data_7HHO
# 
_entry.id   7HHO 
# 
_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   7HHO         pdb_00007hho 10.2210/pdb7hho/pdb 
WWPDB D_1001407486 ?            ?                   
# 
_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                        7HHO 
_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           N 
_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 '~{N}-(3-azanyl-2-methyl-phenyl)propanamide'       178.231   1   ? ?    ? ? 
5 water       nat water                                              18.015    275 ? ?    ? ? 
# 
_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 '~{N}-(3-azanyl-2-methyl-phenyl)propanamide' A1H9U 
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 
A1H9U non-polymer         . '~{N}-(3-azanyl-2-methyl-phenyl)propanamide' 'N-(3-amino-2-methylphenyl)propanamide' 'C10 H14 N2 O'   
178.231 
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 
# 
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        A1H9U 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H9U 
_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 2 SO4   1   101 1   SO4   SO4 B . 
I 2 SO4   1   102 3   SO4   SO4 B . 
J 4 A1H9U 1   103 101 A1H9U LIG B . 
K 3 EDO   1   101 101 EDO   EDO C . 
L 2 SO4   1   102 5   SO4   SO4 C . 
M 5 HOH   1   201 307 HOH   HOH A . 
M 5 HOH   2   202 202 HOH   HOH A . 
M 5 HOH   3   203 335 HOH   HOH A . 
M 5 HOH   4   204 139 HOH   HOH A . 
M 5 HOH   5   205 367 HOH   HOH A . 
M 5 HOH   6   206 84  HOH   HOH A . 
M 5 HOH   7   207 259 HOH   HOH A . 
M 5 HOH   8   208 304 HOH   HOH A . 
M 5 HOH   9   209 342 HOH   HOH A . 
M 5 HOH   10  210 293 HOH   HOH A . 
M 5 HOH   11  211 87  HOH   HOH A . 
M 5 HOH   12  212 289 HOH   HOH A . 
M 5 HOH   13  213 352 HOH   HOH A . 
M 5 HOH   14  214 71  HOH   HOH A . 
M 5 HOH   15  215 37  HOH   HOH A . 
M 5 HOH   16  216 91  HOH   HOH A . 
M 5 HOH   17  217 95  HOH   HOH A . 
M 5 HOH   18  218 208 HOH   HOH A . 
M 5 HOH   19  219 32  HOH   HOH A . 
M 5 HOH   20  220 199 HOH   HOH A . 
M 5 HOH   21  221 28  HOH   HOH A . 
M 5 HOH   22  222 337 HOH   HOH A . 
M 5 HOH   23  223 55  HOH   HOH A . 
M 5 HOH   24  224 85  HOH   HOH A . 
M 5 HOH   25  225 188 HOH   HOH A . 
M 5 HOH   26  226 38  HOH   HOH A . 
M 5 HOH   27  227 190 HOH   HOH A . 
M 5 HOH   28  228 23  HOH   HOH A . 
M 5 HOH   29  229 97  HOH   HOH A . 
M 5 HOH   30  230 34  HOH   HOH A . 
M 5 HOH   31  231 167 HOH   HOH A . 
M 5 HOH   32  232 111 HOH   HOH A . 
M 5 HOH   33  233 27  HOH   HOH A . 
M 5 HOH   34  234 41  HOH   HOH A . 
M 5 HOH   35  235 86  HOH   HOH A . 
M 5 HOH   36  236 66  HOH   HOH A . 
M 5 HOH   37  237 7   HOH   HOH A . 
M 5 HOH   38  238 260 HOH   HOH A . 
M 5 HOH   39  239 274 HOH   HOH A . 
M 5 HOH   40  240 26  HOH   HOH A . 
M 5 HOH   41  241 8   HOH   HOH A . 
M 5 HOH   42  242 347 HOH   HOH A . 
M 5 HOH   43  243 287 HOH   HOH A . 
M 5 HOH   44  244 292 HOH   HOH A . 
M 5 HOH   45  245 1   HOH   HOH A . 
M 5 HOH   46  246 203 HOH   HOH A . 
M 5 HOH   47  247 267 HOH   HOH A . 
M 5 HOH   48  248 164 HOH   HOH A . 
M 5 HOH   49  249 99  HOH   HOH A . 
M 5 HOH   50  250 290 HOH   HOH A . 
M 5 HOH   51  251 299 HOH   HOH A . 
M 5 HOH   52  252 297 HOH   HOH A . 
M 5 HOH   53  253 60  HOH   HOH A . 
M 5 HOH   54  254 288 HOH   HOH A . 
M 5 HOH   55  255 47  HOH   HOH A . 
M 5 HOH   56  256 2   HOH   HOH A . 
M 5 HOH   57  257 12  HOH   HOH A . 
M 5 HOH   58  258 179 HOH   HOH A . 
M 5 HOH   59  259 145 HOH   HOH A . 
M 5 HOH   60  260 78  HOH   HOH A . 
M 5 HOH   61  261 77  HOH   HOH A . 
M 5 HOH   62  262 109 HOH   HOH A . 
M 5 HOH   63  263 20  HOH   HOH A . 
M 5 HOH   64  264 42  HOH   HOH A . 
M 5 HOH   65  265 18  HOH   HOH A . 
M 5 HOH   66  266 14  HOH   HOH A . 
M 5 HOH   67  267 21  HOH   HOH A . 
M 5 HOH   68  268 278 HOH   HOH A . 
M 5 HOH   69  269 143 HOH   HOH A . 
M 5 HOH   70  270 58  HOH   HOH A . 
M 5 HOH   71  271 94  HOH   HOH A . 
M 5 HOH   72  272 222 HOH   HOH A . 
M 5 HOH   73  273 115 HOH   HOH A . 
M 5 HOH   74  274 300 HOH   HOH A . 
M 5 HOH   75  275 113 HOH   HOH A . 
M 5 HOH   76  276 354 HOH   HOH A . 
M 5 HOH   77  277 93  HOH   HOH A . 
M 5 HOH   78  278 16  HOH   HOH A . 
M 5 HOH   79  279 19  HOH   HOH A . 
M 5 HOH   80  280 281 HOH   HOH A . 
M 5 HOH   81  281 116 HOH   HOH A . 
M 5 HOH   82  282 9   HOH   HOH A . 
M 5 HOH   83  283 301 HOH   HOH A . 
M 5 HOH   84  284 73  HOH   HOH A . 
M 5 HOH   85  285 211 HOH   HOH A . 
M 5 HOH   86  286 35  HOH   HOH A . 
M 5 HOH   87  287 318 HOH   HOH A . 
M 5 HOH   88  288 64  HOH   HOH A . 
M 5 HOH   89  289 165 HOH   HOH A . 
M 5 HOH   90  290 131 HOH   HOH A . 
M 5 HOH   91  291 218 HOH   HOH A . 
M 5 HOH   92  292 31  HOH   HOH A . 
M 5 HOH   93  293 22  HOH   HOH A . 
M 5 HOH   94  294 358 HOH   HOH A . 
M 5 HOH   95  295 296 HOH   HOH A . 
M 5 HOH   96  296 327 HOH   HOH A . 
M 5 HOH   97  297 210 HOH   HOH A . 
M 5 HOH   98  298 152 HOH   HOH A . 
M 5 HOH   99  299 63  HOH   HOH A . 
M 5 HOH   100 300 270 HOH   HOH A . 
M 5 HOH   101 301 340 HOH   HOH A . 
M 5 HOH   102 302 185 HOH   HOH A . 
M 5 HOH   103 303 83  HOH   HOH A . 
M 5 HOH   104 304 219 HOH   HOH A . 
M 5 HOH   105 305 205 HOH   HOH A . 
M 5 HOH   106 306 336 HOH   HOH A . 
M 5 HOH   107 307 57  HOH   HOH A . 
M 5 HOH   108 308 351 HOH   HOH A . 
M 5 HOH   109 309 283 HOH   HOH A . 
M 5 HOH   110 310 75  HOH   HOH A . 
M 5 HOH   111 311 313 HOH   HOH A . 
M 5 HOH   112 312 156 HOH   HOH A . 
M 5 HOH   113 313 125 HOH   HOH A . 
M 5 HOH   114 314 370 HOH   HOH A . 
M 5 HOH   115 315 332 HOH   HOH A . 
N 5 HOH   1   201 247 HOH   HOH B . 
N 5 HOH   2   202 89  HOH   HOH B . 
N 5 HOH   3   203 331 HOH   HOH B . 
N 5 HOH   4   204 177 HOH   HOH B . 
N 5 HOH   5   205 242 HOH   HOH B . 
N 5 HOH   6   206 258 HOH   HOH B . 
N 5 HOH   7   207 69  HOH   HOH B . 
N 5 HOH   8   208 272 HOH   HOH B . 
N 5 HOH   9   209 98  HOH   HOH B . 
N 5 HOH   10  210 329 HOH   HOH B . 
N 5 HOH   11  211 123 HOH   HOH B . 
N 5 HOH   12  212 17  HOH   HOH B . 
N 5 HOH   13  213 215 HOH   HOH B . 
N 5 HOH   14  214 72  HOH   HOH B . 
N 5 HOH   15  215 76  HOH   HOH B . 
N 5 HOH   16  216 320 HOH   HOH B . 
N 5 HOH   17  217 184 HOH   HOH B . 
N 5 HOH   18  218 54  HOH   HOH B . 
N 5 HOH   19  219 119 HOH   HOH B . 
N 5 HOH   20  220 366 HOH   HOH B . 
N 5 HOH   21  221 249 HOH   HOH B . 
N 5 HOH   22  222 117 HOH   HOH B . 
N 5 HOH   23  223 170 HOH   HOH B . 
N 5 HOH   24  224 157 HOH   HOH B . 
N 5 HOH   25  225 6   HOH   HOH B . 
N 5 HOH   26  226 68  HOH   HOH B . 
N 5 HOH   27  227 172 HOH   HOH B . 
N 5 HOH   28  228 10  HOH   HOH B . 
N 5 HOH   29  229 137 HOH   HOH B . 
N 5 HOH   30  230 5   HOH   HOH B . 
N 5 HOH   31  231 280 HOH   HOH B . 
N 5 HOH   32  232 315 HOH   HOH B . 
N 5 HOH   33  233 169 HOH   HOH B . 
N 5 HOH   34  234 223 HOH   HOH B . 
N 5 HOH   35  235 168 HOH   HOH B . 
N 5 HOH   36  236 261 HOH   HOH B . 
N 5 HOH   37  237 25  HOH   HOH B . 
N 5 HOH   38  238 341 HOH   HOH B . 
N 5 HOH   39  239 372 HOH   HOH B . 
N 5 HOH   40  240 59  HOH   HOH B . 
N 5 HOH   41  241 224 HOH   HOH B . 
N 5 HOH   42  242 175 HOH   HOH B . 
N 5 HOH   43  243 24  HOH   HOH B . 
N 5 HOH   44  244 150 HOH   HOH B . 
N 5 HOH   45  245 13  HOH   HOH B . 
N 5 HOH   46  246 96  HOH   HOH B . 
N 5 HOH   47  247 101 HOH   HOH B . 
N 5 HOH   48  248 61  HOH   HOH B . 
N 5 HOH   49  249 373 HOH   HOH B . 
N 5 HOH   50  250 153 HOH   HOH B . 
N 5 HOH   51  251 182 HOH   HOH B . 
N 5 HOH   52  252 74  HOH   HOH B . 
N 5 HOH   53  253 217 HOH   HOH B . 
N 5 HOH   54  254 319 HOH   HOH B . 
N 5 HOH   55  255 36  HOH   HOH B . 
N 5 HOH   56  256 344 HOH   HOH B . 
N 5 HOH   57  257 279 HOH   HOH B . 
N 5 HOH   58  258 214 HOH   HOH B . 
N 5 HOH   59  259 120 HOH   HOH B . 
N 5 HOH   60  260 197 HOH   HOH B . 
N 5 HOH   61  261 361 HOH   HOH B . 
N 5 HOH   62  262 303 HOH   HOH B . 
N 5 HOH   63  263 46  HOH   HOH B . 
N 5 HOH   64  264 369 HOH   HOH B . 
N 5 HOH   65  265 79  HOH   HOH B . 
N 5 HOH   66  266 316 HOH   HOH B . 
N 5 HOH   67  267 44  HOH   HOH B . 
N 5 HOH   68  268 374 HOH   HOH B . 
N 5 HOH   69  269 104 HOH   HOH B . 
N 5 HOH   70  270 291 HOH   HOH B . 
N 5 HOH   71  271 371 HOH   HOH B . 
N 5 HOH   72  272 322 HOH   HOH B . 
N 5 HOH   73  273 160 HOH   HOH B . 
N 5 HOH   74  274 333 HOH   HOH B . 
N 5 HOH   75  275 357 HOH   HOH B . 
N 5 HOH   76  276 201 HOH   HOH B . 
N 5 HOH   77  277 346 HOH   HOH B . 
N 5 HOH   78  278 163 HOH   HOH B . 
N 5 HOH   79  279 365 HOH   HOH B . 
N 5 HOH   80  280 343 HOH   HOH B . 
N 5 HOH   81  281 103 HOH   HOH B . 
N 5 HOH   82  282 359 HOH   HOH B . 
N 5 HOH   83  283 314 HOH   HOH B . 
N 5 HOH   84  284 107 HOH   HOH B . 
N 5 HOH   85  285 312 HOH   HOH B . 
O 5 HOH   1   201 321 HOH   HOH C . 
O 5 HOH   2   202 349 HOH   HOH C . 
O 5 HOH   3   203 345 HOH   HOH C . 
O 5 HOH   4   204 323 HOH   HOH C . 
O 5 HOH   5   205 254 HOH   HOH C . 
O 5 HOH   6   206 330 HOH   HOH C . 
O 5 HOH   7   207 364 HOH   HOH C . 
O 5 HOH   8   208 362 HOH   HOH C . 
O 5 HOH   9   209 338 HOH   HOH C . 
O 5 HOH   10  210 325 HOH   HOH C . 
O 5 HOH   11  211 226 HOH   HOH C . 
O 5 HOH   12  212 271 HOH   HOH C . 
O 5 HOH   13  213 317 HOH   HOH C . 
O 5 HOH   14  214 148 HOH   HOH C . 
O 5 HOH   15  215 173 HOH   HOH C . 
O 5 HOH   16  216 90  HOH   HOH C . 
O 5 HOH   17  217 134 HOH   HOH C . 
O 5 HOH   18  218 49  HOH   HOH C . 
O 5 HOH   19  219 209 HOH   HOH C . 
O 5 HOH   20  220 15  HOH   HOH C . 
O 5 HOH   21  221 118 HOH   HOH C . 
O 5 HOH   22  222 269 HOH   HOH C . 
O 5 HOH   23  223 302 HOH   HOH C . 
O 5 HOH   24  224 309 HOH   HOH C . 
O 5 HOH   25  225 82  HOH   HOH C . 
O 5 HOH   26  226 126 HOH   HOH C . 
O 5 HOH   27  227 142 HOH   HOH C . 
O 5 HOH   28  228 40  HOH   HOH C . 
O 5 HOH   29  229 198 HOH   HOH C . 
O 5 HOH   30  230 189 HOH   HOH C . 
O 5 HOH   31  231 353 HOH   HOH C . 
O 5 HOH   32  232 360 HOH   HOH C . 
O 5 HOH   33  233 284 HOH   HOH C . 
O 5 HOH   34  234 102 HOH   HOH C . 
O 5 HOH   35  235 348 HOH   HOH C . 
O 5 HOH   36  236 43  HOH   HOH C . 
O 5 HOH   37  237 161 HOH   HOH C . 
O 5 HOH   38  238 132 HOH   HOH C . 
O 5 HOH   39  239 45  HOH   HOH C . 
O 5 HOH   40  240 295 HOH   HOH C . 
O 5 HOH   41  241 4   HOH   HOH C . 
O 5 HOH   42  242 298 HOH   HOH C . 
O 5 HOH   43  243 48  HOH   HOH C . 
O 5 HOH   44  244 275 HOH   HOH C . 
O 5 HOH   45  245 122 HOH   HOH C . 
O 5 HOH   46  246 146 HOH   HOH C . 
O 5 HOH   47  247 62  HOH   HOH C . 
O 5 HOH   48  248 135 HOH   HOH C . 
O 5 HOH   49  249 326 HOH   HOH C . 
O 5 HOH   50  250 328 HOH   HOH C . 
O 5 HOH   51  251 294 HOH   HOH C . 
O 5 HOH   52  252 56  HOH   HOH C . 
O 5 HOH   53  253 53  HOH   HOH C . 
O 5 HOH   54  254 171 HOH   HOH C . 
O 5 HOH   55  255 151 HOH   HOH C . 
O 5 HOH   56  256 130 HOH   HOH C . 
O 5 HOH   57  257 67  HOH   HOH C . 
O 5 HOH   58  258 368 HOH   HOH C . 
O 5 HOH   59  259 149 HOH   HOH C . 
O 5 HOH   60  260 305 HOH   HOH C . 
O 5 HOH   61  261 65  HOH   HOH C . 
O 5 HOH   62  262 241 HOH   HOH C . 
O 5 HOH   63  263 246 HOH   HOH C . 
O 5 HOH   64  264 324 HOH   HOH C . 
O 5 HOH   65  265 356 HOH   HOH C . 
O 5 HOH   66  266 334 HOH   HOH C . 
O 5 HOH   67  267 339 HOH   HOH C . 
O 5 HOH   68  268 70  HOH   HOH C . 
O 5 HOH   69  269 108 HOH   HOH C . 
O 5 HOH   70  270 310 HOH   HOH C . 
O 5 HOH   71  271 350 HOH   HOH C . 
O 5 HOH   72  272 92  HOH   HOH C . 
O 5 HOH   73  273 363 HOH   HOH C . 
O 5 HOH   74  274 206 HOH   HOH C . 
O 5 HOH   75  275 355 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 LYS 73 ? CD  ? A LYS 74 CD  
4  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
5  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
6  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
7  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
8  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
9  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
10 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
11 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
12 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
13 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
14 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
15 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
16 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
17 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
18 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
19 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
20 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
21 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
22 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
23 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
24 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
25 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
26 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
27 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
28 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
29 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
30 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
31 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
32 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
33 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
34 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
35 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
36 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
37 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
38 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
39 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
40 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
41 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
42 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
43 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
44 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
45 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
46 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
47 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
48 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
49 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
50 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
51 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
52 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           7HHO 
_cell.length_a           41.600 
_cell.length_b           42.160 
_cell.length_c           159.390 
_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                         7HHO 
_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          7HHO 
_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                     7HHO 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.69 
_reflns.d_resolution_high            1.76 
_reflns.number_obs                   28772 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.122 
_reflns.pdbx_netI_over_sigmaI        8.2 
_reflns.pdbx_redundancy              6.5 
_reflns.pdbx_Rrim_I_all              0.133 
_reflns.pdbx_Rpim_I_all              0.052 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     185934 
_reflns.pdbx_chi_squared             0.99 
_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                  1.76 
_reflns_shell.d_res_low                   1.81 
_reflns_shell.number_measured_all         14163 
_reflns_shell.number_unique_obs           2091 
_reflns_shell.Rmerge_I_obs                2.693 
_reflns_shell.pdbx_chi_squared            0.89 
_reflns_shell.pdbx_redundancy             6.8 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             2.913 
_reflns_shell.pdbx_Rpim_I_all             1.102 
_reflns_shell.pdbx_CC_half                0.307 
_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                                 7HHO 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     27222 
_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                             79.69 
_refine.ls_d_res_high                            1.76 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_R_factor_obs                          0.19891 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19636 
_refine.ls_R_factor_R_free                       0.24417 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  1482 
_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          0.950 
_refine.B_iso_mean                               41.237 
_refine.aniso_B[1][1]                            0.80 
_refine.aniso_B[2][2]                            -0.59 
_refine.aniso_B[3][3]                            -0.21 
_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                       0.133 
_refine.pdbx_overall_ESU_R_Free                  0.132 
_refine.overall_SU_ML                            0.123 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.243 
_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        2143 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             275 
_refine_hist.number_atoms_total               2469 
_refine_hist.d_res_high                       1.76 
_refine_hist.d_res_low                        79.69 
# 
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             0.008  0.012  ? 2297 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.732  1.834  ? 3125 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.241  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.521  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.870 10.000 ? 303  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.130  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1916 '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                  3.715  3.875  ? 1073 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.187  6.916  ? 1337 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.896  4.181  ? 1224 '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       9.789  59.66  ? 3641 '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                       1.760 
_refine_ls_shell.d_res_low                        1.806 
_refine_ls_shell.number_reflns_R_work             1972 
_refine_ls_shell.R_factor_R_work                  0.362 
_refine_ls_shell.percent_reflns_obs               99.86 
_refine_ls_shell.R_factor_R_free                  0.386 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             109 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHO 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z235361315' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHO 
_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 2 ? 
I N N 2 ? 
J N N 4 ? 
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 7HHO A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHO B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHO 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 7HHO GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHO SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHO GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHO SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHO GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHO 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,M 
2 1 B,H,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 ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
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 TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
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                   7HHO 
_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   B HOH 231 ? ? O B HOH 272 ? ? 1.75 
2  1 O   A HOH 251 ? ? O C HOH 209 ? ? 1.78 
3  1 O   A HOH 227 ? ? O A HOH 308 ? ? 1.96 
4  1 O   A HOH 213 ? ? O A HOH 275 ? ? 1.97 
5  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 2.00 
6  1 OH  C TYR 40  ? ? O C HOH 202 ? ? 2.07 
7  1 O   B HOH 209 ? ? O B HOH 282 ? ? 2.11 
8  1 O   B HOH 204 ? ? O B HOH 277 ? ? 2.11 
9  1 OE1 C GLN 85  ? ? O C HOH 203 ? ? 2.12 
10 1 O   A HOH 209 ? ? O A HOH 293 ? ? 2.13 
11 1 O   A HOH 300 ? ? O C HOH 203 ? ? 2.13 
12 1 O   A HOH 271 ? ? O A HOH 299 ? ? 2.18 
13 1 O   B HOH 227 ? ? O B HOH 243 ? ? 2.18 
14 1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 281 ? ? 1_555 O C HOH 246 ? ? 4_445 1.79 
2 1 O A HOH 244 ? ? 1_555 O A HOH 272 ? ? 4_545 1.97 
3 1 O A HOH 281 ? ? 1_555 O C HOH 264 ? ? 4_445 2.04 
4 1 O A HOH 286 ? ? 1_555 O A HOH 309 ? ? 4_545 2.15 
5 1 O A HOH 233 ? ? 1_555 O C HOH 267 ? ? 4_445 2.16 
6 1 O B HOH 238 ? ? 1_555 O C HOH 224 ? ? 2_644 2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                86.96 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -13.24 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                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 ? ? -152.82 65.10 
2 1 ASN B 38 ? ? 78.82   -0.61 
3 1 ASN B 87 ? ? -158.10 59.87 
4 1 ALA C 4  ? ? -174.08 88.58 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            146.76 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.088 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 315 ? 5.95 . 
2 1 O ? C HOH 275 ? 6.98 . 
# 
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 
A1H9U N1   N N N 1   
A1H9U C4   C Y N 2   
A1H9U C5   C Y N 3   
A1H9U C6   C Y N 4   
A1H9U C7   C Y N 5   
A1H9U C8   C Y N 6   
A1H9U C10  C N N 7   
A1H9U C1   C N N 8   
A1H9U C2   C N N 9   
A1H9U C3   C N N 10  
A1H9U C9   C Y N 11  
A1H9U N2   N N N 12  
A1H9U O1   O N N 13  
A1H9U H6   H N N 14  
A1H9U H7   H N N 15  
A1H9U H8   H N N 16  
A1H9U H9   H N N 17  
A1H9U H14  H N N 18  
A1H9U H13  H N N 19  
A1H9U H12  H N N 20  
A1H9U H2   H N N 21  
A1H9U H1   H N N 22  
A1H9U H3   H N N 23  
A1H9U H4   H N N 24  
A1H9U H5   H N N 25  
A1H9U H11  H N N 26  
A1H9U H10  H N N 27  
ALA   N    N N N 28  
ALA   CA   C N S 29  
ALA   C    C N N 30  
ALA   O    O N N 31  
ALA   CB   C N N 32  
ALA   OXT  O N N 33  
ALA   H    H N N 34  
ALA   H2   H N N 35  
ALA   HA   H N N 36  
ALA   HB1  H N N 37  
ALA   HB2  H N N 38  
ALA   HB3  H N N 39  
ALA   HXT  H N N 40  
ARG   N    N N N 41  
ARG   CA   C N S 42  
ARG   C    C N N 43  
ARG   O    O N N 44  
ARG   CB   C N N 45  
ARG   CG   C N N 46  
ARG   CD   C N N 47  
ARG   NE   N N N 48  
ARG   CZ   C N N 49  
ARG   NH1  N N N 50  
ARG   NH2  N N N 51  
ARG   OXT  O N N 52  
ARG   H    H N N 53  
ARG   H2   H N N 54  
ARG   HA   H N N 55  
ARG   HB2  H N N 56  
ARG   HB3  H N N 57  
ARG   HG2  H N N 58  
ARG   HG3  H N N 59  
ARG   HD2  H N N 60  
ARG   HD3  H N N 61  
ARG   HE   H N N 62  
ARG   HH11 H N N 63  
ARG   HH12 H N N 64  
ARG   HH21 H N N 65  
ARG   HH22 H N N 66  
ARG   HXT  H N N 67  
ASN   N    N N N 68  
ASN   CA   C N S 69  
ASN   C    C N N 70  
ASN   O    O N N 71  
ASN   CB   C N N 72  
ASN   CG   C N N 73  
ASN   OD1  O N N 74  
ASN   ND2  N N N 75  
ASN   OXT  O N N 76  
ASN   H    H N N 77  
ASN   H2   H N N 78  
ASN   HA   H N N 79  
ASN   HB2  H N N 80  
ASN   HB3  H N N 81  
ASN   HD21 H N N 82  
ASN   HD22 H N N 83  
ASN   HXT  H N N 84  
ASP   N    N N N 85  
ASP   CA   C N S 86  
ASP   C    C N N 87  
ASP   O    O N N 88  
ASP   CB   C N N 89  
ASP   CG   C N N 90  
ASP   OD1  O N N 91  
ASP   OD2  O N N 92  
ASP   OXT  O N N 93  
ASP   H    H N N 94  
ASP   H2   H N N 95  
ASP   HA   H N N 96  
ASP   HB2  H N N 97  
ASP   HB3  H N N 98  
ASP   HD2  H N N 99  
ASP   HXT  H N N 100 
CYS   N    N N N 101 
CYS   CA   C N R 102 
CYS   C    C N N 103 
CYS   O    O N N 104 
CYS   CB   C N N 105 
CYS   SG   S N N 106 
CYS   OXT  O N N 107 
CYS   H    H N N 108 
CYS   H2   H N N 109 
CYS   HA   H N N 110 
CYS   HB2  H N N 111 
CYS   HB3  H N N 112 
CYS   HG   H N N 113 
CYS   HXT  H N N 114 
EDO   C1   C N N 115 
EDO   O1   O N N 116 
EDO   C2   C N N 117 
EDO   O2   O N N 118 
EDO   H11  H N N 119 
EDO   H12  H N N 120 
EDO   HO1  H N N 121 
EDO   H21  H N N 122 
EDO   H22  H N N 123 
EDO   HO2  H N N 124 
GLN   N    N N N 125 
GLN   CA   C N S 126 
GLN   C    C N N 127 
GLN   O    O N N 128 
GLN   CB   C N N 129 
GLN   CG   C N N 130 
GLN   CD   C N N 131 
GLN   OE1  O N N 132 
GLN   NE2  N N N 133 
GLN   OXT  O N N 134 
GLN   H    H N N 135 
GLN   H2   H N N 136 
GLN   HA   H N N 137 
GLN   HB2  H N N 138 
GLN   HB3  H N N 139 
GLN   HG2  H N N 140 
GLN   HG3  H N N 141 
GLN   HE21 H N N 142 
GLN   HE22 H N N 143 
GLN   HXT  H N N 144 
GLU   N    N N N 145 
GLU   CA   C N S 146 
GLU   C    C N N 147 
GLU   O    O N N 148 
GLU   CB   C N N 149 
GLU   CG   C N N 150 
GLU   CD   C N N 151 
GLU   OE1  O N N 152 
GLU   OE2  O N N 153 
GLU   OXT  O N N 154 
GLU   H    H N N 155 
GLU   H2   H N N 156 
GLU   HA   H N N 157 
GLU   HB2  H N N 158 
GLU   HB3  H N N 159 
GLU   HG2  H N N 160 
GLU   HG3  H N N 161 
GLU   HE2  H N N 162 
GLU   HXT  H N N 163 
GLY   N    N N N 164 
GLY   CA   C N N 165 
GLY   C    C N N 166 
GLY   O    O N N 167 
GLY   OXT  O N N 168 
GLY   H    H N N 169 
GLY   H2   H N N 170 
GLY   HA2  H N N 171 
GLY   HA3  H N N 172 
GLY   HXT  H N N 173 
HIS   N    N N N 174 
HIS   CA   C N S 175 
HIS   C    C N N 176 
HIS   O    O N N 177 
HIS   CB   C N N 178 
HIS   CG   C Y N 179 
HIS   ND1  N Y N 180 
HIS   CD2  C Y N 181 
HIS   CE1  C Y N 182 
HIS   NE2  N Y N 183 
HIS   OXT  O N N 184 
HIS   H    H N N 185 
HIS   H2   H N N 186 
HIS   HA   H N N 187 
HIS   HB2  H N N 188 
HIS   HB3  H N N 189 
HIS   HD1  H N N 190 
HIS   HD2  H N N 191 
HIS   HE1  H N N 192 
HIS   HE2  H N N 193 
HIS   HXT  H N N 194 
HOH   O    O N N 195 
HOH   H1   H N N 196 
HOH   H2   H N N 197 
ILE   N    N N N 198 
ILE   CA   C N S 199 
ILE   C    C N N 200 
ILE   O    O N N 201 
ILE   CB   C N S 202 
ILE   CG1  C N N 203 
ILE   CG2  C N N 204 
ILE   CD1  C N N 205 
ILE   OXT  O N N 206 
ILE   H    H N N 207 
ILE   H2   H N N 208 
ILE   HA   H N N 209 
ILE   HB   H N N 210 
ILE   HG12 H N N 211 
ILE   HG13 H N N 212 
