04902  0.02119  105 GLU A OE1 
779  O  OE2 . GLU A 105 ? 0.31273 0.36195 0.26913 -0.01647 0.05556  0.01572  105 GLU A OE2 
780  N  N   . TRP A 106 ? 0.24202 0.25641 0.17386 -0.00832 0.03177  0.01762  106 TRP A N   
781  C  CA  . TRP A 106 ? 0.24690 0.25599 0.18055 -0.00666 0.02653  0.01699  106 TRP A CA  
782  C  C   . TRP A 106 ? 0.23932 0.24783 0.16728 -0.00358 0.02364  0.01410  106 TRP A C   
783  O  O   . TRP A 106 ? 0.23732 0.24570 0.16951 -0.00163 0.02093  0.01046  106 TRP A O   
784  C  CB  . TRP A 106 ? 0.24765 0.25048 0.17910 -0.00845 0.02483  0.02226  106 TRP A CB  
785  C  CG  . TRP A 106 ? 0.25279 0.25009 0.18562 -0.00661 0.01969  0.02214  106 TRP A CG  
786  C  CD1 . TRP A 106 ? 0.26813 0.26151 0.19458 -0.00474 0.01621  0.02366  106 TRP A CD1 
787  C  CD2 . TRP A 106 ? 0.25381 0.24932 0.19495 -0.00648 0.01758  0.02053  106 TRP A CD2 
788  N  NE1 . TRP A 106 ? 0.25576 0.24542 0.18679 -0.00329 0.01227  0.02291  106 TRP A NE1 
789  C  CE2 . TRP A 106 ? 0.23728 0.22810 0.17693 -0.00434 0.01320  0.02088  106 TRP A CE2 
790  C  CE3 . TRP A 106 ? 0.24940 0.24727 0.19896 -0.00787 0.01888  0.01872  106 TRP A CE3 
791  C  CZ2 . TRP A 106 ? 0.22095 0.20944 0.16706 -0.00357 0.01059  0.01930  106 TRP A CZ2 
792  C  CZ3 . TRP A 106 ? 0.23444 0.22966 0.18965 -0.00722 0.01597  0.01726  106 TRP A CZ3 
793  C  CH2 . TRP A 106 ? 0.23506 0.22567 0.18838 -0.00506 0.01209  0.01745  106 TRP A CH2 
794  N  N   . ARG A 107 ? 0.25773 0.26607 0.17591 -0.00334 0.02417  0.01573  107 ARG A N   
795  C  CA  . ARG A 107 ? 0.25565 0.26339 0.16810 -0.00070 0.02088  0.01299  107 ARG A CA  
796  C  C   . ARG A 107 ? 0.26545 0.27760 0.17989 0.00099  0.02215  0.00701  107 ARG A C   
797  O  O   . ARG A 107 ? 0.27476 0.28605 0.18987 0.00296  0.01871  0.00349  107 ARG A O   
798  C  CB  . ARG A 107 ? 0.28151 0.28818 0.18221 -0.00094 0.02096  0.01633  107 ARG A CB  
799  C  CG  . ARG A 107 ? 0.32868 0.32962 0.22697 -0.00202 0.01867  0.02241  107 ARG A CG  
800  C  CD  . ARG A 107 ? 0.39450 0.39343 0.28139 -0.00078 0.01583  0.02473  107 ARG A CD  
801  N  NE  . ARG A 107 ? 0.44522 0.43875 0.32773 -0.00210 0.01483  0.03166  107 ARG A NE  
802  C  CZ  . ARG A 107 ? 0.48855 0.47645 0.37396 -0.00108 0.01039  0.03412  107 ARG A CZ  
803  N  NH1 . ARG A 107 ? 0.50035 0.48809 0.39301 0.00112  0.00678  0.03018  107 ARG A NH1 
804  N  NH2 . ARG A 107 ? 0.49886 0.48121 0.38002 -0.00222 0.00967  0.04059  107 ARG A NH2 
805  N  N   . LYS A 108 ? 0.25757 0.27448 0.17326 0.00025  0.02708  0.00575  108 LYS A N   
806  C  CA  . LYS A 108 ? 0.26415 0.28471 0.18236 0.00223  0.02837  -0.00007 108 LYS A CA  
807  C  C   . LYS A 108 ? 0.24628 0.26584 0.17452 0.00319  0.02598  -0.00271 108 LYS A C   
808  O  O   . LYS A 108 ? 0.25929 0.27804 0.18834 0.00512  0.02358  -0.00679 108 LYS A O   
809  C  CB  . LYS A 108 ? 0.30626 0.33262 0.22521 0.00149  0.03430  -0.00072 108 LYS A CB  
810  C  CG  . LYS A 108 ? 0.39233 0.42227 0.31385 0.00398  0.03593  -0.00684 108 LYS A CG  
811  C  CD  . LYS A 108 ? 0.46801 0.50451 0.38939 0.00350  0.04217  -0.00736 108 LYS A CD  
812  C  CE  . LYS A 108 ? 0.50985 0.54934 0.44030 0.00113  0.04478  -0.00405 108 LYS A CE  
813  N  NZ  . LYS A 108 ? 0.53625 0.58027 0.46346 -0.00157 0.05005  -0.00040 108 LYS A NZ  
814  N  N   . LEU A 109 ? 0.23298 0.25243 0.16870 0.00165  0.02647  -0.00035 109 LEU A N   
815  C  CA  . LEU A 109 ? 0.20937 0.22816 0.15381 0.00242  0.02433  -0.00245 109 LEU A CA  
816  C  C   . LEU A 109 ? 0.23470 0.24914 0.17836 0.00339  0.01944  -0.00291 109 LEU A C   
817  O  O   . LEU A 109 ? 0.23926 0.25340 0.18643 0.00479  0.01755  -0.00620 109 LEU A O   
818  C  CB  . LEU A 109 ? 0.21939 0.23900 0.17097 0.00036  0.02550  0.00020  109 LEU A CB  
819  C  CG  . LEU A 109 ? 0.21480 0.23430 0.17486 0.00106  0.02345  -0.00176 109 LEU A CG  
820  C  CD1 . LEU A 109 ? 0.21064 0.23416 0.17802 -0.00031 0.02599  -0.00113 109 LEU A CD1 
821  C  CD2 . LEU A 109 ? 0.22548 0.24033 0.18643 0.00074  0.01951  -0.00032 109 LEU A CD2 
822  N  N   . LEU A 110 ? 0.21321 0.22434 0.15270 0.00267  0.01738  0.00050  110 LEU A N   
823  C  CA  . LEU A 110 ? 0.24523 0.25318 0.18507 0.00375  0.01282  0.00006  110 LEU A CA  
824  C  C   . LEU A 110 ? 0.24017 0.24856 0.17542 0.00544  0.01087  -0.00333 110 LEU A C   
825  O  O   . LEU A 110 ? 0.23740 0.24486 0.17572 0.00634  0.00769  -0.00548 110 LEU A O   
826  C  CB  . LEU A 110 ? 0.25343 0.25770 0.19021 0.00307  0.01096  0.00446  110 LEU A CB  
827  C  CG  . LEU A 110 ? 0.27660 0.27896 0.21898 0.00142  0.01159  0.00724  110 LEU A CG  
828  C  CD1 . LEU A 110 ? 0.31463 0.31232 0.25331 0.00122  0.00944  0.01136  110 LEU A CD1 
829  C  CD2 . LEU A 110 ? 0.26919 0.27184 0.21969 0.00186  0.01015  0.00482  110 LEU A CD2 
830  N  N   . ALA A 111 ? 0.22454 0.23462 0.15255 0.00569  0.01281  -0.00408 111 ALA A N   
831  C  CA  . ALA A 111 ? 0.22294 0.23336 0.14626 0.00717  0.01077  -0.00795 111 ALA A CA  
832  C  C   . ALA A 111 ? 0.23665 0.24779 0.16639 0.00806  0.01061  -0.01273 111 ALA A C   
833  O  O   . ALA A 111 ? 0.25044 0.26040 0.18082 0.00877  0.00726  -0.01546 111 ALA A O   
834  C  CB  . ALA A 111 ? 0.24618 0.25861 0.16007 0.00729  0.01339  -0.00831 111 ALA A CB  
835  N  N   . VAL A 112 ? 0.23127 0.24431 0.16622 0.00798  0.01405  -0.01358 112 VAL A N   
836  C  CA  . VAL A 112 ? 0.22975 0.24280 0.17088 0.00901  0.01381  -0.01753 112 VAL A CA  
837  C  C   . VAL A 112 ? 0.21413 0.22541 0.16278 0.00846  0.01133  -0.01637 112 VAL A C   
838  O  O   . VAL A 112 ? 0.23538 0.24501 0.18648 0.00885  0.00865  -0.01868 112 VAL A O   
839  C  CB  . VAL A 112 ? 0.22869 0.24487 0.17285 0.00960  0.01819  -0.01885 112 VAL A CB  
840  C  CG1 . VAL A 112 ? 0.23968 0.25502 0.19060 0.01093  0.01755  -0.02237 112 VAL A CG1 
841  C  CG2 . VAL A 112 ? 0.26461 0.28319 0.20096 0.01025  0.02114  -0.02051 112 VAL A CG2 
842  N  N   . ASN A 113 ? 0.21221 0.22392 0.16455 0.00733  0.01231  -0.01291 113 ASN A N   
843  C  CA  . ASN A 113 ? 0.18596 0.19682 0.14555 0.00688  0.01086  -0.01220 113 ASN A CA  
844  C  C   . ASN A 113 ? 0.22076 0.22943 0.18030 0.00656  0.00732  -0.01107 113 ASN A C   
845  O  O   . ASN A 113 ? 0.23638 0.24450 0.20104 0.00642  0.00579  -0.01156 113 ASN A O   
846  C  CB  . ASN A 113 ? 0.18964 0.20193 0.15297 0.00567  0.01298  -0.00936 113 ASN A CB  
847  C  CG  . ASN A 113 ? 0.21678 0.23238 0.18313 0.00604  0.01630  -0.01049 113 ASN A CG  
848  O  OD1 . ASN A 113 ? 0.21849 0.23536 0.18290 0.00738  0.01779  -0.01322 113 ASN A OD1 
849  N  ND2 . ASN A 113 ? 0.21636 0.23365 0.18787 0.00495  0.01739  -0.00866 113 ASN A ND2 
850  N  N   . LEU A 114 ? 0.22661 0.23430 0.18070 0.00649  0.00614  -0.00923 114 LEU A N   
851  C  CA  . LEU A 114 ? 0.20649 0.21261 0.16116 0.00663  0.00276  -0.00810 114 LEU A CA  
852  C  C   . LEU A 114 ? 0.21065 0.21672 0.16094 0.00751  -0.00008 -0.00997 114 LEU A C   
853  O  O   . LEU A 114 ? 0.21179 0.21810 0.16556 0.00768  -0.00254 -0.01189 114 LEU A O   
854  C  CB  . LEU A 114 ? 0.21560 0.22007 0.16869 0.00610  0.00284  -0.00412 114 LEU A CB  
855  C  CG  . LEU A 114 ? 0.24244 0.24523 0.19632 0.00684  -0.00064 -0.00292 114 LEU A CG  
856  C  CD1 . LEU A 114 ? 0.21267 0.21643 0.17332 0.00696  -0.00193 -0.00496 114 LEU A CD1 
857  C  CD2 . LEU A 114 ? 0.24948 0.24957 0.20271 0.00636  -0.00028 0.00087  114 LEU A CD2 
858  N  N   . ASP A 115 ? 0.20706 0.21322 0.14973 0.00786  0.00022  -0.00953 115 ASP A N   
859  C  CA  . ASP A 115 ? 0.20301 0.20949 0.14103 0.00865  -0.00288 -0.01168 115 ASP A CA  
860  C  C   . ASP A 115 ? 0.21916 0.22628 0.16006 0.00870  -0.00326 -0.01642 115 ASP A C   
861  O  O   . ASP A 115 ? 0.24026 0.24759 0.18282 0.00872  -0.00660 -0.01849 115 ASP A O   
862  C  CB  . ASP A 115 ? 0.22680 0.23354 0.15508 0.00896  -0.00207 -0.01079 115 ASP A CB  
863  C  CG  . ASP A 115 ? 0.27298 0.27820 0.19738 0.00882  -0.00232 -0.00565 115 ASP A CG  
864  O  OD1 . ASP A 115 ? 0.29015 0.29380 0.21914 0.00886  -0.00393 -0.00321 115 ASP A OD1 
865  O  OD2 . ASP A 115 ? 0.32488 0.33030 0.24128 0.00864  -0.00065 -0.00403 115 ASP A OD2 
866  N  N   . GLY A 116 ? 0.23825 0.24567 0.18033 0.00869  0.00005  -0.01820 116 GLY A N   
867  C  CA  . GLY A 116 ? 0.24758 0.25454 0.19224 0.00892  -0.00035 -0.02265 116 GLY A CA  
868  C  C   . GLY A 116 ? 0.23301 0.23914 0.18543 0.00819  -0.00240 -0.02305 116 GLY A C   
869  O  O   . GLY A 116 ? 0.22549 0.23087 0.17927 0.00785  -0.00468 -0.02612 116 GLY A O   
870  N  N   . VAL A 117 ? 0.21247 0.21878 0.16997 0.00770  -0.00149 -0.02007 117 VAL A N   
871  C  CA  . VAL A 117 ? 0.20507 0.21109 0.16937 0.00689  -0.00294 -0.02009 117 VAL A CA  
872  C  C   . VAL A 117 ? 0.20496 0.21189 0.16954 0.00656  -0.00640 -0.01986 117 VAL A C   
873  O  O   . VAL A 117 ? 0.21223 0.21944 0.18091 0.00570  -0.00823 -0.02147 117 VAL A O   
874  C  CB  . VAL A 117 ? 0.21254 0.21888 0.18122 0.00654  -0.00104 -0.01729 117 VAL A CB  
875  C  CG1 . VAL A 117 ? 0.20150 0.20795 0.17610 0.00564  -0.00236 -0.01713 117 VAL A CG1 
876  C  CG2 . VAL A 117 ? 0.23857 0.24485 0.20822 0.00698  0.00196  -0.01785 117 VAL A CG2 
877  N  N   . PHE A 118 ? 0.19594 0.20344 0.15642 0.00723  -0.00740 -0.01773 118 PHE A N   
878  C  CA  . PHE A 118 ? 0.19949 0.20836 0.16010 0.00749  -0.01106 -0.01766 118 PHE A CA  
879  C  C   . PHE A 118 ? 0.20815 0.21766 0.16643 0.00723  -0.01358 -0.02125 118 PHE A C   
880  O  O   . PHE A 118 ? 0.20623 0.21732 0.16887 0.00649  -0.01620 -0.02278 118 PHE A O   
881  C  CB  . PHE A 118 ? 0.19781 0.20633 0.15380 0.00861  -0.01177 -0.01436 118 PHE A CB  
882  C  CG  . PHE A 118 ? 0.21746 0.22753 0.17176 0.00953  -0.01602 -0.01440 118 PHE A CG  
883  C  CD1 . PHE A 118 ? 0.21707 0.22927 0.17787 0.00967  -0.01836 -0.01459 118 PHE A CD1 
884  C  CD2 . PHE A 118 ? 0.20790 0.21783 0.15418 0.01030  -0.01764 -0.01425 118 PHE A CD2 
885  C  CE1 . PHE A 118 ? 0.21645 0.23087 0.17680 0.01073  -0.02245 -0.01471 118 PHE A CE1 
886  C  CE2 . PHE A 118 ? 0.22490 0.23660 0.16977 0.01131  -0.02203 -0.01415 118 PHE A CE2 
887  C  CZ  . PHE A 118 ? 0.22653 0.24064 0.17900 0.01160  -0.02458 -0.01444 118 PHE A CZ  
888  N  N   . PHE A 119 ? 0.21529 0.22388 0.16682 0.00769  -0.01277 -0.02290 119 PHE A N   
889  C  CA  . PHE A 119 ? 0.22937 0.23828 0.17807 0.00739  -0.01535 -0.02696 119 PHE A CA  
890  C  C   . PHE A 119 ? 0.22698 0.23495 0.18227 0.00598  -0.01564 -0.03015 119 PHE A C   
891  O  O   . PHE A 119 ? 0.23663 0.24552 0.19381 0.00495  -0.01891 -0.03272 119 PHE A O   
892  C  CB  . PHE A 119 ? 0.22354 0.23155 0.16380 0.00818  -0.01366 -0.02886 119 PHE A CB  
893  C  CG  . PHE A 119 ? 0.23409 0.24288 0.16625 0.00921  -0.01358 -0.02575 119 PHE A CG  
894  C  CD1 . PHE A 119 ? 0.23983 0.24981 0.17078 0.00968  -0.01704 -0.02299 119 PHE A CD1 
895  C  CD2 . PHE A 119 ? 0.24206 0.25046 0.16802 0.00974  -0.00983 -0.02536 119 PHE A CD2 
896  C  CE1 . PHE A 119 ? 0.24916 0.25900 0.17223 0.01061  -0.01708 -0.01951 119 PHE A CE1 
897  C  CE2 . PHE A 119 ? 0.25392 0.26278 0.17200 0.01027  -0.00944 -0.02187 119 PHE A CE2 
898  C  CZ  . PHE A 119 ? 0.25649 0.26559 0.17290 0.01067  -0.01317 -0.01877 119 PHE A CZ  
899  N  N   . GLY A 120 ? 0.21851 0.22455 0.17729 0.00580  -0.01242 -0.02999 120 GLY A N   
900  C  CA  . GLY A 120 ? 0.20307 0.20732 0.16775 0.00447  -0.01266 -0.03236 120 GLY A CA  
901  C  C   . GLY A 120 ? 0.20691 0.21283 0.17866 0.00293  -0.01423 -0.03071 120 GLY A C   
902  O  O   . GLY A 120 ? 0.21904 0.22467 0.19473 0.00120  -0.01615 -0.03288 120 GLY A O   
903  N  N   . THR A 121 ? 0.19056 0.19824 0.16420 0.00338  -0.01322 -0.02702 121 THR A N   
904  C  CA  . THR A 121 ? 0.19399 0.20403 0.17408 0.00217  -0.01430 -0.02566 121 THR A CA  
905  C  C   . THR A 121 ? 0.19659 0.20980 0.17743 0.00174  -0.01804 -0.02698 121 THR A C   
906  O  O   . THR A 121 ? 0.22157 0.23647 0.20799 -0.00014 -0.01947 -0.02820 121 THR A O   
907  C  CB  . THR A 121 ? 0.18244 0.19357 0.16367 0.00308  -0.01256 -0.02209 121 THR A CB  
908  O  OG1 . THR A 121 ? 0.20645 0.21525 0.18752 0.00329  -0.00943 -0.02103 121 THR A OG1 
909  C  CG2 . THR A 121 ? 0.16148 0.17543 0.14925 0.00200  -0.01311 -0.02113 121 THR A CG2 
910  N  N   . ARG A 122 ? 0.19218 0.20652 0.16763 0.00336  -0.01975 -0.02653 122 ARG A N   
911  C  CA  . ARG A 122 ? 0.20660 0.22447 0.18268 0.00336  -0.02387 -0.02764 122 ARG A CA  
912  C  C   . ARG A 122 ? 0.20955 0.22736 0.18643 0.00145  -0.02616 -0.03185 122 ARG A C   
913  O  O   . ARG A 122 ? 0.22126 0.24230 0.20411 -0.00018 -0.02860 -0.03311 122 ARG A O   
914  C  CB  . ARG A 122 ? 0.20595 0.22409 0.17462 0.00557  -0.02543 -0.02614 122 ARG A CB  
915  C  CG  . ARG A 122 ? 0.20965 0.23176 0.17863 0.00607  -0.03027 -0.02695 122 ARG A CG  
916  C  CD  . ARG A 122 ? 0.22092 0.24250 0.18125 0.00832  -0.03192 -0.02496 122 ARG A CD  
917  N  NE  . ARG A 122 ? 0.22971 0.24862 0.18152 0.00813  -0.03099 -0.02691 122 ARG A NE  
918  C  CZ  . ARG A 122 ? 0.26665 0.28451 0.20924 0.00960  -0.03135 -0.02528 122 ARG A CZ  
919  N  NH1 . ARG A 122 ? 0.23736 0.25581 0.17793 0.01140  -0.03298 -0.02130 122 ARG A NH1 
920  N  NH2 . ARG A 122 ? 0.25812 0.27419 0.19339 0.00932  -0.02994 -0.02768 122 ARG A NH2 
921  N  N   . LEU A 123 ? 0.21057 0.22489 0.18171 0.00157  -0.02539 -0.03432 123 LEU A N   
922  C  CA  . LEU A 123 ? 0.22311 0.23636 0.19462 -0.00023 -0.02760 -0.03892 123 LEU A CA  
923  C  C   . LEU A 123 ? 0.23051 0.24230 0.21030 -0.00282 -0.02665 -0.03967 123 LEU A C   
924  O  O   . LEU A 123 ? 0.22018 0.23300 0.20412 -0.00517 -0.02936 -0.04232 123 LEU A O   
925  C  CB  . LEU A 123 ? 0.22993 0.23936 0.19365 0.00083  -0.02621 -0.04164 123 LEU A CB  
926  C  CG  . LEU A 123 ? 0.23294 0.24000 0.19569 -0.00064 -0.02824 -0.04721 123 LEU A CG  
927  C  CD1 . LEU A 123 ? 0.26167 0.27243 0.22443 -0.00190 -0.03346 -0.04959 123 LEU A CD1 
928  C  CD2 . LEU A 123 ? 0.25751 0.26161 0.21170 0.00117  -0.02632 -0.04976 123 LEU A CD2 
929  N  N   . GLY A 124 ? 0.22378 0.23304 0.20583 -0.00259 -0.02292 -0.03729 124 GLY A N   
930  C  CA  . GLY A 124 ? 0.19088 0.19840 0.18002 -0.00499 -0.02190 -0.03714 124 GLY A CA  
931  C  C   . GLY A 124 ? 0.20382 0.21614 0.20001 -0.00711 -0.02360 -0.03605 124 GLY A C   
932  O  O   . GLY A 124 ? 0.23069 0.24262 0.23207 -0.01004 -0.02472 -0.03764 124 GLY A O   
933  N  N   . ILE A 125 ? 0.18659 0.20344 0.18349 -0.00571 -0.02357 -0.03329 125 ILE A N   
934  C  CA  . ILE A 125 ? 0.17295 0.19547 0.17697 -0.00727 -0.02501 -0.03260 125 ILE A CA  
935  C  C   . ILE A 125 ? 0.17778 0.20306 0.18346 -0.00889 -0.02919 -0.03601 125 ILE A C   
936  O  O   . ILE A 125 ? 0.20397 0.23192 0.21675 -0.01194 -0.03018 -0.03695 125 ILE A O   
937  C  CB  . ILE A 125 ? 0.19689 0.22349 0.20097 -0.00476 -0.02466 -0.02974 125 ILE A CB  
938  C  CG1 . ILE A 125 ? 0.21474 0.23885 0.21803 -0.00375 -0.02067 -0.02671 125 ILE A CG1 
939  C  CG2 . ILE A 125 ? 0.18246 0.21598 0.19434 -0.00590 -0.02640 -0.02976 125 ILE A CG2 
940  C  CD1 . ILE A 125 ? 0.22374 0.24965 0.22522 -0.00095 -0.02025 -0.02433 125 ILE A CD1 
941  N  N   . GLN A 126 ? 0.19259 0.21766 0.19170 -0.00707 -0.03180 -0.03783 126 GLN A N   
942  C  CA  . GLN A 126 ? 0.20816 0.23665 0.20839 -0.00841 -0.03647 -0.04119 126 GLN A CA  
943  C  C   . GLN A 126 ? 0.22151 0.24650 0.22406 -0.01183 -0.03725 -0.04498 126 GLN A C   
944  O  O   . GLN A 126 ? 0.25770 0.28628 0.26593 -0.01460 -0.04037 -0.04726 126 GLN A O   
945  C  CB  . GLN A 126 ? 0.23296 0.26157 0.22417 -0.00563 -0.03907 -0.04209 126 GLN A CB  
946  C  CG  . GLN A 126 ? 0.27149 0.30329 0.26120 -0.00244 -0.03902 -0.03812 126 GLN A CG  
947  C  CD  . GLN A 126 ? 0.36410 0.39486 0.34382 0.00033  -0.04075 -0.03771 126 GLN A CD  
948  O  OE1 . GLN A 126 ? 0.38368 0.41003 0.35581 0.00069  -0.03945 -0.03912 126 GLN A OE1 
949  N  NE2 . GLN A 126 ? 0.42988 0.46479 0.40953 0.00247  -0.04360 -0.03559 126 GLN A NE2 
950  N  N   . ARG A 127 ? 0.22998 0.24801 0.22902 -0.01177 -0.03450 -0.04570 127 ARG A N   
