data_7HG3
# 
_entry.id   7HG3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   7HG3         pdb_00007hg3 10.2210/pdb7hg3/pdb 
WWPDB D_1001407429 ?            ?                   
# 
_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       2024-11-06 
# 
_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.entry_id                        7HG3 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
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 'Hepatoma-derived growth factor-related protein 2'                 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                     62.068    2   ? ?    ? ? 
4 non-polymer syn '3-[(2S)-1-(methanesulfonyl)pyrrolidin-2-yl]-5-methyl-1,2-oxazole' 230.284   1   ? ?    ? ? 
5 water       nat water                                                              18.015    236 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_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       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                                      SO4 
3 1,2-ETHANEDIOL                                                     EDO 
4 '3-[(2S)-1-(methanesulfonyl)pyrrolidin-2-yl]-5-methyl-1,2-oxazole' ZQD 
5 water                                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER 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                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_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 
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 
SO4 non-polymer         . 'SULFATE ION'                                                      ?                 'O4 S -2'        
96.063  
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 
ZQD non-polymer         . '3-[(2S)-1-(methanesulfonyl)pyrrolidin-2-yl]-5-methyl-1,2-oxazole' ?                 'C9 H14 N2 O3 S' 
230.284 
# 
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  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZQD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZQD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 2 SO4 1   104 4   SO4 SO4 A . 
H 4 ZQD 1   105 101 ZQD LIG A . 
I 2 SO4 1   101 1   SO4 SO4 B . 
J 2 SO4 1   102 3   SO4 SO4 B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 202 HOH HOH A . 
M 5 HOH 2   202 307 HOH HOH A . 
M 5 HOH 3   203 259 HOH HOH A . 
M 5 HOH 4   204 84  HOH HOH A . 
M 5 HOH 5   205 91  HOH HOH A . 
M 5 HOH 6   206 66  HOH HOH A . 
M 5 HOH 7   207 304 HOH HOH A . 
M 5 HOH 8   208 87  HOH HOH A . 
M 5 HOH 9   209 86  HOH HOH A . 
M 5 HOH 10  210 199 HOH HOH A . 
M 5 HOH 11  211 28  HOH HOH A . 
M 5 HOH 12  212 8   HOH HOH A . 
M 5 HOH 13  213 34  HOH HOH A . 
M 5 HOH 14  214 208 HOH HOH A . 
M 5 HOH 15  215 55  HOH HOH A . 
M 5 HOH 16  216 85  HOH HOH A . 
M 5 HOH 17  217 293 HOH HOH A . 
M 5 HOH 18  218 37  HOH HOH A . 
M 5 HOH 19  219 139 HOH HOH A . 
M 5 HOH 20  220 167 HOH HOH A . 
M 5 HOH 21  221 142 HOH HOH A . 
M 5 HOH 22  222 71  HOH HOH A . 
M 5 HOH 23  223 289 HOH HOH A . 
M 5 HOH 24  224 111 HOH HOH A . 
M 5 HOH 25  225 188 HOH HOH A . 
M 5 HOH 26  226 26  HOH HOH A . 
M 5 HOH 27  227 23  HOH HOH A . 
M 5 HOH 28  228 179 HOH HOH A . 
M 5 HOH 29  229 97  HOH HOH A . 
M 5 HOH 30  230 260 HOH HOH A . 
M 5 HOH 31  231 267 HOH HOH A . 
M 5 HOH 32  232 300 HOH HOH A . 
M 5 HOH 33  233 152 HOH HOH A . 
M 5 HOH 34  234 2   HOH HOH A . 
M 5 HOH 35  235 292 HOH HOH A . 
M 5 HOH 36  236 109 HOH HOH A . 
M 5 HOH 37  237 1   HOH HOH A . 
M 5 HOH 38  238 12  HOH HOH A . 
M 5 HOH 39  239 32  HOH HOH A . 
M 5 HOH 40  240 41  HOH HOH A . 
M 5 HOH 41  241 78  HOH HOH A . 
M 5 HOH 42  242 288 HOH HOH A . 
M 5 HOH 43  243 27  HOH HOH A . 
M 5 HOH 44  244 42  HOH HOH A . 
M 5 HOH 45  245 190 HOH HOH A . 
M 5 HOH 46  246 77  HOH HOH A . 
M 5 HOH 47  247 115 HOH HOH A . 
M 5 HOH 48  248 38  HOH HOH A . 
M 5 HOH 49  249 7   HOH HOH A . 
M 5 HOH 50  250 334 HOH HOH A . 
M 5 HOH 51  251 73  HOH HOH A . 
M 5 HOH 52  252 145 HOH HOH A . 
M 5 HOH 53  253 58  HOH HOH A . 
M 5 HOH 54  254 60  HOH HOH A . 
M 5 HOH 55  255 297 HOH HOH A . 
M 5 HOH 56  256 164 HOH HOH A . 
M 5 HOH 57  257 18  HOH HOH A . 
M 5 HOH 58  258 211 HOH HOH A . 
M 5 HOH 59  259 14  HOH HOH A . 
M 5 HOH 60  260 278 HOH HOH A . 
M 5 HOH 61  261 31  HOH HOH A . 
M 5 HOH 62  262 99  HOH HOH A . 
M 5 HOH 63  263 274 HOH HOH A . 
M 5 HOH 64  264 93  HOH HOH A . 
M 5 HOH 65  265 20  HOH HOH A . 
M 5 HOH 66  266 21  HOH HOH A . 
M 5 HOH 67  267 299 HOH HOH A . 
M 5 HOH 68  268 203 HOH HOH A . 
M 5 HOH 69  269 64  HOH HOH A . 
M 5 HOH 70  270 94  HOH HOH A . 
M 5 HOH 71  271 47  HOH HOH A . 
M 5 HOH 72  272 131 HOH HOH A . 
M 5 HOH 73  273 222 HOH HOH A . 
M 5 HOH 74  274 95  HOH HOH A . 
M 5 HOH 75  275 143 HOH HOH A . 
M 5 HOH 76  276 281 HOH HOH A . 
M 5 HOH 77  277 165 HOH HOH A . 
M 5 HOH 78  278 16  HOH HOH A . 
M 5 HOH 79  279 9   HOH HOH A . 
M 5 HOH 80  280 218 HOH HOH A . 
M 5 HOH 81  281 116 HOH HOH A . 
M 5 HOH 82  282 19  HOH HOH A . 
M 5 HOH 83  283 113 HOH HOH A . 
M 5 HOH 84  284 327 HOH HOH A . 
M 5 HOH 85  285 301 HOH HOH A . 
M 5 HOH 86  286 318 HOH HOH A . 
M 5 HOH 87  287 296 HOH HOH A . 
M 5 HOH 88  288 22  HOH HOH A . 
M 5 HOH 89  289 146 HOH HOH A . 
M 5 HOH 90  290 210 HOH HOH A . 
M 5 HOH 91  291 63  HOH HOH A . 
M 5 HOH 92  292 83  HOH HOH A . 
M 5 HOH 93  293 108 HOH HOH A . 
M 5 HOH 94  294 75  HOH HOH A . 
M 5 HOH 95  295 185 HOH HOH A . 
M 5 HOH 96  296 335 HOH HOH A . 
M 5 HOH 97  297 219 HOH HOH A . 
M 5 HOH 98  298 35  HOH HOH A . 
M 5 HOH 99  299 205 HOH HOH A . 
M 5 HOH 100 300 283 HOH HOH A . 
M 5 HOH 101 301 57  HOH HOH A . 
M 5 HOH 102 302 156 HOH HOH A . 
M 5 HOH 103 303 332 HOH HOH A . 
N 5 HOH 1   201 329 HOH HOH B . 
N 5 HOH 2   202 247 HOH HOH B . 
N 5 HOH 3   203 272 HOH HOH B . 
N 5 HOH 4   204 184 HOH HOH B . 
N 5 HOH 5   205 172 HOH HOH B . 
N 5 HOH 6   206 258 HOH HOH B . 
N 5 HOH 7   207 242 HOH HOH B . 
N 5 HOH 8   208 69  HOH HOH B . 
N 5 HOH 9   209 123 HOH HOH B . 
N 5 HOH 10  210 331 HOH HOH B . 
N 5 HOH 11  211 98  HOH HOH B . 
N 5 HOH 12  212 72  HOH HOH B . 
N 5 HOH 13  213 215 HOH HOH B . 
N 5 HOH 14  214 89  HOH HOH B . 
N 5 HOH 15  215 17  HOH HOH B . 
N 5 HOH 16  216 333 HOH HOH B . 
N 5 HOH 17  217 119 HOH HOH B . 
N 5 HOH 18  218 68  HOH HOH B . 
N 5 HOH 19  219 54  HOH HOH B . 
N 5 HOH 20  220 249 HOH HOH B . 
N 5 HOH 21  221 137 HOH HOH B . 
N 5 HOH 22  222 6   HOH HOH B . 
N 5 HOH 23  223 153 HOH HOH B . 
N 5 HOH 24  224 223 HOH HOH B . 
N 5 HOH 25  225 10  HOH HOH B . 
N 5 HOH 26  226 320 HOH HOH B . 
N 5 HOH 27  227 117 HOH HOH B . 
N 5 HOH 28  228 224 HOH HOH B . 
N 5 HOH 29  229 5   HOH HOH B . 
N 5 HOH 30  230 13  HOH HOH B . 
N 5 HOH 31  231 120 HOH HOH B . 
N 5 HOH 32  232 261 HOH HOH B . 
N 5 HOH 33  233 150 HOH HOH B . 
N 5 HOH 34  234 61  HOH HOH B . 
N 5 HOH 35  235 25  HOH HOH B . 
N 5 HOH 36  236 59  HOH HOH B . 
N 5 HOH 37  237 24  HOH HOH B . 
N 5 HOH 38  238 101 HOH HOH B . 
N 5 HOH 39  239 96  HOH HOH B . 
N 5 HOH 40  240 168 HOH HOH B . 
N 5 HOH 41  241 36  HOH HOH B . 
N 5 HOH 42  242 169 HOH HOH B . 
N 5 HOH 43  243 157 HOH HOH B . 
N 5 HOH 44  244 280 HOH HOH B . 
N 5 HOH 45  245 214 HOH HOH B . 
N 5 HOH 46  246 79  HOH HOH B . 
N 5 HOH 47  247 315 HOH HOH B . 
N 5 HOH 48  248 76  HOH HOH B . 
N 5 HOH 49  249 74  HOH HOH B . 
N 5 HOH 50  250 217 HOH HOH B . 
N 5 HOH 51  251 175 HOH HOH B . 
N 5 HOH 52  252 197 HOH HOH B . 
N 5 HOH 53  253 177 HOH HOH B . 
N 5 HOH 54  254 303 HOH HOH B . 
N 5 HOH 55  255 44  HOH HOH B . 
N 5 HOH 56  256 104 HOH HOH B . 
N 5 HOH 57  257 46  HOH HOH B . 
N 5 HOH 58  258 182 HOH HOH B . 
N 5 HOH 59  259 316 HOH HOH B . 
N 5 HOH 60  260 279 HOH HOH B . 
N 5 HOH 61  261 319 HOH HOH B . 
N 5 HOH 62  262 163 HOH HOH B . 
N 5 HOH 63  263 160 HOH HOH B . 
N 5 HOH 64  264 291 HOH HOH B . 
N 5 HOH 65  265 201 HOH HOH B . 
N 5 HOH 66  266 170 HOH HOH B . 
N 5 HOH 67  267 103 HOH HOH B . 
N 5 HOH 68  268 322 HOH HOH B . 
N 5 HOH 69  269 314 HOH HOH B . 
N 5 HOH 70  270 92  HOH HOH B . 
N 5 HOH 71  271 107 HOH HOH B . 
N 5 HOH 72  272 312 HOH HOH B . 
N 5 HOH 73  273 310 HOH HOH B . 
O 5 HOH 1   201 321 HOH HOH C . 
O 5 HOH 2   202 254 HOH HOH C . 
O 5 HOH 3   203 323 HOH HOH C . 
O 5 HOH 4   204 317 HOH HOH C . 
O 5 HOH 5   205 161 HOH HOH C . 
O 5 HOH 6   206 226 HOH HOH C . 
O 5 HOH 7   207 325 HOH HOH C . 
O 5 HOH 8   208 189 HOH HOH C . 
O 5 HOH 9   209 118 HOH HOH C . 
O 5 HOH 10  210 326 HOH HOH C . 
O 5 HOH 11  211 134 HOH HOH C . 
O 5 HOH 12  212 90  HOH HOH C . 
O 5 HOH 13  213 15  HOH HOH C . 
O 5 HOH 14  214 151 HOH HOH C . 
O 5 HOH 15  215 82  HOH HOH C . 
O 5 HOH 16  216 271 HOH HOH C . 
O 5 HOH 17  217 173 HOH HOH C . 
O 5 HOH 18  218 284 HOH HOH C . 
O 5 HOH 19  219 126 HOH HOH C . 
O 5 HOH 20  220 56  HOH HOH C . 
O 5 HOH 21  221 48  HOH HOH C . 
O 5 HOH 22  222 45  HOH HOH C . 
O 5 HOH 23  223 4   HOH HOH C . 
O 5 HOH 24  224 302 HOH HOH C . 
O 5 HOH 25  225 49  HOH HOH C . 
O 5 HOH 26  226 53  HOH HOH C . 
O 5 HOH 27  227 269 HOH HOH C . 
O 5 HOH 28  228 290 HOH HOH C . 
O 5 HOH 29  229 149 HOH HOH C . 
O 5 HOH 30  230 102 HOH HOH C . 
O 5 HOH 31  231 122 HOH HOH C . 
O 5 HOH 32  232 130 HOH HOH C . 
O 5 HOH 33  233 40  HOH HOH C . 
O 5 HOH 34  234 43  HOH HOH C . 
O 5 HOH 35  235 135 HOH HOH C . 
O 5 HOH 36  236 295 HOH HOH C . 
O 5 HOH 37  237 294 HOH HOH C . 
O 5 HOH 38  238 287 HOH HOH C . 
O 5 HOH 39  239 67  HOH HOH C . 
O 5 HOH 40  240 148 HOH HOH C . 
O 5 HOH 41  241 198 HOH HOH C . 
O 5 HOH 42  242 309 HOH HOH C . 
O 5 HOH 43  243 132 HOH HOH C . 
O 5 HOH 44  244 275 HOH HOH C . 
O 5 HOH 45  245 62  HOH HOH C . 
O 5 HOH 46  246 298 HOH HOH C . 
O 5 HOH 47  247 328 HOH HOH C . 
O 5 HOH 48  248 171 HOH HOH C . 
O 5 HOH 49  249 330 HOH HOH C . 
O 5 HOH 50  250 246 HOH HOH C . 
O 5 HOH 51  251 65  HOH HOH C . 
O 5 HOH 52  252 209 HOH HOH C . 
O 5 HOH 53  253 241 HOH HOH C . 
O 5 HOH 54  254 305 HOH HOH C . 
O 5 HOH 55  255 270 HOH HOH C . 
O 5 HOH 56  256 70  HOH HOH C . 
O 5 HOH 57  257 324 HOH HOH C . 
O 5 HOH 58  258 206 HOH HOH C . 
O 5 HOH 59  259 313 HOH HOH C . 
O 5 HOH 60  260 125 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A ASP 62 ? CG  ? A ASP 63 CG  
4  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
5  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
6  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
7  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
8  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
9  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
10 1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
11 1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
12 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
13 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
14 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
15 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
16 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
17 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
18 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
19 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
20 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
21 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
22 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
23 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
24 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
25 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
26 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
27 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
28 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
29 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
30 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
31 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
32 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
33 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
34 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
35 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
36 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
37 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
38 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
39 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
40 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
41 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
42 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
43 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
44 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
45 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
46 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
47 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
48 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
49 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
50 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
51 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
52 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
53 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
54 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
55 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
56 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
57 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
58 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
59 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
60 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
61 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
62 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
63 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
64 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HG3 
_cell.length_a           41.600 
_cell.length_b           42.080 
_cell.length_c           159.020 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HG3 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.entry_id          7HG3 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.76 
_exptl_crystal.density_percent_sol   55.0 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '28% PEG MME 2000; 0.15 M ammonium sulfate; 0.1 M sodium acetate pH 4.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2021-05-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.918076 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.918076 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HG3 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.01 
_reflns.d_resolution_high            1.45 
_reflns.number_obs                   50527 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.pdbx_netI_over_sigmaI        13.4 
_reflns.pdbx_redundancy              5.7 
_reflns.pdbx_Rrim_I_all              0.057 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     288161 
_reflns.pdbx_chi_squared             0.95 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.45 
_reflns_shell.d_res_low                   1.49 
_reflns_shell.number_measured_all         15575 
_reflns_shell.number_unique_obs           3678 
_reflns_shell.Rmerge_I_obs                1.412 
_reflns_shell.pdbx_chi_squared            0.70 
_reflns_shell.pdbx_redundancy             4.2 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.617 
_reflns_shell.pdbx_Rpim_I_all             0.777 
_reflns_shell.pdbx_CC_half                0.318 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HG3 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     47781 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.71 
_refine.ls_d_res_high                            1.45 
_refine.ls_percent_reflns_obs                    99.72 
_refine.ls_R_factor_obs                          0.20747 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20615 
_refine.ls_R_factor_R_free                       0.23109 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  2662 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_refine.B_iso_mean                               32.860 
_refine.aniso_B[1][1]                            0.72 
_refine.aniso_B[2][2]                            -0.41 
_refine.aniso_B[3][3]                            -0.31 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.077 
_refine.pdbx_overall_ESU_R_Free                  0.077 
_refine.overall_SU_ML                            0.068 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.862 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        2130 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.number_atoms_solvent             236 
_refine_hist.number_atoms_total               2419 
_refine_hist.d_res_high                       1.45 
_refine_hist.d_res_low                        40.71 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.011  0.012  ? 2286 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.994  1.831  ? 3114 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.202  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.993  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.435 10.000 ? 298  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.137  0.200  ? 289  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.012  0.020  ? 1890 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.039  3.062  ? 1074 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.264  5.477  ? 1337 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.283  3.348  ? 1212 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.136  43.17  ? 3456 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.450 
_refine_ls_shell.d_res_low                        1.488 
_refine_ls_shell.number_reflns_R_work             3477 
_refine_ls_shell.R_factor_R_work                  0.348 
_refine_ls_shell.percent_reflns_obs               99.81 
_refine_ls_shell.R_factor_R_free                  0.359 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             185 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HG3 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z319891284' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HG3 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 4 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HG3 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HG3 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HG3 C 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HG3 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HG3 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HG3 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HG3 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HG3 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HG3 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,H,M 
2 1 B,I,J,N       
3 1 C,K,L,O       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-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 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
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 ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HG3 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  A HOH 274 ? ? O A HOH 278 ? ? 1.52 
2 1 O  B HOH 244 ? ? O B HOH 268 ? ? 1.70 
3 1 O  B HOH 254 ? ? O B HOH 268 ? ? 1.76 
4 1 O4 A SO4 104 ? ? O A HOH 201 ? ? 1.98 
5 1 O2 A SO4 104 ? ? O A HOH 202 ? ? 2.02 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 261 ? ? 1_555 O C HOH 237 ? ? 4_435 2.02 
2 1 O A HOH 289 ? ? 1_555 O C HOH 257 ? ? 4_445 2.15 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A MET 15 ? ? SD A MET 15 ? ? CE  A MET 15 ? ? 86.84  100.20 -13.36 1.60 N 
2 1 NE A ARG 24 ? ? CZ A ARG 24 ? ? NH2 A ARG 24 ? ? 116.12 120.30 -4.18  0.50 N 
3 1 CG B MET 15 ? ? SD B MET 15 ? ? CE  B MET 15 ? ? 111.40 100.20 11.20  1.60 N 
4 1 NE C ARG 74 ? ? CZ C ARG 74 ? ? NH1 C ARG 74 ? ? 116.40 120.30 -3.90  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -157.40 65.28 
2 1 ASN B 38 ? ? 78.92   -6.18 
3 1 ASN B 87 ? ? -163.07 60.63 
4 1 ASN C 87 ? ? -163.79 52.25 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 VAL A 11 ? ? PHE A 12 ? ? 147.74 
2 1 VAL B 11 ? ? PHE B 12 ? ? 148.78 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       303 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.81 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ALA 29 ? C ALA 30 
11 1 Y 1 C ASP 30 ? C ASP 31 
12 1 Y 1 C GLY 31 ? C GLY 32 
13 1 Y 1 C ALA 32 ? C ALA 33 
14 1 Y 1 C VAL 33 ? C VAL 34 
15 1 Y 1 C SER 93 ? C SER 94 
# 
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 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
SO4 S    S N N 314 
SO4 O1   O N N 315 
SO4 O2   O N N 316 
SO4 O3   O N N 317 
SO4 O4   O N N 318 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TRP N    N N N 336 
TRP CA   C N S 337 
TRP C    C N N 338 
TRP O    O N N 339 
TRP CB   C N N 340 
TRP CG   C Y N 341 
TRP CD1  C Y N 342 
TRP CD2  C Y N 343 
TRP NE1  N Y N 344 
TRP CE2  C Y N 345 
TRP CE3  C Y N 346 
TRP CZ2  C Y N 347 
TRP CZ3  C Y N 348 
TRP CH2  C Y N 349 
TRP OXT  O N N 350 
TRP H    H N N 351 
TRP H2   H N N 352 
TRP HA   H N N 353 
TRP HB2  H N N 354 
TRP HB3  H N N 355 
TRP HD1  H N N 356 
TRP HE1  H N N 357 
TRP HE3  H N N 358 
TRP HZ2  H N N 359 
TRP HZ3  H N N 360 
TRP HH2  H N N 361 
TRP HXT  H N N 362 
TYR N    N N N 363 
TYR CA   C N S 364 
TYR C    C N N 365 
TYR O    O N N 366 
TYR CB   C N N 367 
TYR CG   C Y N 368 
TYR CD1  C Y N 369 
TYR CD2  C Y N 370 
TYR CE1  C Y N 371 
TYR CE2  C Y N 372 
TYR CZ   C Y N 373 
TYR OH   O N N 374 
TYR OXT  O N N 375 
TYR H    H N N 376 
TYR H2   H N N 377 
TYR HA   H N N 378 
TYR HB2  H N N 379 
TYR HB3  H N N 380 
TYR HD1  H N N 381 
TYR HD2  H N N 382 
TYR HE1  H N N 383 
TYR HE2  H N N 384 
TYR HH   H N N 385 
TYR HXT  H N N 386 
VAL N    N N N 387 
VAL CA   C N S 388 
VAL C    C N N 389 
VAL O    O N N 390 
VAL CB   C N N 391 
VAL CG1  C N N 392 
VAL CG2  C N N 393 
VAL OXT  O N N 394 
VAL H    H N N 395 
VAL H2   H N N 396 
VAL HA   H N N 397 
VAL HB   H N N 398 
VAL HG11 H N N 399 
VAL HG12 H N N 400 
VAL HG13 H N N 401 
VAL HG21 H N N 402 
VAL HG22 H N N 403 
VAL HG23 H N N 404 
VAL HXT  H N N 405 
ZQD C10  C N N 406 
ZQD C15  C N N 407 
ZQD C01  C N N 408 
ZQD C02  C Y N 409 
ZQD C03  C Y N 410 
ZQD C04  C Y N 411 
ZQD N05  N Y N 412 
ZQD O06  O Y N 413 
ZQD C07  C N S 414 
ZQD C08  C N N 415 
ZQD C09  C N N 416 
ZQD N11  N N N 417 
ZQD S12  S N N 418 
ZQD O13  O N N 419 
ZQD O14  O N N 420 
ZQD H1   H N N 421 
ZQD H2   H N N 422 
ZQD H3   H N N 423 
ZQD H4   H N N 424 
ZQD H5   H N N 425 
ZQD H6   H N N 426 
ZQD H7   H N N 427 
ZQD H8   H N N 428 
ZQD H9   H N N 429 
ZQD H10  H N N 430 
ZQD H11  H N N 431 
ZQD H12  H N N 432 
ZQD H13  H N N 433 
ZQD H14  H N N 434 
# 
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 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
ZQD C09 C10  sing N N 389 
ZQD C09 C08  sing N N 390 
ZQD C10 N11  sing N N 391 
ZQD C08 C07  sing N N 392 
ZQD C07 N11  sing N N 393 
ZQD C07 C04  sing N N 394 
ZQD N11 S12  sing N N 395 
ZQD C15 S12  sing N N 396 
ZQD N05 C04  doub Y N 397 
ZQD N05 O06  sing Y N 398 
ZQD C04 C03  sing Y N 399 
ZQD O14 S12  doub N N 400 
ZQD S12 O13  doub N N 401 
ZQD O06 C02  sing Y N 402 
ZQD C03 C02  doub Y N 403 
ZQD C02 C01  sing N N 404 
ZQD C10 H1   sing N N 405 
ZQD C10 H2   sing N N 406 
ZQD C15 H3   sing N N 407 
ZQD C15 H4   sing N N 408 
ZQD C15 H5   sing N N 409 
ZQD C01 H6   sing N N 410 
ZQD C01 H7   sing N N 411 
ZQD C01 H8   sing N N 412 
ZQD C03 H9   sing N N 413 
ZQD C07 H10  sing N N 414 
ZQD C08 H11  sing N N 415 
ZQD C08 H12  sing N N 416 
ZQD C09 H13  sing N N 417 
ZQD C09 H14  sing N N 418 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HG3 
_atom_sites.fract_transf_matrix[1][1]   0.024038 
_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]   0.023764 
_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]   0.006289 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 2  ? 0.791   4.253   2.477   1.00 41.07  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.302  3.550   1.747   1.00 43.07  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.269   2.477   0.815   1.00 40.43  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.398   2.585   0.335   1.00 39.04  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.256  4.534   1.053   1.00 45.57  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.274  5.182   1.991   1.00 52.53  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.578  4.196   2.778   1.00 54.29  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.365  5.419   3.839   1.00 58.66  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.435  1.332   0.642   1.00 35.97  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.022   0.237   -0.228  1.00 35.29  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.206   0.611   -1.702  1.00 34.32  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.540  1.435   -2.254  1.00 33.64  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.168  -0.779  -0.074  1.00 36.98  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.724  -0.511  1.313   1.00 40.13  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.675  1.003   1.372   1.00 37.37  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.196   -0.014  -2.336  1.00 32.17  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.369   0.084   -3.768  1.00 33.73  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.850   -1.217  -4.367  1.00 30.38  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.394   -2.113  -3.643  1.00 29.31  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.861   0.218   -4.112  1.00 38.42  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.488   1.490   -3.628  1.00 50.37  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.413   1.955   -2.331  1.00 58.16  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.243   2.380   -4.291  1.00 55.92  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.074   3.099   -2.230  1.00 58.27  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.594   3.371   -3.407  1.00 53.58  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.857   -1.315  -5.689  1.00 26.01  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.634   -2.613  -6.295  1.00 24.33  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.781   -3.565  -5.945  1.00 23.47  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.880   -3.160  -5.516  1.00 26.06  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.520   -2.460  -7.802  1.00 29.37  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.500   -4.855  -6.078  1.00 22.42  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.487   -5.897  -5.902  1.00 20.79  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.622   -5.706  -6.906  1.00 23.71  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.415   -5.274  -8.037  1.00 25.79  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.915   -7.311  -6.010  1.00 23.05  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.135   -7.659  -4.740  1.00 23.44  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.809   -7.892  -3.523  1.00 21.38  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.245  -7.852  -4.801  1.00 23.21  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.104   -8.252  -2.355  1.00 20.51  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.926  -8.236  -3.642  1.00 23.53  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.273  -8.411  -2.446  1.00 23.20  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.847   -5.990  -6.433  1.00 20.54  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.982   -5.949  -7.339  1.00 22.89  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.901   -7.136  -7.042  1.00 20.07  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.886   -7.735  -5.959  1.00 19.96  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.774   -4.642  -7.129  1.00 23.83  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.381   -4.527  -5.750  1.00 24.92  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.987   -3.143  -5.436  1.00 30.71  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.557   -3.099  -4.026  1.00 32.52  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.622   -3.257  -2.911  1.00 32.00  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.773   -7.525  -7.980  1.00 21.65  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.726   -8.602  -7.717  1.00 20.81  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.525   -8.327  -6.436  1.00 20.26  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.003  -7.212  -6.159  1.00 21.83  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.629   -8.615  -8.999  1.00 23.41  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.738   -8.012  -10.052 1.00 26.72  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.915   -6.933  -9.330  1.00 25.02  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.673   -9.392  -5.629  1.00 19.22  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.429  -9.379  -4.392  1.00 19.02  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.481   -9.258  -3.186  1.00 19.41  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.855   -9.511  -2.045  1.00 20.36  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.234   -8.788  -3.399  1.00 18.05  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.321   -8.742  -2.257  1.00 16.68  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.048   -10.131 -1.656  1.00 16.67  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.907   -11.116 -2.388  1.00 17.13  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.003   -8.122  -2.724  1.00 17.60  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.999   -6.618  -2.921  1.00 21.07  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.949   -5.930  -2.457  1.00 22.43  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.995   -6.120  -3.487  1.00 22.69  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.929   -10.169 -0.311  1.00 17.63  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.786   -11.406 0.440   1.00 16.70  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.315   -11.507 0.841   1.00 15.54  