ILE   HG21 H N N 213 
ILE   HG22 H N N 214 
ILE   HG23 H N N 215 
ILE   HD11 H N N 216 
ILE   HD12 H N N 217 
ILE   HD13 H N N 218 
ILE   HXT  H N N 219 
LEU   N    N N N 220 
LEU   CA   C N S 221 
LEU   C    C N N 222 
LEU   O    O N N 223 
LEU   CB   C N N 224 
LEU   CG   C N N 225 
LEU   CD1  C N N 226 
LEU   CD2  C N N 227 
LEU   OXT  O N N 228 
LEU   H    H N N 229 
LEU   H2   H N N 230 
LEU   HA   H N N 231 
LEU   HB2  H N N 232 
LEU   HB3  H N N 233 
LEU   HG   H N N 234 
LEU   HD11 H N N 235 
LEU   HD12 H N N 236 
LEU   HD13 H N N 237 
LEU   HD21 H N N 238 
LEU   HD22 H N N 239 
LEU   HD23 H N N 240 
LEU   HXT  H N N 241 
LYS   N    N N N 242 
LYS   CA   C N S 243 
LYS   C    C N N 244 
LYS   O    O N N 245 
LYS   CB   C N N 246 
LYS   CG   C N N 247 
LYS   CD   C N N 248 
LYS   CE   C N N 249 
LYS   NZ   N N N 250 
LYS   OXT  O N N 251 
LYS   H    H N N 252 
LYS   H2   H N N 253 
LYS   HA   H N N 254 
LYS   HB2  H N N 255 
LYS   HB3  H N N 256 
LYS   HG2  H N N 257 
LYS   HG3  H N N 258 
LYS   HD2  H N N 259 
LYS   HD3  H N N 260 
LYS   HE2  H N N 261 
LYS   HE3  H N N 262 
LYS   HZ1  H N N 263 
LYS   HZ2  H N N 264 
LYS   HZ3  H N N 265 
LYS   HXT  H N N 266 
MET   N    N N N 267 
MET   CA   C N S 268 
MET   C    C N N 269 
MET   O    O N N 270 
MET   CB   C N N 271 
MET   CG   C N N 272 
MET   SD   S N N 273 
MET   CE   C N N 274 
MET   OXT  O N N 275 
MET   H    H N N 276 
MET   H2   H N N 277 
MET   HA   H N N 278 
MET   HB2  H N N 279 
MET   HB3  H N N 280 
MET   HG2  H N N 281 
MET   HG3  H N N 282 
MET   HE1  H N N 283 
MET   HE2  H N N 284 
MET   HE3  H N N 285 
MET   HXT  H N N 286 
PHE   N    N N N 287 
PHE   CA   C N S 288 
PHE   C    C N N 289 
PHE   O    O N N 290 
PHE   CB   C N N 291 
PHE   CG   C Y N 292 
PHE   CD1  C Y N 293 
PHE   CD2  C Y N 294 
PHE   CE1  C Y N 295 
PHE   CE2  C Y N 296 
PHE   CZ   C Y N 297 
PHE   OXT  O N N 298 
PHE   H    H N N 299 
PHE   H2   H N N 300 
PHE   HA   H N N 301 
PHE   HB2  H N N 302 
PHE   HB3  H N N 303 
PHE   HD1  H N N 304 
PHE   HD2  H N N 305 
PHE   HE1  H N N 306 
PHE   HE2  H N N 307 
PHE   HZ   H N N 308 
PHE   HXT  H N N 309 
PRO   N    N N N 310 
PRO   CA   C N S 311 
PRO   C    C N N 312 
PRO   O    O N N 313 
PRO   CB   C N N 314 
PRO   CG   C N N 315 
PRO   CD   C N N 316 
PRO   OXT  O N N 317 
PRO   H    H N N 318 
PRO   HA   H N N 319 
PRO   HB2  H N N 320 
PRO   HB3  H N N 321 
PRO   HG2  H N N 322 
PRO   HG3  H N N 323 
PRO   HD2  H N N 324 
PRO   HD3  H N N 325 
PRO   HXT  H N N 326 
SER   N    N N N 327 
SER   CA   C N S 328 
SER   C    C N N 329 
SER   O    O N N 330 
SER   CB   C N N 331 
SER   OG   O N N 332 
SER   OXT  O N N 333 
SER   H    H N N 334 
SER   H2   H N N 335 
SER   HA   H N N 336 
SER   HB2  H N N 337 
SER   HB3  H N N 338 
SER   HG   H N N 339 
SER   HXT  H N N 340 
SO4   S    S N N 341 
SO4   O1   O N N 342 
SO4   O2   O N N 343 
SO4   O3   O N N 344 
SO4   O4   O N N 345 
THR   N    N N N 346 
THR   CA   C N S 347 
THR   C    C N N 348 
THR   O    O N N 349 
THR   CB   C N R 350 
THR   OG1  O N N 351 
THR   CG2  C N N 352 
THR   OXT  O N N 353 
THR   H    H N N 354 
THR   H2   H N N 355 
THR   HA   H N N 356 
THR   HB   H N N 357 
THR   HG1  H N N 358 
THR   HG21 H N N 359 
THR   HG22 H N N 360 
THR   HG23 H N N 361 
THR   HXT  H N N 362 
TRP   N    N N N 363 
TRP   CA   C N S 364 
TRP   C    C N N 365 
TRP   O    O N N 366 
TRP   CB   C N N 367 
TRP   CG   C Y N 368 
TRP   CD1  C Y N 369 
TRP   CD2  C Y N 370 
TRP   NE1  N Y N 371 
TRP   CE2  C Y N 372 
TRP   CE3  C Y N 373 
TRP   CZ2  C Y N 374 
TRP   CZ3  C Y N 375 
TRP   CH2  C Y N 376 
TRP   OXT  O N N 377 
TRP   H    H N N 378 
TRP   H2   H N N 379 
TRP   HA   H N N 380 
TRP   HB2  H N N 381 
TRP   HB3  H N N 382 
TRP   HD1  H N N 383 
TRP   HE1  H N N 384 
TRP   HE3  H N N 385 
TRP   HZ2  H N N 386 
TRP   HZ3  H N N 387 
TRP   HH2  H N N 388 
TRP   HXT  H N N 389 
TYR   N    N N N 390 
TYR   CA   C N S 391 
TYR   C    C N N 392 
TYR   O    O N N 393 
TYR   CB   C N N 394 
TYR   CG   C Y N 395 
TYR   CD1  C Y N 396 
TYR   CD2  C Y N 397 
TYR   CE1  C Y N 398 
TYR   CE2  C Y N 399 
TYR   CZ   C Y N 400 
TYR   OH   O N N 401 
TYR   OXT  O N N 402 
TYR   H    H N N 403 
TYR   H2   H N N 404 
TYR   HA   H N N 405 
TYR   HB2  H N N 406 
TYR   HB3  H N N 407 
TYR   HD1  H N N 408 
TYR   HD2  H N N 409 
TYR   HE1  H N N 410 
TYR   HE2  H N N 411 
TYR   HH   H N N 412 
TYR   HXT  H N N 413 
VAL   N    N N N 414 
VAL   CA   C N S 415 
VAL   C    C N N 416 
VAL   O    O N N 417 
VAL   CB   C N N 418 
VAL   CG1  C N N 419 
VAL   CG2  C N N 420 
VAL   OXT  O N N 421 
VAL   H    H N N 422 
VAL   H2   H N N 423 
VAL   HA   H N N 424 
VAL   HB   H N N 425 
VAL   HG11 H N N 426 
VAL   HG12 H N N 427 
VAL   HG13 H N N 428 
VAL   HG21 H N N 429 
VAL   HG22 H N N 430 
VAL   HG23 H N N 431 
VAL   HXT  H N N 432 
# 
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 
A1H9U C1  C2   sing N N 1   
A1H9U C2  C3   sing N N 2   
A1H9U C3  O1   doub N N 3   
A1H9U C3  N1   sing N N 4   
A1H9U N1  C4   sing N N 5   
A1H9U C4  C5   doub Y N 6   
A1H9U C5  C6   sing Y N 7   
A1H9U C6  C7   doub Y N 8   
A1H9U C7  C8   sing Y N 9   
A1H9U C8  N2   sing N N 10  
A1H9U C8  C9   doub Y N 11  
A1H9U C9  C10  sing N N 12  
A1H9U C4  C9   sing Y N 13  
A1H9U N1  H6   sing N N 14  
A1H9U C5  H7   sing N N 15  
A1H9U C6  H8   sing N N 16  
A1H9U C7  H9   sing N N 17  
A1H9U C10 H14  sing N N 18  
A1H9U C10 H13  sing N N 19  
A1H9U C10 H12  sing N N 20  
A1H9U C1  H2   sing N N 21  
A1H9U C1  H1   sing N N 22  
A1H9U C1  H3   sing N N 23  
A1H9U C2  H4   sing N N 24  
A1H9U C2  H5   sing N N 25  
A1H9U N2  H11  sing N N 26  
A1H9U N2  H10  sing N N 27  
ALA   N   CA   sing N N 28  
ALA   N   H    sing N N 29  
ALA   N   H2   sing N N 30  
ALA   CA  C    sing N N 31  
ALA   CA  CB   sing N N 32  
ALA   CA  HA   sing N N 33  
ALA   C   O    doub N N 34  
ALA   C   OXT  sing N N 35  
ALA   CB  HB1  sing N N 36  
ALA   CB  HB2  sing N N 37  
ALA   CB  HB3  sing N N 38  
ALA   OXT HXT  sing N N 39  
ARG   N   CA   sing N N 40  
ARG   N   H    sing N N 41  
ARG   N   H2   sing N N 42  
ARG   CA  C    sing N N 43  
ARG   CA  CB   sing N N 44  
ARG   CA  HA   sing N N 45  
ARG   C   O    doub N N 46  
ARG   C   OXT  sing N N 47  
ARG   CB  CG   sing N N 48  
ARG   CB  HB2  sing N N 49  
ARG   CB  HB3  sing N N 50  
ARG   CG  CD   sing N N 51  
ARG   CG  HG2  sing N N 52  
ARG   CG  HG3  sing N N 53  
ARG   CD  NE   sing N N 54  
ARG   CD  HD2  sing N N 55  
ARG   CD  HD3  sing N N 56  
ARG   NE  CZ   sing N N 57  
ARG   NE  HE   sing N N 58  
ARG   CZ  NH1  sing N N 59  
ARG   CZ  NH2  doub N N 60  
ARG   NH1 HH11 sing N N 61  
ARG   NH1 HH12 sing N N 62  
ARG   NH2 HH21 sing N N 63  
ARG   NH2 HH22 sing N N 64  
ARG   OXT HXT  sing N N 65  
ASN   N   CA   sing N N 66  
ASN   N   H    sing N N 67  
ASN   N   H2   sing N N 68  
ASN   CA  C    sing N N 69  
ASN   CA  CB   sing N N 70  
ASN   CA  HA   sing N N 71  
ASN   C   O    doub N N 72  
ASN   C   OXT  sing N N 73  
ASN   CB  CG   sing N N 74  
ASN   CB  HB2  sing N N 75  
ASN   CB  HB3  sing N N 76  
ASN   CG  OD1  doub N N 77  
ASN   CG  ND2  sing N N 78  
ASN   ND2 HD21 sing N N 79  
ASN   ND2 HD22 sing N N 80  
ASN   OXT HXT  sing N N 81  
ASP   N   CA   sing N N 82  
ASP   N   H    sing N N 83  
ASP   N   H2   sing N N 84  
ASP   CA  C    sing N N 85  
ASP   CA  CB   sing N N 86  
ASP   CA  HA   sing N N 87  
ASP   C   O    doub N N 88  
ASP   C   OXT  sing N N 89  
ASP   CB  CG   sing N N 90  
ASP   CB  HB2  sing N N 91  
ASP   CB  HB3  sing N N 92  
ASP   CG  OD1  doub N N 93  
ASP   CG  OD2  sing N N 94  
ASP   OD2 HD2  sing N N 95  
ASP   OXT HXT  sing N N 96  
CYS   N   CA   sing N N 97  
CYS   N   H    sing N N 98  
CYS   N   H2   sing N N 99  
CYS   CA  C    sing N N 100 
CYS   CA  CB   sing N N 101 
CYS   CA  HA   sing N N 102 
CYS   C   O    doub N N 103 
CYS   C   OXT  sing N N 104 
CYS   CB  SG   sing N N 105 
CYS   CB  HB2  sing N N 106 
CYS   CB  HB3  sing N N 107 
CYS   SG  HG   sing N N 108 
CYS   OXT HXT  sing N N 109 
EDO   C1  O1   sing N N 110 
EDO   C1  C2   sing N N 111 
EDO   C1  H11  sing N N 112 
EDO   C1  H12  sing N N 113 
EDO   O1  HO1  sing N N 114 
EDO   C2  O2   sing N N 115 
EDO   C2  H21  sing N N 116 
EDO   C2  H22  sing N N 117 
EDO   O2  HO2  sing N N 118 
GLN   N   CA   sing N N 119 
GLN   N   H    sing N N 120 
GLN   N   H2   sing N N 121 
GLN   CA  C    sing N N 122 
GLN   CA  CB   sing N N 123 
GLN   CA  HA   sing N N 124 
GLN   C   O    doub N N 125 
GLN   C   OXT  sing N N 126 
GLN   CB  CG   sing N N 127 
GLN   CB  HB2  sing N N 128 
GLN   CB  HB3  sing N N 129 
GLN   CG  CD   sing N N 130 
GLN   CG  HG2  sing N N 131 
GLN   CG  HG3  sing N N 132 
GLN   CD  OE1  doub N N 133 
GLN   CD  NE2  sing N N 134 
GLN   NE2 HE21 sing N N 135 
GLN   NE2 HE22 sing N N 136 
GLN   OXT HXT  sing N N 137 
GLU   N   CA   sing N N 138 
GLU   N   H    sing N N 139 
GLU   N   H2   sing N N 140 
GLU   CA  C    sing N N 141 
GLU   CA  CB   sing N N 142 
GLU   CA  HA   sing N N 143 
GLU   C   O    doub N N 144 
GLU   C   OXT  sing N N 145 
GLU   CB  CG   sing N N 146 
GLU   CB  HB2  sing N N 147 
GLU   CB  HB3  sing N N 148 
GLU   CG  CD   sing N N 149 
GLU   CG  HG2  sing N N 150 
GLU   CG  HG3  sing N N 151 
GLU   CD  OE1  doub N N 152 
GLU   CD  OE2  sing N N 153 
GLU   OE2 HE2  sing N N 154 
GLU   OXT HXT  sing N N 155 
GLY   N   CA   sing N N 156 
GLY   N   H    sing N N 157 
GLY   N   H2   sing N N 158 
GLY   CA  C    sing N N 159 
GLY   CA  HA2  sing N N 160 
GLY   CA  HA3  sing N N 161 
GLY   C   O    doub N N 162 
GLY   C   OXT  sing N N 163 
GLY   OXT HXT  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
SO4   S   O1   doub N N 326 
SO4   S   O2   doub N N 327 
SO4   S   O3   sing N N 328 
SO4   S   O4   sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
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                    7HHO 
_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]   0.023719 
_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]   0.006274 
_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  ? 1.001   4.353   2.325   1.00 52.54  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.072  3.518   1.725   1.00 61.16  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.517   2.439   0.810   1.00 58.55  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.633   2.569   0.307   1.00 54.94  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.097  4.386   0.981   1.00 70.38  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.064  5.129   1.900   1.00 85.58  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.437  4.218   2.648   1.00 78.46  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -3.690  5.188   4.142   1.00 81.24  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.210  1.313   0.609   1.00 51.50  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.191   0.252   -0.328  1.00 50.24  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.457   0.599   -1.797  1.00 46.14  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.244  1.392   -2.423  1.00 47.92  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.013  -0.753  -0.180  1.00 46.18  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.487  -0.533  1.256   1.00 49.57  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.445  0.978   1.347   1.00 47.52  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.464   -0.059  -2.362  1.00 39.09  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.697   0.023   -3.792  1.00 41.77  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 1.080   -1.235  -4.391  1.00 38.38  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.563   -2.075  -3.652  1.00 38.70  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 3.203   0.200   -4.047  1.00 48.83  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.743   1.532   -3.597  1.00 59.63  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.871   1.906   -2.275  1.00 65.93  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.167   2.592   -4.311  1.00 66.35  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.359   3.141   -2.204  1.00 65.73  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.546   3.577   -3.430  1.00 64.93  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 1.118   -1.361  -5.717  1.00 32.80  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.927   -2.655  -6.351  1.00 32.21  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 2.045   -3.635  -5.982  1.00 29.45  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 3.143   -3.250  -5.574  1.00 29.50  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.828   -2.469  -7.852  1.00 39.75  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.757   -4.923  -6.158  1.00 27.37  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.771   -5.942  -5.965  1.00 30.44  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.933   -5.702  -6.935  1.00 32.01  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.714   -5.235  -8.062  1.00 29.33  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 2.155   -7.341  -6.058  1.00 26.98  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.419   -7.729  -4.776  1.00 29.75  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 2.131   -7.973  -3.585  1.00 26.70  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? 0.021   -7.852  -4.752  1.00 28.41  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.478   -8.314  -2.398  1.00 27.16  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.620  -8.244  -3.573  1.00 24.01  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? 0.087   -8.433  -2.404  1.00 28.35  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 5.160   -5.996  -6.464  1.00 25.19  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.313   -5.945  -7.342  1.00 27.16  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 7.211   -7.145  -7.032  1.00 26.04  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 7.198   -7.710  -5.938  1.00 26.24  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 7.047   -4.613  -7.149  1.00 29.63  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.612   -4.454  -5.745  1.00 31.97  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.321   -3.123  -5.464  1.00 40.97  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 9.032   -3.144  -4.128  1.00 40.19  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 8.076   -3.170  -3.012  1.00 37.70  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 8.066   -7.553  -7.978  1.00 27.39  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 9.033   -8.627  -7.712  1.00 27.79  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.823   -8.322  -6.444  1.00 26.94  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.282  -7.189  -6.243  1.00 26.55  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.913   -8.524  -8.989  1.00 29.09  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.920   -8.070  -10.069 1.00 30.79  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 8.197   -6.953  -9.325  1.00 30.34  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 10.032  -9.377  -5.635  1.00 23.90  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.732  -9.277  -4.378  1.00 22.60  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.776   -9.205  -3.191  1.00 24.38  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 10.170  -9.503  -2.056  1.00 24.97  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.510   -8.804  -3.426  1.00 22.64  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.603   -8.708  -2.287  1.00 20.97  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.370   -10.076 -1.639  1.00 20.07  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.228   -11.066 -2.340  1.00 20.83  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.261   -8.128  -2.713  1.00 23.58  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.262   -6.622  -2.899  1.00 26.97  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 7.253   -5.959  -2.455  1.00 25.20  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.295   -6.121  -3.499  1.00 24.79  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.289   -10.127 -0.291  1.00 20.66  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 7.117   -11.404 0.395   1.00 21.42  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.653   -11.484 0.787   1.00 23.71  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 5.087   -10.465 1.240   1.00 23.62  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 8.006   -11.457 1.630   1.00 21.65  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.499   -11.245 1.302   1.00 21.75  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.341  -11.294 2.587   1.00 25.92  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.958   -12.292 0.256   1.00 22.03  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 5.089   -12.701 0.692   1.00 23.65  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.651   -12.868 0.919   1.00 20.54  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.392   -14.232 1.546   1.00 25.72  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.263   -15.114 1.572   1.00 22.66  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.832   -12.763 -0.383  1.00 22.03  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.986   -11.367 -0.985  1.00 21.86  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 3.224   -13.870 -1.387  1.00 23.26  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 2.157   -14.423 2.015   1.00 23.39  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.631   -15.773 2.020   1.00 23.53  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.631   -15.867 0.873   1.00 26.81  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.189  -14.964 0.683   1.00 24.34  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.848   -16.146 3.291   1.00 24.15  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.750   -16.253 4.506   1.00 26.11  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 2.137   -15.123 5.222   1.00 27.09  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.220   -17.500 4.907   1.00 25.44  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 3.007   -15.243 6.296   1.00 35.00  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 3.100   -17.620 5.981   1.00 29.79  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.483   -16.498 6.675   1.00 29.35  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.704   -16.986 0.137   1.00 25.16  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.057  -17.133 -1.083  1.00 25.62  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.026  -18.304 -0.917  1.00 28.35  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.670  -19.366 -0.400  1.00 27.52  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.846   -17.293 -2.316  1.00 23.73  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.258  -18.074 -1.366  1.00 26.45  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.347  -19.003 -1.082  1.00 27.60  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.698  -19.716 -2.379  1.00 27.37  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.082  -19.079 -3.354  1.00 29.95  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.583  -18.327 -0.466  1.00 27.25  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.677  -19.359 -0.064  1.00 31.16  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.186  -20.321 1.019   1.00 31.41  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.258  -21.181 1.694   1.00 35.27  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.829  -22.129 0.728   1.00 34.92  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.614  -21.048 -2.324  1.00 30.39  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.131  -21.909 -3.365  1.00 31.36  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.209  -22.826 -2.770  1.00 35.24  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.102  -23.257 -1.624  1.00 29.38  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -2.999  -22.849 -3.775  1.00 35.98  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -2.986  -23.023 -5.259  1.00 61.46  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.697  -21.958 -5.924  1.00 45.12  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -0.893  -23.452 -6.501  1.00 44.39  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.213  -23.158 -3.580  1.00 39.52  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.284  -24.078 -3.204  1.00 40.18  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.711  -25.355 -2.628  1.00 40.53  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.816  -25.962 -3.220  1.00 41.51  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -7.989  -24.535 -4.486  1.00 53.59  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.437  -24.986 -4.321  1.00 61.87  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.337 -23.898 -3.740  1.00 70.34  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.224  -25.761 -1.461  1.00 40.56  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -6.839  -27.047 -0.918  1.00 37.61  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -5.533  -26.986 -0.132  1.00 45.46  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -5.091  -27.986 0.422   1.00 53.25  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -4.916  -25.804 -0.038  1.00 41.78  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -3.665  -25.756 0.687   1.00 35.33  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -3.696  -24.598 1.654   1.00 33.06  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -4.387  -23.619 1.397   1.00 32.75  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.575  -25.308 -0.282  1.00 43.39  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -2.162  -26.297 -1.352  1.00 41.29  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -1.135  -27.196 -1.117  1.00 49.67  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -2.738  -26.274 -2.619  1.00 44.56  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -0.720  -28.078 -2.102  1.00 55.66  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -2.331  -27.154 -3.614  1.00 49.46  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -1.306  -28.048 -3.356  1.00 55.66  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -0.875  -28.929 -4.318  1.00 72.41  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -2.913  -24.641 2.753   1.00 30.13  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -2.920  -23.545 3.726   1.00 33.46  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.184  -22.368 3.073   1.00 31.65  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -1.445  -22.591 2.128   1.00 30.76  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -2.174  -24.132 4.939   1.00 36.08  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.311  -25.236 4.342   1.00 37.34  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -1.980  -25.743 3.077   1.00 35.98  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -2.438  -21.148 3.535   1.00 28.90  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -1.693  -19.959 3.139   1.00 28.55  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.186  -20.232 3.260   1.00 29.36  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? 0.285   -20.620 4.340   1.00 29.17  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.112  -18.781 4.017   1.00 29.61  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -3.560  -18.404 3.872   1.00 28.82  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -4.549  -19.090 4.550   1.00 30.96  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.190  -17.440 3.142   1.00 28.91  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -5.727  -18.542 4.270   1.00 32.07  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -5.538  -17.528 3.427   1.00 31.56  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? 