951  C  CA  . ARG A 127 ? 0.25536 0.26848 0.25612 -0.01461 -0.03523 -0.04948 127 ARG A CA  
952  C  C   . ARG A 127 ? 0.22707 0.23855 0.23617 -0.01780 -0.03314 -0.04766 127 ARG A C   
953  O  O   . ARG A 127 ? 0.24637 0.25541 0.25968 -0.02125 -0.03471 -0.05037 127 ARG A O   
954  C  CB  . ARG A 127 ? 0.27444 0.28067 0.26760 -0.01253 -0.03335 -0.05150 127 ARG A CB  
955  C  CG  . ARG A 127 ? 0.31302 0.32011 0.29674 -0.00995 -0.03526 -0.05402 127 ARG A CG  
956  C  CD  . ARG A 127 ? 0.30543 0.30975 0.28687 -0.01159 -0.03846 -0.06015 127 ARG A CD  
957  N  NE  . ARG A 127 ? 0.27809 0.28449 0.25015 -0.00944 -0.04081 -0.06246 127 ARG A NE  
958  C  CZ  . ARG A 127 ? 0.26138 0.26400 0.22632 -0.00876 -0.04143 -0.06744 127 ARG A CZ  
959  N  NH1 . ARG A 127 ? 0.27198 0.26804 0.23880 -0.00988 -0.04007 -0.07101 127 ARG A NH1 
960  N  NH2 . ARG A 127 ? 0.27204 0.27733 0.22775 -0.00686 -0.04349 -0.06887 127 ARG A NH2 
961  N  N   . MET A 128 ? 0.19897 0.21135 0.21022 -0.01694 -0.02968 -0.04315 128 MET A N   
962  C  CA  . MET A 128 ? 0.19717 0.20733 0.21474 -0.01985 -0.02744 -0.04105 128 MET A CA  
963  C  C   . MET A 128 ? 0.20109 0.21847 0.22657 -0.02236 -0.02751 -0.03884 128 MET A C   
964  O  O   . MET A 128 ? 0.24664 0.26293 0.27788 -0.02581 -0.02620 -0.03749 128 MET A O   
965  C  CB  . MET A 128 ? 0.26229 0.26811 0.27690 -0.01759 -0.02348 -0.03781 128 MET A CB  
966  C  CG  . MET A 128 ? 0.32126 0.32073 0.32909 -0.01513 -0.02323 -0.04047 128 MET A CG  
967  S  SD  . MET A 128 ? 0.42409 0.41846 0.42986 -0.01274 -0.01911 -0.03735 128 MET A SD  
968  C  CE  . MET A 128 ? 0.17799 0.17955 0.18423 -0.01147 -0.01768 -0.03298 128 MET A CE  
969  N  N   . LYS A 129 ? 0.20336 0.22807 0.22946 -0.02073 -0.02899 -0.03844 129 LYS A N   
970  C  CA  . LYS A 129 ? 0.22023 0.25256 0.25423 -0.02249 -0.02850 -0.03647 129 LYS A CA  
971  C  C   . LYS A 129 ? 0.22816 0.26328 0.26984 -0.02728 -0.03080 -0.03874 129 LYS A C   
972  O  O   . LYS A 129 ? 0.23360 0.26721 0.27436 -0.02849 -0.03436 -0.04259 129 LYS A O   
973  C  CB  . LYS A 129 ? 0.22927 0.26854 0.26266 -0.01917 -0.03005 -0.03597 129 LYS A CB  
974  C  CG  . LYS A 129 ? 0.24855 0.29031 0.28002 -0.01847 -0.03501 -0.03942 129 LYS A CG  
975  C  CD  . LYS A 129 ? 0.29016 0.33867 0.32200 -0.01509 -0.03661 -0.03817 129 LYS A CD  
976  C  CE  . LYS A 129 ? 0.32880 0.38012 0.35811 -0.01405 -0.04189 -0.04101 129 LYS A CE  
977  N  NZ  . LYS A 129 ? 0.34641 0.40453 0.37772 -0.01067 -0.04352 -0.03921 129 LYS A NZ  
978  N  N   . ASN A 130 ? 0.22787 0.26719 0.27709 -0.03024 -0.02857 -0.03635 130 ASN A N   
979  C  CA  . ASN A 130 ? 0.23151 0.27616 0.28983 -0.03504 -0.03032 -0.03780 130 ASN A CA  
980  C  C   . ASN A 130 ? 0.24568 0.28301 0.30492 -0.03923 -0.03176 -0.04021 130 ASN A C   
981  O  O   . ASN A 130 ? 0.28292 0.32351 0.34821 -0.04302 -0.03479 -0.04300 130 ASN A O   
982  C  CB  . ASN A 130 ? 0.25041 0.30384 0.31170 -0.03385 -0.03451 -0.04042 130 ASN A CB  
983  C  CG  . ASN A 130 ? 0.27268 0.33326 0.33460 -0.02985 -0.03321 -0.03807 130 ASN A CG  
984  O  OD1 . ASN A 130 ? 0.29295 0.35545 0.35736 -0.02990 -0.02909 -0.03488 130 ASN A OD1 
985  N  ND2 . ASN A 130 ? 0.28449 0.34879 0.34395 -0.02631 -0.03681 -0.03965 130 ASN A ND2 
986  N  N   . LYS A 131 ? 0.24779 0.27518 0.30169 -0.03866 -0.02977 -0.03933 131 LYS A N   
987  C  CA  . LYS A 131 ? 0.26406 0.28315 0.31869 -0.04211 -0.03106 -0.04171 131 LYS A CA  
988  C  C   . LYS A 131 ? 0.26690 0.28070 0.32481 -0.04536 -0.02763 -0.03784 131 LYS A C   
989  O  O   . LYS A 131 ? 0.29784 0.30310 0.35630 -0.04800 -0.02838 -0.03920 131 LYS A O   
990  C  CB  . LYS A 131 ? 0.27855 0.28964 0.32425 -0.03852 -0.03238 -0.04489 131 LYS A CB  
991  C  CG  . LYS A 131 ? 0.30942 0.32491 0.35192 -0.03668 -0.03660 -0.04929 131 LYS A CG  
992  C  CD  . LYS A 131 ? 0.35315 0.36135 0.38663 -0.03363 -0.03777 -0.05297 131 LYS A CD  
993  C  CE  . LYS A 131 ? 0.40879 0.42201 0.43879 -0.03232 -0.04222 -0.05701 131 LYS A CE  
994  N  NZ  . LYS A 131 ? 0.44395 0.45207 0.46352 -0.02843 -0.04260 -0.05985 131 LYS A NZ  
995  N  N   . GLY A 132 ? 0.26114 0.27941 0.32083 -0.04513 -0.02399 -0.03309 132 GLY A N   
996  C  CA  . GLY A 132 ? 0.26115 0.27488 0.32315 -0.04825 -0.02079 -0.02885 132 GLY A CA  
997  C  C   . GLY A 132 ? 0.26601 0.26839 0.32178 -0.04603 -0.01980 -0.02786 132 GLY A C   
998  O  O   . GLY A 132 ? 0.27104 0.26661 0.32875 -0.04912 -0.01869 -0.02550 132 GLY A O   
999  N  N   . LEU A 133 ? 0.26199 0.26233 0.31061 -0.04073 -0.02014 -0.02938 133 LEU A N   
1000 C  CA  . LEU A 133 ? 0.23886 0.22934 0.28218 -0.03813 -0.01934 -0.02903 133 LEU A CA  
1001 C  C   . LEU A 133 ? 0.21692 0.20677 0.25751 -0.03590 -0.01586 -0.02392 133 LEU A C   
1002 O  O   . LEU A 133 ? 0.22374 0.20592 0.26108 -0.03391 -0.01515 -0.02300 133 LEU A O   
1003 C  CB  . LEU A 133 ? 0.23665 0.22544 0.27363 -0.03373 -0.02120 -0.03343 133 LEU A CB  
1004 C  CG  . LEU A 133 ? 0.27120 0.25998 0.30906 -0.03535 -0.02508 -0.03912 133 LEU A CG  
1005 C  CD1 . LEU A 133 ? 0.27761 0.26739 0.30809 -0.03066 -0.02631 -0.04241 133 LEU A CD1 
1006 C  CD2 . LEU A 133 ? 0.30914 0.28814 0.34893 -0.03811 -0.02632 -0.04144 133 LEU A CD2 
1007 N  N   . GLY A 134 ? 0.19780 0.19566 0.23967 -0.03594 -0.01386 -0.02091 134 GLY A N   
1008 C  CA  . GLY A 134 ? 0.19298 0.19091 0.23133 -0.03345 -0.01098 -0.01683 134 GLY A CA  
1009 C  C   . GLY A 134 ? 0.20954 0.20558 0.24163 -0.02824 -0.01137 -0.01863 134 GLY A C   
1010 O  O   . GLY A 134 ? 0.20706 0.19750 0.23572 -0.02595 -0.01040 -0.01717 134 GLY A O   
1011 N  N   . ALA A 135 ? 0.18186 0.18280 0.21259 -0.02634 -0.01287 -0.02168 135 ALA A N   
1012 C  CA  . ALA A 135 ? 0.17694 0.17573 0.20169 -0.02204 -0.01345 -0.02381 135 ALA A CA  
1013 C  C   . ALA A 135 ? 0.18023 0.18112 0.20149 -0.01886 -0.01110 -0.02089 135 ALA A C   
1014 O  O   . ALA A 135 ? 0.19720 0.20337 0.22011 -0.01934 -0.00962 -0.01836 135 ALA A O   
1015 C  CB  . ALA A 135 ? 0.18287 0.18573 0.20659 -0.02121 -0.01613 -0.02767 135 ALA A CB  
1016 N  N   . SER A 136 ? 0.17149 0.16840 0.18807 -0.01565 -0.01070 -0.02157 136 SER A N   
1017 C  CA  . SER A 136 ? 0.16687 0.16503 0.18054 -0.01300 -0.00866 -0.01899 136 SER A CA  
1018 C  C   . SER A 136 ? 0.18778 0.18502 0.19653 -0.00959 -0.00887 -0.02112 136 SER A C   
1019 O  O   . SER A 136 ? 0.20314 0.19576 0.21027 -0.00870 -0.00946 -0.02355 136 SER A O   
1020 C  CB  . SER A 136 ? 0.17052 0.16424 0.18498 -0.01341 -0.00722 -0.01597 136 SER A CB  
1021 O  OG  . SER A 136 ? 0.18674 0.18221 0.19875 -0.01114 -0.00557 -0.01360 136 SER A OG  
1022 N  N   . ILE A 137 ? 0.16222 0.16375 0.16866 -0.00778 -0.00828 -0.02030 137 ILE A N   
1023 C  CA  . ILE A 137 ? 0.17156 0.17271 0.17317 -0.00485 -0.00789 -0.02129 137 ILE A CA  
1024 C  C   . ILE A 137 ? 0.16416 0.16557 0.16502 -0.00345 -0.00572 -0.01844 137 ILE A C   
1025 O  O   . ILE A 137 ? 0.17172 0.17628 0.17385 -0.00391 -0.00501 -0.01622 137 ILE A O   
1026 C  CB  . ILE A 137 ? 0.17594 0.18108 0.17538 -0.00404 -0.00925 -0.02232 137 ILE A CB  
1027 C  CG1 . ILE A 137 ? 0.16544 0.17072 0.16565 -0.00549 -0.01194 -0.02546 137 ILE A CG1 
1028 C  CG2 . ILE A 137 ? 0.21914 0.22377 0.21319 -0.00140 -0.00845 -0.02253 137 ILE A CG2 
1029 C  CD1 . ILE A 137 ? 0.19139 0.20126 0.19025 -0.00477 -0.01407 -0.02620 137 ILE A CD1 
1030 N  N   . ILE A 138 ? 0.17475 0.17310 0.17391 -0.00177 -0.00473 -0.01878 138 ILE A N   
1031 C  CA  . ILE A 138 ? 0.16951 0.16817 0.16857 -0.00050 -0.00302 -0.01637 138 ILE A CA  
1032 C  C   . ILE A 138 ? 0.16246 0.16239 0.15793 0.00161  -0.00211 -0.01718 138 ILE A C   
1033 O  O   . ILE A 138 ? 0.18464 0.18269 0.17831 0.00293  -0.00180 -0.01939 138 ILE A O   
1034 C  CB  . ILE A 138 ? 0.15989 0.15450 0.16107 -0.00021 -0.00270 -0.01579 138 ILE A CB  
1035 C  CG1 . ILE A 138 ? 0.20861 0.20150 0.21299 -0.00284 -0.00354 -0.01443 138 ILE A CG1 
1036 C  CG2 . ILE A 138 ? 0.17619 0.17201 0.17748 0.00126  -0.00139 -0.01345 138 ILE A CG2 
1037 C  CD1 . ILE A 138 ? 0.23628 0.22331 0.24269 -0.00270 -0.00392 -0.01441 138 ILE A CD1 
1038 N  N   . ASN A 139 ? 0.17084 0.17384 0.16515 0.00185  -0.00157 -0.01559 139 ASN A N   
1039 C  CA  . ASN A 139 ? 0.16195 0.16599 0.15283 0.00331  -0.00063 -0.01581 139 ASN A CA  
1040 C  C   . ASN A 139 ? 0.17285 0.17755 0.16477 0.00406  0.00107  -0.01412 139 ASN A C   
1041 O  O   . ASN A 139 ? 0.17112 0.17708 0.16492 0.00340  0.00119  -0.01214 139 ASN A O   
1042 C  CB  . ASN A 139 ? 0.19197 0.19815 0.18097 0.00315  -0.00141 -0.01517 139 ASN A CB  
1043 C  CG  . ASN A 139 ? 0.19797 0.20414 0.18549 0.00287  -0.00339 -0.01718 139 ASN A CG  
1044 O  OD1 . ASN A 139 ? 0.19126 0.19560 0.17777 0.00295  -0.00384 -0.01947 139 ASN A OD1 
1045 N  ND2 . ASN A 139 ? 0.18871 0.19698 0.17648 0.00265  -0.00478 -0.01663 139 ASN A ND2 
1046 N  N   . MET A 140 ? 0.18272 0.18695 0.17369 0.00542  0.00233  -0.01519 140 MET A N   
1047 C  CA  . MET A 140 ? 0.18872 0.19444 0.18150 0.00619  0.00383  -0.01384 140 MET A CA  
1048 C  C   . MET A 140 ? 0.19599 0.20410 0.18708 0.00572  0.00465  -0.01232 140 MET A C   
1049 O  O   . MET A 140 ? 0.21566 0.22418 0.20332 0.00596  0.00535  -0.01281 140 MET A O   
1050 C  CB  . MET A 140 ? 0.21923 0.22450 0.21217 0.00800  0.00522  -0.01577 140 MET A CB  
1051 C  CG  . MET A 140 ? 0.26737 0.27430 0.26414 0.00903  0.00623  -0.01462 140 MET A CG  
1052 S  SD  . MET A 140 ? 0.26588 0.27056 0.26684 0.00884  0.00442  -0.01295 140 MET A SD  
1053 C  CE  . MET A 140 ? 0.29062 0.29009 0.29155 0.00929  0.00336  -0.01545 140 MET A CE  
1054 N  N   . SER A 141 ? 0.22017 0.22956 0.21335 0.00494  0.00448  -0.01042 141 SER A N   
1055 C  CA  . SER A 141 ? 0.23649 0.24755 0.22894 0.00435  0.00525  -0.00910 141 SER A CA  
1056 C  C   . SER A 141 ? 0.25658 0.26983 0.25208 0.00462  0.00635  -0.00840 141 SER A C   
1057 O  O   . SER A 141 ? 0.31230 0.32609 0.30894 0.00588  0.00734  -0.00940 141 SER A O   
1058 C  CB  . SER A 141 ? 0.28361 0.29450 0.27596 0.00332  0.00405  -0.00818 141 SER A CB  
1059 O  OG  . SER A 141 ? 0.29568 0.30735 0.28787 0.00265  0.00459  -0.00706 141 SER A OG  
1060 N  N   . SER A 142 ? 0.23464 0.24934 0.23189 0.00364  0.00599  -0.00707 142 SER A N   
1061 C  CA  . SER A 142 ? 0.19516 0.21278 0.19551 0.00360  0.00677  -0.00645 142 SER A CA  
1062 C  C   . SER A 142 ? 0.18721 0.20572 0.18859 0.00218  0.00560  -0.00541 142 SER A C   
1063 O  O   . SER A 142 ? 0.18374 0.20059 0.18298 0.00133  0.00491  -0.00535 142 SER A O   
1064 C  CB  . SER A 142 ? 0.20752 0.22665 0.20707 0.00334  0.00886  -0.00648 142 SER A CB  
1065 O  OG  . SER A 142 ? 0.19646 0.21925 0.19988 0.00285  0.00965  -0.00586 142 SER A OG  
1066 N  N   . ILE A 143 ? 0.18149 0.20291 0.18628 0.00208  0.00528  -0.00486 143 ILE A N   
1067 C  CA  . ILE A 143 ? 0.15988 0.18256 0.16530 0.00040  0.00437  -0.00437 143 ILE A CA  
1068 C  C   . ILE A 143 ? 0.15530 0.17686 0.15918 -0.00103 0.00541  -0.00439 143 ILE A C   
1069 O  O   . ILE A 143 ? 0.15955 0.18004 0.16264 -0.00235 0.00456  -0.00448 143 ILE A O   
1070 C  CB  . ILE A 143 ? 0.15438 0.18117 0.16409 0.00034  0.00370  -0.00390 143 ILE A CB  
1071 C  CG1 . ILE A 143 ? 0.16986 0.19958 0.18278 0.00104  0.00560  -0.00408 143 ILE A CG1 
1072 C  CG2 . ILE A 143 ? 0.18498 0.21194 0.19540 0.00160  0.00197  -0.00325 143 ILE A CG2 
1073 C  CD1 . ILE A 143 ? 0.17512 0.21015 0.19350 0.00077  0.00492  -0.00372 143 ILE A CD1 
1074 N  N   . PHE A 144 ? 0.17015 0.19163 0.17328 -0.00075 0.00726  -0.00430 144 PHE A N   
1075 C  CA  . PHE A 144 ? 0.14310 0.16304 0.14431 -0.00216 0.00832  -0.00362 144 PHE A CA  
1076 C  C   . PHE A 144 ? 0.16208 0.17789 0.15891 -0.00167 0.00772  -0.00365 144 PHE A C   
1077 O  O   . PHE A 144 ? 0.18414 0.19784 0.17861 -0.00239 0.00837  -0.00271 144 PHE A O   
1078 C  CB  . PHE A 144 ? 0.15011 0.17268 0.15227 -0.00225 0.01083  -0.00319 144 PHE A CB  
1079 C  CG  . PHE A 144 ? 0.15628 0.18380 0.16399 -0.00287 0.01126  -0.00316 144 PHE A CG  
1080 C  CD1 . PHE A 144 ? 0.18468 0.21314 0.19501 -0.00489 0.00995  -0.00282 144 PHE A CD1 
1081 C  CD2 . PHE A 144 ? 0.18449 0.21577 0.19512 -0.00117 0.01255  -0.00385 144 PHE A CD2 
1082 C  CE1 . PHE A 144 ? 0.18652 0.22022 0.20247 -0.00552 0.00975  -0.00291 144 PHE A CE1 
1083 C  CE2 . PHE A 144 ? 0.16899 0.20564 0.18575 -0.00143 0.01255  -0.00383 144 PHE A CE2 
1084 C  CZ  . PHE A 144 ? 0.17455 0.21261 0.19395 -0.00371 0.01101  -0.00326 144 PHE A CZ  
1085 N  N   . GLY A 145 ? 0.15522 0.17002 0.15127 -0.00054 0.00636  -0.00449 145 GLY A N   
1086 C  CA  . GLY A 145 ? 0.15424 0.16623 0.14780 -0.00026 0.00525  -0.00472 145 GLY A CA  
1087 C  C   . GLY A 145 ? 0.15947 0.17099 0.15399 -0.00100 0.00411  -0.00511 145 GLY A C   
1088 O  O   . GLY A 145 ? 0.16716 0.17667 0.16031 -0.00054 0.00332  -0.00554 145 GLY A O   
1089 N  N   . PHE A 146 ? 0.15888 0.17254 0.15579 -0.00195 0.00388  -0.00521 146 PHE A N   
1090 C  CA  . PHE A 146 ? 0.16755 0.18115 0.16493 -0.00280 0.00278  -0.00604 146 PHE A CA  
1091 C  C   . PHE A 146 ? 0.17454 0.18770 0.17329 -0.00459 0.00284  -0.00597 146 PHE A C   
1092 O  O   . PHE A 146 ? 0.21467 0.22538 0.21278 -0.00523 0.00216  -0.00687 146 PHE A O   
1093 C  CB  . PHE A 146 ? 0.16948 0.18601 0.16798 -0.00273 0.00193  -0.00625 146 PHE A CB  
1094 C  CG  . PHE A 146 ? 0.19021 0.20665 0.18734 -0.00174 0.00164  -0.00642 146 PHE A CG  
1095 C  CD1 . PHE A 146 ? 0.21049 0.22683 0.20629 -0.00188 0.00117  -0.00745 146 PHE A CD1 
1096 C  CD2 . PHE A 146 ? 0.19718 0.21381 0.19463 -0.00082 0.00195  -0.00573 146 PHE A CD2 
1097 C  CE1 . PHE A 146 ? 0.19725 0.21429 0.19227 -0.00138 0.00124  -0.00741 146 PHE A CE1 
1098 C  CE2 . PHE A 146 ? 0.21510 0.23156 0.21178 -0.00048 0.00168  -0.00571 146 PHE A CE2 
1099 C  CZ  . PHE A 146 ? 0.21453 0.23154 0.21012 -0.00090 0.00144  -0.00637 146 PHE A CZ  
1100 N  N   . VAL A 147 ? 0.16377 0.17946 0.16495 -0.00550 0.00363  -0.00513 147 VAL A N   
1101 C  CA  . VAL A 147 ? 0.15647 0.17254 0.15992 -0.00776 0.00365  -0.00503 147 VAL A CA  
1102 C  C   . VAL A 147 ? 0.16637 0.18235 0.17025 -0.00854 0.00570  -0.00341 147 VAL A C   
1103 O  O   . VAL A 147 ? 0.17608 0.19347 0.17925 -0.00718 0.00705  -0.00276 147 VAL A O   
1104 C  CB  . VAL A 147 ? 0.15346 0.17420 0.16045 -0.00866 0.00251  -0.00560 147 VAL A CB  
1105 C  CG1 . VAL A 147 ? 0.15628 0.17680 0.16170 -0.00840 0.00052  -0.00711 147 VAL A CG1 
1106 C  CG2 . VAL A 147 ? 0.16777 0.19252 0.17681 -0.00712 0.00308  -0.00482 147 VAL A CG2 
1107 N  N   . GLY A 148 ? 0.17033 0.18450 0.17518 -0.01088 0.00601  -0.00283 148 GLY A N   
1108 C  CA  . GLY A 148 ? 0.16320 0.17783 0.16853 -0.01227 0.00827  -0.00088 148 GLY A CA  
1109 C  C   . GLY A 148 ? 0.18190 0.20306 0.19207 -0.01321 0.00951  -0.00073 148 GLY A C   
1110 O  O   . GLY A 148 ? 0.18920 0.21417 0.20304 -0.01339 0.00808  -0.00195 148 GLY A O   
1111 N  N   . ASP A 149 ? 0.15329 0.17616 0.16335 -0.01364 0.01224  0.00082  149 ASP A N   
1112 C  CA  . ASP A 149 ? 0.15795 0.18727 0.17339 -0.01511 0.01406  0.00118  149 ASP A CA  
1113 C  C   . ASP A 149 ? 0.17028 0.19813 0.18470 -0.01789 0.01664  0.00353  149 ASP A C   
1114 O  O   . ASP A 149 ? 0.17523 0.19942 0.18406 -0.01702 0.01795  0.00492  149 ASP A O   
1115 C  CB  . ASP A 149 ? 0.17576 0.20994 0.19234 -0.01231 0.01548  0.00045  149 ASP A CB  
1116 C  CG  . ASP A 149 ? 0.22664 0.26834 0.24981 -0.01346 0.01741  0.00056  149 ASP A CG  
1117 O  OD1 . ASP A 149 ? 0.29872 0.34492 0.32709 -0.01275 0.01571  -0.00062 149 ASP A OD1 
1118 O  OD2 . ASP A 149 ? 0.22652 0.27000 0.24997 -0.01527 0.02051  0.00198  149 ASP A OD2 
1119 N  N   . PRO A 150 ? 0.17792 0.20860 0.19744 -0.02141 0.01735  0.00423  150 PRO A N   
1120 C  CA  . PRO A 150 ? 0.17750 0.20574 0.19587 -0.02472 0.01973  0.00702  150 PRO A CA  
1121 C  C   . PRO A 150 ? 0.17721 0.20875 0.19329 -0.02412 0.02367  0.00870  150 PRO A C   
1122 O  O   . PRO A 150 ? 0.19291 0.22103 0.20513 -0.02605 0.02567  0.01156  150 PRO A O   
1123 C  CB  . PRO A 150 ? 0.19254 0.22478 0.21849 -0.02878 0.01951  0.00686  150 PRO A CB  