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.720   -10.505 1.296   1.00 19.08  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.745   -11.475 1.646   1.00 17.05  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.232   -11.258 1.301   1.00 18.44  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.084  -11.340 2.564   1.00 19.76  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.615   -12.280 0.257   1.00 19.58  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.752   -12.723 0.682   1.00 16.22  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.326   -12.920 0.921   1.00 17.69  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.101   -14.286 1.542   1.00 18.47  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.974   -15.152 1.577   1.00 17.84  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.485   -12.864 -0.369  1.00 16.09  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.655   -11.488 -1.016  1.00 19.22  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.916   -13.908 -1.376  1.00 19.35  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.881   -14.486 2.087   1.00 17.17  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.267   -15.807 2.078   1.00 17.39  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.306   -15.882 0.903   1.00 19.18  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.515  -14.951 0.717   1.00 18.97  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.529   -16.170 3.381   1.00 18.54  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.455   -16.230 4.572   1.00 19.14  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.794   -15.080 5.266   1.00 20.60  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.971   -17.455 5.003   1.00 20.29  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.676   -15.160 6.341   1.00 24.44  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.908   -17.529 6.045   1.00 22.07  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.231   -16.385 6.707   1.00 24.55  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.412   -16.959 0.117   1.00 18.93  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.376  -17.113 -1.097  1.00 18.32  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.382  -18.253 -0.870  1.00 20.23  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.013  -19.311 -0.341  1.00 22.06  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.509   -17.384 -2.321  1.00 19.69  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.648  -18.059 -1.289  1.00 19.39  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.628  -19.107 -1.034  1.00 22.49  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.004  -19.794 -2.339  1.00 24.37  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.415  -19.134 -3.290  1.00 25.69  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.875  -18.437 -0.436  1.00 23.30  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -6.005  -19.475 -0.073  1.00 26.46  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.507  -20.370 1.080   1.00 30.80  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.591  -21.163 1.788   1.00 32.95  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.095  -22.243 0.911   1.00 33.43  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.930  -21.140 -2.287  1.00 25.16  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.453  -21.967 -3.352  1.00 29.62  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.547  -22.846 -2.744  1.00 30.01  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.421  -23.251 -1.600  1.00 26.56  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.350  -22.922 -3.788  1.00 31.13  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -3.287  -22.969 -5.286  1.00 50.95  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -2.022  -21.856 -5.928  1.00 35.14  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.094  -23.319 -6.359  1.00 39.90  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.586  -23.106 -3.543  1.00 34.70  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.634  -24.060 -3.211  1.00 37.35  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.039  -25.325 -2.601  1.00 33.35  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.097  -25.923 -3.146  1.00 32.89  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.176  -24.565 -4.552  1.00 37.67  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.570  -25.173 -4.394  1.00 48.44  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.492 -24.293 -3.551  1.00 56.34  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.549  -25.733 -1.421  1.00 34.17  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.098  -27.000 -0.876  1.00 32.61  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.754  -26.959 -0.157  1.00 37.73  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.295  -27.968 0.361   1.00 39.50  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.111  -25.783 -0.101  1.00 31.00  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.875  -25.714 0.640   1.00 30.72  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.956  -24.581 1.644   1.00 26.79  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.680  -23.614 1.439   1.00 27.91  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.740  -25.290 -0.293  1.00 32.88  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.222  -26.337 -1.265  1.00 36.27  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.087  -27.073 -0.954  1.00 46.05  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.809  -26.500 -2.510  1.00 36.32  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.561  -27.983 -1.855  1.00 52.29  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.291  -27.406 -3.431  1.00 45.49  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.165  -28.148 -3.090  1.00 52.12  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -0.614  -29.072 -3.938  1.00 66.52  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.168  -24.652 2.732   1.00 26.65  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.095  -23.576 3.729   1.00 26.02  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.370  -22.380 3.089   1.00 23.22  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.630  -22.568 2.138   1.00 23.74  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.283  -24.196 4.881   1.00 31.65  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.454  -25.281 4.205   1.00 28.86  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.250  -25.778 3.021   1.00 30.99  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.707  -21.205 3.573   1.00 23.07  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.990  -19.982 3.180   1.00 20.01  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.483  -20.231 3.288   1.00 23.49  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -0.005  -20.647 4.351   1.00 21.90  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.448  -18.794 4.035   1.00 21.80  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.881  -18.393 3.868   1.00 21.66  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.916  -19.056 4.525   1.00 27.15  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.425  -17.367 3.184   1.00 22.97  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.070  -18.454 4.193   1.00 26.72  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.814  -17.426 3.395   1.00 25.62  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.269   -19.961 2.183   1.00 20.45  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.572   -20.632 2.020   1.00 19.87  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.634   -19.538 1.873   1.00 19.45  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.462   -18.638 1.081   1.00 19.59  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.600   -21.507 0.767   1.00 19.91  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.702   -22.543 0.831   1.00 21.72  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.037   -22.357 0.645   1.00 23.28  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.520   -23.933 1.139   1.00 25.93  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.717   -23.557 0.765   1.00 20.86  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.797   -24.535 1.090   1.00 23.70  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.412   -24.740 1.415   1.00 25.88  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.009   -25.898 1.327   1.00 27.93  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.625   -26.091 1.658   1.00 27.47  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.903   -26.664 1.619   1.00 29.35  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.789   -19.613 2.598   1.00 18.94  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.849   -18.581 2.452   1.00 17.27  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.377   -18.540 1.012   1.00 17.34  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.675   -19.580 0.393   1.00 18.46  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.934   -19.023 3.431   1.00 17.22  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.721   -20.523 3.622   1.00 16.99  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.141   -20.649 3.575   1.00 20.44  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.445   -17.332 0.433   1.00 16.12  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.757   -17.219 -0.988  1.00 16.86  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.278   -15.820 -1.306  1.00 17.47  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.277   -14.929 -0.471  1.00 16.81  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.523   -17.572 -1.875  1.00 18.53  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.795   -15.681 -2.527  1.00 17.03  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.209   -14.362 -2.988  1.00 16.37  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.652   -14.083 -4.382  1.00 15.77  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.404   -15.044 -5.144  1.00 17.56  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.730   -14.178 -2.939  1.00 17.50  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.466   -15.091 -3.908  1.00 18.19  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 10.989  -14.857 -3.829  1.00 18.50  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.653  -15.701 -4.866  1.00 20.00  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.912  -16.124 -4.735  1.00 19.38  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.619  -15.917 -3.629  1.00 20.49  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.436  -16.737 -5.791  1.00 22.92  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.542   -12.773 -4.715  1.00 17.77  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.327   -12.413 -6.122  1.00 18.18  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.647   -12.536 -6.855  1.00 20.10  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.616   -11.903 -6.471  1.00 20.07  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.827   -10.966 -6.268  1.00 20.02  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.665   -10.651 -5.297  1.00 24.66  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.469   -10.667 -7.737  1.00 20.69  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.349   -11.338 -5.590  1.00 29.14  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.684   -13.370 -7.884  1.00 20.03  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.929   -13.588 -8.610  1.00 23.24  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.094   -12.565 -9.728  1.00 26.03  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.144   -11.968 -10.207 1.00 24.51  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.007   -14.977 -9.205  1.00 22.58  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.052  -15.898 -8.586  1.00 21.83  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.654  -15.497 -7.545  1.00 28.49  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.188  -17.031 -9.033  1.00 25.80  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.358  -12.409 -10.180 1.00 27.19  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.565  -11.731 -11.447 1.00 31.40  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.328  -12.739 -12.579 1.00 29.96  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.197  -13.927 -12.354 1.00 29.85  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.012  -11.285 -11.619 1.00 34.74  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.470  -10.057 -10.840 1.00 45.51  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.108  -8.920  -11.239 1.00 48.02  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.223  -10.254 -9.859  1.00 48.40  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.270  -12.256 -13.804 1.00 33.51  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.222  -13.160 -14.953 1.00 28.84  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.562  -12.967 -15.662 1.00 28.57  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.859  -11.818 -15.964 1.00 30.39  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.089   -12.667 -15.851 1.00 31.85  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.758   -12.694 -15.084 1.00 36.53  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.055   -13.478 -17.160 1.00 29.43  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.733   -11.717 -15.617 1.00 35.94  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.346  -14.044 -15.842 1.00 30.77  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.651  -13.909 -16.507 1.00 26.97  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.445  -13.617 -18.002 1.00 29.07  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.385  -13.881 -18.595 1.00 29.87  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.480  -15.161 -16.307 1.00 29.80  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.381  -12.850 -18.561 1.00 26.80  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.379  -12.724 -20.020 1.00 27.06  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.229  -14.113 -20.622 1.00 24.14  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.910  -15.046 -20.230 1.00 27.82  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.713  -12.125 -20.471 1.00 28.86  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.835  -10.619 -20.323 1.00 33.07  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.807  -9.958  -20.231 1.00 32.56  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.987  -10.122 -20.306 1.00 32.78  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.374  -14.192 -21.651 1.00 25.05  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.177  -15.407 -22.424 1.00 25.31  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.229  -16.410 -21.770 1.00 30.66  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.944  -17.435 -22.377 1.00 29.71  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.814  -16.128 -20.521 1.00 27.98  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.990  -17.051 -19.745 1.00 30.64  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.499   -16.859 -20.040 1.00 27.51  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 9.027   -15.810 -20.452 1.00 27.82  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.282  -16.809 -18.252 1.00 31.30  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.703   -17.907 -19.738 1.00 29.37  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.247   -17.844 -19.911 1.00 30.51  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.603   -16.819 -18.972 1.00 29.47  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.864   -16.817 -17.764 1.00 31.25  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.719   -19.266 -19.624 1.00 29.23  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.195   -19.265 -19.557 1.00 34.25  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.214   -20.250 -20.692 1.00 29.88  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.813   -15.916 -19.553 1.00 29.18  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.099   -14.837 -18.860 1.00 30.57  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.779   -15.344 -18.276 1.00 33.71  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.164   -16.255 -18.815 1.00 33.30  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.788   -13.593 -19.686 1.00 32.14  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 6.041   -12.877 -20.223 1.00 29.34  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.673   -11.742 -21.171 1.00 37.16  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.255   -12.171 -22.562 1.00 36.70  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.132   -10.997 -23.424 1.00 38.11  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.267   -14.711 -17.197 1.00 31.97  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.994   -15.136 -16.622 1.00 30.85  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.879   -14.610 -17.508 1.00 29.63  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.061   -13.667 -18.264 1.00 32.37  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.918   -14.450 -15.251 1.00 30.43  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 2.892   -13.249 -15.317 1.00 32.62  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.866   -13.581 -16.477 1.00 32.77  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.355  -15.112 -17.326 1.00 34.06  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.525  -14.460 -17.933 1.00 36.99  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.757  -13.024 -17.473 1.00 40.20  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.227  -12.613 -16.447 1.00 32.56  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.692  -15.362 -17.510 1.00 37.18  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.076  -16.648 -17.019 1.00 37.17  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.665  -16.334 -16.565 1.00 33.67  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.548  -12.197 -18.199 1.00 36.21  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.950  -10.873 -17.707 1.00 37.99  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.581  -10.923 -16.317 1.00 32.68  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.257  -11.888 -15.977 1.00 39.39  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.978  -10.371 -18.758 1.00 40.39  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.314  -11.610 -19.535 1.00 38.83  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.071  -12.480 -19.558 1.00 42.78  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.272  -9.900  -15.526 1.00 37.64  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.714  -9.692  -14.164 1.00 39.49  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.197  -10.766 -13.212 1.00 33.21  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.632  -10.744 -12.058 1.00 34.95  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.220  -9.497  -14.082 1.00 41.91  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.627  -8.301  -14.911 1.00 49.65  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.553  -7.153  -14.444 1.00 46.40  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -5.996  -8.553  -16.155 1.00 46.69  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.241  -11.624 -13.656 1.00 27.44  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.720  -12.658 -12.761 1.00 23.36  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.233  -12.369 -12.520 1.00 22.11  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.452   -11.724 -13.306 1.00 26.33  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.866  -14.088 -13.263 1.00 24.71  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.296  -14.576 -13.588 1.00 29.14  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.180  -14.306 -12.377 1.00 32.35  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.646  -14.625 -12.608 1.00 42.35  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.881  -16.060 -12.757 1.00 46.07  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.240   -12.747 -11.340 1.00 19.05  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.644   -12.616 -10.939 1.00 20.09  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.257   -13.996 -10.834 1.00 19.87  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.605   -14.974 -10.453 1.00 19.98  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.738   -11.997 -9.515  1.00 21.01  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.254   -10.556 -9.474  1.00 22.45  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.117  -10.285 -9.358  1.00 26.58  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.109   -9.487  -9.676  1.00 24.38  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.612  -8.997  -9.448  1.00 27.50  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.627   -8.175  -9.684  1.00 24.34  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.267   -7.949  -9.572  1.00 30.41  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.253  -6.702  -9.719  1.00 31.50  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.581   -14.141 -11.075 1.00 20.02  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.263   -15.415 -10.857 1.00 19.27  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.630   -15.540 -9.394  1.00 19.19  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.274   -14.638 -8.879  1.00 20.11  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.565   -15.270 -11.719 1.00 20.55  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.736   -13.826 -11.943 1.00 20.72  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.434   -13.061 -11.568 1.00 21.34  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.043   -16.545 -8.741  1.00 19.66  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.260   -16.720 -7.308  1.00 18.13  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.202   -17.891 -7.118  1.00 19.18  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.901   -19.039 -7.550  1.00 21.94  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.918   -16.982 -6.619  1.00 17.77  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.910   -15.849 -6.951  1.00 19.09  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.199   -17.149 -5.113  1.00 18.16  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.457   -14.447 -6.600  1.00 18.71  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.327   -17.624 -6.428  1.00 18.56  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.169   -18.735 -6.051  1.00 18.76  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.876   -19.115 -4.605  1.00 17.77  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.971   -18.300 -3.689  1.00 19.51  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.622   -18.235 -6.190  1.00 19.18  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.682   -19.250 -5.765  1.00 20.78  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.069  -20.259 -6.650  1.00 23.90  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.261  -19.203 -4.491  1.00 23.48  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.004  -21.210 -6.251  1.00 26.14  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.228  -20.153 -4.094  1.00 24.75  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.627  -21.114 -5.011  1.00 25.72  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.595   -20.395 -4.391  1.00 18.77  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.207   -20.912 -3.104  1.00 18.57  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.459   -21.437 -2.405  1.00 20.73  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.224   -22.267 -2.960  1.00 21.14  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.203   -22.059 -3.341  1.00 19.87  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.813   -21.570 -3.718  1.00 19.75  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.480   -21.390 -5.047  1.00 22.30  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.847   -21.389 -2.746  1.00 21.74  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.209   -20.905 -5.392  1.00 26.39  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.590   -20.886 -3.095  1.00 22.39  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.279   -20.677 -4.414  1.00 23.10  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.744   -20.893 -1.225  1.00 18.77  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.926   -21.354 -0.487  1.00 19.21  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.715   -22.796 -0.052  1.00 21.70  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.564   -23.243 0.083   1.00 21.86  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.172   -20.425 0.719   1.00 19.68  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.651   -19.032 0.337   1.00 18.11  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.906  -18.862 -0.227  1.00 17.38  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.883   -17.888 0.582   1.00 19.30  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.357  -17.598 -0.575  1.00 17.49  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.345   -16.620 0.248   1.00 17.73  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.617  -16.468 -0.322  1.00 18.83  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.831   -23.496 0.147   1.00 22.12  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.732   -24.870 0.634   1.00 23.35  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.516   -25.863 -0.516  1.00 28.13  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.382  -26.703 -0.791  1.00 29.55  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.367   -25.783 -1.209  1.00 24.08  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.159   -26.619 -2.379  1.00 26.14  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.961   -26.137 -3.583  1.00 25.49  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.245   -26.915 -4.508  1.00 27.41  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.680   -26.689 -2.727  1.00 26.74  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.299   -25.371 -3.164  1.00 25.65  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.836   -27.235 -1.604  1.00 28.15  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.239   -24.825 -3.651  1.00 22.72  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.923   -24.226 -4.777  1.00 24.61  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.128   -24.389 -6.069  1.00 24.87  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.691   -24.362 -7.158  1.00 28.31  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.389  -24.694 -4.905  1.00 23.54  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.091  -24.737 -3.575  1.00 26.51  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.836  -25.827 -3.177  1.00 28.75  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.172  -23.846 -2.551  1.00 25.67  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.322  -25.614 -1.959  1.00 29.11  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.963  -24.380 -1.577  1.00 24.89  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.804   -24.417 -5.957  1.00 26.14  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.929   -24.472 -7.129  1.00 28.28  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.424   -23.071 -7.488  1.00 25.40  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.574   -22.141 -6.688  1.00 24.13  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.698   -25.329 -6.865  1.00 30.50  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.107   -26.794 -6.693  1.00 39.09  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.063   -27.738 -6.130  1.00 48.92  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.861   -27.386 -6.008  1.00 44.95  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.515   -28.859 -5.794  1.00 51.20  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.003   -22.883 -8.749  1.00 23.31  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.514   -21.593 -9.223  1.00 23.19  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.064   -21.798 -9.653  1.00 23.35  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.758   -22.817 -10.309 1.00 26.40  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.304   -20.991 -10.396 1.00 25.97  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.630   -20.694 -9.972  1.00 27.50  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.638   -19.741 -10.973 1.00 27.60  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.149   -20.900 -9.256  1.00 22.99  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.823   -20.817 -9.848  1.00 22.77  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.509   -19.355 -10.139 1.00 24.30  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.184   -18.438 -9.654  1.00 23.81  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.776   -21.385 -8.884  1.00 23.06  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.446   -19.105 -10.904 1.00 22.06  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.068   -17.766 -11.286 1.00 23.55  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.191  -17.396 -10.525 1.00 25.99  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.187  -18.101 -10.599 1.00 29.16  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.176  -17.769 -12.803 1.00 24.93  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.014   -18.129 -13.667 1.00 26.21  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.222   -17.445 -13.581 1.00 33.17  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.879   -19.145 -14.603 1.00 35.00  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.302   -17.816 -14.383 1.00 39.57  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 1.941   -19.479 -15.412 1.00 37.11  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.142   -18.823 -15.313 1.00 30.55  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.113  -16.301 -9.765  1.00 21.20  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.221  -15.926 -8.901  1.00 18.76  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.473  -14.438 -9.012  1.00 20.79  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.620  -13.621 -9.369  1.00 20.36  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.879  -16.250 -7.445  1.00 23.05  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.802  -17.722 -7.094  1.00 23.33  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.390  -17.822 -5.610  1.00 23.55  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.240  -18.276 -7.241  1.00 27.17  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.764  -14.076 -8.776  1.00 19.31  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.104  -12.664 -8.675  1.00 21.94  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.138  -12.194 -7.214  1.00 18.49  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.039  -13.004 -6.286  1.00 18.11  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.189  -10.868 -7.017  1.00 19.25  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.169  -10.263 -5.682  1.00 18.99  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.133  -10.773 -4.633  1.00 18.52  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.846  -10.735 -3.443  1.00 19.06  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.343  -8.757  -5.932  1.00 20.44  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.774  -8.585  -7.351  1.00 22.02  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.183  -9.851  -8.098  1.00 19.31  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.288  -11.282 -5.117  1.00 20.51  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.249  -11.835 -4.157  1.00 20.88  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.693  -12.988 -3.301  1.00 19.59  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.127  -13.219 -2.167  1.00 19.67  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.550  -12.324 -4.830  1.00 25.21  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.377  -13.638 -5.563  1.00 27.55  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.668  -14.022 -6.310  1.00 34.84  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.594  -15.365 -6.966  1.00 36.44  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.602  -16.472 -5.999  1.00 40.44  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.587  -13.642 -3.777  1.00 18.41  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.035  -14.799 -3.123  1.00 19.91  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.673  -14.452 -2.500  1.00 17.79  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.024  -15.336 -1.988  1.00 20.67  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.925  -15.946 -4.121  1.00 21.36  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.323  -16.500 -4.418  1.00 24.70  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.160  -16.520 -3.472  1.00 26.90  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.564  -16.883 -5.569  1.00 28.31  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.380  -13.159 -2.446  1.00 17.30  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.052  -12.728 -1.955  1.00 16.08  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.162  -11.877 -0.687  1.00 15.60  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.740  -10.768 -0.715  1.00 17.26  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.301  -11.953 -3.055  1.00 17.51  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.129  -12.709 -4.354  1.00 18.33  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.455  -11.847 -5.414  1.00 20.24  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.417  -14.026 -4.193  1.00 17.99  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.576  -12.346 0.416   1.00 17.70  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.651  -11.660 1.728   1.00 17.86  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.271  -11.148 2.125   1.00 18.81  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.645   -11.958 2.325   1.00 19.57  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.154  -12.698 2.736   1.00 19.98  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.588  -13.146 2.474   1.00 19.68  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.908  -14.060 1.479   1.00 19.68  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.587  -12.577 3.260   1.00 21.12  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.246  -14.419 1.241   1.00 23.14  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.887  -12.947 2.986   1.00 21.12  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.205  -13.829 2.020   1.00 21.19  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.044  -9.844  2.230   1.00 19.21  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.317   -9.361  2.520   1.00 18.46  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.840   -10.008 3.802   1.00 19.44  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.191   -10.145 4.831   1.00 21.78  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.096   -7.844  2.663   1.00 22.29  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.063  -7.545  1.628   1.00 23.46  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -1.004  -8.745  1.901   1.00 21.11  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.133   -10.449 3.776   1.00 19.72  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.662   -11.277 4.832   1.00 19.90  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.734   -10.566 6.199   1.00 20.84  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.386   -11.233 7.163   1.00 24.25  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.114   -11.603 4.373   1.00 20.51  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.905   -12.429 5.392   1.00 19.89  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.599   -13.765 5.642   1.00 20.83  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.937   -11.827 6.106   1.00 26.03  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.273   -14.541 6.594   1.00 24.27  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.607   -12.601 7.044   1.00 24.30  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.293   -13.920 7.288   1.00 23.47  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.060   -14.632 8.229   1.00 28.22  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.167   -9.289  6.225   1.00 21.68  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.305   -8.569  7.505   1.00 26.33  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.964   -8.561  8.267   1.00 23.54  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.902   -9.039  9.408   1.00 31.55  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.144   -7.303  7.407   1.00 27.74  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 1.891   -8.155  7.569   1.00 26.15  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 0.569   -8.100  8.195   1.00 27.01  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? 0.067   -9.476  8.641   1.00 29.45  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.651  -9.581  9.646   1.00 28.14  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? -0.413  -7.524  7.163   1.00 26.91  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.870  -7.368  7.686   1.00 28.42  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.670  -6.585  6.653   1.00 29.19  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.642  -5.690  7.333   1.00 41.05  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.790  -6.444  7.844   1.00 42.07  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.389   -10.549 7.890   1.00 24.47  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? -0.306  -11.827 7.976   1.00 24.30  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 0.471   -12.897 8.755   1.00 23.85  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? -0.049  -13.988 9.004   1.00 24.55  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.605  -12.384 6.589   1.00 27.27  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.401  -11.429 5.914   1.00 32.24  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 1.732   -12.626 9.102   1.00 24.55  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 2.559   -13.713 9.622   1.00 27.12  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 2.145   -14.215 11.011  1.00 25.90  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.284   -15.398 11.311  1.00 28.96  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 4.044   -13.339 9.591   1.00 26.19  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.426   -12.147 10.447  1.00 28.75  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 5.936   -12.066 10.257  1.00 38.08  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.503   -11.189 11.342  1.00 42.57  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.009   -9.825  11.116  1.00 49.45  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 1.596   -13.319 11.839  0.50 28.72  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 1.602   -13.313 11.843  0.50 28.92  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 1.121   -13.761 13.146  0.50 31.61  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 1.073   -13.736 13.137  0.50 32.17  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? 0.034   -14.834 12.982  0.50 31.54  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? 0.072   -14.874 12.937  0.50 31.66  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? -0.022  -15.797 13.738  0.50 34.35  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? 0.110   -15.893 13.622  0.50 34.14  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 0.790   -12.581 14.053  0.50 33.65  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.395   -12.595 13.884  0.50 34.98  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 1.968   -11.740 14.533  0.50 35.32  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? -0.117  -12.936 15.279  0.50 39.01  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.131   -12.195 14.403  0.50 38.67  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 0.726   -13.089 16.188  0.50 41.17  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 1.725   -10.619 15.027  0.50 39.43  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.353  -13.041 15.446  0.50 45.55  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.817  -14.700 11.950  1.00 26.81  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -1.898  -15.632 11.734  1.00 25.90  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -1.479  -16.874 10.962  1.00 28.25  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -1.944  -17.967 11.262  1.00 29.90  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -2.980  -14.829 11.012  1.00 28.83  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -4.213  -15.623 10.755  1.00 28.17  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -5.227  -14.651 10.130  1.00 34.28  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.442  -15.363 9.631   1.00 42.12  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.466  -14.375 9.237   1.00 41.64  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.655  -16.707 9.910   1.00 27.77  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? -0.405  -17.829 9.006   1.00 25.82  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 0.995   -18.447 9.160   1.00 22.39  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.211   -19.533 8.609   1.00 25.65  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.611  -17.356 7.550   1.00 22.50  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -2.008  -16.891 7.155   1.00 25.40  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -3.125  -17.642 7.517   1.00 27.32  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -2.189  -15.702 6.434   1.00 23.24  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -4.403  -17.242 7.147   1.00 27.09  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -3.469  -15.305 6.062   1.00 27.43  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -4.566  -16.069 6.427   1.00 28.24  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.810  -15.662 6.023   1.00 28.42  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 1.881   -17.804 9.915   1.00 24.69  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.283   -18.241 10.026  1.00 24.27  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.475   -19.214 11.196  1.00 28.18  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.127   -18.893 12.164  1.00 34.60  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 2.832   -20.360 11.099  1.00 29.40  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 2.903   -21.382 12.127  1.00 32.33  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 3.134   -22.724 11.434  1.00 27.14  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 2.721   -22.963 10.308  1.00 30.76  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 1.642   -21.301 13.008  1.00 33.64  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 1.638   -20.096 13.959  1.00 38.73  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? 0.642   -20.210 15.112  1.00 46.86  ? 70  LYS A CD  1 
ATOM   567  N N   . PRO A 1 72 ? 3.774   -23.723 12.092  1.00 28.87  ? 71  PRO A N   1 
ATOM   568  C CA  . PRO A 1 72 ? 4.050   -24.976 11.387  1.00 28.54  ? 71  PRO A CA  1 
ATOM   569  C C   . PRO A 1 72 ? 2.839   -25.711 10.845  1.00 28.11  ? 71  PRO A C   1 
ATOM   570  O O   . PRO A 1 72 ? 1.744   -25.625 11.411  1.00 37.14  ? 71  PRO A O   1 
ATOM   571  C CB  . PRO A 1 72 ? 4.865   -25.815 12.400  1.00 35.13  ? 71  PRO A CB  1 
ATOM   572  C CG  . PRO A 1 72 ? 5.414   -24.768 13.325  1.00 33.80  ? 71  PRO A CG  1 
ATOM   573  C CD  . PRO A 1 72 ? 4.328   -23.667 13.450  1.00 36.32  ? 71  PRO A CD  1 
ATOM   574  N N   . ASN A 1 73 ? 3.061   -26.452 9.769   1.00 34.49  ? 72  ASN A N   1 
ATOM   575  C CA  . ASN A 1 73 ? 1.998   -27.177 9.119   1.00 38.01  ? 72  ASN A CA  1 
ATOM   576  C C   . ASN A 1 73 ? 2.561   -28.527 8.717   1.00 40.33  ? 72  ASN A C   1 
ATOM   577  O O   . ASN A 1 73 ? 3.737   -28.656 8.396   1.00 39.42  ? 72  ASN A O   1 
ATOM   578  C CB  . ASN A 1 73 ? 1.504   -26.408 7.896   1.00 37.63  ? 72  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 73 ? 0.143   -26.872 7.442   1.00 41.70  ? 72  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 73 ? 0.046   -27.697 6.531   1.00 41.44  ? 72  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 73 ? -0.906  -26.339 8.047   1.00 44.01  ? 72  ASN A ND2 1 
ATOM   582  N N   . LYS A 1 74 ? 1.692   -29.532 8.758   1.00 45.80  ? 73  LYS A N   1 
ATOM   583  C CA  . LYS A 1 74 ? 2.037   -30.896 8.424   1.00 44.70  ? 73  LYS A CA  1 
ATOM   584  C C   . LYS A 1 74 ? 2.435   -31.015 6.953   1.00 42.99  ? 73  LYS A C   1 
ATOM   585  O O   . LYS A 1 74 ? 3.151   -31.951 6.573   1.00 43.37  ? 73  LYS A O   1 
ATOM   586  C CB  . LYS A 1 74 ? 0.831   -31.757 8.848   1.00 46.41  ? 73  LYS A CB  1 
ATOM   587  C CG  . LYS A 1 74 ? -0.322  -31.861 7.846   1.00 44.92  ? 73  LYS A CG  1 
ATOM   588  N N   . ARG A 1 75 ? 1.971   -30.076 6.106   1.00 35.79  ? 74  ARG A N   1 
ATOM   589  C CA  . ARG A 1 75 ? 2.062   -30.285 4.668   1.00 35.95  ? 74  ARG A CA  1 
ATOM   590  C C   . ARG A 1 75 ? 3.513   -30.242 4.183   1.00 35.04  ? 74  ARG A C   1 
ATOM   591  O O   . ARG A 1 75 ? 4.332   -29.482 4.719   1.00 30.48  ? 74  ARG A O   1 
ATOM   592  C CB  . ARG A 1 75 ? 1.119   -29.336 3.910   1.00 39.52  ? 74  ARG A CB  1 
ATOM   593  C CG  . ARG A 1 75 ? -0.334  -29.581 4.287   1.00 47.74  ? 74  ARG A CG  1 
ATOM   594  C CD  . ARG A 1 75 ? -0.946  -30.657 3.423   1.00 44.86  ? 74  ARG A CD  1 
ATOM   595  N NE  . ARG A 1 75 ? -1.789  -30.113 2.352   1.00 66.33  ? 74  ARG A NE  1 
ATOM   596  C CZ  . ARG A 1 75 ? -2.963  -29.508 2.557   1.00 63.60  ? 74  ARG A CZ  1 
ATOM   597  N NH1 . ARG A 1 75 ? -3.712  -29.184 1.524   1.00 65.77  ? 74  ARG A NH1 1 
ATOM   598  N NH2 . ARG A 1 75 ? -3.410  -29.283 3.787   1.00 70.17  ? 74  ARG A NH2 1 
ATOM   599  N N   . LYS A 1 76 ? 3.796   -31.058 3.165   1.00 33.72  ? 75  LYS A N   1 
ATOM   600  C CA  . LYS A 1 76 ? 5.136   -31.236 2.618   1.00 34.51  ? 75  LYS A CA  1 
ATOM   601  C C   . LYS A 1 76 ? 5.718   -29.880 2.219   1.00 29.31  ? 75  LYS A C   1 
ATOM   602  O O   . LYS A 1 76 ? 5.163   -29.200 1.356   1.00 29.49  ? 75  LYS A O   1 
ATOM   603  C CB  . LYS A 1 76 ? 5.137   -32.192 1.417   1.00 37.54  ? 75  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 76 ? 6.451   -32.411 0.701   1.00 42.28  ? 75  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 76 ? 6.333   -33.516 -0.344  1.00 43.64  ? 75  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 76 ? 7.621   -33.965 -0.968  1.00 49.53  ? 75  LYS A CE  1 
ATOM   607  N N   . GLY A 1 77 ? 6.848   -29.543 2.846   1.00 29.58  ? 76  GLY A N   1 
ATOM   608  C CA  . GLY A 1 77 ? 7.628   -28.403 2.399   1.00 28.82  ? 76  GLY A CA  1 
ATOM   609  C C   . GLY A 1 77 ? 7.240   -27.123 3.134   1.00 27.33  ? 76  GLY A C   1 
ATOM   610  O O   . GLY A 1 77 ? 7.905   -26.110 2.974   1.00 25.07  ? 76  GLY A O   1 
ATOM   611  N N   . PHE A 1 78 ? 6.197   -27.160 3.952   1.00 26.49  ? 77  PHE A N   1 
ATOM   612  C CA  . PHE A 1 78 ? 5.707   -25.923 4.516   1.00 25.77  ? 77  PHE A CA  1 
ATOM   613  C C   . PHE A 1 78 ? 6.695   -25.363 5.531   1.00 26.75  ? 77  PHE A C   1 
ATOM   614  O O   . PHE A 1 78 ? 6.976   -24.166 5.556   1.00 25.50  ? 77  PHE A O   1 
ATOM   615  C CB  . PHE A 1 78 ? 4.342   -26.204 5.144   1.00 25.03  ? 77  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 78 ? 3.620   -24.923 5.542   1.00 24.34  ? 77  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 78 ? 3.880   -24.271 6.743   1.00 24.93  ? 77  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 78 ? 2.661   -24.382 4.677   1.00 26.69  ? 77  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 78 ? 3.229   -23.090 7.093   1.00 28.10  ? 77  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 78 ? 1.966   -23.220 5.058   1.00 23.82  ? 77  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 78 ? 2.266   -22.575 6.238   1.00 24.18  ? 77  PHE A CZ  1 
ATOM   622  N N   . ASN A 1 79 ? 7.228   -26.205 6.421   1.00 23.75  ? 78  ASN A N   1 
ATOM   623  C CA  . ASN A 1 79 ? 8.089   -25.686 7.472   1.00 22.96  ? 78  ASN A CA  1 
ATOM   624  C C   . ASN A 1 79 ? 9.454   -25.238 6.893   1.00 22.34  ? 78  ASN A C   1 
ATOM   625  O O   . ASN A 1 79 ? 10.002  -24.242 7.386   1.00 23.87  ? 78  ASN A O   1 
ATOM   626  C CB  . ASN A 1 79 ? 8.267   -26.746 8.568   1.00 26.42  ? 78  ASN A CB  1 
ATOM   627  C CG  . ASN A 1 79 ? 6.942   -27.031 9.232   1.00 31.11  ? 78  ASN A CG  1 
ATOM   628  O OD1 . ASN A 1 79 ? 6.002   -26.216 9.188   1.00 28.93  ? 78  ASN A OD1 1 
ATOM   629  N ND2 . ASN A 1 79 ? 6.866   -28.183 9.896   1.00 29.51  ? 78  ASN A ND2 1 
ATOM   630  N N   . GLU A 1 80 ? 9.974   -25.930 5.858   1.00 22.76  ? 79  GLU A N   1 
ATOM   631  C CA  . GLU A 1 80 ? 11.133  -25.419 5.126   1.00 22.01  ? 79  GLU A CA  1 
ATOM   632  C C   . GLU A 1 80 ? 10.796  -24.035 4.577   1.00 21.04  ? 79  GLU A C   1 
ATOM   633  O O   . GLU A 1 80 ? 11.605  -23.100 4.616   1.00 20.90  ? 79  GLU A O   1 
ATOM   634  C CB  . GLU A 1 80 ? 11.536  -26.340 3.978   1.00 23.81  ? 79  GLU A CB  1 
ATOM   635  C CG  . GLU A 1 80 ? 12.790  -25.870 3.233   1.00 24.62  ? 79  GLU A CG  1 
ATOM   636  C CD  . GLU A 1 80 ? 13.305  -26.892 2.222   1.00 36.54  ? 79  GLU A CD  1 
ATOM   637  O OE1 . GLU A 1 80 ? 12.571  -27.858 1.928   1.00 42.76  ? 79  GLU A OE1 1 
ATOM   638  O OE2 . GLU A 1 80 ? 14.444  -26.737 1.750   1.00 35.38  ? 79  GLU A OE2 1 
ATOM   639  N N   . GLY A 1 81 ? 9.569   -23.925 4.067   1.00 21.83  ? 80  GLY A N   1 
ATOM   640  C CA  . GLY A 1 81 ? 9.137   -22.647 3.487   1.00 22.82  ? 80  GLY A CA  1 
ATOM   641  C C   . GLY A 1 81 ? 9.088   -21.522 4.535   1.00 20.85  ? 80  GLY A C   1 
ATOM   642  O O   . GLY A 1 81 ? 9.452   -20.379 4.222   1.00 19.42  ? 80  GLY A O   1 
ATOM   643  N N   . LEU A 1 82 ? 8.651   -21.804 5.772   1.00 19.07  ? 81  LEU A N   1 
ATOM   644  C CA  . LEU A 1 82 ? 8.681   -20.815 6.823   1.00 20.03  ? 81  LEU A CA  1 
ATOM   645  C C   . LEU A 1 82 ? 10.119  -20.354 7.135   1.00 19.98  ? 81  LEU A C   1 
ATOM   646  O O   . LEU A 1 82 ? 10.339  -19.163 7.392   1.00 21.04  ? 81  LEU A O   1 
ATOM   647  C CB  . LEU A 1 82 ? 8.009   -21.329 8.096   1.00 21.83  ? 81  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 82 ? 6.513   -21.644 7.982   1.00 23.81  ? 81  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 82 ? 6.157   -22.205 9.344   1.00 26.30  ? 81  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 82 ? 5.748   -20.361 7.822   1.00 23.21  ? 81  LEU A CD2 1 
ATOM   651  N N   . TRP A 1 83 ? 11.099  -21.280 7.031   1.00 20.92  ? 82  TRP A N   1 
ATOM   652  C CA  . TRP A 1 83 ? 12.464  -20.884 7.318   1.00 22.04  ? 82  TRP A CA  1 
ATOM   653  C C   . TRP A 1 83 ? 12.930  -19.939 6.218   1.00 19.64  ? 82  TRP A C   1 
ATOM   654  O O   . TRP A 1 83 ? 13.589  -18.955 6.513   1.00 19.80  ? 82  TRP A O   1 
ATOM   655  C CB  . TRP A 1 83 ? 13.401  -22.121 7.432   1.00 21.53  ? 82  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 83 ? 14.842  -21.729 7.709   1.00 20.38  ? 82  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 83 ? 15.456  -21.600 8.925   1.00 24.15  ? 82  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 83 ? 15.819  -21.431 6.690   1.00 19.66  ? 82  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 83 ? 16.767  -21.241 8.727   1.00 24.01  ? 82  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 83 ? 16.998  -21.101 7.376   1.00 22.73  ? 82  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 83 ? 15.777  -21.377 5.286   1.00 20.98  ? 82  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 83 ? 18.159  -20.743 6.685   1.00 23.60  ? 82  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 83 ? 16.929  -21.020 4.595   1.00 22.93  ? 82  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 83 ? 18.115  -20.729 5.303   1.00 24.71  ? 82  TRP A CH2 1 
ATOM   665  N N   . GLU A 1 84 ? 12.648  -20.278 4.964   1.00 19.19  ? 83  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84 ? 13.154  -19.540 3.833   1.00 17.80  ? 83  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84 ? 12.615  -18.115 3.850   1.00 20.61  ? 83  GLU A C   1 
ATOM   668  O O   . GLU A 1 84 ? 13.328  -17.159 3.632   1.00 19.73  ? 83  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84 ? 12.757  -20.194 2.523   1.00 18.31  ? 83  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84 ? 13.474  -21.537 2.367   1.00 19.55  ? 83  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84 ? 13.056  -22.291 1.098   1.00 22.85  ? 83  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84 ? 12.138  -21.895 0.358   1.00 21.16  ? 83  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84 ? 13.647  -23.380 0.777   1.00 24.06  ? 83  GLU A OE2 1 
ATOM   674  N N   . ILE A 1 85 ? 11.301  -17.949 4.099   1.00 17.35  ? 84  ILE A N   1 
ATOM   675  C CA  . ILE A 1 85 ? 10.749  -16.613 3.982   1.00 18.37  ? 84  ILE A CA  1 
ATOM   676  C C   . ILE A 1 85 ? 11.284  -15.705 5.104   1.00 19.22  ? 84  ILE A C   1 
ATOM   677  O O   . ILE A 1 85 ? 11.416  -14.497 4.926   1.00 19.27  ? 84  ILE A O   1 
ATOM   678  C CB  . ILE A 1 85 ? 9.205   -16.647 3.970   1.00 17.70  ? 84  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 85 ? 8.593   -15.280 3.536   1.00 17.16  ? 84  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 85 ? 8.638   -17.028 5.362   1.00 19.53  ? 84  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 85 ? 7.139   -15.432 3.052   1.00 17.11  ? 84  ILE A CD1 1 
ATOM   682  N N   . GLN A 1 86 ? 11.575  -16.284 6.278   1.00 18.53  ? 85  GLN A N   1 
ATOM   683  C CA  . GLN A 1 86 ? 12.124  -15.529 7.425   1.00 20.92  ? 85  GLN A CA  1 
ATOM   684  C C   . GLN A 1 86 ? 13.621  -15.248 7.274   1.00 20.94  ? 85  GLN A C   1 
ATOM   685  O O   . GLN A 1 86 ? 14.070  -14.126 7.656   1.00 23.72  ? 85  GLN A O   1 
ATOM   686  C CB  . GLN A 1 86 ? 11.762  -16.270 8.714   1.00 22.61  ? 85  GLN A CB  1 
ATOM   687  C CG  . GLN A 1 86 ? 12.247  -15.588 9.996   1.00 26.51  ? 85  GLN A CG  1 
ATOM   688  C CD  . GLN A 1 86 ? 11.604  -16.180 11.250  1.00 30.82  ? 85  GLN A CD  1 
ATOM   689  O OE1 . GLN A 1 86 ? 11.319  -17.392 11.320  1.00 34.26  ? 85  GLN A OE1 1 
ATOM   690  N NE2 . GLN A 1 86 ? 11.275  -15.316 12.209  1.00 36.95  ? 85  GLN A NE2 1 
ATOM   691  N N   . ASN A 1 87 ? 14.372  -16.214 6.726   1.00 19.76  ? 86  ASN A N   1 
ATOM   692  C CA  . ASN A 1 87 ? 15.844  -16.214 6.801   1.00 19.54  ? 86  ASN A CA  1 
ATOM   693  C C   . ASN A 1 87 ? 16.566  -15.906 5.508   1.00 20.40  ? 86  ASN A C   1 
ATOM   694  O O   . ASN A 1 87 ? 17.689  -15.332 5.574   1.00 20.77  ? 86  ASN A O   1 
ATOM   695  C CB  . ASN A 1 87 ? 16.371  -17.482 7.463   1.00 20.74  ? 86  ASN A CB  1 
ATOM   696  C CG  . ASN A 1 87 ? 15.888  -17.573 8.895   1.00 23.88  ? 86  ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 87 ? 16.221  -16.694 9.710   1.00 27.74  ? 86  ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 87 ? 14.942  -18.454 9.198   1.00 23.87  ? 86  ASN A ND2 1 
ATOM   699  N N   . ASN A 1 88 ? 15.991  -16.223 4.345   1.00 19.46  ? 87  ASN A N   1 
ATOM   700  C CA  . ASN A 1 88 ? 16.669  -15.891 3.096   1.00 17.57  ? 87  ASN A CA  1 
ATOM   701  C C   . ASN A 1 88 ? 15.622  -15.821 1.970   1.00 20.12  ? 87  ASN A C   1 
ATOM   702  O O   . ASN A 1 88 ? 15.675  -16.547 0.977   1.00 20.23  ? 87  ASN A O   1 
ATOM   703  C CB  . ASN A 1 88 ? 17.862  -16.801 2.776   1.00 21.26  ? 87  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 88 ? 18.909  -16.173 1.879   1.00 23.33  ? 87  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 88 ? 18.679  -15.166 1.198   1.00 22.20  ? 87  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 88 ? 20.129  -16.739 1.880   1.00 27.38  ? 87  ASN A ND2 1 
ATOM   707  N N   . PRO A 1 89 ? 14.718  -14.849 2.073   1.00 18.99  ? 88  PRO A N   1 
ATOM   708  C CA  . PRO A 1 89 ? 13.583  -14.854 1.157   1.00 17.71  ? 88  PRO A CA  1 
ATOM   709  C C   . PRO A 1 89 ? 13.916  -14.421 -0.250  1.00 19.73  ? 88  PRO A C   1 
ATOM   710  O O   . PRO A 1 89 ? 13.118  -14.645 -1.132  1.00 18.84  ? 88  PRO A O   1 
ATOM   711  C CB  . PRO A 1 89 ? 12.639  -13.836 1.813   1.00 17.63  ? 88  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 89 ? 13.581  -12.904 2.523   1.00 17.62  ? 88  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 89 ? 14.633  -13.830 3.136   1.00 18.83  ? 88  PRO A CD  1 
ATOM   714  N N   . HIS A 1 90 ? 15.111  -13.802 -0.479  1.00 16.33  ? 89  HIS A N   1 
ATOM   715  C CA  . HIS A 1 90 ? 15.445  -13.320 -1.805  1.00 18.01  ? 89  HIS A CA  1 
ATOM   716  C C   . HIS A 1 90 ? 16.594  -14.116 -2.469  1.00 17.32  ? 89  HIS A C   1 
ATOM   717  O O   . HIS A 1 90 ? 17.033  -13.732 -3.557  1.00 20.91  ? 89  HIS A O   1 
ATOM   718  C CB  . HIS A 1 90 ? 15.845  -11.834 -1.649  1.00 16.75  ? 89  HIS A CB  1 
ATOM   719  C CG  . HIS A 1 90 ? 14.742  -11.000 -1.081  1.00 15.61  ? 89  HIS A CG  1 
ATOM   720  N ND1 . HIS A 1 90 ? 13.493  -10.888 -1.700  1.00 17.80  ? 89  HIS A ND1 1 
ATOM   721  C CD2 . HIS A 1 90 ? 14.727  -10.255 0.016   1.00 16.75  ? 89  HIS A CD2 1 
ATOM   722  C CE1 . HIS A 1 90 ? 12.756  -10.077 -0.987  1.00 17.32  ? 89  HIS A CE1 1 
ATOM   723  N NE2 . HIS A 1 90 ? 13.444  -9.671  0.069   1.00 19.56  ? 89  HIS A NE2 1 
ATOM   724  N N   . ALA A 1 91 ? 16.843  -15.308 -1.946  1.00 18.22  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 91 ? 17.897  -16.175 -2.490  1.00 19.45  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 91 ? 17.446  -16.861 -3.771  1.00 22.23  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 91 ? 16.266  -16.978 -4.073  1.00 22.79  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 91 ? 18.289  -17.211 -1.477  1.00 20.30  ? 90  ALA A CB  1 
ATOM   729  N N   . SER A 1 92 ? 18.423  -17.359 -4.545  1.00 23.40  ? 91  SER A N   1 
ATOM   730  C CA  . SER A 1 92 ? 18.190  -18.307 -5.620  1.00 26.55  ? 91  SER A CA  1 
ATOM   731  C C   . SER A 1 92 ? 17.915  -19.694 -5.040  1.00 26.50  ? 91  SER A C   1 
ATOM   732  O O   . SER A 1 92 ? 18.720  -20.228 -4.261  1.00 28.99  ? 91  SER A O   1 
ATOM   733  C CB  . SER A 1 92 ? 19.399  -18.311 -6.491  1.00 32.02  ? 91  SER A CB  1 
ATOM   734  O OG  . SER A 1 92 ? 19.279  -19.402 -7.374  1.00 39.67  ? 91  SER A OG  1 
ATOM   735  N N   . TYR A 1 93 ? 16.751  -20.263 -5.372  1.00 25.52  ? 92  TYR A N   1 
ATOM   736  C CA  . TYR A 1 93 ? 16.357  -21.602 -4.950  1.00 26.45  ? 92  TYR A CA  1 
ATOM   737  C C   . TYR A 1 93 ? 16.272  -22.549 -6.146  1.00 31.40  ? 92  TYR A C   1 
ATOM   738  O O   . TYR A 1 93 ? 15.789  -23.665 -5.986  1.00 39.73  ? 92  TYR A O   1 
ATOM   739  C CB  . TYR A 1 93 ? 14.997  -21.554 -4.206  1.00 24.92  ? 92  TYR A CB  1 
ATOM   740  C CG  . TYR A 1 93 ? 15.156  -20.963 -2.815  1.00 22.61  ? 92  TYR A CG  1 
ATOM   741  C CD1 . TYR A 1 93 ? 15.594  -21.712 -1.705  1.00 24.83  ? 92  TYR A CD1 1 
ATOM   742  C CD2 . TYR A 1 93 ? 14.821  -19.614 -2.585  1.00 22.44  ? 92  TYR A CD2 1 
ATOM   743  C CE1 . TYR A 1 93 ? 15.781  -21.134 -0.446  1.00 24.12  ? 92  TYR A CE1 1 
ATOM   744  C CE2 . TYR A 1 93 ? 14.938  -19.077 -1.322  1.00 23.42  ? 92  TYR A CE2 1 
ATOM   745  C CZ  . TYR A 1 93 ? 15.413  -19.808 -0.250  1.00 22.20  ? 92  TYR A CZ  1 
ATOM   746  O OH  . TYR A 1 93 ? 15.666  -19.298 0.993   1.00 25.04  ? 92  TYR A OH  1 
ATOM   747  N N   . SER A 1 94 ? 16.731  -22.088 -7.308  1.00 38.56  ? 93  SER A N   1 
ATOM   748  C CA  . SER A 1 94 ? 16.824  -22.880 -8.530  1.00 53.79  ? 93  SER A CA  1 
ATOM   749  C C   . SER A 1 94 ? 17.930  -23.944 -8.408  1.00 64.08  ? 93  SER A C   1 