0.563   -20.040 2.157   1.00 28.80  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.897   -20.628 2.025   1.00 25.50  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.979   -19.545 1.869   1.00 24.75  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.826   -18.653 1.054   1.00 24.38  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.933   -21.525 0.789   1.00 26.00  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 3.017   -22.568 0.843   1.00 29.72  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 4.358   -22.403 0.639   1.00 28.50  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.820   -23.965 1.136   1.00 30.95  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 5.011   -23.611 0.770   1.00 29.45  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 4.090   -24.586 1.057   1.00 31.96  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.696   -24.755 1.414   1.00 35.48  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 4.271   -25.953 1.296   1.00 36.12  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.877   -26.110 1.619   1.00 34.93  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 3.145   -26.699 1.573   1.00 37.61  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 4.120   -19.598 2.602   1.00 24.35  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 5.156   -18.571 2.438   1.00 22.03  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.635   -18.562 0.990   1.00 20.92  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 5.920   -19.627 0.420   1.00 25.04  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 6.243   -19.048 3.456   1.00 24.10  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 6.038   -20.570 3.601   1.00 23.37  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 4.466   -20.592 3.623   1.00 24.04  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.718   -17.360 0.405   1.00 20.73  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 6.054   -17.196 -1.004  1.00 21.45  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.588   -15.796 -1.291  1.00 20.04  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.608   -14.921 -0.422  1.00 21.58  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.864   -17.512 -1.905  1.00 22.71  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 7.060   -15.626 -2.528  1.00 21.84  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 7.513   -14.322 -2.974  1.00 21.70  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 6.983   -14.087 -4.378  1.00 22.25  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.653   -15.035 -5.093  1.00 23.32  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 9.033   -14.275 -2.933  1.00 20.61  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.708   -15.094 -4.030  1.00 20.90  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 11.269  -14.869 -3.886  1.00 20.97  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 12.003  -15.677 -4.888  1.00 24.62  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 13.255  -16.133 -4.743  1.00 25.23  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.904  -15.974 -3.581  1.00 24.44  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.815  -16.824 -5.735  1.00 24.51  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.907   -12.816 -4.748  1.00 22.21  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.659   -12.454 -6.131  1.00 23.88  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 7.986   -12.551 -6.861  1.00 25.48  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.957   -11.911 -6.439  1.00 27.04  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 6.158   -11.002 -6.245  1.00 25.48  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 5.026   -10.662 -5.248  1.00 31.94  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.801   -10.664 -7.709  1.00 23.52  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.674   -11.196 -5.655  1.00 35.58  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 8.007   -13.340 -7.934  1.00 25.78  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 9.239   -13.484 -8.703  1.00 29.82  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 9.320   -12.458 -9.825  1.00 28.52  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 8.333   -11.824 -10.214 1.00 27.29  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 9.413   -14.857 -9.317  1.00 27.41  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 10.310  -15.807 -8.546  1.00 31.32  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.895  -15.400 -7.526  1.00 33.29  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 10.418  -16.947 -8.966  1.00 28.42  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.555  -12.284 -10.327 1.00 31.64  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.776  -11.622 -11.591 1.00 33.29  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.433  -12.605 -12.713 1.00 31.69  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.285  -13.802 -12.492 1.00 31.51  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 12.242  -11.214 -11.705 1.00 38.08  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.620  -9.904  -11.024 1.00 44.35  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 12.177  -8.837  -11.510 1.00 47.99  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 13.347  -9.962  -10.003 1.00 51.73  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 10.325  -12.105 -13.941 1.00 34.89  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 10.330  -13.001 -15.096 1.00 39.55  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.662  -12.765 -15.811 1.00 38.13  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 11.937  -11.625 -16.174 1.00 35.06  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 9.157   -12.625 -16.022 1.00 41.47  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.799   -12.707 -15.291 1.00 40.47  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 9.185   -13.448 -17.317 1.00 38.78  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.843   -11.580 -15.651 1.00 41.62  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 12.477  -13.822 -15.948 1.00 39.22  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.754  -13.788 -16.661 1.00 34.27  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.500  -13.476 -18.138 1.00 32.44  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.447  -13.813 -18.705 1.00 34.21  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.462  -15.129 -16.527 1.00 33.83  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.448  -12.758 -18.744 1.00 34.95  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.502  -12.639 -20.195 1.00 34.59  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 14.292  -13.997 -20.847 1.00 29.96  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 14.945  -14.976 -20.491 1.00 34.70  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.807  -11.985 -20.629 1.00 34.53  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 15.839  -10.483 -20.396 1.00 36.43  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 14.756  -9.895  -20.284 1.00 41.62  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 16.945  -9.923  -20.333 1.00 39.71  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.344  -14.018 -21.789 1.00 34.00  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 13.054  -15.151 -22.655 1.00 34.40  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 12.195  -16.227 -21.995 1.00 38.91  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 11.944  -17.256 -22.615 1.00 39.18  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.803  -16.011 -20.728 1.00 36.51  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 11.014  -17.007 -20.013 1.00 34.92  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.519   -16.697 -20.201 1.00 32.93  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 9.151   -15.589 -20.596 1.00 33.72  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 11.414  -16.974 -18.534 1.00 35.25  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.665   -17.690 -19.892 1.00 40.04  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 7.206   -17.632 -20.013 1.00 39.87  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.618   -16.582 -19.067 1.00 35.33  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 6.904   -16.600 -17.874 1.00 38.20  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.624   -19.020 -19.660 1.00 40.43  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 5.104   -18.985 -19.620 1.00 40.53  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 7.107   -20.108 -20.612 1.00 43.94  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.800   -15.684 -19.623 1.00 35.11  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 5.138   -14.600 -18.911 1.00 38.38  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.846   -15.130 -18.286 1.00 41.09  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 3.299   -16.139 -18.734 1.00 36.29  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.816   -13.437 -19.855 1.00 40.14  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 6.006   -12.580 -20.295 1.00 46.32  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.713   -11.428 -21.265 1.00 52.32  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.305   -11.876 -22.646 1.00 46.79  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 4.919   -10.750 -23.500 1.00 48.20  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 3.325   -14.507 -17.206 1.00 42.21  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 2.067   -14.977 -16.613 1.00 42.09  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 0.894   -14.451 -17.433 1.00 38.41  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 1.028   -13.469 -18.152 1.00 37.61  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 2.075   -14.390 -15.189 1.00 36.79  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 2.994   -13.177 -15.272 1.00 42.97  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 3.894   -13.345 -16.509 1.00 42.88  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.318  -15.026 -17.297 1.00 39.27  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.507  -14.414 -17.896 1.00 40.74  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.660  -12.991 -17.383 1.00 43.85  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.072  -12.649 -16.356 1.00 39.37  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -2.682  -15.280 -17.444 1.00 40.66  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -2.069  -16.558 -16.928 1.00 36.46  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -0.613  -16.262 -16.552 1.00 41.55  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.462  -12.139 -18.067 1.00 43.13  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -2.801  -10.805 -17.563 1.00 47.51  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.348  -10.794 -16.136 1.00 40.55  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -4.088  -11.684 -15.731 1.00 41.91  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -3.836  -10.227 -18.567 1.00 48.54  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -4.151  -11.373 -19.507 1.00 42.58  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -3.074  -12.426 -19.383 1.00 50.20  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -2.948  -9.770  -15.384 1.00 39.49  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.397  -9.563  -14.020 1.00 43.09  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -2.872  -10.640 -13.064 1.00 36.48  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.265  -10.630 -11.898 1.00 36.62  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -4.913  -9.406  -13.982 1.00 49.76  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.335  -8.125  -14.665 1.00 57.50  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.100  -7.031  -14.134 1.00 56.14  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -5.939  -8.241  -15.834 1.00 50.47  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -2.029  -11.583 -13.540 1.00 32.13  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.457  -12.597 -12.653 1.00 26.78  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? 0.026   -12.288 -12.391 1.00 27.31  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.652   -11.513 -13.133 1.00 29.82  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -1.666  -14.042 -13.133 1.00 30.40  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -3.111  -14.602 -13.270 1.00 35.70  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -4.171  -13.909 -12.417 1.00 39.07  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -5.629  -14.398 -12.467 1.00 43.74  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -5.675  -15.865 -12.566 1.00 40.50  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? 0.548   -12.818 -11.269 1.00 23.05  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.942   -12.621 -10.883 1.00 26.55  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.605   -13.983 -10.832 1.00 25.50  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.973   -14.981 -10.490 1.00 24.64  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 2.099   -12.036 -9.470  1.00 24.87  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.635   -10.594 -9.472  1.00 27.79  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? 0.283   -10.303 -9.404  1.00 34.30  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 2.529   -9.529  -9.594  1.00 30.95  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.171  -8.999  -9.466  1.00 35.27  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 2.090   -8.210  -9.658  1.00 34.34  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.728   -7.960  -9.577  1.00 33.17  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? 0.179   -6.715  -9.656  1.00 36.95  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.921   -14.087 -11.097 1.00 24.51  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 4.584   -15.374 -10.908 1.00 24.60  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.878   -15.499 -9.419  1.00 24.36  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 5.564   -14.635 -8.863  1.00 25.47  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.880   -15.257 -11.736 1.00 25.01  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 6.037   -13.811 -12.021 1.00 24.49  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.805   -12.999 -11.551 1.00 28.03  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 4.359   -16.551 -8.780  1.00 23.67  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 4.550   -16.727 -7.344  1.00 24.16  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 5.518   -17.893 -7.144  1.00 25.90  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 5.279   -18.994 -7.637  1.00 27.51  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 3.208   -16.992 -6.623  1.00 25.65  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 2.191   -15.866 -6.922  1.00 24.16  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 3.410   -17.196 -5.099  1.00 23.71  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.662   -14.435 -6.644  1.00 24.78  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.600   -17.660 -6.400  1.00 21.68  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 7.509   -18.734 -6.038  1.00 23.57  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 7.209   -19.130 -4.597  1.00 26.48  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 7.305   -18.296 -3.693  1.00 25.15  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 8.970   -18.236 -6.194  1.00 25.48  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 10.003  -19.271 -5.769  1.00 28.61  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 10.377  -20.284 -6.664  1.00 28.55  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 10.597  -19.235 -4.501  1.00 30.18  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 11.329  -21.233 -6.306  1.00 28.86  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 11.538  -20.211 -4.135  1.00 31.33  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.909  -21.193 -5.046  1.00 29.16  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.881   -20.416 -4.379  1.00 25.38  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 6.505   -20.926 -3.068  1.00 23.92  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.779   -21.461 -2.417  1.00 26.36  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 8.470   -22.338 -2.980  1.00 25.77  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 5.500   -22.082 -3.267  1.00 29.34  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 4.137   -21.602 -3.746  1.00 26.17  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.880   -21.422 -5.103  1.00 29.17  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 3.129   -21.288 -2.835  1.00 27.07  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 2.650   -20.927 -5.541  1.00 30.11  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 1.897   -20.805 -3.288  1.00 27.71  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 1.654   -20.640 -4.626  1.00 29.59  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 8.125   -20.870 -1.275  1.00 24.19  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 9.259   -21.353 -0.507  1.00 26.65  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 8.992   -22.801 -0.074  1.00 27.34  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.833   -23.256 0.005   1.00 26.29  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 9.422   -20.404 0.687   1.00 24.63  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 9.890   -19.009 0.302   1.00 24.33  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 11.159  -18.836 -0.240  1.00 25.18  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 9.134   -17.870 0.584   1.00 24.12  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 11.607  -17.571 -0.586  1.00 22.34  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 9.624   -16.598 0.260   1.00 22.96  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.867  -16.456 -0.302  1.00 23.47  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 10.079  -23.532 0.195   1.00 28.07  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 9.941   -24.910 0.643   1.00 29.96  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.749   -25.891 -0.518  1.00 35.70  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 10.655  -26.674 -0.795  1.00 34.44  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 8.596   -25.844 -1.207  1.00 34.04  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 8.372   -26.658 -2.400  1.00 34.63  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 9.199   -26.147 -3.572  1.00 38.83  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 9.542   -26.907 -4.484  1.00 33.05  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 6.893   -26.665 -2.803  1.00 36.45  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 6.572   -25.311 -3.106  1.00 35.60  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 5.973   -27.244 -1.750  1.00 33.64  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 9.458   -24.834 -3.594  1.00 29.66  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 10.165  -24.246 -4.719  1.00 32.52  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 9.349   -24.376 -6.003  1.00 32.33  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 9.925   -24.365 -7.092  1.00 31.31  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 11.605  -24.784 -4.865  1.00 30.96  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 12.321  -24.836 -3.572  1.00 35.29  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 13.164  -25.871 -3.237  1.00 32.98  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 12.346  -23.971 -2.536  1.00 30.48  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 13.624  -25.676 -2.005  1.00 40.81  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 13.179  -24.505 -1.579  1.00 39.10  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 8.018   -24.478 -5.891  1.00 32.65  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 7.180   -24.478 -7.089  1.00 32.45  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.737   -23.056 -7.442  1.00 36.78  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 6.846   -22.150 -6.609  1.00 31.76  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 5.953   -25.352 -6.844  1.00 36.17  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 6.330   -26.783 -6.484  1.00 41.78  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 5.171   -27.690 -6.110  1.00 49.65  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 3.992   -27.261 -6.096  1.00 54.47  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 5.493   -28.860 -5.820  1.00 56.02  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 6.293   -22.866 -8.695  1.00 30.37  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.805   -21.580 -9.174  1.00 29.94  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 4.366   -21.762 -9.620  1.00 30.62  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 4.021   -22.775 -10.226 1.00 35.21  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 6.650   -21.082 -10.345 1.00 34.81  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 7.939   -20.730 -9.859  1.00 33.55  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 6.124   -19.790 -10.958 1.00 35.40  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 3.523   -20.798 -9.278  1.00 31.10  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 2.206   -20.732 -9.869  1.00 28.93  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.894   -19.279 -10.170 1.00 27.76  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 2.583   -18.365 -9.700  1.00 26.61  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 1.169   -21.364 -8.965  1.00 30.23  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.841   -19.094 -10.968 1.00 26.44  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? 0.410   -17.771 -11.377 1.00 29.06  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -0.826  -17.389 -10.588 1.00 31.91  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -1.837  -18.103 -10.621 1.00 31.60  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? 0.108   -17.818 -12.883 1.00 33.80  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 1.353   -18.042 -13.724 1.00 35.46  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 2.480   -17.234 -13.545 1.00 41.82  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 1.403   -19.056 -14.686 1.00 41.15  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 3.638   -17.427 -14.307 1.00 47.63  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 2.570   -19.248 -15.443 1.00 39.39  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 3.671   -18.434 -15.264 1.00 39.55  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -0.732  -16.273 -9.854  1.00 26.51  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -1.821  -15.918 -8.953  1.00 26.16  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.109  -14.429 -9.036  1.00 27.72  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.225  -13.608 -9.364  1.00 26.27  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -1.507  -16.282 -7.500  1.00 24.85  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -1.449  -17.760 -7.111  1.00 25.70  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.176  -17.743 -5.602  1.00 26.88  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -2.822  -18.385 -7.376  1.00 29.93  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -3.376  -14.090 -8.745  1.00 24.34  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -3.791  -12.693 -8.692  1.00 23.99  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -3.826  -12.180 -7.249  1.00 22.02  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -3.717  -12.972 -6.307  1.00 23.63  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -3.896  -10.843 -7.038  1.00 22.31  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -3.845  -10.226 -5.698  1.00 24.20  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -4.803  -10.773 -4.642  1.00 25.90  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -4.484  -10.785 -3.457  1.00 23.71  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.179  -8.769  -5.998  1.00 23.83  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -3.623  -8.580  -7.420  1.00 26.19  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -4.016  -9.853  -8.123  1.00 24.49  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -5.973  -11.265 -5.086  1.00 27.80  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -6.928  -11.809 -4.127  1.00 26.81  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.352  -12.969 -3.319  1.00 25.89  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -6.843  -13.239 -2.209  1.00 25.37  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.240  -12.312 -4.743  1.00 30.28  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.110  -13.502 -5.658  1.00 32.24  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.495  -13.814 -6.230  1.00 37.20  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.456  -14.956 -7.190  1.00 39.80  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.100  -16.159 -6.428  1.00 46.82  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.310  -13.644 -3.858  1.00 25.63  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -4.746  -14.765 -3.145  1.00 24.13  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.376  -14.448 -2.519  1.00 23.96  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -2.670  -15.373 -2.088  1.00 22.91  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -4.685  -15.985 -4.055  1.00 27.27  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.071  -16.523 -4.408  1.00 31.24  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -6.912  -16.554 -3.480  1.00 32.13  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.302  -16.882 -5.582  1.00 30.93  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.044  -13.159 -2.427  1.00 23.27  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -1.711  -12.746 -1.974  1.00 21.36  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -1.849  -11.890 -0.709  1.00 18.95  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.416  -10.789 -0.731  1.00 22.68  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -1.010  -11.985 -3.112  1.00 21.11  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -0.945  -12.724 -4.456  1.00 22.71  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.159  -11.854 -5.436  1.00 25.33  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.163  -13.993 -4.311  1.00 22.49  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.291  -12.385 0.403   1.00 21.42  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.376  -11.664 1.680   1.00 23.19  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? 0.017   -11.175 2.064   1.00 24.91  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.919   -11.994 2.275   1.00 26.53  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -1.844  -12.671 2.732   1.00 20.52  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.284  -13.118 2.470   1.00 24.41  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -3.570  -14.032 1.450   1.00 25.94  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.339  -12.614 3.241   1.00 26.29  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -4.876  -14.428 1.176   1.00 29.44  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -5.654  -13.020 2.965   1.00 25.88  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -5.907  -13.940 1.973   1.00 26.10  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? 0.240   -9.854  2.193   1.00 27.13  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.565   -9.368  2.594   1.00 26.52  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 2.141   -10.015 3.855   1.00 28.10  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 1.447   -10.219 4.853   1.00 27.44  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 1.263   -7.849  2.730   1.00 29.30  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? 0.287   -7.605  1.568   1.00 30.49  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -0.691  -8.761  1.839   1.00 26.48  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 3.434   -10.387 3.783   1.00 28.69  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 4.023   -11.271 4.775   1.00 27.24  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 4.036   -10.602 6.157   1.00 25.85  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.631   -11.225 7.130   1.00 28.37  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 5.441   -11.673 4.323   1.00 29.34  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 6.205   -12.446 5.388   1.00 29.13  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.937   -13.791 5.630   1.00 31.01  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 7.217   -11.841 6.131   1.00 32.52  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.633   -14.517 6.595   1.00 31.18  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.911   -12.551 7.102   1.00 31.67  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.614   -13.878 7.337   1.00 32.90  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 8.306   -14.573 8.288   1.00 34.85  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 4.446   -9.335  6.222   1.00 28.04  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.619   -8.663  7.509   1.00 36.30  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 3.287   -8.618  8.246   1.00 35.87  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 3.208   -9.086  9.374   1.00 37.00  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 5.227   -7.276  7.372   1.00 35.25  ? 62  ASP   A CB  1 