1124 C  CG  . PRO A 150 ? 0.17404 0.21387 0.20546 -0.02685 0.01816  0.00430  150 PRO A CG  
1125 C  CD  . PRO A 150 ? 0.17333 0.20959 0.19998 -0.02273 0.01573  0.00264  150 PRO A CD  
1126 N  N   . SER A 151 ? 0.17819 0.21605 0.19625 -0.02138 0.02484  0.00701  151 SER A N   
1127 C  CA  . SER A 151 ? 0.19382 0.23552 0.20978 -0.02052 0.02883  0.00782  151 SER A CA  
1128 C  C   . SER A 151 ? 0.18681 0.22582 0.19627 -0.01642 0.02848  0.00656  151 SER A C   
1129 O  O   . SER A 151 ? 0.18854 0.23159 0.19686 -0.01471 0.03129  0.00583  151 SER A O   
1130 C  CB  . SER A 151 ? 0.25076 0.30236 0.27470 -0.02050 0.03103  0.00653  151 SER A CB  
1131 O  OG  . SER A 151 ? 0.30209 0.35686 0.33217 -0.02490 0.03174  0.00791  151 SER A OG  
1132 N  N   . LEU A 152 ? 0.16494 0.19752 0.17043 -0.01485 0.02511  0.00597  152 LEU A N   
1133 C  CA  . LEU A 152 ? 0.17593 0.20587 0.17581 -0.01137 0.02431  0.00465  152 LEU A CA  
1134 C  C   . LEU A 152 ? 0.18633 0.20876 0.17973 -0.01139 0.02241  0.00613  152 LEU A C   
1135 O  O   . LEU A 152 ? 0.18308 0.20231 0.17421 -0.00916 0.01982  0.00475  152 LEU A O   
1136 C  CB  . LEU A 152 ? 0.17954 0.21070 0.18260 -0.00872 0.02183  0.00192  152 LEU A CB  
1137 C  CG  . LEU A 152 ? 0.19610 0.23413 0.20492 -0.00725 0.02322  0.00019  152 LEU A CG  
1138 C  CD1 . LEU A 152 ? 0.20395 0.24169 0.21540 -0.00499 0.02012  -0.00164 152 LEU A CD1 
1139 C  CD2 . LEU A 152 ? 0.20277 0.24309 0.20863 -0.00540 0.02639  -0.00066 152 LEU A CD2 
1140 N  N   . GLY A 153 ? 0.20029 0.21992 0.19079 -0.01388 0.02371  0.00916  153 GLY A N   
1141 C  CA  . GLY A 153 ? 0.18981 0.20199 0.17513 -0.01372 0.02143  0.01082  153 GLY A CA  
1142 C  C   . GLY A 153 ? 0.18877 0.19867 0.16794 -0.01054 0.02009  0.01001  153 GLY A C   
1143 O  O   . GLY A 153 ? 0.19409 0.20044 0.17265 -0.00888 0.01701  0.00891  153 GLY A O   
1144 N  N   . ALA A 154 ? 0.18061 0.19293 0.15531 -0.00974 0.02239  0.01028  154 ALA A N   
1145 C  CA  . ALA A 154 ? 0.18194 0.19240 0.15064 -0.00697 0.02086  0.00919  154 ALA A CA  
1146 C  C   . ALA A 154 ? 0.19205 0.20419 0.16389 -0.00449 0.01903  0.00538  154 ALA A C   
1147 O  O   . ALA A 154 ? 0.17434 0.18364 0.14410 -0.00275 0.01622  0.00436  154 ALA A O   
1148 C  CB  . ALA A 154 ? 0.20229 0.21533 0.16514 -0.00690 0.02392  0.00994  154 ALA A CB  
1149 N  N   . TYR A 155 ? 0.19045 0.20725 0.16782 -0.00439 0.02047  0.00347  155 TYR A N   
1150 C  CA  . TYR A 155 ? 0.17416 0.19196 0.15485 -0.00232 0.01870  0.00048  155 TYR A CA  
1151 C  C   . TYR A 155 ? 0.17945 0.19389 0.16197 -0.00235 0.01546  0.00046  155 TYR A C   
1152 O  O   . TYR A 155 ? 0.18148 0.19431 0.16303 -0.00069 0.01335  -0.00108 155 TYR A O   
1153 C  CB  . TYR A 155 ? 0.16949 0.19260 0.15657 -0.00231 0.02045  -0.00079 155 TYR A CB  
1154 C  CG  . TYR A 155 ? 0.18198 0.20595 0.17174 0.00013  0.01907  -0.00354 155 TYR A CG  
1155 C  CD1 . TYR A 155 ? 0.21981 0.24422 0.20706 0.00228  0.01993  -0.00572 155 TYR A CD1 
1156 C  CD2 . TYR A 155 ? 0.18330 0.20743 0.17785 0.00016  0.01694  -0.00392 155 TYR A CD2 
1157 C  CE1 . TYR A 155 ? 0.21730 0.24162 0.20723 0.00433  0.01869  -0.00802 155 TYR A CE1 
1158 C  CE2 . TYR A 155 ? 0.19906 0.22339 0.19576 0.00221  0.01569  -0.00578 155 TYR A CE2 
1159 C  CZ  . TYR A 155 ? 0.21006 0.23420 0.20477 0.00424  0.01657  -0.00773 155 TYR A CZ  
1160 O  OH  . TYR A 155 ? 0.25477 0.27815 0.25186 0.00613  0.01524  -0.00942 155 TYR A OH  
1161 N  N   . ASN A 156 ? 0.17121 0.18491 0.15671 -0.00437 0.01517  0.00188  156 ASN A N   
1162 C  CA  . ASN A 156 ? 0.15972 0.17029 0.14660 -0.00443 0.01243  0.00156  156 ASN A CA  
1163 C  C   . ASN A 156 ? 0.16564 0.17191 0.14793 -0.00312 0.01059  0.00197  156 ASN A C   
1164 O  O   . ASN A 156 ? 0.17698 0.18227 0.15997 -0.00184 0.00851  0.00054  156 ASN A O   
1165 C  CB  . ASN A 156 ? 0.16457 0.17391 0.15415 -0.00702 0.01247  0.00293  156 ASN A CB  
1166 C  CG  . ASN A 156 ? 0.16869 0.18222 0.16430 -0.00814 0.01251  0.00173  156 ASN A CG  
1167 O  OD1 . ASN A 156 ? 0.17361 0.18883 0.17217 -0.01056 0.01370  0.00272  156 ASN A OD1 
1168 N  ND2 . ASN A 156 ? 0.16048 0.17569 0.15789 -0.00656 0.01101  -0.00017 156 ASN A ND2 
1169 N  N   . ALA A 157 ? 0.17695 0.18089 0.15470 -0.00353 0.01130  0.00417  157 ALA A N   
1170 C  CA  . ALA A 157 ? 0.17214 0.17236 0.14572 -0.00201 0.00912  0.00479  157 ALA A CA  
1171 C  C   . ALA A 157 ? 0.19290 0.19489 0.16528 0.00014  0.00794  0.00241  157 ALA A C   
1172 O  O   . ALA A 157 ? 0.18637 0.18717 0.15943 0.00143  0.00556  0.00136  157 ALA A O   
1173 C  CB  . ALA A 157 ? 0.18547 0.18328 0.15350 -0.00272 0.01007  0.00795  157 ALA A CB  
1174 N  N   . SER A 158 ? 0.17926 0.18427 0.15037 0.00047  0.00968  0.00128  158 SER A N   
1175 C  CA  . SER A 158 ? 0.18550 0.19148 0.15526 0.00221  0.00850  -0.00118 158 SER A CA  
1176 C  C   . SER A 158 ? 0.18199 0.18884 0.15680 0.00269  0.00716  -0.00322 158 SER A C   
1177 O  O   . SER A 158 ? 0.18734 0.19372 0.16192 0.00369  0.00518  -0.00462 158 SER A O   
1178 C  CB  . SER A 158 ? 0.18591 0.19452 0.15342 0.00259  0.01087  -0.00246 158 SER A CB  
1179 O  OG  . SER A 158 ? 0.18001 0.19153 0.15273 0.00235  0.01263  -0.00363 158 SER A OG  
1180 N  N   . LYS A 159 ? 0.18156 0.19002 0.16093 0.00184  0.00816  -0.00330 159 LYS A N   
1181 C  CA  . LYS A 159 ? 0.17813 0.18748 0.16143 0.00223  0.00700  -0.00479 159 LYS A CA  
1182 C  C   . LYS A 159 ? 0.20268 0.21048 0.18708 0.00205  0.00513  -0.00453 159 LYS A C   
1183 O  O   . LYS A 159 ? 0.20595 0.21416 0.19185 0.00256  0.00390  -0.00570 159 LYS A O   
1184 C  CB  . LYS A 159 ? 0.19069 0.20267 0.17809 0.00165  0.00833  -0.00486 159 LYS A CB  
1185 C  CG  . LYS A 159 ? 0.22331 0.23749 0.21070 0.00249  0.01030  -0.00581 159 LYS A CG  
1186 C  CD  . LYS A 159 ? 0.25524 0.26833 0.24104 0.00404  0.00948  -0.00786 159 LYS A CD  
1187 C  CE  . LYS A 159 ? 0.28384 0.29857 0.26936 0.00528  0.01145  -0.00951 159 LYS A CE  
1188 N  NZ  . LYS A 159 ? 0.30045 0.31335 0.28509 0.00661  0.01034  -0.01194 159 LYS A NZ  
1189 N  N   . GLY A 160 ? 0.16868 0.17459 0.15241 0.00134  0.00503  -0.00309 160 GLY A N   
1190 C  CA  . GLY A 160 ? 0.16184 0.16600 0.14636 0.00174  0.00331  -0.00330 160 GLY A CA  
1191 C  C   . GLY A 160 ? 0.18291 0.18627 0.16537 0.00326  0.00167  -0.00368 160 GLY A C   
1192 O  O   . GLY A 160 ? 0.20678 0.21086 0.19117 0.00398  0.00039  -0.00486 160 GLY A O   
1193 N  N   . ALA A 161 ? 0.17250 0.17498 0.15102 0.00371  0.00169  -0.00274 161 ALA A N   
1194 C  CA  . ALA A 161 ? 0.17537 0.17772 0.15180 0.00515  -0.00036 -0.00325 161 ALA A CA  
1195 C  C   . ALA A 161 ? 0.17787 0.18280 0.15632 0.00538  -0.00094 -0.00560 161 ALA A C   
1196 O  O   . ALA A 161 ? 0.19269 0.19860 0.17290 0.00608  -0.00274 -0.00659 161 ALA A O   
1197 C  CB  . ALA A 161 ? 0.19358 0.19478 0.16442 0.00541  -0.00022 -0.00183 161 ALA A CB  
1198 N  N   . VAL A 162 ? 0.19052 0.19660 0.16925 0.00478  0.00057  -0.00652 162 VAL A N   
1199 C  CA  . VAL A 162 ? 0.19463 0.20206 0.17540 0.00480  -0.00003 -0.00854 162 VAL A CA  
1200 C  C   . VAL A 162 ? 0.17983 0.18836 0.16494 0.00431  -0.00050 -0.00880 162 VAL A C   
1201 O  O   . VAL A 162 ? 0.17400 0.18364 0.16091 0.00425  -0.00175 -0.00988 162 VAL A O   
1202 C  CB  . VAL A 162 ? 0.22745 0.23522 0.20819 0.00463  0.00168  -0.00944 162 VAL A CB  
1203 C  CG1 . VAL A 162 ? 0.20312 0.21113 0.18660 0.00446  0.00089  -0.01121 162 VAL A CG1 
1204 C  CG2 . VAL A 162 ? 0.25293 0.26030 0.22879 0.00522  0.00234  -0.00986 162 VAL A CG2 
1205 N  N   . ARG A 163 ? 0.18275 0.19131 0.16950 0.00378  0.00052  -0.00786 163 ARG A N   
1206 C  CA  . ARG A 163 ? 0.17760 0.18746 0.16747 0.00330  0.00033  -0.00816 163 ARG A CA  
1207 C  C   . ARG A 163 ? 0.18022 0.19091 0.17113 0.00395  -0.00101 -0.00876 163 ARG A C   
1208 O  O   . ARG A 163 ? 0.18419 0.19695 0.17750 0.00356  -0.00129 -0.00956 163 ARG A O   
1209 C  CB  . ARG A 163 ? 0.17649 0.18609 0.16702 0.00268  0.00126  -0.00734 163 ARG A CB  
1210 C  CG  . ARG A 163 ? 0.16713 0.17819 0.15978 0.00219  0.00118  -0.00781 163 ARG A CG  
1211 C  CD  . ARG A 163 ? 0.16572 0.17628 0.15857 0.00149  0.00167  -0.00743 163 ARG A CD  
1212 N  NE  . ARG A 163 ? 0.16956 0.18145 0.16341 0.00115  0.00150  -0.00829 163 ARG A NE  
1213 C  CZ  . ARG A 163 ? 0.19218 0.20359 0.18612 0.00054  0.00149  -0.00873 163 ARG A CZ  
1214 N  NH1 . ARG A 163 ? 0.17257 0.18212 0.16632 -0.00008 0.00164  -0.00810 163 ARG A NH1 
1215 N  NH2 . ARG A 163 ? 0.23139 0.24430 0.22550 0.00036  0.00142  -0.00992 163 ARG A NH2 
1216 N  N   . ILE A 164 ? 0.16159 0.17081 0.15102 0.00498  -0.00181 -0.00822 164 ILE A N   
1217 C  CA  . ILE A 164 ? 0.15186 0.16218 0.14318 0.00613  -0.00312 -0.00891 164 ILE A CA  
1218 C  C   . ILE A 164 ? 0.17112 0.18287 0.16232 0.00689  -0.00494 -0.00952 164 ILE A C   
1219 O  O   . ILE A 164 ? 0.17227 0.18698 0.16676 0.00727  -0.00582 -0.01064 164 ILE A O   
1220 C  CB  . ILE A 164 ? 0.15513 0.16266 0.14567 0.00718  -0.00346 -0.00808 164 ILE A CB  
1221 C  CG1 . ILE A 164 ? 0.17704 0.18326 0.16787 0.00600  -0.00194 -0.00789 164 ILE A CG1 
1222 C  CG2 . ILE A 164 ? 0.18183 0.19076 0.17524 0.00888  -0.00467 -0.00920 164 ILE A CG2 
1223 C  CD1 . ILE A 164 ? 0.17577 0.18489 0.16914 0.00524  -0.00108 -0.00931 164 ILE A CD1 
1224 N  N   A MET A 165 ? 0.17568 0.18592 0.16321 0.00701  -0.00551 -0.00899 165 MET A N   
1225 N  N   B MET A 165 ? 0.17195 0.18220 0.15950 0.00700  -0.00550 -0.00900 165 MET A N   
1226 C  CA  A MET A 165 ? 0.16364 0.17548 0.15070 0.00745  -0.00756 -0.01001 165 MET A CA  
1227 C  CA  B MET A 165 ? 0.16764 0.17948 0.15472 0.00746  -0.00757 -0.01001 165 MET A CA  
1228 C  C   A MET A 165 ? 0.17543 0.18992 0.16606 0.00607  -0.00747 -0.01175 165 MET A C   
1229 C  C   B MET A 165 ? 0.17128 0.18576 0.16187 0.00608  -0.00748 -0.01175 165 MET A C   
1230 O  O   A MET A 165 ? 0.17415 0.19143 0.16740 0.00612  -0.00922 -0.01291 165 MET A O   
1231 O  O   B MET A 165 ? 0.17322 0.19045 0.16634 0.00612  -0.00926 -0.01293 165 MET A O   
1232 C  CB  A MET A 165 ? 0.16700 0.17687 0.14862 0.00756  -0.00777 -0.00957 165 MET A CB  
1233 C  CB  B MET A 165 ? 0.17155 0.18141 0.15317 0.00760  -0.00781 -0.00953 165 MET A CB  
1234 C  CG  A MET A 165 ? 0.17604 0.18752 0.15641 0.00808  -0.01046 -0.01090 165 MET A CG  
1235 C  CG  B MET A 165 ? 0.18478 0.19621 0.16508 0.00807  -0.01043 -0.01088 165 MET A CG  
1236 S  SD  A MET A 165 ? 0.21700 0.22696 0.19100 0.00774  -0.01016 -0.01174 165 MET A SD  
1237 S  SD  B MET A 165 ? 0.21309 0.22541 0.19438 0.00640  -0.01006 -0.01359 165 MET A SD  
1238 C  CE  A MET A 165 ? 0.23990 0.25005 0.21728 0.00610  -0.00828 -0.01398 165 MET A CE  
1239 C  CE  B MET A 165 ? 0.22524 0.23471 0.20046 0.00648  -0.00793 -0.01327 165 MET A CE  
1240 N  N   . SER A 166 ? 0.16748 0.18124 0.15868 0.00475  -0.00555 -0.01175 166 SER A N   
1241 C  CA  . SER A 166 ? 0.16536 0.18059 0.15969 0.00322  -0.00540 -0.01281 166 SER A CA  
1242 C  C   . SER A 166 ? 0.16325 0.18189 0.16201 0.00272  -0.00535 -0.01296 166 SER A C   
1243 O  O   . SER A 166 ? 0.17702 0.19792 0.17887 0.00145  -0.00597 -0.01388 166 SER A O   
1244 C  CB  . SER A 166 ? 0.18017 0.19349 0.17412 0.00235  -0.00357 -0.01226 166 SER A CB  
1245 O  OG  . SER A 166 ? 0.17776 0.18883 0.16829 0.00294  -0.00335 -0.01264 166 SER A OG  
1246 N  N   . LYS A 167 ? 0.16887 0.18803 0.16811 0.00357  -0.00448 -0.01226 167 LYS A N   
1247 C  CA  . LYS A 167 ? 0.14938 0.17235 0.15257 0.00349  -0.00409 -0.01284 167 LYS A CA  
1248 C  C   . LYS A 167 ? 0.15817 0.18421 0.16400 0.00459  -0.00610 -0.01392 167 LYS A C   
1249 O  O   . LYS A 167 ? 0.16699 0.19738 0.17718 0.00371  -0.00603 -0.01479 167 LYS A O   
1250 C  CB  . LYS A 167 ? 0.14779 0.17019 0.15047 0.00447  -0.00288 -0.01253 167 LYS A CB  
1251 C  CG  . LYS A 167 ? 0.16221 0.18283 0.16304 0.00319  -0.00118 -0.01160 167 LYS A CG  
1252 C  CD  . LYS A 167 ? 0.17578 0.19593 0.17607 0.00392  -0.00036 -0.01186 167 LYS A CD  
1253 C  CE  . LYS A 167 ? 0.21401 0.23275 0.21240 0.00264  0.00072  -0.01094 167 LYS A CE  
1254 N  NZ  . LYS A 167 ? 0.32184 0.34344 0.32126 0.00116  0.00176  -0.01070 167 LYS A NZ  
1255 N  N   . SER A 168 ? 0.16271 0.18687 0.16606 0.00643  -0.00800 -0.01368 168 SER A N   
1256 C  CA  . SER A 168 ? 0.15083 0.17809 0.15661 0.00778  -0.01055 -0.01454 168 SER A CA  
1257 C  C   . SER A 168 ? 0.16118 0.19122 0.16918 0.00587  -0.01172 -0.01583 168 SER A C   
1258 O  O   . SER A 168 ? 0.16647 0.20166 0.17982 0.00554  -0.01261 -0.01698 168 SER A O   
1259 C  CB  . SER A 168 ? 0.17511 0.19905 0.17641 0.00986  -0.01260 -0.01345 168 SER A CB  
1260 O  OG  . SER A 168 ? 0.18285 0.21003 0.18633 0.01138  -0.01571 -0.01413 168 SER A OG  
1261 N  N   . ALA A 169 ? 0.16726 0.19405 0.17162 0.00454  -0.01169 -0.01587 169 ALA A N   
1262 C  CA  . ALA A 169 ? 0.16779 0.19580 0.17374 0.00256  -0.01294 -0.01742 169 ALA A CA  
1263 C  C   . ALA A 169 ? 0.15991 0.19057 0.17107 0.00007  -0.01128 -0.01763 169 ALA A C   
1264 O  O   . ALA A 169 ? 0.16513 0.19956 0.18080 -0.00147 -0.01254 -0.01887 169 ALA A O   
1265 C  CB  . ALA A 169 ? 0.18215 0.20540 0.18284 0.00206  -0.01272 -0.01771 169 ALA A CB  
1266 N  N   . ALA A 170 ? 0.15712 0.18620 0.16779 -0.00050 -0.00854 -0.01625 170 ALA A N   
1267 C  CA  . ALA A 170 ? 0.15481 0.18636 0.16951 -0.00289 -0.00675 -0.01581 170 ALA A CA  
1268 C  C   . ALA A 170 ? 0.16165 0.19975 0.18181 -0.00285 -0.00680 -0.01652 170 ALA A C   
1269 O  O   . ALA A 170 ? 0.15360 0.19533 0.17843 -0.00531 -0.00661 -0.01694 170 ALA A O   
1270 C  CB  . ALA A 170 ? 0.14510 0.17447 0.15755 -0.00294 -0.00418 -0.01407 170 ALA A CB  
1271 N  N   . LEU A 171 ? 0.15235 0.19207 0.17247 -0.00011 -0.00691 -0.01670 171 LEU A N   
1272 C  CA  . LEU A 171 ? 0.14003 0.18642 0.16591 0.00055  -0.00670 -0.01771 171 LEU A CA  
1273 C  C   . LEU A 171 ? 0.14133 0.19192 0.17160 0.00020  -0.00954 -0.01914 171 LEU A C   
1274 O  O   . LEU A 171 ? 0.15171 0.20846 0.18819 -0.00155 -0.00902 -0.01991 171 LEU A O   
1275 C  CB  . LEU A 171 ? 0.15250 0.19873 0.17751 0.00406  -0.00663 -0.01792 171 LEU A CB  
1276 C  CG  . LEU A 171 ? 0.16926 0.21249 0.19088 0.00427  -0.00393 -0.01710 171 LEU A CG  
1277 C  CD1 . LEU A 171 ? 0.18020 0.22128 0.20037 0.00765  -0.00459 -0.01747 171 LEU A CD1 
1278 C  CD2 . LEU A 171 ? 0.16776 0.21610 0.19276 0.00257  -0.00105 -0.01744 171 LEU A CD2 
1279 N  N   . ASP A 172 ? 0.14381 0.19155 0.17087 0.00164  -0.01260 -0.01949 172 ASP A N   
1280 C  CA  . ASP A 172 ? 0.14539 0.19751 0.17631 0.00151  -0.01592 -0.02105 172 ASP A CA  
1281 C  C   . ASP A 172 ? 0.16188 0.21548 0.19604 -0.00261 -0.01585 -0.02193 172 ASP A C   
1282 O  O   . ASP A 172 ? 0.15947 0.21960 0.20049 -0.00407 -0.01684 -0.02315 172 ASP A O   
1283 C  CB  . ASP A 172 ? 0.17455 0.22282 0.19980 0.00366  -0.01920 -0.02106 172 ASP A CB  
1284 C  CG  . ASP A 172 ? 0.20925 0.26264 0.23810 0.00431  -0.02335 -0.02262 172 ASP A CG  
1285 O  OD1 . ASP A 172 ? 0.22222 0.28143 0.25676 0.00626  -0.02436 -0.02298 172 ASP A OD1 
1286 O  OD2 . ASP A 172 ? 0.23937 0.29102 0.26526 0.00307  -0.02574 -0.02368 172 ASP A OD2 
1287 N  N   . CYS A 173 ? 0.18239 0.23000 0.21224 -0.00453 -0.01466 -0.02130 173 CYS A N   
1288 C  CA  . CYS A 173 ? 0.14822 0.19551 0.18083 -0.00847 -0.01461 -0.02196 173 CYS A CA  
1289 C  C   . CYS A 173 ? 0.19037 0.24254 0.22916 -0.01113 -0.01186 -0.02102 173 CYS A C   
1290 O  O   . CYS A 173 ? 0.18001 0.23548 0.22428 -0.01445 -0.01247 -0.02184 173 CYS A O   
1291 C  CB  . CYS A 173 ? 0.14969 0.18905 0.17655 -0.00924 -0.01360 -0.02129 173 CYS A CB  
1292 S  SG  . CYS A 173 ? 0.17952 0.21393 0.19960 -0.00730 -0.01664 -0.02311 173 CYS A SG  
1293 N  N   . ALA A 174 ? 0.17802 0.23066 0.21574 -0.01002 -0.00875 -0.01934 174 ALA A N   
1294 C  CA  . ALA A 174 ? 0.15527 0.21294 0.19775 -0.01245 -0.00567 -0.01831 174 ALA A CA  
1295 C  C   . ALA A 174 ? 0.15732 0.22431 0.20736 -0.01209 -0.00618 -0.01988 174 ALA A C   
1296 O  O   . ALA A 174 ? 0.16840 0.24071 0.22462 -0.01550 -0.00519 -0.01992 174 ALA A O   