ATOM   750  O O   . SER A 1 94 ? 18.813  -23.773 -7.538  1.00 64.71  ? 93  SER A O   1 
ATOM   751  C CB  . SER A 1 94 ? 17.095  -21.978 -9.709  1.00 49.48  ? 93  SER A CB  1 
ATOM   752  O OG  . SER A 1 94 ? 16.008  -21.091 -9.926  1.00 59.04  ? 93  SER A OG  1 
ATOM   753  O OXT . SER A 1 94 ? 17.888  -24.907 -9.212  1.00 79.36  ? 93  SER A OXT 1 
ATOM   754  N N   . MET B 1 2  ? 38.768  -10.996 -42.150 1.00 65.23  ? 1   MET B N   1 
ATOM   755  C CA  . MET B 1 2  ? 38.476  -11.967 -43.236 1.00 64.84  ? 1   MET B CA  1 
ATOM   756  C C   . MET B 1 2  ? 36.962  -12.170 -43.286 1.00 57.33  ? 1   MET B C   1 
ATOM   757  O O   . MET B 1 2  ? 36.365  -12.493 -42.257 1.00 58.77  ? 1   MET B O   1 
ATOM   758  C CB  . MET B 1 2  ? 39.208  -13.291 -42.973 1.00 73.53  ? 1   MET B CB  1 
ATOM   759  C CG  . MET B 1 2  ? 39.343  -14.219 -44.176 1.00 90.04  ? 1   MET B CG  1 
ATOM   760  S SD  . MET B 1 2  ? 40.360  -13.620 -45.545 1.00 95.93  ? 1   MET B SD  1 
ATOM   761  C CE  . MET B 1 2  ? 41.742  -12.830 -44.705 1.00 86.62  ? 1   MET B CE  1 
ATOM   762  N N   . PRO B 1 3  ? 36.282  -11.963 -44.448 1.00 47.24  ? 2   PRO B N   1 
ATOM   763  C CA  . PRO B 1 3  ? 34.833  -12.177 -44.522 1.00 43.93  ? 2   PRO B CA  1 
ATOM   764  C C   . PRO B 1 3  ? 34.501  -13.606 -44.108 1.00 47.99  ? 2   PRO B C   1 
ATOM   765  O O   . PRO B 1 3  ? 35.332  -14.497 -44.236 1.00 44.80  ? 2   PRO B O   1 
ATOM   766  C CB  . PRO B 1 3  ? 34.442  -11.875 -45.963 1.00 41.43  ? 2   PRO B CB  1 
ATOM   767  C CG  . PRO B 1 3  ? 35.594  -10.995 -46.450 1.00 40.33  ? 2   PRO B CG  1 
ATOM   768  C CD  . PRO B 1 3  ? 36.845  -11.485 -45.722 1.00 41.85  ? 2   PRO B CD  1 
ATOM   769  N N   . HIS B 1 4  ? 33.306  -13.784 -43.533 1.00 44.29  ? 3   HIS B N   1 
ATOM   770  C CA  . HIS B 1 4  ? 32.891  -15.096 -43.060 1.00 45.25  ? 3   HIS B CA  1 
ATOM   771  C C   . HIS B 1 4  ? 31.534  -15.413 -43.680 1.00 41.61  ? 3   HIS B C   1 
ATOM   772  O O   . HIS B 1 4  ? 30.927  -14.549 -44.324 1.00 40.92  ? 3   HIS B O   1 
ATOM   773  C CB  . HIS B 1 4  ? 32.996  -15.187 -41.532 1.00 48.58  ? 3   HIS B CB  1 
ATOM   774  C CG  . HIS B 1 4  ? 34.406  -15.370 -41.048 1.00 62.02  ? 3   HIS B CG  1 
ATOM   775  N ND1 . HIS B 1 4  ? 35.293  -16.268 -41.617 1.00 63.29  ? 3   HIS B ND1 1 
ATOM   776  C CD2 . HIS B 1 4  ? 35.075  -14.775 -40.037 1.00 56.88  ? 3   HIS B CD2 1 
ATOM   777  C CE1 . HIS B 1 4  ? 36.450  -16.208 -40.969 1.00 56.37  ? 3   HIS B CE1 1 
ATOM   778  N NE2 . HIS B 1 4  ? 36.337  -15.311 -40.006 1.00 60.02  ? 3   HIS B NE2 1 
ATOM   779  N N   . ALA B 1 5  ? 31.049  -16.651 -43.500 1.00 36.26  ? 4   ALA B N   1 
ATOM   780  C CA  . ALA B 1 5  ? 29.734  -16.957 -44.046 1.00 40.34  ? 4   ALA B CA  1 
ATOM   781  C C   . ALA B 1 5  ? 28.729  -15.920 -43.564 1.00 37.26  ? 4   ALA B C   1 
ATOM   782  O O   . ALA B 1 5  ? 27.946  -15.406 -44.353 1.00 40.24  ? 4   ALA B O   1 
ATOM   783  C CB  . ALA B 1 5  ? 29.274  -18.334 -43.630 1.00 39.25  ? 4   ALA B CB  1 
ATOM   784  N N   . PHE B 1 6  ? 28.755  -15.678 -42.249 1.00 40.57  ? 5   PHE B N   1 
ATOM   785  C CA  . PHE B 1 6  ? 27.967  -14.633 -41.608 1.00 39.50  ? 5   PHE B CA  1 
ATOM   786  C C   . PHE B 1 6  ? 28.824  -13.391 -41.362 1.00 34.04  ? 5   PHE B C   1 
ATOM   787  O O   . PHE B 1 6  ? 29.954  -13.478 -40.861 1.00 41.18  ? 5   PHE B O   1 
ATOM   788  C CB  . PHE B 1 6  ? 27.407  -15.100 -40.260 1.00 39.47  ? 5   PHE B CB  1 
ATOM   789  C CG  . PHE B 1 6  ? 26.284  -16.129 -40.353 1.00 32.25  ? 5   PHE B CG  1 
ATOM   790  C CD1 . PHE B 1 6  ? 24.969  -15.733 -40.551 1.00 31.17  ? 5   PHE B CD1 1 
ATOM   791  C CD2 . PHE B 1 6  ? 26.554  -17.497 -40.279 1.00 35.17  ? 5   PHE B CD2 1 
ATOM   792  C CE1 . PHE B 1 6  ? 23.955  -16.674 -40.641 1.00 32.52  ? 5   PHE B CE1 1 
ATOM   793  C CE2 . PHE B 1 6  ? 25.531  -18.429 -40.375 1.00 29.62  ? 5   PHE B CE2 1 
ATOM   794  C CZ  . PHE B 1 6  ? 24.240  -18.021 -40.524 1.00 32.01  ? 5   PHE B CZ  1 
ATOM   795  N N   . LYS B 1 7  ? 28.242  -12.233 -41.655 1.00 36.76  ? 6   LYS B N   1 
ATOM   796  C CA  . LYS B 1 7  ? 28.962  -10.991 -41.432 1.00 38.48  ? 6   LYS B CA  1 
ATOM   797  C C   . LYS B 1 7  ? 28.207  -10.132 -40.417 1.00 35.82  ? 6   LYS B C   1 
ATOM   798  O O   . LYS B 1 7  ? 26.973  -10.223 -40.286 1.00 32.32  ? 6   LYS B O   1 
ATOM   799  C CB  . LYS B 1 7  ? 29.119  -10.250 -42.758 1.00 42.69  ? 6   LYS B CB  1 
ATOM   800  C CG  . LYS B 1 7  ? 27.827  -9.863  -43.433 1.00 39.43  ? 6   LYS B CG  1 
ATOM   801  C CD  . LYS B 1 7  ? 28.038  -9.436  -44.889 1.00 46.61  ? 6   LYS B CD  1 
ATOM   802  C CE  . LYS B 1 7  ? 26.777  -9.000  -45.583 1.00 46.86  ? 6   LYS B CE  1 
ATOM   803  N NZ  . LYS B 1 7  ? 25.806  -10.082 -45.825 1.00 50.17  ? 6   LYS B NZ  1 
ATOM   804  N N   . PRO B 1 8  ? 28.914  -9.205  -39.729 1.00 41.29  ? 7   PRO B N   1 
ATOM   805  C CA  . PRO B 1 8  ? 28.260  -8.257  -38.825 1.00 33.59  ? 7   PRO B CA  1 
ATOM   806  C C   . PRO B 1 8  ? 27.088  -7.580  -39.508 1.00 32.67  ? 7   PRO B C   1 
ATOM   807  O O   . PRO B 1 8  ? 27.192  -7.100  -40.658 1.00 36.53  ? 7   PRO B O   1 
ATOM   808  C CB  . PRO B 1 8  ? 29.395  -7.291  -38.500 1.00 40.54  ? 7   PRO B CB  1 
ATOM   809  C CG  . PRO B 1 8  ? 30.635  -8.180  -38.557 1.00 41.11  ? 7   PRO B CG  1 
ATOM   810  C CD  . PRO B 1 8  ? 30.371  -8.973  -39.817 1.00 44.38  ? 7   PRO B CD  1 
ATOM   811  N N   . GLY B 1 9  ? 25.968  -7.531  -38.777 1.00 27.45  ? 8   GLY B N   1 
ATOM   812  C CA  . GLY B 1 9  ? 24.746  -6.914  -39.248 1.00 27.94  ? 8   GLY B CA  1 
ATOM   813  C C   . GLY B 1 9  ? 23.756  -7.886  -39.880 1.00 26.27  ? 8   GLY B C   1 
ATOM   814  O O   . GLY B 1 9  ? 22.639  -7.527  -40.184 1.00 28.84  ? 8   GLY B O   1 
ATOM   815  N N   . ASP B 1 10 ? 24.216  -9.117  -40.181 1.00 29.54  ? 9   ASP B N   1 
ATOM   816  C CA  . ASP B 1 10 ? 23.324  -10.131 -40.699 1.00 30.65  ? 9   ASP B CA  1 
ATOM   817  C C   . ASP B 1 10 ? 22.253  -10.485 -39.659 1.00 23.17  ? 9   ASP B C   1 
ATOM   818  O O   . ASP B 1 10 ? 22.535  -10.521 -38.456 1.00 26.37  ? 9   ASP B O   1 
ATOM   819  C CB  . ASP B 1 10 ? 24.079  -11.402 -41.036 1.00 32.42  ? 9   ASP B CB  1 
ATOM   820  C CG  . ASP B 1 10 ? 24.782  -11.454 -42.391 1.00 39.34  ? 9   ASP B CG  1 
ATOM   821  O OD1 . ASP B 1 10 ? 24.428  -10.644 -43.272 1.00 36.46  ? 9   ASP B OD1 1 
ATOM   822  O OD2 . ASP B 1 10 ? 25.622  -12.371 -42.552 1.00 34.87  ? 9   ASP B OD2 1 
ATOM   823  N N   . LEU B 1 11 ? 21.050  -10.635 -40.166 1.00 23.34  ? 10  LEU B N   1 
ATOM   824  C CA  . LEU B 1 11 ? 19.909  -10.852 -39.274 1.00 24.02  ? 10  LEU B CA  1 
ATOM   825  C C   . LEU B 1 11 ? 19.603  -12.344 -39.275 1.00 24.17  ? 10  LEU B C   1 
ATOM   826  O O   . LEU B 1 11 ? 19.585  -12.936 -40.359 1.00 27.75  ? 10  LEU B O   1 
ATOM   827  C CB  . LEU B 1 11 ? 18.725  -10.032 -39.745 1.00 24.89  ? 10  LEU B CB  1 
ATOM   828  C CG  . LEU B 1 11 ? 19.037  -8.527  -39.827 1.00 22.56  ? 10  LEU B CG  1 
ATOM   829  C CD1 . LEU B 1 11 ? 17.767  -7.839  -40.234 1.00 25.65  ? 10  LEU B CD1 1 
ATOM   830  C CD2 . LEU B 1 11 ? 19.586  -8.070  -38.489 1.00 26.41  ? 10  LEU B CD2 1 
ATOM   831  N N   . VAL B 1 12 ? 19.276  -12.906 -38.096 1.00 22.87  ? 11  VAL B N   1 
ATOM   832  C CA  . VAL B 1 12 ? 19.028  -14.355 -38.009 1.00 23.25  ? 11  VAL B CA  1 
ATOM   833  C C   . VAL B 1 12 ? 17.907  -14.616 -36.996 1.00 23.17  ? 11  VAL B C   1 
ATOM   834  O O   . VAL B 1 12 ? 17.493  -13.718 -36.240 1.00 22.53  ? 11  VAL B O   1 
ATOM   835  C CB  . VAL B 1 12 ? 20.317  -15.077 -37.552 1.00 23.00  ? 11  VAL B CB  1 
ATOM   836  C CG1 . VAL B 1 12 ? 21.485  -14.882 -38.554 1.00 27.25  ? 11  VAL B CG1 1 
ATOM   837  C CG2 . VAL B 1 12 ? 20.776  -14.699 -36.129 1.00 23.23  ? 11  VAL B CG2 1 
ATOM   838  N N   . PHE B 1 13 ? 17.445  -15.875 -36.952 1.00 21.31  ? 12  PHE B N   1 
ATOM   839  C CA  . PHE B 1 13 ? 16.949  -16.409 -35.702 1.00 22.45  ? 12  PHE B CA  1 
ATOM   840  C C   . PHE B 1 13 ? 18.027  -17.295 -35.117 1.00 22.13  ? 12  PHE B C   1 
ATOM   841  O O   . PHE B 1 13 ? 18.687  -18.042 -35.867 1.00 23.74  ? 12  PHE B O   1 
ATOM   842  C CB  . PHE B 1 13 ? 15.713  -17.251 -35.986 1.00 21.88  ? 12  PHE B CB  1 
ATOM   843  C CG  . PHE B 1 13 ? 14.485  -16.441 -36.358 1.00 22.45  ? 12  PHE B CG  1 
ATOM   844  C CD1 . PHE B 1 13 ? 14.262  -16.095 -37.692 1.00 26.44  ? 12  PHE B CD1 1 
ATOM   845  C CD2 . PHE B 1 13 ? 13.571  -16.031 -35.392 1.00 24.77  ? 12  PHE B CD2 1 
ATOM   846  C CE1 . PHE B 1 13 ? 13.132  -15.368 -38.051 1.00 26.59  ? 12  PHE B CE1 1 
ATOM   847  C CE2 . PHE B 1 13 ? 12.479  -15.264 -35.747 1.00 25.38  ? 12  PHE B CE2 1 
ATOM   848  C CZ  . PHE B 1 13 ? 12.254  -14.948 -37.081 1.00 31.29  ? 12  PHE B CZ  1 
ATOM   849  N N   . ALA B 1 14 ? 18.241  -17.166 -33.797 1.00 23.26  ? 13  ALA B N   1 
ATOM   850  C CA  . ALA B 1 14 ? 19.302  -17.866 -33.097 1.00 21.32  ? 13  ALA B CA  1 
ATOM   851  C C   . ALA B 1 14 ? 18.699  -18.817 -32.058 1.00 20.73  ? 13  ALA B C   1 
ATOM   852  O O   . ALA B 1 14 ? 17.757  -18.446 -31.346 1.00 23.09  ? 13  ALA B O   1 
ATOM   853  C CB  . ALA B 1 14 ? 20.297  -16.919 -32.452 1.00 24.39  ? 13  ALA B CB  1 
ATOM   854  N N   . LYS B 1 15 ? 19.137  -20.068 -32.077 1.00 22.22  ? 14  LYS B N   1 
ATOM   855  C CA  . LYS B 1 15 ? 18.534  -21.102 -31.232 1.00 24.25  ? 14  LYS B CA  1 
ATOM   856  C C   . LYS B 1 15 ? 19.406  -21.442 -30.033 1.00 27.31  ? 14  LYS B C   1 
ATOM   857  O O   . LYS B 1 15 ? 20.578  -21.795 -30.168 1.00 28.21  ? 14  LYS B O   1 
ATOM   858  C CB  . LYS B 1 15 ? 18.353  -22.392 -32.046 1.00 25.51  ? 14  LYS B CB  1 
ATOM   859  C CG  . LYS B 1 15 ? 17.605  -23.520 -31.259 1.00 22.30  ? 14  LYS B CG  1 
ATOM   860  C CD  . LYS B 1 15 ? 16.159  -23.112 -30.973 1.00 28.87  ? 14  LYS B CD  1 
ATOM   861  C CE  . LYS B 1 15 ? 15.283  -24.204 -30.259 1.00 25.80  ? 14  LYS B CE  1 
ATOM   862  N NZ  . LYS B 1 15 ? 15.918  -24.449 -28.965 1.00 27.60  ? 14  LYS B NZ  1 
ATOM   863  N N   . MET B 1 16 ? 18.797  -21.344 -28.841 1.00 27.46  ? 15  MET B N   1 
ATOM   864  C CA  . MET B 1 16 ? 19.438  -21.730 -27.583 1.00 32.06  ? 15  MET B CA  1 
ATOM   865  C C   . MET B 1 16 ? 18.590  -22.814 -26.918 1.00 29.85  ? 15  MET B C   1 
ATOM   866  O O   . MET B 1 16 ? 17.359  -22.791 -27.016 1.00 26.04  ? 15  MET B O   1 
ATOM   867  C CB  . MET B 1 16 ? 19.509  -20.564 -26.593 1.00 34.27  ? 15  MET B CB  1 
ATOM   868  C CG  . MET B 1 16 ? 20.107  -19.284 -27.106 1.00 39.50  ? 15  MET B CG  1 
ATOM   869  S SD  . MET B 1 16 ? 21.858  -19.048 -26.759 1.00 41.86  ? 15  MET B SD  1 
ATOM   870  C CE  . MET B 1 16 ? 22.337  -19.853 -25.223 1.00 38.13  ? 15  MET B CE  1 
ATOM   871  N N   . LYS B 1 17 ? 19.262  -23.743 -26.208 1.00 27.47  ? 16  LYS B N   1 
ATOM   872  C CA  . LYS B 1 17 ? 18.534  -24.786 -25.487 1.00 31.02  ? 16  LYS B CA  1 
ATOM   873  C C   . LYS B 1 17 ? 17.579  -24.109 -24.487 1.00 28.07  ? 16  LYS B C   1 
ATOM   874  O O   . LYS B 1 17 ? 17.966  -23.178 -23.796 1.00 31.71  ? 16  LYS B O   1 
ATOM   875  C CB  . LYS B 1 17 ? 19.532  -25.731 -24.805 1.00 38.65  ? 16  LYS B CB  1 
ATOM   876  C CG  . LYS B 1 17 ? 18.915  -26.938 -24.081 1.00 42.88  ? 16  LYS B CG  1 
ATOM   877  C CD  . LYS B 1 17 ? 19.938  -27.909 -23.491 1.00 43.86  ? 16  LYS B CD  1 
ATOM   878  N N   . GLY B 1 18 ? 16.297  -24.486 -24.553 1.00 31.00  ? 17  GLY B N   1 
ATOM   879  C CA  . GLY B 1 18 ? 15.281  -24.008 -23.628 1.00 30.81  ? 17  GLY B CA  1 
ATOM   880  C C   . GLY B 1 18 ? 14.474  -22.814 -24.148 1.00 31.90  ? 17  GLY B C   1 
ATOM   881  O O   . GLY B 1 18 ? 13.567  -22.338 -23.471 1.00 30.28  ? 17  GLY B O   1 
ATOM   882  N N   . TYR B 1 19 ? 14.814  -22.315 -25.348 1.00 30.50  ? 18  TYR B N   1 
ATOM   883  C CA  . TYR B 1 19 ? 14.146  -21.122 -25.862 1.00 26.31  ? 18  TYR B CA  1 
ATOM   884  C C   . TYR B 1 19 ? 13.772  -21.376 -27.320 1.00 25.17  ? 18  TYR B C   1 
ATOM   885  O O   . TYR B 1 19 ? 14.466  -22.113 -28.016 1.00 26.56  ? 18  TYR B O   1 
ATOM   886  C CB  . TYR B 1 19 ? 15.106  -19.917 -25.843 1.00 23.69  ? 18  TYR B CB  1 
ATOM   887  C CG  . TYR B 1 19 ? 15.620  -19.595 -24.445 1.00 26.30  ? 18  TYR B CG  1 
ATOM   888  C CD1 . TYR B 1 19 ? 14.833  -18.867 -23.547 1.00 31.34  ? 18  TYR B CD1 1 
ATOM   889  C CD2 . TYR B 1 19 ? 16.811  -20.156 -23.985 1.00 28.78  ? 18  TYR B CD2 1 
ATOM   890  C CE1 . TYR B 1 19 ? 15.286  -18.644 -22.244 1.00 30.09  ? 18  TYR B CE1 1 
ATOM   891  C CE2 . TYR B 1 19 ? 17.291  -19.891 -22.704 1.00 31.82  ? 18  TYR B CE2 1 
ATOM   892  C CZ  . TYR B 1 19 ? 16.504  -19.158 -21.828 1.00 31.10  ? 18  TYR B CZ  1 
ATOM   893  O OH  . TYR B 1 19 ? 16.997  -18.928 -20.560 1.00 35.54  ? 18  TYR B OH  1 
ATOM   894  N N   . PRO B 1 20 ? 12.702  -20.738 -27.823 1.00 24.93  ? 19  PRO B N   1 
ATOM   895  C CA  . PRO B 1 20 ? 12.348  -20.804 -29.243 1.00 23.09  ? 19  PRO B CA  1 
ATOM   896  C C   . PRO B 1 20 ? 13.419  -20.091 -30.073 1.00 22.88  ? 19  PRO B C   1 
ATOM   897  O O   . PRO B 1 20 ? 14.092  -19.224 -29.565 1.00 23.78  ? 19  PRO B O   1 
ATOM   898  C CB  . PRO B 1 20 ? 11.030  -20.084 -29.362 1.00 24.01  ? 19  PRO B CB  1 
ATOM   899  C CG  . PRO B 1 20 ? 11.012  -19.160 -28.171 1.00 26.56  ? 19  PRO B CG  1 
ATOM   900  C CD  . PRO B 1 20 ? 11.777  -19.893 -27.053 1.00 22.94  ? 19  PRO B CD  1 
ATOM   901  N N   . HIS B 1 21 ? 13.532  -20.466 -31.346 1.00 22.35  ? 20  HIS B N   1 
ATOM   902  C CA  . HIS B 1 21 ? 14.364  -19.690 -32.290 1.00 22.64  ? 20  HIS B CA  1 
ATOM   903  C C   . HIS B 1 21 ? 14.084  -18.185 -32.148 1.00 22.26  ? 20  HIS B C   1 
ATOM   904  O O   . HIS B 1 21 ? 12.953  -17.754 -32.230 1.00 23.10  ? 20  HIS B O   1 
ATOM   905  C CB  . HIS B 1 21 ? 14.044  -20.165 -33.725 1.00 23.09  ? 20  HIS B CB  1 
ATOM   906  C CG  . HIS B 1 21 ? 14.277  -21.640 -33.953 1.00 22.95  ? 20  HIS B CG  1 
ATOM   907  N ND1 . HIS B 1 21 ? 13.383  -22.620 -33.522 1.00 24.49  ? 20  HIS B ND1 1 
ATOM   908  C CD2 . HIS B 1 21 ? 15.310  -22.306 -34.515 1.00 24.50  ? 20  HIS B CD2 1 
ATOM   909  C CE1 . HIS B 1 21 ? 13.882  -23.810 -33.834 1.00 25.02  ? 20  HIS B CE1 1 
ATOM   910  N NE2 . HIS B 1 21 ? 15.018  -23.666 -34.471 1.00 25.22  ? 20  HIS B NE2 1 
ATOM   911  N N   . TRP B 1 22 ? 15.143  -17.389 -31.959 1.00 22.39  ? 21  TRP B N   1 
ATOM   912  C CA  . TRP B 1 22 ? 14.966  -16.053 -31.359 1.00 20.44  ? 21  TRP B CA  1 
ATOM   913  C C   . TRP B 1 22 ? 15.467  -14.981 -32.325 1.00 20.78  ? 21  TRP B C   1 
ATOM   914  O O   . TRP B 1 22 ? 16.595  -15.131 -32.785 1.00 21.18  ? 21  TRP B O   1 
ATOM   915  C CB  . TRP B 1 22 ? 15.736  -15.951 -30.037 1.00 21.99  ? 21  TRP B CB  1 
ATOM   916  C CG  . TRP B 1 22 ? 15.226  -14.838 -29.141 1.00 21.35  ? 21  TRP B CG  1 
ATOM   917  C CD1 . TRP B 1 22 ? 15.459  -13.496 -29.275 1.00 21.90  ? 21  TRP B CD1 1 
ATOM   918  C CD2 . TRP B 1 22 ? 14.293  -14.957 -28.029 1.00 24.02  ? 21  TRP B CD2 1 
ATOM   919  N NE1 . TRP B 1 22 ? 14.710  -12.764 -28.364 1.00 23.11  ? 21  TRP B NE1 1 
ATOM   920  C CE2 . TRP B 1 22 ? 13.997  -13.640 -27.575 1.00 23.91  ? 21  TRP B CE2 1 
ATOM   921  C CE3 . TRP B 1 22 ? 13.669  -16.060 -27.406 1.00 23.79  ? 21  TRP B CE3 1 
ATOM   922  C CZ2 . TRP B 1 22 ? 13.139  -13.361 -26.509 1.00 23.10  ? 21  TRP B CZ2 1 
ATOM   923  C CZ3 . TRP B 1 22 ? 12.819  -15.779 -26.341 1.00 24.38  ? 21  TRP B CZ3 1 
ATOM   924  C CH2 . TRP B 1 22 ? 12.542  -14.461 -25.935 1.00 25.08  ? 21  TRP B CH2 1 
ATOM   925  N N   . PRO B 1 23 ? 14.721  -13.886 -32.615 1.00 22.76  ? 22  PRO B N   1 
ATOM   926  C CA  . PRO B 1 23 ? 15.235  -12.844 -33.535 1.00 19.94  ? 22  PRO B CA  1 
ATOM   927  C C   . PRO B 1 23 ? 16.536  -12.251 -32.995 1.00 22.45  ? 22  PRO B C   1 
ATOM   928  O O   . PRO B 1 23 ? 16.655  -11.891 -31.822 1.00 22.30  ? 22  PRO B O   1 
ATOM   929  C CB  . PRO B 1 23 ? 14.067  -11.783 -33.578 1.00 21.23  ? 22  PRO B CB  1 
ATOM   930  C CG  . PRO B 1 23 ? 13.320  -12.014 -32.252 1.00 22.15  ? 22  PRO B CG  1 
ATOM   931  C CD  . PRO B 1 23 ? 13.395  -13.543 -32.072 1.00 21.94  ? 22  PRO B CD  1 
ATOM   932  N N   . ALA B 1 24 ? 17.558  -12.162 -33.864 1.00 21.34  ? 23  ALA B N   1 
ATOM   933  C CA  . ALA B 1 24 ? 18.894  -11.832 -33.394 1.00 20.72  ? 23  ALA B CA  1 
ATOM   934  C C   . ALA B 1 24 ? 19.704  -11.281 -34.581 1.00 20.79  ? 23  ALA B C   1 
ATOM   935  O O   . ALA B 1 24 ? 19.225  -11.268 -35.710 1.00 22.42  ? 23  ALA B O   1 
ATOM   936  C CB  . ALA B 1 24 ? 19.582  -13.001 -32.698 1.00 23.04  ? 23  ALA B CB  1 
ATOM   937  N N   . ARG B 1 25 ? 20.840  -10.691 -34.220 1.00 22.99  ? 24  ARG B N   1 
ATOM   938  C CA  . ARG B 1 25 ? 21.796  -10.197 -35.215 1.00 22.52  ? 24  ARG B CA  1 
ATOM   939  C C   . ARG B 1 25 ? 23.188  -10.704 -34.855 1.00 23.32  ? 24  ARG B C   1 
ATOM   940  O O   . ARG B 1 25 ? 23.519  -10.974 -33.720 1.00 24.17  ? 24  ARG B O   1 
ATOM   941  C CB  . ARG B 1 25 ? 21.834  -8.670  -35.381 1.00 22.33  ? 24  ARG B CB  1 
ATOM   942  C CG  . ARG B 1 25 ? 22.408  -7.955  -34.173 1.00 22.03  ? 24  ARG B CG  1 
ATOM   943  C CD  . ARG B 1 25 ? 22.155  -6.426  -34.325 1.00 22.79  ? 24  ARG B CD  1 
ATOM   944  N NE  . ARG B 1 25 ? 22.774  -5.782  -33.167 1.00 25.06  ? 24  ARG B NE  1 
ATOM   945  C CZ  . ARG B 1 25 ? 22.521  -4.517  -32.792 1.00 25.16  ? 24  ARG B CZ  1 
ATOM   946  N NH1 . ARG B 1 25 ? 21.523  -3.849  -33.379 1.00 25.39  ? 24  ARG B NH1 1 
ATOM   947  N NH2 . ARG B 1 25 ? 23.231  -4.003  -31.792 1.00 26.60  ? 24  ARG B NH2 1 
ATOM   948  N N   . ILE B 1 26 ? 24.053  -10.788 -35.900 1.00 24.44  ? 25  ILE B N   1 
ATOM   949  C CA  . ILE B 1 26 ? 25.478  -10.975 -35.711 1.00 28.13  ? 25  ILE B CA  1 
ATOM   950  C C   . ILE B 1 26 ? 26.047  -9.602  -35.378 1.00 27.54  ? 25  ILE B C   1 
ATOM   951  O O   . ILE B 1 26 ? 25.753  -8.647  -36.091 1.00 28.82  ? 25  ILE B O   1 
ATOM   952  C CB  . ILE B 1 26 ? 26.128  -11.461 -37.027 1.00 31.63  ? 25  ILE B CB  1 
ATOM   953  C CG1 . ILE B 1 26 ? 25.354  -12.628 -37.649 1.00 31.21  ? 25  ILE B CG1 1 
ATOM   954  C CG2 . ILE B 1 26 ? 27.623  -11.756 -36.839 1.00 33.45  ? 25  ILE B CG2 1 
ATOM   955  C CD1 . ILE B 1 26 ? 25.361  -13.899 -36.826 1.00 30.39  ? 25  ILE B CD1 1 
ATOM   956  N N   . ASP B 1 27 ? 26.816  -9.559  -34.306 1.00 27.20  ? 26  ASP B N   1 
ATOM   957  C CA  . ASP B 1 27 ? 27.497  -8.333  -33.896 1.00 33.10  ? 26  ASP B CA  1 
ATOM   958  C C   . ASP B 1 27 ? 28.955  -8.347  -34.366 1.00 39.36  ? 26  ASP B C   1 
ATOM   959  O O   . ASP B 1 27 ? 29.500  -9.412  -34.657 1.00 40.59  ? 26  ASP B O   1 
ATOM   960  C CB  . ASP B 1 27 ? 27.429  -8.222  -32.386 1.00 30.35  ? 26  ASP B CB  1 
ATOM   961  C CG  . ASP B 1 27 ? 26.226  -7.489  -31.808 1.00 31.72  ? 26  ASP B CG  1 
ATOM   962  O OD1 . ASP B 1 27 ? 25.430  -6.923  -32.596 1.00 36.30  ? 26  ASP B OD1 1 
ATOM   963  O OD2 . ASP B 1 27 ? 26.135  -7.443  -30.553 1.00 34.08  ? 26  ASP B OD2 1 
ATOM   964  N N   A ASP B 1 28 ? 29.578  -7.158  -34.352 0.50 47.67  ? 27  ASP B N   1 
ATOM   965  N N   B ASP B 1 28 ? 29.593  -7.163  -34.390 0.50 45.00  ? 27  ASP B N   1 
ATOM   966  C CA  A ASP B 1 28 ? 31.007  -6.968  -34.566 0.50 55.01  ? 27  ASP B CA  1 
ATOM   967  C CA  B ASP B 1 28 ? 31.028  -7.034  -34.627 0.50 49.82  ? 27  ASP B CA  1 
ATOM   968  C C   A ASP B 1 28 ? 31.757  -7.450  -33.324 0.50 55.59  ? 27  ASP B C   1 
ATOM   969  C C   B ASP B 1 28 ? 31.749  -7.199  -33.285 0.50 52.01  ? 27  ASP B C   1 
ATOM   970  O O   A ASP B 1 28 ? 31.138  -7.950  -32.386 0.50 59.76  ? 27  ASP B O   1 
ATOM   971  O O   B ASP B 1 28 ? 31.101  -7.220  -32.240 0.50 53.14  ? 27  ASP B O   1 
ATOM   972  C CB  A ASP B 1 28 ? 31.295  -5.501  -34.846 0.50 53.97  ? 27  ASP B CB  1 
ATOM   973  C CB  B ASP B 1 28 ? 31.356  -5.716  -35.319 0.50 44.40  ? 27  ASP B CB  1 
ATOM   974  C CG  A ASP B 1 28 ? 30.114  -4.727  -35.414 0.50 53.21  ? 27  ASP B CG  1 
ATOM   975  C CG  B ASP B 1 28 ? 32.280  -5.794  -36.529 0.50 40.65  ? 27  ASP B CG  1 
ATOM   976  O OD1 A ASP B 1 28 ? 30.185  -4.325  -36.592 0.50 56.82  ? 27  ASP B OD1 1 
ATOM   977  O OD1 B ASP B 1 28 ? 33.251  -6.590  -36.501 0.50 44.13  ? 27  ASP B OD1 1 
ATOM   978  O OD2 A ASP B 1 28 ? 29.122  -4.549  -34.673 0.50 57.56  ? 27  ASP B OD2 1 
ATOM   979  O OD2 B ASP B 1 28 ? 32.055  -5.021  -37.482 0.50 37.95  ? 27  ASP B OD2 1 
ATOM   980  N N   . ILE B 1 29 ? 33.087  -7.291  -33.316 1.00 61.47  ? 28  ILE B N   1 
ATOM   981  C CA  . ILE B 1 29 ? 33.879  -7.675  -32.150 1.00 66.64  ? 28  ILE B CA  1 
ATOM   982  C C   . ILE B 1 29 ? 34.263  -6.439  -31.311 1.00 68.28  ? 28  ILE B C   1 
ATOM   983  O O   . ILE B 1 29 ? 34.839  -5.490  -31.891 1.00 68.44  ? 28  ILE B O   1 
ATOM   984  C CB  . ILE B 1 29 ? 35.101  -8.525  -32.547 1.00 66.35  ? 28  ILE B CB  1 
ATOM   985  N N   . VAL B 1 34 ? 36.851  -9.664  -25.553 1.00 65.22  ? 33  VAL B N   1 
ATOM   986  C CA  . VAL B 1 34 ? 36.690  -11.151 -25.550 1.00 72.44  ? 33  VAL B CA  1 
ATOM   987  C C   . VAL B 1 34 ? 36.210  -11.559 -26.936 1.00 74.20  ? 33  VAL B C   1 
ATOM   988  O O   . VAL B 1 34 ? 35.081  -11.253 -27.306 1.00 85.90  ? 33  VAL B O   1 
ATOM   989  C CB  . VAL B 1 34 ? 35.713  -11.615 -24.447 1.00 69.60  ? 33  VAL B CB  1 
ATOM   990  C CG1 . VAL B 1 34 ? 34.509  -10.687 -24.327 1.00 70.29  ? 33  VAL B CG1 1 
ATOM   991  C CG2 . VAL B 1 34 ? 35.280  -13.073 -24.607 1.00 59.08  ? 33  VAL B CG2 1 
ATOM   992  N N   . LYS B 1 35 ? 37.084  -12.222 -27.701 1.00 74.04  ? 34  LYS B N   1 
ATOM   993  C CA  . LYS B 1 35 ? 36.721  -12.725 -29.019 1.00 66.25  ? 34  LYS B CA  1 
ATOM   994  C C   . LYS B 1 35 ? 35.832  -13.962 -28.856 1.00 65.75  ? 34  LYS B C   1 
ATOM   995  O O   . LYS B 1 35 ? 35.898  -14.642 -27.826 1.00 66.57  ? 34  LYS B O   1 
ATOM   996  C CB  . LYS B 1 35 ? 37.984  -12.994 -29.845 1.00 67.75  ? 34  LYS B CB  1 
ATOM   997  N N   . PRO B 1 36 ? 34.955  -14.291 -29.842 1.00 58.71  ? 35  PRO B N   1 
ATOM   998  C CA  . PRO B 1 36 ? 34.182  -15.538 -29.784 1.00 51.15  ? 35  PRO B CA  1 
ATOM   999  C C   . PRO B 1 36 ? 35.131  -16.727 -29.720 1.00 43.76  ? 35  PRO B C   1 
ATOM   1000 O O   . PRO B 1 36 ? 36.248  -16.635 -30.209 1.00 46.98  ? 35  PRO B O   1 
ATOM   1001 C CB  . PRO B 1 36 ? 33.341  -15.546 -31.081 1.00 49.13  ? 35  PRO B CB  1 
ATOM   1002 C CG  . PRO B 1 36 ? 33.969  -14.473 -31.962 1.00 55.41  ? 35  PRO B CG  1 
ATOM   1003 C CD  . PRO B 1 36 ? 34.642  -13.476 -31.030 1.00 51.51  ? 35  PRO B CD  1 
ATOM   1004 N N   . PRO B 1 37 ? 34.742  -17.866 -29.106 1.00 47.51  ? 36  PRO B N   1 
ATOM   1005 C CA  . PRO B 1 37 ? 35.518  -19.090 -29.260 1.00 48.01  ? 36  PRO B CA  1 
ATOM   1006 C C   . PRO B 1 37 ? 35.551  -19.410 -30.751 1.00 54.61  ? 36  PRO B C   1 
ATOM   1007 O O   . PRO B 1 37 ? 34.715  -18.931 -31.530 1.00 47.32  ? 36  PRO B O   1 
ATOM   1008 C CB  . PRO B 1 37 ? 34.769  -20.160 -28.447 1.00 51.69  ? 36  PRO B CB  1 
ATOM   1009 C CG  . PRO B 1 37 ? 33.793  -19.372 -27.582 1.00 52.68  ? 36  PRO B CG  1 
ATOM   1010 C CD  . PRO B 1 37 ? 33.552  -18.035 -28.256 1.00 50.65  ? 36  PRO B CD  1 
ATOM   1011 N N   . PRO B 1 38 ? 36.508  -20.253 -31.199 1.00 52.31  ? 37  PRO B N   1 
ATOM   1012 C CA  . PRO B 1 38 ? 36.576  -20.639 -32.613 1.00 54.69  ? 37  PRO B CA  1 
ATOM   1013 C C   . PRO B 1 38 ? 35.261  -21.198 -33.171 1.00 45.72  ? 37  PRO B C   1 
ATOM   1014 O O   . PRO B 1 38 ? 34.517  -21.893 -32.473 1.00 46.64  ? 37  PRO B O   1 
ATOM   1015 C CB  . PRO B 1 38 ? 37.752  -21.646 -32.719 1.00 54.93  ? 37  PRO B CB  1 
ATOM   1016 C CG  . PRO B 1 38 ? 38.266  -21.838 -31.292 1.00 48.32  ? 37  PRO B CG  1 
ATOM   1017 C CD  . PRO B 1 38 ? 37.547  -20.876 -30.358 1.00 57.02  ? 37  PRO B CD  1 
ATOM   1018 N N   . ASN B 1 39 ? 34.969  -20.840 -34.426 1.00 45.07  ? 38  ASN B N   1 
ATOM   1019 C CA  . ASN B 1 39 ? 33.800  -21.320 -35.158 1.00 49.07  ? 38  ASN B CA  1 
ATOM   1020 C C   . ASN B 1 39 ? 32.512  -20.593 -34.764 1.00 40.17  ? 38  ASN B C   1 
ATOM   1021 O O   . ASN B 1 39 ? 31.493  -20.810 -35.401 1.00 41.05  ? 38  ASN B O   1 
ATOM   1022 C CB  . ASN B 1 39 ? 33.563  -22.824 -35.016 1.00 49.51  ? 38  ASN B CB  1 
ATOM   1023 C CG  . ASN B 1 39 ? 34.769  -23.669 -35.363 1.00 60.85  ? 38  ASN B CG  1 
ATOM   1024 O OD1 . ASN B 1 39 ? 35.033  -24.664 -34.678 1.00 65.56  ? 38  ASN B OD1 1 
ATOM   1025 N ND2 . ASN B 1 39 ? 35.502  -23.309 -36.412 1.00 54.05  ? 38  ASN B ND2 1 
ATOM   1026 N N   . LYS B 1 40 ? 32.550  -19.717 -33.739 1.00 39.98  ? 39  LYS B N   1 
ATOM   1027 C CA  . LYS B 1 40 ? 31.349  -19.087 -33.193 1.00 37.65  ? 39  LYS B CA  1 
ATOM   1028 C C   . LYS B 1 40 ? 31.309  -17.595 -33.523 1.00 36.79  ? 39  LYS B C   1 
ATOM   1029 O O   . LYS B 1 40 ? 32.331  -17.023 -33.872 1.00 37.65  ? 39  LYS B O   1 
ATOM   1030 C CB  . LYS B 1 40 ? 31.394  -19.388 -31.696 1.00 40.57  ? 39  LYS B CB  1 
ATOM   1031 C CG  . LYS B 1 40 ? 31.064  -20.833 -31.359 1.00 45.18  ? 39  LYS B CG  1 
ATOM   1032 C CD  . LYS B 1 40 ? 30.794  -20.889 -29.859 1.00 56.85  ? 39  LYS B CD  1 
ATOM   1033 C CE  . LYS B 1 40 ? 29.662  -21.762 -29.402 1.00 62.60  ? 39  LYS B CE  1 
ATOM   1034 N NZ  . LYS B 1 40 ? 30.029  -23.178 -29.379 1.00 60.45  ? 39  LYS B NZ  1 
ATOM   1035 N N   . TYR B 1 41 ? 30.131  -16.972 -33.383 1.00 32.58  ? 40  TYR B N   1 
ATOM   1036 C CA  . TYR B 1 41 ? 29.908  -15.568 -33.701 1.00 30.23  ? 40  TYR B CA  1 
ATOM   1037 C C   . TYR B 1 41 ? 29.333  -14.892 -32.467 1.00 31.82  ? 40  TYR B C   1 
ATOM   1038 O O   . TYR B 1 41 ? 28.605  -15.529 -31.702 1.00 30.99  ? 40  TYR B O   1 
ATOM   1039 C CB  . TYR B 1 41 ? 28.860  -15.425 -34.810 1.00 30.77  ? 40  TYR B CB  1 
ATOM   1040 C CG  . TYR B 1 41 ? 29.321  -15.889 -36.188 1.00 33.54  ? 40  TYR B CG  1 
ATOM   1041 C CD1 . TYR B 1 41 ? 30.018  -15.038 -37.040 1.00 31.61  ? 40  TYR B CD1 1 
ATOM   1042 C CD2 . TYR B 1 41 ? 29.078  -17.184 -36.619 1.00 29.09  ? 40  TYR B CD2 1 
ATOM   1043 C CE1 . TYR B 1 41 ? 30.456  -15.461 -38.287 1.00 37.67  ? 40  TYR B CE1 1 
ATOM   1044 C CE2 . TYR B 1 41 ? 29.511  -17.623 -37.858 1.00 34.88  ? 40  TYR B CE2 1 
ATOM   1045 C CZ  . TYR B 1 41 ? 30.225  -16.764 -38.686 1.00 35.98  ? 40  TYR B CZ  1 
ATOM   1046 O OH  . TYR B 1 41 ? 30.619  -17.188 -39.936 1.00 32.09  ? 40  TYR B OH  1 
ATOM   1047 N N   . PRO B 1 42 ? 29.569  -13.571 -32.263 1.00 35.13  ? 41  PRO B N   1 
ATOM   1048 C CA  . PRO B 1 42 ? 28.845  -12.843 -31.221 1.00 31.26  ? 41  PRO B CA  1 
ATOM   1049 C C   . PRO B 1 42 ? 27.423  -12.559 -31.692 1.00 26.77  ? 41  PRO B C   1 
ATOM   1050 O O   . PRO B 1 42 ? 27.244  -11.914 -32.746 1.00 29.38  ? 41  PRO B O   1 
ATOM   1051 C CB  . PRO B 1 42 ? 29.640  -11.518 -31.056 1.00 33.25  ? 41  PRO B CB  1 
ATOM   1052 C CG  . PRO B 1 42 ? 30.506  -11.386 -32.302 1.00 33.93  ? 41  PRO B CG  1 
ATOM   1053 C CD  . PRO B 1 42 ? 30.485  -12.722 -33.048 1.00 35.07  ? 41  PRO B CD  1 
ATOM   1054 N N   . ILE B 1 43 ? 26.422  -13.035 -30.910 1.00 27.98  ? 42  ILE B N   1 
ATOM   1055 C CA  . ILE B 1 43 ? 25.007  -12.833 -31.200 1.00 25.90  ? 42  ILE B CA  1 
ATOM   1056 C C   . ILE B 1 43 ? 24.395  -11.837 -30.218 1.00 25.86  ? 42  ILE B C   1 
ATOM   1057 O O   . ILE B 1 43 ? 24.677  -11.920 -29.033 1.00 29.10  ? 42  ILE B O   1 
ATOM   1058 C CB  . ILE B 1 43 ? 24.270  -14.180 -31.089 1.00 24.87  ? 42  ILE B CB  1 
ATOM   1059 C CG1 . ILE B 1 43 ? 25.043  -15.267 -31.915 1.00 28.45  ? 42  ILE B CG1 1 
ATOM   1060 C CG2 . ILE B 1 43 ? 22.799  -14.027 -31.510 1.00 27.30  ? 42  ILE B CG2 1 
ATOM   1061 C CD1 . ILE B 1 43 ? 25.200  -14.928 -33.380 1.00 26.85  ? 42  ILE B CD1 1 
ATOM   1062 N N   . PHE B 1 44 ? 23.600  -10.929 -30.759 1.00 23.59  ? 43  PHE B N   1 
ATOM   1063 C CA  . PHE B 1 44 ? 22.764  -10.029 -29.973 1.00 26.24  ? 43  PHE B CA  1 
ATOM   1064 C C   . PHE B 1 44 ? 21.323  -10.462 -30.189 1.00 23.90  ? 43  PHE B C   1 
ATOM   1065 O O   . PHE B 1 44 ? 20.818  -10.510 -31.315 1.00 23.53  ? 43  PHE B O   1 
ATOM   1066 C CB  . PHE B 1 44 ? 23.047  -8.554  -30.330 1.00 24.81  ? 43  PHE B CB  1 
ATOM   1067 C CG  . PHE B 1 44 ? 22.070  -7.553  -29.712 1.00 25.05  ? 43  PHE B CG  1 
ATOM   1068 C CD1 . PHE B 1 44 ? 20.911  -7.198  -30.400 1.00 23.04  ? 43  PHE B CD1 1 
ATOM   1069 C CD2 . PHE B 1 44 ? 22.304  -6.997  -28.461 1.00 30.72  ? 43  PHE B CD2 1 
ATOM   1070 C CE1 . PHE B 1 44 ? 20.015  -6.274  -29.870 1.00 27.98  ? 43  PHE B CE1 1 
ATOM   1071 C CE2 . PHE B 1 44 ? 21.408  -6.055  -27.918 1.00 26.95  ? 43  PHE B CE2 1 
ATOM   1072 C CZ  . PHE B 1 44 ? 20.277  -5.710  -28.636 1.00 29.52  ? 43  PHE B CZ  1 
ATOM   1073 N N   . PHE B 1 45 ? 20.599  -10.703 -29.063 1.00 23.70  ? 44  PHE B N   1 
ATOM   1074 C CA  . PHE B 1 45 ? 19.208  -11.098 -29.116 1.00 23.83  ? 44  PHE B CA  1 
ATOM   1075 C C   . PHE B 1 45 ? 18.293  -9.898  -28.949 1.00 22.62  ? 44  PHE B C   1 
ATOM   1076 O O   . PHE B 1 45 ? 18.385  -9.143  -27.950 1.00 24.88  ? 44  PHE B O   1 
ATOM   1077 C CB  . PHE B 1 45 ? 18.912  -12.133 -28.015 1.00 22.28  ? 44  PHE B CB  1 
ATOM   1078 C CG  . PHE B 1 45 ? 19.618  -13.463 -28.178 1.00 22.76  ? 44  PHE B CG  1 
ATOM   1079 C CD1 . PHE B 1 45 ? 20.959  -13.607 -27.832 1.00 24.10  ? 44  PHE B CD1 1 
ATOM   1080 C CD2 . PHE B 1 45 ? 18.979  -14.544 -28.751 1.00 23.53  ? 44  PHE B CD2 1 
ATOM   1081 C CE1 . PHE B 1 45 ? 21.641  -14.809 -28.046 1.00 27.14  ? 44  PHE B CE1 1 
ATOM   1082 C CE2 . PHE B 1 45 ? 19.645  -15.763 -28.860 1.00 26.11  ? 44  PHE B CE2 1 
ATOM   1083 C CZ  . PHE B 1 45 ? 20.971  -15.891 -28.580 1.00 24.61  ? 44  PHE B CZ  1 
ATOM   1084 N N   . PHE B 1 46 ? 17.460  -9.702  -29.960 1.00 21.44  ? 45  PHE B N   1 
ATOM   1085 C CA  . PHE B 1 46 ? 16.509  -8.605  -29.936 1.00 21.67  ? 45  PHE B CA  1 
ATOM   1086 C C   . PHE B 1 46 ? 15.497  -8.785  -28.791 1.00 25.31  ? 45  PHE B C   1 
ATOM   1087 O O   . PHE B 1 46 ? 15.164  -9.900  -28.398 1.00 23.82  ? 45  PHE B O   1 
ATOM   1088 C CB  . PHE B 1 46 ? 15.773  -8.349  -31.249 1.00 23.74  ? 45  PHE B CB  1 
ATOM   1089 C CG  . PHE B 1 46 ? 16.734  -7.887  -32.344 1.00 22.94  ? 45  PHE B CG  1 
ATOM   1090 C CD1 . PHE B 1 46 ? 17.166  -6.559  -32.362 1.00 24.98  ? 45  PHE B CD1 1 