ATOM   495  C CG  . ASP   A 1 63 ? 6.744   -7.232  7.206   1.00 58.37  ? 62  ASP   A CG  1 
ATOM   496  O OD1 . ASP   A 1 63 ? 7.419   -8.207  7.634   1.00 62.23  ? 62  ASP   A OD1 1 
ATOM   497  O OD2 . ASP   A 1 63 ? 7.251   -6.211  6.656   1.00 64.40  ? 62  ASP   A OD2 1 
ATOM   498  N N   . LYS   A 1 64 ? 2.230   -8.155  7.553   1.00 36.53  ? 63  LYS   A N   1 
ATOM   499  C CA  . LYS   A 1 64 ? 0.898   -8.101  8.156   1.00 35.39  ? 63  LYS   A CA  1 
ATOM   500  C C   . LYS   A 1 64 ? 0.360   -9.471  8.579   1.00 35.98  ? 63  LYS   A C   1 
ATOM   501  O O   . LYS   A 1 64 ? -0.397  -9.531  9.551   1.00 36.53  ? 63  LYS   A O   1 
ATOM   502  C CB  . LYS   A 1 64 ? -0.084  -7.464  7.167   1.00 38.18  ? 63  LYS   A CB  1 
ATOM   503  C CG  . LYS   A 1 64 ? -1.529  -7.277  7.663   1.00 42.42  ? 63  LYS   A CG  1 
ATOM   504  C CD  . LYS   A 1 64 ? -2.363  -6.513  6.639   1.00 38.24  ? 63  LYS   A CD  1 
ATOM   505  C CE  . LYS   A 1 64 ? -3.396  -5.698  7.356   1.00 41.09  ? 63  LYS   A CE  1 
ATOM   506  N NZ  . LYS   A 1 64 ? -4.522  -6.500  7.805   1.00 46.30  ? 63  LYS   A NZ  1 
ATOM   507  N N   . SER   A 1 65 ? 0.697   -10.563 7.859   1.00 29.03  ? 64  SER   A N   1 
ATOM   508  C CA  . SER   A 1 65 ? -0.033  -11.827 7.984   1.00 28.87  ? 64  SER   A CA  1 
ATOM   509  C C   . SER   A 1 65 ? 0.722   -12.903 8.767   1.00 32.47  ? 64  SER   A C   1 
ATOM   510  O O   . SER   A 1 65 ? 0.186   -13.991 8.960   1.00 31.60  ? 64  SER   A O   1 
ATOM   511  C CB  . SER   A 1 65 ? -0.371  -12.410 6.608   1.00 30.19  ? 64  SER   A CB  1 
ATOM   512  O OG  . SER   A 1 65 ? -1.279  -11.558 5.919   1.00 41.95  ? 64  SER   A OG  1 
ATOM   513  N N   . LYS   A 1 66 ? 1.992   -12.676 9.121   1.00 31.07  ? 65  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66 ? 2.812   -13.792 9.585   1.00 31.97  ? 65  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66 ? 2.358   -14.315 10.950  1.00 32.57  ? 65  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66 ? 2.477   -15.512 11.219  1.00 35.28  ? 65  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66 ? 4.295   -13.391 9.600   1.00 34.01  ? 65  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66 ? 4.696   -12.233 10.472  1.00 35.59  ? 65  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66 ? 6.207   -12.122 10.275  1.00 53.56  ? 65  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66 ? 6.876   -11.052 11.091  1.00 58.06  ? 65  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66 ? 6.493   -9.701  10.665  1.00 61.19  ? 65  LYS   A NZ  1 
ATOM   522  N N   A ASP   A 1 67 ? 1.797   -13.416 11.774  0.50 36.88  ? 66  ASP   A N   1 
ATOM   523  N N   B ASP   A 1 67 ? 1.866   -13.420 11.816  0.50 36.98  ? 66  ASP   A N   1 
ATOM   524  C CA  A ASP   A 1 67 ? 1.276   -13.745 13.097  0.50 38.64  ? 66  ASP   A CA  1 
ATOM   525  C CA  B ASP   A 1 67 ? 1.301   -13.854 13.088  0.50 38.51  ? 66  ASP   A CA  1 
ATOM   526  C C   A ASP   A 1 67 ? 0.075   -14.693 13.010  0.50 41.18  ? 66  ASP   A C   1 
ATOM   527  C C   B ASP   A 1 67 ? 0.292   -14.971 12.824  0.50 40.46  ? 66  ASP   A C   1 
ATOM   528  O O   A ASP   A 1 67 ? -0.248  -15.377 13.979  0.50 43.75  ? 66  ASP   A O   1 
ATOM   529  O O   B ASP   A 1 67 ? 0.338   -16.038 13.442  0.50 37.86  ? 66  ASP   A O   1 
ATOM   530  C CB  A ASP   A 1 67 ? 0.952   -12.495 13.909  0.50 40.14  ? 66  ASP   A CB  1 
ATOM   531  C CB  B ASP   A 1 67 ? 0.654   -12.703 13.851  0.50 42.81  ? 66  ASP   A CB  1 
ATOM   532  C CG  A ASP   A 1 67 ? 2.133   -11.797 14.572  0.50 43.39  ? 66  ASP   A CG  1 
ATOM   533  C CG  B ASP   A 1 67 ? 0.137   -13.035 15.246  0.50 48.64  ? 66  ASP   A CG  1 
ATOM   534  O OD1 A ASP   A 1 67 ? 3.241   -12.376 14.564  0.50 43.65  ? 66  ASP   A OD1 1 
ATOM   535  O OD1 B ASP   A 1 67 ? 0.970   -13.148 16.174  0.50 48.63  ? 66  ASP   A OD1 1 
ATOM   536  O OD2 A ASP   A 1 67 ? 1.946   -10.672 15.090  0.50 43.80  ? 66  ASP   A OD2 1 
ATOM   537  O OD2 B ASP   A 1 67 ? -1.098  -13.203 15.395  0.50 52.48  ? 66  ASP   A OD2 1 
ATOM   538  N N   . LYS   A 1 68 ? -0.596  -14.734 11.854  1.00 37.16  ? 67  LYS   A N   1 
ATOM   539  C CA  . LYS   A 1 68 ? -1.708  -15.638 11.654  1.00 33.24  ? 67  LYS   A CA  1 
ATOM   540  C C   . LYS   A 1 68 ? -1.266  -16.890 10.901  1.00 34.33  ? 67  LYS   A C   1 
ATOM   541  O O   . LYS   A 1 68 ? -1.753  -17.987 11.176  1.00 38.61  ? 67  LYS   A O   1 
ATOM   542  C CB  . LYS   A 1 68 ? -2.775  -14.852 10.877  1.00 36.76  ? 67  LYS   A CB  1 
ATOM   543  C CG  . LYS   A 1 68 ? -4.037  -15.635 10.592  1.00 40.21  ? 67  LYS   A CG  1 
ATOM   544  C CD  . LYS   A 1 68 ? -5.125  -14.715 10.035  1.00 41.24  ? 67  LYS   A CD  1 
ATOM   545  C CE  . LYS   A 1 68 ? -6.458  -15.377 9.861   1.00 50.22  ? 67  LYS   A CE  1 
ATOM   546  N NZ  . LYS   A 1 68 ? -7.410  -14.487 9.188   1.00 47.97  ? 67  LYS   A NZ  1 
ATOM   547  N N   . TYR   A 1 69 ? -0.389  -16.733 9.898   1.00 33.56  ? 68  TYR   A N   1 
ATOM   548  C CA  . TYR   A 1 69 ? -0.162  -17.821 8.964   1.00 28.57  ? 68  TYR   A CA  1 
ATOM   549  C C   . TYR   A 1 69 ? 1.224   -18.463 9.117   1.00 28.15  ? 68  TYR   A C   1 
ATOM   550  O O   . TYR   A 1 69 ? 1.459   -19.521 8.546   1.00 30.52  ? 68  TYR   A O   1 
ATOM   551  C CB  . TYR   A 1 69 ? -0.335  -17.397 7.501   1.00 27.37  ? 68  TYR   A CB  1 
ATOM   552  C CG  . TYR   A 1 69 ? -1.734  -16.920 7.130   1.00 32.81  ? 68  TYR   A CG  1 
ATOM   553  C CD1 . TYR   A 1 69 ? -2.879  -17.659 7.474   1.00 31.86  ? 68  TYR   A CD1 1 
ATOM   554  C CD2 . TYR   A 1 69 ? -1.904  -15.734 6.424   1.00 31.67  ? 68  TYR   A CD2 1 
ATOM   555  C CE1 . TYR   A 1 69 ? -4.146  -17.220 7.115   1.00 37.14  ? 68  TYR   A CE1 1 
ATOM   556  C CE2 . TYR   A 1 69 ? -3.169  -15.284 6.061   1.00 33.07  ? 68  TYR   A CE2 1 
ATOM   557  C CZ  . TYR   A 1 69 ? -4.284  -16.027 6.417   1.00 33.92  ? 68  TYR   A CZ  1 
ATOM   558  O OH  . TYR   A 1 69 ? -5.521  -15.580 6.058   1.00 35.47  ? 68  TYR   A OH  1 
ATOM   559  N N   . GLY   A 1 70 ? 2.126   -17.828 9.852   1.00 31.98  ? 69  GLY   A N   1 
ATOM   560  C CA  . GLY   A 1 70 ? 3.493   -18.325 9.928   1.00 32.01  ? 69  GLY   A CA  1 
ATOM   561  C C   . GLY   A 1 70 ? 3.684   -19.289 11.103  1.00 34.38  ? 69  GLY   A C   1 
ATOM   562  O O   . GLY   A 1 70 ? 4.445   -19.004 12.002  1.00 40.08  ? 69  GLY   A O   1 
ATOM   563  N N   . LYS   A 1 71 ? 2.943   -20.394 11.100  1.00 39.30  ? 70  LYS   A N   1 
ATOM   564  C CA  . LYS   A 1 71 ? 3.061   -21.415 12.122  1.00 44.29  ? 70  LYS   A CA  1 
ATOM   565  C C   . LYS   A 1 71 ? 3.353   -22.730 11.417  1.00 42.18  ? 70  LYS   A C   1 
ATOM   566  O O   . LYS   A 1 71 ? 3.003   -22.901 10.246  1.00 39.16  ? 70  LYS   A O   1 
ATOM   567  C CB  . LYS   A 1 71 ? 1.806   -21.529 12.994  1.00 49.77  ? 70  LYS   A CB  1 
ATOM   568  C CG  . LYS   A 1 71 ? 1.693   -20.493 14.099  1.00 51.76  ? 70  LYS   A CG  1 
ATOM   569  C CD  . LYS   A 1 71 ? 0.564   -19.513 13.834  1.00 56.57  ? 70  LYS   A CD  1 
ATOM   570  C CE  . LYS   A 1 71 ? -0.060  -19.008 15.098  1.00 63.77  ? 70  LYS   A CE  1 
ATOM   571  N NZ  . LYS   A 1 71 ? -1.466  -18.665 14.847  1.00 66.37  ? 70  LYS   A NZ  1 
ATOM   572  N N   . PRO   A 1 72 ? 4.051   -23.684 12.070  1.00 42.41  ? 71  PRO   A N   1 
ATOM   573  C CA  . PRO   A 1 72 ? 4.358   -24.957 11.414  1.00 39.34  ? 71  PRO   A CA  1 
ATOM   574  C C   . PRO   A 1 72 ? 3.138   -25.724 10.924  1.00 38.56  ? 71  PRO   A C   1 
ATOM   575  O O   . PRO   A 1 72 ? 2.042   -25.570 11.449  1.00 44.50  ? 71  PRO   A O   1 
ATOM   576  C CB  . PRO   A 1 72 ? 5.171   -25.730 12.466  1.00 41.91  ? 71  PRO   A CB  1 
ATOM   577  C CG  . PRO   A 1 72 ? 5.761   -24.628 13.310  1.00 47.33  ? 71  PRO   A CG  1 
ATOM   578  C CD  . PRO   A 1 72 ? 4.681   -23.539 13.392  1.00 42.79  ? 71  PRO   A CD  1 
ATOM   579  N N   . ASN   A 1 73 ? 3.356   -26.559 9.913   1.00 40.98  ? 72  ASN   A N   1 
ATOM   580  C CA  . ASN   A 1 73 ? 2.280   -27.207 9.194   1.00 48.43  ? 72  ASN   A CA  1 
ATOM   581  C C   . ASN   A 1 73 ? 2.835   -28.541 8.737   1.00 53.30  ? 72  ASN   A C   1 
ATOM   582  O O   . ASN   A 1 73 ? 4.030   -28.662 8.476   1.00 57.44  ? 72  ASN   A O   1 
ATOM   583  C CB  . ASN   A 1 73 ? 1.830   -26.330 8.027   1.00 49.97  ? 72  ASN   A CB  1 
ATOM   584  C CG  . ASN   A 1 73 ? 0.547   -26.781 7.368   1.00 61.89  ? 72  ASN   A CG  1 
ATOM   585  O OD1 . ASN   A 1 73 ? 0.550   -27.705 6.545   1.00 58.03  ? 72  ASN   A OD1 1 
ATOM   586  N ND2 . ASN   A 1 73 ? -0.552  -26.099 7.658   1.00 63.00  ? 72  ASN   A ND2 1 
ATOM   587  N N   . LYS   A 1 74 ? 1.951   -29.531 8.657   1.00 51.74  ? 73  LYS   A N   1 
ATOM   588  C CA  . LYS   A 1 74 ? 2.341   -30.898 8.386   1.00 51.38  ? 73  LYS   A CA  1 
ATOM   589  C C   . LYS   A 1 74 ? 2.709   -31.069 6.911   1.00 53.18  ? 73  LYS   A C   1 
ATOM   590  O O   . LYS   A 1 74 ? 3.363   -32.047 6.553   1.00 58.37  ? 73  LYS   A O   1 
ATOM   591  C CB  . LYS   A 1 74 ? 1.198   -31.789 8.905   1.00 54.21  ? 73  LYS   A CB  1 
ATOM   592  C CG  . LYS   A 1 74 ? 0.034   -32.076 7.944   1.00 57.97  ? 73  LYS   A CG  1 
ATOM   593  N N   . ARG   A 1 75 ? 2.307   -30.123 6.050   1.00 45.29  ? 74  ARG   A N   1 
ATOM   594  C CA  . ARG   A 1 75 ? 2.407   -30.325 4.611   1.00 47.66  ? 74  ARG   A CA  1 
ATOM   595  C C   . ARG   A 1 75 ? 3.862   -30.289 4.131   1.00 43.65  ? 74  ARG   A C   1 
ATOM   596  O O   . ARG   A 1 75 ? 4.658   -29.481 4.601   1.00 36.69  ? 74  ARG   A O   1 
ATOM   597  C CB  . ARG   A 1 75 ? 1.538   -29.312 3.850   1.00 50.98  ? 74  ARG   A CB  1 
ATOM   598  C CG  . ARG   A 1 75 ? 0.058   -29.441 4.177   1.00 53.82  ? 74  ARG   A CG  1 
ATOM   599  C CD  . ARG   A 1 75 ? -0.578  -30.646 3.494   1.00 47.12  ? 74  ARG   A CD  1 
ATOM   600  N NE  . ARG   A 1 75 ? -1.182  -30.338 2.195   1.00 61.51  ? 74  ARG   A NE  1 
ATOM   601  C CZ  . ARG   A 1 75 ? -2.330  -29.673 2.044   1.00 65.04  ? 74  ARG   A CZ  1 
ATOM   602  N NH1 . ARG   A 1 75 ? -2.778  -29.410 0.826   1.00 68.66  ? 74  ARG   A NH1 1 
ATOM   603  N NH2 . ARG   A 1 75 ? -3.021  -29.269 3.104   1.00 57.87  ? 74  ARG   A NH2 1 
ATOM   604  N N   . LYS   A 1 76 ? 4.167   -31.168 3.162   1.00 39.44  ? 75  LYS   A N   1 
ATOM   605  C CA  . LYS   A 1 76 ? 5.489   -31.315 2.575   1.00 38.44  ? 75  LYS   A CA  1 
ATOM   606  C C   . LYS   A 1 76 ? 6.005   -29.936 2.171   1.00 36.50  ? 75  LYS   A C   1 
ATOM   607  O O   . LYS   A 1 76 ? 5.404   -29.257 1.330   1.00 32.13  ? 75  LYS   A O   1 
ATOM   608  C CB  . LYS   A 1 76 ? 5.426   -32.252 1.364   1.00 41.37  ? 75  LYS   A CB  1 
ATOM   609  C CG  . LYS   A 1 76 ? 6.721   -32.535 0.616   1.00 49.14  ? 75  LYS   A CG  1 
ATOM   610  C CD  . LYS   A 1 76 ? 6.582   -33.676 -0.391  1.00 53.27  ? 75  LYS   A CD  1 
ATOM   611  C CE  . LYS   A 1 76 ? 7.828   -33.910 -1.195  1.00 62.72  ? 75  LYS   A CE  1 
ATOM   612  N N   . GLY   A 1 77 ? 7.103   -29.519 2.804   1.00 38.89  ? 76  GLY   A N   1 
ATOM   613  C CA  . GLY   A 1 77 ? 7.833   -28.360 2.313   1.00 36.69  ? 76  GLY   A CA  1 
ATOM   614  C C   . GLY   A 1 77 ? 7.515   -27.088 3.089   1.00 36.47  ? 76  GLY   A C   1 
ATOM   615  O O   . GLY   A 1 77 ? 8.267   -26.119 2.990   1.00 36.81  ? 76  GLY   A O   1 
ATOM   616  N N   . PHE   A 1 78 ? 6.467   -27.126 3.921   1.00 33.33  ? 77  PHE   A N   1 
ATOM   617  C CA  . PHE   A 1 78 ? 5.986   -25.912 4.558   1.00 33.98  ? 77  PHE   A CA  1 
ATOM   618  C C   . PHE   A 1 78 ? 6.988   -25.331 5.557   1.00 36.51  ? 77  PHE   A C   1 
ATOM   619  O O   . PHE   A 1 78 ? 7.204   -24.111 5.634   1.00 31.45  ? 77  PHE   A O   1 
ATOM   620  C CB  . PHE   A 1 78 ? 4.610   -26.208 5.154   1.00 29.62  ? 77  PHE   A CB  1 
ATOM   621  C CG  . PHE   A 1 78 ? 3.856   -24.942 5.512   1.00 31.76  ? 77  PHE   A CG  1 
ATOM   622  C CD1 . PHE   A 1 78 ? 4.082   -24.291 6.717   1.00 31.66  ? 77  PHE   A CD1 1 
ATOM   623  C CD2 . PHE   A 1 78 ? 2.931   -24.399 4.628   1.00 33.77  ? 77  PHE   A CD2 1 
ATOM   624  C CE1 . PHE   A 1 78 ? 3.401   -23.128 7.032   1.00 35.12  ? 77  PHE   A CE1 1 
ATOM   625  C CE2 . PHE   A 1 78 ? 2.262   -23.223 4.944   1.00 28.61  ? 77  PHE   A CE2 1 
ATOM   626  C CZ  . PHE   A 1 78 ? 2.483   -22.611 6.159   1.00 29.98  ? 77  PHE   A CZ  1 
ATOM   627  N N   . ASN   A 1 79 ? 7.557   -26.208 6.388   1.00 37.00  ? 78  ASN   A N   1 
ATOM   628  C CA  . ASN   A 1 79 ? 8.428   -25.755 7.468   1.00 37.44  ? 78  ASN   A CA  1 
ATOM   629  C C   . ASN   A 1 79 ? 9.752   -25.255 6.879   1.00 31.41  ? 78  ASN   A C   1 
ATOM   630  O O   . ASN   A 1 79 ? 10.314  -24.257 7.350   1.00 38.25  ? 78  ASN   A O   1 
ATOM   631  C CB  . ASN   A 1 79 ? 8.500   -26.820 8.567   1.00 35.67  ? 78  ASN   A CB  1 
ATOM   632  C CG  . ASN   A 1 79 ? 7.143   -27.047 9.210   1.00 44.64  ? 78  ASN   A CG  1 
ATOM   633  O OD1 . ASN   A 1 79 ? 6.226   -26.212 9.103   1.00 35.58  ? 78  ASN   A OD1 1 
ATOM   634  N ND2 . ASN   A 1 79 ? 6.999   -28.164 9.916   1.00 37.73  ? 78  ASN   A ND2 1 
ATOM   635  N N   . GLU   A 1 80 ? 10.247  -25.953 5.840   1.00 30.46  ? 79  GLU   A N   1 
ATOM   636  C CA  . GLU   A 1 80 ? 11.386  -25.447 5.093   1.00 32.85  ? 79  GLU   A CA  1 
ATOM   637  C C   . GLU   A 1 80 ? 11.075  -24.054 4.526   1.00 30.69  ? 79  GLU   A C   1 
ATOM   638  O O   . GLU   A 1 80 ? 11.910  -23.148 4.590   1.00 30.02  ? 79  GLU   A O   1 
ATOM   639  C CB  . GLU   A 1 80 ? 11.895  -26.408 4.023   1.00 29.71  ? 79  GLU   A CB  1 
ATOM   640  C CG  . GLU   A 1 80 ? 13.162  -25.920 3.321   1.00 30.18  ? 79  GLU   A CG  1 
ATOM   641  C CD  . GLU   A 1 80 ? 13.679  -26.953 2.312   1.00 42.57  ? 79  GLU   A CD  1 
ATOM   642  O OE1 . GLU   A 1 80 ? 13.035  -28.004 2.126   1.00 47.75  ? 79  GLU   A OE1 1 
ATOM   643  O OE2 . GLU   A 1 80 ? 14.712  -26.709 1.667   1.00 44.42  ? 79  GLU   A OE2 1 
ATOM   644  N N   . GLY   A 1 81 ? 9.874   -23.900 3.955   1.00 28.76  ? 80  GLY   A N   1 
ATOM   645  C CA  . GLY   A 1 81 ? 9.408   -22.616 3.435   1.00 28.88  ? 80  GLY   A CA  1 
ATOM   646  C C   . GLY   A 1 81 ? 9.404   -21.492 4.468   1.00 27.60  ? 80  GLY   A C   1 
ATOM   647  O O   . GLY   A 1 81 ? 9.782   -20.354 4.141   1.00 25.58  ? 80  GLY   A O   1 
ATOM   648  N N   . LEU   A 1 82 ? 8.970   -21.806 5.698   1.00 24.82  ? 81  LEU   A N   1 
ATOM   649  C CA  . LEU   A 1 82 ? 8.972   -20.846 6.779   1.00 26.86  ? 81  LEU   A CA  1 
ATOM   650  C C   . LEU   A 1 82 ? 10.397  -20.373 7.035   1.00 27.24  ? 81  LEU   A C   1 
ATOM   651  O O   . LEU   A 1 82 ? 10.590  -19.178 7.303   1.00 25.33  ? 81  LEU   A O   1 
ATOM   652  C CB  . LEU   A 1 82 ? 8.294   -21.300 8.076   1.00 28.74  ? 81  LEU   A CB  1 
ATOM   653  C CG  . LEU   A 1 82 ? 6.790   -21.594 7.958   1.00 33.36  ? 81  LEU   A CG  1 
ATOM   654  C CD1 . LEU   A 1 82 ? 6.348   -22.273 9.237   1.00 34.70  ? 81  LEU   A CD1 1 
ATOM   655  C CD2 . LEU   A 1 82 ? 5.919   -20.341 7.742   1.00 29.08  ? 81  LEU   A CD2 1 
ATOM   656  N N   . TRP   A 1 83 ? 11.373  -21.298 6.943   1.00 25.76  ? 82  TRP   A N   1 
ATOM   657  C CA  . TRP   A 1 83 ? 12.737  -20.917 7.283   1.00 28.77  ? 82  TRP   A CA  1 
ATOM   658  C C   . TRP   A 1 83 ? 13.266  -19.998 6.174   1.00 28.05  ? 82  TRP   A C   1 
ATOM   659  O O   . TRP   A 1 83 ? 13.972  -19.022 6.438   1.00 29.06  ? 82  TRP   A O   1 
ATOM   660  C CB  . TRP   A 1 83 ? 13.626  -22.173 7.486   1.00 30.23  ? 82  TRP   A CB  1 
ATOM   661  C CG  . TRP   A 1 83 ? 15.082  -21.843 7.730   1.00 27.88  ? 82  TRP   A CG  1 
ATOM   662  C CD1 . TRP   A 1 83 ? 15.706  -21.724 8.939   1.00 31.03  ? 82  TRP   A CD1 1 
ATOM   663  C CD2 . TRP   A 1 83 ? 16.052  -21.484 6.732   1.00 28.40  ? 82  TRP   A CD2 1 
ATOM   664  N NE1 . TRP   A 1 83 ? 17.015  -21.364 8.762   1.00 29.82  ? 82  TRP   A NE1 1 
ATOM   665  C CE2 . TRP   A 1 83 ? 17.252  -21.208 7.415   1.00 31.11  ? 82  TRP   A CE2 1 
ATOM   666  C CE3 . TRP   A 1 83 ? 16.020  -21.408 5.330   1.00 30.35  ? 82  TRP   A CE3 1 
ATOM   667  C CZ2 . TRP   A 1 83 ? 18.416  -20.847 6.739   1.00 29.52  ? 82  TRP   A CZ2 1 
ATOM   668  C CZ3 . TRP   A 1 83 ? 17.163  -21.028 4.660   1.00 33.20  ? 82  TRP   A CZ3 1 
ATOM   669  C CH2 . TRP   A 1 83 ? 18.347  -20.745 5.366   1.00 32.29  ? 82  TRP   A CH2 1 
ATOM   670  N N   . GLU   A 1 84 ? 12.925  -20.333 4.917   1.00 24.39  ? 83  GLU   A N   1 
ATOM   671  C CA  . GLU   A 1 84 ? 13.427  -19.588 3.778   1.00 25.71  ? 83  GLU   A CA  1 
ATOM   672  C C   . GLU   A 1 84 ? 12.918  -18.150 3.830   1.00 26.29  ? 83  GLU   A C   1 
ATOM   673  O O   . GLU   A 1 84 ? 13.668  -17.203 3.674   1.00 23.85  ? 83  GLU   A O   1 
ATOM   674  C CB  . GLU   A 1 84 ? 12.996  -20.300 2.489   1.00 25.32  ? 83  GLU   A CB  1 
ATOM   675  C CG  . GLU   A 1 84 ? 13.725  -21.638 2.340   1.00 26.78  ? 83  GLU   A CG  1 
ATOM   676  C CD  . GLU   A 1 84 ? 13.346  -22.365 1.057   1.00 32.10  ? 83  GLU   A CD  1 
ATOM   677  O OE1 . GLU   A 1 84 ? 12.416  -21.898 0.379   1.00 26.97  ? 83  GLU   A OE1 1 
ATOM   678  O OE2 . GLU   A 1 84 ? 13.973  -23.399 0.716   1.00 30.28  ? 83  GLU   A OE2 1 
ATOM   679  N N   . ILE   A 1 85 ? 11.617  -17.976 4.053   1.00 23.01  ? 84  ILE   A N   1 
ATOM   680  C CA  . ILE   A 1 85 ? 11.050  -16.635 3.948   1.00 22.43  ? 84  ILE   A CA  1 
ATOM   681  C C   . ILE   A 1 85 ? 11.614  -15.772 5.081   1.00 21.95  ? 84  ILE   A C   1 
ATOM   682  O O   . ILE   A 1 85 ? 11.767  -14.545 4.950   1.00 24.47  ? 84  ILE   A O   1 
ATOM   683  C CB  . ILE   A 1 85 ? 9.504   -16.665 3.952   1.00 20.91  ? 84  ILE   A CB  1 
ATOM   684  C CG1 . ILE   A 1 85 ? 8.935   -15.273 3.515   1.00 22.37  ? 84  ILE   A CG1 1 
ATOM   685  C CG2 . ILE   A 1 85 ? 8.955   -17.102 5.320   1.00 21.44  ? 84  ILE   A CG2 1 
ATOM   686  C CD1 . ILE   A 1 85 ? 7.475   -15.279 3.006   1.00 22.51  ? 84  ILE   A CD1 1 
ATOM   687  N N   . GLN   A 1 86 ? 11.900  -16.399 6.233   1.00 21.87  ? 85  GLN   A N   1 
ATOM   688  C CA  . GLN   A 1 86 ? 12.418  -15.628 7.358   1.00 26.77  ? 85  GLN   A CA  1 
ATOM   689  C C   . GLN   A 1 86 ? 13.925  -15.348 7.241   1.00 27.81  ? 85  GLN   A C   1 
ATOM   690  O O   . GLN   A 1 86 ? 14.383  -14.272 7.670   1.00 30.67  ? 85  GLN   A O   1 
ATOM   691  C CB  . GLN   A 1 86 ? 12.024  -16.371 8.646   1.00 27.79  ? 85  GLN   A CB  1 
ATOM   692  C CG  . GLN   A 1 86 ? 12.532  -15.739 9.934   1.00 36.24  ? 85  GLN   A CG  1 
ATOM   693  C CD  . GLN   A 1 86 ? 11.890  -16.347 11.176  1.00 48.09  ? 85  GLN   A CD  1 
ATOM   694  O OE1 . GLN   A 1 86 ? 11.698  -17.572 11.291  1.00 40.52  ? 85  GLN   A OE1 1 
ATOM   695  N NE2 . GLN   A 1 86 ? 11.524  -15.481 12.117  1.00 44.89  ? 85  GLN   A NE2 1 
ATOM   696  N N   . ASN   A 1 87 ? 14.695  -16.296 6.692   1.00 25.35  ? 86  ASN   A N   1 
ATOM   697  C CA  . ASN   A 1 87 ? 16.149  -16.298 6.809   1.00 26.17  ? 86  ASN   A CA  1 
ATOM   698  C C   . ASN   A 1 87 ? 16.892  -15.909 5.521   1.00 26.99  ? 86  ASN   A C   1 
ATOM   699  O O   . ASN   A 1 87 ? 17.995  -15.336 5.598   1.00 26.93  ? 86  ASN   A O   1 
ATOM   700  C CB  . ASN   A 1 87 ? 16.657  -17.592 7.442   1.00 24.48  ? 86  ASN   A CB  1 
ATOM   701  C CG  . ASN   A 1 87 ? 16.200  -17.677 8.882   1.00 30.84  ? 86  ASN   A CG  1 
ATOM   702  O OD1 . ASN   A 1 87 ? 16.611  -16.863 9.710   1.00 31.99  ? 86  ASN   A OD1 1 
ATOM   703  N ND2 . ASN   A 1 87 ? 15.234  -18.530 9.189   1.00 25.75  ? 86  ASN   A ND2 1 
ATOM   704  N N   . ASN   A 1 88 ? 16.358  -16.276 4.342   1.00 23.51  ? 87  ASN   A N   1 
ATOM   705  C CA  . ASN   A 1 88 ? 16.992  -15.879 3.098   1.00 25.79  ? 87  ASN   A CA  1 
ATOM   706  C C   . ASN   A 1 88 ? 15.926  -15.801 1.997   1.00 25.90  ? 87  ASN   A C   1 
ATOM   707  O O   . ASN   A 1 88 ? 15.951  -16.540 1.004   1.00 25.77  ? 87  ASN   A O   1 
ATOM   708  C CB  . ASN   A 1 88 ? 18.151  -16.817 2.747   1.00 25.27  ? 87  ASN   A CB  1 
ATOM   709  C CG  . ASN   A 1 88 ? 19.194  -16.188 1.856   1.00 27.42  ? 87  ASN   A CG  1 
ATOM   710  O OD1 . ASN   A 1 88 ? 18.968  -15.171 1.172   1.00 25.74  ? 87  ASN   A OD1 1 
ATOM   711  N ND2 . ASN   A 1 88 ? 20.362  -16.823 1.807   1.00 29.14  ? 87  ASN   A ND2 1 
ATOM   712  N N   . PRO   A 1 89 ? 14.952  -14.862 2.113   1.00 24.59  ? 88  PRO   A N   1 
ATOM   713  C CA  . PRO   A 1 89 ? 13.852  -14.824 1.150   1.00 24.34  ? 88  PRO   A CA  1 
ATOM   714  C C   . PRO   A 1 89 ? 14.210  -14.419 -0.286  1.00 24.78  ? 88  PRO   A C   1 
ATOM   715  O O   . PRO   A 1 89 ? 13.414  -14.640 -1.198  1.00 23.58  ? 88  PRO   A O   1 
ATOM   716  C CB  . PRO   A 1 89 ? 12.861  -13.877 1.827   1.00 21.00  ? 88  PRO   A CB  1 
ATOM   717  C CG  . PRO   A 1 89 ? 13.736  -12.894 2.605   1.00 20.82  ? 88  PRO   A CG  1 
ATOM   718  C CD  . PRO   A 1 89 ? 14.856  -13.826 3.155   1.00 20.80  ? 88  PRO   A CD  1 
ATOM   719  N N   . HIS   A 1 90 ? 15.400  -13.822 -0.490  1.00 23.76  ? 89  HIS   A N   1 
ATOM   720  C CA  . HIS   A 1 90 ? 15.765  -13.273 -1.786  1.00 23.36  ? 89  HIS   A CA  1 
ATOM   721  C C   . HIS   A 1 90 ? 16.866  -14.092 -2.463  1.00 25.90  ? 89  HIS   A C   1 
ATOM   722  O O   . HIS   A 1 90 ? 17.338  -13.686 -3.530  1.00 27.28  ? 89  HIS   A O   1 
ATOM   723  C CB  . HIS   A 1 90 ? 16.190  -11.801 -1.620  1.00 22.91  ? 89  HIS   A CB  1 
ATOM   724  C CG  . HIS   A 1 90 ? 15.090  -10.974 -1.050  1.00 24.46  ? 89  HIS   A CG  1 
ATOM   725  N ND1 . HIS   A 1 90 ? 13.846  -10.892 -1.660  1.00 24.37  ? 89  HIS   A ND1 1 
ATOM   726  C CD2 . HIS   A 1 90 ? 15.017  -10.209 0.052   1.00 24.16  ? 89  HIS   A CD2 1 
ATOM   727  C CE1 . HIS   A 1 90 ? 13.070  -10.055 -0.981  1.00 22.57  ? 89  HIS   A CE1 1 
ATOM   728  N NE2 . HIS   A 1 90 ? 13.745  -9.656  0.083   1.00 28.44  ? 89  HIS   A NE2 1 
ATOM   729  N N   . ALA   A 1 91 ? 17.208  -15.252 -1.884  1.00 24.88  ? 90  ALA   A N   1 
ATOM   730  C CA  . ALA   A 1 91 ? 18.204  -16.161 -2.448  1.00 27.28  ? 90  ALA   A CA  1 
ATOM   731  C C   . ALA   A 1 91 ? 17.736  -16.842 -3.731  1.00 31.80  ? 90  ALA   A C   1 
ATOM   732  O O   . ALA   A 1 91 ? 16.541  -16.972 -4.001  1.00 27.89  ? 90  ALA   A O   1 
ATOM   733  C CB  . ALA   A 1 91 ? 18.588  -17.215 -1.447  1.00 26.01  ? 90  ALA   A CB  1 
ATOM   734  N N   . SER   A 1 92 ? 18.727  -17.348 -4.484  1.00 30.87  ? 91  SER   A N   1 
ATOM   735  C CA  . SER   A 1 92 ? 18.435  -18.268 -5.580  1.00 31.09  ? 91  SER   A CA  1 
ATOM   736  C C   . SER   A 1 92 ? 18.144  -19.657 -5.024  1.00 34.54  ? 91  SER   A C   1 
ATOM   737  O O   . SER   A 1 92 ? 18.974  -20.216 -4.296  1.00 33.16  ? 91  SER   A O   1 
ATOM   738  C CB  . SER   A 1 92 ? 19.610  -18.296 -6.510  1.00 36.97  ? 91  SER   A CB  1 
ATOM   739  O OG  . SER   A 1 92 ? 19.412  -19.326 -7.456  1.00 40.30  ? 91  SER   A OG  1 
ATOM   740  N N   . TYR   A 1 93 ? 16.970  -20.206 -5.373  1.00 30.89  ? 92  TYR   A N   1 
ATOM   741  C CA  . TYR   A 1 93 ? 16.608  -21.542 -4.939  1.00 33.23  ? 92  TYR   A CA  1 
ATOM   742  C C   . TYR   A 1 93 ? 16.511  -22.483 -6.143  1.00 38.55  ? 92  TYR   A C   1 
ATOM   743  O O   . TYR   A 1 93 ? 16.007  -23.591 -6.012  1.00 50.97  ? 92  TYR   A O   1 
ATOM   744  C CB  . TYR   A 1 93 ? 15.290  -21.591 -4.150  1.00 28.59  ? 92  TYR   A CB  1 
ATOM   745  C CG  . TYR   A 1 93 ? 15.432  -20.974 -2.776  1.00 28.41  ? 92  TYR   A CG  1 
ATOM   746  C CD1 . TYR   A 1 93 ? 15.908  -21.728 -1.707  1.00 28.52  ? 92  TYR   A CD1 1 
ATOM   747  C CD2 . TYR   A 1 93 ? 15.107  -19.630 -2.561  1.00 29.69  ? 92  TYR   A CD2 1 
ATOM   748  C CE1 . TYR   A 1 93 ? 16.093  -21.151 -0.456  1.00 33.19  ? 92  TYR   A CE1 1 
ATOM   749  C CE2 . TYR   A 1 93 ? 15.255  -19.059 -1.306  1.00 29.28  ? 92  TYR   A CE2 1 