1297 C  CB  . ALA A 174 ? 0.16248 0.21846 0.20097 -0.01105 -0.00251 -0.01660 174 ALA A CB  
1298 N  N   . LEU A 175 ? 0.14831 0.21743 0.19837 -0.00798 -0.00776 -0.02106 175 LEU A N   
1299 C  CA  . LEU A 175 ? 0.15576 0.23418 0.21362 -0.00673 -0.00831 -0.02266 175 LEU A CA  
1300 C  C   . LEU A 175 ? 0.16788 0.25076 0.23157 -0.00887 -0.01159 -0.02421 175 LEU A C   
1301 O  O   . LEU A 175 ? 0.19320 0.28527 0.26544 -0.00971 -0.01141 -0.02536 175 LEU A O   
1302 C  CB  . LEU A 175 ? 0.16127 0.23937 0.21743 -0.00144 -0.00988 -0.02336 175 LEU A CB  
1303 C  CG  . LEU A 175 ? 0.18968 0.26425 0.24125 0.00063  -0.00677 -0.02244 175 LEU A CG  
1304 C  CD1 . LEU A 175 ? 0.19483 0.26605 0.24335 0.00541  -0.00884 -0.02275 175 LEU A CD1 
1305 C  CD2 . LEU A 175 ? 0.18734 0.26931 0.24424 -0.00008 -0.00293 -0.02304 175 LEU A CD2 
1306 N  N   . LYS A 176 ? 0.15321 0.23030 0.21272 -0.00972 -0.01465 -0.02460 176 LYS A N   
1307 C  CA  . LYS A 176 ? 0.16658 0.24730 0.23078 -0.01173 -0.01838 -0.02656 176 LYS A CA  
1308 C  C   . LYS A 176 ? 0.17722 0.25632 0.24365 -0.01730 -0.01748 -0.02649 176 LYS A C   
1309 O  O   . LYS A 176 ? 0.20026 0.28117 0.27020 -0.01968 -0.02073 -0.02845 176 LYS A O   
1310 C  CB  . LYS A 176 ? 0.18615 0.26218 0.24429 -0.00907 -0.02275 -0.02759 176 LYS A CB  
1311 C  CG  . LYS A 176 ? 0.19358 0.27175 0.25079 -0.00387 -0.02451 -0.02746 176 LYS A CG  
1312 C  CD  . LYS A 176 ? 0.24140 0.31514 0.29196 -0.00171 -0.02888 -0.02800 176 LYS A CD  
1313 C  CE  . LYS A 176 ? 0.30490 0.38098 0.35535 0.00331  -0.03126 -0.02746 176 LYS A CE  
1314 N  NZ  . LYS A 176 ? 0.37546 0.44773 0.41894 0.00510  -0.03563 -0.02757 176 LYS A NZ  
1315 N  N   . ASP A 177 ? 0.16689 0.24236 0.23129 -0.01942 -0.01341 -0.02425 177 ASP A N   
1316 C  CA  . ASP A 177 ? 0.16566 0.23890 0.23235 -0.02474 -0.01217 -0.02343 177 ASP A CA  
1317 C  C   . ASP A 177 ? 0.17620 0.24197 0.23926 -0.02604 -0.01550 -0.02499 177 ASP A C   
1318 O  O   . ASP A 177 ? 0.20095 0.26702 0.26854 -0.03028 -0.01682 -0.02607 177 ASP A O   
1319 C  CB  . ASP A 177 ? 0.18487 0.26804 0.26202 -0.02841 -0.01155 -0.02400 177 ASP A CB  
1320 C  CG  . ASP A 177 ? 0.24793 0.33874 0.32857 -0.02732 -0.00745 -0.02267 177 ASP A CG  
1321 O  OD1 . ASP A 177 ? 0.27708 0.36393 0.35228 -0.02648 -0.00407 -0.02041 177 ASP A OD1 
1322 O  OD2 . ASP A 177 ? 0.33677 0.43791 0.42588 -0.02741 -0.00771 -0.02414 177 ASP A OD2 
1323 N  N   . TYR A 178 ? 0.18792 0.24691 0.24276 -0.02250 -0.01665 -0.02524 178 TYR A N   
1324 C  CA  . TYR A 178 ? 0.20426 0.25640 0.25458 -0.02286 -0.01959 -0.02724 178 TYR A CA  
1325 C  C   . TYR A 178 ? 0.20526 0.24941 0.25359 -0.02580 -0.01790 -0.02622 178 TYR A C   
1326 O  O   . TYR A 178 ? 0.20479 0.24340 0.25078 -0.02674 -0.02018 -0.02845 178 TYR A O   
1327 C  CB  . TYR A 178 ? 0.18792 0.23607 0.23003 -0.01810 -0.02069 -0.02751 178 TYR A CB  
1328 C  CG  . TYR A 178 ? 0.19745 0.25033 0.23939 -0.01515 -0.02423 -0.02917 178 TYR A CG  
1329 C  CD1 . TYR A 178 ? 0.19730 0.25815 0.24663 -0.01647 -0.02698 -0.03094 178 TYR A CD1 
1330 C  CD2 . TYR A 178 ? 0.20781 0.25715 0.24219 -0.01114 -0.02505 -0.02881 178 TYR A CD2 
1331 C  CE1 . TYR A 178 ? 0.21324 0.27810 0.26205 -0.01339 -0.03072 -0.03217 178 TYR A CE1 
1332 C  CE2 . TYR A 178 ? 0.19430 0.24708 0.22766 -0.00834 -0.02851 -0.02972 178 TYR A CE2 
1333 C  CZ  . TYR A 178 ? 0.23719 0.29766 0.27766 -0.00928 -0.03155 -0.03139 178 TYR A CZ  
1334 O  OH  . TYR A 178 ? 0.25597 0.31992 0.29537 -0.00620 -0.03557 -0.03208 178 TYR A OH  
1335 N  N   . ASP A 179 ? 0.18748 0.23060 0.23629 -0.02702 -0.01412 -0.02300 179 ASP A N   
1336 C  CA  . ASP A 179 ? 0.20488 0.23962 0.25099 -0.02892 -0.01261 -0.02131 179 ASP A CA  
1337 C  C   . ASP A 179 ? 0.18698 0.21417 0.22524 -0.02536 -0.01332 -0.02207 179 ASP A C   
1338 O  O   . ASP A 179 ? 0.18869 0.20880 0.22496 -0.02618 -0.01434 -0.02326 179 ASP A O   
1339 C  CB  . ASP A 179 ? 0.23623 0.26874 0.28729 -0.03382 -0.01405 -0.02247 179 ASP A CB  
1340 C  CG  . ASP A 179 ? 0.28182 0.30530 0.33093 -0.03579 -0.01251 -0.02023 179 ASP A CG  
1341 O  OD1 . ASP A 179 ? 0.29563 0.31764 0.34214 -0.03491 -0.00951 -0.01661 179 ASP A OD1 
1342 O  OD2 . ASP A 179 ? 0.32113 0.33872 0.37111 -0.03798 -0.01461 -0.02232 179 ASP A OD2 
1343 N  N   . VAL A 180 ? 0.16614 0.19504 0.20026 -0.02135 -0.01274 -0.02160 180 VAL A N   
1344 C  CA  . VAL A 180 ? 0.16212 0.18521 0.18919 -0.01804 -0.01262 -0.02170 180 VAL A CA  
1345 C  C   . VAL A 180 ? 0.18923 0.21342 0.21411 -0.01597 -0.00983 -0.01881 180 VAL A C   
1346 O  O   . VAL A 180 ? 0.19750 0.22736 0.22386 -0.01476 -0.00938 -0.01842 180 VAL A O   
1347 C  CB  . VAL A 180 ? 0.17044 0.19430 0.19388 -0.01530 -0.01534 -0.02441 180 VAL A CB  
1348 C  CG1 . VAL A 180 ? 0.17640 0.19458 0.19276 -0.01234 -0.01461 -0.02437 180 VAL A CG1 
1349 C  CG2 . VAL A 180 ? 0.20541 0.22952 0.23105 -0.01742 -0.01870 -0.02785 180 VAL A CG2 
1350 N  N   . ARG A 181 ? 0.15737 0.17625 0.17905 -0.01546 -0.00815 -0.01701 181 ARG A N   
1351 C  CA  . ARG A 181 ? 0.18290 0.20233 0.20173 -0.01336 -0.00602 -0.01476 181 ARG A CA  
1352 C  C   . ARG A 181 ? 0.19401 0.21009 0.20758 -0.01015 -0.00647 -0.01558 181 ARG A C   
1353 O  O   . ARG A 181 ? 0.18021 0.19227 0.19184 -0.00973 -0.00769 -0.01736 181 ARG A O   
1354 C  CB  . ARG A 181 ? 0.18124 0.19804 0.20025 -0.01498 -0.00400 -0.01180 181 ARG A CB  
1355 C  CG  . ARG A 181 ? 0.16235 0.18296 0.18619 -0.01851 -0.00302 -0.01049 181 ARG A CG  
1356 C  CD  . ARG A 181 ? 0.17240 0.18984 0.19577 -0.02048 -0.00122 -0.00698 181 ARG A CD  
1357 N  NE  . ARG A 181 ? 0.18776 0.19763 0.21085 -0.02146 -0.00233 -0.00669 181 ARG A NE  
1358 C  CZ  . ARG A 181 ? 0.19428 0.19860 0.21389 -0.01929 -0.00245 -0.00584 181 ARG A CZ  
1359 N  NH1 . ARG A 181 ? 0.19087 0.19655 0.20692 -0.01638 -0.00161 -0.00512 181 ARG A NH1 
1360 N  NH2 . ARG A 181 ? 0.19961 0.19697 0.21981 -0.02002 -0.00349 -0.00586 181 ARG A NH2 
1361 N  N   . VAL A 182 ? 0.15180 0.16964 0.16315 -0.00801 -0.00536 -0.01447 182 VAL A N   
1362 C  CA  . VAL A 182 ? 0.16561 0.18086 0.17233 -0.00537 -0.00534 -0.01473 182 VAL A CA  
1363 C  C   . VAL A 182 ? 0.16026 0.17533 0.16571 -0.00460 -0.00337 -0.01251 182 VAL A C   
1364 O  O   . VAL A 182 ? 0.17437 0.19281 0.18092 -0.00458 -0.00255 -0.01169 182 VAL A O   
1365 C  CB  . VAL A 182 ? 0.16712 0.18463 0.17217 -0.00351 -0.00677 -0.01596 182 VAL A CB  
1366 C  CG1 . VAL A 182 ? 0.15537 0.16981 0.15532 -0.00139 -0.00657 -0.01605 182 VAL A CG1 
1367 C  CG2 . VAL A 182 ? 0.17136 0.19056 0.17827 -0.00446 -0.00924 -0.01817 182 VAL A CG2 
1368 N  N   . ASN A 183 ? 0.14964 0.16112 0.15299 -0.00385 -0.00270 -0.01185 183 ASN A N   
1369 C  CA  . ASN A 183 ? 0.15125 0.16283 0.15358 -0.00323 -0.00130 -0.00989 183 ASN A CA  
1370 C  C   . ASN A 183 ? 0.14481 0.15415 0.14456 -0.00138 -0.00104 -0.01019 183 ASN A C   
1371 O  O   . ASN A 183 ? 0.17372 0.18098 0.17240 -0.00071 -0.00157 -0.01178 183 ASN A O   
1372 C  CB  . ASN A 183 ? 0.17510 0.18546 0.17892 -0.00477 -0.00067 -0.00788 183 ASN A CB  
1373 C  CG  . ASN A 183 ? 0.17729 0.19060 0.18355 -0.00699 -0.00026 -0.00710 183 ASN A CG  
1374 O  OD1 . ASN A 183 ? 0.17255 0.18945 0.17868 -0.00706 0.00073  -0.00644 183 ASN A OD1 
1375 N  ND2 . ASN A 183 ? 0.17892 0.19091 0.18766 -0.00896 -0.00088 -0.00738 183 ASN A ND2 
1376 N  N   . THR A 184 ? 0.16503 0.17521 0.16386 -0.00067 -0.00014 -0.00893 184 THR A N   
1377 C  CA  . THR A 184 ? 0.17169 0.18073 0.16898 0.00074  0.00042  -0.00901 184 THR A CA  
1378 C  C   . THR A 184 ? 0.15590 0.16441 0.15441 0.00087  0.00087  -0.00748 184 THR A C   
1379 O  O   . THR A 184 ? 0.17729 0.18688 0.17653 -0.00005 0.00084  -0.00592 184 THR A O   
1380 C  CB  . THR A 184 ? 0.17290 0.18333 0.16844 0.00142  0.00081  -0.00891 184 THR A CB  
1381 O  OG1 . THR A 184 ? 0.18631 0.19852 0.18254 0.00082  0.00097  -0.00802 184 THR A OG1 
1382 C  CG2 . THR A 184 ? 0.17331 0.18375 0.16718 0.00187  -0.00000 -0.01009 184 THR A CG2 
1383 N  N   . VAL A 185 ? 0.16249 0.16964 0.16114 0.00216  0.00123  -0.00801 185 VAL A N   
1384 C  CA  . VAL A 185 ? 0.16074 0.16782 0.16112 0.00292  0.00138  -0.00670 185 VAL A CA  
1385 C  C   . VAL A 185 ? 0.16578 0.17517 0.16594 0.00382  0.00231  -0.00680 185 VAL A C   
1386 O  O   . VAL A 185 ? 0.18621 0.19576 0.18492 0.00440  0.00317  -0.00815 185 VAL A O   
1387 C  CB  . VAL A 185 ? 0.17809 0.18192 0.18003 0.00395  0.00109  -0.00743 185 VAL A CB  
1388 C  CG1 . VAL A 185 ? 0.18162 0.18579 0.18592 0.00554  0.00110  -0.00625 185 VAL A CG1 
1389 C  CG2 . VAL A 185 ? 0.20391 0.20514 0.20661 0.00241  0.00011  -0.00676 185 VAL A CG2 
1390 N  N   . HIS A 186 ? 0.16087 0.17229 0.16231 0.00366  0.00208  -0.00526 186 HIS A N   
1391 C  CA  . HIS A 186 ? 0.14936 0.16344 0.15130 0.00381  0.00282  -0.00523 186 HIS A CA  
1392 C  C   . HIS A 186 ? 0.15746 0.17328 0.16265 0.00494  0.00256  -0.00445 186 HIS A C   
1393 O  O   . HIS A 186 ? 0.15367 0.17115 0.15986 0.00447  0.00141  -0.00302 186 HIS A O   
1394 C  CB  . HIS A 186 ? 0.14885 0.16430 0.14959 0.00234  0.00241  -0.00465 186 HIS A CB  
1395 C  CG  . HIS A 186 ? 0.16489 0.17902 0.16326 0.00173  0.00249  -0.00543 186 HIS A CG  
1396 N  ND1 . HIS A 186 ? 0.18299 0.19696 0.17993 0.00154  0.00303  -0.00596 186 HIS A ND1 
1397 C  CD2 . HIS A 186 ? 0.17175 0.18493 0.16941 0.00130  0.00199  -0.00564 186 HIS A CD2 
1398 C  CE1 . HIS A 186 ? 0.17857 0.19151 0.17404 0.00143  0.00261  -0.00652 186 HIS A CE1 
1399 N  NE2 . HIS A 186 ? 0.16174 0.17464 0.15792 0.00122  0.00207  -0.00650 186 HIS A NE2 
1400 N  N   . PRO A 187 ? 0.15846 0.17428 0.16537 0.00661  0.00351  -0.00549 187 PRO A N   
1401 C  CA  . PRO A 187 ? 0.15406 0.17238 0.16509 0.00814  0.00327  -0.00493 187 PRO A CA  
1402 C  C   . PRO A 187 ? 0.16096 0.18385 0.17370 0.00724  0.00371  -0.00449 187 PRO A C   
1403 O  O   . PRO A 187 ? 0.17386 0.19762 0.18500 0.00603  0.00514  -0.00513 187 PRO A O   
1404 C  CB  . PRO A 187 ? 0.17604 0.19345 0.18826 0.01029  0.00475  -0.00694 187 PRO A CB  
1405 C  CG  . PRO A 187 ? 0.20016 0.21358 0.20849 0.00970  0.00497  -0.00831 187 PRO A CG  
1406 C  CD  . PRO A 187 ? 0.17078 0.18459 0.17596 0.00740  0.00472  -0.00751 187 PRO A CD  
1407 N  N   . GLY A 188 ? 0.16594 0.19165 0.18211 0.00776  0.00227  -0.00326 188 GLY A N   
1408 C  CA  . GLY A 188 ? 0.16413 0.19508 0.18398 0.00738  0.00263  -0.00325 188 GLY A CA  
1409 C  C   . GLY A 188 ? 0.16647 0.20001 0.19037 0.00956  0.00447  -0.00445 188 GLY A C   
1410 O  O   . GLY A 188 ? 0.18877 0.21977 0.21116 0.01085  0.00609  -0.00588 188 GLY A O   
1411 N  N   . TYR A 189 ? 0.17207 0.21117 0.20142 0.01007  0.00417  -0.00414 189 TYR A N   
1412 C  CA  . TYR A 189 ? 0.15354 0.19630 0.18765 0.01240  0.00624  -0.00551 189 TYR A CA  
1413 C  C   . TYR A 189 ? 0.17653 0.21694 0.21290 0.01600  0.00507  -0.00575 189 TYR A C   
1414 O  O   . TYR A 189 ? 0.18136 0.22107 0.21916 0.01684  0.00207  -0.00396 189 TYR A O   
1415 C  CB  . TYR A 189 ? 0.18456 0.23496 0.22500 0.01177  0.00622  -0.00516 189 TYR A CB  
1416 C  CG  . TYR A 189 ? 0.18695 0.23952 0.22621 0.00816  0.00784  -0.00509 189 TYR A CG  
1417 C  CD1 . TYR A 189 ? 0.21616 0.26718 0.25187 0.00714  0.01111  -0.00593 189 TYR A CD1 
1418 C  CD2 . TYR A 189 ? 0.21631 0.27229 0.25796 0.00572  0.00591  -0.00415 189 TYR A CD2 
1419 C  CE1 . TYR A 189 ? 0.23629 0.28860 0.27103 0.00377  0.01248  -0.00533 189 TYR A CE1 
1420 C  CE2 . TYR A 189 ? 0.24922 0.30648 0.29037 0.00226  0.00728  -0.00409 189 TYR A CE2 
1421 C  CZ  . TYR A 189 ? 0.25642 0.31152 0.29416 0.00131  0.01056  -0.00444 189 TYR A CZ  
1422 O  OH  . TYR A 189 ? 0.32983 0.38535 0.36698 -0.00223 0.01178  -0.00387 189 TYR A OH  
1423 N  N   . ILE A 190 ? 0.18557 0.22434 0.22186 0.01815  0.00735  -0.00796 190 ILE A N   
1424 C  CA  . ILE A 190 ? 0.19563 0.23058 0.23371 0.02162  0.00644  -0.00875 190 ILE A CA  
1425 C  C   . ILE A 190 ? 0.19958 0.23893 0.24297 0.02478  0.00899  -0.01130 190 ILE A C   
1426 O  O   . ILE A 190 ? 0.21502 0.25723 0.25708 0.02401  0.01235  -0.01319 190 ILE A O   
1427 C  CB  . ILE A 190 ? 0.21244 0.23973 0.24447 0.02114  0.00662  -0.00984 190 ILE A CB  
1428 C  CG1 . ILE A 190 ? 0.20708 0.23099 0.23416 0.01795  0.00470  -0.00761 190 ILE A CG1 
1429 C  CG2 . ILE A 190 ? 0.20680 0.22929 0.24106 0.02451  0.00565  -0.01090 190 ILE A CG2 
1430 C  CD1 . ILE A 190 ? 0.22401 0.24640 0.25244 0.01814  0.00142  -0.00465 190 ILE A CD1 
1431 N  N   . LYS A 191 ? 0.18869 0.22862 0.23797 0.02846  0.00749  -0.01130 191 LYS A N   
1432 C  CA  . LYS A 191 ? 0.21199 0.25642 0.26727 0.03218  0.00995  -0.01415 191 LYS A CA  
1433 C  C   . LYS A 191 ? 0.30091 0.33990 0.35220 0.03371  0.01231  -0.01767 191 LYS A C   
1434 O  O   . LYS A 191 ? 0.31514 0.34661 0.36505 0.03539  0.01047  -0.01810 191 LYS A O   
1435 C  CB  . LYS A 191 ? 0.22959 0.27546 0.29247 0.03613  0.00714  -0.01306 191 LYS A CB  
1436 C  CG  . LYS A 191 ? 0.25609 0.30887 0.32728 0.04039  0.00962  -0.01599 191 LYS A CG  
1437 C  CD  . LYS A 191 ? 0.31694 0.37185 0.39628 0.04429  0.00602  -0.01424 191 LYS A CD  
1438 C  CE  . LYS A 191 ? 0.38212 0.44355 0.47066 0.04936  0.00825  -0.01743 191 LYS A CE  
1439 N  NZ  . LYS A 191 ? 0.38725 0.46101 0.48183 0.04802  0.01047  -0.01772 191 LYS A NZ  
1440 N  N   . THR A 192 ? 0.31510 0.35770 0.36412 0.03282  0.01626  -0.02009 192 THR A N   
1441 C  CA  . THR A 192 ? 0.38454 0.42321 0.42870 0.03389  0.01877  -0.02385 192 THR A CA  
1442 C  C   . THR A 192 ? 0.42315 0.46894 0.47160 0.03667  0.02290  -0.02713 192 THR A C   
1443 O  O   . THR A 192 ? 0.39512 0.44918 0.45023 0.03700  0.02386  -0.02606 192 THR A O   
1444 C  CB  . THR A 192 ? 0.41250 0.44880 0.44795 0.02980  0.01970  -0.02341 192 THR A CB  
1445 O  OG1 . THR A 192 ? 0.42673 0.47008 0.46232 0.02723  0.02207  -0.02203 192 THR A OG1 
1446 C  CG2 . THR A 192 ? 0.40373 0.43379 0.43545 0.02721  0.01600  -0.02054 192 THR A CG2 
1447 N  N   . PRO A 193 ? 0.45114 0.49450 0.49617 0.03865  0.02546  -0.03138 193 PRO A N   
1448 C  CA  . PRO A 193 ? 0.46440 0.51544 0.51268 0.04108  0.03015  -0.03475 193 PRO A CA  
1449 C  C   . PRO A 193 ? 0.45846 0.51756 0.50526 0.03744  0.03348  -0.03300 193 PRO A C   
1450 O  O   . PRO A 193 ? 0.45792 0.52613 0.51132 0.03860  0.03645  -0.03359 193 PRO A O   
1451 C  CB  . PRO A 193 ? 0.48779 0.53316 0.52983 0.04293  0.03180  -0.03960 193 PRO A CB  
1452 C  CG  . PRO A 193 ? 0.48514 0.52129 0.51965 0.03992  0.02837  -0.03808 193 PRO A CG  
1453 C  CD  . PRO A 193 ? 0.47990 0.51378 0.51871 0.03904  0.02413  -0.03370 193 PRO A CD  
1454 N  N   . LEU A 194 ? 0.46488 0.52091 0.50367 0.03303  0.03304  -0.03075 194 LEU A N   
1455 C  CA  . LEU A 194 ? 0.49513 0.55760 0.53253 0.02928  0.03586  -0.02849 194 LEU A CA  
1456 C  C   . LEU A 194 ? 0.46713 0.53616 0.51315 0.02810  0.03477  -0.02543 194 LEU A C   
1457 O  O   . LEU A 194 ? 0.48812 0.56577 0.53833 0.02701  0.03813  -0.02508 194 LEU A O   
1458 C  CB  . LEU A 194 ? 0.55034 0.60719 0.57839 0.02516  0.03457  -0.02616 194 LEU A CB  
1459 C  CG  . LEU A 194 ? 0.60623 0.65822 0.62480 0.02531  0.03583  -0.02875 194 LEU A CG  
1460 C  CD1 . LEU A 194 ? 0.61543 0.66310 0.62638 0.02131  0.03410  -0.02573 194 LEU A CD1 
1461 C  CD2 . LEU A 194 ? 0.63004 0.68818 0.64697 0.02645  0.04121  -0.03152 194 LEU A CD2 
1462 N  N   . VAL A 195 ? 0.46279 0.52815 0.51145 0.02808  0.03007  -0.02320 195 VAL A N   
1463 C  CA  . VAL A 195 ? 0.39946 0.47088 0.45588 0.02701  0.02829  -0.02055 195 VAL A CA  
1464 C  C   . VAL A 195 ? 0.39344 0.47331 0.45999 0.03082  0.03003  -0.02249 195 VAL A C   
1465 O  O   . VAL A 195 ? 0.39031 0.47930 0.46333 0.02939  0.03161  -0.02157 195 VAL A O   
1466 C  CB  . VAL A 195 ? 0.34464 0.41024 0.40084 0.02672  0.02287  -0.01806 195 VAL A CB  
1467 C  CG1 . VAL A 195 ? 0.33706 0.40939 0.40155 0.02637  0.02058  -0.01589 195 VAL A CG1 
1468 C  CG2 . VAL A 195 ? 0.36256 0.42156 0.40992 0.02276  0.02151  -0.01616 195 VAL A CG2 