ATOM   1091 C CD2 . PHE B 1 46 ? 17.116  -8.755  -33.384 1.00 23.24  ? 45  PHE B CD2 1 
ATOM   1092 C CE1 . PHE B 1 46 ? 18.079  -6.155  -33.355 1.00 24.02  ? 45  PHE B CE1 1 
ATOM   1093 C CE2 . PHE B 1 46 ? 17.978  -8.338  -34.419 1.00 23.97  ? 45  PHE B CE2 1 
ATOM   1094 C CZ  . PHE B 1 46 ? 18.423  -7.011  -34.397 1.00 22.66  ? 45  PHE B CZ  1 
ATOM   1095 N N   . GLY B 1 47 ? 14.986  -7.655  -28.287 1.00 24.61  ? 46  GLY B N   1 
ATOM   1096 C CA  . GLY B 1 47 ? 13.938  -7.673  -27.253 1.00 24.64  ? 46  GLY B CA  1 
ATOM   1097 C C   . GLY B 1 47 ? 14.535  -7.798  -25.848 1.00 26.34  ? 46  GLY B C   1 
ATOM   1098 O O   . GLY B 1 47 ? 14.387  -6.904  -24.998 1.00 28.92  ? 46  GLY B O   1 
ATOM   1099 N N   . THR B 1 48 ? 15.258  -8.883  -25.599 1.00 24.85  ? 47  THR B N   1 
ATOM   1100 C CA  . THR B 1 48 ? 15.930  -9.137  -24.336 1.00 26.46  ? 47  THR B CA  1 
ATOM   1101 C C   . THR B 1 48 ? 17.220  -8.324  -24.255 1.00 28.65  ? 47  THR B C   1 
ATOM   1102 O O   . THR B 1 48 ? 17.690  -8.021  -23.149 1.00 28.89  ? 47  THR B O   1 
ATOM   1103 C CB  . THR B 1 48 ? 16.236  -10.624 -24.116 1.00 27.98  ? 47  THR B CB  1 
ATOM   1104 O OG1 . THR B 1 48 ? 17.229  -11.037 -25.064 1.00 25.64  ? 47  THR B OG1 1 
ATOM   1105 C CG2 . THR B 1 48 ? 14.991  -11.503 -24.122 1.00 22.98  ? 47  THR B CG2 1 
ATOM   1106 N N   . HIS B 1 49 ? 17.824  -8.062  -25.419 1.00 27.49  ? 48  HIS B N   1 
ATOM   1107 C CA  . HIS B 1 49 ? 19.130  -7.419  -25.548 1.00 29.33  ? 48  HIS B CA  1 
ATOM   1108 C C   . HIS B 1 49 ? 20.224  -8.227  -24.873 1.00 28.64  ? 48  HIS B C   1 
ATOM   1109 O O   . HIS B 1 49 ? 21.242  -7.657  -24.490 1.00 33.94  ? 48  HIS B O   1 
ATOM   1110 C CB  . HIS B 1 49 ? 19.094  -5.932  -25.149 1.00 28.14  ? 48  HIS B CB  1 
ATOM   1111 C CG  . HIS B 1 49 ? 17.907  -5.236  -25.685 1.00 28.10  ? 48  HIS B CG  1 
ATOM   1112 N ND1 . HIS B 1 49 ? 17.170  -4.380  -24.893 1.00 31.27  ? 48  HIS B ND1 1 
ATOM   1113 C CD2 . HIS B 1 49 ? 17.264  -5.268  -26.867 1.00 25.47  ? 48  HIS B CD2 1 
ATOM   1114 C CE1 . HIS B 1 49 ? 16.119  -3.942  -25.583 1.00 36.00  ? 48  HIS B CE1 1 
ATOM   1115 N NE2 . HIS B 1 49 ? 16.182  -4.433  -26.814 1.00 31.22  ? 48  HIS B NE2 1 
ATOM   1116 N N   . GLU B 1 50 ? 20.046  -9.543  -24.753 1.00 29.28  ? 49  GLU B N   1 
ATOM   1117 C CA  . GLU B 1 50 ? 21.077  -10.411 -24.216 1.00 28.57  ? 49  GLU B CA  1 
ATOM   1118 C C   . GLU B 1 50 ? 22.053  -10.760 -25.348 1.00 29.60  ? 49  GLU B C   1 
ATOM   1119 O O   . GLU B 1 50 ? 21.758  -10.508 -26.527 1.00 29.03  ? 49  GLU B O   1 
ATOM   1120 C CB  . GLU B 1 50 ? 20.480  -11.747 -23.752 1.00 34.22  ? 49  GLU B CB  1 
ATOM   1121 C CG  . GLU B 1 50 ? 19.414  -11.613 -22.654 1.00 36.28  ? 49  GLU B CG  1 
ATOM   1122 C CD  . GLU B 1 50 ? 19.951  -11.660 -21.233 1.00 50.15  ? 49  GLU B CD  1 
ATOM   1123 O OE1 . GLU B 1 50 ? 19.158  -11.477 -20.278 1.00 44.18  ? 49  GLU B OE1 1 
ATOM   1124 O OE2 . GLU B 1 50 ? 21.163  -11.897 -21.059 1.00 57.71  ? 49  GLU B OE2 1 
ATOM   1125 N N   . THR B 1 51 ? 23.206  -11.302 -24.952 1.00 28.14  ? 50  THR B N   1 
ATOM   1126 C CA  . THR B 1 51 ? 24.260  -11.749 -25.866 1.00 28.36  ? 50  THR B CA  1 
ATOM   1127 C C   . THR B 1 51 ? 24.707  -13.175 -25.545 1.00 32.48  ? 50  THR B C   1 
ATOM   1128 O O   . THR B 1 51 ? 24.580  -13.652 -24.418 1.00 32.17  ? 50  THR B O   1 
ATOM   1129 C CB  . THR B 1 51 ? 25.416  -10.745 -25.917 1.00 33.49  ? 50  THR B CB  1 
ATOM   1130 O OG1 . THR B 1 51 ? 25.981  -10.797 -24.613 1.00 37.47  ? 50  THR B OG1 1 
ATOM   1131 C CG2 . THR B 1 51 ? 24.975  -9.320  -26.203 1.00 31.30  ? 50  THR B CG2 1 
ATOM   1132 N N   . ALA B 1 52 ? 25.253  -13.864 -26.563 1.00 32.66  ? 51  ALA B N   1 
ATOM   1133 C CA  . ALA B 1 52 ? 25.903  -15.154 -26.408 1.00 33.37  ? 51  ALA B CA  1 
ATOM   1134 C C   . ALA B 1 52 ? 26.778  -15.389 -27.638 1.00 29.86  ? 51  ALA B C   1 
ATOM   1135 O O   . ALA B 1 52 ? 26.669  -14.648 -28.628 1.00 31.37  ? 51  ALA B O   1 
ATOM   1136 C CB  . ALA B 1 52 ? 24.874  -16.248 -26.233 1.00 31.00  ? 51  ALA B CB  1 
ATOM   1137 N N   . PHE B 1 53 ? 27.630  -16.412 -27.533 1.00 30.75  ? 52  PHE B N   1 
ATOM   1138 C CA  . PHE B 1 53 ? 28.386  -16.905 -28.673 1.00 31.19  ? 52  PHE B CA  1 
ATOM   1139 C C   . PHE B 1 53 ? 27.715  -18.184 -29.183 1.00 31.15  ? 52  PHE B C   1 
ATOM   1140 O O   . PHE B 1 53 ? 27.449  -19.121 -28.414 1.00 33.58  ? 52  PHE B O   1 
ATOM   1141 C CB  . PHE B 1 53 ? 29.867  -17.128 -28.328 1.00 31.83  ? 52  PHE B CB  1 
ATOM   1142 C CG  . PHE B 1 53 ? 30.615  -15.893 -27.840 1.00 36.18  ? 52  PHE B CG  1 
ATOM   1143 C CD1 . PHE B 1 53 ? 30.915  -14.849 -28.706 1.00 37.80  ? 52  PHE B CD1 1 
ATOM   1144 C CD2 . PHE B 1 53 ? 31.033  -15.793 -26.515 1.00 40.80  ? 52  PHE B CD2 1 
ATOM   1145 C CE1 . PHE B 1 53 ? 31.599  -13.727 -28.255 1.00 38.14  ? 52  PHE B CE1 1 
ATOM   1146 C CE2 . PHE B 1 53 ? 31.709  -14.665 -26.058 1.00 39.48  ? 52  PHE B CE2 1 
ATOM   1147 C CZ  . PHE B 1 53 ? 31.989  -13.644 -26.928 1.00 37.01  ? 52  PHE B CZ  1 
ATOM   1148 N N   . LEU B 1 54 ? 27.461  -18.207 -30.501 1.00 28.26  ? 53  LEU B N   1 
ATOM   1149 C CA  . LEU B 1 54 ? 26.820  -19.354 -31.138 1.00 27.71  ? 53  LEU B CA  1 
ATOM   1150 C C   . LEU B 1 54 ? 27.555  -19.719 -32.438 1.00 28.58  ? 53  LEU B C   1 
ATOM   1151 O O   . LEU B 1 54 ? 28.047  -18.841 -33.160 1.00 29.81  ? 53  LEU B O   1 
ATOM   1152 C CB  . LEU B 1 54 ? 25.333  -19.172 -31.437 1.00 28.32  ? 53  LEU B CB  1 
ATOM   1153 C CG  . LEU B 1 54 ? 24.366  -19.135 -30.245 1.00 26.63  ? 53  LEU B CG  1 
ATOM   1154 C CD1 . LEU B 1 54 ? 23.001  -18.691 -30.730 1.00 27.72  ? 53  LEU B CD1 1 
ATOM   1155 C CD2 . LEU B 1 54 ? 24.255  -20.534 -29.616 1.00 28.07  ? 53  LEU B CD2 1 
ATOM   1156 N N   . GLY B 1 55 ? 27.454  -21.004 -32.793 1.00 30.09  ? 54  GLY B N   1 
ATOM   1157 C CA  . GLY B 1 55 ? 28.000  -21.532 -34.037 1.00 29.49  ? 54  GLY B CA  1 
ATOM   1158 C C   . GLY B 1 55 ? 26.911  -21.588 -35.108 1.00 28.91  ? 54  GLY B C   1 
ATOM   1159 O O   . GLY B 1 55 ? 25.715  -21.526 -34.789 1.00 27.36  ? 54  GLY B O   1 
ATOM   1160 N N   . PRO B 1 56 ? 27.267  -21.716 -36.407 1.00 25.94  ? 55  PRO B N   1 
ATOM   1161 C CA  . PRO B 1 56 ? 26.282  -21.772 -37.488 1.00 26.52  ? 55  PRO B CA  1 
ATOM   1162 C C   . PRO B 1 56 ? 25.113  -22.743 -37.383 1.00 23.54  ? 55  PRO B C   1 
ATOM   1163 O O   . PRO B 1 56 ? 24.039  -22.491 -37.929 1.00 25.42  ? 55  PRO B O   1 
ATOM   1164 C CB  . PRO B 1 56 ? 27.137  -22.131 -38.725 1.00 28.26  ? 55  PRO B CB  1 
ATOM   1165 C CG  . PRO B 1 56 ? 28.530  -21.715 -38.386 1.00 31.21  ? 55  PRO B CG  1 
ATOM   1166 C CD  . PRO B 1 56 ? 28.664  -21.800 -36.884 1.00 29.40  ? 55  PRO B CD  1 
ATOM   1167 N N   . LYS B 1 57 ? 25.324  -23.868 -36.668 1.00 27.39  ? 56  LYS B N   1 
ATOM   1168 C CA  . LYS B 1 57 ? 24.279  -24.882 -36.578 1.00 27.37  ? 56  LYS B CA  1 
ATOM   1169 C C   . LYS B 1 57 ? 23.017  -24.288 -35.932 1.00 27.19  ? 56  LYS B C   1 
ATOM   1170 O O   . LYS B 1 57 ? 21.895  -24.751 -36.152 1.00 25.87  ? 56  LYS B O   1 
ATOM   1171 C CB  . LYS B 1 57 ? 24.768  -26.147 -35.843 1.00 28.82  ? 56  LYS B CB  1 
ATOM   1172 C CG  . LYS B 1 57 ? 24.834  -25.976 -34.347 1.00 32.23  ? 56  LYS B CG  1 
ATOM   1173 C CD  . LYS B 1 57 ? 25.148  -27.324 -33.700 1.00 37.22  ? 56  LYS B CD  1 
ATOM   1174 C CE  . LYS B 1 57 ? 25.302  -27.332 -32.200 1.00 43.80  ? 56  LYS B CE  1 
ATOM   1175 N NZ  . LYS B 1 57 ? 24.096  -26.911 -31.483 1.00 45.92  ? 56  LYS B NZ  1 
ATOM   1176 N N   . ASP B 1 58 ? 23.213  -23.203 -35.161 1.00 26.71  ? 57  ASP B N   1 
ATOM   1177 C CA  . ASP B 1 58 ? 22.160  -22.589 -34.367 1.00 28.10  ? 57  ASP B CA  1 
ATOM   1178 C C   . ASP B 1 58 ? 21.727  -21.232 -34.942 1.00 25.48  ? 57  ASP B C   1 
ATOM   1179 O O   . ASP B 1 58 ? 20.936  -20.514 -34.302 1.00 24.29  ? 57  ASP B O   1 
ATOM   1180 C CB  . ASP B 1 58 ? 22.585  -22.486 -32.903 1.00 25.37  ? 57  ASP B CB  1 
ATOM   1181 C CG  . ASP B 1 58 ? 22.712  -23.829 -32.185 1.00 29.11  ? 57  ASP B CG  1 
ATOM   1182 O OD1 . ASP B 1 58 ? 21.795  -24.666 -32.342 1.00 31.51  ? 57  ASP B OD1 1 
ATOM   1183 O OD2 . ASP B 1 58 ? 23.678  -23.995 -31.422 1.00 35.63  ? 57  ASP B OD2 1 
ATOM   1184 N N   . LEU B 1 59 ? 22.168  -20.911 -36.173 1.00 23.68  ? 58  LEU B N   1 
ATOM   1185 C CA  . LEU B 1 59 ? 21.885  -19.607 -36.768 1.00 22.73  ? 58  LEU B CA  1 
ATOM   1186 C C   . LEU B 1 59 ? 21.183  -19.793 -38.098 1.00 23.13  ? 58  LEU B C   1 
ATOM   1187 O O   . LEU B 1 59 ? 21.678  -20.448 -39.018 1.00 24.72  ? 58  LEU B O   1 
ATOM   1188 C CB  . LEU B 1 59 ? 23.185  -18.828 -36.966 1.00 25.52  ? 58  LEU B CB  1 
ATOM   1189 C CG  . LEU B 1 59 ? 24.042  -18.614 -35.719 1.00 24.54  ? 58  LEU B CG  1 
ATOM   1190 C CD1 . LEU B 1 59 ? 25.400  -17.968 -36.035 1.00 28.35  ? 58  LEU B CD1 1 
ATOM   1191 C CD2 . LEU B 1 59 ? 23.286  -17.695 -34.759 1.00 26.38  ? 58  LEU B CD2 1 
ATOM   1192 N N   . PHE B 1 60 ? 20.012  -19.219 -38.178 1.00 20.02  ? 59  PHE B N   1 
ATOM   1193 C CA  . PHE B 1 60 ? 19.068  -19.381 -39.263 1.00 22.39  ? 59  PHE B CA  1 
ATOM   1194 C C   . PHE B 1 60 ? 18.892  -18.029 -39.952 1.00 25.88  ? 59  PHE B C   1 
ATOM   1195 O O   . PHE B 1 60 ? 18.320  -17.097 -39.390 1.00 24.35  ? 59  PHE B O   1 
ATOM   1196 C CB  . PHE B 1 60 ? 17.745  -19.912 -38.685 1.00 23.16  ? 59  PHE B CB  1 
ATOM   1197 C CG  . PHE B 1 60 ? 17.832  -21.328 -38.113 1.00 22.01  ? 59  PHE B CG  1 
ATOM   1198 C CD1 . PHE B 1 60 ? 18.383  -21.529 -36.847 1.00 25.51  ? 59  PHE B CD1 1 
ATOM   1199 C CD2 . PHE B 1 60 ? 17.347  -22.415 -38.853 1.00 26.14  ? 59  PHE B CD2 1 
ATOM   1200 C CE1 . PHE B 1 60 ? 18.528  -22.818 -36.326 1.00 25.86  ? 59  PHE B CE1 1 
ATOM   1201 C CE2 . PHE B 1 60 ? 17.432  -23.703 -38.300 1.00 25.44  ? 59  PHE B CE2 1 
ATOM   1202 C CZ  . PHE B 1 60 ? 18.073  -23.892 -37.076 1.00 25.72  ? 59  PHE B CZ  1 
ATOM   1203 N N   . PRO B 1 61 ? 19.412  -17.832 -41.187 1.00 24.78  ? 60  PRO B N   1 
ATOM   1204 C CA  . PRO B 1 61 ? 19.188  -16.541 -41.885 1.00 26.30  ? 60  PRO B CA  1 
ATOM   1205 C C   . PRO B 1 61 ? 17.725  -16.081 -41.816 1.00 23.27  ? 60  PRO B C   1 
ATOM   1206 O O   . PRO B 1 61 ? 16.765  -16.820 -42.059 1.00 26.03  ? 60  PRO B O   1 
ATOM   1207 C CB  . PRO B 1 61 ? 19.707  -16.887 -43.310 1.00 26.84  ? 60  PRO B CB  1 
ATOM   1208 C CG  . PRO B 1 61 ? 20.828  -17.879 -43.064 1.00 34.36  ? 60  PRO B CG  1 
ATOM   1209 C CD  . PRO B 1 61 ? 20.317  -18.764 -41.896 1.00 27.82  ? 60  PRO B CD  1 
ATOM   1210 N N   . TYR B 1 62 ? 17.521  -14.772 -41.485 1.00 24.80  ? 61  TYR B N   1 
ATOM   1211 C CA  . TYR B 1 62 ? 16.211  -14.279 -41.119 1.00 26.08  ? 61  TYR B CA  1 
ATOM   1212 C C   . TYR B 1 62 ? 15.220  -14.299 -42.268 1.00 27.82  ? 61  TYR B C   1 
ATOM   1213 O O   . TYR B 1 62 ? 14.075  -14.735 -42.095 1.00 29.54  ? 61  TYR B O   1 
ATOM   1214 C CB  . TYR B 1 62 ? 16.391  -12.837 -40.612 1.00 29.82  ? 61  TYR B CB  1 
ATOM   1215 C CG  . TYR B 1 62 ? 15.074  -12.128 -40.348 1.00 29.85  ? 61  TYR B CG  1 
ATOM   1216 C CD1 . TYR B 1 62 ? 14.330  -12.393 -39.207 1.00 29.52  ? 61  TYR B CD1 1 
ATOM   1217 C CD2 . TYR B 1 62 ? 14.614  -11.137 -41.219 1.00 35.85  ? 61  TYR B CD2 1 
ATOM   1218 C CE1 . TYR B 1 62 ? 13.140  -11.724 -38.963 1.00 30.43  ? 61  TYR B CE1 1 
ATOM   1219 C CE2 . TYR B 1 62 ? 13.426  -10.460 -40.986 1.00 37.60  ? 61  TYR B CE2 1 
ATOM   1220 C CZ  . TYR B 1 62 ? 12.696  -10.756 -39.847 1.00 34.56  ? 61  TYR B CZ  1 
ATOM   1221 O OH  . TYR B 1 62 ? 11.551  -10.071 -39.638 1.00 38.75  ? 61  TYR B OH  1 
ATOM   1222 N N   . ASP B 1 63 ? 15.683  -13.852 -43.460 1.00 33.04  ? 62  ASP B N   1 
ATOM   1223 C CA  . ASP B 1 63 ? 14.823  -13.842 -44.640 1.00 37.03  ? 62  ASP B CA  1 
ATOM   1224 C C   . ASP B 1 63 ? 14.302  -15.235 -44.967 1.00 31.93  ? 62  ASP B C   1 
ATOM   1225 O O   . ASP B 1 63 ? 13.104  -15.414 -45.127 1.00 39.21  ? 62  ASP B O   1 
ATOM   1226 C CB  . ASP B 1 63 ? 15.498  -13.214 -45.844 1.00 39.88  ? 62  ASP B CB  1 
ATOM   1227 C CG  . ASP B 1 63 ? 15.109  -11.770 -46.095 1.00 57.60  ? 62  ASP B CG  1 
ATOM   1228 O OD1 . ASP B 1 63 ? 14.559  -11.130 -45.158 1.00 60.75  ? 62  ASP B OD1 1 
ATOM   1229 O OD2 . ASP B 1 63 ? 15.319  -11.316 -47.239 1.00 64.97  ? 62  ASP B OD2 1 
ATOM   1230 N N   . LYS B 1 64 ? 15.206  -16.214 -45.022 1.00 34.54  ? 63  LYS B N   1 
ATOM   1231 C CA  . LYS B 1 64 ? 14.805  -17.579 -45.323 1.00 34.71  ? 63  LYS B CA  1 
ATOM   1232 C C   . LYS B 1 64 ? 13.819  -18.109 -44.274 1.00 31.75  ? 63  LYS B C   1 
ATOM   1233 O O   . LYS B 1 64 ? 12.914  -18.863 -44.606 1.00 36.74  ? 63  LYS B O   1 
ATOM   1234 C CB  . LYS B 1 64 ? 16.030  -18.494 -45.374 1.00 38.15  ? 63  LYS B CB  1 
ATOM   1235 C CG  . LYS B 1 64 ? 15.683  -19.905 -45.832 1.00 35.12  ? 63  LYS B CG  1 
ATOM   1236 C CD  . LYS B 1 64 ? 16.925  -20.760 -45.959 1.00 43.11  ? 63  LYS B CD  1 
ATOM   1237 C CE  . LYS B 1 64 ? 16.682  -22.131 -46.551 1.00 48.53  ? 63  LYS B CE  1 
ATOM   1238 N NZ  . LYS B 1 64 ? 15.509  -22.802 -45.995 1.00 47.50  ? 63  LYS B NZ  1 
ATOM   1239 N N   . SER B 1 65 ? 13.969  -17.696 -43.009 1.00 31.96  ? 64  SER B N   1 
ATOM   1240 C CA  . SER B 1 65 ? 13.273  -18.463 -41.968 1.00 33.70  ? 64  SER B CA  1 
ATOM   1241 C C   . SER B 1 65 ? 12.146  -17.682 -41.267 1.00 30.55  ? 64  SER B C   1 
ATOM   1242 O O   . SER B 1 65 ? 11.507  -18.212 -40.373 1.00 31.24  ? 64  SER B O   1 
ATOM   1243 C CB  . SER B 1 65 ? 14.293  -19.011 -41.006 1.00 33.82  ? 64  SER B CB  1 
ATOM   1244 O OG  . SER B 1 65 ? 14.971  -17.945 -40.368 1.00 43.74  ? 64  SER B OG  1 
ATOM   1245 N N   . LYS B 1 66 ? 11.849  -16.435 -41.664 1.00 30.40  ? 65  LYS B N   1 
ATOM   1246 C CA  . LYS B 1 66 ? 10.924  -15.618 -40.874 1.00 34.11  ? 65  LYS B CA  1 
ATOM   1247 C C   . LYS B 1 66 ? 9.482   -16.131 -40.858 1.00 34.70  ? 65  LYS B C   1 
ATOM   1248 O O   . LYS B 1 66 ? 8.766   -15.962 -39.869 1.00 36.07  ? 65  LYS B O   1 
ATOM   1249 C CB  . LYS B 1 66 ? 10.984  -14.120 -41.199 1.00 33.37  ? 65  LYS B CB  1 
ATOM   1250 C CG  . LYS B 1 66 ? 10.654  -13.839 -42.670 1.00 39.17  ? 65  LYS B CG  1 
ATOM   1251 N N   . ASP B 1 67 ? 8.985   -16.749 -41.926 1.00 35.13  ? 66  ASP B N   1 
ATOM   1252 C CA  . ASP B 1 67 ? 7.598   -17.172 -41.779 1.00 43.03  ? 66  ASP B CA  1 
ATOM   1253 C C   . ASP B 1 67 ? 7.482   -18.419 -40.895 1.00 42.77  ? 66  ASP B C   1 
ATOM   1254 O O   . ASP B 1 67 ? 6.429   -18.660 -40.293 1.00 45.00  ? 66  ASP B O   1 
ATOM   1255 C CB  . ASP B 1 67 ? 6.798   -17.106 -43.070 1.00 57.13  ? 66  ASP B CB  1 
ATOM   1256 C CG  . ASP B 1 67 ? 7.454   -17.789 -44.255 1.00 69.16  ? 66  ASP B CG  1 
ATOM   1257 O OD1 . ASP B 1 67 ? 6.929   -17.644 -45.386 1.00 75.14  ? 66  ASP B OD1 1 
ATOM   1258 O OD2 . ASP B 1 67 ? 8.488   -18.451 -44.029 1.00 71.04  ? 66  ASP B OD2 1 
ATOM   1259 N N   . LYS B 1 68 ? 8.574   -19.177 -40.767 1.00 37.33  ? 67  LYS B N   1 
ATOM   1260 C CA  . LYS B 1 68 ? 8.551   -20.323 -39.873 1.00 32.86  ? 67  LYS B CA  1 
ATOM   1261 C C   . LYS B 1 68 ? 8.713   -19.876 -38.418 1.00 32.16  ? 67  LYS B C   1 
ATOM   1262 O O   . LYS B 1 68 ? 7.925   -20.289 -37.555 1.00 32.36  ? 67  LYS B O   1 
ATOM   1263 C CB  . LYS B 1 68 ? 9.572   -21.369 -40.321 1.00 35.96  ? 67  LYS B CB  1 
ATOM   1264 C CG  . LYS B 1 68 ? 9.704   -22.620 -39.466 1.00 43.72  ? 67  LYS B CG  1 
ATOM   1265 C CD  . LYS B 1 68 ? 10.756  -23.528 -40.099 1.00 53.94  ? 67  LYS B CD  1 
ATOM   1266 C CE  . LYS B 1 68 ? 10.989  -24.830 -39.391 1.00 61.75  ? 67  LYS B CE  1 
ATOM   1267 N NZ  . LYS B 1 68 ? 9.750   -25.595 -39.220 1.00 63.31  ? 67  LYS B NZ  1 
ATOM   1268 N N   . TYR B 1 69 ? 9.695   -18.996 -38.141 1.00 28.27  ? 68  TYR B N   1 
ATOM   1269 C CA  . TYR B 1 69 ? 10.071  -18.744 -36.750 1.00 26.22  ? 68  TYR B CA  1 
ATOM   1270 C C   . TYR B 1 69 ? 9.572   -17.400 -36.229 1.00 31.11  ? 68  TYR B C   1 
ATOM   1271 O O   . TYR B 1 69 ? 9.746   -17.118 -35.035 1.00 30.89  ? 68  TYR B O   1 
ATOM   1272 C CB  . TYR B 1 69 ? 11.586  -18.814 -36.545 1.00 23.67  ? 68  TYR B CB  1 
ATOM   1273 C CG  . TYR B 1 69 ? 12.214  -20.177 -36.827 1.00 28.93  ? 68  TYR B CG  1 
ATOM   1274 C CD1 . TYR B 1 69 ? 11.689  -21.349 -36.285 1.00 27.48  ? 68  TYR B CD1 1 
ATOM   1275 C CD2 . TYR B 1 69 ? 13.303  -20.283 -37.674 1.00 28.70  ? 68  TYR B CD2 1 
ATOM   1276 C CE1 . TYR B 1 69 ? 12.261  -22.588 -36.557 1.00 28.01  ? 68  TYR B CE1 1 
ATOM   1277 C CE2 . TYR B 1 69 ? 13.877  -21.510 -37.964 1.00 30.39  ? 68  TYR B CE2 1 
ATOM   1278 C CZ  . TYR B 1 69 ? 13.364  -22.664 -37.390 1.00 30.86  ? 68  TYR B CZ  1 
ATOM   1279 O OH  . TYR B 1 69 ? 13.940  -23.862 -37.727 1.00 31.65  ? 68  TYR B OH  1 
ATOM   1280 N N   . GLY B 1 70 ? 8.999   -16.569 -37.116 1.00 32.75  ? 69  GLY B N   1 
ATOM   1281 C CA  . GLY B 1 70 ? 8.767   -15.176 -36.756 1.00 33.05  ? 69  GLY B CA  1 
ATOM   1282 C C   . GLY B 1 70 ? 7.378   -14.934 -36.166 1.00 36.26  ? 69  GLY B C   1 
ATOM   1283 O O   . GLY B 1 70 ? 6.845   -13.852 -36.380 1.00 36.51  ? 69  GLY B O   1 
ATOM   1284 N N   . LYS B 1 71 ? 6.817   -15.917 -35.438 1.00 36.19  ? 70  LYS B N   1 
ATOM   1285 C CA  . LYS B 1 71 ? 5.457   -15.806 -34.925 1.00 38.03  ? 70  LYS B CA  1 
ATOM   1286 C C   . LYS B 1 71 ? 5.525   -15.406 -33.463 1.00 38.16  ? 70  LYS B C   1 
ATOM   1287 O O   . LYS B 1 71 ? 6.409   -15.871 -32.739 1.00 35.22  ? 70  LYS B O   1 
ATOM   1288 C CB  . LYS B 1 71 ? 4.680   -17.129 -34.849 1.00 39.17  ? 70  LYS B CB  1 
ATOM   1289 C CG  . LYS B 1 71 ? 3.808   -17.457 -36.063 1.00 55.61  ? 70  LYS B CG  1 
ATOM   1290 C CD  . LYS B 1 71 ? 4.601   -17.738 -37.330 1.00 52.78  ? 70  LYS B CD  1 
ATOM   1291 C CE  . LYS B 1 71 ? 3.750   -18.272 -38.447 1.00 55.28  ? 70  LYS B CE  1 
ATOM   1292 N NZ  . LYS B 1 71 ? 4.329   -17.877 -39.741 1.00 61.78  ? 70  LYS B NZ  1 
ATOM   1293 N N   . PRO B 1 72 ? 4.616   -14.513 -33.002 1.00 37.73  ? 71  PRO B N   1 
ATOM   1294 C CA  . PRO B 1 72 ? 4.581   -14.141 -31.585 1.00 37.16  ? 71  PRO B CA  1 
ATOM   1295 C C   . PRO B 1 72 ? 4.374   -15.320 -30.631 1.00 37.12  ? 71  PRO B C   1 
ATOM   1296 O O   . PRO B 1 72 ? 3.755   -16.326 -30.973 1.00 34.76  ? 71  PRO B O   1 
ATOM   1297 C CB  . PRO B 1 72 ? 3.519   -13.042 -31.430 1.00 38.74  ? 71  PRO B CB  1 
ATOM   1298 C CG  . PRO B 1 72 ? 3.068   -12.744 -32.846 1.00 42.21  ? 71  PRO B CG  1 
ATOM   1299 C CD  . PRO B 1 72 ? 3.692   -13.738 -33.842 1.00 37.44  ? 71  PRO B CD  1 
ATOM   1300 N N   . ASN B 1 73 ? 4.947   -15.209 -29.426 1.00 34.45  ? 72  ASN B N   1 
ATOM   1301 C CA  . ASN B 1 73 ? 4.751   -16.217 -28.399 1.00 31.92  ? 72  ASN B CA  1 
ATOM   1302 C C   . ASN B 1 73 ? 4.725   -15.530 -27.020 1.00 35.68  ? 72  ASN B C   1 
ATOM   1303 O O   . ASN B 1 73 ? 4.754   -14.302 -26.916 1.00 39.94  ? 72  ASN B O   1 
ATOM   1304 C CB  . ASN B 1 73 ? 5.794   -17.343 -28.472 1.00 32.76  ? 72  ASN B CB  1 
ATOM   1305 C CG  . ASN B 1 73 ? 7.214   -16.895 -28.205 1.00 32.42  ? 72  ASN B CG  1 
ATOM   1306 O OD1 . ASN B 1 73 ? 7.489   -16.211 -27.206 1.00 31.11  ? 72  ASN B OD1 1 
ATOM   1307 N ND2 . ASN B 1 73 ? 8.135   -17.318 -29.072 1.00 27.11  ? 72  ASN B ND2 1 
ATOM   1308 N N   . LYS B 1 74 ? 4.766   -16.323 -25.944 1.00 35.62  ? 73  LYS B N   1 
ATOM   1309 C CA  . LYS B 1 74 ? 4.588   -15.745 -24.610 1.00 42.58  ? 73  LYS B CA  1 
ATOM   1310 C C   . LYS B 1 74 ? 5.901   -15.679 -23.811 1.00 40.88  ? 73  LYS B C   1 
ATOM   1311 O O   . LYS B 1 74 ? 5.872   -15.486 -22.589 1.00 35.55  ? 73  LYS B O   1 
ATOM   1312 C CB  . LYS B 1 74 ? 3.486   -16.474 -23.826 1.00 39.27  ? 73  LYS B CB  1 
ATOM   1313 N N   . ARG B 1 75 ? 7.053   -15.841 -24.481 1.00 28.43  ? 74  ARG B N   1 
ATOM   1314 C CA  . ARG B 1 75 ? 8.348   -15.643 -23.841 1.00 26.79  ? 74  ARG B CA  1 
ATOM   1315 C C   . ARG B 1 75 ? 8.657   -14.147 -23.706 1.00 27.67  ? 74  ARG B C   1 
ATOM   1316 O O   . ARG B 1 75 ? 8.511   -13.347 -24.627 1.00 28.88  ? 74  ARG B O   1 
ATOM   1317 C CB  . ARG B 1 75 ? 9.524   -16.380 -24.527 1.00 26.39  ? 74  ARG B CB  1 
ATOM   1318 C CG  . ARG B 1 75 ? 9.281   -17.875 -24.731 1.00 26.07  ? 74  ARG B CG  1 
ATOM   1319 C CD  . ARG B 1 75 ? 9.169   -18.614 -23.406 1.00 25.75  ? 74  ARG B CD  1 
ATOM   1320 N NE  . ARG B 1 75 ? 9.370   -20.047 -23.668 1.00 26.91  ? 74  ARG B NE  1 
ATOM   1321 C CZ  . ARG B 1 75 ? 10.499  -20.704 -23.521 1.00 25.96  ? 74  ARG B CZ  1 
ATOM   1322 N NH1 . ARG B 1 75 ? 11.601  -20.094 -23.091 1.00 31.96  ? 74  ARG B NH1 1 
ATOM   1323 N NH2 . ARG B 1 75 ? 10.561  -21.997 -23.837 1.00 30.89  ? 74  ARG B NH2 1 
ATOM   1324 N N   . LYS B 1 76 ? 9.047   -13.731 -22.495 1.00 25.23  ? 75  LYS B N   1 
ATOM   1325 C CA  . LYS B 1 76 ? 9.396   -12.347 -22.230 1.00 23.73  ? 75  LYS B CA  1 
ATOM   1326 C C   . LYS B 1 76 ? 10.483  -11.834 -23.199 1.00 23.06  ? 75  LYS B C   1 
ATOM   1327 O O   . LYS B 1 76 ? 11.546  -12.457 -23.266 1.00 26.28  ? 75  LYS B O   1 
ATOM   1328 C CB  . LYS B 1 76 ? 9.922   -12.304 -20.775 1.00 27.80  ? 75  LYS B CB  1 
ATOM   1329 C CG  . LYS B 1 76 ? 10.300  -10.897 -20.288 1.00 27.38  ? 75  LYS B CG  1 
ATOM   1330 C CD  . LYS B 1 76 ? 10.781  -10.821 -18.845 1.00 29.19  ? 75  LYS B CD  1 
ATOM   1331 C CE  . LYS B 1 76 ? 11.246  -9.427  -18.527 1.00 29.52  ? 75  LYS B CE  1 
ATOM   1332 N NZ  . LYS B 1 76 ? 11.567  -9.268  -17.099 1.00 37.20  ? 75  LYS B NZ  1 
ATOM   1333 N N   . GLY B 1 77 ? 10.147  -10.727 -23.870 1.00 24.59  ? 76  GLY B N   1 
ATOM   1334 C CA  . GLY B 1 77 ? 11.066  -10.012 -24.766 1.00 24.48  ? 76  GLY B CA  1 
ATOM   1335 C C   . GLY B 1 77 ? 10.918  -10.480 -26.206 1.00 26.44  ? 76  GLY B C   1 
ATOM   1336 O O   . GLY B 1 77 ? 11.465  -9.866  -27.109 1.00 23.54  ? 76  GLY B O   1 
ATOM   1337 N N   . PHE B 1 78 ? 10.171  -11.568 -26.448 1.00 26.10  ? 77  PHE B N   1 
ATOM   1338 C CA  . PHE B 1 78 ? 10.074  -12.095 -27.818 1.00 24.43  ? 77  PHE B CA  1 
ATOM   1339 C C   . PHE B 1 78 ? 9.343   -11.152 -28.775 1.00 25.23  ? 77  PHE B C   1 
ATOM   1340 O O   . PHE B 1 78 ? 9.812   -10.854 -29.897 1.00 23.68  ? 77  PHE B O   1 
ATOM   1341 C CB  . PHE B 1 78 ? 9.384   -13.452 -27.874 1.00 23.68  ? 77  PHE B CB  1 
ATOM   1342 C CG  . PHE B 1 78 ? 9.688   -14.189 -29.168 1.00 22.37  ? 77  PHE B CG  1 
ATOM   1343 C CD1 . PHE B 1 78 ? 10.779  -15.045 -29.237 1.00 22.67  ? 77  PHE B CD1 1 
ATOM   1344 C CD2 . PHE B 1 78 ? 8.797   -14.087 -30.235 1.00 26.12  ? 77  PHE B CD2 1 
ATOM   1345 C CE1 . PHE B 1 78 ? 11.053  -15.708 -30.430 1.00 23.45  ? 77  PHE B CE1 1 
ATOM   1346 C CE2 . PHE B 1 78 ? 9.056   -14.787 -31.414 1.00 27.70  ? 77  PHE B CE2 1 
ATOM   1347 C CZ  . PHE B 1 78 ? 10.149  -15.630 -31.471 1.00 23.52  ? 77  PHE B CZ  1 
ATOM   1348 N N   . ASN B 1 79 ? 8.148   -10.682 -28.417 1.00 25.73  ? 78  ASN B N   1 
ATOM   1349 C CA  . ASN B 1 79 ? 7.412   -9.805  -29.320 1.00 27.73  ? 78  ASN B CA  1 
ATOM   1350 C C   . ASN B 1 79 ? 8.133   -8.454  -29.488 1.00 29.39  ? 78  ASN B C   1 
ATOM   1351 O O   . ASN B 1 79 ? 8.175   -7.911  -30.596 1.00 29.17  ? 78  ASN B O   1 
ATOM   1352 C CB  . ASN B 1 79 ? 5.918   -9.723  -28.995 1.00 31.27  ? 78  ASN B CB  1 
ATOM   1353 C CG  . ASN B 1 79 ? 5.259   -11.090 -28.938 1.00 36.39  ? 78  ASN B CG  1 
ATOM   1354 O OD1 . ASN B 1 79 ? 5.817   -12.087 -29.422 1.00 32.51  ? 78  ASN B OD1 1 
ATOM   1355 N ND2 . ASN B 1 79 ? 4.104   -11.181 -28.290 1.00 37.40  ? 78  ASN B ND2 1 
ATOM   1356 N N   . GLU B 1 80 ? 8.775   -7.962  -28.438 1.00 25.67  ? 79  GLU B N   1 
ATOM   1357 C CA  . GLU B 1 80 ? 9.587   -6.761  -28.580 1.00 29.50  ? 79  GLU B CA  1 
ATOM   1358 C C   . GLU B 1 80 ? 10.694  -7.028  -29.608 1.00 24.72  ? 79  GLU B C   1 
ATOM   1359 O O   . GLU B 1 80 ? 10.921  -6.169  -30.465 1.00 25.80  ? 79  GLU B O   1 
ATOM   1360 C CB  . GLU B 1 80 ? 10.212  -6.253  -27.285 1.00 29.65  ? 79  GLU B CB  1 
ATOM   1361 C CG  . GLU B 1 80 ? 9.213   -5.556  -26.370 1.00 40.66  ? 79  GLU B CG  1 
ATOM   1362 N N   . GLY B 1 81 ? 11.337  -8.213  -29.507 1.00 23.83  ? 80  GLY B N   1 
ATOM   1363 C CA  . GLY B 1 81 ? 12.438  -8.636  -30.387 1.00 25.21  ? 80  GLY B CA  1 
ATOM   1364 C C   . GLY B 1 81 ? 11.964  -8.701  -31.842 1.00 25.78  ? 80  GLY B C   1 
ATOM   1365 O O   . GLY B 1 81 ? 12.689  -8.249  -32.763 1.00 23.43  ? 80  GLY B O   1 
ATOM   1366 N N   . LEU B 1 82 ? 10.721  -9.158  -32.079 1.00 23.10  ? 81  LEU B N   1 
ATOM   1367 C CA  . LEU B 1 82 ? 10.171  -9.163  -33.432 1.00 24.24  ? 81  LEU B CA  1 
ATOM   1368 C C   . LEU B 1 82 ? 10.042  -7.736  -33.952 1.00 26.99  ? 81  LEU B C   1 
ATOM   1369 O O   . LEU B 1 82 ? 10.263  -7.492  -35.139 1.00 26.36  ? 81  LEU B O   1 
ATOM   1370 C CB  . LEU B 1 82 ? 8.845   -9.932  -33.540 1.00 25.22  ? 81  LEU B CB  1 
ATOM   1371 C CG  . LEU B 1 82 ? 8.917   -11.446 -33.304 1.00 27.08  ? 81  LEU B CG  1 
ATOM   1372 C CD1 . LEU B 1 82 ? 7.509   -12.073 -33.297 1.00 26.09  ? 81  LEU B CD1 1 
ATOM   1373 C CD2 . LEU B 1 82 ? 9.854   -12.163 -34.288 1.00 25.94  ? 81  LEU B CD2 1 
ATOM   1374 N N   . TRP B 1 83 ? 9.595   -6.822  -33.077 1.00 25.75  ? 82  TRP B N   1 
ATOM   1375 C CA  . TRP B 1 83 ? 9.493   -5.415  -33.425 1.00 26.33  ? 82  TRP B CA  1 
ATOM   1376 C C   . TRP B 1 83 ? 10.862  -4.862  -33.824 1.00 27.69  ? 82  TRP B C   1 
ATOM   1377 O O   . TRP B 1 83 ? 10.969  -4.254  -34.895 1.00 27.59  ? 82  TRP B O   1 
ATOM   1378 C CB  . TRP B 1 83 ? 8.852   -4.584  -32.298 1.00 28.80  ? 82  TRP B CB  1 
ATOM   1379 C CG  . TRP B 1 83 ? 8.585   -3.179  -32.785 1.00 28.41  ? 82  TRP B CG  1 
ATOM   1380 C CD1 . TRP B 1 83 ? 7.449   -2.717  -33.386 1.00 34.01  ? 82  TRP B CD1 1 
ATOM   1381 C CD2 . TRP B 1 83 ? 9.529   -2.080  -32.806 1.00 32.67  ? 82  TRP B CD2 1 
ATOM   1382 N NE1 . TRP B 1 83 ? 7.613   -1.406  -33.762 1.00 34.23  ? 82  TRP B NE1 1 
ATOM   1383 C CE2 . TRP B 1 83 ? 8.870   -0.992  -33.421 1.00 32.90  ? 82  TRP B CE2 1 
ATOM   1384 C CE3 . TRP B 1 83 ? 10.847  -1.904  -32.356 1.00 30.47  ? 82  TRP B CE3 1 
ATOM   1385 C CZ2 . TRP B 1 83 ? 9.487   0.254   -33.582 1.00 30.52  ? 82  TRP B CZ2 1 
ATOM   1386 C CZ3 . TRP B 1 83 ? 11.456  -0.666  -32.492 1.00 32.36  ? 82  TRP B CZ3 1 
ATOM   1387 C CH2 . TRP B 1 83 ? 10.776  0.400   -33.093 1.00 31.18  ? 82  TRP B CH2 1 
ATOM   1388 N N   . GLU B 1 84 ? 11.908  -5.171  -33.041 1.00 23.00  ? 83  GLU B N   1 
ATOM   1389 C CA  . GLU B 1 84 ? 13.206  -4.576  -33.271 1.00 26.54  ? 83  GLU B CA  1 
ATOM   1390 C C   . GLU B 1 84 ? 13.821  -5.089  -34.577 1.00 25.68  ? 83  GLU B C   1 
ATOM   1391 O O   . GLU B 1 84 ? 14.429  -4.313  -35.320 1.00 24.20  ? 83  GLU B O   1 
ATOM   1392 C CB  . GLU B 1 84 ? 14.119  -4.833  -32.097 1.00 23.30  ? 83  GLU B CB  1 
ATOM   1393 C CG  . GLU B 1 84 ? 13.625  -4.164  -30.811 1.00 25.12  ? 83  GLU B CG  1 
ATOM   1394 C CD  . GLU B 1 84 ? 14.542  -4.491  -29.670 1.00 25.91  ? 83  GLU B CD  1 
ATOM   1395 O OE1 . GLU B 1 84 ? 15.470  -5.323  -29.761 1.00 25.12  ? 83  GLU B OE1 1 
ATOM   1396 O OE2 . GLU B 1 84 ? 14.288  -3.900  -28.553 1.00 26.86  ? 83  GLU B OE2 1 
ATOM   1397 N N   . ILE B 1 85 ? 13.668  -6.389  -34.865 1.00 25.14  ? 84  ILE B N   1 
ATOM   1398 C CA  . ILE B 1 85 ? 14.388  -6.921  -36.027 1.00 23.36  ? 84  ILE B CA  1 
ATOM   1399 C C   . ILE B 1 85 ? 13.744  -6.387  -37.317 1.00 23.16  ? 84  ILE B C   1 
ATOM   1400 O O   . ILE B 1 85 ? 14.437  -6.174  -38.325 1.00 24.28  ? 84  ILE B O   1 
ATOM   1401 C CB  . ILE B 1 85 ? 14.470  -8.466  -36.000 1.00 23.38  ? 84  ILE B CB  1 
ATOM   1402 C CG1 . ILE B 1 85 ? 15.511  -9.001  -36.992 1.00 23.26  ? 84  ILE B CG1 1 
ATOM   1403 C CG2 . ILE B 1 85 ? 13.115  -9.119  -36.247 1.00 24.11  ? 84  ILE B CG2 1 
ATOM   1404 C CD1 . ILE B 1 85 ? 15.819  -10.458 -36.744 1.00 23.53  ? 84  ILE B CD1 1 
ATOM   1405 N N   . GLN B 1 86 ? 12.444  -6.078  -37.264 1.00 24.39  ? 85  GLN B N   1 
ATOM   1406 C CA  . GLN B 1 86 ? 11.630  -5.561  -38.353 1.00 27.16  ? 85  GLN B CA  1 
ATOM   1407 C C   . GLN B 1 86 ? 11.910  -4.067  -38.523 1.00 29.65  ? 85  GLN B C   1 
ATOM   1408 O O   . GLN B 1 86 ? 12.078  -3.589  -39.647 1.00 34.47  ? 85  GLN B O   1 
ATOM   1409 C CB  . GLN B 1 86 ? 10.150  -5.880  -38.074 1.00 35.01  ? 85  GLN B CB  1 
ATOM   1410 C CG  . GLN B 1 86 ? 9.729   -7.333  -38.350 1.00 45.06  ? 85  GLN B CG  1 
ATOM   1411 C CD  . GLN B 1 86 ? 8.556   -7.906  -37.551 1.00 53.90  ? 85  GLN B CD  1 
ATOM   1412 O OE1 . GLN B 1 86 ? 7.467   -7.326  -37.402 1.00 52.62  ? 85  GLN B OE1 1 
ATOM   1413 N NE2 . GLN B 1 86 ? 8.767   -9.112  -37.037 1.00 44.59  ? 85  GLN B NE2 1 
ATOM   1414 N N   . ASN B 1 87 ? 12.002  -3.326  -37.412 1.00 24.68  ? 86  ASN B N   1 
ATOM   1415 C CA  . ASN B 1 87 ? 11.864  -1.866  -37.542 1.00 26.40  ? 86  ASN B CA  1 
ATOM   1416 C C   . ASN B 1 87 ? 13.174  -1.139  -37.321 1.00 26.54  ? 86  ASN B C   1 
ATOM   1417 O O   . ASN B 1 87 ? 13.297  0.009   -37.776 1.00 28.36  ? 86  ASN B O   1 
ATOM   1418 C CB  . ASN B 1 87 ? 10.804  -1.337  -36.565 1.00 30.15  ? 86  ASN B CB  1 
ATOM   1419 C CG  . ASN B 1 87 ? 9.431   -1.780  -37.017 1.00 36.17  ? 86  ASN B CG  1 
ATOM   1420 O OD1 . ASN B 1 87 ? 8.936   -1.318  -38.043 1.00 43.50  ? 86  ASN B OD1 1 
ATOM   1421 N ND2 . ASN B 1 87 ? 8.831   -2.747  -36.352 1.00 37.96  ? 86  ASN B ND2 1 
ATOM   1422 N N   . ASN B 1 88 ? 14.142  -1.731  -36.616 1.00 24.84  ? 87  ASN B N   1 
ATOM   1423 C CA  . ASN B 1 88 ? 15.387  -1.018  -36.359 1.00 26.62  ? 87  ASN B CA  1 
ATOM   1424 C C   . ASN B 1 88 ? 16.455  -2.010  -35.927 1.00 23.72  ? 87  ASN B C   1 
ATOM   1425 O O   . ASN B 1 88 ? 17.038  -1.932  -34.842 1.00 23.81  ? 87  ASN B O   1 
ATOM   1426 C CB  . ASN B 1 88 ? 15.196  0.209   -35.464 1.00 29.95  ? 87  ASN B CB  1 
ATOM   1427 C CG  . ASN B 1 88 ? 16.303  1.225   -35.622 1.00 29.94  ? 87  ASN B CG  1 
ATOM   1428 O OD1 . ASN B 1 88 ? 17.374  0.979   -36.215 1.00 28.28  ? 87  ASN B OD1 1 
ATOM   1429 N ND2 . ASN B 1 88 ? 16.066  2.385   -35.024 1.00 30.66  ? 87  ASN B ND2 1 
ATOM   1430 N N   . PRO B 1 89 ? 16.743  -2.964  -36.842 1.00 23.98  ? 88  PRO B N   1 
ATOM   1431 C CA  . PRO B 1 89 ? 17.670  -4.044  -36.514 1.00 22.66  ? 88  PRO B CA  1 