ATOM   750  C CZ  . TYR   A 1 93 ? 15.735  -19.825 -0.255  1.00 27.61  ? 92  TYR   A CZ  1 
ATOM   751  O OH  . TYR   A 1 93 ? 15.950  -19.314 0.986   1.00 28.40  ? 92  TYR   A OH  1 
ATOM   752  N N   . SER   A 1 94 ? 16.996  -22.051 -7.311  1.00 49.63  ? 93  SER   A N   1 
ATOM   753  C CA  . SER   A 1 94 ? 17.057  -22.958 -8.450  1.00 64.29  ? 93  SER   A CA  1 
ATOM   754  C C   . SER   A 1 94 ? 18.166  -24.006 -8.227  1.00 73.41  ? 93  SER   A C   1 
ATOM   755  O O   . SER   A 1 94 ? 19.303  -23.599 -7.884  1.00 68.39  ? 93  SER   A O   1 
ATOM   756  C CB  . SER   A 1 94 ? 17.167  -22.228 -9.778  1.00 64.58  ? 93  SER   A CB  1 
ATOM   757  O OG  . SER   A 1 94 ? 18.133  -21.184 -9.727  1.00 69.26  ? 93  SER   A OG  1 
ATOM   758  O OXT . SER   A 1 94 ? 17.842  -25.207 -8.353  1.00 85.75  ? 93  SER   A OXT 1 
ATOM   759  N N   . MET   B 1 2  ? 38.935  -11.054 -42.467 1.00 73.05  ? 1   MET   B N   1 
ATOM   760  C CA  . MET   B 1 2  ? 38.562  -12.145 -43.406 1.00 73.58  ? 1   MET   B CA  1 
ATOM   761  C C   . MET   B 1 2  ? 37.045  -12.342 -43.355 1.00 70.25  ? 1   MET   B C   1 
ATOM   762  O O   . MET   B 1 2  ? 36.512  -12.731 -42.313 1.00 73.66  ? 1   MET   B O   1 
ATOM   763  C CB  . MET   B 1 2  ? 39.329  -13.435 -43.070 1.00 84.68  ? 1   MET   B CB  1 
ATOM   764  C CG  . MET   B 1 2  ? 39.475  -14.437 -44.216 1.00 98.33  ? 1   MET   B CG  1 
ATOM   765  S SD  . MET   B 1 2  ? 40.367  -13.882 -45.687 1.00 102.43 ? 1   MET   B SD  1 
ATOM   766  C CE  . MET   B 1 2  ? 41.713  -12.921 -44.979 1.00 98.00  ? 1   MET   B CE  1 
ATOM   767  N N   . PRO   B 1 3  ? 36.308  -12.063 -44.465 1.00 60.47  ? 2   PRO   B N   1 
ATOM   768  C CA  . PRO   B 1 3  ? 34.847  -12.205 -44.486 1.00 56.66  ? 2   PRO   B CA  1 
ATOM   769  C C   . PRO   B 1 3  ? 34.483  -13.644 -44.129 1.00 54.03  ? 2   PRO   B C   1 
ATOM   770  O O   . PRO   B 1 3  ? 35.226  -14.539 -44.491 1.00 47.70  ? 2   PRO   B O   1 
ATOM   771  C CB  . PRO   B 1 3  ? 34.461  -11.841 -45.930 1.00 60.34  ? 2   PRO   B CB  1 
ATOM   772  C CG  . PRO   B 1 3  ? 35.621  -11.003 -46.430 1.00 57.58  ? 2   PRO   B CG  1 
ATOM   773  C CD  . PRO   B 1 3  ? 36.846  -11.596 -45.755 1.00 58.50  ? 2   PRO   B CD  1 
ATOM   774  N N   . HIS   B 1 4  ? 33.385  -13.848 -43.373 1.00 51.60  ? 3   HIS   B N   1 
ATOM   775  C CA  . HIS   B 1 4  ? 32.930  -15.192 -43.027 1.00 52.98  ? 3   HIS   B CA  1 
ATOM   776  C C   . HIS   B 1 4  ? 31.562  -15.453 -43.660 1.00 47.08  ? 3   HIS   B C   1 
ATOM   777  O O   . HIS   B 1 4  ? 31.021  -14.582 -44.351 1.00 45.78  ? 3   HIS   B O   1 
ATOM   778  C CB  . HIS   B 1 4  ? 33.080  -15.479 -41.528 1.00 59.85  ? 3   HIS   B CB  1 
ATOM   779  C CG  . HIS   B 1 4  ? 34.502  -15.497 -41.052 1.00 76.12  ? 3   HIS   B CG  1 
ATOM   780  N ND1 . HIS   B 1 4  ? 35.445  -16.386 -41.534 1.00 77.39  ? 3   HIS   B ND1 1 
ATOM   781  C CD2 . HIS   B 1 4  ? 35.149  -14.722 -40.157 1.00 69.97  ? 3   HIS   B CD2 1 
ATOM   782  C CE1 . HIS   B 1 4  ? 36.606  -16.163 -40.932 1.00 67.54  ? 3   HIS   B CE1 1 
ATOM   783  N NE2 . HIS   B 1 4  ? 36.449  -15.159 -40.092 1.00 70.98  ? 3   HIS   B NE2 1 
ATOM   784  N N   . ALA   B 1 5  ? 31.025  -16.670 -43.462 1.00 40.95  ? 4   ALA   B N   1 
ATOM   785  C CA  . ALA   B 1 5  ? 29.712  -16.999 -43.992 1.00 43.85  ? 4   ALA   B CA  1 
ATOM   786  C C   . ALA   B 1 5  ? 28.695  -15.961 -43.514 1.00 44.86  ? 4   ALA   B C   1 
ATOM   787  O O   . ALA   B 1 5  ? 27.800  -15.563 -44.274 1.00 43.24  ? 4   ALA   B O   1 
ATOM   788  C CB  . ALA   B 1 5  ? 29.321  -18.378 -43.522 1.00 45.73  ? 4   ALA   B CB  1 
ATOM   789  N N   . PHE   B 1 6  ? 28.830  -15.585 -42.229 1.00 46.28  ? 5   PHE   B N   1 
ATOM   790  C CA  . PHE   B 1 6  ? 28.015  -14.573 -41.563 1.00 47.66  ? 5   PHE   B CA  1 
ATOM   791  C C   . PHE   B 1 6  ? 28.892  -13.347 -41.285 1.00 43.63  ? 5   PHE   B C   1 
ATOM   792  O O   . PHE   B 1 6  ? 29.999  -13.487 -40.782 1.00 48.60  ? 5   PHE   B O   1 
ATOM   793  C CB  . PHE   B 1 6  ? 27.419  -15.052 -40.231 1.00 44.12  ? 5   PHE   B CB  1 
ATOM   794  C CG  . PHE   B 1 6  ? 26.349  -16.127 -40.354 1.00 41.85  ? 5   PHE   B CG  1 
ATOM   795  C CD1 . PHE   B 1 6  ? 25.026  -15.778 -40.608 1.00 36.19  ? 5   PHE   B CD1 1 
ATOM   796  C CD2 . PHE   B 1 6  ? 26.670  -17.476 -40.236 1.00 38.76  ? 5   PHE   B CD2 1 
ATOM   797  C CE1 . PHE   B 1 6  ? 24.044  -16.741 -40.758 1.00 39.32  ? 5   PHE   B CE1 1 
ATOM   798  C CE2 . PHE   B 1 6  ? 25.685  -18.440 -40.396 1.00 33.68  ? 5   PHE   B CE2 1 
ATOM   799  C CZ  . PHE   B 1 6  ? 24.370  -18.077 -40.624 1.00 36.92  ? 5   PHE   B CZ  1 
ATOM   800  N N   . LYS   B 1 7  ? 28.394  -12.161 -41.659 1.00 48.50  ? 6   LYS   B N   1 
ATOM   801  C CA  . LYS   B 1 7  ? 29.110  -10.905 -41.471 1.00 44.08  ? 6   LYS   B CA  1 
ATOM   802  C C   . LYS   B 1 7  ? 28.341  -10.056 -40.456 1.00 45.18  ? 6   LYS   B C   1 
ATOM   803  O O   . LYS   B 1 7  ? 27.116  -10.194 -40.353 1.00 40.55  ? 6   LYS   B O   1 
ATOM   804  C CB  . LYS   B 1 7  ? 29.211  -10.207 -42.833 1.00 49.60  ? 6   LYS   B CB  1 
ATOM   805  C CG  . LYS   B 1 7  ? 27.897  -9.902  -43.538 1.00 47.52  ? 6   LYS   B CG  1 
ATOM   806  C CD  . LYS   B 1 7  ? 28.109  -9.159  -44.856 1.00 56.52  ? 6   LYS   B CD  1 
ATOM   807  C CE  . LYS   B 1 7  ? 26.871  -8.846  -45.638 1.00 54.98  ? 6   LYS   B CE  1 
ATOM   808  N NZ  . LYS   B 1 7  ? 26.080  -10.043 -45.954 1.00 63.48  ? 6   LYS   B NZ  1 
ATOM   809  N N   . PRO   B 1 8  ? 29.006  -9.150  -39.690 1.00 47.70  ? 7   PRO   B N   1 
ATOM   810  C CA  . PRO   B 1 8  ? 28.296  -8.246  -38.778 1.00 40.67  ? 7   PRO   B CA  1 
ATOM   811  C C   . PRO   B 1 8  ? 27.110  -7.589  -39.467 1.00 37.67  ? 7   PRO   B C   1 
ATOM   812  O O   . PRO   B 1 8  ? 27.211  -7.164  -40.621 1.00 45.82  ? 7   PRO   B O   1 
ATOM   813  C CB  . PRO   B 1 8  ? 29.438  -7.280  -38.486 1.00 42.23  ? 7   PRO   B CB  1 
ATOM   814  C CG  . PRO   B 1 8  ? 30.602  -8.248  -38.300 1.00 45.07  ? 7   PRO   B CG  1 
ATOM   815  C CD  . PRO   B 1 8  ? 30.469  -8.954  -39.637 1.00 45.55  ? 7   PRO   B CD  1 
ATOM   816  N N   . GLY   B 1 9  ? 25.958  -7.592  -38.782 1.00 36.06  ? 8   GLY   B N   1 
ATOM   817  C CA  . GLY   B 1 9  ? 24.768  -6.917  -39.277 1.00 31.91  ? 8   GLY   B CA  1 
ATOM   818  C C   . GLY   B 1 9  ? 23.789  -7.875  -39.947 1.00 32.45  ? 8   GLY   B C   1 
ATOM   819  O O   . GLY   B 1 9  ? 22.654  -7.492  -40.235 1.00 32.34  ? 8   GLY   B O   1 
ATOM   820  N N   . ASP   B 1 10 ? 24.244  -9.110  -40.231 1.00 31.18  ? 9   ASP   B N   1 
ATOM   821  C CA  . ASP   B 1 10 ? 23.342  -10.110 -40.803 1.00 31.59  ? 9   ASP   B CA  1 
ATOM   822  C C   . ASP   B 1 10 ? 22.223  -10.408 -39.793 1.00 25.12  ? 9   ASP   B C   1 
ATOM   823  O O   . ASP   B 1 10 ? 22.484  -10.456 -38.600 1.00 30.10  ? 9   ASP   B O   1 
ATOM   824  C CB  . ASP   B 1 10 ? 24.092  -11.408 -41.069 1.00 31.99  ? 9   ASP   B CB  1 
ATOM   825  C CG  . ASP   B 1 10 ? 24.952  -11.438 -42.333 1.00 47.36  ? 9   ASP   B CG  1 
ATOM   826  O OD1 . ASP   B 1 10 ? 24.720  -10.581 -43.217 1.00 41.74  ? 9   ASP   B OD1 1 
ATOM   827  O OD2 . ASP   B 1 10 ? 25.861  -12.315 -42.415 1.00 41.09  ? 9   ASP   B OD2 1 
ATOM   828  N N   . LEU   B 1 11 ? 20.991  -10.507 -40.266 1.00 29.49  ? 10  LEU   B N   1 
ATOM   829  C CA  . LEU   B 1 11 ? 19.869  -10.750 -39.369 1.00 30.91  ? 10  LEU   B CA  1 
ATOM   830  C C   . LEU   B 1 11 ? 19.578  -12.243 -39.376 1.00 30.71  ? 10  LEU   B C   1 
ATOM   831  O O   . LEU   B 1 11 ? 19.547  -12.813 -40.458 1.00 32.37  ? 10  LEU   B O   1 
ATOM   832  C CB  . LEU   B 1 11 ? 18.664  -9.952  -39.856 1.00 31.00  ? 10  LEU   B CB  1 
ATOM   833  C CG  . LEU   B 1 11 ? 18.926  -8.443  -39.979 1.00 29.63  ? 10  LEU   B CG  1 
ATOM   834  C CD1 . LEU   B 1 11 ? 17.580  -7.777  -40.273 1.00 31.34  ? 10  LEU   B CD1 1 
ATOM   835  C CD2 . LEU   B 1 11 ? 19.600  -8.000  -38.665 1.00 25.51  ? 10  LEU   B CD2 1 
ATOM   836  N N   . VAL   B 1 12 ? 19.283  -12.822 -38.202 1.00 28.13  ? 11  VAL   B N   1 
ATOM   837  C CA  . VAL   B 1 12 ? 19.030  -14.268 -38.099 1.00 27.32  ? 11  VAL   B CA  1 
ATOM   838  C C   . VAL   B 1 12 ? 17.890  -14.543 -37.123 1.00 31.85  ? 11  VAL   B C   1 
ATOM   839  O O   . VAL   B 1 12 ? 17.482  -13.636 -36.394 1.00 27.74  ? 11  VAL   B O   1 
ATOM   840  C CB  . VAL   B 1 12 ? 20.295  -15.042 -37.674 1.00 30.72  ? 11  VAL   B CB  1 
ATOM   841  C CG1 . VAL   B 1 12 ? 21.424  -14.878 -38.706 1.00 29.98  ? 11  VAL   B CG1 1 
ATOM   842  C CG2 . VAL   B 1 12 ? 20.773  -14.713 -36.251 1.00 29.35  ? 11  VAL   B CG2 1 
ATOM   843  N N   . PHE   B 1 13 ? 17.382  -15.794 -37.115 1.00 28.53  ? 12  PHE   B N   1 
ATOM   844  C CA  . PHE   B 1 13 ? 16.894  -16.332 -35.849 1.00 27.55  ? 12  PHE   B CA  1 
ATOM   845  C C   . PHE   B 1 13 ? 17.981  -17.208 -35.244 1.00 27.92  ? 12  PHE   B C   1 
ATOM   846  O O   . PHE   B 1 13 ? 18.572  -18.011 -35.980 1.00 30.42  ? 12  PHE   B O   1 
ATOM   847  C CB  . PHE   B 1 13 ? 15.649  -17.178 -36.106 1.00 27.80  ? 12  PHE   B CB  1 
ATOM   848  C CG  . PHE   B 1 13 ? 14.441  -16.338 -36.459 1.00 31.11  ? 12  PHE   B CG  1 
ATOM   849  C CD1 . PHE   B 1 13 ? 14.169  -16.024 -37.789 1.00 31.02  ? 12  PHE   B CD1 1 
ATOM   850  C CD2 . PHE   B 1 13 ? 13.594  -15.874 -35.460 1.00 31.36  ? 12  PHE   B CD2 1 
ATOM   851  C CE1 . PHE   B 1 13 ? 13.054  -15.265 -38.105 1.00 36.78  ? 12  PHE   B CE1 1 
ATOM   852  C CE2 . PHE   B 1 13 ? 12.472  -15.113 -35.783 1.00 33.92  ? 12  PHE   B CE2 1 
ATOM   853  C CZ  . PHE   B 1 13 ? 12.212  -14.815 -37.110 1.00 36.21  ? 12  PHE   B CZ  1 
ATOM   854  N N   . ALA   B 1 14 ? 18.235  -17.051 -33.924 1.00 23.73  ? 13  ALA   B N   1 
ATOM   855  C CA  . ALA   B 1 14 ? 19.262  -17.799 -33.230 1.00 27.87  ? 13  ALA   B CA  1 
ATOM   856  C C   . ALA   B 1 14 ? 18.639  -18.730 -32.191 1.00 27.67  ? 13  ALA   B C   1 
ATOM   857  O O   . ALA   B 1 14 ? 17.699  -18.363 -31.485 1.00 29.19  ? 13  ALA   B O   1 
ATOM   858  C CB  . ALA   B 1 14 ? 20.298  -16.868 -32.607 1.00 26.30  ? 13  ALA   B CB  1 
ATOM   859  N N   . LYS   B 1 15 ? 19.199  -19.933 -32.095 1.00 26.81  ? 14  LYS   B N   1 
ATOM   860  C CA  . LYS   B 1 15 ? 18.554  -20.995 -31.334 1.00 28.67  ? 14  LYS   B CA  1 
ATOM   861  C C   . LYS   B 1 15 ? 19.431  -21.295 -30.129 1.00 30.92  ? 14  LYS   B C   1 
ATOM   862  O O   . LYS   B 1 15 ? 20.611  -21.647 -30.278 1.00 36.64  ? 14  LYS   B O   1 
ATOM   863  C CB  . LYS   B 1 15 ? 18.363  -22.272 -32.172 1.00 28.66  ? 14  LYS   B CB  1 
ATOM   864  C CG  . LYS   B 1 15 ? 17.619  -23.386 -31.364 1.00 31.05  ? 14  LYS   B CG  1 
ATOM   865  C CD  . LYS   B 1 15 ? 16.139  -23.039 -31.157 1.00 34.83  ? 14  LYS   B CD  1 
ATOM   866  C CE  . LYS   B 1 15 ? 15.264  -24.158 -30.545 1.00 32.73  ? 14  LYS   B CE  1 
ATOM   867  N NZ  . LYS   B 1 15 ? 15.710  -24.397 -29.167 1.00 29.57  ? 14  LYS   B NZ  1 
ATOM   868  N N   . MET   B 1 16 ? 18.857  -21.074 -28.945 1.00 35.45  ? 15  MET   B N   1 
ATOM   869  C CA  . MET   B 1 16 ? 19.490  -21.423 -27.686 1.00 37.55  ? 15  MET   B CA  1 
ATOM   870  C C   . MET   B 1 16 ? 18.647  -22.476 -26.968 1.00 38.88  ? 15  MET   B C   1 
ATOM   871  O O   . MET   B 1 16 ? 17.413  -22.421 -26.989 1.00 31.91  ? 15  MET   B O   1 
ATOM   872  C CB  . MET   B 1 16 ? 19.701  -20.182 -26.811 1.00 37.79  ? 15  MET   B CB  1 
ATOM   873  C CG  . MET   B 1 16 ? 20.949  -19.394 -27.198 1.00 50.38  ? 15  MET   B CG  1 
ATOM   874  S SD  . MET   B 1 16 ? 21.337  -18.153 -25.953 1.00 68.23  ? 15  MET   B SD  1 
ATOM   875  C CE  . MET   B 1 16 ? 21.427  -19.066 -24.406 1.00 56.81  ? 15  MET   B CE  1 
ATOM   876  N N   . LYS   B 1 17 ? 19.331  -23.442 -26.344 1.00 40.19  ? 16  LYS   B N   1 
ATOM   877  C CA  . LYS   B 1 17 ? 18.646  -24.468 -25.564 1.00 43.07  ? 16  LYS   B CA  1 
ATOM   878  C C   . LYS   B 1 17 ? 17.678  -23.808 -24.575 1.00 36.24  ? 16  LYS   B C   1 
ATOM   879  O O   . LYS   B 1 17 ? 18.047  -22.858 -23.889 1.00 37.60  ? 16  LYS   B O   1 
ATOM   880  C CB  . LYS   B 1 17 ? 19.696  -25.308 -24.830 1.00 44.81  ? 16  LYS   B CB  1 
ATOM   881  C CG  . LYS   B 1 17 ? 19.231  -26.728 -24.499 1.00 54.91  ? 16  LYS   B CG  1 
ATOM   882  C CD  . LYS   B 1 17 ? 19.826  -27.339 -23.234 1.00 52.85  ? 16  LYS   B CD  1 
ATOM   883  N N   . GLY   B 1 18 ? 16.429  -24.284 -24.570 1.00 37.52  ? 17  GLY   B N   1 
ATOM   884  C CA  . GLY   B 1 18 ? 15.380  -23.811 -23.671 1.00 40.09  ? 17  GLY   B CA  1 
ATOM   885  C C   . GLY   B 1 18 ? 14.546  -22.649 -24.225 1.00 39.84  ? 17  GLY   B C   1 
ATOM   886  O O   . GLY   B 1 18 ? 13.681  -22.132 -23.512 1.00 38.55  ? 17  GLY   B O   1 
ATOM   887  N N   . TYR   B 1 19 ? 14.833  -22.185 -25.458 1.00 35.31  ? 18  TYR   B N   1 
ATOM   888  C CA  . TYR   B 1 19 ? 14.146  -20.998 -25.971 1.00 31.74  ? 18  TYR   B CA  1 
ATOM   889  C C   . TYR   B 1 19 ? 13.747  -21.210 -27.431 1.00 29.01  ? 18  TYR   B C   1 
ATOM   890  O O   . TYR   B 1 19 ? 14.405  -21.957 -28.148 1.00 34.58  ? 18  TYR   B O   1 
ATOM   891  C CB  . TYR   B 1 19 ? 15.047  -19.754 -25.976 1.00 32.83  ? 18  TYR   B CB  1 
ATOM   892  C CG  . TYR   B 1 19 ? 15.618  -19.416 -24.608 1.00 37.63  ? 18  TYR   B CG  1 
ATOM   893  C CD1 . TYR   B 1 19 ? 14.967  -18.522 -23.760 1.00 35.66  ? 18  TYR   B CD1 1 
ATOM   894  C CD2 . TYR   B 1 19 ? 16.748  -20.070 -24.130 1.00 40.79  ? 18  TYR   B CD2 1 
ATOM   895  C CE1 . TYR   B 1 19 ? 15.479  -18.237 -22.499 1.00 39.32  ? 18  TYR   B CE1 1 
ATOM   896  C CE2 . TYR   B 1 19 ? 17.262  -19.801 -22.870 1.00 43.61  ? 18  TYR   B CE2 1 
ATOM   897  C CZ  . TYR   B 1 19 ? 16.614  -18.894 -22.050 1.00 40.10  ? 18  TYR   B CZ  1 
ATOM   898  O OH  . TYR   B 1 19 ? 17.147  -18.638 -20.823 1.00 44.46  ? 18  TYR   B OH  1 
ATOM   899  N N   . PRO   B 1 20 ? 12.665  -20.574 -27.925 1.00 29.34  ? 19  PRO   B N   1 
ATOM   900  C CA  . PRO   B 1 20 ? 12.303  -20.702 -29.341 1.00 29.07  ? 19  PRO   B CA  1 
ATOM   901  C C   . PRO   B 1 20 ? 13.369  -19.978 -30.171 1.00 30.43  ? 19  PRO   B C   1 
ATOM   902  O O   . PRO   B 1 20 ? 14.068  -19.123 -29.630 1.00 30.56  ? 19  PRO   B O   1 
ATOM   903  C CB  . PRO   B 1 20 ? 10.978  -19.992 -29.419 1.00 27.30  ? 19  PRO   B CB  1 
ATOM   904  C CG  . PRO   B 1 20 ? 10.990  -18.988 -28.275 1.00 29.96  ? 19  PRO   B CG  1 
ATOM   905  C CD  . PRO   B 1 20 ? 11.800  -19.647 -27.172 1.00 29.30  ? 19  PRO   B CD  1 
ATOM   906  N N   . HIS   B 1 21 ? 13.523  -20.365 -31.443 1.00 27.50  ? 20  HIS   B N   1 
ATOM   907  C CA  . HIS   B 1 21 ? 14.306  -19.583 -32.409 1.00 28.00  ? 20  HIS   B CA  1 
ATOM   908  C C   . HIS   B 1 21 ? 14.035  -18.091 -32.228 1.00 25.71  ? 20  HIS   B C   1 
ATOM   909  O O   . HIS   B 1 21 ? 12.876  -17.663 -32.306 1.00 27.29  ? 20  HIS   B O   1 
ATOM   910  C CB  . HIS   B 1 21 ? 13.961  -20.042 -33.831 1.00 27.76  ? 20  HIS   B CB  1 
ATOM   911  C CG  . HIS   B 1 21 ? 14.183  -21.536 -34.007 1.00 32.37  ? 20  HIS   B CG  1 
ATOM   912  N ND1 . HIS   B 1 21 ? 13.291  -22.519 -33.587 1.00 30.67  ? 20  HIS   B ND1 1 
ATOM   913  C CD2 . HIS   B 1 21 ? 15.265  -22.198 -34.511 1.00 32.12  ? 20  HIS   B CD2 1 
ATOM   914  C CE1 . HIS   B 1 21 ? 13.791  -23.722 -33.893 1.00 30.55  ? 20  HIS   B CE1 1 
ATOM   915  N NE2 . HIS   B 1 21 ? 15.003  -23.558 -34.420 1.00 30.80  ? 20  HIS   B NE2 1 
ATOM   916  N N   . TRP   B 1 22 ? 15.107  -17.314 -32.011 1.00 27.34  ? 21  TRP   B N   1 
ATOM   917  C CA  . TRP   B 1 22 ? 14.950  -15.977 -31.443 1.00 26.22  ? 21  TRP   B CA  1 
ATOM   918  C C   . TRP   B 1 22 ? 15.486  -14.914 -32.409 1.00 31.48  ? 21  TRP   B C   1 
ATOM   919  O O   . TRP   B 1 22 ? 16.605  -15.057 -32.886 1.00 28.18  ? 21  TRP   B O   1 
ATOM   920  C CB  . TRP   B 1 22 ? 15.696  -15.872 -30.106 1.00 24.74  ? 21  TRP   B CB  1 
ATOM   921  C CG  . TRP   B 1 22 ? 15.184  -14.711 -29.282 1.00 28.42  ? 21  TRP   B CG  1 
ATOM   922  C CD1 . TRP   B 1 22 ? 15.497  -13.376 -29.398 1.00 29.82  ? 21  TRP   B CD1 1 
ATOM   923  C CD2 . TRP   B 1 22 ? 14.224  -14.794 -28.196 1.00 30.02  ? 21  TRP   B CD2 1 
ATOM   924  N NE1 . TRP   B 1 22 ? 14.766  -12.633 -28.488 1.00 29.13  ? 21  TRP   B NE1 1 
ATOM   925  C CE2 . TRP   B 1 22 ? 14.001  -13.477 -27.722 1.00 28.20  ? 21  TRP   B CE2 1 
ATOM   926  C CE3 . TRP   B 1 22 ? 13.547  -15.857 -27.581 1.00 32.69  ? 21  TRP   B CE3 1 
ATOM   927  C CZ2 . TRP   B 1 22 ? 13.132  -13.198 -26.659 1.00 27.11  ? 21  TRP   B CZ2 1 
ATOM   928  C CZ3 . TRP   B 1 22 ? 12.715  -15.588 -26.514 1.00 30.04  ? 21  TRP   B CZ3 1 
ATOM   929  C CH2 . TRP   B 1 22 ? 12.475  -14.280 -26.098 1.00 28.59  ? 21  TRP   B CH2 1 
ATOM   930  N N   . PRO   B 1 23 ? 14.744  -13.808 -32.678 1.00 28.86  ? 22  PRO   B N   1 
ATOM   931  C CA  . PRO   B 1 23 ? 15.192  -12.793 -33.637 1.00 28.73  ? 22  PRO   B CA  1 
ATOM   932  C C   . PRO   B 1 23 ? 16.480  -12.203 -33.093 1.00 27.43  ? 22  PRO   B C   1 
ATOM   933  O O   . PRO   B 1 23 ? 16.559  -11.872 -31.920 1.00 30.00  ? 22  PRO   B O   1 
ATOM   934  C CB  . PRO   B 1 23 ? 14.019  -11.753 -33.678 1.00 28.98  ? 22  PRO   B CB  1 
ATOM   935  C CG  . PRO   B 1 23 ? 13.298  -11.980 -32.343 1.00 28.56  ? 22  PRO   B CG  1 
ATOM   936  C CD  . PRO   B 1 23 ? 13.416  -13.508 -32.128 1.00 26.32  ? 22  PRO   B CD  1 
ATOM   937  N N   . ALA   B 1 24 ? 17.511  -12.134 -33.941 1.00 26.51  ? 23  ALA   B N   1 
ATOM   938  C CA  . ALA   B 1 24 ? 18.834  -11.712 -33.501 1.00 27.20  ? 23  ALA   B CA  1 
ATOM   939  C C   . ALA   B 1 24 ? 19.647  -11.158 -34.673 1.00 26.75  ? 23  ALA   B C   1 
ATOM   940  O O   . ALA   B 1 24 ? 19.228  -11.233 -35.842 1.00 29.40  ? 23  ALA   B O   1 
ATOM   941  C CB  . ALA   B 1 24 ? 19.574  -12.879 -32.840 1.00 27.67  ? 23  ALA   B CB  1 
ATOM   942  N N   . ARG   B 1 25 ? 20.838  -10.641 -34.328 1.00 30.50  ? 24  ARG   B N   1 
ATOM   943  C CA  . ARG   B 1 25 ? 21.788  -10.186 -35.333 1.00 32.15  ? 24  ARG   B CA  1 
ATOM   944  C C   . ARG   B 1 25 ? 23.196  -10.631 -34.943 1.00 29.39  ? 24  ARG   B C   1 
ATOM   945  O O   . ARG   B 1 25 ? 23.465  -10.925 -33.785 1.00 30.64  ? 24  ARG   B O   1 
ATOM   946  C CB  . ARG   B 1 25 ? 21.739  -8.663  -35.464 1.00 30.46  ? 24  ARG   B CB  1 
ATOM   947  C CG  . ARG   B 1 25 ? 22.370  -7.973  -34.263 1.00 30.79  ? 24  ARG   B CG  1 
ATOM   948  C CD  . ARG   B 1 25 ? 22.168  -6.449  -34.354 1.00 28.06  ? 24  ARG   B CD  1 
ATOM   949  N NE  . ARG   B 1 25 ? 22.795  -5.720  -33.246 1.00 29.17  ? 24  ARG   B NE  1 
ATOM   950  C CZ  . ARG   B 1 25 ? 22.517  -4.450  -32.895 1.00 35.32  ? 24  ARG   B CZ  1 
ATOM   951  N NH1 . ARG   B 1 25 ? 21.571  -3.787  -33.539 1.00 30.13  ? 24  ARG   B NH1 1 
ATOM   952  N NH2 . ARG   B 1 25 ? 23.168  -3.878  -31.889 1.00 28.96  ? 24  ARG   B NH2 1 
ATOM   953  N N   . ILE   B 1 26 ? 24.071  -10.760 -35.960 1.00 30.41  ? 25  ILE   B N   1 
ATOM   954  C CA  . ILE   B 1 26 ? 25.491  -10.947 -35.758 1.00 32.63  ? 25  ILE   B CA  1 
ATOM   955  C C   . ILE   B 1 26 ? 26.026  -9.558  -35.425 1.00 33.44  ? 25  ILE   B C   1 
ATOM   956  O O   . ILE   B 1 26 ? 25.735  -8.634  -36.171 1.00 35.32  ? 25  ILE   B O   1 
ATOM   957  C CB  . ILE   B 1 26 ? 26.145  -11.415 -37.072 1.00 38.05  ? 25  ILE   B CB  1 
ATOM   958  C CG1 . ILE   B 1 26 ? 25.455  -12.634 -37.692 1.00 34.70  ? 25  ILE   B CG1 1 
ATOM   959  C CG2 . ILE   B 1 26 ? 27.656  -11.590 -36.906 1.00 40.04  ? 25  ILE   B CG2 1 
ATOM   960  C CD1 . ILE   B 1 26 ? 25.446  -13.846 -36.782 1.00 34.11  ? 25  ILE   B CD1 1 
ATOM   961  N N   . ASP   B 1 27 ? 26.800  -9.461  -34.344 1.00 35.41  ? 26  ASP   B N   1 
ATOM   962  C CA  . ASP   B 1 27 ? 27.441  -8.226  -33.926 1.00 45.50  ? 26  ASP   B CA  1 
ATOM   963  C C   . ASP   B 1 27 ? 28.897  -8.211  -34.393 1.00 48.63  ? 26  ASP   B C   1 
ATOM   964  O O   . ASP   B 1 27 ? 29.433  -9.263  -34.723 1.00 43.56  ? 26  ASP   B O   1 
ATOM   965  C CB  . ASP   B 1 27 ? 27.349  -8.107  -32.417 1.00 43.25  ? 26  ASP   B CB  1 
ATOM   966  C CG  . ASP   B 1 27 ? 26.139  -7.347  -31.902 1.00 43.91  ? 26  ASP   B CG  1 
ATOM   967  O OD1 . ASP   B 1 27 ? 25.400  -6.753  -32.740 1.00 43.70  ? 26  ASP   B OD1 1 
ATOM   968  O OD2 . ASP   B 1 27 ? 25.978  -7.315  -30.660 1.00 39.08  ? 26  ASP   B OD2 1 
ATOM   969  N N   A ASP   B 1 28 ? 29.502  -7.013  -34.388 0.50 53.55  ? 27  ASP   B N   1 
ATOM   970  N N   B ASP   B 1 28 ? 29.519  -7.022  -34.415 0.50 53.08  ? 27  ASP   B N   1 
ATOM   971  C CA  A ASP   B 1 28 ? 30.925  -6.786  -34.608 0.50 57.63  ? 27  ASP   B CA  1 
ATOM   972  C CA  B ASP   B 1 28 ? 30.950  -6.901  -34.662 0.50 56.83  ? 27  ASP   B CA  1 
ATOM   973  C C   A ASP   B 1 28 ? 31.697  -7.216  -33.357 0.50 61.67  ? 27  ASP   B C   1 
ATOM   974  C C   B ASP   B 1 28 ? 31.701  -7.111  -33.347 0.50 61.89  ? 27  ASP   B C   1 
ATOM   975  O O   A ASP   B 1 28 ? 31.093  -7.575  -32.349 0.50 62.32  ? 27  ASP   B O   1 
ATOM   976  O O   B ASP   B 1 28 ? 31.084  -7.200  -32.287 0.50 63.12  ? 27  ASP   B O   1 
ATOM   977  C CB  A ASP   B 1 28 ? 31.178  -5.320  -34.934 0.50 51.12  ? 27  ASP   B CB  1 
ATOM   978  C CB  B ASP   B 1 28 ? 31.310  -5.572  -35.312 0.50 49.78  ? 27  ASP   B CB  1 
ATOM   979  C CG  A ASP   B 1 28 ? 30.018  -4.592  -35.604 0.50 51.17  ? 27  ASP   B CG  1 
ATOM   980  C CG  B ASP   B 1 28 ? 32.216  -5.692  -36.529 0.50 49.84  ? 27  ASP   B CG  1 
ATOM   981  O OD1 A ASP   B 1 28 ? 30.194  -4.113  -36.745 0.50 52.94  ? 27  ASP   B OD1 1 
ATOM   982  O OD1 B ASP   B 1 28 ? 33.097  -6.578  -36.520 0.50 52.19  ? 27  ASP   B OD1 1 
ATOM   983  O OD2 A ASP   B 1 28 ? 28.936  -4.513  -34.988 0.50 50.06  ? 27  ASP   B OD2 1 
ATOM   984  O OD2 B ASP   B 1 28 ? 32.016  -4.918  -37.489 0.50 45.68  ? 27  ASP   B OD2 1 
ATOM   985  N N   . ILE   B 1 29 ? 33.036  -7.183  -33.428 1.00 69.44  ? 28  ILE   B N   1 
ATOM   986  C CA  . ILE   B 1 29 ? 33.883  -7.374  -32.256 1.00 71.28  ? 28  ILE   B CA  1 
ATOM   987  C C   . ILE   B 1 29 ? 34.778  -6.132  -32.096 1.00 77.80  ? 28  ILE   B C   1 
ATOM   988  O O   . ILE   B 1 29 ? 34.453  -5.309  -31.213 1.00 79.38  ? 28  ILE   B O   1 
ATOM   989  C CB  . ILE   B 1 29 ? 34.711  -8.671  -32.350 1.00 68.19  ? 28  ILE   B CB  1 
ATOM   990  N N   . VAL   B 1 34 ? 36.672  -10.070 -24.591 1.00 79.54  ? 33  VAL   B N   1 
ATOM   991  C CA  . VAL   B 1 34 ? 36.561  -11.453 -25.146 1.00 82.24  ? 33  VAL   B CA  1 
ATOM   992  C C   . VAL   B 1 34 ? 36.624  -11.363 -26.669 1.00 80.36  ? 33  VAL   B C   1 
ATOM   993  O O   . VAL   B 1 34 ? 36.328  -10.315 -27.239 1.00 91.98  ? 33  VAL   B O   1 
ATOM   994  C CB  . VAL   B 1 34 ? 35.240  -12.087 -24.657 1.00 79.69  ? 33  VAL   B CB  1 
ATOM   995  C CG1 . VAL   B 1 34 ? 34.012  -11.382 -25.233 1.00 76.59  ? 33  VAL   B CG1 1 
ATOM   996  C CG2 . VAL   B 1 34 ? 35.176  -13.592 -24.904 1.00 67.87  ? 33  VAL   B CG2 1 
ATOM   997  N N   . LYS   B 1 35 ? 37.064  -12.455 -27.308 1.00 83.87  ? 34  LYS   B N   1 
ATOM   998  C CA  . LYS   B 1 35 ? 36.791  -12.726 -28.715 1.00 73.04  ? 34  LYS   B CA  1 
ATOM   999  C C   . LYS   B 1 35 ? 36.054  -14.069 -28.800 1.00 73.18  ? 34  LYS   B C   1 
ATOM   1000 O O   . LYS   B 1 35 ? 36.274  -14.941 -27.956 1.00 79.13  ? 34  LYS   B O   1 
ATOM   1001 C CB  . LYS   B 1 35 ? 38.067  -12.598 -29.558 1.00 64.45  ? 34  LYS   B CB  1 
ATOM   1002 N N   . PRO   B 1 36 ? 35.116  -14.278 -29.764 1.00 68.17  ? 35  PRO   B N   1 
ATOM   1003 C CA  . PRO   B 1 36 ? 34.334  -15.523 -29.816 1.00 57.30  ? 35  PRO   B CA  1 
ATOM   1004 C C   . PRO   B 1 36 ? 35.171  -16.793 -29.683 1.00 51.58  ? 35  PRO   B C   1 
ATOM   1005 O O   . PRO   B 1 36 ? 36.321  -16.804 -30.096 1.00 55.46  ? 35  PRO   B O   1 
ATOM   1006 C CB  . PRO   B 1 36 ? 33.580  -15.468 -31.159 1.00 60.67  ? 35  PRO   B CB  1 
ATOM   1007 C CG  . PRO   B 1 36 ? 34.077  -14.211 -31.858 1.00 64.83  ? 35  PRO   B CG  1 
ATOM   1008 C CD  . PRO   B 1 36 ? 34.741  -13.321 -30.823 1.00 60.29  ? 35  PRO   B CD  1 
ATOM   1009 N N   . PRO   B 1 37 ? 34.660  -17.891 -29.079 1.00 51.32  ? 36  PRO   B N   1 
ATOM   1010 C CA  . PRO   B 1 37 ? 35.361  -19.172 -29.127 1.00 54.94  ? 36  PRO   B CA  1 
ATOM   1011 C C   . PRO   B 1 37 ? 35.507  -19.505 -30.609 1.00 61.51  ? 36  PRO   B C   1 
ATOM   1012 O O   . PRO   B 1 37 ? 34.863  -18.876 -31.453 1.00 56.03  ? 36  PRO   B O   1 
ATOM   1013 C CB  . PRO   B 1 37 ? 34.400  -20.142 -28.405 1.00 55.61  ? 36  PRO   B CB  1 
ATOM   1014 C CG  . PRO   B 1 37 ? 33.504  -19.251 -27.560 1.00 51.43  ? 36  PRO   B CG  1 
ATOM   1015 C CD  . PRO   B 1 37 ? 33.386  -17.966 -28.346 1.00 53.39  ? 36  PRO   B CD  1 
ATOM   1016 N N   . PRO   B 1 38 ? 36.356  -20.491 -30.989 1.00 67.06  ? 37  PRO   B N   1 
ATOM   1017 C CA  . PRO   B 1 38 ? 36.484  -20.877 -32.401 1.00 66.90  ? 37  PRO   B CA  1 
ATOM   1018 C C   . PRO   B 1 38 ? 35.148  -21.300 -33.016 1.00 59.32  ? 37  PRO   B C   1 
ATOM   1019 O O   . PRO   B 1 38 ? 34.345  -21.961 -32.361 1.00 60.37  ? 37  PRO   B O   1 
ATOM   1020 C CB  . PRO   B 1 38 ? 37.525  -22.021 -32.377 1.00 63.16  ? 37  PRO   B CB  1 
ATOM   1021 C CG  . PRO   B 1 38 ? 38.289  -21.789 -31.087 1.00 64.70  ? 37  PRO   B CG  1 
ATOM   1022 C CD  . PRO   B 1 38 ? 37.253  -21.251 -30.098 1.00 66.68  ? 37  PRO   B CD  1 
ATOM   1023 N N   . ASN   B 1 39 ? 34.906  -20.855 -34.257 1.00 54.77  ? 38  ASN   B N   1 
ATOM   1024 C CA  . ASN   B 1 39 ? 33.769  -21.284 -35.066 1.00 56.28  ? 38  ASN   B CA  1 
ATOM   1025 C C   . ASN   B 1 39 ? 32.459  -20.589 -34.676 1.00 51.39  ? 38  ASN   B C   1 
ATOM   1026 O O   . ASN   B 1 39 ? 31.439  -20.864 -35.285 1.00 41.01  ? 38  ASN   B O   1 
ATOM   1027 C CB  . ASN   B 1 39 ? 33.533  -22.790 -34.986 1.00 58.57  ? 38  ASN   B CB  1 
ATOM   1028 C CG  . ASN   B 1 39 ? 34.745  -23.594 -35.395 1.00 66.01  ? 38  ASN   B CG  1 
ATOM   1029 O OD1 . ASN   B 1 39 ? 35.111  -24.550 -34.702 1.00 71.13  ? 38  ASN   B OD1 1 
ATOM   1030 N ND2 . ASN   B 1 39 ? 35.369  -23.238 -36.510 1.00 59.52  ? 38  ASN   B ND2 1 