1469 N  N   . ASP A 196 ? 0.39329 0.47033 0.46194 0.03575  0.02974  -0.02536 196 ASP A N   
1470 C  CA  . ASP A 196 ? 0.42370 0.50866 0.50281 0.04013  0.03109  -0.02739 196 ASP A CA  
1471 C  C   . ASP A 196 ? 0.44542 0.53932 0.52635 0.04011  0.03726  -0.03001 196 ASP A C   
1472 O  O   . ASP A 196 ? 0.44418 0.54756 0.53509 0.04273  0.03900  -0.03124 196 ASP A O   
1473 C  CB  . ASP A 196 ? 0.46383 0.54259 0.54474 0.04572  0.02933  -0.03006 196 ASP A CB  
1474 C  CG  . ASP A 196 ? 0.50150 0.57307 0.58274 0.04616  0.02333  -0.02691 196 ASP A CG  
1475 O  OD1 . ASP A 196 ? 0.50008 0.57446 0.58324 0.04341  0.02049  -0.02313 196 ASP A OD1 
1476 O  OD2 . ASP A 196 ? 0.51616 0.57912 0.59548 0.04911  0.02150  -0.02826 196 ASP A OD2 
1477 N  N   . ASP A 197 ? 0.44519 0.53674 0.51683 0.03726  0.04058  -0.03073 197 ASP A N   
1478 C  CA  . ASP A 197 ? 0.46018 0.56001 0.53188 0.03663  0.04680  -0.03268 197 ASP A CA  
1479 C  C   . ASP A 197 ? 0.44542 0.55259 0.51905 0.03126  0.04849  -0.02904 197 ASP A C   
1480 O  O   . ASP A 197 ? 0.43773 0.55283 0.51229 0.03005  0.05388  -0.02986 197 ASP A O   
1481 C  CB  . ASP A 197 ? 0.46944 0.56321 0.52943 0.03631  0.04948  -0.03516 197 ASP A CB  
1482 C  CG  . ASP A 197 ? 0.48348 0.57350 0.54336 0.04208  0.05008  -0.04052 197 ASP A CG  
1483 O  OD1 . ASP A 197 ? 0.48477 0.58032 0.55435 0.04663  0.05101  -0.04300 197 ASP A OD1 
1484 O  OD2 . ASP A 197 ? 0.47511 0.55662 0.52555 0.04213  0.04945  -0.04242 197 ASP A OD2 
1485 N  N   . LEU A 198 ? 0.43690 0.54163 0.51118 0.02790  0.04419  -0.02517 198 LEU A N   
1486 C  CA  . LEU A 198 ? 0.42298 0.53360 0.49946 0.02257  0.04526  -0.02191 198 LEU A CA  
1487 C  C   . LEU A 198 ? 0.37133 0.48985 0.46001 0.02299  0.04271  -0.02083 198 LEU A C   
1488 O  O   . LEU A 198 ? 0.31519 0.42945 0.40482 0.02294  0.03728  -0.01906 198 LEU A O   
1489 C  CB  . LEU A 198 ? 0.44372 0.54565 0.51119 0.01802  0.04243  -0.01868 198 LEU A CB  
1490 C  CG  . LEU A 198 ? 0.48479 0.58040 0.54043 0.01638  0.04486  -0.01881 198 LEU A CG  
1491 C  CD1 . LEU A 198 ? 0.47840 0.56395 0.52647 0.01409  0.04052  -0.01653 198 LEU A CD1 
1492 C  CD2 . LEU A 198 ? 0.50785 0.60980 0.56250 0.01248  0.04997  -0.01734 198 LEU A CD2 
1493 N  N   . PRO A 199 ? 0.37837 0.50881 0.47649 0.02327  0.04633  -0.02177 199 PRO A N   
1494 C  CA  . PRO A 199 ? 0.34837 0.48716 0.45896 0.02406  0.04338  -0.02102 199 PRO A CA  
1495 C  C   . PRO A 199 ? 0.30509 0.44200 0.41506 0.01876  0.03921  -0.01736 199 PRO A C   
1496 O  O   . PRO A 199 ? 0.32032 0.45631 0.42562 0.01330  0.04112  -0.01539 199 PRO A O   
1497 C  CB  . PRO A 199 ? 0.37803 0.53054 0.49770 0.02393  0.04919  -0.02255 199 PRO A CB  
1498 C  CG  . PRO A 199 ? 0.38704 0.53753 0.49950 0.02598  0.05477  -0.02541 199 PRO A CG  
1499 C  CD  . PRO A 199 ? 0.38465 0.52225 0.48280 0.02317  0.05334  -0.02376 199 PRO A CD  
1500 N  N   . GLY A 200 ? 0.27068 0.40641 0.38488 0.02049  0.03332  -0.01645 200 GLY A N   
1501 C  CA  . GLY A 200 ? 0.22187 0.35616 0.33563 0.01597  0.02901  -0.01364 200 GLY A CA  
1502 C  C   . GLY A 200 ? 0.20972 0.33123 0.31156 0.01402  0.02607  -0.01204 200 GLY A C   
1503 O  O   . GLY A 200 ? 0.21015 0.32974 0.31122 0.01101  0.02203  -0.01016 200 GLY A O   
1504 N  N   . ALA A 201 ? 0.21041 0.32370 0.30317 0.01556  0.02805  -0.01299 201 ALA A N   
1505 C  CA  . ALA A 201 ? 0.20881 0.31090 0.29085 0.01361  0.02567  -0.01160 201 ALA A CA  
1506 C  C   . ALA A 201 ? 0.19458 0.29206 0.27651 0.01535  0.01986  -0.01057 201 ALA A C   
1507 O  O   . ALA A 201 ? 0.18227 0.27573 0.26027 0.01221  0.01682  -0.00875 201 ALA A O   
1508 C  CB  . ALA A 201 ? 0.23574 0.33107 0.30935 0.01548  0.02850  -0.01321 201 ALA A CB  
1509 N  N   . GLU A 202 ? 0.20562 0.30337 0.29159 0.02043  0.01833  -0.01168 202 GLU A N   
1510 C  CA  . GLU A 202 ? 0.17780 0.27030 0.26254 0.02211  0.01297  -0.01015 202 GLU A CA  
1511 C  C   . GLU A 202 ? 0.16674 0.26459 0.25632 0.01979  0.00909  -0.00821 202 GLU A C   
1512 O  O   . GLU A 202 ? 0.16994 0.26271 0.25457 0.01808  0.00533  -0.00642 202 GLU A O   
1513 C  CB  . GLU A 202 ? 0.18289 0.27481 0.27206 0.02809  0.01205  -0.01142 202 GLU A CB  
1514 C  CG  . GLU A 202 ? 0.21716 0.30399 0.30550 0.02989  0.00649  -0.00918 202 GLU A CG  
1515 C  CD  . GLU A 202 ? 0.28938 0.37263 0.38051 0.03567  0.00548  -0.01010 202 GLU A CD  
1516 O  OE1 . GLU A 202 ? 0.30851 0.39326 0.40242 0.03867  0.00917  -0.01314 202 GLU A OE1 
1517 O  OE2 . GLU A 202 ? 0.30047 0.37922 0.39090 0.03724  0.00100  -0.00776 202 GLU A OE2 
1518 N  N   . GLU A 203 ? 0.16894 0.27748 0.26814 0.01949  0.01004  -0.00875 203 GLU A N   
1519 C  CA  . GLU A 203 ? 0.15970 0.27400 0.26392 0.01699  0.00607  -0.00731 203 GLU A CA  
1520 C  C   . GLU A 203 ? 0.15666 0.26707 0.25424 0.01111  0.00579  -0.00632 203 GLU A C   
1521 O  O   . GLU A 203 ? 0.16543 0.27388 0.26073 0.00934  0.00139  -0.00510 203 GLU A O   
1522 C  CB  . GLU A 203 ? 0.16085 0.28825 0.27752 0.01730  0.00754  -0.00833 203 GLU A CB  
1523 C  CG  . GLU A 203 ? 0.16456 0.29890 0.28711 0.01410  0.00323  -0.00722 203 GLU A CG  
1524 C  CD  . GLU A 203 ? 0.20282 0.35090 0.33913 0.01517  0.00384  -0.00822 203 GLU A CD  
1525 O  OE1 . GLU A 203 ? 0.18386 0.33866 0.32625 0.01314  -0.00022 -0.00760 203 GLU A OE1 
1526 O  OE2 . GLU A 203 ? 0.23689 0.38960 0.37817 0.01805  0.00838  -0.00987 203 GLU A OE2 
1527 N  N   . ALA A 204 ? 0.16633 0.27517 0.26024 0.00818  0.01041  -0.00685 204 ALA A N   
1528 C  CA  . ALA A 204 ? 0.16234 0.26650 0.25004 0.00293  0.01021  -0.00589 204 ALA A CA  
1529 C  C   . ALA A 204 ? 0.15439 0.24802 0.23225 0.00330  0.00748  -0.00514 204 ALA A C   
1530 O  O   . ALA A 204 ? 0.18711 0.27798 0.26180 0.00038  0.00458  -0.00446 204 ALA A O   
1531 C  CB  . ALA A 204 ? 0.17409 0.27773 0.25910 0.00025  0.01564  -0.00607 204 ALA A CB  
1532 N  N   . MET A 205 ? 0.13885 0.22681 0.21206 0.00678  0.00845  -0.00553 205 MET A N   
1533 C  CA  . MET A 205 ? 0.13872 0.21737 0.20330 0.00707  0.00624  -0.00481 205 MET A CA  
1534 C  C   . MET A 205 ? 0.15697 0.23539 0.22233 0.00828  0.00122  -0.00362 205 MET A C   
1535 O  O   . MET A 205 ? 0.18348 0.25576 0.24208 0.00713  -0.00084 -0.00279 205 MET A O   
1536 C  CB  . MET A 205 ? 0.16962 0.24297 0.23020 0.01033  0.00838  -0.00571 205 MET A CB  
1537 C  CG  . MET A 205 ? 0.19197 0.26421 0.24908 0.00898  0.01297  -0.00671 205 MET A CG  
1538 S  SD  . MET A 205 ? 0.26602 0.33455 0.32090 0.01354  0.01510  -0.00871 205 MET A SD  
1539 C  CE  . MET A 205 ? 0.30926 0.37653 0.35807 0.01120  0.01995  -0.00951 205 MET A CE  
1540 N  N   . SER A 206 ? 0.16094 0.24616 0.23426 0.01073  -0.00071 -0.00346 206 SER A N   
1541 C  CA  . SER A 206 ? 0.15952 0.24499 0.23359 0.01237  -0.00573 -0.00192 206 SER A CA  
1542 C  C   . SER A 206 ? 0.15407 0.24447 0.23011 0.00902  -0.00903 -0.00151 206 SER A C   
1543 O  O   . SER A 206 ? 0.16803 0.25893 0.24364 0.01004  -0.01351 -0.00013 206 SER A O   
1544 C  CB  . SER A 206 ? 0.17794 0.26804 0.25988 0.01734  -0.00672 -0.00183 206 SER A CB  
1545 O  OG  . SER A 206 ? 0.18725 0.27276 0.26782 0.02055  -0.00367 -0.00286 206 SER A OG  
1546 N  N   . GLN A 207 ? 0.15514 0.24924 0.23343 0.00503  -0.00712 -0.00262 207 GLN A N   
1547 C  CA  . GLN A 207 ? 0.18653 0.28443 0.26633 0.00145  -0.01048 -0.00274 207 GLN A CA  
1548 C  C   . GLN A 207 ? 0.16969 0.26008 0.23991 0.00022  -0.01319 -0.00217 207 GLN A C   
1549 O  O   . GLN A 207 ? 0.15723 0.23977 0.21996 -0.00001 -0.01106 -0.00212 207 GLN A O   
1550 C  CB  . GLN A 207 ? 0.21817 0.31897 0.30078 -0.00321 -0.00762 -0.00392 207 GLN A CB  
1551 C  CG  . GLN A 207 ? 0.21978 0.32900 0.31189 -0.00266 -0.00420 -0.00448 207 GLN A CG  
1552 C  CD  . GLN A 207 ? 0.28891 0.40816 0.39107 -0.00046 -0.00741 -0.00450 207 GLN A CD  
1553 O  OE1 . GLN A 207 ? 0.35528 0.47945 0.46372 0.00346  -0.00582 -0.00469 207 GLN A OE1 
1554 N  NE2 . GLN A 207 ? 0.28393 0.40654 0.38791 -0.00280 -0.01210 -0.00454 207 GLN A NE2 
1555 N  N   . ARG A 208 ? 0.17288 0.26628 0.24339 -0.00060 -0.01791 -0.00188 208 ARG A N   
1556 C  CA  . ARG A 208 ? 0.14446 0.23163 0.20565 -0.00144 -0.02039 -0.00143 208 ARG A CA  
1557 C  C   . ARG A 208 ? 0.16224 0.24376 0.21754 -0.00523 -0.01818 -0.00302 208 ARG A C   
1558 O  O   . ARG A 208 ? 0.17827 0.25312 0.22539 -0.00522 -0.01819 -0.00283 208 ARG A O   
1559 C  CB  . ARG A 208 ? 0.15111 0.24348 0.21343 -0.00209 -0.02586 -0.00123 208 ARG A CB  
1560 C  CG  . ARG A 208 ? 0.18042 0.27872 0.24884 0.00183  -0.02900 0.00065  208 ARG A CG  
1561 C  CD  . ARG A 208 ? 0.17853 0.27086 0.24159 0.00581  -0.02963 0.00332  208 ARG A CD  
1562 N  NE  . ARG A 208 ? 0.17173 0.26936 0.23997 0.00938  -0.03387 0.00543  208 ARG A NE  
1563 C  CZ  . ARG A 208 ? 0.16660 0.26027 0.23104 0.01272  -0.03614 0.00843  208 ARG A CZ  
1564 N  NH1 . ARG A 208 ? 0.16128 0.24595 0.21687 0.01266  -0.03430 0.00957  208 ARG A NH1 
1565 N  NH2 . ARG A 208 ? 0.19833 0.29710 0.26815 0.01606  -0.04035 0.01047  208 ARG A NH2 
1566 N  N   . THR A 209 ? 0.17278 0.25694 0.23245 -0.00848 -0.01629 -0.00448 209 THR A N   
1567 C  CA  . THR A 209 ? 0.16996 0.24824 0.22492 -0.01186 -0.01409 -0.00575 209 THR A CA  
1568 C  C   . THR A 209 ? 0.19424 0.26582 0.24442 -0.01040 -0.01002 -0.00506 209 THR A C   
1569 O  O   . THR A 209 ? 0.19980 0.26548 0.24500 -0.01240 -0.00859 -0.00577 209 THR A O   
1570 C  CB  . THR A 209 ? 0.21705 0.29961 0.27852 -0.01582 -0.01298 -0.00687 209 THR A CB  
1571 O  OG1 . THR A 209 ? 0.23673 0.32568 0.30600 -0.01447 -0.01056 -0.00602 209 THR A OG1 
1572 C  CG2 . THR A 209 ? 0.23145 0.31898 0.29602 -0.01846 -0.01751 -0.00835 209 THR A CG2 
1573 N  N   . LYS A 210 ? 0.16801 0.24032 0.21974 -0.00687 -0.00842 -0.00390 210 LYS A N   
1574 C  CA  . LYS A 210 ? 0.17162 0.23779 0.21849 -0.00520 -0.00517 -0.00348 210 LYS A CA  
1575 C  C   . LYS A 210 ? 0.15828 0.22053 0.20051 -0.00216 -0.00685 -0.00249 210 LYS A C   
1576 O  O   . LYS A 210 ? 0.15596 0.21229 0.19141 -0.00267 -0.00689 -0.00252 210 LYS A O   
1577 C  CB  . LYS A 210 ? 0.19172 0.26119 0.24349 -0.00380 -0.00160 -0.00343 210 LYS A CB  
1578 C  CG  . LYS A 210 ? 0.23894 0.31186 0.29465 -0.00727 0.00089  -0.00389 210 LYS A CG  
1579 C  CD  . LYS A 210 ? 0.30687 0.37249 0.35582 -0.00990 0.00262  -0.00391 210 LYS A CD  
1580 C  CE  . LYS A 210 ? 0.36567 0.43369 0.41811 -0.01372 0.00505  -0.00375 210 LYS A CE  
1581 N  NZ  . LYS A 210 ? 0.40724 0.46753 0.45306 -0.01556 0.00680  -0.00327 210 LYS A NZ  
1582 N  N   . THR A 211 ? 0.15099 0.21648 0.19710 0.00099  -0.00829 -0.00148 211 THR A N   
1583 C  CA  . THR A 211 ? 0.14102 0.20242 0.18313 0.00364  -0.01000 0.00001  211 THR A CA  
1584 C  C   . THR A 211 ? 0.14342 0.20827 0.18636 0.00401  -0.01448 0.00126  211 THR A C   
1585 O  O   . THR A 211 ? 0.15092 0.22159 0.20052 0.00586  -0.01623 0.00183  211 THR A O   
1586 C  CB  . THR A 211 ? 0.16520 0.22590 0.21035 0.00736  -0.00836 0.00040  211 THR A CB  
1587 O  OG1 . THR A 211 ? 0.15902 0.21745 0.20312 0.00688  -0.00428 -0.00102 211 THR A OG1 
1588 C  CG2 . THR A 211 ? 0.18280 0.23762 0.22333 0.00949  -0.00984 0.00209  211 THR A CG2 
1589 N  N   . PRO A 212 ? 0.14519 0.20713 0.18158 0.00249  -0.01648 0.00168  212 PRO A N   
1590 C  CA  . PRO A 212 ? 0.14851 0.21421 0.18467 0.00254  -0.02096 0.00282  212 PRO A CA  
1591 C  C   . PRO A 212 ? 0.15109 0.21783 0.18964 0.00630  -0.02334 0.00559  212 PRO A C   
1592 O  O   . PRO A 212 ? 0.15370 0.22580 0.19522 0.00698  -0.02719 0.00656  212 PRO A O   
1593 C  CB  . PRO A 212 ? 0.16585 0.22696 0.19300 0.00058  -0.02147 0.00265  212 PRO A CB  
1594 C  CG  . PRO A 212 ? 0.16485 0.22226 0.19020 -0.00150 -0.01786 0.00042  212 PRO A CG  
1595 C  CD  . PRO A 212 ? 0.14456 0.20083 0.17399 0.00031  -0.01467 0.00063  212 PRO A CD  
1596 N  N   . MET A 213 ? 0.15232 0.21393 0.18993 0.00881  -0.02142 0.00682  213 MET A N   
1597 C  CA  . MET A 213 ? 0.16620 0.22772 0.20665 0.01263  -0.02370 0.00948  213 MET A CA  
1598 C  C   . MET A 213 ? 0.16755 0.23590 0.21800 0.01513  -0.02430 0.00884  213 MET A C   
1599 O  O   . MET A 213 ? 0.16970 0.23922 0.22367 0.01860  -0.02707 0.01100  213 MET A O   
1600 C  CB  . MET A 213 ? 0.16743 0.22125 0.20503 0.01441  -0.02138 0.01041  213 MET A CB  
1601 C  CG  . MET A 213 ? 0.17472 0.22277 0.20381 0.01290  -0.02193 0.01234  213 MET A CG  
1602 S  SD  . MET A 213 ? 0.20152 0.24109 0.22922 0.01504  -0.02002 0.01373  213 MET A SD  
1603 C  CE  . MET A 213 ? 0.23962 0.27451 0.25806 0.01258  -0.02086 0.01648  213 MET A CE  
1604 N  N   . GLY A 214 ? 0.15591 0.22874 0.21117 0.01353  -0.02168 0.00611  214 GLY A N   
1605 C  CA  . GLY A 214 ? 0.14937 0.23038 0.21486 0.01549  -0.02207 0.00536  214 GLY A CA  
1606 C  C   . GLY A 214 ? 0.14922 0.22930 0.21958 0.01937  -0.01918 0.00476  214 GLY A C   
1607 O  O   . GLY A 214 ? 0.15661 0.24350 0.23595 0.02208  -0.01969 0.00433  214 GLY A O   
1608 N  N   . HIS A 215 ? 0.18282 0.25485 0.24764 0.01988  -0.01640 0.00452  215 HIS A N   
1609 C  CA  . HIS A 215 ? 0.16243 0.23231 0.23041 0.02333  -0.01347 0.00329  215 HIS A CA  
1610 C  C   . HIS A 215 ? 0.18839 0.25051 0.24868 0.02144  -0.01018 0.00224  215 HIS A C   
1611 O  O   . HIS A 215 ? 0.18842 0.24670 0.24174 0.01837  -0.01080 0.00306  215 HIS A O   
1612 C  CB  . HIS A 215 ? 0.16767 0.23474 0.23804 0.02800  -0.01637 0.00534  215 HIS A CB  
1613 C  CG  . HIS A 215 ? 0.18832 0.24684 0.25059 0.02744  -0.01854 0.00811  215 HIS A CG  
1614 N  ND1 . HIS A 215 ? 0.21222 0.26231 0.26880 0.02701  -0.01616 0.00765  215 HIS A ND1 
1615 C  CD2 . HIS A 215 ? 0.20812 0.26569 0.26700 0.02702  -0.02276 0.01143  215 HIS A CD2 
1616 C  CE1 . HIS A 215 ? 0.21840 0.26287 0.26896 0.02615  -0.01854 0.01064  215 HIS A CE1 
1617 N  NE2 . HIS A 215 ? 0.22350 0.27225 0.27486 0.02616  -0.02243 0.01307  215 HIS A NE2 
1618 N  N   . ILE A 216 ? 0.17400 0.23432 0.23569 0.02341  -0.00675 0.00019  216 ILE A N   
1619 C  CA  . ILE A 216 ? 0.17625 0.22954 0.23104 0.02202  -0.00400 -0.00096 216 ILE A CA  
1620 C  C   . ILE A 216 ? 0.17661 0.22211 0.22893 0.02461  -0.00517 -0.00011 216 ILE A C   
1621 O  O   . ILE A 216 ? 0.18208 0.22724 0.23821 0.02777  -0.00775 0.00139  216 ILE A O   
1622 C  CB  . ILE A 216 ? 0.19347 0.24935 0.24972 0.02185  0.00057  -0.00390 216 ILE A CB  
1623 C  CG1 . ILE A 216 ? 0.20323 0.26152 0.26593 0.02635  0.00204  -0.00574 216 ILE A CG1 
1624 C  CG2 . ILE A 216 ? 0.21961 0.28255 0.27831 0.01863  0.00160  -0.00410 216 ILE A CG2 
1625 C  CD1 . ILE A 216 ? 0.23003 0.29146 0.29337 0.02616  0.00695  -0.00870 216 ILE A CD1 
1626 N  N   . GLY A 217 ? 0.15825 0.19721 0.20422 0.02307  -0.00351 -0.00090 217 GLY A N   
1627 C  CA  . GLY A 217 ? 0.18563 0.21666 0.22879 0.02441  -0.00456 -0.00008 217 GLY A CA  
1628 C  C   . GLY A 217 ? 0.20381 0.23241 0.24990 0.02778  -0.00258 -0.00286 217 GLY A C   
1629 O  O   . GLY A 217 ? 0.20524 0.23908 0.25594 0.02959  -0.00040 -0.00524 217 GLY A O   
1630 N  N   . GLU A 218 ? 0.18430 0.20494 0.22782 0.02855  -0.00329 -0.00270 218 GLU A N   
1631 C  CA  . GLU A 218 ? 0.21109 0.22793 0.25653 0.03161  -0.00165 -0.00588 218 GLU A CA  
1632 C  C   . GLU A 218 ? 0.19951 0.20952 0.23874 0.02934  -0.00060 -0.00734 218 GLU A C   
1633 O  O   . GLU A 218 ? 0.19190 0.19954 0.22639 0.02597  -0.00163 -0.00521 218 GLU A O   
1634 C  CB  . GLU A 218 ? 0.24648 0.25956 0.29683 0.03563  -0.00427 -0.00450 218 GLU A CB  
1635 C  CG  . GLU A 218 ? 0.31631 0.32288 0.36314 0.03396  -0.00741 -0.00039 218 GLU A CG  
1636 C  CD  . GLU A 218 ? 0.40412 0.40296 0.45363 0.03720  -0.00938 0.00048  218 GLU A CD  
1637 O  OE1 . GLU A 218 ? 0.43480 0.43302 0.48925 0.04124  -0.00838 -0.00267 218 GLU A OE1 
1638 O  OE2 . GLU A 218 ? 0.42900 0.42215 0.47562 0.03566  -0.01183 0.00435  218 GLU A OE2 
1639 N  N   . PRO A 219 ? 0.20233 0.20969 0.24151 0.03109  0.00149  -0.01129 219 PRO A N   
1640 C  CA  . PRO A 219 ? 0.21697 0.21876 0.25033 0.02872  0.00224  -0.01308 219 PRO A CA  
1641 C  C   . PRO A 219 ? 0.20760 0.20202 0.23880 0.02693  -0.00036 -0.01053 219 PRO A C   