ATOM   1432 C C   . PRO B 1 89 ? 19.108  -3.630  -36.250 1.00 22.83  ? 88  PRO B C   1 
ATOM   1433 O O   . PRO B 1 89 ? 19.872  -4.372  -35.643 1.00 24.11  ? 88  PRO B O   1 
ATOM   1434 C CB  . PRO B 1 89 ? 17.581  -4.997  -37.742 1.00 21.98  ? 88  PRO B CB  1 
ATOM   1435 C CG  . PRO B 1 89 ? 17.181  -4.052  -38.905 1.00 23.42  ? 88  PRO B CG  1 
ATOM   1436 C CD  . PRO B 1 89 ? 16.238  -3.029  -38.238 1.00 23.31  ? 88  PRO B CD  1 
ATOM   1437 N N   . HIS B 1 90 ? 19.504  -2.414  -36.741 1.00 22.50  ? 89  HIS B N   1 
ATOM   1438 C CA  . HIS B 1 90 ? 20.910  -2.017  -36.696 1.00 24.77  ? 89  HIS B CA  1 
ATOM   1439 C C   . HIS B 1 90 ? 21.174  -0.920  -35.651 1.00 25.66  ? 89  HIS B C   1 
ATOM   1440 O O   . HIS B 1 90 ? 22.302  -0.452  -35.513 1.00 26.53  ? 89  HIS B O   1 
ATOM   1441 C CB  . HIS B 1 90 ? 21.384  -1.598  -38.101 1.00 22.87  ? 89  HIS B CB  1 
ATOM   1442 C CG  . HIS B 1 90 ? 21.230  -2.737  -39.067 1.00 25.35  ? 89  HIS B CG  1 
ATOM   1443 N ND1 . HIS B 1 90 ? 21.853  -3.961  -38.938 1.00 25.61  ? 89  HIS B ND1 1 
ATOM   1444 C CD2 . HIS B 1 90 ? 20.596  -2.744  -40.254 1.00 24.45  ? 89  HIS B CD2 1 
ATOM   1445 C CE1 . HIS B 1 90 ? 21.540  -4.689  -40.021 1.00 22.77  ? 89  HIS B CE1 1 
ATOM   1446 N NE2 . HIS B 1 90 ? 20.791  -3.988  -40.811 1.00 25.30  ? 89  HIS B NE2 1 
ATOM   1447 N N   . ALA B 1 91 ? 20.187  -0.680  -34.782 1.00 25.16  ? 90  ALA B N   1 
ATOM   1448 C CA  . ALA B 1 91 ? 20.307  0.355   -33.760 1.00 27.96  ? 90  ALA B CA  1 
ATOM   1449 C C   . ALA B 1 91 ? 21.261  -0.055  -32.636 1.00 30.22  ? 90  ALA B C   1 
ATOM   1450 O O   . ALA B 1 91 ? 21.584  -1.216  -32.423 1.00 28.68  ? 90  ALA B O   1 
ATOM   1451 C CB  . ALA B 1 91 ? 18.915  0.722   -33.270 1.00 26.77  ? 90  ALA B CB  1 
ATOM   1452 N N   . SER B 1 92 ? 21.723  0.950   -31.869 1.00 28.64  ? 91  SER B N   1 
ATOM   1453 C CA  . SER B 1 92 ? 22.343  0.716   -30.591 1.00 30.90  ? 91  SER B CA  1 
ATOM   1454 C C   . SER B 1 92 ? 21.231  0.545   -29.554 1.00 32.65  ? 91  SER B C   1 
ATOM   1455 O O   . SER B 1 92 ? 20.332  1.397   -29.462 1.00 35.13  ? 91  SER B O   1 
ATOM   1456 C CB  . SER B 1 92 ? 23.189  1.966   -30.255 1.00 32.27  ? 91  SER B CB  1 
ATOM   1457 O OG  . SER B 1 92 ? 23.640  1.813   -28.924 1.00 41.74  ? 91  SER B OG  1 
ATOM   1458 N N   . TYR B 1 93 ? 21.305  -0.587  -28.828 1.00 33.92  ? 92  TYR B N   1 
ATOM   1459 C CA  . TYR B 1 93 ? 20.421  -0.994  -27.757 1.00 34.27  ? 92  TYR B CA  1 
ATOM   1460 C C   . TYR B 1 93 ? 21.183  -0.925  -26.430 1.00 40.07  ? 92  TYR B C   1 
ATOM   1461 O O   . TYR B 1 93 ? 20.707  -1.400  -25.399 1.00 43.89  ? 92  TYR B O   1 
ATOM   1462 C CB  . TYR B 1 93 ? 19.863  -2.389  -28.080 1.00 30.25  ? 92  TYR B CB  1 
ATOM   1463 C CG  . TYR B 1 93 ? 18.853  -2.295  -29.211 1.00 26.00  ? 92  TYR B CG  1 
ATOM   1464 C CD1 . TYR B 1 93 ? 17.542  -1.887  -28.965 1.00 28.01  ? 92  TYR B CD1 1 
ATOM   1465 C CD2 . TYR B 1 93 ? 19.194  -2.640  -30.532 1.00 28.78  ? 92  TYR B CD2 1 
ATOM   1466 C CE1 . TYR B 1 93 ? 16.617  -1.722  -29.988 1.00 26.26  ? 92  TYR B CE1 1 
ATOM   1467 C CE2 . TYR B 1 93 ? 18.272  -2.498  -31.556 1.00 27.55  ? 92  TYR B CE2 1 
ATOM   1468 C CZ  . TYR B 1 93 ? 16.981  -2.063  -31.289 1.00 28.73  ? 92  TYR B CZ  1 
ATOM   1469 O OH  . TYR B 1 93 ? 16.022  -1.922  -32.269 1.00 28.91  ? 92  TYR B OH  1 
ATOM   1470 N N   . SER B 1 94 ? 22.375  -0.306  -26.466 1.00 49.81  ? 93  SER B N   1 
ATOM   1471 C CA  . SER B 1 94 ? 23.154  0.057   -25.287 1.00 56.37  ? 93  SER B CA  1 
ATOM   1472 C C   . SER B 1 94 ? 22.228  0.325   -24.087 1.00 66.51  ? 93  SER B C   1 
ATOM   1473 O O   . SER B 1 94 ? 21.323  1.195   -24.225 1.00 57.01  ? 93  SER B O   1 
ATOM   1474 C CB  . SER B 1 94 ? 23.990  1.281   -25.573 1.00 63.33  ? 93  SER B CB  1 
ATOM   1475 O OG  . SER B 1 94 ? 24.993  0.997   -26.536 1.00 62.25  ? 93  SER B OG  1 
ATOM   1476 N N   . HIS C 1 4  ? 32.381  -22.703 27.194  1.00 76.41  ? 3   HIS C N   1 
ATOM   1477 C CA  . HIS C 1 4  ? 31.315  -21.915 27.876  1.00 76.87  ? 3   HIS C CA  1 
ATOM   1478 C C   . HIS C 1 4  ? 30.737  -22.755 29.017  1.00 77.01  ? 3   HIS C C   1 
ATOM   1479 O O   . HIS C 1 4  ? 31.397  -23.675 29.505  1.00 78.05  ? 3   HIS C O   1 
ATOM   1480 C CB  . HIS C 1 4  ? 30.282  -21.429 26.845  1.00 74.87  ? 3   HIS C CB  1 
ATOM   1481 N N   . ALA C 1 5  ? 29.520  -22.399 29.455  1.00 71.97  ? 4   ALA C N   1 
ATOM   1482 C CA  . ALA C 1 5  ? 28.659  -23.278 30.233  1.00 68.91  ? 4   ALA C CA  1 
ATOM   1483 C C   . ALA C 1 5  ? 27.225  -23.162 29.729  1.00 64.88  ? 4   ALA C C   1 
ATOM   1484 O O   . ALA C 1 5  ? 26.943  -22.382 28.821  1.00 66.35  ? 4   ALA C O   1 
ATOM   1485 C CB  . ALA C 1 5  ? 28.716  -22.924 31.692  1.00 77.80  ? 4   ALA C CB  1 
ATOM   1486 N N   . PHE C 1 6  ? 26.323  -23.926 30.352  1.00 47.84  ? 5   PHE C N   1 
ATOM   1487 C CA  . PHE C 1 6  ? 24.952  -23.969 29.885  1.00 45.55  ? 5   PHE C CA  1 
ATOM   1488 C C   . PHE C 1 6  ? 24.025  -24.087 31.088  1.00 47.46  ? 5   PHE C C   1 
ATOM   1489 O O   . PHE C 1 6  ? 24.256  -24.916 31.964  1.00 60.22  ? 5   PHE C O   1 
ATOM   1490 C CB  . PHE C 1 6  ? 24.882  -25.178 28.936  1.00 39.27  ? 5   PHE C CB  1 
ATOM   1491 C CG  . PHE C 1 6  ? 25.746  -25.144 27.672  1.00 42.28  ? 5   PHE C CG  1 
ATOM   1492 C CD1 . PHE C 1 6  ? 26.916  -25.888 27.570  1.00 41.56  ? 5   PHE C CD1 1 
ATOM   1493 C CD2 . PHE C 1 6  ? 25.397  -24.348 26.581  1.00 44.02  ? 5   PHE C CD2 1 
ATOM   1494 C CE1 . PHE C 1 6  ? 27.682  -25.866 26.406  1.00 43.08  ? 5   PHE C CE1 1 
ATOM   1495 C CE2 . PHE C 1 6  ? 26.168  -24.334 25.416  1.00 38.69  ? 5   PHE C CE2 1 
ATOM   1496 C CZ  . PHE C 1 6  ? 27.302  -25.088 25.325  1.00 39.02  ? 5   PHE C CZ  1 
ATOM   1497 N N   . LYS C 1 7  ? 22.976  -23.262 31.125  1.00 48.13  ? 6   LYS C N   1 
ATOM   1498 C CA  . LYS C 1 7  ? 21.984  -23.365 32.181  1.00 47.44  ? 6   LYS C CA  1 
ATOM   1499 C C   . LYS C 1 7  ? 20.663  -23.790 31.558  1.00 44.08  ? 6   LYS C C   1 
ATOM   1500 O O   . LYS C 1 7  ? 20.494  -23.686 30.335  1.00 46.13  ? 6   LYS C O   1 
ATOM   1501 C CB  . LYS C 1 7  ? 21.896  -22.028 32.934  1.00 48.78  ? 6   LYS C CB  1 
ATOM   1502 N N   . PRO C 1 8  ? 19.685  -24.291 32.351  1.00 44.01  ? 7   PRO C N   1 
ATOM   1503 C CA  . PRO C 1 8  ? 18.389  -24.696 31.803  1.00 46.86  ? 7   PRO C CA  1 
ATOM   1504 C C   . PRO C 1 8  ? 17.800  -23.543 30.995  1.00 52.32  ? 7   PRO C C   1 
ATOM   1505 O O   . PRO C 1 8  ? 17.750  -22.409 31.466  1.00 58.73  ? 7   PRO C O   1 
ATOM   1506 C CB  . PRO C 1 8  ? 17.579  -25.045 33.073  1.00 50.90  ? 7   PRO C CB  1 
ATOM   1507 C CG  . PRO C 1 8  ? 18.644  -25.533 34.037  1.00 44.59  ? 7   PRO C CG  1 
ATOM   1508 C CD  . PRO C 1 8  ? 19.807  -24.565 33.799  1.00 42.35  ? 7   PRO C CD  1 
ATOM   1509 N N   . GLY C 1 9  ? 17.400  -23.828 29.752  1.00 49.58  ? 8   GLY C N   1 
ATOM   1510 C CA  . GLY C 1 9  ? 16.681  -22.848 28.956  1.00 45.37  ? 8   GLY C CA  1 
ATOM   1511 C C   . GLY C 1 9  ? 17.546  -22.269 27.839  1.00 48.70  ? 8   GLY C C   1 
ATOM   1512 O O   . GLY C 1 9  ? 16.993  -21.703 26.898  1.00 46.66  ? 8   GLY C O   1 
ATOM   1513 N N   . ASP C 1 10 ? 18.876  -22.436 27.951  1.00 41.75  ? 9   ASP C N   1 
ATOM   1514 C CA  . ASP C 1 10 ? 19.856  -22.027 26.956  1.00 34.46  ? 9   ASP C CA  1 
ATOM   1515 C C   . ASP C 1 10 ? 19.669  -22.744 25.613  1.00 40.60  ? 9   ASP C C   1 
ATOM   1516 O O   . ASP C 1 10 ? 19.439  -23.948 25.557  1.00 35.78  ? 9   ASP C O   1 
ATOM   1517 C CB  . ASP C 1 10 ? 21.278  -22.260 27.419  1.00 37.83  ? 9   ASP C CB  1 
ATOM   1518 C CG  . ASP C 1 10 ? 21.843  -21.230 28.395  1.00 53.07  ? 9   ASP C CG  1 
ATOM   1519 O OD1 . ASP C 1 10 ? 21.045  -20.391 28.885  1.00 61.55  ? 9   ASP C OD1 1 
ATOM   1520 O OD2 . ASP C 1 10 ? 23.076  -21.267 28.648  1.00 53.81  ? 9   ASP C OD2 1 
ATOM   1521 N N   . LEU C 1 11 ? 19.769  -21.983 24.511  1.00 39.25  ? 10  LEU C N   1 
ATOM   1522 C CA  . LEU C 1 11 ? 19.475  -22.522 23.189  1.00 35.15  ? 10  LEU C CA  1 
ATOM   1523 C C   . LEU C 1 11 ? 20.765  -22.934 22.502  1.00 30.33  ? 10  LEU C C   1 
ATOM   1524 O O   . LEU C 1 11 ? 21.733  -22.198 22.541  1.00 30.88  ? 10  LEU C O   1 
ATOM   1525 C CB  . LEU C 1 11 ? 18.743  -21.447 22.381  1.00 34.98  ? 10  LEU C CB  1 
ATOM   1526 C CG  . LEU C 1 11 ? 17.423  -20.976 22.982  1.00 32.62  ? 10  LEU C CG  1 
ATOM   1527 C CD1 . LEU C 1 11 ? 16.839  -19.896 22.066  1.00 36.62  ? 10  LEU C CD1 1 
ATOM   1528 C CD2 . LEU C 1 11 ? 16.379  -22.066 23.226  1.00 34.92  ? 10  LEU C CD2 1 
ATOM   1529 N N   . VAL C 1 12 ? 20.748  -24.109 21.813  1.00 27.13  ? 11  VAL C N   1 
ATOM   1530 C CA  . VAL C 1 12 ? 21.932  -24.765 21.302  1.00 27.96  ? 11  VAL C CA  1 
ATOM   1531 C C   . VAL C 1 12 ? 21.553  -25.517 20.015  1.00 26.45  ? 11  VAL C C   1 
ATOM   1532 O O   . VAL C 1 12 ? 20.360  -25.706 19.742  1.00 27.12  ? 11  VAL C O   1 
ATOM   1533 C CB  . VAL C 1 12 ? 22.608  -25.745 22.287  1.00 31.93  ? 11  VAL C CB  1 
ATOM   1534 C CG1 . VAL C 1 12 ? 23.012  -25.082 23.604  1.00 34.56  ? 11  VAL C CG1 1 
ATOM   1535 C CG2 . VAL C 1 12 ? 21.762  -26.987 22.543  1.00 31.25  ? 11  VAL C CG2 1 
ATOM   1536 N N   . PHE C 1 13 ? 22.590  -25.864 19.253  1.00 28.43  ? 12  PHE C N   1 
ATOM   1537 C CA  . PHE C 1 13 ? 22.550  -27.021 18.353  1.00 24.59  ? 12  PHE C CA  1 
ATOM   1538 C C   . PHE C 1 13 ? 23.265  -28.176 19.042  1.00 25.32  ? 12  PHE C C   1 
ATOM   1539 O O   . PHE C 1 13 ? 24.385  -28.044 19.579  1.00 27.36  ? 12  PHE C O   1 
ATOM   1540 C CB  . PHE C 1 13 ? 23.196  -26.746 16.977  1.00 28.58  ? 12  PHE C CB  1 
ATOM   1541 C CG  . PHE C 1 13 ? 22.402  -25.754 16.143  1.00 29.23  ? 12  PHE C CG  1 
ATOM   1542 C CD1 . PHE C 1 13 ? 21.371  -26.191 15.304  1.00 29.34  ? 12  PHE C CD1 1 
ATOM   1543 C CD2 . PHE C 1 13 ? 22.693  -24.391 16.197  1.00 29.90  ? 12  PHE C CD2 1 
ATOM   1544 C CE1 . PHE C 1 13 ? 20.644  -25.274 14.562  1.00 32.71  ? 12  PHE C CE1 1 
ATOM   1545 C CE2 . PHE C 1 13 ? 21.933  -23.481 15.495  1.00 34.00  ? 12  PHE C CE2 1 
ATOM   1546 C CZ  . PHE C 1 13 ? 20.928  -23.933 14.667  1.00 31.00  ? 12  PHE C CZ  1 
ATOM   1547 N N   . ALA C 1 14 ? 22.615  -29.349 19.005  1.00 26.12  ? 13  ALA C N   1 
ATOM   1548 C CA  . ALA C 1 14 ? 23.061  -30.531 19.739  1.00 22.71  ? 13  ALA C CA  1 
ATOM   1549 C C   . ALA C 1 14 ? 23.351  -31.650 18.741  1.00 25.67  ? 13  ALA C C   1 
ATOM   1550 O O   . ALA C 1 14 ? 22.514  -31.965 17.905  1.00 24.17  ? 13  ALA C O   1 
ATOM   1551 C CB  . ALA C 1 14 ? 22.014  -30.941 20.730  1.00 23.63  ? 13  ALA C CB  1 
ATOM   1552 N N   . LYS C 1 15 ? 24.539  -32.239 18.849  1.00 26.54  ? 14  LYS C N   1 
ATOM   1553 C CA  . LYS C 1 15 ? 24.969  -33.233 17.874  1.00 24.55  ? 14  LYS C CA  1 
ATOM   1554 C C   . LYS C 1 15 ? 24.999  -34.594 18.526  1.00 23.67  ? 14  LYS C C   1 
ATOM   1555 O O   . LYS C 1 15 ? 25.726  -34.811 19.492  1.00 27.27  ? 14  LYS C O   1 
ATOM   1556 C CB  . LYS C 1 15 ? 26.395  -32.924 17.384  1.00 25.80  ? 14  LYS C CB  1 
ATOM   1557 C CG  . LYS C 1 15 ? 26.914  -33.826 16.236  1.00 27.89  ? 14  LYS C CG  1 
ATOM   1558 C CD  . LYS C 1 15 ? 26.035  -33.762 14.976  1.00 26.99  ? 14  LYS C CD  1 
ATOM   1559 C CE  . LYS C 1 15 ? 26.561  -34.624 13.797  1.00 29.21  ? 14  LYS C CE  1 
ATOM   1560 N NZ  . LYS C 1 15 ? 26.362  -36.066 13.985  1.00 29.43  ? 14  LYS C NZ  1 
ATOM   1561 N N   . MET C 1 16 ? 24.244  -35.527 17.941  1.00 22.92  ? 15  MET C N   1 
ATOM   1562 C CA  . MET C 1 16 ? 24.247  -36.942 18.295  1.00 23.44  ? 15  MET C CA  1 
ATOM   1563 C C   . MET C 1 16 ? 24.721  -37.738 17.080  1.00 27.24  ? 15  MET C C   1 
ATOM   1564 O O   . MET C 1 16 ? 24.407  -37.410 15.936  1.00 23.79  ? 15  MET C O   1 
ATOM   1565 C CB  . MET C 1 16 ? 22.834  -37.442 18.632  1.00 27.16  ? 15  MET C CB  1 
ATOM   1566 C CG  . MET C 1 16 ? 22.202  -36.767 19.838  1.00 31.81  ? 15  MET C CG  1 
ATOM   1567 S SD  . MET C 1 16 ? 20.618  -37.552 20.203  1.00 34.11  ? 15  MET C SD  1 
ATOM   1568 C CE  . MET C 1 16 ? 19.659  -36.880 18.830  1.00 29.01  ? 15  MET C CE  1 
ATOM   1569 N N   . LYS C 1 17 ? 25.459  -38.842 17.327  1.00 26.88  ? 16  LYS C N   1 
ATOM   1570 C CA  . LYS C 1 17 ? 25.778  -39.733 16.210  1.00 28.17  ? 16  LYS C CA  1 
ATOM   1571 C C   . LYS C 1 17 ? 24.497  -40.182 15.495  1.00 23.10  ? 16  LYS C C   1 
ATOM   1572 O O   . LYS C 1 17 ? 23.537  -40.630 16.125  1.00 28.06  ? 16  LYS C O   1 
ATOM   1573 C CB  . LYS C 1 17 ? 26.530  -40.939 16.794  1.00 27.25  ? 16  LYS C CB  1 
ATOM   1574 C CG  . LYS C 1 17 ? 27.107  -41.953 15.785  1.00 32.64  ? 16  LYS C CG  1 
ATOM   1575 C CD  . LYS C 1 17 ? 28.299  -41.235 15.178  1.00 33.54  ? 16  LYS C CD  1 
ATOM   1576 C CE  . LYS C 1 17 ? 29.019  -42.154 14.236  1.00 47.54  ? 16  LYS C CE  1 
ATOM   1577 N NZ  . LYS C 1 17 ? 30.319  -41.557 13.933  1.00 40.77  ? 16  LYS C NZ  1 
ATOM   1578 N N   . GLY C 1 18 ? 24.542  -40.050 14.154  1.00 26.98  ? 17  GLY C N   1 
ATOM   1579 C CA  . GLY C 1 18 ? 23.477  -40.558 13.301  1.00 26.03  ? 17  GLY C CA  1 
ATOM   1580 C C   . GLY C 1 18 ? 22.517  -39.430 12.919  1.00 27.54  ? 17  GLY C C   1 
ATOM   1581 O O   . GLY C 1 18 ? 21.516  -39.707 12.284  1.00 26.33  ? 17  GLY C O   1 
ATOM   1582 N N   . TYR C 1 19 ? 22.808  -38.199 13.350  1.00 27.02  ? 18  TYR C N   1 
ATOM   1583 C CA  . TYR C 1 19 ? 21.839  -37.097 13.188  1.00 24.61  ? 18  TYR C CA  1 
ATOM   1584 C C   . TYR C 1 19 ? 22.595  -35.809 12.935  1.00 24.32  ? 18  TYR C C   1 
ATOM   1585 O O   . TYR C 1 19 ? 23.723  -35.633 13.409  1.00 24.53  ? 18  TYR C O   1 
ATOM   1586 C CB  . TYR C 1 19 ? 21.022  -36.808 14.450  1.00 23.17  ? 18  TYR C CB  1 
ATOM   1587 C CG  . TYR C 1 19 ? 20.196  -38.012 14.841  1.00 24.13  ? 18  TYR C CG  1 
ATOM   1588 C CD1 . TYR C 1 19 ? 20.723  -39.019 15.647  1.00 25.54  ? 18  TYR C CD1 1 
ATOM   1589 C CD2 . TYR C 1 19 ? 18.912  -38.124 14.348  1.00 25.95  ? 18  TYR C CD2 1 
ATOM   1590 C CE1 . TYR C 1 19 ? 19.954  -40.117 15.986  1.00 27.79  ? 18  TYR C CE1 1 
ATOM   1591 C CE2 . TYR C 1 19 ? 18.140  -39.216 14.691  1.00 32.23  ? 18  TYR C CE2 1 
ATOM   1592 C CZ  . TYR C 1 19 ? 18.660  -40.198 15.508  1.00 31.44  ? 18  TYR C CZ  1 
ATOM   1593 O OH  . TYR C 1 19 ? 17.798  -41.235 15.788  1.00 40.65  ? 18  TYR C OH  1 
ATOM   1594 N N   . PRO C 1 20 ? 22.046  -34.869 12.143  1.00 23.42  ? 19  PRO C N   1 
ATOM   1595 C CA  . PRO C 1 20 ? 22.718  -33.591 11.929  1.00 22.53  ? 19  PRO C CA  1 
ATOM   1596 C C   . PRO C 1 20 ? 22.638  -32.760 13.212  1.00 22.88  ? 19  PRO C C   1 
ATOM   1597 O O   . PRO C 1 20 ? 21.855  -33.020 14.117  1.00 22.35  ? 19  PRO C O   1 
ATOM   1598 C CB  . PRO C 1 20 ? 21.871  -32.958 10.778  1.00 26.75  ? 19  PRO C CB  1 
ATOM   1599 C CG  . PRO C 1 20 ? 20.494  -33.498 11.015  1.00 25.19  ? 19  PRO C CG  1 
ATOM   1600 C CD  . PRO C 1 20 ? 20.748  -34.959 11.435  1.00 23.32  ? 19  PRO C CD  1 
ATOM   1601 N N   . HIS C 1 21 ? 23.428  -31.698 13.219  1.00 22.36  ? 20  HIS C N   1 
ATOM   1602 C CA  . HIS C 1 21 ? 23.379  -30.798 14.356  1.00 22.47  ? 20  HIS C CA  1 
ATOM   1603 C C   . HIS C 1 21 ? 21.956  -30.259 14.513  1.00 25.09  ? 20  HIS C C   1 
ATOM   1604 O O   . HIS C 1 21 ? 21.405  -29.713 13.560  1.00 25.10  ? 20  HIS C O   1 
ATOM   1605 C CB  . HIS C 1 21 ? 24.318  -29.612 14.154  1.00 26.19  ? 20  HIS C CB  1 
ATOM   1606 C CG  . HIS C 1 21 ? 25.755  -30.022 14.200  1.00 28.89  ? 20  HIS C CG  1 
ATOM   1607 N ND1 . HIS C 1 21 ? 26.414  -30.611 13.149  1.00 31.70  ? 20  HIS C ND1 1 
ATOM   1608 C CD2 . HIS C 1 21 ? 26.665  -29.854 15.200  1.00 29.32  ? 20  HIS C CD2 1 
ATOM   1609 C CE1 . HIS C 1 21 ? 27.678  -30.829 13.504  1.00 33.63  ? 20  HIS C CE1 1 
ATOM   1610 N NE2 . HIS C 1 21 ? 27.860  -30.374 14.734  1.00 31.87  ? 20  HIS C NE2 1 
ATOM   1611 N N   . TRP C 1 22 ? 21.376  -30.412 15.712  1.00 22.65  ? 21  TRP C N   1 
ATOM   1612 C CA  . TRP C 1 22 ? 19.918  -30.316 15.841  1.00 20.40  ? 21  TRP C CA  1 
ATOM   1613 C C   . TRP C 1 22 ? 19.511  -29.150 16.739  1.00 22.44  ? 21  TRP C C   1 
ATOM   1614 O O   . TRP C 1 22 ? 20.088  -28.963 17.828  1.00 22.66  ? 21  TRP C O   1 
ATOM   1615 C CB  . TRP C 1 22 ? 19.359  -31.625 16.435  1.00 19.79  ? 21  TRP C CB  1 
ATOM   1616 C CG  . TRP C 1 22 ? 17.909  -31.847 16.061  1.00 21.46  ? 21  TRP C CG  1 
ATOM   1617 C CD1 . TRP C 1 22 ? 16.822  -31.252 16.642  1.00 24.51  ? 21  TRP C CD1 1 
ATOM   1618 C CD2 . TRP C 1 22 ? 17.407  -32.728 15.031  1.00 21.42  ? 21  TRP C CD2 1 
ATOM   1619 N NE1 . TRP C 1 22 ? 15.682  -31.668 16.004  1.00 24.87  ? 21  TRP C NE1 1 
ATOM   1620 C CE2 . TRP C 1 22 ? 15.998  -32.587 15.044  1.00 22.79  ? 21  TRP C CE2 1 
ATOM   1621 C CE3 . TRP C 1 22 ? 18.008  -33.628 14.141  1.00 23.45  ? 21  TRP C CE3 1 
ATOM   1622 C CZ2 . TRP C 1 22 ? 15.199  -33.311 14.152  1.00 23.72  ? 21  TRP C CZ2 1 
ATOM   1623 C CZ3 . TRP C 1 22 ? 17.219  -34.323 13.235  1.00 24.37  ? 21  TRP C CZ3 1 
ATOM   1624 C CH2 . TRP C 1 22 ? 15.831  -34.167 13.283  1.00 23.77  ? 21  TRP C CH2 1 
ATOM   1625 N N   . PRO C 1 23 ? 18.480  -28.349 16.387  1.00 23.83  ? 22  PRO C N   1 
ATOM   1626 C CA  . PRO C 1 23 ? 18.132  -27.249 17.284  1.00 22.13  ? 22  PRO C CA  1 
ATOM   1627 C C   . PRO C 1 23 ? 17.568  -27.814 18.583  1.00 20.97  ? 22  PRO C C   1 
ATOM   1628 O O   . PRO C 1 23 ? 16.700  -28.685 18.584  1.00 23.13  ? 22  PRO C O   1 
ATOM   1629 C CB  . PRO C 1 23 ? 17.071  -26.498 16.410  1.00 27.14  ? 22  PRO C CB  1 
ATOM   1630 C CG  . PRO C 1 23 ? 16.508  -27.550 15.461  1.00 23.51  ? 22  PRO C CG  1 
ATOM   1631 C CD  . PRO C 1 23 ? 17.771  -28.307 15.080  1.00 21.45  ? 22  PRO C CD  1 
ATOM   1632 N N   . ALA C 1 24 ? 18.017  -27.250 19.693  1.00 24.36  ? 23  ALA C N   1 
ATOM   1633 C CA  . ALA C 1 24 ? 17.664  -27.808 20.996  1.00 25.75  ? 23  ALA C CA  1 
ATOM   1634 C C   . ALA C 1 24 ? 17.766  -26.759 22.110  1.00 28.51  ? 23  ALA C C   1 
ATOM   1635 O O   . ALA C 1 24 ? 18.263  -25.643 21.910  1.00 27.81  ? 23  ALA C O   1 
ATOM   1636 C CB  . ALA C 1 24 ? 18.606  -28.995 21.268  1.00 25.11  ? 23  ALA C CB  1 
ATOM   1637 N N   . ARG C 1 25 ? 17.384  -27.167 23.329  1.00 27.87  ? 24  ARG C N   1 
ATOM   1638 C CA  . ARG C 1 25 ? 17.797  -26.358 24.467  1.00 28.75  ? 24  ARG C CA  1 
ATOM   1639 C C   . ARG C 1 25 ? 18.274  -27.266 25.609  1.00 29.36  ? 24  ARG C C   1 
ATOM   1640 O O   . ARG C 1 25 ? 17.932  -28.447 25.635  1.00 31.86  ? 24  ARG C O   1 
ATOM   1641 C CB  . ARG C 1 25 ? 16.614  -25.515 24.951  1.00 34.39  ? 24  ARG C CB  1 
ATOM   1642 C CG  . ARG C 1 25 ? 15.340  -26.287 25.237  1.00 35.78  ? 24  ARG C CG  1 
ATOM   1643 C CD  . ARG C 1 25 ? 14.373  -25.370 26.006  1.00 37.98  ? 24  ARG C CD  1 
ATOM   1644 N NE  . ARG C 1 25 ? 13.198  -26.222 26.205  1.00 47.91  ? 24  ARG C NE  1 
ATOM   1645 C CZ  . ARG C 1 25 ? 11.935  -25.970 25.920  1.00 52.27  ? 24  ARG C CZ  1 
ATOM   1646 N NH1 . ARG C 1 25 ? 11.573  -24.793 25.428  1.00 47.96  ? 24  ARG C NH1 1 
ATOM   1647 N NH2 . ARG C 1 25 ? 11.040  -26.916 26.148  1.00 52.63  ? 24  ARG C NH2 1 
ATOM   1648 N N   . ILE C 1 26 ? 18.988  -26.648 26.548  1.00 32.22  ? 25  ILE C N   1 
ATOM   1649 C CA  . ILE C 1 26 ? 19.334  -27.244 27.833  1.00 33.36  ? 25  ILE C CA  1 
ATOM   1650 C C   . ILE C 1 26 ? 18.087  -27.278 28.715  1.00 41.68  ? 25  ILE C C   1 
ATOM   1651 O O   . ILE C 1 26 ? 17.399  -26.273 28.890  1.00 44.97  ? 25  ILE C O   1 
ATOM   1652 C CB  . ILE C 1 26 ? 20.468  -26.452 28.505  1.00 35.96  ? 25  ILE C CB  1 
ATOM   1653 C CG1 . ILE C 1 26 ? 21.573  -26.037 27.556  1.00 37.34  ? 25  ILE C CG1 1 
ATOM   1654 C CG2 . ILE C 1 26 ? 20.998  -27.180 29.751  1.00 38.64  ? 25  ILE C CG2 1 
ATOM   1655 C CD1 . ILE C 1 26 ? 22.592  -27.095 27.174  1.00 40.19  ? 25  ILE C CD1 1 
ATOM   1656 N N   . ASP C 1 27 ? 17.784  -28.450 29.261  1.00 40.53  ? 26  ASP C N   1 
ATOM   1657 C CA  . ASP C 1 27 ? 16.737  -28.591 30.261  1.00 53.47  ? 26  ASP C CA  1 
ATOM   1658 C C   . ASP C 1 27 ? 17.288  -28.470 31.680  1.00 57.21  ? 26  ASP C C   1 
ATOM   1659 O O   . ASP C 1 27 ? 18.508  -28.465 31.881  1.00 58.47  ? 26  ASP C O   1 
ATOM   1660 C CB  . ASP C 1 27 ? 16.026  -29.926 30.143  1.00 51.64  ? 26  ASP C CB  1 
ATOM   1661 C CG  . ASP C 1 27 ? 14.749  -29.861 29.331  1.00 62.07  ? 26  ASP C CG  1 
ATOM   1662 O OD1 . ASP C 1 27 ? 14.600  -28.838 28.626  1.00 56.57  ? 26  ASP C OD1 1 
ATOM   1663 O OD2 . ASP C 1 27 ? 13.914  -30.803 29.464  1.00 54.68  ? 26  ASP C OD2 1 
ATOM   1664 N N   . ASP C 1 28 ? 16.347  -28.359 32.639  1.00 72.26  ? 27  ASP C N   1 
ATOM   1665 C CA  . ASP C 1 28 ? 16.576  -28.506 34.071  1.00 67.52  ? 27  ASP C CA  1 
ATOM   1666 C C   . ASP C 1 28 ? 16.524  -29.992 34.398  1.00 68.19  ? 27  ASP C C   1 
ATOM   1667 O O   . ASP C 1 28 ? 15.851  -30.739 33.694  1.00 72.63  ? 27  ASP C O   1 
ATOM   1668 C CB  . ASP C 1 28 ? 15.492  -27.814 34.881  1.00 70.27  ? 27  ASP C CB  1 
ATOM   1669 N N   . ILE C 1 29 ? 17.229  -30.404 35.462  1.00 69.19  ? 28  ILE C N   1 
ATOM   1670 C CA  . ILE C 1 29 ? 17.293  -31.808 35.842  1.00 71.38  ? 28  ILE C CA  1 
ATOM   1671 C C   . ILE C 1 29 ? 15.951  -32.217 36.477  1.00 72.37  ? 28  ILE C C   1 
ATOM   1672 O O   . ILE C 1 29 ? 15.658  -31.700 37.572  1.00 73.63  ? 28  ILE C O   1 
ATOM   1673 C CB  . ILE C 1 29 ? 18.488  -32.076 36.779  1.00 68.64  ? 28  ILE C CB  1 
ATOM   1674 N N   . LYS C 1 35 ? 19.429  -38.712 37.655  1.00 57.97  ? 34  LYS C N   1 
ATOM   1675 C CA  . LYS C 1 35 ? 20.523  -37.713 37.508  1.00 54.41  ? 34  LYS C CA  1 
ATOM   1676 C C   . LYS C 1 35 ? 21.323  -38.013 36.238  1.00 50.98  ? 34  LYS C C   1 
ATOM   1677 O O   . LYS C 1 35 ? 21.454  -39.169 35.832  1.00 54.17  ? 34  LYS C O   1 
ATOM   1678 C CB  . LYS C 1 35 ? 21.380  -37.704 38.780  1.00 57.72  ? 34  LYS C CB  1 
ATOM   1679 N N   . PRO C 1 36 ? 21.899  -36.992 35.561  1.00 49.73  ? 35  PRO C N   1 
ATOM   1680 C CA  . PRO C 1 36 ? 22.630  -37.241 34.316  1.00 47.62  ? 35  PRO C CA  1 
ATOM   1681 C C   . PRO C 1 36 ? 23.780  -38.225 34.536  1.00 51.31  ? 35  PRO C C   1 
ATOM   1682 O O   . PRO C 1 36 ? 24.238  -38.433 35.667  1.00 49.02  ? 35  PRO C O   1 
ATOM   1683 C CB  . PRO C 1 36 ? 23.125  -35.836 33.910  1.00 53.19  ? 35  PRO C CB  1 
ATOM   1684 C CG  . PRO C 1 36 ? 22.222  -34.869 34.659  1.00 53.25  ? 35  PRO C CG  1 
ATOM   1685 C CD  . PRO C 1 36 ? 21.913  -35.574 35.974  1.00 50.78  ? 35  PRO C CD  1 
ATOM   1686 N N   . PRO C 1 37 ? 24.294  -38.898 33.485  1.00 48.73  ? 36  PRO C N   1 
ATOM   1687 C CA  . PRO C 1 37 ? 25.632  -39.468 33.580  1.00 45.15  ? 36  PRO C CA  1 
ATOM   1688 C C   . PRO C 1 37 ? 26.589  -38.325 33.908  1.00 40.81  ? 36  PRO C C   1 
ATOM   1689 O O   . PRO C 1 37 ? 26.288  -37.151 33.674  1.00 36.32  ? 36  PRO C O   1 
ATOM   1690 C CB  . PRO C 1 37 ? 25.842  -40.042 32.171  1.00 42.95  ? 36  PRO C CB  1 
ATOM   1691 C CG  . PRO C 1 37 ? 24.452  -40.450 31.776  1.00 41.31  ? 36  PRO C CG  1 
ATOM   1692 C CD  . PRO C 1 37 ? 23.616  -39.263 32.228  1.00 43.50  ? 36  PRO C CD  1 
ATOM   1693 N N   . PRO C 1 38 ? 27.767  -38.643 34.487  1.00 38.74  ? 37  PRO C N   1 
ATOM   1694 C CA  . PRO C 1 38 ? 28.777  -37.634 34.784  1.00 36.10  ? 37  PRO C CA  1 
ATOM   1695 C C   . PRO C 1 38 ? 29.049  -36.743 33.585  1.00 33.03  ? 37  PRO C C   1 
ATOM   1696 O O   . PRO C 1 38 ? 29.272  -37.248 32.490  1.00 33.10  ? 37  PRO C O   1 
ATOM   1697 C CB  . PRO C 1 38 ? 29.999  -38.544 35.127  1.00 35.60  ? 37  PRO C CB  1 
ATOM   1698 C CG  . PRO C 1 38 ? 29.337  -39.729 35.763  1.00 37.08  ? 37  PRO C CG  1 
ATOM   1699 C CD  . PRO C 1 38 ? 28.178  -40.012 34.845  1.00 44.18  ? 37  PRO C CD  1 
ATOM   1700 N N   . ASN C 1 39 ? 29.007  -35.420 33.827  1.00 34.82  ? 38  ASN C N   1 
ATOM   1701 C CA  . ASN C 1 39 ? 29.430  -34.375 32.914  1.00 33.45  ? 38  ASN C CA  1 
ATOM   1702 C C   . ASN C 1 39 ? 28.518  -34.320 31.686  1.00 34.67  ? 38  ASN C C   1 
ATOM   1703 O O   . ASN C 1 39 ? 28.990  -33.959 30.614  1.00 38.75  ? 38  ASN C O   1 
ATOM   1704 C CB  . ASN C 1 39 ? 30.864  -34.565 32.431  1.00 35.56  ? 38  ASN C CB  1 
ATOM   1705 C CG  . ASN C 1 39 ? 31.473  -33.296 31.874  1.00 42.88  ? 38  ASN C CG  1 
ATOM   1706 O OD1 . ASN C 1 39 ? 31.087  -32.187 32.264  1.00 54.63  ? 38  ASN C OD1 1 
ATOM   1707 N ND2 . ASN C 1 39 ? 32.419  -33.424 30.954  1.00 46.80  ? 38  ASN C ND2 1 
ATOM   1708 N N   . LYS C 1 40 ? 27.255  -34.753 31.826  1.00 29.95  ? 39  LYS C N   1 
ATOM   1709 C CA  . LYS C 1 40 ? 26.330  -34.628 30.706  1.00 28.82  ? 39  LYS C CA  1 
ATOM   1710 C C   . LYS C 1 40 ? 25.148  -33.738 31.075  1.00 30.22  ? 39  LYS C C   1 
ATOM   1711 O O   . LYS C 1 40 ? 24.735  -33.637 32.213  1.00 33.03  ? 39  LYS C O   1 
ATOM   1712 C CB  . LYS C 1 40 ? 25.667  -35.969 30.374  1.00 29.79  ? 39  LYS C CB  1 
ATOM   1713 C CG  . LYS C 1 40 ? 26.671  -37.045 30.052  1.00 34.16  ? 39  LYS C CG  1 
ATOM   1714 C CD  . LYS C 1 40 ? 27.490  -36.861 28.785  1.00 39.19  ? 39  LYS C CD  1 
ATOM   1715 C CE  . LYS C 1 40 ? 28.464  -38.008 28.627  1.00 39.36  ? 39  LYS C CE  1 
ATOM   1716 N NZ  . LYS C 1 40 ? 29.277  -37.764 27.430  1.00 46.06  ? 39  LYS C NZ  1 
ATOM   1717 N N   . TYR C 1 41 ? 24.592  -33.081 30.053  1.00 28.11  ? 40  TYR C N   1 
ATOM   1718 C CA  . TYR C 1 41 ? 23.466  -32.172 30.201  1.00 28.43  ? 40  TYR C CA  1 
ATOM   1719 C C   . TYR C 1 41 ? 22.212  -32.826 29.650  1.00 30.10  ? 40  TYR C C   1 
ATOM   1720 O O   . TYR C 1 41 ? 22.272  -33.546 28.644  1.00 29.60  ? 40  TYR C O   1 
ATOM   1721 C CB  . TYR C 1 41 ? 23.604  -30.960 29.271  1.00 27.58  ? 40  TYR C CB  1 
ATOM   1722 C CG  . TYR C 1 41 ? 24.720  -30.017 29.703  1.00 27.89  ? 40  TYR C CG  1 
ATOM   1723 C CD1 . TYR C 1 41 ? 26.021  -30.149 29.234  1.00 28.99  ? 40  TYR C CD1 1 
ATOM   1724 C CD2 . TYR C 1 41 ? 24.456  -28.997 30.612  1.00 32.50  ? 40  TYR C CD2 1 
ATOM   1725 C CE1 . TYR C 1 41 ? 27.030  -29.293 29.637  1.00 39.48  ? 40  TYR C CE1 1 
ATOM   1726 C CE2 . TYR C 1 41 ? 25.448  -28.111 30.989  1.00 34.31  ? 40  TYR C CE2 1 
ATOM   1727 C CZ  . TYR C 1 41 ? 26.738  -28.274 30.530  1.00 35.34  ? 40  TYR C CZ  1 
ATOM   1728 O OH  . TYR C 1 41 ? 27.726  -27.410 30.911  1.00 48.46  ? 40  TYR C OH  1 
ATOM   1729 N N   . PRO C 1 42 ? 21.042  -32.530 30.258  1.00 32.03  ? 41  PRO C N   1 
ATOM   1730 C CA  . PRO C 1 42 ? 19.753  -32.945 29.709  1.00 29.88  ? 41  PRO C CA  1 
ATOM   1731 C C   . PRO C 1 42 ? 19.412  -31.969 28.591  1.00 29.40  ? 41  PRO C C   1 
ATOM   1732 O O   . PRO C 1 42 ? 19.487  -30.745 28.790  1.00 30.80  ? 41  PRO C O   1 
ATOM   1733 C CB  . PRO C 1 42 ? 18.792  -32.846 30.899  1.00 31.70  ? 41  PRO C CB  1 
ATOM   1734 C CG  . PRO C 1 42 ? 19.427  -31.814 31.784  1.00 33.69  ? 41  PRO C CG  1 
ATOM   1735 C CD  . PRO C 1 42 ? 20.913  -31.749 31.510  1.00 34.46  ? 41  PRO C CD  1 
ATOM   1736 N N   . ILE C 1 43 ? 19.131  -32.571 27.436  1.00 28.81  ? 42  ILE C N   1 
ATOM   1737 C CA  . ILE C 1 43 ? 18.814  -31.798 26.236  1.00 26.44  ? 42  ILE C CA  1 
ATOM   1738 C C   . ILE C 1 43 ? 17.388  -32.096 25.803  1.00 28.53  ? 42  ILE C C   1 
ATOM   1739 O O   . ILE C 1 43 ? 16.941  -33.245 25.806  1.00 31.62  ? 42  ILE C O   1 
ATOM   1740 C CB  . ILE C 1 43 ? 19.813  -32.175 25.131  1.00 26.79  ? 42  ILE C CB  1 
ATOM   1741 C CG1 . ILE C 1 43 ? 21.277  -31.928 25.565  1.00 28.19  ? 42  ILE C CG1 1 
ATOM   1742 C CG2 . ILE C 1 43 ? 19.452  -31.446 23.822  1.00 27.50  ? 42  ILE C CG2 1 
ATOM   1743 C CD1 . ILE C 1 43 ? 21.586  -30.492 25.916  1.00 30.54  ? 42  ILE C CD1 1 
ATOM   1744 N N   . PHE C 1 44 ? 16.687  -31.036 25.332  1.00 30.21  ? 43  PHE C N   1 
ATOM   1745 C CA  . PHE C 1 44 ? 15.392  -31.219 24.710  1.00 29.19  ? 43  PHE C CA  1 
ATOM   1746 C C   . PHE C 1 44 ? 15.507  -30.754 23.256  1.00 25.74  ? 43  PHE C C   1 
ATOM   1747 O O   . PHE C 1 44 ? 16.068  -29.660 23.010  1.00 27.74  ? 43  PHE C O   1 
ATOM   1748 C CB  . PHE C 1 44 ? 14.434  -30.246 25.403  1.00 33.41  ? 43  PHE C CB  1 
ATOM   1749 C CG  . PHE C 1 44 ? 13.064  -30.151 24.753  1.00 33.58  ? 43  PHE C CG  1 
ATOM   1750 C CD1 . PHE C 1 44 ? 12.050  -31.077 25.031  1.00 32.69  ? 43  PHE C CD1 1 
ATOM   1751 C CD2 . PHE C 1 44 ? 12.787  -29.103 23.870  1.00 34.55  ? 43  PHE C CD2 1 
ATOM   1752 C CE1 . PHE C 1 44 ? 10.791  -30.965 24.433  1.00 41.27  ? 43  PHE C CE1 1 
ATOM   1753 C CE2 . PHE C 1 44 ? 11.536  -28.994 23.270  1.00 37.21  ? 43  PHE C CE2 1 
ATOM   1754 C CZ  . PHE C 1 44 ? 10.542  -29.915 23.555  1.00 37.55  ? 43  PHE C CZ  1 
ATOM   1755 N N   . PHE C 1 45 ? 15.039  -31.620 22.364  1.00 25.83  ? 44  PHE C N   1 
ATOM   1756 C CA  . PHE C 1 45 ? 15.198  -31.433 20.933  1.00 27.03  ? 44  PHE C CA  1 
ATOM   1757 C C   . PHE C 1 45 ? 13.948  -30.761 20.398  1.00 25.65  ? 44  PHE C C   1 
ATOM   1758 O O   . PHE C 1 45 ? 12.826  -31.282 20.554  1.00 28.94  ? 44  PHE C O   1 
ATOM   1759 C CB  . PHE C 1 45 ? 15.555  -32.697 20.162  1.00 24.18  ? 44  PHE C CB  1 
ATOM   1760 C CG  . PHE C 1 45 ? 16.940  -33.240 20.487  1.00 24.74  ? 44  PHE C CG  1 
ATOM   1761 C CD1 . PHE C 1 45 ? 18.063  -32.841 19.757  1.00 25.09  ? 44  PHE C CD1 1 
ATOM   1762 C CD2 . PHE C 1 45 ? 17.094  -34.179 21.514  1.00 26.06  ? 44  PHE C CD2 1 
ATOM   1763 C CE1 . PHE C 1 45 ? 19.320  -33.364 20.042  1.00 29.11  ? 44  PHE C CE1 1 
ATOM   1764 C CE2 . PHE C 1 45 ? 18.354  -34.714 21.773  1.00 30.37  ? 44  PHE C CE2 1 
ATOM   1765 C CZ  . PHE C 1 45 ? 19.461  -34.307 21.049  1.00 27.25  ? 44  PHE C CZ  1 
ATOM   1766 N N   . PHE C 1 46 ? 14.160  -29.597 19.757  1.00 25.71  ? 45  PHE C N   1 
ATOM   1767 C CA  . PHE C 1 46 ? 13.018  -29.001 19.082  1.00 24.76  ? 45  PHE C CA  1 
ATOM   1768 C C   . PHE C 1 46 ? 12.537  -29.851 17.903  1.00 27.80  ? 45  PHE C C   1 
ATOM   1769 O O   . PHE C 1 46 ? 13.274  -30.609 17.278  1.00 26.40  ? 45  PHE C O   1 
ATOM   1770 C CB  . PHE C 1 46 ? 13.284  -27.555 18.657  1.00 24.24  ? 45  PHE C CB  1 
ATOM   1771 C CG  . PHE C 1 46 ? 13.505  -26.567 19.788  1.00 23.81  ? 45  PHE C CG  1 
ATOM   1772 C CD1 . PHE C 1 46 ? 12.434  -26.142 20.586  1.00 26.42  ? 45  PHE C CD1 1 