ATOM   1031 N N   . LYS   B 1 40 ? 32.480  -19.705 -33.668 1.00 49.30  ? 39  LYS   B N   1 
ATOM   1032 C CA  . LYS   B 1 40 ? 31.263  -19.122 -33.126 1.00 47.69  ? 39  LYS   B CA  1 
ATOM   1033 C C   . LYS   B 1 40 ? 31.222  -17.631 -33.427 1.00 47.90  ? 39  LYS   B C   1 
ATOM   1034 O O   . LYS   B 1 40 ? 32.235  -17.044 -33.787 1.00 43.49  ? 39  LYS   B O   1 
ATOM   1035 C CB  . LYS   B 1 40 ? 31.241  -19.407 -31.625 1.00 49.05  ? 39  LYS   B CB  1 
ATOM   1036 C CG  . LYS   B 1 40 ? 31.038  -20.874 -31.265 1.00 49.21  ? 39  LYS   B CG  1 
ATOM   1037 C CD  . LYS   B 1 40 ? 30.991  -20.979 -29.746 1.00 61.60  ? 39  LYS   B CD  1 
ATOM   1038 C CE  . LYS   B 1 40 ? 29.901  -21.827 -29.160 1.00 64.89  ? 39  LYS   B CE  1 
ATOM   1039 N NZ  . LYS   B 1 40 ? 29.988  -23.237 -29.542 1.00 61.00  ? 39  LYS   B NZ  1 
ATOM   1040 N N   . TYR   B 1 41 ? 30.031  -17.037 -33.302 1.00 42.26  ? 40  TYR   B N   1 
ATOM   1041 C CA  . TYR   B 1 41 ? 29.832  -15.629 -33.604 1.00 40.64  ? 40  TYR   B CA  1 
ATOM   1042 C C   . TYR   B 1 41 ? 29.198  -14.904 -32.414 1.00 37.68  ? 40  TYR   B C   1 
ATOM   1043 O O   . TYR   B 1 41 ? 28.417  -15.489 -31.667 1.00 36.02  ? 40  TYR   B O   1 
ATOM   1044 C CB  . TYR   B 1 41 ? 28.865  -15.515 -34.778 1.00 38.52  ? 40  TYR   B CB  1 
ATOM   1045 C CG  . TYR   B 1 41 ? 29.363  -15.966 -36.144 1.00 38.14  ? 40  TYR   B CG  1 
ATOM   1046 C CD1 . TYR   B 1 41 ? 30.065  -15.104 -36.989 1.00 37.65  ? 40  TYR   B CD1 1 
ATOM   1047 C CD2 . TYR   B 1 41 ? 29.084  -17.244 -36.610 1.00 41.08  ? 40  TYR   B CD2 1 
ATOM   1048 C CE1 . TYR   B 1 41 ? 30.517  -15.530 -38.233 1.00 43.39  ? 40  TYR   B CE1 1 
ATOM   1049 C CE2 . TYR   B 1 41 ? 29.506  -17.669 -37.859 1.00 40.80  ? 40  TYR   B CE2 1 
ATOM   1050 C CZ  . TYR   B 1 41 ? 30.237  -16.816 -38.674 1.00 43.49  ? 40  TYR   B CZ  1 
ATOM   1051 O OH  . TYR   B 1 41 ? 30.625  -17.251 -39.925 1.00 41.09  ? 40  TYR   B OH  1 
ATOM   1052 N N   . PRO   B 1 42 ? 29.463  -13.583 -32.249 1.00 40.96  ? 41  PRO   B N   1 
ATOM   1053 C CA  . PRO   B 1 42 ? 28.786  -12.788 -31.232 1.00 34.91  ? 41  PRO   B CA  1 
ATOM   1054 C C   . PRO   B 1 42 ? 27.359  -12.564 -31.718 1.00 35.40  ? 41  PRO   B C   1 
ATOM   1055 O O   . PRO   B 1 42 ? 27.128  -11.933 -32.760 1.00 38.49  ? 41  PRO   B O   1 
ATOM   1056 C CB  . PRO   B 1 42 ? 29.586  -11.468 -31.136 1.00 38.73  ? 41  PRO   B CB  1 
ATOM   1057 C CG  . PRO   B 1 42 ? 30.401  -11.396 -32.422 1.00 39.20  ? 41  PRO   B CG  1 
ATOM   1058 C CD  . PRO   B 1 42 ? 30.381  -12.778 -33.079 1.00 38.91  ? 41  PRO   B CD  1 
ATOM   1059 N N   . ILE   B 1 43 ? 26.398  -13.055 -30.918 1.00 33.05  ? 42  ILE   B N   1 
ATOM   1060 C CA  . ILE   B 1 43 ? 24.987  -12.853 -31.230 1.00 31.84  ? 42  ILE   B CA  1 
ATOM   1061 C C   . ILE   B 1 43 ? 24.366  -11.782 -30.329 1.00 29.93  ? 42  ILE   B C   1 
ATOM   1062 O O   . ILE   B 1 43 ? 24.626  -11.766 -29.144 1.00 31.04  ? 42  ILE   B O   1 
ATOM   1063 C CB  . ILE   B 1 43 ? 24.237  -14.185 -31.107 1.00 26.77  ? 42  ILE   B CB  1 
ATOM   1064 C CG1 . ILE   B 1 43 ? 24.949  -15.285 -31.919 1.00 31.28  ? 42  ILE   B CG1 1 
ATOM   1065 C CG2 . ILE   B 1 43 ? 22.780  -14.008 -31.544 1.00 29.80  ? 42  ILE   B CG2 1 
ATOM   1066 C CD1 . ILE   B 1 43 ? 25.136  -14.944 -33.391 1.00 31.90  ? 42  ILE   B CD1 1 
ATOM   1067 N N   . PHE   B 1 44 ? 23.520  -10.912 -30.902 1.00 32.58  ? 43  PHE   B N   1 
ATOM   1068 C CA  . PHE   B 1 44 ? 22.736  -9.967  -30.113 1.00 32.82  ? 43  PHE   B CA  1 
ATOM   1069 C C   . PHE   B 1 44 ? 21.265  -10.334 -30.287 1.00 29.51  ? 43  PHE   B C   1 
ATOM   1070 O O   . PHE   B 1 44 ? 20.761  -10.351 -31.408 1.00 30.74  ? 43  PHE   B O   1 
ATOM   1071 C CB  . PHE   B 1 44 ? 22.956  -8.508  -30.538 1.00 29.92  ? 43  PHE   B CB  1 
ATOM   1072 C CG  . PHE   B 1 44 ? 22.031  -7.510  -29.842 1.00 30.86  ? 43  PHE   B CG  1 
ATOM   1073 C CD1 . PHE   B 1 44 ? 20.854  -7.074  -30.449 1.00 33.73  ? 43  PHE   B CD1 1 
ATOM   1074 C CD2 . PHE   B 1 44 ? 22.351  -7.001  -28.582 1.00 34.35  ? 43  PHE   B CD2 1 
ATOM   1075 C CE1 . PHE   B 1 44 ? 20.019  -6.144  -29.827 1.00 33.77  ? 43  PHE   B CE1 1 
ATOM   1076 C CE2 . PHE   B 1 44 ? 21.512  -6.068  -27.963 1.00 29.64  ? 43  PHE   B CE2 1 
ATOM   1077 C CZ  . PHE   B 1 44 ? 20.355  -5.655  -28.580 1.00 33.25  ? 43  PHE   B CZ  1 
ATOM   1078 N N   . PHE   B 1 45 ? 20.563  -10.608 -29.174 1.00 29.39  ? 44  PHE   B N   1 
ATOM   1079 C CA  . PHE   B 1 45 ? 19.161  -10.993 -29.212 1.00 28.09  ? 44  PHE   B CA  1 
ATOM   1080 C C   . PHE   B 1 45 ? 18.279  -9.761  -29.072 1.00 29.78  ? 44  PHE   B C   1 
ATOM   1081 O O   . PHE   B 1 45 ? 18.365  -9.037  -28.073 1.00 31.96  ? 44  PHE   B O   1 
ATOM   1082 C CB  . PHE   B 1 45 ? 18.946  -11.962 -28.033 1.00 28.54  ? 44  PHE   B CB  1 
ATOM   1083 C CG  . PHE   B 1 45 ? 19.638  -13.310 -28.236 1.00 27.50  ? 44  PHE   B CG  1 
ATOM   1084 C CD1 . PHE   B 1 45 ? 20.917  -13.541 -27.762 1.00 28.34  ? 44  PHE   B CD1 1 
ATOM   1085 C CD2 . PHE   B 1 45 ? 18.990  -14.363 -28.895 1.00 30.82  ? 44  PHE   B CD2 1 
ATOM   1086 C CE1 . PHE   B 1 45 ? 21.574  -14.737 -27.991 1.00 30.21  ? 44  PHE   B CE1 1 
ATOM   1087 C CE2 . PHE   B 1 45 ? 19.633  -15.582 -29.083 1.00 29.47  ? 44  PHE   B CE2 1 
ATOM   1088 C CZ  . PHE   B 1 45 ? 20.918  -15.771 -28.629 1.00 30.40  ? 44  PHE   B CZ  1 
ATOM   1089 N N   . PHE   B 1 46 ? 17.437  -9.535  -30.083 1.00 26.34  ? 45  PHE   B N   1 
ATOM   1090 C CA  . PHE   B 1 46 ? 16.485  -8.438  -30.073 1.00 29.66  ? 45  PHE   B CA  1 
ATOM   1091 C C   . PHE   B 1 46 ? 15.462  -8.651  -28.950 1.00 32.07  ? 45  PHE   B C   1 
ATOM   1092 O O   . PHE   B 1 46 ? 15.190  -9.789  -28.537 1.00 28.49  ? 45  PHE   B O   1 
ATOM   1093 C CB  . PHE   B 1 46 ? 15.778  -8.292  -31.415 1.00 25.78  ? 45  PHE   B CB  1 
ATOM   1094 C CG  . PHE   B 1 46 ? 16.705  -7.825  -32.535 1.00 32.30  ? 45  PHE   B CG  1 
ATOM   1095 C CD1 . PHE   B 1 46 ? 17.237  -6.526  -32.544 1.00 34.35  ? 45  PHE   B CD1 1 
ATOM   1096 C CD2 . PHE   B 1 46 ? 17.035  -8.686  -33.583 1.00 30.31  ? 45  PHE   B CD2 1 
ATOM   1097 C CE1 . PHE   B 1 46 ? 18.075  -6.102  -33.577 1.00 31.11  ? 45  PHE   B CE1 1 
ATOM   1098 C CE2 . PHE   B 1 46 ? 17.859  -8.252  -34.625 1.00 31.64  ? 45  PHE   B CE2 1 
ATOM   1099 C CZ  . PHE   B 1 46 ? 18.348  -6.950  -34.627 1.00 28.81  ? 45  PHE   B CZ  1 
ATOM   1100 N N   . GLY   B 1 47 ? 14.913  -7.536  -28.448 1.00 32.76  ? 46  GLY   B N   1 
ATOM   1101 C CA  . GLY   B 1 47 ? 13.888  -7.606  -27.414 1.00 29.33  ? 46  GLY   B CA  1 
ATOM   1102 C C   . GLY   B 1 47 ? 14.524  -7.763  -26.031 1.00 30.27  ? 46  GLY   B C   1 
ATOM   1103 O O   . GLY   B 1 47 ? 14.399  -6.883  -25.192 1.00 32.11  ? 46  GLY   B O   1 
ATOM   1104 N N   . THR   B 1 48 ? 15.238  -8.865  -25.801 1.00 31.66  ? 47  THR   B N   1 
ATOM   1105 C CA  . THR   B 1 48 ? 15.878  -9.085  -24.523 1.00 32.57  ? 47  THR   B CA  1 
ATOM   1106 C C   . THR   B 1 48 ? 17.136  -8.235  -24.438 1.00 35.66  ? 47  THR   B C   1 
ATOM   1107 O O   . THR   B 1 48 ? 17.554  -7.853  -23.338 1.00 32.28  ? 47  THR   B O   1 
ATOM   1108 C CB  . THR   B 1 48 ? 16.199  -10.565 -24.289 1.00 34.52  ? 47  THR   B CB  1 
ATOM   1109 O OG1 . THR   B 1 48 ? 17.223  -10.990 -25.197 1.00 33.86  ? 47  THR   B OG1 1 
ATOM   1110 C CG2 . THR   B 1 48 ? 14.956  -11.445 -24.231 1.00 29.83  ? 47  THR   B CG2 1 
ATOM   1111 N N   . HIS   B 1 49 ? 17.756  -7.999  -25.603 1.00 31.47  ? 48  HIS   B N   1 
ATOM   1112 C CA  . HIS   B 1 49 ? 19.040  -7.316  -25.686 1.00 34.55  ? 48  HIS   B CA  1 
ATOM   1113 C C   . HIS   B 1 49 ? 20.136  -8.077  -24.955 1.00 35.25  ? 48  HIS   B C   1 
ATOM   1114 O O   . HIS   B 1 49 ? 21.107  -7.457  -24.519 1.00 41.30  ? 48  HIS   B O   1 
ATOM   1115 C CB  . HIS   B 1 49 ? 18.978  -5.833  -25.268 1.00 32.47  ? 48  HIS   B CB  1 
ATOM   1116 C CG  . HIS   B 1 49 ? 17.806  -5.106  -25.828 1.00 36.11  ? 48  HIS   B CG  1 
ATOM   1117 N ND1 . HIS   B 1 49 ? 17.033  -4.272  -25.049 1.00 38.54  ? 48  HIS   B ND1 1 
ATOM   1118 C CD2 . HIS   B 1 49 ? 17.234  -5.104  -27.049 1.00 31.83  ? 48  HIS   B CD2 1 
ATOM   1119 C CE1 . HIS   B 1 49 ? 16.028  -3.792  -25.783 1.00 42.53  ? 48  HIS   B CE1 1 
ATOM   1120 N NE2 . HIS   B 1 49 ? 16.139  -4.278  -27.012 1.00 38.82  ? 48  HIS   B NE2 1 
ATOM   1121 N N   . GLU   B 1 50 ? 20.027  -9.411  -24.868 1.00 32.01  ? 49  GLU   B N   1 
ATOM   1122 C CA  . GLU   B 1 50 ? 21.078  -10.220 -24.265 1.00 34.39  ? 49  GLU   B CA  1 
ATOM   1123 C C   . GLU   B 1 50 ? 22.075  -10.629 -25.355 1.00 35.87  ? 49  GLU   B C   1 
ATOM   1124 O O   . GLU   B 1 50 ? 21.805  -10.428 -26.547 1.00 35.93  ? 49  GLU   B O   1 
ATOM   1125 C CB  . GLU   B 1 50 ? 20.471  -11.525 -23.754 1.00 39.33  ? 49  GLU   B CB  1 
ATOM   1126 C CG  . GLU   B 1 50 ? 19.491  -11.336 -22.599 1.00 39.34  ? 49  GLU   B CG  1 
ATOM   1127 C CD  . GLU   B 1 50 ? 20.089  -11.182 -21.203 1.00 50.94  ? 49  GLU   B CD  1 
ATOM   1128 O OE1 . GLU   B 1 50 ? 21.325  -11.206 -21.000 1.00 45.67  ? 49  GLU   B OE1 1 
ATOM   1129 O OE2 . GLU   B 1 50 ? 19.260  -11.042 -20.279 1.00 52.17  ? 49  GLU   B OE2 1 
ATOM   1130 N N   . THR   B 1 51 ? 23.196  -11.239 -24.953 1.00 31.56  ? 50  THR   B N   1 
ATOM   1131 C CA  . THR   B 1 51 ? 24.185  -11.685 -25.927 1.00 35.96  ? 50  THR   B CA  1 
ATOM   1132 C C   . THR   B 1 51 ? 24.586  -13.124 -25.602 1.00 36.71  ? 50  THR   B C   1 
ATOM   1133 O O   . THR   B 1 51 ? 24.418  -13.578 -24.472 1.00 38.35  ? 50  THR   B O   1 
ATOM   1134 C CB  . THR   B 1 51 ? 25.375  -10.719 -26.013 1.00 39.07  ? 50  THR   B CB  1 
ATOM   1135 O OG1 . THR   B 1 51 ? 25.971  -10.673 -24.726 1.00 41.74  ? 50  THR   B OG1 1 
ATOM   1136 C CG2 . THR   B 1 51 ? 24.982  -9.277  -26.288 1.00 35.58  ? 50  THR   B CG2 1 
ATOM   1137 N N   . ALA   B 1 52 ? 25.046  -13.866 -26.620 1.00 39.55  ? 51  ALA   B N   1 
ATOM   1138 C CA  . ALA   B 1 52 ? 25.759  -15.122 -26.447 1.00 38.82  ? 51  ALA   B CA  1 
ATOM   1139 C C   . ALA   B 1 52 ? 26.629  -15.374 -27.678 1.00 37.14  ? 51  ALA   B C   1 
ATOM   1140 O O   . ALA   B 1 52 ? 26.554  -14.625 -28.656 1.00 36.77  ? 51  ALA   B O   1 
ATOM   1141 C CB  . ALA   B 1 52 ? 24.805  -16.274 -26.204 1.00 36.55  ? 51  ALA   B CB  1 
ATOM   1142 N N   . PHE   B 1 53 ? 27.490  -16.398 -27.593 1.00 34.60  ? 52  PHE   B N   1 
ATOM   1143 C CA  . PHE   B 1 53 ? 28.223  -16.882 -28.752 1.00 38.83  ? 52  PHE   B CA  1 
ATOM   1144 C C   . PHE   B 1 53 ? 27.540  -18.162 -29.250 1.00 39.35  ? 52  PHE   B C   1 
ATOM   1145 O O   . PHE   B 1 53 ? 27.256  -19.072 -28.466 1.00 42.67  ? 52  PHE   B O   1 
ATOM   1146 C CB  . PHE   B 1 53 ? 29.696  -17.139 -28.395 1.00 38.22  ? 52  PHE   B CB  1 
ATOM   1147 C CG  . PHE   B 1 53 ? 30.526  -15.950 -27.936 1.00 40.88  ? 52  PHE   B CG  1 
ATOM   1148 C CD1 . PHE   B 1 53 ? 30.834  -14.913 -28.810 1.00 45.98  ? 52  PHE   B CD1 1 
ATOM   1149 C CD2 . PHE   B 1 53 ? 31.031  -15.895 -26.639 1.00 45.86  ? 52  PHE   B CD2 1 
ATOM   1150 C CE1 . PHE   B 1 53 ? 31.588  -13.822 -28.390 1.00 43.94  ? 52  PHE   B CE1 1 
ATOM   1151 C CE2 . PHE   B 1 53 ? 31.793  -14.809 -26.218 1.00 48.58  ? 52  PHE   B CE2 1 
ATOM   1152 C CZ  . PHE   B 1 53 ? 32.060  -13.772 -27.090 1.00 45.78  ? 52  PHE   B CZ  1 
ATOM   1153 N N   . LEU   B 1 54 ? 27.266  -18.228 -30.562 1.00 36.89  ? 53  LEU   B N   1 
ATOM   1154 C CA  . LEU   B 1 54 ? 26.616  -19.379 -31.168 1.00 33.85  ? 53  LEU   B CA  1 
ATOM   1155 C C   . LEU   B 1 54 ? 27.353  -19.734 -32.460 1.00 38.10  ? 53  LEU   B C   1 
ATOM   1156 O O   . LEU   B 1 54 ? 27.928  -18.852 -33.126 1.00 33.12  ? 53  LEU   B O   1 
ATOM   1157 C CB  . LEU   B 1 54 ? 25.132  -19.118 -31.465 1.00 34.62  ? 53  LEU   B CB  1 
ATOM   1158 C CG  . LEU   B 1 54 ? 24.188  -19.011 -30.267 1.00 37.50  ? 53  LEU   B CG  1 
ATOM   1159 C CD1 . LEU   B 1 54 ? 22.810  -18.665 -30.788 1.00 31.13  ? 53  LEU   B CD1 1 
ATOM   1160 C CD2 . LEU   B 1 54 ? 24.148  -20.389 -29.614 1.00 39.71  ? 53  LEU   B CD2 1 
ATOM   1161 N N   . GLY   B 1 55 ? 27.296  -21.028 -32.795 1.00 37.97  ? 54  GLY   B N   1 
ATOM   1162 C CA  . GLY   B 1 55 ? 27.835  -21.556 -34.042 1.00 35.95  ? 54  GLY   B CA  1 
ATOM   1163 C C   . GLY   B 1 55 ? 26.762  -21.552 -35.130 1.00 33.80  ? 54  GLY   B C   1 
ATOM   1164 O O   . GLY   B 1 55 ? 25.562  -21.419 -34.849 1.00 33.65  ? 54  GLY   B O   1 
ATOM   1165 N N   . PRO   B 1 56 ? 27.166  -21.660 -36.414 1.00 32.80  ? 55  PRO   B N   1 
ATOM   1166 C CA  . PRO   B 1 56 ? 26.226  -21.749 -37.534 1.00 33.41  ? 55  PRO   B CA  1 
ATOM   1167 C C   . PRO   B 1 56 ? 25.054  -22.722 -37.425 1.00 30.70  ? 55  PRO   B C   1 
ATOM   1168 O O   . PRO   B 1 56 ? 24.003  -22.462 -37.993 1.00 31.10  ? 55  PRO   B O   1 
ATOM   1169 C CB  . PRO   B 1 56 ? 27.090  -22.031 -38.780 1.00 38.06  ? 55  PRO   B CB  1 
ATOM   1170 C CG  . PRO   B 1 56 ? 28.526  -22.095 -38.274 1.00 36.18  ? 55  PRO   B CG  1 
ATOM   1171 C CD  . PRO   B 1 56 ? 28.573  -21.652 -36.830 1.00 33.94  ? 55  PRO   B CD  1 
ATOM   1172 N N   . LYS   B 1 57 ? 25.204  -23.823 -36.677 1.00 30.59  ? 56  LYS   B N   1 
ATOM   1173 C CA  . LYS   B 1 57 ? 24.140  -24.827 -36.665 1.00 33.27  ? 56  LYS   B CA  1 
ATOM   1174 C C   . LYS   B 1 57 ? 22.887  -24.250 -36.007 1.00 31.31  ? 56  LYS   B C   1 
ATOM   1175 O O   . LYS   B 1 57 ? 21.769  -24.760 -36.205 1.00 30.71  ? 56  LYS   B O   1 
ATOM   1176 C CB  . LYS   B 1 57 ? 24.593  -26.130 -35.988 1.00 39.76  ? 56  LYS   B CB  1 
ATOM   1177 C CG  . LYS   B 1 57 ? 24.672  -26.071 -34.475 1.00 41.54  ? 56  LYS   B CG  1 
ATOM   1178 C CD  . LYS   B 1 57 ? 24.790  -27.465 -33.866 1.00 41.90  ? 56  LYS   B CD  1 
ATOM   1179 C CE  . LYS   B 1 57 ? 25.082  -27.431 -32.387 1.00 45.51  ? 56  LYS   B CE  1 
ATOM   1180 N NZ  . LYS   B 1 57 ? 23.941  -26.979 -31.595 1.00 44.55  ? 56  LYS   B NZ  1 
ATOM   1181 N N   . ASP   B 1 58 ? 23.095  -23.164 -35.243 1.00 28.58  ? 57  ASP   B N   1 
ATOM   1182 C CA  . ASP   B 1 58 ? 22.024  -22.556 -34.465 1.00 30.82  ? 57  ASP   B CA  1 
ATOM   1183 C C   . ASP   B 1 58 ? 21.612  -21.206 -35.043 1.00 31.47  ? 57  ASP   B C   1 
ATOM   1184 O O   . ASP   B 1 58 ? 20.859  -20.470 -34.381 1.00 29.74  ? 57  ASP   B O   1 
ATOM   1185 C CB  . ASP   B 1 58 ? 22.443  -22.414 -33.015 1.00 30.15  ? 57  ASP   B CB  1 
ATOM   1186 C CG  . ASP   B 1 58 ? 22.601  -23.737 -32.266 1.00 37.71  ? 57  ASP   B CG  1 
ATOM   1187 O OD1 . ASP   B 1 58 ? 21.658  -24.571 -32.339 1.00 33.52  ? 57  ASP   B OD1 1 
ATOM   1188 O OD2 . ASP   B 1 58 ? 23.643  -23.901 -31.606 1.00 39.50  ? 57  ASP   B OD2 1 
ATOM   1189 N N   . LEU   B 1 59 ? 22.116  -20.889 -36.247 1.00 30.93  ? 58  LEU   B N   1 
ATOM   1190 C CA  . LEU   B 1 59 ? 21.854  -19.592 -36.864 1.00 31.83  ? 58  LEU   B CA  1 
ATOM   1191 C C   . LEU   B 1 59 ? 21.097  -19.750 -38.173 1.00 30.01  ? 58  LEU   B C   1 
ATOM   1192 O O   . LEU   B 1 59 ? 21.547  -20.429 -39.095 1.00 33.04  ? 58  LEU   B O   1 
ATOM   1193 C CB  . LEU   B 1 59 ? 23.159  -18.825 -37.057 1.00 30.34  ? 58  LEU   B CB  1 
ATOM   1194 C CG  . LEU   B 1 59 ? 23.992  -18.633 -35.794 1.00 30.98  ? 58  LEU   B CG  1 
ATOM   1195 C CD1 . LEU   B 1 59 ? 25.313  -17.906 -36.085 1.00 31.47  ? 58  LEU   B CD1 1 
ATOM   1196 C CD2 . LEU   B 1 59 ? 23.175  -17.787 -34.823 1.00 33.07  ? 58  LEU   B CD2 1 
ATOM   1197 N N   . PHE   B 1 60 ? 19.931  -19.112 -38.234 1.00 27.21  ? 59  PHE   B N   1 
ATOM   1198 C CA  . PHE   B 1 60 ? 18.999  -19.271 -39.331 1.00 29.09  ? 59  PHE   B CA  1 
ATOM   1199 C C   . PHE   B 1 60 ? 18.814  -17.910 -39.996 1.00 29.26  ? 59  PHE   B C   1 
ATOM   1200 O O   . PHE   B 1 60 ? 18.150  -17.044 -39.425 1.00 26.57  ? 59  PHE   B O   1 
ATOM   1201 C CB  . PHE   B 1 60 ? 17.644  -19.856 -38.895 1.00 27.12  ? 59  PHE   B CB  1 
ATOM   1202 C CG  . PHE   B 1 60 ? 17.758  -21.268 -38.319 1.00 31.25  ? 59  PHE   B CG  1 
ATOM   1203 C CD1 . PHE   B 1 60 ? 18.252  -21.466 -37.032 1.00 28.27  ? 59  PHE   B CD1 1 
ATOM   1204 C CD2 . PHE   B 1 60 ? 17.319  -22.381 -39.048 1.00 33.16  ? 59  PHE   B CD2 1 
ATOM   1205 C CE1 . PHE   B 1 60 ? 18.363  -22.755 -36.493 1.00 31.37  ? 59  PHE   B CE1 1 
ATOM   1206 C CE2 . PHE   B 1 60 ? 17.419  -23.665 -38.511 1.00 33.98  ? 59  PHE   B CE2 1 
ATOM   1207 C CZ  . PHE   B 1 60 ? 17.945  -23.856 -37.241 1.00 32.46  ? 59  PHE   B CZ  1 
ATOM   1208 N N   . PRO   B 1 61 ? 19.391  -17.682 -41.209 1.00 34.21  ? 60  PRO   B N   1 
ATOM   1209 C CA  . PRO   B 1 61 ? 19.152  -16.438 -41.954 1.00 35.06  ? 60  PRO   B CA  1 
ATOM   1210 C C   . PRO   B 1 61 ? 17.704  -15.954 -41.900 1.00 35.97  ? 60  PRO   B C   1 
ATOM   1211 O O   . PRO   B 1 61 ? 16.764  -16.705 -42.150 1.00 32.43  ? 60  PRO   B O   1 
ATOM   1212 C CB  . PRO   B 1 61 ? 19.633  -16.776 -43.374 1.00 31.47  ? 60  PRO   B CB  1 
ATOM   1213 C CG  . PRO   B 1 61 ? 20.788  -17.720 -43.114 1.00 42.06  ? 60  PRO   B CG  1 
ATOM   1214 C CD  . PRO   B 1 61 ? 20.310  -18.594 -41.925 1.00 38.67  ? 60  PRO   B CD  1 
ATOM   1215 N N   . TYR   B 1 62 ? 17.529  -14.669 -41.548 1.00 33.44  ? 61  TYR   B N   1 
ATOM   1216 C CA  . TYR   B 1 62 ? 16.221  -14.162 -41.189 1.00 33.30  ? 61  TYR   B CA  1 
ATOM   1217 C C   . TYR   B 1 62 ? 15.200  -14.242 -42.324 1.00 34.33  ? 61  TYR   B C   1 
ATOM   1218 O O   . TYR   B 1 62 ? 14.061  -14.651 -42.096 1.00 36.16  ? 61  TYR   B O   1 
ATOM   1219 C CB  . TYR   B 1 62 ? 16.394  -12.715 -40.723 1.00 35.16  ? 61  TYR   B CB  1 
ATOM   1220 C CG  . TYR   B 1 62 ? 15.084  -12.000 -40.465 1.00 37.23  ? 61  TYR   B CG  1 
ATOM   1221 C CD1 . TYR   B 1 62 ? 14.299  -12.320 -39.365 1.00 39.48  ? 61  TYR   B CD1 1 
ATOM   1222 C CD2 . TYR   B 1 62 ? 14.656  -10.973 -41.303 1.00 45.45  ? 61  TYR   B CD2 1 
ATOM   1223 C CE1 . TYR   B 1 62 ? 13.109  -11.649 -39.121 1.00 38.26  ? 61  TYR   B CE1 1 
ATOM   1224 C CE2 . TYR   B 1 62 ? 13.474  -10.287 -41.066 1.00 47.66  ? 61  TYR   B CE2 1 
ATOM   1225 C CZ  . TYR   B 1 62 ? 12.700  -10.634 -39.970 1.00 44.55  ? 61  TYR   B CZ  1 
ATOM   1226 O OH  . TYR   B 1 62 ? 11.535  -9.978  -39.734 1.00 46.78  ? 61  TYR   B OH  1 
ATOM   1227 N N   . ASP   B 1 63 ? 15.598  -13.804 -43.528 1.00 40.69  ? 62  ASP   B N   1 
ATOM   1228 C CA  . ASP   B 1 63 ? 14.716  -13.740 -44.691 1.00 48.01  ? 62  ASP   B CA  1 
ATOM   1229 C C   . ASP   B 1 63 ? 14.170  -15.129 -45.026 1.00 38.49  ? 62  ASP   B C   1 
ATOM   1230 O O   . ASP   B 1 63 ? 12.957  -15.312 -45.121 1.00 45.87  ? 62  ASP   B O   1 
ATOM   1231 C CB  . ASP   B 1 63 ? 15.403  -13.063 -45.868 1.00 53.53  ? 62  ASP   B CB  1 
ATOM   1232 C CG  . ASP   B 1 63 ? 15.340  -11.540 -45.893 1.00 73.33  ? 62  ASP   B CG  1 
ATOM   1233 O OD1 . ASP   B 1 63 ? 14.501  -10.953 -45.154 1.00 75.29  ? 62  ASP   B OD1 1 
ATOM   1234 O OD2 . ASP   B 1 63 ? 16.137  -10.939 -46.650 1.00 82.43  ? 62  ASP   B OD2 1 
ATOM   1235 N N   . LYS   B 1 64 ? 15.064  -16.110 -45.144 1.00 43.15  ? 63  LYS   B N   1 
ATOM   1236 C CA  . LYS   B 1 64 ? 14.650  -17.487 -45.377 1.00 43.63  ? 63  LYS   B CA  1 
ATOM   1237 C C   . LYS   B 1 64 ? 13.666  -17.988 -44.307 1.00 42.17  ? 63  LYS   B C   1 
ATOM   1238 O O   . LYS   B 1 64 ? 12.736  -18.742 -44.625 1.00 42.82  ? 63  LYS   B O   1 
ATOM   1239 C CB  . LYS   B 1 64 ? 15.877  -18.405 -45.400 1.00 45.85  ? 63  LYS   B CB  1 
ATOM   1240 C CG  . LYS   B 1 64 ? 15.561  -19.850 -45.741 1.00 44.31  ? 63  LYS   B CG  1 
ATOM   1241 C CD  . LYS   B 1 64 ? 16.825  -20.686 -45.880 1.00 46.89  ? 63  LYS   B CD  1 
ATOM   1242 C CE  . LYS   B 1 64 ? 16.578  -21.926 -46.710 1.00 49.68  ? 63  LYS   B CE  1 
ATOM   1243 N NZ  . LYS   B 1 64 ? 15.553  -22.812 -46.156 1.00 48.88  ? 63  LYS   B NZ  1 
ATOM   1244 N N   . SER   B 1 65 ? 13.861  -17.597 -43.040 1.00 40.15  ? 64  SER   B N   1 
ATOM   1245 C CA  . SER   B 1 65 ? 13.212  -18.337 -41.948 1.00 42.30  ? 64  SER   B CA  1 
ATOM   1246 C C   . SER   B 1 65 ? 12.094  -17.561 -41.248 1.00 41.93  ? 64  SER   B C   1 
ATOM   1247 O O   . SER   B 1 65 ? 11.414  -18.092 -40.358 1.00 40.12  ? 64  SER   B O   1 
ATOM   1248 C CB  . SER   B 1 65 ? 14.227  -18.859 -40.969 1.00 40.95  ? 64  SER   B CB  1 
ATOM   1249 O OG  . SER   B 1 65 ? 15.056  -17.783 -40.553 1.00 56.06  ? 64  SER   B OG  1 
ATOM   1250 N N   . LYS   B 1 66 ? 11.845  -16.324 -41.685 1.00 39.07  ? 65  LYS   B N   1 
ATOM   1251 C CA  . LYS   B 1 66 ? 10.967  -15.444 -40.920 1.00 42.09  ? 65  LYS   B CA  1 
ATOM   1252 C C   . LYS   B 1 66 ? 9.530   -15.966 -40.856 1.00 46.41  ? 65  LYS   B C   1 
ATOM   1253 O O   . LYS   B 1 66 ? 8.839   -15.777 -39.856 1.00 53.37  ? 65  LYS   B O   1 
ATOM   1254 C CB  . LYS   B 1 66 ? 11.007  -13.992 -41.412 1.00 37.91  ? 65  LYS   B CB  1 
ATOM   1255 C CG  . LYS   B 1 66 ? 10.546  -13.794 -42.850 1.00 43.30  ? 65  LYS   B CG  1 
ATOM   1256 N N   . ASP   B 1 67 ? 9.047   -16.615 -41.912 1.00 45.31  ? 66  ASP   B N   1 
ATOM   1257 C CA  . ASP   B 1 67 ? 7.637   -16.965 -41.869 1.00 51.13  ? 66  ASP   B CA  1 
ATOM   1258 C C   . ASP   B 1 67 ? 7.428   -18.185 -40.965 1.00 50.03  ? 66  ASP   B C   1 
ATOM   1259 O O   . ASP   B 1 67 ? 6.351   -18.366 -40.392 1.00 53.50  ? 66  ASP   B O   1 
ATOM   1260 C CB  . ASP   B 1 67 ? 6.981   -16.898 -43.240 1.00 65.48  ? 66  ASP   B CB  1 
ATOM   1261 C CG  . ASP   B 1 67 ? 7.642   -17.725 -44.331 1.00 78.88  ? 66  ASP   B CG  1 
ATOM   1262 O OD1 . ASP   B 1 67 ? 7.803   -17.201 -45.462 1.00 82.31  ? 66  ASP   B OD1 1 
ATOM   1263 O OD2 . ASP   B 1 67 ? 8.005   -18.881 -44.031 1.00 81.91  ? 66  ASP   B OD2 1 
ATOM   1264 N N   . LYS   B 1 68 ? 8.483   -18.987 -40.802 1.00 43.04  ? 67  LYS   B N   1 
ATOM   1265 C CA  . LYS   B 1 68 ? 8.455   -20.162 -39.934 1.00 40.84  ? 67  LYS   B CA  1 
ATOM   1266 C C   . LYS   B 1 68 ? 8.648   -19.779 -38.467 1.00 35.91  ? 67  LYS   B C   1 
ATOM   1267 O O   . LYS   B 1 68 ? 7.919   -20.284 -37.609 1.00 37.40  ? 67  LYS   B O   1 
ATOM   1268 C CB  . LYS   B 1 68 ? 9.507   -21.166 -40.409 1.00 42.65  ? 67  LYS   B CB  1 
ATOM   1269 C CG  . LYS   B 1 68 ? 9.707   -22.401 -39.561 1.00 49.74  ? 67  LYS   B CG  1 
ATOM   1270 C CD  . LYS   B 1 68 ? 10.521  -23.386 -40.394 1.00 57.70  ? 67  LYS   B CD  1 
ATOM   1271 C CE  . LYS   B 1 68 ? 10.972  -24.596 -39.639 1.00 62.75  ? 67  LYS   B CE  1 
ATOM   1272 N NZ  . LYS   B 1 68 ? 9.859   -25.458 -39.229 1.00 67.96  ? 67  LYS   B NZ  1 
ATOM   1273 N N   . TYR   B 1 69 ? 9.633   -18.905 -38.179 1.00 30.94  ? 68  TYR   B N   1 
ATOM   1274 C CA  . TYR   B 1 69 ? 10.067  -18.659 -36.804 1.00 31.56  ? 68  TYR   B CA  1 
ATOM   1275 C C   . TYR   B 1 69 ? 9.484   -17.354 -36.275 1.00 37.69  ? 68  TYR   B C   1 
ATOM   1276 O O   . TYR   B 1 69 ? 9.502   -17.135 -35.069 1.00 40.34  ? 68  TYR   B O   1 
ATOM   1277 C CB  . TYR   B 1 69 ? 11.583  -18.730 -36.585 1.00 32.21  ? 68  TYR   B CB  1 
ATOM   1278 C CG  . TYR   B 1 69 ? 12.187  -20.106 -36.861 1.00 34.65  ? 68  TYR   B CG  1 
ATOM   1279 C CD1 . TYR   B 1 69 ? 11.637  -21.259 -36.304 1.00 36.60  ? 68  TYR   B CD1 1 
ATOM   1280 C CD2 . TYR   B 1 69 ? 13.264  -20.258 -37.734 1.00 37.03  ? 68  TYR   B CD2 1 
ATOM   1281 C CE1 . TYR   B 1 69 ? 12.174  -22.516 -36.567 1.00 41.09  ? 68  TYR   B CE1 1 
ATOM   1282 C CE2 . TYR   B 1 69 ? 13.810  -21.503 -38.009 1.00 37.82  ? 68  TYR   B CE2 1 
ATOM   1283 C CZ  . TYR   B 1 69 ? 13.252  -22.632 -37.428 1.00 41.66  ? 68  TYR   B CZ  1 
ATOM   1284 O OH  . TYR   B 1 69 ? 13.788  -23.852 -37.683 1.00 36.86  ? 68  TYR   B OH  1 
ATOM   1285 N N   . GLY   B 1 70 ? 9.001   -16.484 -37.176 1.00 37.56  ? 69  GLY   B N   1 
ATOM   1286 C CA  . GLY   B 1 70 ? 8.710   -15.113 -36.786 1.00 45.94  ? 69  GLY   B CA  1 
ATOM   1287 C C   . GLY   B 1 70 ? 7.274   -14.892 -36.311 1.00 49.56  ? 69  GLY   B C   1 
ATOM   1288 O O   . GLY   B 1 70 ? 6.673   -13.871 -36.656 1.00 49.15  ? 69  GLY   B O   1 
ATOM   1289 N N   . LYS   B 1 71 ? 6.745   -15.831 -35.510 1.00 50.15  ? 70  LYS   B N   1 
ATOM   1290 C CA  . LYS   B 1 71 ? 5.400   -15.720 -34.975 1.00 49.99  ? 70  LYS   B CA  1 
ATOM   1291 C C   . LYS   B 1 71 ? 5.483   -15.258 -33.531 1.00 51.97  ? 70  LYS   B C   1 
ATOM   1292 O O   . LYS   B 1 71 ? 6.327   -15.753 -32.778 1.00 47.49  ? 70  LYS   B O   1 
ATOM   1293 C CB  . LYS   B 1 71 ? 4.688   -17.069 -34.816 1.00 57.97  ? 70  LYS   B CB  1 
ATOM   1294 C CG  . LYS   B 1 71 ? 3.740   -17.507 -35.919 1.00 72.87  ? 70  LYS   B CG  1 
ATOM   1295 C CD  . LYS   B 1 71 ? 4.416   -17.981 -37.198 1.00 73.39  ? 70  LYS   B CD  1 
ATOM   1296 C CE  . LYS   B 1 71 ? 3.436   -18.675 -38.086 1.00 81.78  ? 70  LYS   B CE  1 
ATOM   1297 N NZ  . LYS   B 1 71 ? 4.022   -18.968 -39.397 1.00 88.51  ? 70  LYS   B NZ  1 
ATOM   1298 N N   . PRO   B 1 72 ? 4.589   -14.343 -33.086 1.00 51.35  ? 71  PRO   B N   1 
ATOM   1299 C CA  . PRO   B 1 72 ? 4.514   -14.005 -31.663 1.00 48.27  ? 71  PRO   B CA  1 
ATOM   1300 C C   . PRO   B 1 72 ? 4.299   -15.238 -30.787 1.00 48.44  ? 71  PRO   B C   1 
ATOM   1301 O O   . PRO   B 1 72 ? 3.699   -16.212 -31.238 1.00 40.30  ? 71  PRO   B O   1 
ATOM   1302 C CB  . PRO   B 1 72 ? 3.379   -12.970 -31.594 1.00 47.86  ? 71  PRO   B CB  1 
ATOM   1303 C CG  . PRO   B 1 72 ? 3.407   -12.354 -32.974 1.00 53.50  ? 71  PRO   B CG  1 
ATOM   1304 C CD  . PRO   B 1 72 ? 3.679   -13.533 -33.913 1.00 48.86  ? 71  PRO   B CD  1 
ATOM   1305 N N   . ASN   B 1 73 ? 4.852   -15.188 -29.558 1.00 49.38  ? 72  ASN   B N   1 
ATOM   1306 C CA  . ASN   B 1 73 ? 4.624   -16.186 -28.516 1.00 41.35  ? 72  ASN   B CA  1 
ATOM   1307 C C   . ASN   B 1 73 ? 4.555   -15.456 -27.162 1.00 48.09  ? 72  ASN   B C   1 
ATOM   1308 O O   . ASN   B 1 73 ? 4.541   -14.221 -27.109 1.00 45.26  ? 72  ASN   B O   1 
ATOM   1309 C CB  . ASN   B 1 73 ? 5.659   -17.314 -28.570 1.00 41.08  ? 72  ASN   B CB  1 
ATOM   1310 C CG  . ASN   B 1 73 ? 7.067   -16.812 -28.334 1.00 42.99  ? 72  ASN   B CG  1 
ATOM   1311 O OD1 . ASN   B 1 73 ? 7.300   -16.046 -27.385 1.00 36.87  ? 72  ASN   B OD1 1 