1642 O  O   . PRO A 219 ? 0.21104 0.20364 0.23747 0.02356  -0.00023 -0.01041 219 PRO A O   
1643 C  CB  . PRO A 219 ? 0.20404 0.20395 0.23861 0.03179  0.00430  -0.01792 219 PRO A CB  
1644 C  CG  . PRO A 219 ? 0.21906 0.22717 0.25854 0.03444  0.00635  -0.01903 219 PRO A CG  
1645 C  CD  . PRO A 219 ? 0.21243 0.22361 0.25650 0.03494  0.00374  -0.01476 219 PRO A CD  
1646 N  N   . ASN A 220 ? 0.20754 0.19785 0.24227 0.02903  -0.00269 -0.00830 220 ASN A N   
1647 C  CA  . ASN A 220 ? 0.21590 0.19914 0.24838 0.02681  -0.00490 -0.00527 220 ASN A CA  
1648 C  C   . ASN A 220 ? 0.20836 0.19469 0.23714 0.02302  -0.00571 -0.00144 220 ASN A C   
1649 O  O   . ASN A 220 ? 0.21629 0.19835 0.24194 0.02004  -0.00640 0.00025  220 ASN A O   
1650 C  CB  . ASN A 220 ? 0.25488 0.23291 0.29168 0.02989  -0.00741 -0.00286 220 ASN A CB  
1651 C  CG  . ASN A 220 ? 0.29223 0.26349 0.33172 0.03288  -0.00703 -0.00673 220 ASN A CG  
1652 O  OD1 . ASN A 220 ? 0.31516 0.28416 0.35204 0.03164  -0.00534 -0.01078 220 ASN A OD1 
1653 N  ND2 . ASN A 220 ? 0.31908 0.28714 0.36380 0.03704  -0.00876 -0.00575 220 ASN A ND2 
1654 N  N   . ASP A 221 ? 0.17316 0.16701 0.20232 0.02288  -0.00544 -0.00044 221 ASP A N   
1655 C  CA  . ASP A 221 ? 0.19675 0.19348 0.22192 0.01933  -0.00594 0.00225  221 ASP A CA  
1656 C  C   . ASP A 221 ? 0.20414 0.20014 0.22493 0.01622  -0.00422 0.00030  221 ASP A C   
1657 O  O   . ASP A 221 ? 0.22105 0.21595 0.23856 0.01330  -0.00471 0.00226  221 ASP A O   
1658 C  CB  . ASP A 221 ? 0.18631 0.19098 0.21288 0.01957  -0.00590 0.00270  221 ASP A CB  
1659 C  CG  . ASP A 221 ? 0.20299 0.20961 0.23383 0.02226  -0.00836 0.00527  221 ASP A CG  
1660 O  OD1 . ASP A 221 ? 0.23173 0.23399 0.26198 0.02254  -0.01072 0.00863  221 ASP A OD1 
1661 O  OD2 . ASP A 221 ? 0.18953 0.20235 0.22452 0.02402  -0.00802 0.00412  221 ASP A OD2 
1662 N  N   . ILE A 222 ? 0.17851 0.17536 0.19917 0.01691  -0.00218 -0.00355 222 ILE A N   
1663 C  CA  . ILE A 222 ? 0.17453 0.17063 0.19110 0.01427  -0.00107 -0.00523 222 ILE A CA  
1664 C  C   . ILE A 222 ? 0.20818 0.19754 0.22412 0.01357  -0.00173 -0.00623 222 ILE A C   
1665 O  O   . ILE A 222 ? 0.20805 0.19633 0.22138 0.01071  -0.00189 -0.00592 222 ILE A O   
1666 C  CB  . ILE A 222 ? 0.18614 0.18613 0.20177 0.01491  0.00116  -0.00840 222 ILE A CB  
1667 C  CG1 . ILE A 222 ? 0.18186 0.18832 0.19896 0.01510  0.00174  -0.00717 222 ILE A CG1 
1668 C  CG2 . ILE A 222 ? 0.20574 0.20511 0.21695 0.01245  0.00182  -0.00982 222 ILE A CG2 
1669 C  CD1 . ILE A 222 ? 0.18874 0.19725 0.20412 0.01259  0.00051  -0.00424 222 ILE A CD1 
1670 N  N   . ALA A 223 ? 0.19646 0.18122 0.21530 0.01609  -0.00223 -0.00748 223 ALA A N   
1671 C  CA  . ALA A 223 ? 0.19045 0.16799 0.20913 0.01510  -0.00313 -0.00849 223 ALA A CA  
1672 C  C   . ALA A 223 ? 0.19878 0.17373 0.21660 0.01195  -0.00461 -0.00433 223 ALA A C   
1673 O  O   . ALA A 223 ? 0.19109 0.16357 0.20739 0.00907  -0.00473 -0.00492 223 ALA A O   
1674 C  CB  . ALA A 223 ? 0.20570 0.17798 0.22816 0.01864  -0.00370 -0.01019 223 ALA A CB  
1675 N  N   . TYR A 224 ? 0.18547 0.16165 0.20411 0.01229  -0.00571 -0.00007 224 TYR A N   
1676 C  CA  . TYR A 224 ? 0.19819 0.17151 0.21557 0.00938  -0.00688 0.00415  224 TYR A CA  
1677 C  C   . TYR A 224 ? 0.19441 0.17200 0.20837 0.00569  -0.00583 0.00456  224 TYR A C   
1678 O  O   . TYR A 224 ? 0.19545 0.17044 0.20862 0.00260  -0.00595 0.00602  224 TYR A O   
1679 C  CB  . TYR A 224 ? 0.20667 0.18067 0.22484 0.01081  -0.00851 0.00868  224 TYR A CB  
1680 C  CG  . TYR A 224 ? 0.23202 0.19968 0.25395 0.01399  -0.01022 0.00966  224 TYR A CG  
1681 C  CD1 . TYR A 224 ? 0.27187 0.23097 0.29482 0.01304  -0.01100 0.01013  224 TYR A CD1 
1682 C  CD2 . TYR A 224 ? 0.24674 0.21704 0.27176 0.01798  -0.01118 0.01005  224 TYR A CD2 
1683 C  CE1 . TYR A 224 ? 0.32308 0.27547 0.34973 0.01629  -0.01275 0.01100  224 TYR A CE1 
1684 C  CE2 . TYR A 224 ? 0.28709 0.25173 0.31613 0.02144  -0.01290 0.01089  224 TYR A CE2 
1685 C  CZ  . TYR A 224 ? 0.32256 0.27783 0.35225 0.02074  -0.01369 0.01136  224 TYR A CZ  
1686 O  OH  . TYR A 224 ? 0.39262 0.34146 0.42661 0.02458  -0.01558 0.01215  224 TYR A OH  
1687 N  N   . ILE A 225 ? 0.19543 0.17955 0.20777 0.00589  -0.00475 0.00332  225 ILE A N   
1688 C  CA  . ILE A 225 ? 0.19561 0.18335 0.20520 0.00290  -0.00383 0.00333  225 ILE A CA  
1689 C  C   . ILE A 225 ? 0.18178 0.16787 0.19128 0.00165  -0.00324 -0.00003 225 ILE A C   
1690 O  O   . ILE A 225 ? 0.19507 0.18190 0.20378 -0.00117 -0.00300 0.00035  225 ILE A O   
1691 C  CB  . ILE A 225 ? 0.18890 0.18308 0.19689 0.00338  -0.00309 0.00297  225 ILE A CB  
1692 C  CG1 . ILE A 225 ? 0.22355 0.22105 0.22899 0.00067  -0.00230 0.00321  225 ILE A CG1 
1693 C  CG2 . ILE A 225 ? 0.19203 0.18801 0.20071 0.00546  -0.00215 -0.00044 225 ILE A CG2 
1694 C  CD1 . ILE A 225 ? 0.24278 0.23983 0.24709 -0.00155 -0.00262 0.00662  225 ILE A CD1 
1695 N  N   . CYS A 226 ? 0.18051 0.16459 0.19094 0.00371  -0.00308 -0.00343 226 CYS A N   
1696 C  CA  . CYS A 226 ? 0.16923 0.15160 0.17909 0.00249  -0.00302 -0.00677 226 CYS A CA  
1697 C  C   . CYS A 226 ? 0.19702 0.17364 0.20868 0.00032  -0.00413 -0.00616 226 CYS A C   
1698 O  O   . CYS A 226 ? 0.20127 0.17806 0.21276 -0.00222 -0.00436 -0.00755 226 CYS A O   
1699 C  CB  . CYS A 226 ? 0.18541 0.16713 0.19496 0.00522  -0.00245 -0.01079 226 CYS A CB  
1700 S  SG  . CYS A 226 ? 0.19837 0.18695 0.20536 0.00653  -0.00082 -0.01180 226 CYS A SG  
1701 N  N   . VAL A 227 ? 0.18793 0.15938 0.20167 0.00117  -0.00501 -0.00395 227 VAL A N   
1702 C  CA  . VAL A 227 ? 0.20005 0.16538 0.21560 -0.00145 -0.00605 -0.00270 227 VAL A CA  
1703 C  C   . VAL A 227 ? 0.20633 0.17486 0.22108 -0.00541 -0.00560 0.00060  227 VAL A C   
1704 O  O   . VAL A 227 ? 0.20604 0.17346 0.22192 -0.00866 -0.00576 -0.00013 227 VAL A O   
1705 C  CB  . VAL A 227 ? 0.20978 0.16849 0.22757 0.00043  -0.00723 -0.00015 227 VAL A CB  
1706 C  CG1 . VAL A 227 ? 0.22159 0.17358 0.24105 -0.00305 -0.00824 0.00248  227 VAL A CG1 
1707 C  CG2 . VAL A 227 ? 0.21455 0.16997 0.23396 0.00451  -0.00745 -0.00429 227 VAL A CG2 
1708 N  N   . TYR A 228 ? 0.18313 0.15616 0.19609 -0.00525 -0.00499 0.00399  228 TYR A N   
1709 C  CA  . TYR A 228 ? 0.19519 0.17216 0.20698 -0.00866 -0.00411 0.00676  228 TYR A CA  
1710 C  C   . TYR A 228 ? 0.17811 0.15986 0.18993 -0.01032 -0.00328 0.00351  228 TYR A C   
1711 O  O   . TYR A 228 ? 0.19183 0.17441 0.20505 -0.01370 -0.00291 0.00406  228 TYR A O   
1712 C  CB  . TYR A 228 ? 0.18453 0.16607 0.19366 -0.00759 -0.00367 0.00974  228 TYR A CB  
1713 C  CG  . TYR A 228 ? 0.18928 0.17664 0.19654 -0.01034 -0.00224 0.01105  228 TYR A CG  
1714 C  CD1 . TYR A 228 ? 0.18242 0.16901 0.18949 -0.01368 -0.00167 0.01466  228 TYR A CD1 
1715 C  CD2 . TYR A 228 ? 0.16711 0.16058 0.17295 -0.00958 -0.00130 0.00864  228 TYR A CD2 
1716 C  CE1 . TYR A 228 ? 0.19321 0.18599 0.19879 -0.01606 0.00011  0.01544  228 TYR A CE1 
1717 C  CE2 . TYR A 228 ? 0.19840 0.19718 0.20294 -0.01163 0.00010  0.00930  228 TYR A CE2 
1718 C  CZ  . TYR A 228 ? 0.18634 0.18514 0.19078 -0.01471 0.00091  0.01250  228 TYR A CZ  
1719 O  OH  . TYR A 228 ? 0.20871 0.21361 0.21206 -0.01650 0.00273  0.01266  228 TYR A OH  
1720 N  N   . LEU A 229 ? 0.17823 0.16327 0.18882 -0.00800 -0.00305 0.00025  229 LEU A N   
1721 C  CA  . LEU A 229 ? 0.18881 0.17844 0.19918 -0.00906 -0.00265 -0.00242 229 LEU A CA  
1722 C  C   . LEU A 229 ? 0.19256 0.17938 0.20494 -0.01051 -0.00371 -0.00544 229 LEU A C   
1723 O  O   . LEU A 229 ? 0.20426 0.19478 0.21767 -0.01246 -0.00378 -0.00668 229 LEU A O   
1724 C  CB  . LEU A 229 ? 0.17040 0.16353 0.17849 -0.00631 -0.00225 -0.00454 229 LEU A CB  
1725 C  CG  . LEU A 229 ? 0.19556 0.19277 0.20185 -0.00549 -0.00134 -0.00235 229 LEU A CG  
1726 C  CD1 . LEU A 229 ? 0.18760 0.18695 0.19217 -0.00302 -0.00102 -0.00433 229 LEU A CD1 
1727 C  CD2 . LEU A 229 ? 0.20004 0.20167 0.20623 -0.00770 -0.00053 -0.00123 229 LEU A CD2 
1728 N  N   . ALA A 230 ? 0.18750 0.16812 0.20067 -0.00944 -0.00470 -0.00703 230 ALA A N   
1729 C  CA  . ALA A 230 ? 0.20052 0.17781 0.21544 -0.01106 -0.00601 -0.01035 230 ALA A CA  
1730 C  C   . ALA A 230 ? 0.21203 0.18651 0.23032 -0.01511 -0.00643 -0.00817 230 ALA A C   
1731 O  O   . ALA A 230 ? 0.20883 0.18305 0.22935 -0.01774 -0.00747 -0.01053 230 ALA A O   
1732 C  CB  . ALA A 230 ? 0.19454 0.16585 0.20902 -0.00834 -0.00678 -0.01345 230 ALA A CB  
1733 N  N   A SER A 231 ? 0.21565 0.18849 0.23428 -0.01593 -0.00569 -0.00351 231 SER A N   
1734 N  N   B SER A 231 ? 0.21518 0.18777 0.23386 -0.01591 -0.00573 -0.00355 231 SER A N   
1735 C  CA  A SER A 231 ? 0.20482 0.17390 0.22625 -0.01986 -0.00584 -0.00053 231 SER A CA  
1736 C  CA  B SER A 231 ? 0.20547 0.17440 0.22704 -0.01994 -0.00591 -0.00077 231 SER A CA  
1737 C  C   A SER A 231 ? 0.20978 0.18595 0.23240 -0.02349 -0.00450 0.00118  231 SER A C   
1738 C  C   B SER A 231 ? 0.20935 0.18550 0.23204 -0.02348 -0.00456 0.00095  231 SER A C   
1739 O  O   A SER A 231 ? 0.20329 0.18660 0.22400 -0.02237 -0.00330 0.00128  231 SER A O   
1740 O  O   B SER A 231 ? 0.20346 0.18678 0.22427 -0.02232 -0.00340 0.00090  231 SER A O   
1741 C  CB  A SER A 231 ? 0.20197 0.16613 0.22252 -0.01889 -0.00575 0.00420  231 SER A CB  
1742 C  CB  B SER A 231 ? 0.20537 0.16904 0.22632 -0.01928 -0.00585 0.00403  231 SER A CB  
1743 O  OG  A SER A 231 ? 0.20558 0.16696 0.22796 -0.02305 -0.00546 0.00831  231 SER A OG  
1744 O  OG  B SER A 231 ? 0.19194 0.16139 0.21046 -0.01946 -0.00435 0.00784  231 SER A OG  
1745 N  N   . ASN A 232 ? 0.21313 0.18724 0.23936 -0.02791 -0.00464 0.00235  232 ASN A N   
1746 C  CA  . ASN A 232 ? 0.21746 0.19866 0.24559 -0.03163 -0.00291 0.00443  232 ASN A CA  
1747 C  C   . ASN A 232 ? 0.22241 0.20635 0.24752 -0.03166 -0.00080 0.00956  232 ASN A C   
1748 O  O   . ASN A 232 ? 0.19078 0.18200 0.21653 -0.03389 0.00119  0.01094  232 ASN A O   
1749 C  CB  . ASN A 232 ? 0.20788 0.18607 0.24105 -0.03679 -0.00342 0.00483  232 ASN A CB  
1750 C  CG  . ASN A 232 ? 0.22771 0.20431 0.26364 -0.03700 -0.00580 -0.00085 232 ASN A CG  
1751 O  OD1 . ASN A 232 ? 0.23442 0.21564 0.26890 -0.03418 -0.00652 -0.00476 232 ASN A OD1 
1752 N  ND2 . ASN A 232 ? 0.22507 0.19476 0.26459 -0.04035 -0.00718 -0.00130 232 ASN A ND2 
1753 N  N   . GLU A 233 ? 0.20609 0.18500 0.22786 -0.02897 -0.00125 0.01210  233 GLU A N   
1754 C  CA  . GLU A 233 ? 0.19836 0.18061 0.21626 -0.02842 0.00028  0.01637  233 GLU A CA  
1755 C  C   . GLU A 233 ? 0.20794 0.19920 0.22385 -0.02672 0.00164  0.01431  233 GLU A C   
1756 O  O   . GLU A 233 ? 0.23625 0.23243 0.24973 -0.02765 0.00346  0.01703  233 GLU A O   
1757 C  CB  . GLU A 233 ? 0.19828 0.17490 0.21325 -0.02484 -0.00108 0.01844  233 GLU A CB  
1758 C  CG  . GLU A 233 ? 0.21034 0.17728 0.22693 -0.02591 -0.00251 0.02129  233 GLU A CG  
1759 C  CD  . GLU A 233 ? 0.26323 0.22492 0.27824 -0.02137 -0.00430 0.02213  233 GLU A CD  
1760 O  OE1 . GLU A 233 ? 0.27558 0.24197 0.28800 -0.01801 -0.00422 0.02126  233 GLU A OE1 
1761 O  OE2 . GLU A 233 ? 0.30074 0.25359 0.31767 -0.02125 -0.00585 0.02357  233 GLU A OE2 
1762 N  N   . SER A 234 ? 0.17794 0.17114 0.19441 -0.02413 0.00076  0.00960  234 SER A N   
1763 C  CA  . SER A 234 ? 0.17085 0.17116 0.18545 -0.02202 0.00166  0.00756  234 SER A CA  
1764 C  C   . SER A 234 ? 0.17077 0.17703 0.18859 -0.02352 0.00215  0.00465  234 SER A C   
1765 O  O   . SER A 234 ? 0.17637 0.18676 0.19342 -0.02119 0.00206  0.00192  234 SER A O   
1766 C  CB  . SER A 234 ? 0.18828 0.18684 0.20072 -0.01781 0.00042  0.00505  234 SER A CB  
1767 O  OG  . SER A 234 ? 0.19906 0.19448 0.21342 -0.01720 -0.00107 0.00152  234 SER A OG  
1768 N  N   . LYS A 235 ? 0.17686 0.18384 0.19854 -0.02747 0.00265  0.00554  235 LYS A N   
1769 C  CA  . LYS A 235 ? 0.17133 0.18426 0.19750 -0.02924 0.00271  0.00278  235 LYS A CA  
1770 C  C   . LYS A 235 ? 0.19389 0.21569 0.21998 -0.02833 0.00461  0.00220  235 LYS A C   
1771 O  O   . LYS A 235 ? 0.19154 0.21882 0.22150 -0.02864 0.00426  -0.00055 235 LYS A O   
1772 C  CB  . LYS A 235 ? 0.17468 0.18683 0.20559 -0.03432 0.00314  0.00448  235 LYS A CB  
1773 C  CG  . LYS A 235 ? 0.20777 0.22221 0.23803 -0.03739 0.00603  0.00939  235 LYS A CG  
1774 C  CD  . LYS A 235 ? 0.24445 0.25647 0.27954 -0.04276 0.00625  0.01136  235 LYS A CD  
1775 C  CE  . LYS A 235 ? 0.32542 0.34335 0.36145 -0.04668 0.00972  0.01536  235 LYS A CE  
1776 N  NZ  . LYS A 235 ? 0.33276 0.34965 0.36234 -0.04548 0.01141  0.01956  235 LYS A NZ  
1777 N  N   . PHE A 236 ? 0.17243 0.19596 0.19451 -0.02719 0.00643  0.00447  236 PHE A N   
1778 C  CA  . PHE A 236 ? 0.16491 0.19601 0.18644 -0.02571 0.00815  0.00322  236 PHE A CA  
1779 C  C   . PHE A 236 ? 0.17641 0.20649 0.19391 -0.02140 0.00721  0.00141  236 PHE A C   
1780 O  O   . PHE A 236 ? 0.19076 0.22580 0.20725 -0.01980 0.00845  0.00026  236 PHE A O   
1781 C  CB  . PHE A 236 ? 0.16224 0.19694 0.18192 -0.02794 0.01116  0.00663  236 PHE A CB  
1782 C  CG  . PHE A 236 ? 0.15961 0.20331 0.18035 -0.02735 0.01358  0.00490  236 PHE A CG  
1783 C  CD1 . PHE A 236 ? 0.15867 0.20869 0.18567 -0.02809 0.01396  0.00226  236 PHE A CD1 
1784 C  CD2 . PHE A 236 ? 0.17100 0.21705 0.18671 -0.02599 0.01538  0.00575  236 PHE A CD2 
1785 C  CE1 . PHE A 236 ? 0.17670 0.23507 0.20521 -0.02702 0.01626  0.00044  236 PHE A CE1 
1786 C  CE2 . PHE A 236 ? 0.16033 0.21426 0.17687 -0.02514 0.01776  0.00367  236 PHE A CE2 
1787 C  CZ  . PHE A 236 ? 0.16989 0.23012 0.19316 -0.02557 0.01839  0.00104  236 PHE A CZ  
1788 N  N   . ALA A 237 ? 0.15702 0.18085 0.17242 -0.01953 0.00521  0.00103  237 ALA A N   
1789 C  CA  . ALA A 237 ? 0.15900 0.18189 0.17098 -0.01594 0.00449  -0.00038 237 ALA A CA  
1790 C  C   . ALA A 237 ? 0.16912 0.19213 0.18258 -0.01415 0.00283  -0.00376 237 ALA A C   
1791 O  O   . ALA A 237 ? 0.16880 0.18808 0.18332 -0.01445 0.00126  -0.00477 237 ALA A O   
1792 C  CB  . ALA A 237 ? 0.16827 0.18526 0.17723 -0.01479 0.00358  0.00136  237 ALA A CB  
1793 N  N   . THR A 238 ? 0.14542 0.17244 0.15867 -0.01224 0.00307  -0.00552 238 THR A N   
1794 C  CA  . THR A 238 ? 0.14367 0.17041 0.15725 -0.01022 0.00129  -0.00810 238 THR A CA  
1795 C  C   . THR A 238 ? 0.17446 0.20288 0.18594 -0.00755 0.00162  -0.00894 238 THR A C   
1796 O  O   . THR A 238 ? 0.16958 0.20145 0.18116 -0.00747 0.00318  -0.00867 238 THR A O   
1797 C  CB  . THR A 238 ? 0.15324 0.18359 0.17141 -0.01151 0.00031  -0.00978 238 THR A CB  
1798 O  OG1 . THR A 238 ? 0.16990 0.19832 0.18726 -0.00988 -0.00204 -0.01187 238 THR A OG1 
1799 C  CG2 . THR A 238 ? 0.15898 0.19625 0.18011 -0.01106 0.00142  -0.01057 238 THR A CG2 
1800 N  N   . GLY A 239 ? 0.15926 0.18497 0.16862 -0.00546 0.00024  -0.01001 239 GLY A N   
1801 C  CA  . GLY A 239 ? 0.16522 0.19140 0.17271 -0.00319 0.00036  -0.01058 239 GLY A CA  
1802 C  C   . GLY A 239 ? 0.19634 0.22061 0.20084 -0.00281 0.00142  -0.00938 239 GLY A C   
1803 O  O   . GLY A 239 ? 0.18973 0.21440 0.19306 -0.00140 0.00167  -0.00995 239 GLY A O   
1804 N  N   . SER A 240 ? 0.19184 0.21393 0.19537 -0.00398 0.00178  -0.00780 240 SER A N   
1805 C  CA  . SER A 240 ? 0.18790 0.20908 0.18910 -0.00383 0.00244  -0.00648 240 SER A CA  
1806 C  C   . SER A 240 ? 0.17309 0.19078 0.17284 -0.00281 0.00174  -0.00613 240 SER A C   
1807 O  O   . SER A 240 ? 0.18258 0.19802 0.18275 -0.00252 0.00107  -0.00662 240 SER A O   
1808 C  CB  . SER A 240 ? 0.23384 0.25574 0.23509 -0.00574 0.00326  -0.00441 240 SER A CB  
1809 O  OG  . SER A 240 ? 0.30387 0.33001 0.30604 -0.00670 0.00454  -0.00472 240 SER A OG  
1810 N  N   . GLU A 241 ? 0.17518 0.19291 0.17336 -0.00232 0.00197  -0.00554 241 GLU A N   
1811 C  CA  . GLU A 241 ? 0.15740 0.17316 0.15495 -0.00142 0.00160  -0.00513 241 GLU A CA  
1812 C  C   . GLU A 241 ? 0.14037 0.15578 0.13796 -0.00185 0.00137  -0.00321 241 GLU A C   
1813 O  O   . GLU A 241 ? 0.17064 0.18786 0.16714 -0.00257 0.00147  -0.00227 241 GLU A O   
1814 C  CB  . GLU A 241 ? 0.21601 0.23237 0.21250 -0.00078 0.00171  -0.00582 241 GLU A CB  