ATOM   1773 C CD2 . PHE C 1 46 ? 14.775  -26.033 20.026  1.00 26.77  ? 45  PHE C CD2 1 
ATOM   1774 C CE1 . PHE C 1 46 ? 12.673  -25.223 21.617  1.00 28.18  ? 45  PHE C CE1 1 
ATOM   1775 C CE2 . PHE C 1 46 ? 15.017  -25.139 21.071  1.00 27.34  ? 45  PHE C CE2 1 
ATOM   1776 C CZ  . PHE C 1 46 ? 13.956  -24.684 21.835  1.00 26.14  ? 45  PHE C CZ  1 
ATOM   1777 N N   . GLY C 1 47 ? 11.242  -29.744 17.599  1.00 24.28  ? 46  GLY C N   1 
ATOM   1778 C CA  . GLY C 1 47 ? 10.689  -30.431 16.446  1.00 29.06  ? 46  GLY C CA  1 
ATOM   1779 C C   . GLY C 1 47 ? 10.247  -31.851 16.801  1.00 31.43  ? 46  GLY C C   1 
ATOM   1780 O O   . GLY C 1 47 ? 9.057   -32.180 16.767  1.00 33.81  ? 46  GLY C O   1 
ATOM   1781 N N   . THR C 1 48 ? 11.206  -32.714 17.177  1.00 28.48  ? 47  THR C N   1 
ATOM   1782 C CA  . THR C 1 48 ? 10.832  -34.054 17.629  1.00 30.24  ? 47  THR C CA  1 
ATOM   1783 C C   . THR C 1 48 ? 10.327  -34.008 19.084  1.00 29.58  ? 47  THR C C   1 
ATOM   1784 O O   . THR C 1 48 ? 9.571   -34.900 19.496  1.00 34.43  ? 47  THR C O   1 
ATOM   1785 C CB  . THR C 1 48 ? 12.046  -34.973 17.540  1.00 26.20  ? 47  THR C CB  1 
ATOM   1786 O OG1 . THR C 1 48 ? 12.877  -34.401 18.564  1.00 31.08  ? 47  THR C OG1 1 
ATOM   1787 C CG2 . THR C 1 48 ? 12.646  -35.057 16.147  1.00 26.67  ? 47  THR C CG2 1 
ATOM   1788 N N   . HIS C 1 49 ? 10.724  -33.001 19.864  1.00 28.87  ? 48  HIS C N   1 
ATOM   1789 C CA  . HIS C 1 49 ? 10.444  -32.883 21.295  1.00 32.01  ? 48  HIS C CA  1 
ATOM   1790 C C   . HIS C 1 49 ? 10.892  -34.111 22.100  1.00 30.85  ? 48  HIS C C   1 
ATOM   1791 O O   . HIS C 1 49 ? 10.232  -34.460 23.089  1.00 35.53  ? 48  HIS C O   1 
ATOM   1792 C CB  . HIS C 1 49 ? 8.954   -32.612 21.558  1.00 36.50  ? 48  HIS C CB  1 
ATOM   1793 C CG  . HIS C 1 49 ? 8.435   -31.529 20.680  1.00 37.14  ? 48  HIS C CG  1 
ATOM   1794 N ND1 . HIS C 1 49 ? 7.326   -31.710 19.875  1.00 43.91  ? 48  HIS C ND1 1 
ATOM   1795 C CD2 . HIS C 1 49 ? 8.908   -30.312 20.407  1.00 36.15  ? 48  HIS C CD2 1 
ATOM   1796 C CE1 . HIS C 1 49 ? 7.135   -30.609 19.156  1.00 44.46  ? 48  HIS C CE1 1 
ATOM   1797 N NE2 . HIS C 1 49 ? 8.074   -29.747 19.469  1.00 41.41  ? 48  HIS C NE2 1 
ATOM   1798 N N   . GLU C 1 50 ? 11.990  -34.744 21.674  1.00 33.06  ? 49  GLU C N   1 
ATOM   1799 C CA  . GLU C 1 50 ? 12.609  -35.832 22.417  1.00 34.54  ? 49  GLU C CA  1 
ATOM   1800 C C   . GLU C 1 50 ? 13.707  -35.309 23.345  1.00 33.96  ? 49  GLU C C   1 
ATOM   1801 O O   . GLU C 1 50 ? 14.110  -34.151 23.281  1.00 34.20  ? 49  GLU C O   1 
ATOM   1802 C CB  . GLU C 1 50 ? 13.107  -36.873 21.425  1.00 34.82  ? 49  GLU C CB  1 
ATOM   1803 C CG  . GLU C 1 50 ? 11.952  -37.453 20.617  1.00 40.08  ? 49  GLU C CG  1 
ATOM   1804 C CD  . GLU C 1 50 ? 12.441  -38.411 19.563  1.00 49.60  ? 49  GLU C CD  1 
ATOM   1805 O OE1 . GLU C 1 50 ? 13.668  -38.627 19.476  1.00 53.80  ? 49  GLU C OE1 1 
ATOM   1806 O OE2 . GLU C 1 50 ? 11.585  -38.909 18.814  1.00 58.48  ? 49  GLU C OE2 1 
ATOM   1807 N N   . THR C 1 51 ? 14.171  -36.182 24.259  1.00 35.91  ? 50  THR C N   1 
ATOM   1808 C CA  . THR C 1 51 ? 15.246  -35.799 25.173  1.00 34.25  ? 50  THR C CA  1 
ATOM   1809 C C   . THR C 1 51 ? 16.405  -36.788 25.105  1.00 28.97  ? 50  THR C C   1 
ATOM   1810 O O   . THR C 1 51 ? 16.256  -37.929 24.673  1.00 32.64  ? 50  THR C O   1 
ATOM   1811 C CB  . THR C 1 51 ? 14.744  -35.661 26.606  1.00 35.68  ? 50  THR C CB  1 
ATOM   1812 O OG1 . THR C 1 51 ? 14.176  -36.937 26.905  1.00 38.32  ? 50  THR C OG1 1 
ATOM   1813 C CG2 . THR C 1 51 ? 13.761  -34.520 26.805  1.00 37.92  ? 50  THR C CG2 1 
ATOM   1814 N N   . ALA C 1 52 ? 17.592  -36.293 25.468  1.00 32.93  ? 51  ALA C N   1 
ATOM   1815 C CA  . ALA C 1 52 ? 18.782  -37.124 25.586  1.00 30.96  ? 51  ALA C CA  1 
ATOM   1816 C C   . ALA C 1 52 ? 19.766  -36.458 26.548  1.00 31.49  ? 51  ALA C C   1 
ATOM   1817 O O   . ALA C 1 52 ? 19.573  -35.323 26.985  1.00 35.60  ? 51  ALA C O   1 
ATOM   1818 C CB  . ALA C 1 52 ? 19.408  -37.373 24.246  1.00 31.33  ? 51  ALA C CB  1 
ATOM   1819 N N   . PHE C 1 53 ? 20.834  -37.183 26.914  1.00 31.74  ? 52  PHE C N   1 
ATOM   1820 C CA  . PHE C 1 53 ? 21.924  -36.568 27.672  1.00 30.64  ? 52  PHE C CA  1 
ATOM   1821 C C   . PHE C 1 53 ? 23.129  -36.441 26.752  1.00 31.73  ? 52  PHE C C   1 
ATOM   1822 O O   . PHE C 1 53 ? 23.493  -37.404 26.079  1.00 32.77  ? 52  PHE C O   1 
ATOM   1823 C CB  . PHE C 1 53 ? 22.388  -37.433 28.860  1.00 33.97  ? 52  PHE C CB  1 
ATOM   1824 C CG  . PHE C 1 53 ? 21.382  -37.433 29.990  1.00 31.65  ? 52  PHE C CG  1 
ATOM   1825 C CD1 . PHE C 1 53 ? 21.120  -36.273 30.707  1.00 35.42  ? 52  PHE C CD1 1 
ATOM   1826 C CD2 . PHE C 1 53 ? 20.667  -38.585 30.303  1.00 45.83  ? 52  PHE C CD2 1 
ATOM   1827 C CE1 . PHE C 1 53 ? 20.171  -36.252 31.722  1.00 43.09  ? 52  PHE C CE1 1 
ATOM   1828 C CE2 . PHE C 1 53 ? 19.729  -38.563 31.335  1.00 48.41  ? 52  PHE C CE2 1 
ATOM   1829 C CZ  . PHE C 1 53 ? 19.475  -37.399 32.036  1.00 44.10  ? 52  PHE C CZ  1 
ATOM   1830 N N   . LEU C 1 54 ? 23.768  -35.267 26.744  1.00 26.81  ? 53  LEU C N   1 
ATOM   1831 C CA  . LEU C 1 54 ? 24.935  -35.054 25.897  1.00 26.13  ? 53  LEU C CA  1 
ATOM   1832 C C   . LEU C 1 54 ? 25.992  -34.267 26.658  1.00 27.14  ? 53  LEU C C   1 
ATOM   1833 O O   . LEU C 1 54 ? 25.654  -33.462 27.519  1.00 27.64  ? 53  LEU C O   1 
ATOM   1834 C CB  . LEU C 1 54 ? 24.555  -34.309 24.613  1.00 27.58  ? 53  LEU C CB  1 
ATOM   1835 C CG  . LEU C 1 54 ? 23.631  -35.046 23.635  1.00 29.00  ? 53  LEU C CG  1 
ATOM   1836 C CD1 . LEU C 1 54 ? 23.319  -34.126 22.504  1.00 30.18  ? 53  LEU C CD1 1 
ATOM   1837 C CD2 . LEU C 1 54 ? 24.344  -36.293 23.063  1.00 38.69  ? 53  LEU C CD2 1 
ATOM   1838 N N   . GLY C 1 55 ? 27.247  -34.522 26.310  1.00 30.60  ? 54  GLY C N   1 
ATOM   1839 C CA  . GLY C 1 55 ? 28.375  -33.772 26.843  1.00 30.79  ? 54  GLY C CA  1 
ATOM   1840 C C   . GLY C 1 55 ? 28.608  -32.443 26.124  1.00 35.67  ? 54  GLY C C   1 
ATOM   1841 O O   . GLY C 1 55 ? 28.098  -32.183 25.018  1.00 30.96  ? 54  GLY C O   1 
ATOM   1842 N N   . PRO C 1 56 ? 29.356  -31.520 26.770  1.00 35.20  ? 55  PRO C N   1 
ATOM   1843 C CA  . PRO C 1 56 ? 29.472  -30.144 26.294  1.00 35.56  ? 55  PRO C CA  1 
ATOM   1844 C C   . PRO C 1 56 ? 30.100  -30.046 24.909  1.00 36.57  ? 55  PRO C C   1 
ATOM   1845 O O   . PRO C 1 56 ? 29.853  -29.085 24.180  1.00 43.78  ? 55  PRO C O   1 
ATOM   1846 C CB  . PRO C 1 56 ? 30.327  -29.436 27.409  1.00 41.02  ? 55  PRO C CB  1 
ATOM   1847 C CG  . PRO C 1 56 ? 31.068  -30.581 28.062  1.00 39.68  ? 55  PRO C CG  1 
ATOM   1848 C CD  . PRO C 1 56 ? 30.097  -31.752 28.032  1.00 37.00  ? 55  PRO C CD  1 
ATOM   1849 N N   . LYS C 1 57 ? 30.881  -31.058 24.548  1.00 35.95  ? 56  LYS C N   1 
ATOM   1850 C CA  . LYS C 1 57 ? 31.559  -31.123 23.267  1.00 36.47  ? 56  LYS C CA  1 
ATOM   1851 C C   . LYS C 1 57 ? 30.531  -31.197 22.139  1.00 38.11  ? 56  LYS C C   1 
ATOM   1852 O O   . LYS C 1 57 ? 30.847  -30.887 20.992  1.00 37.05  ? 56  LYS C O   1 
ATOM   1853 C CB  . LYS C 1 57 ? 32.377  -32.417 23.167  1.00 41.36  ? 56  LYS C CB  1 
ATOM   1854 N N   . ASP C 1 58 ? 29.330  -31.680 22.481  1.00 33.41  ? 57  ASP C N   1 
ATOM   1855 C CA  . ASP C 1 58 ? 28.293  -31.955 21.490  1.00 34.33  ? 57  ASP C CA  1 
ATOM   1856 C C   . ASP C 1 58 ? 27.327  -30.786 21.331  1.00 34.63  ? 57  ASP C C   1 
ATOM   1857 O O   . ASP C 1 58 ? 26.326  -30.916 20.612  1.00 30.34  ? 57  ASP C O   1 
ATOM   1858 C CB  . ASP C 1 58 ? 27.471  -33.154 21.918  1.00 34.05  ? 57  ASP C CB  1 
ATOM   1859 C CG  . ASP C 1 58 ? 28.241  -34.459 21.984  1.00 39.79  ? 57  ASP C CG  1 
ATOM   1860 O OD1 . ASP C 1 58 ? 29.276  -34.528 21.321  1.00 38.05  ? 57  ASP C OD1 1 
ATOM   1861 O OD2 . ASP C 1 58 ? 27.774  -35.391 22.675  1.00 43.12  ? 57  ASP C OD2 1 
ATOM   1862 N N   . LEU C 1 59 ? 27.591  -29.664 22.008  1.00 27.18  ? 58  LEU C N   1 
ATOM   1863 C CA  . LEU C 1 59 ? 26.645  -28.567 22.115  1.00 32.59  ? 58  LEU C CA  1 
ATOM   1864 C C   . LEU C 1 59 ? 27.275  -27.290 21.584  1.00 33.00  ? 58  LEU C C   1 
ATOM   1865 O O   . LEU C 1 59 ? 28.437  -27.024 21.892  1.00 37.14  ? 58  LEU C O   1 
ATOM   1866 C CB  . LEU C 1 59 ? 26.250  -28.369 23.576  1.00 30.50  ? 58  LEU C CB  1 
ATOM   1867 C CG  . LEU C 1 59 ? 25.729  -29.622 24.262  1.00 29.68  ? 58  LEU C CG  1 
ATOM   1868 C CD1 . LEU C 1 59 ? 25.487  -29.300 25.730  1.00 31.11  ? 58  LEU C CD1 1 
ATOM   1869 C CD2 . LEU C 1 59 ? 24.412  -30.105 23.595  1.00 25.33  ? 58  LEU C CD2 1 
ATOM   1870 N N   . PHE C 1 60 ? 26.478  -26.521 20.837  1.00 32.32  ? 59  PHE C N   1 
ATOM   1871 C CA  . PHE C 1 60 ? 26.931  -25.283 20.206  1.00 32.61  ? 59  PHE C CA  1 
ATOM   1872 C C   . PHE C 1 60 ? 25.941  -24.163 20.495  1.00 34.98  ? 59  PHE C C   1 
ATOM   1873 O O   . PHE C 1 60 ? 24.771  -24.306 20.206  1.00 34.04  ? 59  PHE C O   1 
ATOM   1874 C CB  . PHE C 1 60 ? 27.085  -25.563 18.703  1.00 29.36  ? 59  PHE C CB  1 
ATOM   1875 C CG  . PHE C 1 60 ? 28.080  -26.685 18.418  1.00 30.60  ? 59  PHE C CG  1 
ATOM   1876 C CD1 . PHE C 1 60 ? 27.674  -28.016 18.399  1.00 28.19  ? 59  PHE C CD1 1 
ATOM   1877 C CD2 . PHE C 1 60 ? 29.430  -26.418 18.193  1.00 37.23  ? 59  PHE C CD2 1 
ATOM   1878 C CE1 . PHE C 1 60 ? 28.567  -29.060 18.215  1.00 29.68  ? 59  PHE C CE1 1 
ATOM   1879 C CE2 . PHE C 1 60 ? 30.313  -27.462 17.949  1.00 35.65  ? 59  PHE C CE2 1 
ATOM   1880 C CZ  . PHE C 1 60 ? 29.887  -28.774 17.966  1.00 35.94  ? 59  PHE C CZ  1 
ATOM   1881 N N   . PRO C 1 61 ? 26.307  -22.999 21.104  1.00 35.16  ? 60  PRO C N   1 
ATOM   1882 C CA  . PRO C 1 61 ? 25.296  -21.982 21.412  1.00 35.71  ? 60  PRO C CA  1 
ATOM   1883 C C   . PRO C 1 61 ? 24.634  -21.488 20.130  1.00 33.59  ? 60  PRO C C   1 
ATOM   1884 O O   . PRO C 1 61 ? 25.302  -21.342 19.113  1.00 37.66  ? 60  PRO C O   1 
ATOM   1885 C CB  . PRO C 1 61 ? 26.005  -20.838 22.177  1.00 38.41  ? 60  PRO C CB  1 
ATOM   1886 C CG  . PRO C 1 61 ? 27.446  -21.305 22.307  1.00 40.33  ? 60  PRO C CG  1 
ATOM   1887 C CD  . PRO C 1 61 ? 27.662  -22.614 21.544  1.00 45.07  ? 60  PRO C CD  1 
ATOM   1888 N N   . TYR C 1 62 ? 23.299  -21.336 20.213  1.00 34.31  ? 61  TYR C N   1 
ATOM   1889 C CA  . TYR C 1 62 ? 22.400  -21.076 19.102  1.00 34.37  ? 61  TYR C CA  1 
ATOM   1890 C C   . TYR C 1 62 ? 22.820  -19.805 18.360  1.00 38.21  ? 61  TYR C C   1 
ATOM   1891 O O   . TYR C 1 62 ? 22.902  -19.803 17.136  1.00 37.45  ? 61  TYR C O   1 
ATOM   1892 C CB  . TYR C 1 62 ? 20.947  -20.994 19.573  1.00 37.79  ? 61  TYR C CB  1 
ATOM   1893 C CG  . TYR C 1 62 ? 20.012  -20.623 18.435  1.00 39.04  ? 61  TYR C CG  1 
ATOM   1894 C CD1 . TYR C 1 62 ? 19.867  -21.468 17.329  1.00 39.41  ? 61  TYR C CD1 1 
ATOM   1895 C CD2 . TYR C 1 62 ? 19.273  -19.442 18.477  1.00 42.17  ? 61  TYR C CD2 1 
ATOM   1896 C CE1 . TYR C 1 62 ? 19.036  -21.115 16.272  1.00 35.90  ? 61  TYR C CE1 1 
ATOM   1897 C CE2 . TYR C 1 62 ? 18.420  -19.096 17.442  1.00 42.29  ? 61  TYR C CE2 1 
ATOM   1898 C CZ  . TYR C 1 62 ? 18.308  -19.935 16.343  1.00 39.57  ? 61  TYR C CZ  1 
ATOM   1899 O OH  . TYR C 1 62 ? 17.492  -19.567 15.320  1.00 39.79  ? 61  TYR C OH  1 
ATOM   1900 N N   . ASP C 1 63 ? 23.132  -18.740 19.102  1.00 43.33  ? 62  ASP C N   1 
ATOM   1901 C CA  . ASP C 1 63 ? 23.410  -17.480 18.427  1.00 46.18  ? 62  ASP C CA  1 
ATOM   1902 C C   . ASP C 1 63 ? 24.704  -17.559 17.638  1.00 42.69  ? 62  ASP C C   1 
ATOM   1903 O O   . ASP C 1 63 ? 24.769  -17.062 16.515  1.00 46.14  ? 62  ASP C O   1 
ATOM   1904 C CB  . ASP C 1 63 ? 23.336  -16.282 19.353  1.00 51.06  ? 62  ASP C CB  1 
ATOM   1905 C CG  . ASP C 1 63 ? 22.005  -15.562 19.254  1.00 68.71  ? 62  ASP C CG  1 
ATOM   1906 O OD1 . ASP C 1 63 ? 21.234  -15.632 20.236  1.00 68.14  ? 62  ASP C OD1 1 
ATOM   1907 O OD2 . ASP C 1 63 ? 21.743  -14.975 18.171  1.00 75.65  ? 62  ASP C OD2 1 
ATOM   1908 N N   . LYS C 1 64 ? 25.712  -18.185 18.240  1.00 38.01  ? 63  LYS C N   1 
ATOM   1909 C CA  . LYS C 1 64 ? 27.036  -18.265 17.661  1.00 36.32  ? 63  LYS C CA  1 
ATOM   1910 C C   . LYS C 1 64 ? 27.038  -19.172 16.435  1.00 39.16  ? 63  LYS C C   1 
ATOM   1911 O O   . LYS C 1 64 ? 27.833  -18.967 15.531  1.00 39.84  ? 63  LYS C O   1 
ATOM   1912 C CB  . LYS C 1 64 ? 28.082  -18.733 18.685  1.00 43.69  ? 63  LYS C CB  1 
ATOM   1913 N N   . SER C 1 65 ? 26.145  -20.184 16.388  1.00 35.11  ? 64  SER C N   1 
ATOM   1914 C CA  . SER C 1 65 ? 26.367  -21.230 15.397  1.00 32.43  ? 64  SER C CA  1 
ATOM   1915 C C   . SER C 1 65 ? 25.234  -21.327 14.369  1.00 29.29  ? 64  SER C C   1 
ATOM   1916 O O   . SER C 1 65 ? 25.323  -22.163 13.470  1.00 30.35  ? 64  SER C O   1 
ATOM   1917 C CB  . SER C 1 65 ? 26.633  -22.603 16.034  1.00 35.82  ? 64  SER C CB  1 
ATOM   1918 O OG  . SER C 1 65 ? 25.466  -23.088 16.691  1.00 38.48  ? 64  SER C OG  1 
ATOM   1919 N N   . LYS C 1 66 ? 24.186  -20.511 14.518  1.00 30.42  ? 65  LYS C N   1 
ATOM   1920 C CA  . LYS C 1 66 ? 23.034  -20.696 13.642  1.00 32.01  ? 65  LYS C CA  1 
ATOM   1921 C C   . LYS C 1 66 ? 23.405  -20.405 12.191  1.00 32.30  ? 65  LYS C C   1 
ATOM   1922 O O   . LYS C 1 66 ? 22.816  -20.986 11.300  1.00 30.85  ? 65  LYS C O   1 
ATOM   1923 C CB  . LYS C 1 66 ? 21.791  -19.890 14.007  1.00 34.43  ? 65  LYS C CB  1 
ATOM   1924 C CG  . LYS C 1 66 ? 22.107  -18.404 14.118  1.00 31.12  ? 65  LYS C CG  1 
ATOM   1925 C CD  . LYS C 1 66 ? 20.850  -17.700 14.601  1.00 38.22  ? 65  LYS C CD  1 
ATOM   1926 C CE  . LYS C 1 66 ? 21.050  -16.239 14.755  1.00 41.03  ? 65  LYS C CE  1 
ATOM   1927 N NZ  . LYS C 1 66 ? 19.799  -15.815 15.375  1.00 45.94  ? 65  LYS C NZ  1 
ATOM   1928 N N   . ASP C 1 67 ? 24.360  -19.506 11.935  1.00 33.54  ? 66  ASP C N   1 
ATOM   1929 C CA  . ASP C 1 67 ? 24.770  -19.268 10.546  1.00 38.13  ? 66  ASP C CA  1 
ATOM   1930 C C   . ASP C 1 67 ? 25.226  -20.568 9.874   1.00 39.20  ? 66  ASP C C   1 
ATOM   1931 O O   . ASP C 1 67 ? 24.971  -20.787 8.692   1.00 39.84  ? 66  ASP C O   1 
ATOM   1932 C CB  . ASP C 1 67 ? 25.725  -18.077 10.386  1.00 36.65  ? 66  ASP C CB  1 
ATOM   1933 C CG  . ASP C 1 67 ? 27.151  -18.216 10.919  1.00 49.58  ? 66  ASP C CG  1 
ATOM   1934 O OD1 . ASP C 1 67 ? 27.471  -19.263 11.541  1.00 53.47  ? 66  ASP C OD1 1 
ATOM   1935 O OD2 . ASP C 1 67 ? 27.937  -17.239 10.759  1.00 48.97  ? 66  ASP C OD2 1 
ATOM   1936 N N   . LYS C 1 68 ? 25.864  -21.463 10.643  1.00 33.35  ? 67  LYS C N   1 
ATOM   1937 C CA  . LYS C 1 68 ? 26.371  -22.717 10.125  1.00 30.74  ? 67  LYS C CA  1 
ATOM   1938 C C   . LYS C 1 68 ? 25.359  -23.883 10.168  1.00 30.71  ? 67  LYS C C   1 
ATOM   1939 O O   . LYS C 1 68 ? 25.252  -24.644 9.214   1.00 32.65  ? 67  LYS C O   1 
ATOM   1940 C CB  . LYS C 1 68 ? 27.621  -23.045 10.934  1.00 35.83  ? 67  LYS C CB  1 
ATOM   1941 C CG  . LYS C 1 68 ? 28.321  -24.287 10.467  1.00 37.16  ? 67  LYS C CG  1 
ATOM   1942 C CD  . LYS C 1 68 ? 29.626  -24.359 11.271  1.00 50.52  ? 67  LYS C CD  1 
ATOM   1943 C CE  . LYS C 1 68 ? 30.282  -25.698 11.379  1.00 56.60  ? 67  LYS C CE  1 
ATOM   1944 N NZ  . LYS C 1 68 ? 30.624  -26.306 10.089  1.00 69.67  ? 67  LYS C NZ  1 
ATOM   1945 N N   . TYR C 1 69 ? 24.613  -24.034 11.272  1.00 29.34  ? 68  TYR C N   1 
ATOM   1946 C CA  . TYR C 1 69 ? 23.771  -25.221 11.408  1.00 25.27  ? 68  TYR C CA  1 
ATOM   1947 C C   . TYR C 1 69 ? 22.281  -24.897 11.209  1.00 28.64  ? 68  TYR C C   1 
ATOM   1948 O O   . TYR C 1 69 ? 21.471  -25.810 11.075  1.00 28.21  ? 68  TYR C O   1 
ATOM   1949 C CB  . TYR C 1 69 ? 23.929  -25.820 12.813  1.00 25.42  ? 68  TYR C CB  1 
ATOM   1950 C CG  . TYR C 1 69 ? 25.354  -26.265 13.119  1.00 24.98  ? 68  TYR C CG  1 
ATOM   1951 C CD1 . TYR C 1 69 ? 26.083  -27.050 12.238  1.00 26.81  ? 68  TYR C CD1 1 
ATOM   1952 C CD2 . TYR C 1 69 ? 25.962  -25.827 14.288  1.00 31.09  ? 68  TYR C CD2 1 
ATOM   1953 C CE1 . TYR C 1 69 ? 27.377  -27.466 12.536  1.00 30.64  ? 68  TYR C CE1 1 
ATOM   1954 C CE2 . TYR C 1 69 ? 27.244  -26.249 14.601  1.00 28.53  ? 68  TYR C CE2 1 
ATOM   1955 C CZ  . TYR C 1 69 ? 27.949  -27.046 13.723  1.00 30.79  ? 68  TYR C CZ  1 
ATOM   1956 O OH  . TYR C 1 69 ? 29.230  -27.383 14.114  1.00 35.76  ? 68  TYR C OH  1 
ATOM   1957 N N   . GLY C 1 70 ? 21.904  -23.617 11.250  1.00 27.23  ? 69  GLY C N   1 
ATOM   1958 C CA  . GLY C 1 70 ? 20.495  -23.250 11.151  1.00 28.55  ? 69  GLY C CA  1 
ATOM   1959 C C   . GLY C 1 70 ? 20.094  -23.115 9.689   1.00 27.36  ? 69  GLY C C   1 
ATOM   1960 O O   . GLY C 1 70 ? 19.984  -22.016 9.152   1.00 29.53  ? 69  GLY C O   1 
ATOM   1961 N N   . LYS C 1 71 ? 20.012  -24.266 9.042   1.00 26.39  ? 70  LYS C N   1 
ATOM   1962 C CA  . LYS C 1 71 ? 19.646  -24.347 7.631   1.00 29.29  ? 70  LYS C CA  1 
ATOM   1963 C C   . LYS C 1 71 ? 18.762  -25.572 7.498   1.00 29.46  ? 70  LYS C C   1 
ATOM   1964 O O   . LYS C 1 71 ? 18.943  -26.540 8.232   1.00 28.07  ? 70  LYS C O   1 
ATOM   1965 C CB  . LYS C 1 71 ? 20.883  -24.568 6.751   1.00 31.86  ? 70  LYS C CB  1 
ATOM   1966 C CG  . LYS C 1 71 ? 21.965  -25.479 7.321   1.00 36.27  ? 70  LYS C CG  1 
ATOM   1967 C CD  . LYS C 1 71 ? 23.058  -26.018 6.410   1.00 45.57  ? 70  LYS C CD  1 
ATOM   1968 C CE  . LYS C 1 71 ? 23.940  -26.929 7.216   1.00 49.45  ? 70  LYS C CE  1 
ATOM   1969 N N   . PRO C 1 72 ? 17.773  -25.600 6.585   1.00 24.75  ? 71  PRO C N   1 
ATOM   1970 C CA  . PRO C 1 72 ? 16.843  -26.716 6.562   1.00 24.28  ? 71  PRO C CA  1 
ATOM   1971 C C   . PRO C 1 72 ? 17.484  -28.052 6.247   1.00 27.47  ? 71  PRO C C   1 
ATOM   1972 O O   . PRO C 1 72 ? 18.484  -28.116 5.520   1.00 29.73  ? 71  PRO C O   1 
ATOM   1973 C CB  . PRO C 1 72 ? 15.863  -26.311 5.439   1.00 26.66  ? 71  PRO C CB  1 
ATOM   1974 C CG  . PRO C 1 72 ? 15.910  -24.806 5.526   1.00 28.79  ? 71  PRO C CG  1 
ATOM   1975 C CD  . PRO C 1 72 ? 17.394  -24.492 5.684   1.00 25.01  ? 71  PRO C CD  1 
ATOM   1976 N N   . ASN C 1 73 ? 16.764  -29.087 6.658   1.00 28.20  ? 72  ASN C N   1 
ATOM   1977 C CA  . ASN C 1 73 ? 17.055  -30.348 6.010   1.00 35.65  ? 72  ASN C CA  1 
ATOM   1978 C C   . ASN C 1 73 ? 15.853  -31.250 6.184   1.00 27.37  ? 72  ASN C C   1 
ATOM   1979 O O   . ASN C 1 73 ? 14.899  -30.928 6.889   1.00 29.18  ? 72  ASN C O   1 
ATOM   1980 C CB  . ASN C 1 73 ? 18.394  -30.963 6.400   1.00 38.47  ? 72  ASN C CB  1 
ATOM   1981 C CG  . ASN C 1 73 ? 18.322  -31.529 7.795   1.00 35.41  ? 72  ASN C CG  1 
ATOM   1982 O OD1 . ASN C 1 73 ? 17.613  -32.515 8.030   1.00 37.17  ? 72  ASN C OD1 1 
ATOM   1983 N ND2 . ASN C 1 73 ? 19.076  -30.945 8.705   1.00 42.14  ? 72  ASN C ND2 1 
ATOM   1984 N N   . LYS C 1 74 ? 15.932  -32.402 5.537   1.00 29.35  ? 73  LYS C N   1 
ATOM   1985 C CA  . LYS C 1 74 ? 14.704  -33.159 5.335   1.00 25.97  ? 73  LYS C CA  1 
ATOM   1986 C C   . LYS C 1 74 ? 14.470  -34.180 6.445   1.00 30.16  ? 73  LYS C C   1 
ATOM   1987 O O   . LYS C 1 74 ? 13.471  -34.905 6.419   1.00 33.39  ? 73  LYS C O   1 
ATOM   1988 C CB  . LYS C 1 74 ? 14.708  -33.898 3.983   1.00 31.11  ? 73  LYS C CB  1 
ATOM   1989 N N   . ARG C 1 75 ? 15.345  -34.227 7.465   1.00 25.58  ? 74  ARG C N   1 
ATOM   1990 C CA  . ARG C 1 75 ? 15.147  -35.160 8.561   1.00 24.05  ? 74  ARG C CA  1 
ATOM   1991 C C   . ARG C 1 75 ? 13.850  -34.861 9.323   1.00 25.79  ? 74  ARG C C   1 
ATOM   1992 O O   . ARG C 1 75 ? 13.453  -33.699 9.550   1.00 27.66  ? 74  ARG C O   1 
ATOM   1993 C CB  . ARG C 1 75 ? 16.401  -35.257 9.480   1.00 26.80  ? 74  ARG C CB  1 
ATOM   1994 C CG  . ARG C 1 75 ? 17.780  -35.494 8.857   1.00 33.92  ? 74  ARG C CG  1 
ATOM   1995 C CD  . ARG C 1 75 ? 18.051  -36.873 8.225   1.00 36.66  ? 74  ARG C CD  1 
ATOM   1996 N NE  . ARG C 1 75 ? 18.019  -37.837 9.321   1.00 32.13  ? 74  ARG C NE  1 
ATOM   1997 C CZ  . ARG C 1 75 ? 19.171  -38.248 9.901   1.00 31.22  ? 74  ARG C CZ  1 
ATOM   1998 N NH1 . ARG C 1 75 ? 19.062  -38.809 11.071  1.00 36.87  ? 74  ARG C NH1 1 
ATOM   1999 N NH2 . ARG C 1 75 ? 20.354  -37.935 9.357   1.00 31.74  ? 74  ARG C NH2 1 
ATOM   2000 N N   . LYS C 1 76 ? 13.200  -35.948 9.760   1.00 32.24  ? 75  LYS C N   1 
ATOM   2001 C CA  . LYS C 1 76 ? 11.921  -35.889 10.443  1.00 30.62  ? 75  LYS C CA  1 
ATOM   2002 C C   . LYS C 1 76 ? 11.955  -34.893 11.603  1.00 29.57  ? 75  LYS C C   1 
ATOM   2003 O O   . LYS C 1 76 ? 12.738  -35.014 12.550  1.00 28.27  ? 75  LYS C O   1 
ATOM   2004 C CB  . LYS C 1 76 ? 11.359  -37.255 10.865  1.00 33.42  ? 75  LYS C CB  1 
ATOM   2005 C CG  . LYS C 1 76 ? 9.862   -37.159 11.169  1.00 40.75  ? 75  LYS C CG  1 
ATOM   2006 C CD  . LYS C 1 76 ? 9.170   -38.234 12.014  1.00 48.03  ? 75  LYS C CD  1 
ATOM   2007 N N   . GLY C 1 77 ? 11.099  -33.861 11.514  1.00 30.23  ? 76  GLY C N   1 
ATOM   2008 C CA  . GLY C 1 77 ? 10.883  -32.946 12.630  1.00 24.97  ? 76  GLY C CA  1 
ATOM   2009 C C   . GLY C 1 77 ? 11.882  -31.764 12.614  1.00 24.70  ? 76  GLY C C   1 
ATOM   2010 O O   . GLY C 1 77 ? 11.735  -30.840 13.398  1.00 27.11  ? 76  GLY C O   1 
ATOM   2011 N N   . PHE C 1 78 ? 12.873  -31.772 11.717  1.00 25.52  ? 77  PHE C N   1 
ATOM   2012 C CA  . PHE C 1 78 ? 13.970  -30.816 11.770  1.00 24.20  ? 77  PHE C CA  1 
ATOM   2013 C C   . PHE C 1 78 ? 13.448  -29.385 11.540  1.00 25.06  ? 77  PHE C C   1 
ATOM   2014 O O   . PHE C 1 78 ? 13.813  -28.423 12.228  1.00 23.66  ? 77  PHE C O   1 
ATOM   2015 C CB  . PHE C 1 78 ? 15.087  -31.191 10.783  1.00 27.81  ? 77  PHE C CB  1 
ATOM   2016 C CG  . PHE C 1 78 ? 16.368  -30.413 11.053  1.00 24.01  ? 77  PHE C CG  1 
ATOM   2017 C CD1 . PHE C 1 78 ? 16.548  -29.146 10.520  1.00 25.73  ? 77  PHE C CD1 1 
ATOM   2018 C CD2 . PHE C 1 78 ? 17.372  -30.944 11.848  1.00 23.25  ? 77  PHE C CD2 1 
ATOM   2019 C CE1 . PHE C 1 78 ? 17.725  -28.454 10.731  1.00 25.11  ? 77  PHE C CE1 1 
ATOM   2020 C CE2 . PHE C 1 78 ? 18.537  -30.225 12.096  1.00 23.04  ? 77  PHE C CE2 1 
ATOM   2021 C CZ  . PHE C 1 78 ? 18.697  -28.981 11.561  1.00 23.08  ? 77  PHE C CZ  1 
ATOM   2022 N N   . ASN C 1 79 ? 12.702  -29.232 10.447  1.00 26.14  ? 78  ASN C N   1 
ATOM   2023 C CA  . ASN C 1 79 ? 12.364  -27.886 10.024  1.00 28.42  ? 78  ASN C CA  1 
ATOM   2024 C C   . ASN C 1 79 ? 11.356  -27.273 10.986  1.00 27.15  ? 78  ASN C C   1 
ATOM   2025 O O   . ASN C 1 79 ? 11.403  -26.066 11.286  1.00 24.61  ? 78  ASN C O   1 
ATOM   2026 C CB  . ASN C 1 79 ? 11.896  -27.903 8.576   1.00 24.61  ? 78  ASN C CB  1 
ATOM   2027 C CG  . ASN C 1 79 ? 13.017  -28.249 7.629   1.00 25.08  ? 78  ASN C CG  1 
ATOM   2028 O OD1 . ASN C 1 79 ? 14.172  -27.927 7.929   1.00 25.46  ? 78  ASN C OD1 1 
ATOM   2029 N ND2 . ASN C 1 79 ? 12.692  -28.768 6.451   1.00 26.33  ? 78  ASN C ND2 1 
ATOM   2030 N N   . GLU C 1 80 ? 10.467  -28.106 11.514  1.00 27.62  ? 79  GLU C N   1 
ATOM   2031 C CA  . GLU C 1 80 ? 9.603   -27.605 12.574  1.00 26.35  ? 79  GLU C CA  1 
ATOM   2032 C C   . GLU C 1 80 ? 10.444  -27.192 13.778  1.00 29.50  ? 79  GLU C C   1 
ATOM   2033 O O   . GLU C 1 80 ? 10.174  -26.186 14.445  1.00 28.35  ? 79  GLU C O   1 
ATOM   2034 C CB  . GLU C 1 80 ? 8.567   -28.678 12.916  1.00 32.26  ? 79  GLU C CB  1 
ATOM   2035 C CG  . GLU C 1 80 ? 7.595   -28.201 13.986  1.00 31.68  ? 79  GLU C CG  1 
ATOM   2036 C CD  . GLU C 1 80 ? 6.395   -29.090 14.181  1.00 45.44  ? 79  GLU C CD  1 
ATOM   2037 O OE1 . GLU C 1 80 ? 6.470   -30.269 13.758  1.00 46.70  ? 79  GLU C OE1 1 
ATOM   2038 O OE2 . GLU C 1 80 ? 5.376   -28.588 14.730  1.00 42.01  ? 79  GLU C OE2 1 
ATOM   2039 N N   . GLY C 1 81 ? 11.524  -27.969 14.059  1.00 25.09  ? 80  GLY C N   1 
ATOM   2040 C CA  . GLY C 1 81 ? 12.399  -27.545 15.138  1.00 26.66  ? 80  GLY C CA  1 
ATOM   2041 C C   . GLY C 1 81 ? 13.044  -26.181 14.905  1.00 25.62  ? 80  GLY C C   1 
ATOM   2042 O O   . GLY C 1 81 ? 13.234  -25.416 15.842  1.00 24.75  ? 80  GLY C O   1 
ATOM   2043 N N   . LEU C 1 82 ? 13.491  -25.937 13.664  1.00 26.24  ? 81  LEU C N   1 
ATOM   2044 C CA  . LEU C 1 82 ? 14.045  -24.630 13.314  1.00 24.81  ? 81  LEU C CA  1 
ATOM   2045 C C   . LEU C 1 82 ? 13.021  -23.524 13.560  1.00 23.44  ? 81  LEU C C   1 
ATOM   2046 O O   . LEU C 1 82 ? 13.420  -22.435 14.013  1.00 26.27  ? 81  LEU C O   1 
ATOM   2047 C CB  . LEU C 1 82 ? 14.483  -24.645 11.848  1.00 24.93  ? 81  LEU C CB  1 
ATOM   2048 C CG  . LEU C 1 82 ? 15.782  -25.387 11.501  1.00 25.28  ? 81  LEU C CG  1 
ATOM   2049 C CD1 . LEU C 1 82 ? 16.047  -25.264 10.006  1.00 27.43  ? 81  LEU C CD1 1 
ATOM   2050 C CD2 . LEU C 1 82 ? 17.023  -24.938 12.269  1.00 24.78  ? 81  LEU C CD2 1 
ATOM   2051 N N   . TRP C 1 83 ? 11.747  -23.821 13.262  1.00 23.17  ? 82  TRP C N   1 
ATOM   2052 C CA  . TRP C 1 83 ? 10.712  -22.795 13.495  1.00 27.34  ? 82  TRP C CA  1 
ATOM   2053 C C   . TRP C 1 83 ? 10.602  -22.524 15.001  1.00 30.56  ? 82  TRP C C   1 
ATOM   2054 O O   . TRP C 1 83 ? 10.680  -21.364 15.455  1.00 29.84  ? 82  TRP C O   1 
ATOM   2055 C CB  . TRP C 1 83 ? 9.362   -23.136 12.860  1.00 27.29  ? 82  TRP C CB  1 
ATOM   2056 C CG  . TRP C 1 83 ? 8.367   -22.010 13.041  1.00 30.55  ? 82  TRP C CG  1 
ATOM   2057 C CD1 . TRP C 1 83 ? 8.166   -20.966 12.177  1.00 32.91  ? 82  TRP C CD1 1 
ATOM   2058 C CD2 . TRP C 1 83 ? 7.480   -21.784 14.166  1.00 34.18  ? 82  TRP C CD2 1 
ATOM   2059 N NE1 . TRP C 1 83 ? 7.199   -20.129 12.662  1.00 33.20  ? 82  TRP C NE1 1 
ATOM   2060 C CE2 . TRP C 1 83 ? 6.762   -20.596 13.877  1.00 34.24  ? 82  TRP C CE2 1 
ATOM   2061 C CE3 . TRP C 1 83 ? 7.235   -22.468 15.370  1.00 31.81  ? 82  TRP C CE3 1 
ATOM   2062 C CZ2 . TRP C 1 83 ? 5.825   -20.083 14.772  1.00 40.85  ? 82  TRP C CZ2 1 
ATOM   2063 C CZ3 . TRP C 1 83 ? 6.316   -21.955 16.263  1.00 40.18  ? 82  TRP C CZ3 1 
ATOM   2064 C CH2 . TRP C 1 83 ? 5.627   -20.773 15.959  1.00 40.49  ? 82  TRP C CH2 1 
ATOM   2065 N N   . GLU C 1 84 ? 10.614  -23.617 15.785  1.00 26.79  ? 83  GLU C N   1 
ATOM   2066 C CA  . GLU C 1 84 ? 10.425  -23.482 17.229  1.00 31.46  ? 83  GLU C CA  1 
ATOM   2067 C C   . GLU C 1 84 ? 11.561  -22.715 17.917  1.00 30.17  ? 83  GLU C C   1 
ATOM   2068 O O   . GLU C 1 84 ? 11.313  -21.857 18.791  1.00 32.76  ? 83  GLU C O   1 
ATOM   2069 C CB  . GLU C 1 84 ? 10.286  -24.848 17.896  1.00 27.51  ? 83  GLU C CB  1 
ATOM   2070 C CG  . GLU C 1 84 ? 8.997   -25.553 17.503  1.00 33.01  ? 83  GLU C CG  1 
ATOM   2071 C CD  . GLU C 1 84 ? 8.967   -26.959 18.030  1.00 35.05  ? 83  GLU C CD  1 
ATOM   2072 O OE1 . GLU C 1 84 ? 9.960   -27.344 18.724  1.00 32.95  ? 83  GLU C OE1 1 
ATOM   2073 O OE2 . GLU C 1 84 ? 7.979   -27.650 17.697  1.00 35.08  ? 83  GLU C OE2 1 
ATOM   2074 N N   . ILE C 1 85 ? 12.821  -22.958 17.506  1.00 29.37  ? 84  ILE C N   1 
ATOM   2075 C CA  . ILE C 1 85 ? 13.981  -22.359 18.151  1.00 29.36  ? 84  ILE C CA  1 
ATOM   2076 C C   . ILE C 1 85 ? 14.078  -20.849 17.884  1.00 33.08  ? 84  ILE C C   1 
ATOM   2077 O O   . ILE C 1 85 ? 14.545  -20.102 18.730  1.00 31.20  ? 84  ILE C O   1 
ATOM   2078 C CB  . ILE C 1 85 ? 15.281  -23.101 17.812  1.00 27.95  ? 84  ILE C CB  1 
ATOM   2079 C CG1 . ILE C 1 85 ? 16.395  -22.698 18.808  1.00 26.55  ? 84  ILE C CG1 1 
ATOM   2080 C CG2 . ILE C 1 85 ? 15.736  -22.900 16.355  1.00 28.95  ? 84  ILE C CG2 1 
ATOM   2081 C CD1 . ILE C 1 85 ? 17.617  -23.609 18.890  1.00 30.11  ? 84  ILE C CD1 1 
ATOM   2082 N N   . GLN C 1 86 ? 13.633  -20.421 16.702  1.00 30.00  ? 85  GLN C N   1 
ATOM   2083 C CA  . GLN C 1 86 ? 13.650  -18.999 16.385  1.00 29.46  ? 85  GLN C CA  1 
ATOM   2084 C C   . GLN C 1 86 ? 12.382  -18.263 16.864  1.00 29.40  ? 85  GLN C C   1 
ATOM   2085 O O   . GLN C 1 86 ? 12.478  -17.079 17.209  1.00 36.30  ? 85  GLN C O   1 
ATOM   2086 C CB  . GLN C 1 86 ? 13.932  -18.910 14.877  1.00 30.31  ? 85  GLN C CB  1 
ATOM   2087 C CG  . GLN C 1 86 ? 13.956  -17.475 14.337  1.00 29.71  ? 85  GLN C CG  1 
ATOM   2088 C CD  . GLN C 1 86 ? 14.365  -17.426 12.874  1.00 29.45  ? 85  GLN C CD  1 
ATOM   2089 O OE1 . GLN C 1 86 ? 14.269  -18.414 12.119  1.00 30.95  ? 85  GLN C OE1 1 
ATOM   2090 N NE2 . GLN C 1 86 ? 14.916  -16.289 12.465  1.00 32.02  ? 85  GLN C NE2 1 
ATOM   2091 N N   . ASN C 1 87 ? 11.248  -18.941 16.944  1.00 30.59  ? 86  ASN C N   1 
ATOM   2092 C CA  . ASN C 1 87 ? 9.949   -18.275 17.070  1.00 35.43  ? 86  ASN C CA  1 
ATOM   2093 C C   . ASN C 1 87 ? 9.198   -18.641 18.360  1.00 42.54  ? 86  ASN C C   1 
ATOM   2094 O O   . ASN C 1 87 ? 8.206   -17.997 18.678  1.00 38.89  ? 86  ASN C O   1 
ATOM   2095 C CB  . ASN C 1 87 ? 9.046   -18.552 15.870  1.00 34.13  ? 86  ASN C CB  1 
ATOM   2096 C CG  . ASN C 1 87 ? 9.653   -17.968 14.615  1.00 35.66  ? 86  ASN C CG  1 
ATOM   2097 O OD1 . ASN C 1 87 ? 9.689   -16.740 14.489  1.00 35.59  ? 86  ASN C OD1 1 
ATOM   2098 N ND2 . ASN C 1 87 ? 10.137  -18.805 13.701  1.00 32.51  ? 86  ASN C ND2 1 
ATOM   2099 N N   . ASN C 1 88 ? 9.617   -19.681 19.097  1.00 41.17  ? 87  ASN C N   1 
ATOM   2100 C CA  . ASN C 1 88 ? 8.846   -20.113 20.267  1.00 37.31  ? 87  ASN C CA  1 
ATOM   2101 C C   . ASN C 1 88 ? 9.708   -21.016 21.146  1.00 37.49  ? 87  ASN C C   1 
ATOM   2102 O O   . ASN C 1 88 ? 9.279   -22.132 21.473  1.00 38.88  ? 87  ASN C O   1 
ATOM   2103 C CB  . ASN C 1 88 ? 7.622   -20.934 19.857  1.00 45.06  ? 87  ASN C CB  1 
ATOM   2104 C CG  . ASN C 1 88 ? 6.510   -20.977 20.886  1.00 48.66  ? 87  ASN C CG  1 
ATOM   2105 O OD1 . ASN C 1 88 ? 6.484   -20.183 21.831  1.00 49.30  ? 87  ASN C OD1 1 
ATOM   2106 N ND2 . ASN C 1 88 ? 5.566   -21.886 20.701  1.00 52.42  ? 87  ASN C ND2 1 
ATOM   2107 N N   . PRO C 1 89 ? 10.924  -20.569 21.524  1.00 35.05  ? 88  PRO C N   1 
ATOM   2108 C CA  . PRO C 1 89 ? 11.923  -21.451 22.128  1.00 37.33  ? 88  PRO C CA  1 
ATOM   2109 C C   . PRO C 1 89 ? 11.704  -21.858 23.575  1.00 42.69  ? 88  PRO C C   1 
ATOM   2110 O O   . PRO C 1 89 ? 12.451  -22.713 24.074  1.00 41.91  ? 88  PRO C O   1 
ATOM   2111 C CB  . PRO C 1 89 ? 13.233  -20.700 21.997  1.00 32.88  ? 88  PRO C CB  1 
ATOM   2112 C CG  . PRO C 1 89 ? 12.818  -19.241 21.997  1.00 38.18  ? 88  PRO C CG  1 
ATOM   2113 C CD  . PRO C 1 89 ? 11.463  -19.225 21.285  1.00 38.28  ? 88  PRO C CD  1 