ATOM   1312 N ND2 . ASN   B 1 73 ? 8.007   -17.167 -29.211 1.00 36.70  ? 72  ASN   B ND2 1 
ATOM   1313 N N   . LYS   B 1 74 ? 4.581   -16.220 -26.065 1.00 42.72  ? 73  LYS   B N   1 
ATOM   1314 C CA  . LYS   B 1 74 ? 4.452   -15.673 -24.717 1.00 47.05  ? 73  LYS   B CA  1 
ATOM   1315 C C   . LYS   B 1 74 ? 5.805   -15.459 -24.015 1.00 47.62  ? 73  LYS   B C   1 
ATOM   1316 O O   . LYS   B 1 74 ? 5.824   -15.201 -22.810 1.00 47.54  ? 73  LYS   B O   1 
ATOM   1317 C CB  . LYS   B 1 74 ? 3.681   -16.682 -23.845 1.00 46.53  ? 73  LYS   B CB  1 
ATOM   1318 C CG  . LYS   B 1 74 ? 2.242   -16.998 -24.230 1.00 45.62  ? 73  LYS   B CG  1 
ATOM   1319 N N   . ARG   B 1 75 ? 6.942   -15.599 -24.713 1.00 35.12  ? 74  ARG   B N   1 
ATOM   1320 C CA  . ARG   B 1 75 ? 8.217   -15.479 -24.018 1.00 34.23  ? 74  ARG   B CA  1 
ATOM   1321 C C   . ARG   B 1 75 ? 8.543   -14.000 -23.849 1.00 34.46  ? 74  ARG   B C   1 
ATOM   1322 O O   . ARG   B 1 75 ? 8.297   -13.197 -24.757 1.00 38.89  ? 74  ARG   B O   1 
ATOM   1323 C CB  . ARG   B 1 75 ? 9.378   -16.250 -24.651 1.00 35.84  ? 74  ARG   B CB  1 
ATOM   1324 C CG  . ARG   B 1 75 ? 9.205   -17.752 -24.842 1.00 33.23  ? 74  ARG   B CG  1 
ATOM   1325 C CD  . ARG   B 1 75 ? 9.100   -18.576 -23.544 1.00 33.41  ? 74  ARG   B CD  1 
ATOM   1326 N NE  . ARG   B 1 75 ? 9.321   -19.987 -23.872 1.00 32.50  ? 74  ARG   B NE  1 
ATOM   1327 C CZ  . ARG   B 1 75 ? 10.450  -20.614 -23.616 1.00 35.11  ? 74  ARG   B CZ  1 
ATOM   1328 N NH1 . ARG   B 1 75 ? 11.492  -19.949 -23.122 1.00 35.24  ? 74  ARG   B NH1 1 
ATOM   1329 N NH2 . ARG   B 1 75 ? 10.565  -21.880 -23.957 1.00 35.83  ? 74  ARG   B NH2 1 
ATOM   1330 N N   . LYS   B 1 76 ? 9.054   -13.651 -22.661 1.00 34.70  ? 75  LYS   B N   1 
ATOM   1331 C CA  . LYS   B 1 76 ? 9.403   -12.283 -22.318 1.00 32.86  ? 75  LYS   B CA  1 
ATOM   1332 C C   . LYS   B 1 76 ? 10.478  -11.742 -23.267 1.00 30.67  ? 75  LYS   B C   1 
ATOM   1333 O O   . LYS   B 1 76 ? 11.584  -12.310 -23.361 1.00 30.31  ? 75  LYS   B O   1 
ATOM   1334 C CB  . LYS   B 1 76 ? 9.967   -12.191 -20.893 1.00 33.07  ? 75  LYS   B CB  1 
ATOM   1335 C CG  . LYS   B 1 76 ? 10.318  -10.752 -20.507 1.00 35.03  ? 75  LYS   B CG  1 
ATOM   1336 C CD  . LYS   B 1 76 ? 10.766  -10.616 -19.059 1.00 36.45  ? 75  LYS   B CD  1 
ATOM   1337 C CE  . LYS   B 1 76 ? 10.969  -9.193  -18.638 1.00 41.15  ? 75  LYS   B CE  1 
ATOM   1338 N NZ  . LYS   B 1 76 ? 11.528  -9.199  -17.273 1.00 48.45  ? 75  LYS   B NZ  1 
ATOM   1339 N N   . GLY   B 1 77 ? 10.124  -10.634 -23.930 1.00 30.36  ? 76  GLY   B N   1 
ATOM   1340 C CA  . GLY   B 1 77 ? 11.038  -9.924  -24.820 1.00 32.53  ? 76  GLY   B CA  1 
ATOM   1341 C C   . GLY   B 1 77 ? 10.895  -10.364 -26.284 1.00 31.99  ? 76  GLY   B C   1 
ATOM   1342 O O   . GLY   B 1 77 ? 11.457  -9.727  -27.174 1.00 35.53  ? 76  GLY   B O   1 
ATOM   1343 N N   . PHE   B 1 78 ? 10.147  -11.452 -26.553 1.00 30.29  ? 77  PHE   B N   1 
ATOM   1344 C CA  . PHE   B 1 78 ? 10.053  -12.002 -27.908 1.00 29.76  ? 77  PHE   B CA  1 
ATOM   1345 C C   . PHE   B 1 78 ? 9.337   -11.054 -28.862 1.00 33.51  ? 77  PHE   B C   1 
ATOM   1346 O O   . PHE   B 1 78 ? 9.841   -10.754 -29.946 1.00 29.62  ? 77  PHE   B O   1 
ATOM   1347 C CB  . PHE   B 1 78 ? 9.333   -13.353 -27.951 1.00 31.21  ? 77  PHE   B CB  1 
ATOM   1348 C CG  . PHE   B 1 78 ? 9.565   -14.082 -29.264 1.00 30.94  ? 77  PHE   B CG  1 
ATOM   1349 C CD1 . PHE   B 1 78 ? 10.697  -14.885 -29.432 1.00 29.50  ? 77  PHE   B CD1 1 
ATOM   1350 C CD2 . PHE   B 1 78 ? 8.632   -13.993 -30.299 1.00 32.30  ? 77  PHE   B CD2 1 
ATOM   1351 C CE1 . PHE   B 1 78 ? 10.912  -15.558 -30.634 1.00 28.99  ? 77  PHE   B CE1 1 
ATOM   1352 C CE2 . PHE   B 1 78 ? 8.849   -14.671 -31.498 1.00 34.84  ? 77  PHE   B CE2 1 
ATOM   1353 C CZ  . PHE   B 1 78 ? 10.000  -15.431 -31.655 1.00 31.67  ? 77  PHE   B CZ  1 
ATOM   1354 N N   . ASN   B 1 79 ? 8.140   -10.593 -28.502 1.00 32.41  ? 78  ASN   B N   1 
ATOM   1355 C CA  . ASN   B 1 79 ? 7.419   -9.738  -29.436 1.00 33.87  ? 78  ASN   B CA  1 
ATOM   1356 C C   . ASN   B 1 79 ? 8.133   -8.386  -29.623 1.00 36.48  ? 78  ASN   B C   1 
ATOM   1357 O O   . ASN   B 1 79 ? 8.095   -7.807  -30.709 1.00 36.83  ? 78  ASN   B O   1 
ATOM   1358 C CB  . ASN   B 1 79 ? 5.936   -9.615  -29.085 1.00 38.35  ? 78  ASN   B CB  1 
ATOM   1359 C CG  . ASN   B 1 79 ? 5.215   -10.946 -29.070 1.00 47.55  ? 78  ASN   B CG  1 
ATOM   1360 O OD1 . ASN   B 1 79 ? 5.682   -11.930 -29.659 1.00 45.53  ? 78  ASN   B OD1 1 
ATOM   1361 N ND2 . ASN   B 1 79 ? 4.090   -11.013 -28.373 1.00 43.31  ? 78  ASN   B ND2 1 
ATOM   1362 N N   . GLU   B 1 80 ? 8.791   -7.878  -28.579 1.00 35.27  ? 79  GLU   B N   1 
ATOM   1363 C CA  . GLU   B 1 80 ? 9.596   -6.673  -28.738 1.00 36.27  ? 79  GLU   B CA  1 
ATOM   1364 C C   . GLU   B 1 80 ? 10.730  -6.946  -29.731 1.00 37.59  ? 79  GLU   B C   1 
ATOM   1365 O O   . GLU   B 1 80 ? 11.050  -6.071  -30.541 1.00 35.20  ? 79  GLU   B O   1 
ATOM   1366 C CB  . GLU   B 1 80 ? 10.157  -6.124  -27.426 1.00 33.52  ? 79  GLU   B CB  1 
ATOM   1367 C CG  . GLU   B 1 80 ? 9.152   -5.255  -26.681 1.00 43.31  ? 79  GLU   B CG  1 
ATOM   1368 N N   . GLY   B 1 81 ? 11.314  -8.160  -29.671 1.00 30.82  ? 80  GLY   B N   1 
ATOM   1369 C CA  . GLY   B 1 81 ? 12.401  -8.570  -30.564 1.00 31.65  ? 80  GLY   B CA  1 
ATOM   1370 C C   . GLY   B 1 81 ? 11.932  -8.619  -32.012 1.00 31.39  ? 80  GLY   B C   1 
ATOM   1371 O O   . GLY   B 1 81 ? 12.642  -8.198  -32.937 1.00 31.55  ? 80  GLY   B O   1 
ATOM   1372 N N   . LEU   B 1 82 ? 10.711  -9.102  -32.207 1.00 29.08  ? 81  LEU   B N   1 
ATOM   1373 C CA  . LEU   B 1 82 ? 10.142  -9.118  -33.548 1.00 34.22  ? 81  LEU   B CA  1 
ATOM   1374 C C   . LEU   B 1 82 ? 10.014  -7.689  -34.067 1.00 34.38  ? 81  LEU   B C   1 
ATOM   1375 O O   . LEU   B 1 82 ? 10.346  -7.428  -35.217 1.00 33.50  ? 81  LEU   B O   1 
ATOM   1376 C CB  . LEU   B 1 82 ? 8.808   -9.861  -33.623 1.00 32.01  ? 81  LEU   B CB  1 
ATOM   1377 C CG  . LEU   B 1 82 ? 8.872   -11.356 -33.309 1.00 33.05  ? 81  LEU   B CG  1 
ATOM   1378 C CD1 . LEU   B 1 82 ? 7.478   -12.000 -33.310 1.00 30.38  ? 81  LEU   B CD1 1 
ATOM   1379 C CD2 . LEU   B 1 82 ? 9.825   -12.071 -34.269 1.00 28.08  ? 81  LEU   B CD2 1 
ATOM   1380 N N   . TRP   B 1 83 ? 9.536   -6.768  -33.219 1.00 31.25  ? 82  TRP   B N   1 
ATOM   1381 C CA  . TRP   B 1 83 ? 9.400   -5.366  -33.586 1.00 32.08  ? 82  TRP   B CA  1 
ATOM   1382 C C   . TRP   B 1 83 ? 10.745  -4.784  -34.019 1.00 32.79  ? 82  TRP   B C   1 
ATOM   1383 O O   . TRP   B 1 83 ? 10.821  -4.145  -35.072 1.00 31.95  ? 82  TRP   B O   1 
ATOM   1384 C CB  . TRP   B 1 83 ? 8.767   -4.505  -32.480 1.00 32.89  ? 82  TRP   B CB  1 
ATOM   1385 C CG  . TRP   B 1 83 ? 8.507   -3.102  -32.972 1.00 34.57  ? 82  TRP   B CG  1 
ATOM   1386 C CD1 . TRP   B 1 83 ? 7.377   -2.646  -33.584 1.00 42.23  ? 82  TRP   B CD1 1 
ATOM   1387 C CD2 . TRP   B 1 83 ? 9.438   -1.997  -32.983 1.00 36.24  ? 82  TRP   B CD2 1 
ATOM   1388 N NE1 . TRP   B 1 83 ? 7.530   -1.334  -33.948 1.00 43.74  ? 82  TRP   B NE1 1 
ATOM   1389 C CE2 . TRP   B 1 83 ? 8.784   -0.910  -33.599 1.00 40.05  ? 82  TRP   B CE2 1 
ATOM   1390 C CE3 . TRP   B 1 83 ? 10.754  -1.817  -32.531 1.00 36.44  ? 82  TRP   B CE3 1 
ATOM   1391 C CZ2 . TRP   B 1 83 ? 9.395   0.340   -33.755 1.00 40.76  ? 82  TRP   B CZ2 1 
ATOM   1392 C CZ3 . TRP   B 1 83 ? 11.361  -0.588  -32.700 1.00 40.01  ? 82  TRP   B CZ3 1 
ATOM   1393 C CH2 . TRP   B 1 83 ? 10.695  0.472   -33.314 1.00 38.18  ? 82  TRP   B CH2 1 
ATOM   1394 N N   . GLU   B 1 84 ? 11.800  -5.078  -33.251 1.00 28.87  ? 83  GLU   B N   1 
ATOM   1395 C CA  . GLU   B 1 84 ? 13.119  -4.500  -33.468 1.00 32.98  ? 83  GLU   B CA  1 
ATOM   1396 C C   . GLU   B 1 84 ? 13.784  -5.015  -34.747 1.00 34.93  ? 83  GLU   B C   1 
ATOM   1397 O O   . GLU   B 1 84 ? 14.371  -4.208  -35.464 1.00 33.51  ? 83  GLU   B O   1 
ATOM   1398 C CB  . GLU   B 1 84 ? 14.057  -4.741  -32.294 1.00 32.06  ? 83  GLU   B CB  1 
ATOM   1399 C CG  . GLU   B 1 84 ? 13.578  -4.032  -31.029 1.00 35.07  ? 83  GLU   B CG  1 
ATOM   1400 C CD  . GLU   B 1 84 ? 14.446  -4.359  -29.844 1.00 36.46  ? 83  GLU   B CD  1 
ATOM   1401 O OE1 . GLU   B 1 84 ? 15.396  -5.183  -29.963 1.00 34.79  ? 83  GLU   B OE1 1 
ATOM   1402 O OE2 . GLU   B 1 84 ? 14.183  -3.750  -28.774 1.00 39.39  ? 83  GLU   B OE2 1 
ATOM   1403 N N   . ILE   B 1 85 ? 13.721  -6.332  -35.016 1.00 33.64  ? 84  ILE   B N   1 
ATOM   1404 C CA  . ILE   B 1 85 ? 14.418  -6.911  -36.169 1.00 33.64  ? 84  ILE   B CA  1 
ATOM   1405 C C   . ILE   B 1 85 ? 13.802  -6.349  -37.450 1.00 31.40  ? 84  ILE   B C   1 
ATOM   1406 O O   . ILE   B 1 85 ? 14.472  -6.173  -38.476 1.00 31.44  ? 84  ILE   B O   1 
ATOM   1407 C CB  . ILE   B 1 85 ? 14.389  -8.451  -36.157 1.00 29.93  ? 84  ILE   B CB  1 
ATOM   1408 C CG1 . ILE   B 1 85 ? 15.374  -9.051  -37.178 1.00 32.00  ? 84  ILE   B CG1 1 
ATOM   1409 C CG2 . ILE   B 1 85 ? 12.974  -8.978  -36.419 1.00 30.07  ? 84  ILE   B CG2 1 
ATOM   1410 C CD1 . ILE   B 1 85 ? 15.926  -10.431 -36.801 1.00 30.88  ? 84  ILE   B CD1 1 
ATOM   1411 N N   . GLN   B 1 86 ? 12.512  -6.057  -37.356 1.00 31.90  ? 85  GLN   B N   1 
ATOM   1412 C CA  . GLN   B 1 86 ? 11.713  -5.513  -38.441 1.00 33.73  ? 85  GLN   B CA  1 
ATOM   1413 C C   . GLN   B 1 86 ? 11.937  -4.008  -38.626 1.00 38.39  ? 85  GLN   B C   1 
ATOM   1414 O O   . GLN   B 1 86 ? 11.930  -3.523  -39.753 1.00 36.58  ? 85  GLN   B O   1 
ATOM   1415 C CB  . GLN   B 1 86 ? 10.263  -5.816  -38.096 1.00 38.66  ? 85  GLN   B CB  1 
ATOM   1416 N N   . ASN   B 1 87 ? 12.117  -3.247  -37.543 1.00 33.90  ? 86  ASN   B N   1 
ATOM   1417 C CA  . ASN   B 1 87 ? 11.906  -1.810  -37.707 1.00 34.15  ? 86  ASN   B CA  1 
ATOM   1418 C C   . ASN   B 1 87 ? 13.196  -1.037  -37.511 1.00 35.30  ? 86  ASN   B C   1 
ATOM   1419 O O   . ASN   B 1 87 ? 13.325  0.080   -38.013 1.00 39.44  ? 86  ASN   B O   1 
ATOM   1420 C CB  . ASN   B 1 87 ? 10.861  -1.252  -36.739 1.00 37.08  ? 86  ASN   B CB  1 
ATOM   1421 C CG  . ASN   B 1 87 ? 9.510   -1.844  -37.037 1.00 43.87  ? 86  ASN   B CG  1 
ATOM   1422 O OD1 . ASN   B 1 87 ? 8.878   -1.466  -38.024 1.00 50.70  ? 86  ASN   B OD1 1 
ATOM   1423 N ND2 . ASN   B 1 87 ? 9.102   -2.845  -36.274 1.00 46.12  ? 86  ASN   B ND2 1 
ATOM   1424 N N   . ASN   B 1 88 ? 14.133  -1.603  -36.753 1.00 32.84  ? 87  ASN   B N   1 
ATOM   1425 C CA  . ASN   B 1 88 ? 15.398  -0.918  -36.540 1.00 32.53  ? 87  ASN   B CA  1 
ATOM   1426 C C   . ASN   B 1 88 ? 16.472  -1.921  -36.135 1.00 30.57  ? 87  ASN   B C   1 
ATOM   1427 O O   . ASN   B 1 88 ? 17.083  -1.811  -35.060 1.00 28.60  ? 87  ASN   B O   1 
ATOM   1428 C CB  . ASN   B 1 88 ? 15.246  0.255   -35.578 1.00 37.56  ? 87  ASN   B CB  1 
ATOM   1429 C CG  . ASN   B 1 88 ? 16.352  1.274   -35.743 1.00 36.31  ? 87  ASN   B CG  1 
ATOM   1430 O OD1 . ASN   B 1 88 ? 17.422  0.994   -36.297 1.00 34.67  ? 87  ASN   B OD1 1 
ATOM   1431 N ND2 . ASN   B 1 88 ? 16.143  2.455   -35.192 1.00 39.05  ? 87  ASN   B ND2 1 
ATOM   1432 N N   . PRO   B 1 89 ? 16.744  -2.921  -37.021 1.00 30.43  ? 88  PRO   B N   1 
ATOM   1433 C CA  . PRO   B 1 89 ? 17.677  -4.000  -36.706 1.00 26.69  ? 88  PRO   B CA  1 
ATOM   1434 C C   . PRO   B 1 89 ? 19.089  -3.537  -36.418 1.00 26.36  ? 88  PRO   B C   1 
ATOM   1435 O O   . PRO   B 1 89 ? 19.862  -4.291  -35.843 1.00 27.50  ? 88  PRO   B O   1 
ATOM   1436 C CB  . PRO   B 1 89 ? 17.665  -4.919  -37.974 1.00 25.98  ? 88  PRO   B CB  1 
ATOM   1437 C CG  . PRO   B 1 89 ? 17.080  -4.018  -39.088 1.00 30.10  ? 88  PRO   B CG  1 
ATOM   1438 C CD  . PRO   B 1 89 ? 16.114  -3.085  -38.344 1.00 28.51  ? 88  PRO   B CD  1 
ATOM   1439 N N   . HIS   B 1 90 ? 19.463  -2.335  -36.911 1.00 27.98  ? 89  HIS   B N   1 
ATOM   1440 C CA  . HIS   B 1 90 ? 20.859  -1.936  -36.817 1.00 31.00  ? 89  HIS   B CA  1 
ATOM   1441 C C   . HIS   B 1 90 ? 21.132  -0.868  -35.746 1.00 34.16  ? 89  HIS   B C   1 
ATOM   1442 O O   . HIS   B 1 90 ? 22.283  -0.390  -35.637 1.00 31.48  ? 89  HIS   B O   1 
ATOM   1443 C CB  . HIS   B 1 90 ? 21.419  -1.551  -38.191 1.00 29.75  ? 89  HIS   B CB  1 
ATOM   1444 C CG  . HIS   B 1 90 ? 21.259  -2.648  -39.206 1.00 30.46  ? 89  HIS   B CG  1 
ATOM   1445 N ND1 . HIS   B 1 90 ? 21.852  -3.889  -39.108 1.00 29.74  ? 89  HIS   B ND1 1 
ATOM   1446 C CD2 . HIS   B 1 90 ? 20.543  -2.660  -40.341 1.00 28.73  ? 89  HIS   B CD2 1 
ATOM   1447 C CE1 . HIS   B 1 90 ? 21.506  -4.609  -40.172 1.00 26.64  ? 89  HIS   B CE1 1 
ATOM   1448 N NE2 . HIS   B 1 90 ? 20.705  -3.878  -40.920 1.00 29.58  ? 89  HIS   B NE2 1 
ATOM   1449 N N   . ALA   B 1 91 ? 20.113  -0.587  -34.914 1.00 31.58  ? 90  ALA   B N   1 
ATOM   1450 C CA  . ALA   B 1 91 ? 20.246  0.433   -33.883 1.00 29.77  ? 90  ALA   B CA  1 
ATOM   1451 C C   . ALA   B 1 91 ? 21.221  0.021   -32.789 1.00 38.32  ? 90  ALA   B C   1 
ATOM   1452 O O   . ALA   B 1 91 ? 21.528  -1.150  -32.580 1.00 33.79  ? 90  ALA   B O   1 
ATOM   1453 C CB  . ALA   B 1 91 ? 18.891  0.814   -33.300 1.00 28.61  ? 90  ALA   B CB  1 
ATOM   1454 N N   . SER   B 1 92 ? 21.699  1.040   -32.073 1.00 38.41  ? 91  SER   B N   1 
ATOM   1455 C CA  . SER   B 1 92 ? 22.397  0.841   -30.823 1.00 42.27  ? 91  SER   B CA  1 
ATOM   1456 C C   . SER   B 1 92 ? 21.335  0.603   -29.753 1.00 44.80  ? 91  SER   B C   1 
ATOM   1457 O O   . SER   B 1 92 ? 20.425  1.424   -29.608 1.00 42.77  ? 91  SER   B O   1 
ATOM   1458 C CB  . SER   B 1 92 ? 23.215  2.075   -30.504 1.00 43.28  ? 91  SER   B CB  1 
ATOM   1459 O OG  . SER   B 1 92 ? 23.533  2.067   -29.128 1.00 45.59  ? 91  SER   B OG  1 
ATOM   1460 N N   . TYR   B 1 93 ? 21.449  -0.544  -29.073 1.00 43.94  ? 92  TYR   B N   1 
ATOM   1461 C CA  . TYR   B 1 93 ? 20.581  -0.985  -27.989 1.00 47.10  ? 92  TYR   B CA  1 
ATOM   1462 C C   . TYR   B 1 93 ? 21.345  -0.814  -26.677 1.00 55.77  ? 92  TYR   B C   1 
ATOM   1463 O O   . TYR   B 1 93 ? 20.965  -1.366  -25.645 1.00 53.53  ? 92  TYR   B O   1 
ATOM   1464 C CB  . TYR   B 1 93 ? 19.984  -2.382  -28.241 1.00 39.53  ? 92  TYR   B CB  1 
ATOM   1465 C CG  . TYR   B 1 93 ? 18.956  -2.310  -29.358 1.00 35.23  ? 92  TYR   B CG  1 
ATOM   1466 C CD1 . TYR   B 1 93 ? 17.676  -1.829  -29.107 1.00 34.38  ? 92  TYR   B CD1 1 
ATOM   1467 C CD2 . TYR   B 1 93 ? 19.284  -2.639  -30.681 1.00 33.09  ? 92  TYR   B CD2 1 
ATOM   1468 C CE1 . TYR   B 1 93 ? 16.755  -1.659  -30.122 1.00 35.83  ? 92  TYR   B CE1 1 
ATOM   1469 C CE2 . TYR   B 1 93 ? 18.357  -2.475  -31.704 1.00 32.14  ? 92  TYR   B CE2 1 
ATOM   1470 C CZ  . TYR   B 1 93 ? 17.087  -2.006  -31.421 1.00 33.33  ? 92  TYR   B CZ  1 
ATOM   1471 O OH  . TYR   B 1 93 ? 16.138  -1.873  -32.408 1.00 33.99  ? 92  TYR   B OH  1 
ATOM   1472 N N   . SER   B 1 94 ? 22.418  -0.011  -26.752 1.00 68.98  ? 93  SER   B N   1 
ATOM   1473 C CA  . SER   B 1 94 ? 23.253  0.371   -25.625 1.00 75.40  ? 93  SER   B CA  1 
ATOM   1474 C C   . SER   B 1 94 ? 22.451  1.207   -24.616 1.00 86.18  ? 93  SER   B C   1 
ATOM   1475 O O   . SER   B 1 94 ? 21.527  1.926   -25.060 1.00 85.67  ? 93  SER   B O   1 
ATOM   1476 C CB  . SER   B 1 94 ? 24.471  1.121   -26.096 1.00 72.69  ? 93  SER   B CB  1 
ATOM   1477 O OG  . SER   B 1 94 ? 25.460  0.201   -26.530 1.00 71.59  ? 93  SER   B OG  1 
ATOM   1478 O OXT . SER   B 1 94 ? 22.789  1.115   -23.415 1.00 102.93 ? 93  SER   B OXT 1 
ATOM   1479 N N   . HIS   C 1 4  ? 32.787  -24.378 27.285  1.00 75.87  ? 3   HIS   C N   1 
ATOM   1480 C CA  . HIS   C 1 4  ? 31.863  -23.214 27.385  1.00 89.39  ? 3   HIS   C CA  1 
ATOM   1481 C C   . HIS   C 1 4  ? 31.237  -23.188 28.785  1.00 96.45  ? 3   HIS   C C   1 
ATOM   1482 O O   . HIS   C 1 4  ? 31.948  -23.305 29.783  1.00 95.46  ? 3   HIS   C O   1 
ATOM   1483 C CB  . HIS   C 1 4  ? 30.901  -23.193 26.185  1.00 95.56  ? 3   HIS   C CB  1 
ATOM   1484 C CG  . HIS   C 1 4  ? 30.201  -21.889 25.949  1.00 101.45 ? 3   HIS   C CG  1 
ATOM   1485 N ND1 . HIS   C 1 4  ? 30.705  -20.910 25.119  1.00 102.25 ? 3   HIS   C ND1 1 
ATOM   1486 C CD2 . HIS   C 1 4  ? 29.040  -21.404 26.424  1.00 102.61 ? 3   HIS   C CD2 1 
ATOM   1487 C CE1 . HIS   C 1 4  ? 29.878  -19.873 25.108  1.00 104.25 ? 3   HIS   C CE1 1 
ATOM   1488 N NE2 . HIS   C 1 4  ? 28.858  -20.152 25.892  1.00 104.41 ? 3   HIS   C NE2 1 
ATOM   1489 N N   . ALA   C 1 5  ? 29.901  -23.075 28.840  1.00 94.71  ? 4   ALA   C N   1 
ATOM   1490 C CA  . ALA   C 1 5  ? 29.153  -22.660 30.017  1.00 87.35  ? 4   ALA   C CA  1 
ATOM   1491 C C   . ALA   C 1 5  ? 27.658  -22.795 29.735  1.00 85.78  ? 4   ALA   C C   1 
ATOM   1492 O O   . ALA   C 1 5  ? 27.023  -21.846 29.272  1.00 83.29  ? 4   ALA   C O   1 
ATOM   1493 C CB  . ALA   C 1 5  ? 29.487  -21.212 30.308  1.00 83.51  ? 4   ALA   C CB  1 
ATOM   1494 N N   . PHE   C 1 6  ? 27.100  -23.978 30.007  1.00 74.49  ? 5   PHE   C N   1 
ATOM   1495 C CA  . PHE   C 1 6  ? 25.730  -24.235 29.601  1.00 67.17  ? 5   PHE   C CA  1 
ATOM   1496 C C   . PHE   C 1 6  ? 24.851  -24.313 30.844  1.00 71.07  ? 5   PHE   C C   1 
ATOM   1497 O O   . PHE   C 1 6  ? 25.055  -25.190 31.680  1.00 89.26  ? 5   PHE   C O   1 
ATOM   1498 C CB  . PHE   C 1 6  ? 25.603  -25.462 28.683  1.00 59.19  ? 5   PHE   C CB  1 
ATOM   1499 C CG  . PHE   C 1 6  ? 26.357  -25.364 27.363  1.00 51.28  ? 5   PHE   C CG  1 
ATOM   1500 C CD1 . PHE   C 1 6  ? 27.536  -26.071 27.146  1.00 53.84  ? 5   PHE   C CD1 1 
ATOM   1501 C CD2 . PHE   C 1 6  ? 25.901  -24.535 26.342  1.00 54.64  ? 5   PHE   C CD2 1 
ATOM   1502 C CE1 . PHE   C 1 6  ? 28.229  -25.961 25.939  1.00 54.09  ? 5   PHE   C CE1 1 
ATOM   1503 C CE2 . PHE   C 1 6  ? 26.587  -24.439 25.137  1.00 50.12  ? 5   PHE   C CE2 1 
ATOM   1504 C CZ  . PHE   C 1 6  ? 27.750  -25.141 24.934  1.00 45.60  ? 5   PHE   C CZ  1 
ATOM   1505 N N   . LYS   C 1 7  ? 23.884  -23.389 30.941  1.00 64.16  ? 6   LYS   C N   1 
ATOM   1506 C CA  . LYS   C 1 7  ? 22.901  -23.347 32.018  1.00 62.66  ? 6   LYS   C CA  1 
ATOM   1507 C C   . LYS   C 1 7  ? 21.547  -23.724 31.427  1.00 58.12  ? 6   LYS   C C   1 
ATOM   1508 O O   . LYS   C 1 7  ? 21.383  -23.685 30.208  1.00 61.38  ? 6   LYS   C O   1 
ATOM   1509 C CB  . LYS   C 1 7  ? 22.815  -21.958 32.675  1.00 63.28  ? 6   LYS   C CB  1 
ATOM   1510 N N   . PRO   C 1 8  ? 20.543  -24.122 32.241  1.00 60.75  ? 7   PRO   C N   1 
ATOM   1511 C CA  . PRO   C 1 8  ? 19.211  -24.428 31.711  1.00 59.30  ? 7   PRO   C CA  1 
ATOM   1512 C C   . PRO   C 1 8  ? 18.609  -23.292 30.883  1.00 69.92  ? 7   PRO   C C   1 
ATOM   1513 O O   . PRO   C 1 8  ? 18.783  -22.113 31.206  1.00 68.30  ? 7   PRO   C O   1 
ATOM   1514 C CB  . PRO   C 1 8  ? 18.403  -24.730 32.972  1.00 60.08  ? 7   PRO   C CB  1 
ATOM   1515 C CG  . PRO   C 1 8  ? 19.442  -25.273 33.913  1.00 61.65  ? 7   PRO   C CG  1 
ATOM   1516 C CD  . PRO   C 1 8  ? 20.652  -24.373 33.690  1.00 61.33  ? 7   PRO   C CD  1 
ATOM   1517 N N   . GLY   C 1 9  ? 17.923  -23.671 29.796  1.00 66.67  ? 8   GLY   C N   1 
ATOM   1518 C CA  . GLY   C 1 9  ? 17.225  -22.731 28.935  1.00 59.20  ? 8   GLY   C CA  1 
ATOM   1519 C C   . GLY   C 1 9  ? 18.076  -22.246 27.760  1.00 57.35  ? 8   GLY   C C   1 
ATOM   1520 O O   . GLY   C 1 9  ? 17.514  -21.800 26.763  1.00 66.05  ? 8   GLY   C O   1 
ATOM   1521 N N   . ASP   C 1 10 ? 19.414  -22.327 27.887  1.00 48.27  ? 9   ASP   C N   1 
ATOM   1522 C CA  . ASP   C 1 10 ? 20.355  -21.967 26.842  1.00 47.63  ? 9   ASP   C CA  1 
ATOM   1523 C C   . ASP   C 1 10 ? 20.032  -22.732 25.554  1.00 51.62  ? 9   ASP   C C   1 
ATOM   1524 O O   . ASP   C 1 10 ? 19.868  -23.954 25.577  1.00 47.69  ? 9   ASP   C O   1 
ATOM   1525 C CB  . ASP   C 1 10 ? 21.797  -22.251 27.247  1.00 50.06  ? 9   ASP   C CB  1 
ATOM   1526 C CG  . ASP   C 1 10 ? 22.459  -21.309 28.250  1.00 62.05  ? 9   ASP   C CG  1 
ATOM   1527 O OD1 . ASP   C 1 10 ? 21.818  -20.312 28.626  1.00 61.04  ? 9   ASP   C OD1 1 
ATOM   1528 O OD2 . ASP   C 1 10 ? 23.619  -21.585 28.658  1.00 58.35  ? 9   ASP   C OD2 1 
ATOM   1529 N N   . LEU   C 1 11 ? 19.988  -21.995 24.433  1.00 49.41  ? 10  LEU   C N   1 
ATOM   1530 C CA  . LEU   C 1 11 ? 19.716  -22.529 23.104  1.00 48.48  ? 10  LEU   C CA  1 
ATOM   1531 C C   . LEU   C 1 11 ? 21.017  -22.983 22.443  1.00 41.73  ? 10  LEU   C C   1 
ATOM   1532 O O   . LEU   C 1 11 ? 22.009  -22.248 22.422  1.00 41.98  ? 10  LEU   C O   1 
ATOM   1533 C CB  . LEU   C 1 11 ? 18.980  -21.491 22.249  1.00 44.47  ? 10  LEU   C CB  1 
ATOM   1534 C CG  . LEU   C 1 11 ? 17.731  -20.851 22.871  1.00 45.10  ? 10  LEU   C CG  1 
ATOM   1535 C CD1 . LEU   C 1 11 ? 17.079  -19.908 21.863  1.00 48.50  ? 10  LEU   C CD1 1 
ATOM   1536 C CD2 . LEU   C 1 11 ? 16.725  -21.909 23.317  1.00 48.30  ? 10  LEU   C CD2 1 
ATOM   1537 N N   . VAL   C 1 12 ? 20.991  -24.196 21.868  1.00 39.87  ? 11  VAL   C N   1 
ATOM   1538 C CA  . VAL   C 1 12 ? 22.171  -24.816 21.279  1.00 34.17  ? 11  VAL   C CA  1 
ATOM   1539 C C   . VAL   C 1 12 ? 21.785  -25.553 19.982  1.00 35.40  ? 11  VAL   C C   1 
ATOM   1540 O O   . VAL   C 1 12 ? 20.601  -25.681 19.667  1.00 35.47  ? 11  VAL   C O   1 
ATOM   1541 C CB  . VAL   C 1 12 ? 22.782  -25.814 22.291  1.00 36.34  ? 11  VAL   C CB  1 
ATOM   1542 C CG1 . VAL   C 1 12 ? 23.086  -25.144 23.637  1.00 37.52  ? 11  VAL   C CG1 1 
ATOM   1543 C CG2 . VAL   C 1 12 ? 21.860  -27.012 22.484  1.00 34.11  ? 11  VAL   C CG2 1 
ATOM   1544 N N   . PHE   C 1 13 ? 22.816  -25.980 19.234  1.00 34.11  ? 12  PHE   C N   1 
ATOM   1545 C CA  . PHE   C 1 13 ? 22.776  -27.139 18.348  1.00 33.61  ? 12  PHE   C CA  1 
ATOM   1546 C C   . PHE   C 1 13 ? 23.493  -28.304 19.034  1.00 31.48  ? 12  PHE   C C   1 
ATOM   1547 O O   . PHE   C 1 13 ? 24.593  -28.148 19.577  1.00 34.83  ? 12  PHE   C O   1 
ATOM   1548 C CB  . PHE   C 1 13 ? 23.465  -26.921 16.995  1.00 35.51  ? 12  PHE   C CB  1 
ATOM   1549 C CG  . PHE   C 1 13 ? 22.714  -25.941 16.121  1.00 37.68  ? 12  PHE   C CG  1 
ATOM   1550 C CD1 . PHE   C 1 13 ? 21.703  -26.377 15.269  1.00 34.16  ? 12  PHE   C CD1 1 
ATOM   1551 C CD2 . PHE   C 1 13 ? 23.003  -24.580 16.174  1.00 37.77  ? 12  PHE   C CD2 1 
ATOM   1552 C CE1 . PHE   C 1 13 ? 20.994  -25.472 14.497  1.00 36.33  ? 12  PHE   C CE1 1 
ATOM   1553 C CE2 . PHE   C 1 13 ? 22.286  -23.682 15.404  1.00 39.99  ? 12  PHE   C CE2 1 
ATOM   1554 C CZ  . PHE   C 1 13 ? 21.295  -24.135 14.556  1.00 38.33  ? 12  PHE   C CZ  1 
ATOM   1555 N N   . ALA   C 1 14 ? 22.836  -29.470 19.027  1.00 30.98  ? 13  ALA   C N   1 
ATOM   1556 C CA  . ALA   C 1 14 ? 23.316  -30.618 19.778  1.00 29.74  ? 13  ALA   C CA  1 
ATOM   1557 C C   . ALA   C 1 14 ? 23.598  -31.735 18.785  1.00 34.34  ? 13  ALA   C C   1 
ATOM   1558 O O   . ALA   C 1 14 ? 22.715  -32.058 17.978  1.00 27.96  ? 13  ALA   C O   1 
ATOM   1559 C CB  . ALA   C 1 14 ? 22.280  -31.038 20.792  1.00 31.15  ? 13  ALA   C CB  1 
ATOM   1560 N N   . LYS   C 1 15 ? 24.824  -32.291 18.853  1.00 32.95  ? 14  LYS   C N   1 
ATOM   1561 C CA  . LYS   C 1 15 ? 25.247  -33.317 17.909  1.00 32.69  ? 14  LYS   C CA  1 
ATOM   1562 C C   . LYS   C 1 15 ? 25.208  -34.700 18.552  1.00 35.00  ? 14  LYS   C C   1 
ATOM   1563 O O   . LYS   C 1 15 ? 25.906  -34.955 19.520  1.00 35.47  ? 14  LYS   C O   1 
ATOM   1564 C CB  . LYS   C 1 15 ? 26.648  -33.074 17.327  1.00 36.97  ? 14  LYS   C CB  1 
ATOM   1565 C CG  . LYS   C 1 15 ? 27.084  -34.160 16.309  1.00 34.07  ? 14  LYS   C CG  1 
ATOM   1566 C CD  . LYS   C 1 15 ? 26.274  -34.022 15.021  1.00 36.96  ? 14  LYS   C CD  1 
ATOM   1567 C CE  . LYS   C 1 15 ? 26.760  -34.871 13.844  1.00 34.49  ? 14  LYS   C CE  1 
ATOM   1568 N NZ  . LYS   C 1 15 ? 26.637  -36.300 14.149  1.00 36.34  ? 14  LYS   C NZ  1 
ATOM   1569 N N   . MET   C 1 16 ? 24.413  -35.602 17.965  1.00 32.68  ? 15  MET   C N   1 
ATOM   1570 C CA  . MET   C 1 16 ? 24.399  -37.013 18.327  1.00 31.30  ? 15  MET   C CA  1 
ATOM   1571 C C   . MET   C 1 16 ? 24.894  -37.821 17.128  1.00 36.62  ? 15  MET   C C   1 
ATOM   1572 O O   . MET   C 1 16 ? 24.701  -37.443 15.961  1.00 29.29  ? 15  MET   C O   1 
ATOM   1573 C CB  . MET   C 1 16 ? 22.965  -37.474 18.618  1.00 32.71  ? 15  MET   C CB  1 
ATOM   1574 C CG  . MET   C 1 16 ? 22.324  -36.826 19.836  1.00 39.98  ? 15  MET   C CG  1 
ATOM   1575 S SD  . MET   C 1 16 ? 20.764  -37.616 20.286  1.00 43.41  ? 15  MET   C SD  1 
ATOM   1576 C CE  . MET   C 1 16 ? 19.688  -37.112 18.935  1.00 44.27  ? 15  MET   C CE  1 
ATOM   1577 N N   . LYS   C 1 17 ? 25.519  -38.965 17.418  1.00 33.97  ? 16  LYS   C N   1 
ATOM   1578 C CA  . LYS   C 1 17 ? 25.970  -39.813 16.324  1.00 38.31  ? 16  LYS   C CA  1 
ATOM   1579 C C   . LYS   C 1 17 ? 24.742  -40.233 15.516  1.00 33.68  ? 16  LYS   C C   1 
ATOM   1580 O O   . LYS   C 1 17 ? 23.743  -40.683 16.079  1.00 35.36  ? 16  LYS   C O   1 
ATOM   1581 C CB  . LYS   C 1 17 ? 26.673  -41.058 16.887  1.00 36.56  ? 16  LYS   C CB  1 
ATOM   1582 C CG  . LYS   C 1 17 ? 27.329  -41.986 15.869  1.00 42.93  ? 16  LYS   C CG  1 
ATOM   1583 C CD  . LYS   C 1 17 ? 28.567  -41.324 15.285  1.00 50.19  ? 16  LYS   C CD  1 
ATOM   1584 C CE  . LYS   C 1 17 ? 29.437  -42.249 14.490  1.00 55.41  ? 16  LYS   C CE  1 
ATOM   1585 N NZ  . LYS   C 1 17 ? 30.603  -41.475 14.048  1.00 46.55  ? 16  LYS   C NZ  1 
ATOM   1586 N N   . GLY   C 1 18 ? 24.821  -40.082 14.196  1.00 35.64  ? 17  GLY   C N   1 
ATOM   1587 C CA  . GLY   C 1 18 ? 23.719  -40.595 13.396  1.00 35.23  ? 17  GLY   C CA  1 
ATOM   1588 C C   . GLY   C 1 18 ? 22.761  -39.482 12.965  1.00 36.40  ? 17  GLY   C C   1 
ATOM   1589 O O   . GLY   C 1 18 ? 21.746  -39.765 12.321  1.00 33.51  ? 17  GLY   C O   1 
ATOM   1590 N N   . TYR   C 1 19 ? 23.053  -38.237 13.386  1.00 34.15  ? 18  TYR   C N   1 
ATOM   1591 C CA  . TYR   C 1 19 ? 22.125  -37.122 13.195  1.00 36.28  ? 18  TYR   C CA  1 
ATOM   1592 C C   . TYR   C 1 19 ? 22.886  -35.835 12.928  1.00 32.15  ? 18  TYR   C C   1 