1815 C  CG  . GLU A 241 ? 0.25905 0.27489 0.25517 -0.00004 0.00167  -0.00715 241 GLU A CG  
1816 C  CD  . GLU A 241 ? 0.27736 0.29473 0.27335 -0.00001 0.00186  -0.00809 241 GLU A CD  
1817 O  OE1 . GLU A 241 ? 0.31298 0.33252 0.30937 -0.00074 0.00231  -0.00804 241 GLU A OE1 
1818 O  OE2 . GLU A 241 ? 0.23167 0.24797 0.22718 0.00076  0.00167  -0.00889 241 GLU A OE2 
1819 N  N   . PHE A 242 ? 0.16037 0.17350 0.15900 -0.00114 0.00096  -0.00271 242 PHE A N   
1820 C  CA  . PHE A 242 ? 0.15824 0.17049 0.15741 -0.00109 0.00033  -0.00060 242 PHE A CA  
1821 C  C   . PHE A 242 ? 0.16262 0.17520 0.16279 0.00048  -0.00001 -0.00072 242 PHE A C   
1822 O  O   . PHE A 242 ? 0.18613 0.19746 0.18742 0.00167  0.00035  -0.00201 242 PHE A O   
1823 C  CB  . PHE A 242 ? 0.17402 0.18300 0.17451 -0.00151 0.00002  0.00013  242 PHE A CB  
1824 C  CG  . PHE A 242 ? 0.19832 0.20787 0.19862 -0.00361 0.00047  0.00066  242 PHE A CG  
1825 C  CD1 . PHE A 242 ? 0.18731 0.19774 0.18821 -0.00416 0.00086  -0.00139 242 PHE A CD1 
1826 C  CD2 . PHE A 242 ? 0.22794 0.23775 0.22748 -0.00506 0.00052  0.00337  242 PHE A CD2 
1827 C  CE1 . PHE A 242 ? 0.19864 0.21083 0.20034 -0.00616 0.00142  -0.00099 242 PHE A CE1 
1828 C  CE2 . PHE A 242 ? 0.22703 0.23834 0.22671 -0.00731 0.00144  0.00395  242 PHE A CE2 
1829 C  CZ  . PHE A 242 ? 0.19389 0.20667 0.19509 -0.00782 0.00194  0.00164  242 PHE A CZ  
1830 N  N   . VAL A 243 ? 0.15760 0.17249 0.15736 0.00038  -0.00063 0.00038  243 VAL A N   
1831 C  CA  . VAL A 243 ? 0.16172 0.17839 0.16317 0.00144  -0.00099 0.00013  243 VAL A CA  
1832 C  C   . VAL A 243 ? 0.16850 0.18506 0.17186 0.00260  -0.00234 0.00210  243 VAL A C   
1833 O  O   . VAL A 243 ? 0.17337 0.19009 0.17534 0.00201  -0.00348 0.00420  243 VAL A O   
1834 C  CB  . VAL A 243 ? 0.18404 0.20358 0.18423 0.00042  -0.00123 -0.00041 243 VAL A CB  
1835 C  CG1 . VAL A 243 ? 0.19557 0.21755 0.19835 0.00099  -0.00172 -0.00060 243 VAL A CG1 
1836 C  CG2 . VAL A 243 ? 0.19972 0.21867 0.19831 -0.00031 -0.00011 -0.00223 243 VAL A CG2 
1837 N  N   . VAL A 244 ? 0.16442 0.18102 0.17091 0.00440  -0.00219 0.00150  244 VAL A N   
1838 C  CA  . VAL A 244 ? 0.16476 0.18143 0.17414 0.00621  -0.00362 0.00313  244 VAL A CA  
1839 C  C   . VAL A 244 ? 0.16199 0.18276 0.17490 0.00737  -0.00337 0.00204  244 VAL A C   
1840 O  O   . VAL A 244 ? 0.17421 0.19492 0.18934 0.00873  -0.00189 0.00033  244 VAL A O   
1841 C  CB  . VAL A 244 ? 0.16315 0.17514 0.17385 0.00765  -0.00348 0.00313  244 VAL A CB  
1842 C  CG1 . VAL A 244 ? 0.16877 0.18015 0.18281 0.00998  -0.00520 0.00497  244 VAL A CG1 
1843 C  CG2 . VAL A 244 ? 0.18982 0.19811 0.19755 0.00573  -0.00344 0.00405  244 VAL A CG2 
1844 N  N   . ASP A 245 ? 0.14999 0.17477 0.16330 0.00655  -0.00465 0.00276  245 ASP A N   
1845 C  CA  . ASP A 245 ? 0.15830 0.18748 0.17491 0.00653  -0.00402 0.00140  245 ASP A CA  
1846 C  C   . ASP A 245 ? 0.15219 0.18615 0.17206 0.00691  -0.00633 0.00252  245 ASP A C   
1847 O  O   . ASP A 245 ? 0.16236 0.20057 0.18500 0.00601  -0.00604 0.00145  245 ASP A O   
1848 C  CB  . ASP A 245 ? 0.16781 0.19722 0.18169 0.00411  -0.00268 -0.00010 245 ASP A CB  
1849 C  CG  . ASP A 245 ? 0.18111 0.21143 0.19203 0.00218  -0.00424 0.00029  245 ASP A CG  
1850 O  OD1 . ASP A 245 ? 0.15788 0.18868 0.16764 0.00238  -0.00623 0.00191  245 ASP A OD1 
1851 O  OD2 . ASP A 245 ? 0.17465 0.20492 0.18400 0.00047  -0.00345 -0.00109 245 ASP A OD2 
1852 N  N   . GLY A 246 ? 0.14664 0.18013 0.16637 0.00806  -0.00878 0.00481  246 GLY A N   
1853 C  CA  . GLY A 246 ? 0.14806 0.18654 0.17101 0.00873  -0.01153 0.00597  246 GLY A CA  
1854 C  C   . GLY A 246 ? 0.16205 0.20397 0.18279 0.00605  -0.01282 0.00537  246 GLY A C   
1855 O  O   . GLY A 246 ? 0.15677 0.20385 0.18085 0.00614  -0.01513 0.00561  246 GLY A O   
1856 N  N   . GLY A 247 ? 0.16449 0.20373 0.17992 0.00377  -0.01158 0.00436  247 GLY A N   
1857 C  CA  . GLY A 247 ? 0.16845 0.20985 0.18128 0.00129  -0.01252 0.00307  247 GLY A CA  
1858 C  C   . GLY A 247 ? 0.15743 0.19963 0.17204 -0.00047 -0.01068 0.00050  247 GLY A C   
1859 O  O   . GLY A 247 ? 0.15443 0.19788 0.16748 -0.00258 -0.01157 -0.00095 247 GLY A O   
1860 N  N   . TYR A 248 ? 0.15232 0.19369 0.16998 0.00028  -0.00821 -0.00009 248 TYR A N   
1861 C  CA  . TYR A 248 ? 0.14022 0.18249 0.15976 -0.00152 -0.00645 -0.00181 248 TYR A CA  
1862 C  C   . TYR A 248 ? 0.15594 0.19508 0.17092 -0.00374 -0.00610 -0.00321 248 TYR A C   
1863 O  O   . TYR A 248 ? 0.16743 0.20793 0.18350 -0.00590 -0.00660 -0.00450 248 TYR A O   
1864 C  CB  . TYR A 248 ? 0.14784 0.18856 0.16891 -0.00029 -0.00348 -0.00201 248 TYR A CB  
1865 C  CG  . TYR A 248 ? 0.14523 0.18733 0.16851 -0.00208 -0.00138 -0.00300 248 TYR A CG  
1866 C  CD1 . TYR A 248 ? 0.14004 0.17879 0.15994 -0.00418 -0.00051 -0.00376 248 TYR A CD1 
1867 C  CD2 . TYR A 248 ? 0.13783 0.18466 0.16683 -0.00162 -0.00015 -0.00301 248 TYR A CD2 
1868 C  CE1 . TYR A 248 ? 0.14479 0.18406 0.16641 -0.00607 0.00140  -0.00404 248 TYR A CE1 
1869 C  CE2 . TYR A 248 ? 0.13806 0.18635 0.16892 -0.00372 0.00212  -0.00345 248 TYR A CE2 
1870 C  CZ  . TYR A 248 ? 0.14938 0.19353 0.17632 -0.00607 0.00278  -0.00373 248 TYR A CZ  
1871 O  OH  . TYR A 248 ? 0.18815 0.23290 0.21651 -0.00835 0.00496  -0.00358 248 TYR A OH  
1872 N  N   . THR A 249 ? 0.16466 0.19960 0.17506 -0.00322 -0.00525 -0.00315 249 THR A N   
1873 C  CA  . THR A 249 ? 0.16846 0.20043 0.17523 -0.00467 -0.00463 -0.00470 249 THR A CA  
1874 C  C   . THR A 249 ? 0.16800 0.20068 0.17140 -0.00556 -0.00649 -0.00546 249 THR A C   
1875 O  O   . THR A 249 ? 0.21880 0.24940 0.21963 -0.00658 -0.00612 -0.00731 249 THR A O   
1876 C  CB  . THR A 249 ? 0.18205 0.21003 0.18615 -0.00370 -0.00277 -0.00463 249 THR A CB  
1877 O  OG1 . THR A 249 ? 0.18120 0.20869 0.18379 -0.00243 -0.00313 -0.00331 249 THR A OG1 
1878 C  CG2 . THR A 249 ? 0.16984 0.19678 0.17592 -0.00314 -0.00083 -0.00445 249 THR A CG2 
1879 N  N   . ALA A 250 ? 0.14509 0.18064 0.14826 -0.00505 -0.00853 -0.00416 250 ALA A N   
1880 C  CA  . ALA A 250 ? 0.16133 0.19806 0.16031 -0.00594 -0.01031 -0.00483 250 ALA A CA  
1881 C  C   . ALA A 250 ? 0.18516 0.22439 0.18524 -0.00784 -0.01218 -0.00700 250 ALA A C   
1882 O  O   . ALA A 250 ? 0.16677 0.20651 0.16277 -0.00882 -0.01344 -0.00860 250 ALA A O   
1883 C  CB  . ALA A 250 ? 0.16877 0.20742 0.16637 -0.00476 -0.01212 -0.00209 250 ALA A CB  
1884 N  N   . GLN A 251 ? 0.16929 0.21048 0.17483 -0.00852 -0.01241 -0.00721 251 GLN A N   
1885 C  CA  . GLN A 251 ? 0.15127 0.19457 0.15877 -0.01091 -0.01411 -0.00946 251 GLN A CA  
1886 C  C   . GLN A 251 ? 0.16554 0.20532 0.17480 -0.01251 -0.01202 -0.01106 251 GLN A C   
1887 O  O   . GLN A 251 ? 0.18720 0.22416 0.19705 -0.01151 -0.00940 -0.00995 251 GLN A O   
1888 C  CB  . GLN A 251 ? 0.15107 0.20032 0.16438 -0.01100 -0.01628 -0.00836 251 GLN A CB  
1889 C  CG  . GLN A 251 ? 0.16641 0.21694 0.18568 -0.00983 -0.01419 -0.00669 251 GLN A CG  
1890 C  CD  . GLN A 251 ? 0.18018 0.23761 0.20605 -0.00946 -0.01634 -0.00580 251 GLN A CD  
1891 O  OE1 . GLN A 251 ? 0.21110 0.27221 0.23674 -0.00970 -0.01983 -0.00586 251 GLN A OE1 
1892 N  NE2 . GLN A 251 ? 0.18754 0.24718 0.21931 -0.00873 -0.01428 -0.00504 251 GLN A NE2 
1893 O  OXT . GLN A 251 ? 0.16780 0.20736 0.17787 -0.01487 -0.01310 -0.01334 251 GLN A OXT 
1894 P  PA  . NAP B .   ? 0.50438 0.53707 0.50210 0.02757  0.03246  -0.03753 301 NAP A PA  
1895 O  O1A . NAP B .   ? 0.52582 0.56026 0.53305 0.02847  0.03108  -0.03522 301 NAP A O1A 
1896 O  O2A . NAP B .   ? 0.51094 0.54270 0.50640 0.03085  0.03446  -0.04331 301 NAP A O2A 
1897 O  O5B . NAP B .   ? 0.39673 0.42238 0.38895 0.02490  0.02824  -0.03585 301 NAP A O5B 
1898 C  C5B . NAP B .   ? 0.31339 0.33288 0.30908 0.02541  0.02433  -0.03587 301 NAP A C5B 
1899 C  C4B . NAP B .   ? 0.26953 0.28278 0.25977 0.02550  0.02240  -0.03932 301 NAP A C4B 
1900 O  O4B . NAP B .   ? 0.26502 0.27817 0.24748 0.02276  0.02182  -0.03823 301 NAP A O4B 
1901 C  C3B . NAP B .   ? 0.27308 0.28555 0.26152 0.02862  0.02446  -0.04520 301 NAP A C3B 
1902 O  O3B . NAP B .   ? 0.28001 0.28498 0.26825 0.02909  0.02134  -0.04802 301 NAP A O3B 
1903 C  C2B . NAP B .   ? 0.26662 0.28236 0.24618 0.02728  0.02671  -0.04606 301 NAP A C2B 
1904 O  O2B . NAP B .   ? 0.25923 0.27273 0.23425 0.02933  0.02753  -0.05196 301 NAP A O2B 
1905 C  C1B . NAP B .   ? 0.24910 0.26177 0.22504 0.02382  0.02316  -0.04262 301 NAP A C1B 
1906 N  N9A . NAP B .   ? 0.22487 0.24041 0.19326 0.02168  0.02413  -0.04067 301 NAP A N9A 
1907 C  C8A . NAP B .   ? 0.24389 0.26503 0.21112 0.02070  0.02726  -0.03764 301 NAP A C8A 
1908 N  N7A . NAP B .   ? 0.25280 0.27433 0.21226 0.01876  0.02710  -0.03594 301 NAP A N7A 
1909 C  C5A . NAP B .   ? 0.23079 0.24736 0.18632 0.01859  0.02348  -0.03824 301 NAP A C5A 
1910 C  C6A . NAP B .   ? 0.24648 0.26137 0.19401 0.01714  0.02116  -0.03794 301 NAP A C6A 
1911 N  N6A . NAP B .   ? 0.23645 0.25379 0.17773 0.01571  0.02220  -0.03476 301 NAP A N6A 
1912 N  N1A . NAP B .   ? 0.23092 0.24143 0.17742 0.01717  0.01748  -0.04094 301 NAP A N1A 
1913 C  C2A . NAP B .   ? 0.23027 0.23754 0.18297 0.01836  0.01644  -0.04376 301 NAP A C2A 
1914 N  N3A . NAP B .   ? 0.20665 0.21436 0.16660 0.01997  0.01830  -0.04399 301 NAP A N3A 
1915 C  C4A . NAP B .   ? 0.21816 0.23102 0.17928 0.02013  0.02175  -0.04123 301 NAP A C4A 
1916 O  O3  . NAP B .   ? 0.51422 0.55301 0.50775 0.02479  0.03582  -0.03487 301 NAP A O3  
1917 P  PN  . NAP B .   ? 0.55770 0.59952 0.54234 0.02399  0.03964  -0.03620 301 NAP A PN  
1918 O  O1N . NAP B .   ? 0.55172 0.58968 0.52842 0.02072  0.03734  -0.03320 301 NAP A O1N 
1919 O  O2N . NAP B .   ? 0.50279 0.54422 0.48494 0.02742  0.04158  -0.04215 301 NAP A O2N 
1920 O  O5D . NAP B .   ? 0.58377 0.63443 0.57351 0.02297  0.04384  -0.03367 301 NAP A O5D 
1921 C  C5D . NAP B .   ? 0.62163 0.67539 0.60570 0.01952  0.04631  -0.03022 301 NAP A C5D 
1922 C  C4D . NAP B .   ? 0.64438 0.70165 0.63545 0.01685  0.04614  -0.02563 301 NAP A C4D 
1923 O  O4D . NAP B .   ? 0.65554 0.72003 0.65630 0.01875  0.04872  -0.02699 301 NAP A O4D 
1924 C  C3D . NAP B .   ? 0.66035 0.72056 0.64736 0.01280  0.04869  -0.02136 301 NAP A C3D 
1925 O  O3D . NAP B .   ? 0.67150 0.72486 0.65177 0.01049  0.04518  -0.01849 301 NAP A O3D 
1926 C  C2D . NAP B .   ? 0.65879 0.72507 0.65623 0.01132  0.04967  -0.01899 301 NAP A C2D 
1927 O  O2D . NAP B .   ? 0.65597 0.71861 0.65556 0.00857  0.04589  -0.01528 301 NAP A O2D 
1928 C  C1D . NAP B .   ? 0.65792 0.72652 0.66401 0.01548  0.04899  -0.02274 301 NAP A C1D 
1929 N  N1N . NAP B .   ? 0.66308 0.74149 0.67736 0.01660  0.05325  -0.02392 301 NAP A N1N 
1930 C  C2N . NAP B .   ? 0.66692 0.75188 0.67942 0.01411  0.05831  -0.02248 301 NAP A C2N 
1931 C  C3N . NAP B .   ? 0.66003 0.75530 0.68113 0.01507  0.06260  -0.02374 301 NAP A C3N 
1932 C  C7N . NAP B .   ? 0.66174 0.76434 0.68066 0.01180  0.06850  -0.02179 301 NAP A C7N 
1933 O  O7N . NAP B .   ? 0.67519 0.77512 0.68312 0.01056  0.07065  -0.02134 301 NAP A O7N 
1934 N  N7N . NAP B .   ? 0.64815 0.76013 0.67708 0.01008  0.07111  -0.02037 301 NAP A N7N 
1935 C  C4N . NAP B .   ? 0.65395 0.75266 0.68546 0.01898  0.06137  -0.02648 301 NAP A C4N 
1936 C  C5N . NAP B .   ? 0.65072 0.74193 0.68329 0.02158  0.05599  -0.02758 301 NAP A C5N 
1937 C  C6N . NAP B .   ? 0.65662 0.73786 0.68054 0.02016  0.05216  -0.02627 301 NAP A C6N 
1938 P  P2B . NAP B .   ? 0.27656 0.29594 0.24379 0.02953  0.03185  -0.05370 301 NAP A P2B 
1939 O  O1X . NAP B .   ? 0.31417 0.34126 0.28510 0.02937  0.03581  -0.05032 301 NAP A O1X 
1940 O  O2X . NAP B .   ? 0.29849 0.31602 0.26477 0.03302  0.03326  -0.06068 301 NAP A O2X 
1941 O  O3X . NAP B .   ? 0.25988 0.27754 0.21834 0.02650  0.02961  -0.05201 301 NAP A O3X 
1942 O  O1  . PG4 C .   ? 0.47093 0.40121 0.50977 -0.04067 -0.00943 0.01178  302 PG4 A O1  
1943 C  C1  . PG4 C .   ? 0.44580 0.38378 0.48008 -0.03679 -0.00798 0.01313  302 PG4 A C1  
1944 C  C2  . PG4 C .   ? 0.44507 0.39094 0.47825 -0.04008 -0.00544 0.01809  302 PG4 A C2  
1945 O  O2  . PG4 C .   ? 0.43516 0.38902 0.46402 -0.03637 -0.00421 0.01821  302 PG4 A O2  
1946 C  C3  . PG4 C .   ? 0.43401 0.39531 0.46127 -0.03906 -0.00167 0.02239  302 PG4 A C3  
1947 C  C4  . PG4 C .   ? 0.44713 0.41657 0.47795 -0.04238 -0.00042 0.01951  302 PG4 A C4  
1948 O  O3  . PG4 C .   ? 0.48650 0.46024 0.51790 -0.04700 0.00216  0.02421  302 PG4 A O3  
1949 C  C5  . PG4 C .   ? 0.50863 0.48515 0.54608 -0.05203 0.00265  0.02273  302 PG4 A C5  
1950 C  C6  . PG4 C .   ? 0.50924 0.49685 0.54856 -0.05117 0.00347  0.01825  302 PG4 A C6  
1951 O  O4  . PG4 C .   ? 0.52922 0.51568 0.57286 -0.05134 0.00097  0.01272  302 PG4 A O4  
1952 C  C7  . PG4 C .   ? 0.53009 0.52691 0.57818 -0.05317 0.00174  0.00989  302 PG4 A C7  
1953 C  C8  . PG4 C .   ? 0.52965 0.52711 0.57911 -0.05058 -0.00124 0.00356  302 PG4 A C8  
1954 O  O5  . PG4 C .   ? 0.53229 0.53257 0.57680 -0.04495 -0.00140 0.00159  302 PG4 A O5  
1955 MG MG  . MG  D .   ? 0.16351 0.19620 0.17609 0.00000  0.00000  -0.00988 303 MG  A MG  
1956 MG MG  . MG  E .   ? 0.44225 0.47907 0.42541 0.03207  0.04096  -0.04939 304 MG  A MG  
1957 C  C1  . EDO F .   ? 0.54560 0.48821 0.59807 -0.04915 -0.02476 -0.03471 305 EDO A C1  
1958 O  O1  . EDO F .   ? 0.56614 0.50005 0.61598 -0.04694 -0.02708 -0.04078 305 EDO A O1  
1959 C  C2  . EDO F .   ? 0.52764 0.48276 0.57856 -0.04780 -0.02515 -0.03659 305 EDO A C2  
1960 O  O2  . EDO F .   ? 0.52267 0.48624 0.57918 -0.05209 -0.02396 -0.03275 305 EDO A O2  
1961 O  O   . HOH G .   ? 0.31168 0.43001 0.41730 0.01228  -0.00940 -0.00320 401 HOH A O   
1962 O  O   . HOH G .   ? 0.59536 0.48554 0.59230 0.06917  0.01088  -0.15450 402 HOH A O   
1963 O  O   . HOH G .   ? 0.29651 0.33861 0.31444 -0.00069 -0.02381 -0.02437 403 HOH A O   
1964 O  O   . HOH G .   ? 0.37092 0.42418 0.40251 -0.00431 0.01759  -0.00324 404 HOH A O   
1965 O  O   . HOH G .   ? 0.52425 0.51820 0.42969 0.00290  0.00647  0.01998  405 HOH A O   
1966 O  O   . HOH G .   ? 0.52662 0.40850 0.56593 -0.00581 -0.01862 0.00185  406 HOH A O   
1967 O  O   . HOH G .   ? 0.36708 0.42102 0.40362 -0.00880 0.01106  -0.00277 407 HOH A O   
1968 O  O   . HOH G .   ? 0.18870 0.21710 0.17213 -0.00746 0.02851  0.00457  408 HOH A O   
1969 O  O   . HOH G .   ? 0.29186 0.34109 0.30236 -0.03240 0.04482  0.01939  409 HOH A O   
1970 O  O   . HOH G .   ? 0.40350 0.49349 0.49545 0.03807  0.01953  -0.01885 410 HOH A O   
1971 O  O   . HOH G .   ? 0.32949 0.48119 0.46519 0.00092  -0.00000 -0.00694 411 HOH A O   
1972 O  O   . HOH G .   ? 0.31318 0.32316 0.28828 0.00670  0.00842  -0.01322 412 HOH A O   
1973 O  O   . HOH G .   ? 0.26968 0.27262 0.23923 0.03486  0.02680  -0.06752 413 HOH A O   
1974 O  O   . HOH G .   ? 0.32628 0.34389 0.30858 0.01794  0.02121  -0.02943 414 HOH A O   
1975 O  O   . HOH G .   ? 0.40908 0.30113 0.44989 -0.02398 -0.02078 -0.02711 415 HOH A O   
1976 O  O   . HOH G .   ? 0.24914 0.25517 0.25468 -0.02352 0.00524  0.01746  416 HOH A O   
1977 O  O   . HOH G .   ? 0.27877 0.23195 0.30920 -0.03311 -0.02874 -0.05236 417 HOH A O   
1978 O  O   . HOH G .   ? 0.18208 0.21709 0.20345 -0.01218 0.00505  -0.00373 418 HOH A O   
1979 O  O   . HOH G .   ? 0.48277 0.41336 0.46975 0.04566  0.00841  -0.11004 419 HOH A O   
1980 O  O   . HOH G .   ? 0.58150 0.46672 0.62088 0.00772  -0.01987 0.01007  420 HOH A O   
1981 O  O   . HOH G .   ? 0.28723 0.31114 0.28682 -0.00765 -0.00378 -0.01017 421 HOH A O   
1982 O  O   . HOH G .   ? 0.27876 0.27650 0.22815 0.01517  0.00590  -0.04868 422 HOH A O   
1983 O  O   . HOH G .   ? 0.44250 0.47014 0.45307 -0.05864 0.05032  0.04092  423 HOH A O   
1984 O  O   . HOH G .   ? 0.37010 0.38995 0.32422 0.00422  -0.03537 -0.03739 424 HOH A O   
1985 O  O   . HOH G .   ? 0.44802 0.39937 0.39722 0.01826  -0.00809 -0.10203 425 HOH A O   
1986 O  O   . HOH G .   ? 0.52899 0.52512 0.53869 -0.02842 -0.04633 -0.07055 426 HOH A O   