ATOM   2114 N N   . HIS C 1 90 ? 10.725  -21.204 24.225  1.00 44.13  ? 89  HIS C N   1 
ATOM   2115 C CA  . HIS C 1 90 ? 10.432  -21.498 25.620  1.00 43.82  ? 89  HIS C CA  1 
ATOM   2116 C C   . HIS C 1 90 ? 8.979   -21.934 25.823  1.00 47.04  ? 89  HIS C C   1 
ATOM   2117 O O   . HIS C 1 90 ? 8.476   -21.916 26.943  1.00 52.04  ? 89  HIS C O   1 
ATOM   2118 C CB  . HIS C 1 90 ? 10.976  -20.397 26.534  1.00 39.00  ? 89  HIS C CB  1 
ATOM   2119 C CG  . HIS C 1 90 ? 12.419  -20.031 26.330  1.00 39.75  ? 89  HIS C CG  1 
ATOM   2120 N ND1 . HIS C 1 90 ? 12.846  -18.805 25.859  1.00 42.98  ? 89  HIS C ND1 1 
ATOM   2121 C CD2 . HIS C 1 90 ? 13.540  -20.721 26.600  1.00 42.22  ? 89  HIS C CD2 1 
ATOM   2122 C CE1 . HIS C 1 90 ? 14.178  -18.766 25.828  1.00 40.08  ? 89  HIS C CE1 1 
ATOM   2123 N NE2 . HIS C 1 90 ? 14.619  -19.919 26.292  1.00 44.28  ? 89  HIS C NE2 1 
ATOM   2124 N N   . ALA C 1 91 ? 8.301   -22.362 24.756  1.00 51.08  ? 90  ALA C N   1 
ATOM   2125 C CA  . ALA C 1 91 ? 7.027   -23.042 24.930  1.00 55.25  ? 90  ALA C CA  1 
ATOM   2126 C C   . ALA C 1 91 ? 7.266   -24.416 25.561  1.00 63.90  ? 90  ALA C C   1 
ATOM   2127 O O   . ALA C 1 91 ? 8.413   -24.853 25.684  1.00 64.06  ? 90  ALA C O   1 
ATOM   2128 C CB  . ALA C 1 91 ? 6.262   -23.135 23.621  1.00 55.28  ? 90  ALA C CB  1 
ATOM   2129 N N   . SER C 1 92 ? 6.163   -25.096 25.913  1.00 65.90  ? 91  SER C N   1 
ATOM   2130 C CA  . SER C 1 92 ? 6.169   -26.296 26.740  1.00 67.81  ? 91  SER C CA  1 
ATOM   2131 C C   . SER C 1 92 ? 6.397   -27.567 25.925  1.00 69.80  ? 91  SER C C   1 
ATOM   2132 O O   . SER C 1 92 ? 7.161   -28.439 26.337  1.00 70.82  ? 91  SER C O   1 
ATOM   2133 C CB  . SER C 1 92 ? 4.887   -26.394 27.531  1.00 66.64  ? 91  SER C CB  1 
ATOM   2134 O OG  . SER C 1 92 ? 4.894   -25.442 28.583  1.00 70.85  ? 91  SER C OG  1 
ATOM   2135 N N   . TYR C 1 93 ? 5.673   -27.687 24.807  1.00 73.70  ? 92  TYR C N   1 
ATOM   2136 C CA  . TYR C 1 93 ? 5.703   -28.866 23.953  1.00 74.38  ? 92  TYR C CA  1 
ATOM   2137 C C   . TYR C 1 93 ? 5.482   -30.125 24.811  1.00 76.42  ? 92  TYR C C   1 
ATOM   2138 O O   . TYR C 1 93 ? 5.775   -31.240 24.323  1.00 80.18  ? 92  TYR C O   1 
ATOM   2139 C CB  . TYR C 1 93 ? 6.979   -28.878 23.099  1.00 72.68  ? 92  TYR C CB  1 
ATOM   2140 C CG  . TYR C 1 93 ? 7.207   -27.608 22.282  1.00 58.95  ? 92  TYR C CG  1 
ATOM   2141 C CD1 . TYR C 1 93 ? 6.423   -27.325 21.164  1.00 55.97  ? 92  TYR C CD1 1 
ATOM   2142 C CD2 . TYR C 1 93 ? 8.203   -26.698 22.629  1.00 52.85  ? 92  TYR C CD2 1 
ATOM   2143 C CE1 . TYR C 1 93 ? 6.610   -26.168 20.425  1.00 50.49  ? 92  TYR C CE1 1 
ATOM   2144 C CE2 . TYR C 1 93 ? 8.408   -25.543 21.889  1.00 46.78  ? 92  TYR C CE2 1 
ATOM   2145 C CZ  . TYR C 1 93 ? 7.615   -25.282 20.785  1.00 52.26  ? 92  TYR C CZ  1 
ATOM   2146 O OH  . TYR C 1 93 ? 7.827   -24.128 20.080  1.00 47.84  ? 92  TYR C OH  1 
HETATM 2147 S S   . SO4 D 2 .  ? 1.221   -33.775 1.788   1.00 80.74  ? 101 SO4 A S   1 
HETATM 2148 O O1  . SO4 D 2 .  ? 1.761   -34.367 0.587   1.00 67.77  ? 101 SO4 A O1  1 
HETATM 2149 O O2  . SO4 D 2 .  ? 1.335   -32.338 1.724   1.00 67.60  ? 101 SO4 A O2  1 
HETATM 2150 O O3  . SO4 D 2 .  ? -0.168  -34.142 1.919   1.00 86.35  ? 101 SO4 A O3  1 
HETATM 2151 O O4  . SO4 D 2 .  ? 1.948   -34.254 2.931   1.00 77.76  ? 101 SO4 A O4  1 
HETATM 2152 S S   . SO4 E 2 .  ? -9.654  -24.777 1.319   1.00 102.54 ? 102 SO4 A S   1 
HETATM 2153 O O1  . SO4 E 2 .  ? -9.506  -24.583 -0.099  1.00 95.23  ? 102 SO4 A O1  1 
HETATM 2154 O O2  . SO4 E 2 .  ? -9.544  -23.508 1.992   1.00 92.76  ? 102 SO4 A O2  1 
HETATM 2155 O O3  . SO4 E 2 .  ? -10.946 -25.359 1.587   1.00 110.42 ? 102 SO4 A O3  1 
HETATM 2156 O O4  . SO4 E 2 .  ? -8.621  -25.662 1.798   1.00 95.49  ? 102 SO4 A O4  1 
HETATM 2157 C C1  . EDO F 3 .  ? 13.822  -19.486 -7.324  1.00 34.95  ? 103 EDO A C1  1 
HETATM 2158 O O1  . EDO F 3 .  ? 15.056  -18.763 -7.244  1.00 29.61  ? 103 EDO A O1  1 
HETATM 2159 C C2  . EDO F 3 .  ? 12.909  -19.069 -8.462  1.00 31.49  ? 103 EDO A C2  1 
HETATM 2160 O O2  . EDO F 3 .  ? 12.463  -17.730 -8.376  1.00 29.08  ? 103 EDO A O2  1 
HETATM 2161 S S   . SO4 G 2 .  ? 8.928   -29.492 5.827   1.00 46.00  ? 104 SO4 A S   1 
HETATM 2162 O O1  . SO4 G 2 .  ? 9.663   -28.634 5.003   1.00 42.15  ? 104 SO4 A O1  1 
HETATM 2163 O O2  . SO4 G 2 .  ? 8.535   -30.649 5.017   1.00 52.19  ? 104 SO4 A O2  1 
HETATM 2164 O O3  . SO4 G 2 .  ? 9.730   -29.914 6.965   1.00 51.47  ? 104 SO4 A O3  1 
HETATM 2165 O O4  . SO4 G 2 .  ? 7.732   -28.850 6.298   1.00 55.60  ? 104 SO4 A O4  1 
HETATM 2166 C C10 . ZQD H 4 .  ? 19.890  -15.326 -24.860 0.68 30.58  ? 105 ZQD A C10 1 
HETATM 2167 C C15 . ZQD H 4 .  ? 16.753  -16.134 -25.577 0.68 33.53  ? 105 ZQD A C15 1 
HETATM 2168 C C01 . ZQD H 4 .  ? 17.793  -14.495 -18.447 0.68 42.74  ? 105 ZQD A C01 1 
HETATM 2169 C C02 . ZQD H 4 .  ? 18.356  -15.048 -19.708 0.68 45.10  ? 105 ZQD A C02 1 
HETATM 2170 C C03 . ZQD H 4 .  ? 17.827  -15.624 -20.794 0.68 42.44  ? 105 ZQD A C03 1 
HETATM 2171 C C04 . ZQD H 4 .  ? 18.935  -15.948 -21.614 0.68 38.50  ? 105 ZQD A C04 1 
HETATM 2172 N N05 . ZQD H 4 .  ? 20.058  -15.605 -21.061 0.68 41.53  ? 105 ZQD A N05 1 
HETATM 2173 O O06 . ZQD H 4 .  ? 19.697  -15.009 -19.823 0.68 44.57  ? 105 ZQD A O06 1 
HETATM 2174 C C07 . ZQD H 4 .  ? 18.781  -16.523 -23.004 0.68 36.94  ? 105 ZQD A C07 1 
HETATM 2175 C C08 . ZQD H 4 .  ? 19.967  -17.361 -23.501 0.68 34.33  ? 105 ZQD A C08 1 
HETATM 2176 C C09 . ZQD H 4 .  ? 20.803  -16.427 -24.365 0.68 33.20  ? 105 ZQD A C09 1 
HETATM 2177 N N11 . ZQD H 4 .  ? 18.734  -15.367 -23.929 0.68 34.70  ? 105 ZQD A N11 1 
HETATM 2178 S S12 . ZQD H 4 .  ? 17.313  -14.871 -24.501 0.68 32.53  ? 105 ZQD A S12 1 
HETATM 2179 O O13 . ZQD H 4 .  ? 17.566  -13.692 -25.264 0.68 27.75  ? 105 ZQD A O13 1 
HETATM 2180 O O14 . ZQD H 4 .  ? 16.419  -14.791 -23.389 0.68 33.39  ? 105 ZQD A O14 1 
HETATM 2181 S S   . SO4 I 2 .  ? 7.453   -8.527  -24.785 1.00 59.35  ? 101 SO4 B S   1 
HETATM 2182 O O1  . SO4 I 2 .  ? 8.555   -8.618  -25.712 1.00 37.08  ? 101 SO4 B O1  1 
HETATM 2183 O O2  . SO4 I 2 .  ? 6.234   -8.922  -25.443 1.00 50.88  ? 101 SO4 B O2  1 
HETATM 2184 O O3  . SO4 I 2 .  ? 7.634   -9.395  -23.606 1.00 39.64  ? 101 SO4 B O3  1 
HETATM 2185 O O4  . SO4 I 2 .  ? 7.398   -7.126  -24.410 1.00 52.84  ? 101 SO4 B O4  1 
HETATM 2186 S S   . SO4 J 2 .  ? 14.506  -27.029 -26.557 1.00 47.02  ? 102 SO4 B S   1 
HETATM 2187 O O1  . SO4 J 2 .  ? 15.858  -26.704 -26.229 1.00 51.69  ? 102 SO4 B O1  1 
HETATM 2188 O O2  . SO4 J 2 .  ? 14.477  -28.338 -27.159 1.00 59.05  ? 102 SO4 B O2  1 
HETATM 2189 O O3  . SO4 J 2 .  ? 13.726  -27.032 -25.352 1.00 55.41  ? 102 SO4 B O3  1 
HETATM 2190 O O4  . SO4 J 2 .  ? 13.948  -26.072 -27.474 1.00 48.57  ? 102 SO4 B O4  1 
HETATM 2191 C C1  . EDO K 3 .  ? 16.596  -36.273 16.322  1.00 29.93  ? 101 EDO C C1  1 
HETATM 2192 O O1  . EDO K 3 .  ? 15.555  -37.028 15.699  1.00 33.19  ? 101 EDO C O1  1 
HETATM 2193 C C2  . EDO K 3 .  ? 16.166  -35.325 17.420  1.00 28.36  ? 101 EDO C C2  1 
HETATM 2194 O O2  . EDO K 3 .  ? 15.313  -35.824 18.423  1.00 28.51  ? 101 EDO C O2  1 
HETATM 2195 S S   . SO4 L 2 .  ? 29.272  -38.268 12.391  1.00 91.40  ? 102 SO4 C S   1 
HETATM 2196 O O1  . SO4 L 2 .  ? 30.505  -37.714 11.886  1.00 95.55  ? 102 SO4 C O1  1 
HETATM 2197 O O2  . SO4 L 2 .  ? 28.188  -37.387 12.061  1.00 93.54  ? 102 SO4 C O2  1 
HETATM 2198 O O3  . SO4 L 2 .  ? 29.035  -39.557 11.801  1.00 82.24  ? 102 SO4 C O3  1 
HETATM 2199 O O4  . SO4 L 2 .  ? 29.356  -38.402 13.823  1.00 95.31  ? 102 SO4 C O4  1 
HETATM 2200 O O   . HOH M 5 .  ? 5.830   -28.869 6.859   1.00 43.81  ? 201 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? 8.811   -32.336 3.950   1.00 55.36  ? 202 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 3.806   -34.437 4.246   1.00 49.64  ? 203 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? -5.826  -13.660 -16.474 1.00 52.63  ? 204 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? -2.362  3.113   -1.983  1.00 39.35  ? 205 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? 10.886  -29.666 3.080   1.00 42.48  ? 206 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? -2.624  -30.585 -3.822  1.00 52.32  ? 207 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 7.051   -10.636 -12.094 1.00 37.89  ? 208 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 15.675  -24.476 2.055   1.00 38.44  ? 209 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 8.321   -17.836 -15.864 1.00 45.74  ? 210 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 4.418   -3.554  -3.273  1.00 30.98  ? 211 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 19.684  -15.610 7.292   1.00 26.96  ? 212 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? 9.486   -6.009  -1.689  1.00 32.61  ? 213 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 0.701   -24.834 13.726  1.00 48.48  ? 214 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 8.935   -18.234 -11.047 1.00 32.28  ? 215 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 9.355   -22.666 -9.511  1.00 32.74  ? 216 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? -3.857  -10.911 6.842   1.00 37.29  ? 217 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 4.566   -7.822  1.132   1.00 32.77  ? 218 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 0.506   -10.575 -15.751 1.00 45.15  ? 219 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -0.748  -29.371 9.932   1.00 49.53  ? 220 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 4.855   -1.493  -6.358  1.00 33.18  ? 221 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? -0.119  -33.677 4.612   1.00 48.75  ? 222 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 13.929  -15.616 -9.292  1.00 34.33  ? 223 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 3.203   -29.624 -0.499  1.00 35.71  ? 224 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? -4.314  -21.200 6.130   1.00 33.44  ? 225 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 11.065  -23.722 9.874   1.00 33.18  ? 226 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 11.362  -11.939 5.955   1.00 34.23  ? 227 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 13.008  -28.055 -4.800  1.00 42.76  ? 228 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 10.777  -5.098  -7.766  1.00 30.62  ? 229 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? -7.910  -17.357 6.634   1.00 42.58  ? 230 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 13.225  -11.968 -4.236  1.00 21.39  ? 231 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? -1.275  -11.721 11.302  1.00 33.22  ? 232 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 8.614   -2.085  -0.595  1.00 62.27  ? 233 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? -1.866  -22.017 -0.638  1.00 24.13  ? 234 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 12.821  -9.428  -7.230  1.00 43.68  ? 235 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 11.246  -5.952  -4.006  1.00 45.87  ? 236 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 17.101  -12.873 1.356   1.00 18.79  ? 237 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? -5.847  -15.865 -8.071  1.00 28.35  ? 238 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? -8.196  -15.707 -1.007  1.00 33.78  ? 239 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 1.787   0.627   -7.473  1.00 35.26  ? 240 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? -7.931  -16.710 1.694   1.00 36.22  ? 241 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 15.686  -12.074 -5.383  1.00 32.08  ? 242 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 1.746   -4.682  -10.226 1.00 34.72  ? 243 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? -6.279  -11.466 -11.395 1.00 39.79  ? 244 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 9.912   -13.053 9.673   1.00 37.19  ? 245 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 16.517  -11.789 -17.032 1.00 39.15  ? 246 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 6.395   -16.224 -15.028 1.00 45.51  ? 247 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? -8.655  -21.111 -1.179  1.00 38.37  ? 248 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? -0.766  -20.939 7.077   1.00 30.87  ? 249 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 11.550  -16.573 -14.799 1.00 38.27  ? 250 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? -11.239 -15.871 -3.744  1.00 49.40  ? 251 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? -1.315  -7.512  11.505  1.00 42.76  ? 252 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 8.307   -17.707 8.790   1.00 42.26  ? 253 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? -5.996  -19.749 -5.604  1.00 35.54  ? 254 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 2.462   -6.316  5.436   1.00 35.74  ? 255 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 12.536  -13.386 -8.552  1.00 37.28  ? 256 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 1.714   -10.424 11.720  1.00 33.03  ? 257 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 15.379  -28.030 -0.673  1.00 48.80  ? 258 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 5.073   -7.668  3.995   1.00 32.92  ? 259 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 2.222   -25.035 -6.488  1.00 50.68  ? 260 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? -6.403  -26.587 3.443   1.00 43.16  ? 261 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 1.676   -18.759 -18.659 1.00 35.73  ? 262 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? 11.484  -12.374 -6.201  1.00 25.87  ? 263 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? -4.573  -25.898 -5.637  1.00 38.98  ? 264 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? 7.868   -7.854  1.215   1.00 27.76  ? 265 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 8.811   -16.356 -13.237 1.00 36.61  ? 266 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 9.489   -30.433 9.868   1.00 32.06  ? 267 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 0.080   -23.391 9.019   1.00 41.66  ? 268 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 9.871   -27.610 -7.358  1.00 56.15  ? 269 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -7.497  -21.531 -5.939  1.00 42.11  ? 270 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 9.858   -20.406 -18.494 1.00 39.89  ? 271 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 14.496  -13.158 10.492  1.00 45.84  ? 272 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? -6.144  -12.757 6.808   1.00 35.89  ? 273 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? -7.302  -10.061 -7.740  1.00 40.59  ? 274 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 6.072   -5.868  0.486   1.00 44.67  ? 275 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 22.040  -16.609 -0.544  1.00 35.50  ? 276 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 12.931  -15.369 -12.119 1.00 49.84  ? 277 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? -7.329  -11.552 -8.026  1.00 26.90  ? 278 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 10.905  -7.846  0.353   1.00 24.23  ? 279 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? -0.431  -20.675 11.095  1.00 59.27  ? 280 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 3.007   -9.875  -13.309 1.00 42.20  ? 281 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? 21.365  -16.663 -3.484  1.00 26.76  ? 282 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? -8.091  -19.617 -3.469  1.00 46.33  ? 283 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? -3.895  -26.933 6.955   1.00 48.40  ? 284 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 17.021  -18.008 -9.833  1.00 46.00  ? 285 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -3.922  -7.912  10.675  1.00 41.25  ? 286 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? 1.114   -28.720 -7.293  1.00 52.02  ? 287 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 8.749   -9.131  -13.758 1.00 36.42  ? 288 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? -0.191  -8.223  -13.277 1.00 45.33  ? 289 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 16.802  -10.113 -9.700  1.00 42.34  ? 290 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? -5.870  -23.404 -7.075  1.00 39.42  ? 291 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? -7.390  -14.095 -9.222  1.00 37.04  ? 292 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? 4.815   -7.009  -10.987 1.00 46.19  ? 293 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? 7.437   -30.387 -2.917  1.00 52.62  ? 294 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? -10.563 -28.060 -1.795  1.00 63.76  ? 295 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? 12.660  -18.761 -12.168 1.00 51.29  ? 296 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 11.164  -2.100  -1.329  1.00 49.09  ? 297 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 7.957   -8.284  4.522   1.00 35.56  ? 298 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -6.254  -22.938 5.752   1.00 50.05  ? 299 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? -11.368 -13.502 -2.757  1.00 41.50  ? 300 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 4.569   -9.710  -11.425 1.00 43.09  ? 301 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? -6.968  -19.080 8.653   1.00 44.68  ? 302 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? 4.387   -3.340  2.073   1.00 61.53  ? 303 HOH A O   1 
HETATM 2303 O O   . HOH N 5 .  ? 10.239  -19.699 -43.241 1.00 45.70  ? 201 HOH B O   1 
HETATM 2304 O O   . HOH N 5 .  ? 30.838  -8.204  -30.087 1.00 50.73  ? 202 HOH B O   1 
HETATM 2305 O O   . HOH N 5 .  ? 10.151  -11.234 -38.085 1.00 42.54  ? 203 HOH B O   1 
HETATM 2306 O O   . HOH N 5 .  ? 30.036  -12.819 -45.800 1.00 66.96  ? 204 HOH B O   1 
HETATM 2307 O O   . HOH N 5 .  ? 13.110  -4.528  -41.692 1.00 53.64  ? 205 HOH B O   1 
HETATM 2308 O O   . HOH N 5 .  ? 27.854  -8.198  -28.902 1.00 45.28  ? 206 HOH B O   1 
HETATM 2309 O O   . HOH N 5 .  ? 6.244   -7.474  -32.163 1.00 50.11  ? 207 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 30.364  -19.680 -40.378 1.00 36.50  ? 208 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 26.080  -4.658  -33.584 1.00 40.82  ? 209 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 20.161  -21.947 -23.326 1.00 46.92  ? 210 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 25.116  -5.170  -29.928 1.00 33.83  ? 211 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 23.529  -11.282 -21.869 1.00 44.14  ? 212 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 34.898  -23.101 -30.223 1.00 60.59  ? 213 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 6.583   -12.325 -26.056 1.00 36.06  ? 214 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 26.121  -23.075 -31.274 1.00 34.53  ? 215 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 15.460  -17.386 -19.111 1.00 39.31  ? 216 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 32.604  -18.461 -42.390 1.00 52.03  ? 217 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 10.489  -16.761 -44.474 1.00 42.10  ? 218 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 25.471  -6.001  -35.929 1.00 40.23  ? 219 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 24.528  -1.707  -36.318 1.00 46.47  ? 220 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 20.839  -13.364 -42.777 1.00 37.47  ? 221 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 10.485  -18.911 -33.072 1.00 26.38  ? 222 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 21.140  -26.405 -30.293 1.00 54.77  ? 223 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 3.187   -8.848  -27.091 1.00 47.07  ? 224 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 16.805  -19.315 -28.879 1.00 22.79  ? 225 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 17.456  -19.555 -42.199 1.00 50.38  ? 226 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 27.857  -17.679 -25.036 1.00 39.14  ? 227 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 20.156  -2.763  -22.994 1.00 59.65  ? 228 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 18.261  -0.516  -38.441 1.00 26.21  ? 229 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 10.762  -21.828 -32.793 1.00 32.51  ? 230 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 18.303  -25.980 -29.005 1.00 38.73  ? 231 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 22.606  -23.261 -28.822 1.00 37.11  ? 232 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 23.539  -2.340  -29.119 1.00 34.15  ? 233 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 20.599  -9.949  -42.928 1.00 36.72  ? 234 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 23.804  -4.179  -36.826 1.00 28.36  ? 235 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 8.812   -8.670  -16.493 1.00 38.00  ? 236 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 14.416  -6.349  -41.209 1.00 39.29  ? 237 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 7.737   -18.535 -31.671 1.00 36.02  ? 238 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 19.788  -25.576 -34.237 1.00 37.61  ? 239 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 8.301   -27.991 -38.414 1.00 52.99  ? 240 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 21.259  -6.470  -42.530 1.00 34.80  ? 241 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 12.604  -22.734 -20.740 1.00 56.95  ? 242 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 7.713   -12.666 -38.931 1.00 51.31  ? 243 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 21.014  3.681   -32.740 1.00 32.42  ? 244 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 18.008  -15.771 -45.852 1.00 37.58  ? 245 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 17.803  -3.626  -22.104 1.00 49.61  ? 246 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 7.154   -19.060 -34.973 1.00 51.33  ? 247 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 7.356   -8.227  -20.895 1.00 44.36  ? 248 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 14.715  -24.407 -40.551 1.00 42.69  ? 249 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 31.909  -21.318 -38.327 1.00 46.19  ? 250 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 27.459  -10.767 -28.641 1.00 44.65  ? 251 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 1.701   -13.049 -28.455 1.00 46.17  ? 252 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 17.791  -0.512  -25.478 1.00 49.91  ? 253 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 18.138  4.604   -34.431 1.00 36.36  ? 254 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 24.853  -6.731  -42.737 1.00 45.14  ? 255 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 27.934  -24.837 -35.174 1.00 34.68  ? 256 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 17.096  -9.614  -43.997 1.00 40.11  ? 257 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 6.440   -20.664 -24.964 1.00 37.96  ? 258 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 39.125  -13.182 -39.699 1.00 73.56  ? 259 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 26.065  -0.401  -29.533 1.00 52.55  ? 260 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 7.572   -23.705 -24.303 1.00 50.36  ? 261 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 12.729  -20.392 -19.747 1.00 57.12  ? 262 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 17.186  -25.316 -20.907 1.00 59.32  ? 263 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 9.838   -6.117  -41.131 1.00 44.74  ? 264 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 15.069  -8.084  -42.977 1.00 46.09  ? 265 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 31.695  -11.907 -37.787 1.00 54.53  ? 266 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 11.524  -24.155 -29.835 1.00 38.04  ? 267 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 19.593  4.131   -33.565 1.00 47.55  ? 268 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 15.390  -21.880 -41.905 1.00 44.55  ? 269 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 7.697   -21.557 -29.912 1.00 39.52  ? 270 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 7.428   -9.877  -18.650 1.00 39.94  ? 271 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 22.587  -29.312 -35.676 1.00 40.66  ? 272 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 16.900  3.132   -26.576 1.00 61.45  ? 273 HOH B O   1 
HETATM 2376 O O   . HOH O 5 .  ? 26.864  -37.717 10.227  1.00 37.04  ? 201 HOH C O   1 
HETATM 2377 O O   . HOH O 5 .  ? 26.584  -38.993 12.770  1.00 35.34  ? 202 HOH C O   1 
HETATM 2378 O O   . HOH O 5 .  ? 19.778  -21.103 30.799  1.00 67.90  ? 203 HOH C O   1 
HETATM 2379 O O   . HOH O 5 .  ? 12.249  -28.258 28.102  1.00 51.68  ? 204 HOH C O   1 
HETATM 2380 O O   . HOH O 5 .  ? 9.233   -37.079 18.252  1.00 52.55  ? 205 HOH C O   1 
HETATM 2381 O O   . HOH O 5 .  ? 7.471   -31.766 11.959  1.00 49.14  ? 206 HOH C O   1 
HETATM 2382 O O   . HOH O 5 .  ? 15.065  -39.170 17.025  1.00 52.65  ? 207 HOH C O   1 
HETATM 2383 O O   . HOH O 5 .  ? 14.133  -37.190 13.548  1.00 38.01  ? 208 HOH C O   1 
HETATM 2384 O O   . HOH O 5 .  ? 17.574  -16.970 14.732  1.00 43.14  ? 209 HOH C O   1 
HETATM 2385 O O   . HOH O 5 .  ? 16.055  -37.837 20.092  1.00 45.94  ? 210 HOH C O   1 
HETATM 2386 O O   . HOH O 5 .  ? 23.081  -41.493 18.524  1.00 35.53  ? 211 HOH C O   1 
HETATM 2387 O O   . HOH O 5 .  ? 12.736  -31.546 8.204   1.00 28.77  ? 212 HOH C O   1 
HETATM 2388 O O   . HOH O 5 .  ? 19.898  -41.757 12.172  1.00 27.46  ? 213 HOH C O   1 
HETATM 2389 O O   . HOH O 5 .  ? 30.393  -17.328 9.838   1.00 50.94  ? 214 HOH C O   1 
HETATM 2390 O O   . HOH O 5 .  ? 25.367  -33.951 34.750  1.00 46.81  ? 215 HOH C O   1 
HETATM 2391 O O   . HOH O 5 .  ? 18.990  -20.015 10.547  1.00 36.60  ? 216 HOH C O   1 
HETATM 2392 O O   . HOH O 5 .  ? 5.565   -26.696 16.617  1.00 46.82  ? 217 HOH C O   1 
HETATM 2393 O O   . HOH O 5 .  ? 30.247  -30.987 15.788  1.00 41.38  ? 218 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 15.362  -17.627 19.426  1.00 40.09  ? 219 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 31.200  -39.670 27.207  1.00 39.77  ? 220 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 29.812  -39.710 31.414  1.00 33.67  ? 221 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 22.136  -28.469 11.131  1.00 26.82  ? 222 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 22.054  -34.338 16.601  1.00 23.27  ? 223 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 31.801  -33.308 25.857  1.00 45.69  ? 224 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 28.176  -37.221 16.038  1.00 33.23  ? 225 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 22.854  -18.393 21.842  1.00 49.95  ? 226 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 15.178  -21.119 12.307  1.00 31.54  ? 227 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 23.051  -37.952 10.047  1.00 33.75  ? 228 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 31.522  -43.103 11.953  1.00 49.80  ? 229 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 25.134  -31.316 10.775  1.00 34.48  ? 230 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 20.788  -28.740 8.506   1.00 30.19  ? 231 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 20.723  -29.659 4.795   1.00 47.30  ? 232 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 6.917   -18.007 10.805  1.00 37.29  ? 233 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 20.703  -39.962 26.302  1.00 36.52  ? 234 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 31.321  -43.429 15.852  1.00 50.63  ? 235 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 19.675  -41.194 39.063  1.00 69.75  ? 236 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 27.626  -37.708 25.074  1.00 43.19  ? 237 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 14.214  -29.405 4.031   1.00 36.18  ? 238 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 25.507  -17.774 21.139  1.00 53.46  ? 239 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 8.957   -18.886 23.710  1.00 43.52  ? 240 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 19.753  -19.064 25.047  1.00 46.72  ? 241 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 33.213  -24.443 31.727  1.00 48.34  ? 242 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 19.010  -26.659 2.959   1.00 45.01  ? 243 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 25.839  -17.544 13.755  1.00 43.27  ? 244 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 25.403  -39.591 20.234  1.00 35.33  ? 245 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 30.773  -35.424 28.636  1.00 47.53  ? 246 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 14.471  -38.698 9.419   1.00 49.33  ? 247 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 2.549   -28.865 13.583  1.00 58.75  ? 248 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 12.676  -23.205 27.944  1.00 65.22  ? 249 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 4.983   -24.179 18.534  1.00 59.22  ? 250 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 30.118  -32.547 18.285  1.00 40.22  ? 251 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 28.080  -14.784 13.025  1.00 55.61  ? 252 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 17.425  -36.675 29.178  1.00 61.36  ? 253 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 30.406  -25.263 32.449  1.00 49.54  ? 254 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 11.856  -21.199 10.672  1.00 36.74  ? 255 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 29.236  -41.645 27.266  1.00 38.58  ? 256 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 22.510  -13.823 13.348  1.00 45.13  ? 257 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 33.510  -44.482 15.254  1.00 37.25  ? 258 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 29.334  -40.437 19.371  1.00 51.15  ? 259 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 15.675  -41.975 7.977   1.00 50.24  ? 260 HOH C O   1 
# 