1987 O  O   . HOH G .   ? 0.37033 0.39000 0.36891 0.06297  0.04795  -0.09426 427 HOH A O   
1988 O  O   . HOH G .   ? 0.47609 0.45000 0.52141 0.03621  -0.01465 0.00717  428 HOH A O   
1989 O  O   . HOH G .   ? 0.30886 0.45792 0.44625 0.02385  0.01852  -0.01355 429 HOH A O   
1990 O  O   . HOH G .   ? 0.45184 0.46054 0.35385 0.00961  -0.00009 -0.00991 430 HOH A O   
1991 O  O   . HOH G .   ? 0.27675 0.24839 0.28225 -0.01460 -0.00468 0.02760  431 HOH A O   
1992 O  O   . HOH G .   ? 0.41866 0.41140 0.43979 0.05108  0.02351  -0.06405 432 HOH A O   
1993 O  O   . HOH G .   ? 0.23474 0.31003 0.31609 0.03045  -0.00563 -0.00229 433 HOH A O   
1994 O  O   . HOH G .   ? 0.27457 0.33948 0.29351 -0.01236 -0.02664 -0.00841 434 HOH A O   
1995 O  O   . HOH G .   ? 0.42888 0.39079 0.46918 0.03755  -0.00307 -0.02111 435 HOH A O   
1996 O  O   . HOH G .   ? 0.24687 0.27172 0.26037 -0.04476 0.03733  0.02682  436 HOH A O   
1997 O  O   . HOH G .   ? 0.31994 0.32794 0.21912 0.01777  0.00901  -0.06030 437 HOH A O   
1998 O  O   . HOH G .   ? 0.34260 0.37382 0.38236 -0.03158 0.00066  -0.00607 438 HOH A O   
1999 O  O   . HOH G .   ? 0.38726 0.46915 0.45725 0.02515  -0.03312 0.01295  439 HOH A O   
2000 O  O   . HOH G .   ? 0.22178 0.20076 0.24199 -0.01820 -0.01023 -0.01924 440 HOH A O   
2001 O  O   . HOH G .   ? 0.21581 0.23852 0.19254 -0.01374 0.03093  0.01269  441 HOH A O   
2002 O  O   . HOH G .   ? 0.18699 0.23697 0.21512 -0.00812 -0.00666 -0.00484 442 HOH A O   
2003 O  O   . HOH G .   ? 0.30598 0.38751 0.38207 -0.02659 -0.02721 -0.03292 443 HOH A O   
2004 O  O   . HOH G .   ? 0.46600 0.49833 0.45068 0.01743  0.03027  -0.02649 444 HOH A O   
2005 O  O   . HOH G .   ? 0.20649 0.21733 0.20718 -0.02575 0.02239  0.01475  445 HOH A O   
2006 O  O   . HOH G .   ? 0.25118 0.25293 0.21724 0.00942  0.00232  -0.02969 446 HOH A O   
2007 O  O   . HOH G .   ? 0.38168 0.42534 0.30040 -0.01807 0.06044  0.02433  447 HOH A O   
2008 O  O   . HOH G .   ? 0.30692 0.31828 0.33815 -0.02587 -0.00668 -0.01303 448 HOH A O   
2009 O  O   . HOH G .   ? 0.50267 0.52934 0.40626 0.01968  0.03230  -0.04803 449 HOH A O   
2010 O  O   . HOH G .   ? 0.28163 0.31130 0.30880 -0.02449 -0.04084 -0.04953 450 HOH A O   
2011 O  O   . HOH G .   ? 0.29909 0.40784 0.38380 -0.00456 -0.00855 -0.02749 451 HOH A O   
2012 O  O   . HOH G .   ? 0.16823 0.20448 0.19396 -0.01164 -0.00521 -0.01537 452 HOH A O   
2013 O  O   . HOH G .   ? 0.50713 0.49481 0.41883 0.00107  -0.03801 -0.09715 453 HOH A O   
2014 O  O   . HOH G .   ? 0.19468 0.19805 0.21433 0.01519  -0.01056 0.01174  454 HOH A O   
2015 O  O   . HOH G .   ? 0.40689 0.29756 0.43912 0.00115  -0.01752 -0.04025 455 HOH A O   
2016 O  O   . HOH G .   ? 0.18589 0.21686 0.19299 -0.01121 0.00643  -0.00307 456 HOH A O   
2017 O  O   . HOH G .   ? 0.37317 0.41706 0.41386 0.02485  -0.02932 0.02065  457 HOH A O   
2018 O  O   . HOH G .   ? 0.51260 0.38691 0.55524 0.03186  -0.01423 -0.05251 458 HOH A O   
2019 O  O   . HOH G .   ? 0.31078 0.45540 0.44129 0.01008  -0.01126 -0.00478 459 HOH A O   
2020 O  O   . HOH G .   ? 0.31757 0.30946 0.35443 0.04015  0.00845  -0.03117 460 HOH A O   
2021 O  O   . HOH G .   ? 0.53258 0.48922 0.57596 0.03459  -0.01663 0.00967  461 HOH A O   
2022 O  O   . HOH G .   ? 0.28770 0.25143 0.32586 -0.03544 -0.01859 -0.02858 462 HOH A O   
2023 O  O   . HOH G .   ? 0.35962 0.28031 0.39602 -0.03301 -0.02681 -0.04949 463 HOH A O   
2024 O  O   . HOH G .   ? 0.32247 0.30845 0.31991 -0.01707 -0.03244 -0.06037 464 HOH A O   
2025 O  O   . HOH G .   ? 0.21026 0.21427 0.21828 -0.00785 -0.00357 -0.01165 465 HOH A O   
2026 O  O   . HOH G .   ? 0.37462 0.40238 0.36733 -0.00591 -0.00495 -0.00868 466 HOH A O   
2027 O  O   . HOH G .   ? 0.40903 0.34774 0.36619 0.00285  -0.02604 -0.10961 467 HOH A O   
2028 O  O   . HOH G .   ? 0.43325 0.44621 0.30742 0.01253  -0.01261 -0.04067 468 HOH A O   
2029 O  O   . HOH G .   ? 0.25220 0.25912 0.21294 0.00989  0.00701  -0.02449 469 HOH A O   
2030 O  O   . HOH G .   ? 0.35657 0.38337 0.36739 0.00663  0.00993  -0.00720 470 HOH A O   
2031 O  O   . HOH G .   ? 0.38456 0.39568 0.26987 0.01214  -0.01539 -0.01818 471 HOH A O   
2032 O  O   . HOH G .   ? 0.28098 0.27308 0.29350 -0.02276 -0.03184 -0.05324 472 HOH A O   
2033 O  O   . HOH G .   ? 0.28443 0.37977 0.36286 -0.00940 0.00525  -0.00440 473 HOH A O   
2034 O  O   . HOH G .   ? 0.18504 0.21955 0.19914 -0.00966 -0.00406 -0.00700 474 HOH A O   
2035 O  O   . HOH G .   ? 0.24298 0.26339 0.28560 0.02790  -0.01371 0.00917  475 HOH A O   
2036 O  O   . HOH G .   ? 0.41547 0.42758 0.41750 0.01526  0.01184  -0.01926 476 HOH A O   
2037 O  O   . HOH G .   ? 0.33795 0.35111 0.32640 0.01042  0.01229  -0.01712 477 HOH A O   
2038 O  O   . HOH G .   ? 0.32094 0.25244 0.35122 -0.03276 -0.03095 -0.06059 478 HOH A O   
2039 O  O   . HOH G .   ? 0.42830 0.48671 0.46797 -0.01886 0.02154  0.00149  479 HOH A O   
2040 O  O   . HOH G .   ? 0.25232 0.26038 0.24732 -0.00261 0.00110  -0.00934 480 HOH A O   
2041 O  O   . HOH G .   ? 0.47533 0.48201 0.35134 0.01479  -0.00737 -0.06847 481 HOH A O   
2042 O  O   . HOH G .   ? 0.43104 0.45096 0.42313 0.00975  0.01583  -0.01447 482 HOH A O   
2043 O  O   . HOH G .   ? 0.37070 0.27433 0.37806 0.03521  -0.00431 -0.09472 483 HOH A O   
2044 O  O   . HOH G .   ? 0.30936 0.44525 0.42607 0.00372  0.01924  -0.00853 484 HOH A O   
2045 O  O   . HOH G .   ? 0.49340 0.55602 0.46918 -0.01268 0.05763  0.00744  485 HOH A O   
2046 O  O   . HOH G .   ? 0.46146 0.53707 0.56300 0.04874  -0.00210 -0.00865 486 HOH A O   
2047 O  O   . HOH G .   ? 0.30414 0.31645 0.24827 0.00625  -0.02540 -0.03485 487 HOH A O   
2048 O  O   . HOH G .   ? 0.42313 0.44571 0.31262 -0.00176 0.03530  0.01043  488 HOH A O   
2049 O  O   . HOH G .   ? 0.47977 0.47343 0.37030 0.02622  0.01009  -0.09979 489 HOH A O   
2050 O  O   . HOH G .   ? 0.43949 0.42987 0.45298 0.05620  0.02828  -0.07851 490 HOH A O   
2051 O  O   . HOH G .   ? 0.33672 0.24801 0.36841 -0.02000 -0.02069 -0.04017 491 HOH A O   
2052 O  O   . HOH G .   ? 0.48259 0.48138 0.38470 0.01773  0.00158  -0.07386 492 HOH A O   
2053 O  O   . HOH G .   ? 0.46914 0.37246 0.51361 0.04049  -0.00915 -0.04245 493 HOH A O   
2054 O  O   . HOH G .   ? 0.23480 0.25297 0.22986 -0.00230 -0.00094 0.00262  494 HOH A O   
2055 O  O   . HOH G .   ? 0.38792 0.44498 0.45882 -0.03852 -0.02093 -0.02928 495 HOH A O   
2056 O  O   . HOH G .   ? 0.50452 0.44274 0.53525 0.06878  0.01636  -0.09710 496 HOH A O   
2057 O  O   . HOH G .   ? 0.32307 0.31482 0.37023 0.03868  -0.00289 -0.01110 497 HOH A O   
2058 O  O   . HOH G .   ? 0.29243 0.30715 0.33485 -0.03285 -0.02155 -0.03161 498 HOH A O   
2059 O  O   . HOH G .   ? 0.32825 0.27207 0.36681 -0.03637 -0.01146 -0.00480 499 HOH A O   
2060 O  O   . HOH G .   ? 0.47236 0.45067 0.44197 -0.01812 -0.04927 -0.09418 500 HOH A O   
2061 O  O   . HOH G .   ? 0.39162 0.32580 0.36392 0.03141  0.00037  -0.10591 501 HOH A O   
2062 O  O   . HOH G .   ? 0.32811 0.41666 0.40067 -0.01628 -0.00081 -0.00506 502 HOH A O   
2063 O  O   . HOH G .   ? 0.31095 0.25813 0.35405 -0.03966 -0.01685 -0.02056 503 HOH A O   
2064 O  O   . HOH G .   ? 0.38518 0.36577 0.43848 -0.04870 -0.01408 -0.01668 504 HOH A O   
2065 O  O   . HOH G .   ? 0.54319 0.54905 0.46534 -0.00352 -0.05061 -0.08325 505 HOH A O   
2066 O  O   . HOH G .   ? 0.35879 0.39791 0.42510 -0.04315 -0.02095 -0.02928 506 HOH A O   
2067 O  O   . HOH G .   ? 0.45574 0.52053 0.50213 -0.02606 0.02660  0.00444  507 HOH A O   
2068 O  O   . HOH G .   ? 0.29333 0.30105 0.27221 0.00862  0.00769  -0.01853 508 HOH A O   
2069 O  O   . HOH G .   ? 0.19233 0.20762 0.18936 0.00101  0.00005  -0.00932 509 HOH A O   
2070 O  O   . HOH G .   ? 0.21639 0.25628 0.25426 -0.03596 0.00922  0.00279  510 HOH A O   
2071 O  O   . HOH G .   ? 0.42357 0.48621 0.47705 -0.02684 -0.04693 -0.04739 511 HOH A O   
2072 O  O   . HOH G .   ? 0.19485 0.23022 0.20284 -0.00468 0.00546  -0.00975 512 HOH A O   
2073 O  O   . HOH G .   ? 0.48055 0.43332 0.52270 0.05339  0.00625  -0.05349 513 HOH A O   
2074 O  O   . HOH G .   ? 0.25108 0.20595 0.28165 -0.02909 -0.00840 -0.00084 514 HOH A O   
2075 O  O   . HOH G .   ? 0.25554 0.27033 0.24869 -0.00143 0.00091  -0.01213 515 HOH A O   
2076 O  O   . HOH G .   ? 0.39302 0.37872 0.30074 0.02132  0.00131  -0.09378 516 HOH A O   
2077 O  O   . HOH G .   ? 0.39368 0.43913 0.37002 0.03366  0.04844  -0.05367 517 HOH A O   
2078 O  O   . HOH G .   ? 0.40287 0.41471 0.28950 0.01174  -0.00699 -0.02667 518 HOH A O   
2079 O  O   . HOH G .   ? 0.16774 0.21196 0.19911 0.00721  -0.00152 -0.00131 519 HOH A O   
2080 O  O   . HOH G .   ? 0.36288 0.34814 0.39236 0.02315  -0.01277 0.01174  520 HOH A O   
2081 O  O   . HOH G .   ? 0.43308 0.43799 0.34044 0.00524  0.00883  0.00553  521 HOH A O   
2082 O  O   . HOH G .   ? 0.27454 0.27189 0.30449 -0.02894 -0.00439 -0.00583 522 HOH A O   
2083 O  O   . HOH G .   ? 0.27151 0.22680 0.30295 -0.03057 -0.02228 -0.03959 523 HOH A O   
2084 O  O   . HOH G .   ? 0.42717 0.47475 0.42569 0.03550  0.04541  -0.04901 524 HOH A O   
2085 O  O   . HOH G .   ? 0.41375 0.39025 0.33388 0.00470  -0.02801 -0.09914 525 HOH A O   
2086 O  O   . HOH G .   ? 0.32838 0.35683 0.32400 -0.00323 -0.00503 -0.00237 526 HOH A O   
2087 O  O   . HOH G .   ? 0.42349 0.35506 0.44661 0.00215  -0.01412 0.02110  527 HOH A O   
2088 O  O   . HOH G .   ? 0.24548 0.25192 0.24848 0.02334  0.01492  -0.03108 528 HOH A O   
2089 O  O   . HOH G .   ? 0.36548 0.37621 0.29546 0.00633  -0.02761 -0.04362 529 HOH A O   
2090 O  O   . HOH G .   ? 0.44839 0.40149 0.48906 0.04662  0.00245  -0.04247 530 HOH A O   
2091 O  O   . HOH G .   ? 0.38680 0.43204 0.41502 -0.03430 0.03255  0.01374  531 HOH A O   
2092 O  O   . HOH G .   ? 0.26641 0.28469 0.26155 0.00115  0.00223  -0.01171 532 HOH A O   
2093 O  O   . HOH G .   ? 0.54262 0.59937 0.48271 -0.01921 0.06577  0.01984  533 HOH A O   
2094 O  O   . HOH G .   ? 0.27312 0.24058 0.31611 -0.04059 -0.01256 -0.01363 534 HOH A O   
2095 O  O   . HOH G .   ? 0.42052 0.43984 0.34736 0.04326  0.04434  -0.09531 535 HOH A O   
2096 O  O   . HOH G .   ? 0.34816 0.39639 0.39379 -0.02274 -0.00771 -0.01806 536 HOH A O   
2097 O  O   . HOH G .   ? 0.17911 0.21906 0.19965 -0.01524 -0.00760 -0.00969 537 HOH A O   
2098 O  O   . HOH G .   ? 0.31827 0.42316 0.41188 0.02893  0.02597  -0.01768 538 HOH A O   
2099 O  O   . HOH G .   ? 0.20957 0.33316 0.32411 0.02633  0.01810  -0.01350 539 HOH A O   
2100 O  O   . HOH G .   ? 0.54260 0.47246 0.50384 0.02435  -0.00696 -0.11474 540 HOH A O   
2101 O  O   . HOH G .   ? 0.52524 0.59968 0.52782 -0.01684 0.05791  0.00762  541 HOH A O   
2102 O  O   . HOH G .   ? 0.44950 0.46608 0.33673 0.01304  0.01190  -0.03289 542 HOH A O   
2103 O  O   . HOH G .   ? 0.35309 0.42883 0.39420 -0.01234 -0.02417 -0.00700 543 HOH A O   
2104 O  O   . HOH G .   ? 0.44869 0.49142 0.48037 0.01585  0.01453  -0.01116 544 HOH A O   
2105 O  O   . HOH G .   ? 0.21624 0.33085 0.30711 -0.00190 -0.02263 -0.00296 545 HOH A O   
2106 O  O   . HOH G .   ? 0.42627 0.50179 0.48106 -0.01543 -0.04383 -0.03964 546 HOH A O   
2107 O  O   . HOH G .   ? 0.44206 0.50569 0.43245 -0.00605 0.05138  -0.00054 547 HOH A O   
2108 O  O   . HOH G .   ? 0.40019 0.41033 0.43697 0.04664  0.02039  -0.04372 548 HOH A O   
2109 O  O   . HOH G .   ? 0.56758 0.49621 0.60038 0.01891  -0.01762 0.01674  549 HOH A O   
2110 O  O   . HOH G .   ? 0.32152 0.33777 0.21323 -0.02051 0.04862  0.04129  550 HOH A O   
2111 O  O   . HOH G .   ? 0.35404 0.38520 0.41079 0.03415  -0.01203 0.00475  551 HOH A O   
2112 O  O   . HOH G .   ? 0.20031 0.19974 0.19728 -0.03282 0.02438  0.02259  552 HOH A O   
2113 O  O   . HOH G .   ? 0.47580 0.51868 0.46462 0.01197  0.03505  -0.01853 553 HOH A O   
2114 O  O   . HOH G .   ? 0.47835 0.38547 0.51758 0.03064  -0.01061 -0.03376 554 HOH A O   
2115 O  O   . HOH G .   ? 0.37706 0.33604 0.41885 -0.04766 -0.00486 0.01081  555 HOH A O   
2116 O  O   . HOH G .   ? 0.33340 0.39782 0.38814 -0.02449 -0.00120 -0.01545 556 HOH A O   
2117 O  O   . HOH G .   ? 0.55884 0.60437 0.57341 0.03598  0.03940  -0.04344 557 HOH A O   
2118 O  O   . HOH G .   ? 0.41857 0.39114 0.34394 0.02548  0.00356  -0.10213 558 HOH A O   
2119 O  O   . HOH G .   ? 0.25384 0.29709 0.28475 -0.01662 0.00880  -0.00218 559 HOH A O   
2120 O  O   . HOH G .   ? 0.39603 0.41000 0.40027 0.07420  0.05135  -0.11027 560 HOH A O   
2121 O  O   . HOH G .   ? 0.25205 0.29900 0.27675 -0.01907 -0.01312 -0.01262 561 HOH A O   
2122 O  O   . HOH G .   ? 0.27762 0.29546 0.27853 -0.00036 -0.00170 -0.01105 562 HOH A O   
2123 O  O   . HOH G .   ? 0.31924 0.32271 0.22539 -0.02813 0.04648  0.05132  563 HOH A O   
2124 O  O   . HOH G .   ? 0.37770 0.48366 0.45944 -0.01106 -0.02007 -0.00567 564 HOH A O   
2125 O  O   . HOH G .   ? 0.53259 0.43034 0.52015 0.00037  -0.02818 -0.11404 565 HOH A O   
2126 O  O   . HOH G .   ? 0.50588 0.55722 0.45842 0.01916  0.05080  -0.03509 566 HOH A O   
2127 O  O   . HOH G .   ? 0.18518 0.21036 0.19087 -0.01136 -0.00473 -0.01109 567 HOH A O   
2128 O  O   . HOH G .   ? 0.44960 0.47976 0.39477 0.01512  0.03357  -0.02957 568 HOH A O   
2129 O  O   . HOH G .   ? 0.47945 0.47877 0.39894 0.00650  0.00153  0.00751  569 HOH A O   
2130 O  O   . HOH G .   ? 0.41792 0.47658 0.44980 -0.00929 0.02541  -0.00095 570 HOH A O   
2131 O  O   . HOH G .   ? 0.54973 0.51503 0.47840 0.00080  -0.03334 -0.10955 571 HOH A O   
2132 O  O   . HOH G .   ? 0.48159 0.50958 0.39439 0.03719  0.04576  -0.08518 572 HOH A O   
2133 O  O   . HOH G .   ? 0.33114 0.46100 0.44377 -0.00305 0.00851  -0.00627 573 HOH A O   
2134 O  O   . HOH G .   ? 0.46530 0.55393 0.54190 -0.02184 -0.03529 -0.03660 574 HOH A O   
2135 O  O   . HOH G .   ? 0.57542 0.39991 0.61886 0.01148  0.00000  0.00000  575 HOH A O   
2136 O  O   . HOH G .   ? 0.40306 0.41354 0.44720 0.04379  0.01381  -0.03230 576 HOH A O   
2137 O  O   . HOH G .   ? 0.59832 0.46409 0.64349 0.01595  -0.01941 -0.02903 577 HOH A O   
2138 O  O   . HOH G .   ? 0.55429 0.59472 0.49871 0.01273  0.04200  -0.02464 578 HOH A O   
2139 O  O   . HOH G .   ? 0.44810 0.49388 0.48559 -0.02669 -0.04840 -0.05228 579 HOH A O   
2140 O  O   . HOH G .   ? 0.51254 0.52043 0.40056 0.00744  0.00622  0.00121  580 HOH A O   
2141 O  O   . HOH G .   ? 0.41804 0.43861 0.40957 0.00000  0.00169  0.00000  581 HOH A O   
2142 O  O   . HOH G .   ? 0.35459 0.37677 0.34660 0.00000  0.00182  0.00000  582 HOH A O   
2143 O  O   . HOH G .   ? 0.55258 0.55067 0.44443 0.01546  -0.00660 -0.07873 583 HOH A O   
2144 O  O   . HOH G .   ? 0.51868 0.58033 0.57027 -0.03648 0.02651  0.00750  584 HOH A O   
2145 O  O   . HOH G .   ? 0.37410 0.33459 0.41715 -0.04411 -0.03328 -0.05370 585 HOH A O   
2146 O  O   . HOH G .   ? 0.42151 0.43128 0.43520 0.06088  0.03860  -0.08301 586 HOH A O   
2147 O  O   . HOH G .   ? 0.53839 0.44953 0.52052 0.03077  -0.00541 -0.11407 587 HOH A O   
2148 O  O   . HOH G .   ? 0.52483 0.63155 0.60852 0.00122  -0.02453 -0.03019 588 HOH A O   
2149 O  O   . HOH G .   ? 0.48880 0.39798 0.48330 0.03971  -0.00050 -0.11011 589 HOH A O   
2150 O  O   . HOH G .   ? 0.38081 0.40585 0.37615 0.00055  0.00419  -0.01331 590 HOH A O   
2151 O  O   . HOH G .   ? 0.36343 0.44218 0.39510 -0.01517 -0.03304 -0.00997 591 HOH A O   
2152 O  O   . HOH G .   ? 0.36057 0.37585 0.35516 -0.00398 -0.00032 -0.01142 592 HOH A O   
2153 O  O   . HOH G .   ? 0.41767 0.45629 0.46735 -0.04429 0.00721  0.00217  593 HOH A O   
2154 O  O   . HOH G .   ? 0.45052 0.54156 0.51844 0.00670  -0.02198 -0.02726 594 HOH A O   
2155 O  O   . HOH G .   ? 0.49265 0.47326 0.39339 0.01176  -0.01913 -0.10260 595 HOH A O   
2156 O  O   . HOH G .   ? 0.40999 0.44055 0.40516 -0.00189 0.00605  -0.01123 596 HOH A O   
2157 O  O   . HOH G .   ? 0.39801 0.50373 0.47809 0.00549  -0.00738 -0.02841 597 HOH A O   
2158 O  O   . HOH G .   ? 0.49124 0.47983 0.38552 0.01619  -0.00914 -0.09431 598 HOH A O   
2159 O  O   . HOH G .   ? 0.53079 0.55041 0.43717 -0.03577 0.06096  0.05484  599 HOH A O   
# 