ATOM   1593 O O   . TYR   C 1 19 ? 23.977  -35.624 13.452  1.00 32.98  ? 18  TYR   C O   1 
ATOM   1594 C CB  . TYR   C 1 19 ? 21.271  -36.783 14.423  1.00 31.15  ? 18  TYR   C CB  1 
ATOM   1595 C CG  . TYR   C 1 19 ? 20.413  -37.966 14.826  1.00 31.55  ? 18  TYR   C CG  1 
ATOM   1596 C CD1 . TYR   C 1 19 ? 20.945  -39.007 15.589  1.00 33.10  ? 18  TYR   C CD1 1 
ATOM   1597 C CD2 . TYR   C 1 19 ? 19.079  -38.034 14.457  1.00 33.44  ? 18  TYR   C CD2 1 
ATOM   1598 C CE1 . TYR   C 1 19 ? 20.170  -40.092 15.960  1.00 34.79  ? 18  TYR   C CE1 1 
ATOM   1599 C CE2 . TYR   C 1 19 ? 18.302  -39.128 14.804  1.00 38.78  ? 18  TYR   C CE2 1 
ATOM   1600 C CZ  . TYR   C 1 19 ? 18.852  -40.153 15.556  1.00 40.97  ? 18  TYR   C CZ  1 
ATOM   1601 O OH  . TYR   C 1 19 ? 18.096  -41.235 15.906  1.00 50.53  ? 18  TYR   C OH  1 
ATOM   1602 N N   . PRO   C 1 20 ? 22.294  -34.938 12.111  1.00 31.84  ? 19  PRO   C N   1 
ATOM   1603 C CA  . PRO   C 1 20 ? 22.889  -33.621 11.863  1.00 31.92  ? 19  PRO   C CA  1 
ATOM   1604 C C   . PRO   C 1 20 ? 22.863  -32.828 13.175  1.00 32.70  ? 19  PRO   C C   1 
ATOM   1605 O O   . PRO   C 1 20 ? 22.100  -33.162 14.096  1.00 30.79  ? 19  PRO   C O   1 
ATOM   1606 C CB  . PRO   C 1 20 ? 21.931  -33.046 10.780  1.00 33.05  ? 19  PRO   C CB  1 
ATOM   1607 C CG  . PRO   C 1 20 ? 20.604  -33.684 11.096  1.00 31.35  ? 19  PRO   C CG  1 
ATOM   1608 C CD  . PRO   C 1 20 ? 20.959  -35.116 11.498  1.00 30.65  ? 19  PRO   C CD  1 
ATOM   1609 N N   . HIS   C 1 21 ? 23.711  -31.785 13.266  1.00 31.43  ? 20  HIS   C N   1 
ATOM   1610 C CA  . HIS   C 1 21 ? 23.644  -30.881 14.405  1.00 31.09  ? 20  HIS   C CA  1 
ATOM   1611 C C   . HIS   C 1 21 ? 22.224  -30.330 14.517  1.00 30.75  ? 20  HIS   C C   1 
ATOM   1612 O O   . HIS   C 1 21 ? 21.713  -29.764 13.541  1.00 31.41  ? 20  HIS   C O   1 
ATOM   1613 C CB  . HIS   C 1 21 ? 24.617  -29.715 14.226  1.00 33.57  ? 20  HIS   C CB  1 
ATOM   1614 C CG  . HIS   C 1 21 ? 26.053  -30.139 14.224  1.00 35.71  ? 20  HIS   C CG  1 
ATOM   1615 N ND1 . HIS   C 1 21 ? 26.673  -30.748 13.155  1.00 37.06  ? 20  HIS   C ND1 1 
ATOM   1616 C CD2 . HIS   C 1 21 ? 26.985  -30.059 15.202  1.00 42.70  ? 20  HIS   C CD2 1 
ATOM   1617 C CE1 . HIS   C 1 21 ? 27.932  -31.033 13.479  1.00 41.37  ? 20  HIS   C CE1 1 
ATOM   1618 N NE2 . HIS   C 1 21 ? 28.152  -30.587 14.706  1.00 39.60  ? 20  HIS   C NE2 1 
ATOM   1619 N N   . TRP   C 1 22 ? 21.602  -30.496 15.704  1.00 28.52  ? 21  TRP   C N   1 
ATOM   1620 C CA  . TRP   C 1 22 ? 20.146  -30.376 15.796  1.00 26.65  ? 21  TRP   C CA  1 
ATOM   1621 C C   . TRP   C 1 22 ? 19.776  -29.222 16.724  1.00 29.04  ? 21  TRP   C C   1 
ATOM   1622 O O   . TRP   C 1 22 ? 20.317  -29.122 17.826  1.00 30.54  ? 21  TRP   C O   1 
ATOM   1623 C CB  . TRP   C 1 22 ? 19.541  -31.683 16.338  1.00 30.24  ? 21  TRP   C CB  1 
ATOM   1624 C CG  . TRP   C 1 22 ? 18.090  -31.885 15.952  1.00 32.72  ? 21  TRP   C CG  1 
ATOM   1625 C CD1 . TRP   C 1 22 ? 16.963  -31.325 16.495  1.00 33.46  ? 21  TRP   C CD1 1 
ATOM   1626 C CD2 . TRP   C 1 22 ? 17.624  -32.800 14.929  1.00 30.51  ? 21  TRP   C CD2 1 
ATOM   1627 N NE1 . TRP   C 1 22 ? 15.834  -31.797 15.859  1.00 32.88  ? 21  TRP   C NE1 1 
ATOM   1628 C CE2 . TRP   C 1 22 ? 16.206  -32.706 14.901  1.00 32.23  ? 21  TRP   C CE2 1 
ATOM   1629 C CE3 . TRP   C 1 22 ? 18.267  -33.677 14.044  1.00 29.45  ? 21  TRP   C CE3 1 
ATOM   1630 C CZ2 . TRP   C 1 22 ? 15.432  -33.464 14.017  1.00 31.64  ? 21  TRP   C CZ2 1 
ATOM   1631 C CZ3 . TRP   C 1 22 ? 17.503  -34.410 13.154  1.00 31.97  ? 21  TRP   C CZ3 1 
ATOM   1632 C CH2 . TRP   C 1 22 ? 16.102  -34.330 13.171  1.00 28.42  ? 21  TRP   C CH2 1 
ATOM   1633 N N   . PRO   C 1 23 ? 18.802  -28.349 16.371  1.00 35.93  ? 22  PRO   C N   1 
ATOM   1634 C CA  . PRO   C 1 23 ? 18.402  -27.261 17.268  1.00 32.84  ? 22  PRO   C CA  1 
ATOM   1635 C C   . PRO   C 1 23 ? 17.803  -27.822 18.551  1.00 30.98  ? 22  PRO   C C   1 
ATOM   1636 O O   . PRO   C 1 23 ? 16.990  -28.735 18.516  1.00 29.76  ? 22  PRO   C O   1 
ATOM   1637 C CB  . PRO   C 1 23 ? 17.357  -26.483 16.425  1.00 33.79  ? 22  PRO   C CB  1 
ATOM   1638 C CG  . PRO   C 1 23 ? 16.767  -27.541 15.503  1.00 32.36  ? 22  PRO   C CG  1 
ATOM   1639 C CD  . PRO   C 1 23 ? 18.012  -28.369 15.127  1.00 32.79  ? 22  PRO   C CD  1 
ATOM   1640 N N   . ALA   C 1 24 ? 18.237  -27.277 19.693  1.00 31.83  ? 23  ALA   C N   1 
ATOM   1641 C CA  . ALA   C 1 24 ? 17.897  -27.860 20.980  1.00 31.95  ? 23  ALA   C CA  1 
ATOM   1642 C C   . ALA   C 1 24 ? 18.050  -26.812 22.086  1.00 35.10  ? 23  ALA   C C   1 
ATOM   1643 O O   . ALA   C 1 24 ? 18.577  -25.716 21.853  1.00 35.61  ? 23  ALA   C O   1 
ATOM   1644 C CB  . ALA   C 1 24 ? 18.843  -29.049 21.228  1.00 30.96  ? 23  ALA   C CB  1 
ATOM   1645 N N   . ARG   C 1 25 ? 17.631  -27.176 23.306  1.00 37.80  ? 24  ARG   C N   1 
ATOM   1646 C CA  . ARG   C 1 25 ? 17.983  -26.368 24.463  1.00 35.68  ? 24  ARG   C CA  1 
ATOM   1647 C C   . ARG   C 1 25 ? 18.410  -27.267 25.637  1.00 38.64  ? 24  ARG   C C   1 
ATOM   1648 O O   . ARG   C 1 25 ? 18.005  -28.430 25.715  1.00 37.69  ? 24  ARG   C O   1 
ATOM   1649 C CB  . ARG   C 1 25 ? 16.802  -25.477 24.854  1.00 38.26  ? 24  ARG   C CB  1 
ATOM   1650 C CG  . ARG   C 1 25 ? 15.629  -26.189 25.510  1.00 41.02  ? 24  ARG   C CG  1 
ATOM   1651 C CD  . ARG   C 1 25 ? 14.527  -25.281 26.088  1.00 47.92  ? 24  ARG   C CD  1 
ATOM   1652 N NE  . ARG   C 1 25 ? 13.332  -26.120 26.277  1.00 50.99  ? 24  ARG   C NE  1 
ATOM   1653 C CZ  . ARG   C 1 25 ? 12.088  -25.910 25.860  1.00 55.09  ? 24  ARG   C CZ  1 
ATOM   1654 N NH1 . ARG   C 1 25 ? 11.742  -24.775 25.275  1.00 55.43  ? 24  ARG   C NH1 1 
ATOM   1655 N NH2 . ARG   C 1 25 ? 11.171  -26.843 26.066  1.00 56.70  ? 24  ARG   C NH2 1 
ATOM   1656 N N   . ILE   C 1 26 ? 19.224  -26.699 26.535  1.00 40.62  ? 25  ILE   C N   1 
ATOM   1657 C CA  . ILE   C 1 26 ? 19.560  -27.277 27.832  1.00 44.66  ? 25  ILE   C CA  1 
ATOM   1658 C C   . ILE   C 1 26 ? 18.323  -27.209 28.722  1.00 51.18  ? 25  ILE   C C   1 
ATOM   1659 O O   . ILE   C 1 26 ? 17.783  -26.126 28.943  1.00 53.01  ? 25  ILE   C O   1 
ATOM   1660 C CB  . ILE   C 1 26 ? 20.710  -26.511 28.524  1.00 44.87  ? 25  ILE   C CB  1 
ATOM   1661 C CG1 . ILE   C 1 26 ? 21.877  -26.138 27.614  1.00 49.52  ? 25  ILE   C CG1 1 
ATOM   1662 C CG2 . ILE   C 1 26 ? 21.170  -27.232 29.797  1.00 46.27  ? 25  ILE   C CG2 1 
ATOM   1663 C CD1 . ILE   C 1 26 ? 22.697  -27.300 27.078  1.00 50.29  ? 25  ILE   C CD1 1 
ATOM   1664 N N   . ASP   C 1 27 ? 17.901  -28.365 29.241  1.00 53.44  ? 26  ASP   C N   1 
ATOM   1665 C CA  . ASP   C 1 27 ? 16.898  -28.432 30.292  1.00 61.98  ? 26  ASP   C CA  1 
ATOM   1666 C C   . ASP   C 1 27 ? 17.555  -28.397 31.673  1.00 67.80  ? 26  ASP   C C   1 
ATOM   1667 O O   . ASP   C 1 27 ? 18.741  -28.700 31.813  1.00 67.15  ? 26  ASP   C O   1 
ATOM   1668 C CB  . ASP   C 1 27 ? 16.114  -29.726 30.202  1.00 58.04  ? 26  ASP   C CB  1 
ATOM   1669 C CG  . ASP   C 1 27 ? 14.912  -29.703 29.275  1.00 66.45  ? 26  ASP   C CG  1 
ATOM   1670 O OD1 . ASP   C 1 27 ? 14.667  -28.637 28.651  1.00 66.78  ? 26  ASP   C OD1 1 
ATOM   1671 O OD2 . ASP   C 1 27 ? 14.220  -30.745 29.223  1.00 62.68  ? 26  ASP   C OD2 1 
ATOM   1672 N N   . ASP   C 1 28 ? 16.768  -28.021 32.695  1.00 81.17  ? 27  ASP   C N   1 
ATOM   1673 C CA  . ASP   C 1 28 ? 17.144  -28.286 34.076  1.00 79.01  ? 27  ASP   C CA  1 
ATOM   1674 C C   . ASP   C 1 28 ? 16.758  -29.727 34.386  1.00 77.11  ? 27  ASP   C C   1 
ATOM   1675 O O   . ASP   C 1 28 ? 15.857  -30.261 33.744  1.00 68.42  ? 27  ASP   C O   1 
ATOM   1676 C CB  . ASP   C 1 28 ? 16.572  -27.273 35.060  1.00 80.46  ? 27  ASP   C CB  1 
ATOM   1677 C CG  . ASP   C 1 28 ? 17.366  -27.128 36.355  1.00 85.43  ? 27  ASP   C CG  1 
ATOM   1678 O OD1 . ASP   C 1 28 ? 17.790  -25.987 36.674  1.00 67.92  ? 27  ASP   C OD1 1 
ATOM   1679 O OD2 . ASP   C 1 28 ? 17.589  -28.163 37.026  1.00 84.28  ? 27  ASP   C OD2 1 
ATOM   1680 N N   . ILE   C 1 29 ? 17.463  -30.343 35.347  1.00 79.33  ? 28  ILE   C N   1 
ATOM   1681 C CA  . ILE   C 1 29 ? 17.303  -31.756 35.656  1.00 76.76  ? 28  ILE   C CA  1 
ATOM   1682 C C   . ILE   C 1 29 ? 16.371  -31.905 36.872  1.00 74.37  ? 28  ILE   C C   1 
ATOM   1683 O O   . ILE   C 1 29 ? 16.682  -31.277 37.908  1.00 73.48  ? 28  ILE   C O   1 
ATOM   1684 C CB  . ILE   C 1 29 ? 18.673  -32.429 35.876  1.00 70.64  ? 28  ILE   C CB  1 
ATOM   1685 N N   . LYS   C 1 35 ? 19.810  -38.751 38.044  1.00 69.04  ? 34  LYS   C N   1 
ATOM   1686 C CA  . LYS   C 1 35 ? 20.660  -37.596 37.647  1.00 68.40  ? 34  LYS   C CA  1 
ATOM   1687 C C   . LYS   C 1 35 ? 21.352  -37.947 36.329  1.00 65.20  ? 34  LYS   C C   1 
ATOM   1688 O O   . LYS   C 1 35 ? 21.388  -39.116 35.938  1.00 56.14  ? 34  LYS   C O   1 
ATOM   1689 C CB  . LYS   C 1 35 ? 21.623  -37.226 38.785  1.00 64.22  ? 34  LYS   C CB  1 
ATOM   1690 N N   . PRO   C 1 36 ? 21.921  -36.960 35.598  1.00 65.21  ? 35  PRO   C N   1 
ATOM   1691 C CA  . PRO   C 1 36 ? 22.641  -37.257 34.357  1.00 62.31  ? 35  PRO   C CA  1 
ATOM   1692 C C   . PRO   C 1 36 ? 23.794  -38.232 34.614  1.00 63.23  ? 35  PRO   C C   1 
ATOM   1693 O O   . PRO   C 1 36 ? 24.270  -38.366 35.746  1.00 56.13  ? 35  PRO   C O   1 
ATOM   1694 C CB  . PRO   C 1 36 ? 23.161  -35.873 33.886  1.00 65.23  ? 35  PRO   C CB  1 
ATOM   1695 C CG  . PRO   C 1 36 ? 22.332  -34.853 34.640  1.00 63.12  ? 35  PRO   C CG  1 
ATOM   1696 C CD  . PRO   C 1 36 ? 21.924  -35.525 35.946  1.00 66.01  ? 35  PRO   C CD  1 
ATOM   1697 N N   . PRO   C 1 37 ? 24.282  -38.965 33.588  1.00 56.98  ? 36  PRO   C N   1 
ATOM   1698 C CA  . PRO   C 1 37 ? 25.610  -39.571 33.684  1.00 55.58  ? 36  PRO   C CA  1 
ATOM   1699 C C   . PRO   C 1 37 ? 26.606  -38.439 33.962  1.00 55.65  ? 36  PRO   C C   1 
ATOM   1700 O O   . PRO   C 1 37 ? 26.294  -37.261 33.743  1.00 45.18  ? 36  PRO   C O   1 
ATOM   1701 C CB  . PRO   C 1 37 ? 25.803  -40.276 32.324  1.00 54.04  ? 36  PRO   C CB  1 
ATOM   1702 C CG  . PRO   C 1 37 ? 24.382  -40.473 31.832  1.00 51.53  ? 36  PRO   C CG  1 
ATOM   1703 C CD  . PRO   C 1 37 ? 23.584  -39.283 32.329  1.00 55.61  ? 36  PRO   C CD  1 
ATOM   1704 N N   . PRO   C 1 38 ? 27.788  -38.746 34.553  1.00 51.80  ? 37  PRO   C N   1 
ATOM   1705 C CA  . PRO   C 1 38 ? 28.794  -37.723 34.853  1.00 48.86  ? 37  PRO   C CA  1 
ATOM   1706 C C   . PRO   C 1 38 ? 29.132  -36.835 33.660  1.00 46.46  ? 37  PRO   C C   1 
ATOM   1707 O O   . PRO   C 1 38 ? 29.340  -37.335 32.549  1.00 44.32  ? 37  PRO   C O   1 
ATOM   1708 C CB  . PRO   C 1 38 ? 30.000  -38.578 35.278  1.00 48.22  ? 37  PRO   C CB  1 
ATOM   1709 C CG  . PRO   C 1 38 ? 29.367  -39.795 35.907  1.00 50.68  ? 37  PRO   C CG  1 
ATOM   1710 C CD  . PRO   C 1 38 ? 28.189  -40.093 34.999  1.00 52.22  ? 37  PRO   C CD  1 
ATOM   1711 N N   . ASN   C 1 39 ? 29.175  -35.521 33.922  1.00 42.97  ? 38  ASN   C N   1 
ATOM   1712 C CA  . ASN   C 1 39 ? 29.561  -34.495 32.966  1.00 39.02  ? 38  ASN   C CA  1 
ATOM   1713 C C   . ASN   C 1 39 ? 28.595  -34.419 31.776  1.00 48.20  ? 38  ASN   C C   1 
ATOM   1714 O O   . ASN   C 1 39 ? 28.987  -33.909 30.718  1.00 53.49  ? 38  ASN   C O   1 
ATOM   1715 C CB  . ASN   C 1 39 ? 31.011  -34.645 32.512  1.00 46.18  ? 38  ASN   C CB  1 
ATOM   1716 C CG  . ASN   C 1 39 ? 31.603  -33.371 31.941  1.00 61.30  ? 38  ASN   C CG  1 
ATOM   1717 O OD1 . ASN   C 1 39 ? 31.331  -32.268 32.434  1.00 71.67  ? 38  ASN   C OD1 1 
ATOM   1718 N ND2 . ASN   C 1 39 ? 32.416  -33.488 30.900  1.00 59.91  ? 38  ASN   C ND2 1 
ATOM   1719 N N   . LYS   C 1 40 ? 27.341  -34.880 31.937  1.00 38.57  ? 39  LYS   C N   1 
ATOM   1720 C CA  . LYS   C 1 40 ? 26.388  -34.778 30.833  1.00 38.80  ? 39  LYS   C CA  1 
ATOM   1721 C C   . LYS   C 1 40 ? 25.287  -33.770 31.146  1.00 40.88  ? 39  LYS   C C   1 
ATOM   1722 O O   . LYS   C 1 40 ? 24.910  -33.626 32.294  1.00 44.00  ? 39  LYS   C O   1 
ATOM   1723 C CB  . LYS   C 1 40 ? 25.621  -36.089 30.610  1.00 36.33  ? 39  LYS   C CB  1 
ATOM   1724 C CG  . LYS   C 1 40 ? 26.463  -37.272 30.224  1.00 37.93  ? 39  LYS   C CG  1 
ATOM   1725 C CD  . LYS   C 1 40 ? 27.263  -37.069 28.952  1.00 45.21  ? 39  LYS   C CD  1 
ATOM   1726 C CE  . LYS   C 1 40 ? 28.074  -38.285 28.633  1.00 51.56  ? 39  LYS   C CE  1 
ATOM   1727 N NZ  . LYS   C 1 40 ? 29.193  -37.954 27.746  1.00 53.72  ? 39  LYS   C NZ  1 
ATOM   1728 N N   . TYR   C 1 41 ? 24.740  -33.116 30.107  1.00 38.44  ? 40  TYR   C N   1 
ATOM   1729 C CA  . TYR   C 1 41 ? 23.648  -32.157 30.249  1.00 36.76  ? 40  TYR   C CA  1 
ATOM   1730 C C   . TYR   C 1 41 ? 22.366  -32.770 29.701  1.00 38.80  ? 40  TYR   C C   1 
ATOM   1731 O O   . TYR   C 1 41 ? 22.424  -33.518 28.719  1.00 36.27  ? 40  TYR   C O   1 
ATOM   1732 C CB  . TYR   C 1 41 ? 23.844  -30.957 29.312  1.00 37.17  ? 40  TYR   C CB  1 
ATOM   1733 C CG  . TYR   C 1 41 ? 25.001  -30.079 29.758  1.00 40.56  ? 40  TYR   C CG  1 
ATOM   1734 C CD1 . TYR   C 1 41 ? 26.298  -30.316 29.306  1.00 38.26  ? 40  TYR   C CD1 1 
ATOM   1735 C CD2 . TYR   C 1 41 ? 24.785  -29.026 30.650  1.00 43.50  ? 40  TYR   C CD2 1 
ATOM   1736 C CE1 . TYR   C 1 41 ? 27.360  -29.544 29.744  1.00 46.20  ? 40  TYR   C CE1 1 
ATOM   1737 C CE2 . TYR   C 1 41 ? 25.838  -28.227 31.064  1.00 46.33  ? 40  TYR   C CE2 1 
ATOM   1738 C CZ  . TYR   C 1 41 ? 27.121  -28.501 30.628  1.00 51.58  ? 40  TYR   C CZ  1 
ATOM   1739 O OH  . TYR   C 1 41 ? 28.142  -27.723 31.073  1.00 61.38  ? 40  TYR   C OH  1 
ATOM   1740 N N   . PRO   C 1 42 ? 21.186  -32.442 30.290  1.00 38.89  ? 41  PRO   C N   1 
ATOM   1741 C CA  . PRO   C 1 42 ? 19.900  -32.901 29.768  1.00 38.60  ? 41  PRO   C CA  1 
ATOM   1742 C C   . PRO   C 1 42 ? 19.523  -31.956 28.628  1.00 40.23  ? 41  PRO   C C   1 
ATOM   1743 O O   . PRO   C 1 42 ? 19.456  -30.735 28.815  1.00 39.71  ? 41  PRO   C O   1 
ATOM   1744 C CB  . PRO   C 1 42 ? 18.929  -32.794 30.958  1.00 39.48  ? 41  PRO   C CB  1 
ATOM   1745 C CG  . PRO   C 1 42 ? 19.582  -31.782 31.881  1.00 40.24  ? 41  PRO   C CG  1 
ATOM   1746 C CD  . PRO   C 1 42 ? 21.031  -31.567 31.467  1.00 41.46  ? 41  PRO   C CD  1 
ATOM   1747 N N   . ILE   C 1 43 ? 19.288  -32.561 27.458  1.00 38.35  ? 42  ILE   C N   1 
ATOM   1748 C CA  . ILE   C 1 43 ? 19.000  -31.828 26.235  1.00 36.26  ? 42  ILE   C CA  1 
ATOM   1749 C C   . ILE   C 1 43 ? 17.558  -32.128 25.824  1.00 39.33  ? 42  ILE   C C   1 
ATOM   1750 O O   . ILE   C 1 43 ? 17.105  -33.281 25.873  1.00 41.71  ? 42  ILE   C O   1 
ATOM   1751 C CB  . ILE   C 1 43 ? 20.013  -32.239 25.146  1.00 35.80  ? 42  ILE   C CB  1 
ATOM   1752 C CG1 . ILE   C 1 43 ? 21.468  -31.989 25.601  1.00 32.80  ? 42  ILE   C CG1 1 
ATOM   1753 C CG2 . ILE   C 1 43 ? 19.693  -31.594 23.785  1.00 35.43  ? 42  ILE   C CG2 1 
ATOM   1754 C CD1 . ILE   C 1 43 ? 21.824  -30.535 25.887  1.00 34.43  ? 42  ILE   C CD1 1 
ATOM   1755 N N   . PHE   C 1 44 ? 16.851  -31.073 25.396  1.00 38.49  ? 43  PHE   C N   1 
ATOM   1756 C CA  . PHE   C 1 44 ? 15.578  -31.222 24.707  1.00 35.11  ? 43  PHE   C CA  1 
ATOM   1757 C C   . PHE   C 1 44 ? 15.750  -30.783 23.253  1.00 31.84  ? 43  PHE   C C   1 
ATOM   1758 O O   . PHE   C 1 44 ? 16.332  -29.728 23.008  1.00 32.02  ? 43  PHE   C O   1 
ATOM   1759 C CB  . PHE   C 1 44 ? 14.634  -30.226 25.383  1.00 41.73  ? 43  PHE   C CB  1 
ATOM   1760 C CG  . PHE   C 1 44 ? 13.280  -30.119 24.706  1.00 39.48  ? 43  PHE   C CG  1 
ATOM   1761 C CD1 . PHE   C 1 44 ? 12.352  -31.149 24.821  1.00 39.44  ? 43  PHE   C CD1 1 
ATOM   1762 C CD2 . PHE   C 1 44 ? 12.954  -28.999 23.941  1.00 43.59  ? 43  PHE   C CD2 1 
ATOM   1763 C CE1 . PHE   C 1 44 ? 11.115  -31.060 24.197  1.00 49.63  ? 43  PHE   C CE1 1 
ATOM   1764 C CE2 . PHE   C 1 44 ? 11.720  -28.918 23.306  1.00 45.96  ? 43  PHE   C CE2 1 
ATOM   1765 C CZ  . PHE   C 1 44 ? 10.803  -29.941 23.438  1.00 49.76  ? 43  PHE   C CZ  1 
ATOM   1766 N N   . PHE   C 1 45 ? 15.315  -31.633 22.325  1.00 35.19  ? 44  PHE   C N   1 
ATOM   1767 C CA  . PHE   C 1 45 ? 15.496  -31.390 20.904  1.00 37.55  ? 44  PHE   C CA  1 
ATOM   1768 C C   . PHE   C 1 45 ? 14.213  -30.770 20.355  1.00 35.70  ? 44  PHE   C C   1 
ATOM   1769 O O   . PHE   C 1 45 ? 13.134  -31.349 20.498  1.00 39.72  ? 44  PHE   C O   1 
ATOM   1770 C CB  . PHE   C 1 45 ? 15.844  -32.669 20.138  1.00 33.27  ? 44  PHE   C CB  1 
ATOM   1771 C CG  . PHE   C 1 45 ? 17.211  -33.248 20.472  1.00 33.66  ? 44  PHE   C CG  1 
ATOM   1772 C CD1 . PHE   C 1 45 ? 18.341  -32.867 19.756  1.00 32.59  ? 44  PHE   C CD1 1 
ATOM   1773 C CD2 . PHE   C 1 45 ? 17.356  -34.174 21.513  1.00 36.11  ? 44  PHE   C CD2 1 
ATOM   1774 C CE1 . PHE   C 1 45 ? 19.599  -33.411 20.067  1.00 34.97  ? 44  PHE   C CE1 1 
ATOM   1775 C CE2 . PHE   C 1 45 ? 18.604  -34.710 21.836  1.00 38.84  ? 44  PHE   C CE2 1 
ATOM   1776 C CZ  . PHE   C 1 45 ? 19.726  -34.333 21.102  1.00 35.99  ? 44  PHE   C CZ  1 
ATOM   1777 N N   . PHE   C 1 46 ? 14.343  -29.598 19.715  1.00 36.93  ? 45  PHE   C N   1 
ATOM   1778 C CA  . PHE   C 1 46 ? 13.191  -28.994 19.061  1.00 31.80  ? 45  PHE   C CA  1 
ATOM   1779 C C   . PHE   C 1 46 ? 12.755  -29.839 17.865  1.00 34.37  ? 45  PHE   C C   1 
ATOM   1780 O O   . PHE   C 1 46 ? 13.539  -30.601 17.269  1.00 34.63  ? 45  PHE   C O   1 
ATOM   1781 C CB  . PHE   C 1 46 ? 13.453  -27.548 18.618  1.00 31.91  ? 45  PHE   C CB  1 
ATOM   1782 C CG  . PHE   C 1 46 ? 13.752  -26.588 19.751  1.00 33.70  ? 45  PHE   C CG  1 
ATOM   1783 C CD1 . PHE   C 1 46 ? 12.728  -26.135 20.584  1.00 38.82  ? 45  PHE   C CD1 1 
ATOM   1784 C CD2 . PHE   C 1 46 ? 15.046  -26.104 19.941  1.00 31.15  ? 45  PHE   C CD2 1 
ATOM   1785 C CE1 . PHE   C 1 46 ? 13.011  -25.242 21.618  1.00 41.17  ? 45  PHE   C CE1 1 
ATOM   1786 C CE2 . PHE   C 1 46 ? 15.305  -25.178 20.947  1.00 36.70  ? 45  PHE   C CE2 1 
ATOM   1787 C CZ  . PHE   C 1 46 ? 14.299  -24.767 21.790  1.00 36.10  ? 45  PHE   C CZ  1 
ATOM   1788 N N   . GLY   C 1 47 ? 11.486  -29.667 17.491  1.00 33.73  ? 46  GLY   C N   1 
ATOM   1789 C CA  . GLY   C 1 47 ? 10.953  -30.392 16.351  1.00 37.07  ? 46  GLY   C CA  1 
ATOM   1790 C C   . GLY   C 1 47 ? 10.502  -31.796 16.746  1.00 44.09  ? 46  GLY   C C   1 
ATOM   1791 O O   . GLY   C 1 47 ? 9.312   -32.082 16.683  1.00 46.74  ? 46  GLY   C O   1 
ATOM   1792 N N   . THR   C 1 48 ? 11.454  -32.667 17.121  1.00 37.90  ? 47  THR   C N   1 
ATOM   1793 C CA  . THR   C 1 48 ? 11.116  -34.028 17.538  1.00 39.72  ? 47  THR   C CA  1 
ATOM   1794 C C   . THR   C 1 48 ? 10.562  -34.019 18.970  1.00 36.90  ? 47  THR   C C   1 
ATOM   1795 O O   . THR   C 1 48 ? 9.772   -34.893 19.330  1.00 39.60  ? 47  THR   C O   1 
ATOM   1796 C CB  . THR   C 1 48 ? 12.328  -34.959 17.456  1.00 40.14  ? 47  THR   C CB  1 
ATOM   1797 O OG1 . THR   C 1 48 ? 13.236  -34.495 18.453  1.00 40.14  ? 47  THR   C OG1 1 
ATOM   1798 C CG2 . THR   C 1 48 ? 12.937  -35.081 16.070  1.00 36.69  ? 47  THR   C CG2 1 
ATOM   1799 N N   . HIS   C 1 49 ? 10.993  -33.050 19.783  1.00 36.01  ? 48  HIS   C N   1 
ATOM   1800 C CA  . HIS   C 1 49 ? 10.610  -32.913 21.185  1.00 42.65  ? 48  HIS   C CA  1 
ATOM   1801 C C   . HIS   C 1 49 ? 11.072  -34.114 22.025  1.00 44.58  ? 48  HIS   C C   1 
ATOM   1802 O O   . HIS   C 1 49 ? 10.436  -34.428 23.022  1.00 46.75  ? 48  HIS   C O   1 
ATOM   1803 C CB  . HIS   C 1 49 ? 9.107   -32.642 21.356  1.00 42.75  ? 48  HIS   C CB  1 
ATOM   1804 C CG  . HIS   C 1 49 ? 8.589   -31.531 20.497  1.00 49.59  ? 48  HIS   C CG  1 
ATOM   1805 N ND1 . HIS   C 1 49 ? 7.465   -31.676 19.709  1.00 50.73  ? 48  HIS   C ND1 1 
ATOM   1806 C CD2 . HIS   C 1 49 ? 9.039   -30.293 20.270  1.00 50.54  ? 48  HIS   C CD2 1 
ATOM   1807 C CE1 . HIS   C 1 49 ? 7.258   -30.561 19.026  1.00 53.04  ? 48  HIS   C CE1 1 
ATOM   1808 N NE2 . HIS   C 1 49 ? 8.194   -29.701 19.357  1.00 49.01  ? 48  HIS   C NE2 1 
ATOM   1809 N N   . GLU   C 1 50 ? 12.189  -34.757 21.644  1.00 39.79  ? 49  GLU   C N   1 
ATOM   1810 C CA  . GLU   C 1 50 ? 12.772  -35.835 22.430  1.00 39.42  ? 49  GLU   C CA  1 
ATOM   1811 C C   . GLU   C 1 50 ? 13.867  -35.298 23.353  1.00 39.34  ? 49  GLU   C C   1 
ATOM   1812 O O   . GLU   C 1 50 ? 14.185  -34.105 23.346  1.00 33.70  ? 49  GLU   C O   1 
ATOM   1813 C CB  . GLU   C 1 50 ? 13.272  -36.952 21.519  1.00 41.24  ? 49  GLU   C CB  1 
ATOM   1814 C CG  . GLU   C 1 50 ? 12.182  -37.541 20.629  1.00 52.44  ? 49  GLU   C CG  1 
ATOM   1815 C CD  . GLU   C 1 50 ? 12.777  -38.394 19.526  1.00 58.68  ? 49  GLU   C CD  1 
ATOM   1816 O OE1 . GLU   C 1 50 ? 14.004  -38.645 19.533  1.00 65.72  ? 49  GLU   C OE1 1 
ATOM   1817 O OE2 . GLU   C 1 50 ? 12.005  -38.801 18.639  1.00 66.68  ? 49  GLU   C OE2 1 
ATOM   1818 N N   . THR   C 1 51 ? 14.396  -36.190 24.209  1.00 46.78  ? 50  THR   C N   1 
ATOM   1819 C CA  . THR   C 1 51 ? 15.408  -35.831 25.199  1.00 40.67  ? 50  THR   C CA  1 
ATOM   1820 C C   . THR   C 1 51 ? 16.563  -36.829 25.120  1.00 36.59  ? 50  THR   C C   1 
ATOM   1821 O O   . THR   C 1 51 ? 16.418  -37.937 24.613  1.00 38.22  ? 50  THR   C O   1 
ATOM   1822 C CB  . THR   C 1 51 ? 14.846  -35.758 26.625  1.00 44.45  ? 50  THR   C CB  1 
ATOM   1823 O OG1 . THR   C 1 51 ? 14.287  -37.051 26.843  1.00 41.87  ? 50  THR   C OG1 1 
ATOM   1824 C CG2 . THR   C 1 51 ? 13.844  -34.640 26.871  1.00 45.88  ? 50  THR   C CG2 1 
ATOM   1825 N N   . ALA   C 1 52 ? 17.736  -36.390 25.575  1.00 38.00  ? 51  ALA   C N   1 
ATOM   1826 C CA  . ALA   C 1 52 ? 18.930  -37.210 25.642  1.00 40.66  ? 51  ALA   C CA  1 
ATOM   1827 C C   . ALA   C 1 52 ? 19.922  -36.485 26.543  1.00 43.55  ? 51  ALA   C C   1 
ATOM   1828 O O   . ALA   C 1 52 ? 19.713  -35.323 26.874  1.00 39.88  ? 51  ALA   C O   1 
ATOM   1829 C CB  . ALA   C 1 52 ? 19.490  -37.449 24.256  1.00 38.14  ? 51  ALA   C CB  1 
ATOM   1830 N N   . PHE   C 1 53 ? 20.972  -37.198 26.967  1.00 44.57  ? 52  PHE   C N   1 
ATOM   1831 C CA  . PHE   C 1 53 ? 22.047  -36.617 27.752  1.00 42.62  ? 52  PHE   C CA  1 
ATOM   1832 C C   . PHE   C 1 53 ? 23.236  -36.493 26.822  1.00 39.35  ? 52  PHE   C C   1 
ATOM   1833 O O   . PHE   C 1 53 ? 23.587  -37.464 26.167  1.00 42.40  ? 52  PHE   C O   1 
ATOM   1834 C CB  . PHE   C 1 53 ? 22.432  -37.584 28.879  1.00 43.90  ? 52  PHE   C CB  1 
ATOM   1835 C CG  . PHE   C 1 53 ? 21.434  -37.545 30.023  1.00 46.16  ? 52  PHE   C CG  1 
ATOM   1836 C CD1 . PHE   C 1 53 ? 21.278  -36.395 30.795  1.00 44.54  ? 52  PHE   C CD1 1 
ATOM   1837 C CD2 . PHE   C 1 53 ? 20.643  -38.652 30.316  1.00 58.40  ? 52  PHE   C CD2 1 
ATOM   1838 C CE1 . PHE   C 1 53 ? 20.348  -36.347 31.823  1.00 51.40  ? 52  PHE   C CE1 1 
ATOM   1839 C CE2 . PHE   C 1 53 ? 19.721  -38.603 31.358  1.00 59.90  ? 52  PHE   C CE2 1 
ATOM   1840 C CZ  . PHE   C 1 53 ? 19.572  -37.450 32.105  1.00 49.25  ? 52  PHE   C CZ  1 
ATOM   1841 N N   . LEU   C 1 54 ? 23.844  -35.305 26.767  1.00 35.07  ? 53  LEU   C N   1 
ATOM   1842 C CA  . LEU   C 1 54 ? 25.012  -35.110 25.924  1.00 33.83  ? 53  LEU   C CA  1 
ATOM   1843 C C   . LEU   C 1 54 ? 26.066  -34.366 26.730  1.00 35.89  ? 53  LEU   C C   1 
ATOM   1844 O O   . LEU   C 1 54 ? 25.730  -33.651 27.664  1.00 39.26  ? 53  LEU   C O   1 
ATOM   1845 C CB  . LEU   C 1 54 ? 24.661  -34.363 24.636  1.00 34.48  ? 53  LEU   C CB  1 
ATOM   1846 C CG  . LEU   C 1 54 ? 23.770  -35.111 23.634  1.00 43.62  ? 53  LEU   C CG  1 
ATOM   1847 C CD1 . LEU   C 1 54 ? 23.295  -34.163 22.544  1.00 41.81  ? 53  LEU   C CD1 1 
ATOM   1848 C CD2 . LEU   C 1 54 ? 24.539  -36.286 23.021  1.00 46.60  ? 53  LEU   C CD2 1 
ATOM   1849 N N   . GLY   C 1 55 ? 27.333  -34.564 26.358  1.00 38.42  ? 54  GLY   C N   1 
ATOM   1850 C CA  . GLY   C 1 55 ? 28.452  -33.852 26.952  1.00 38.90  ? 54  GLY   C CA  1 
ATOM   1851 C C   . GLY   C 1 55 ? 28.728  -32.535 26.226  1.00 44.55  ? 54  GLY   C C   1 
ATOM   1852 O O   . GLY   C 1 55 ? 28.183  -32.270 25.138  1.00 38.84  ? 54  GLY   C O   1 
ATOM   1853 N N   . PRO   C 1 56 ? 29.580  -31.661 26.813  1.00 43.32  ? 55  PRO   C N   1 
ATOM   1854 C CA  . PRO   C 1 56 ? 29.717  -30.286 26.338  1.00 45.70  ? 55  PRO   C CA  1 
ATOM   1855 C C   . PRO   C 1 56 ? 30.341  -30.194 24.951  1.00 45.81  ? 55  PRO   C C   1 
ATOM   1856 O O   . PRO   C 1 56 ? 30.069  -29.242 24.220  1.00 52.85  ? 55  PRO   C O   1 
ATOM   1857 C CB  . PRO   C 1 56 ? 30.556  -29.573 27.443  1.00 46.29  ? 55  PRO   C CB  1 
ATOM   1858 C CG  . PRO   C 1 56 ? 31.312  -30.705 28.126  1.00 39.03  ? 55  PRO   C CG  1 
ATOM   1859 C CD  . PRO   C 1 56 ? 30.404  -31.925 28.009  1.00 47.40  ? 55  PRO   C CD  1 
ATOM   1860 N N   . LYS   C 1 57 ? 31.122  -31.217 24.585  1.00 44.18  ? 56  LYS   C N   1 
ATOM   1861 C CA  . LYS   C 1 57 ? 31.777  -31.261 23.288  1.00 48.41  ? 56  LYS   C CA  1 
ATOM   1862 C C   . LYS   C 1 57 ? 30.735  -31.353 22.173  1.00 50.69  ? 56  LYS   C C   1 
ATOM   1863 O O   . LYS   C 1 57 ? 31.040  -31.049 21.019  1.00 47.00  ? 56  LYS   C O   1 
ATOM   1864 C CB  . LYS   C 1 57 ? 32.712  -32.468 23.160  1.00 51.79  ? 56  LYS   C CB  1 
ATOM   1865 N N   . ASP   C 1 58 ? 29.516  -31.780 22.531  1.00 46.93  ? 57  ASP   C N   1 
ATOM   1866 C CA  . ASP   C 1 58 ? 28.502  -32.110 21.538  1.00 43.86  ? 57  ASP   C CA  1 
ATOM   1867 C C   . ASP   C 1 58 ? 27.526  -30.957 21.356  1.00 43.74  ? 57  ASP   C C   1 
ATOM   1868 O O   . ASP   C 1 58 ? 26.518  -31.106 20.669  1.00 42.30  ? 57  ASP   C O   1 
ATOM   1869 C CB  . ASP   C 1 58 ? 27.764  -33.386 21.905  1.00 44.64  ? 57  ASP   C CB  1 
ATOM   1870 C CG  . ASP   C 1 58 ? 28.636  -34.629 21.974  1.00 46.18  ? 57  ASP   C CG  1 
ATOM   1871 O OD1 . ASP   C 1 58 ? 29.539  -34.746 21.131  1.00 44.32  ? 57  ASP   C OD1 1 
ATOM   1872 O OD2 . ASP   C 1 58 ? 28.389  -35.471 22.856  1.00 48.15  ? 57  ASP   C OD2 1 
ATOM   1873 N N   . LEU   C 1 59 ? 27.819  -29.817 21.984  1.00 37.94  ? 58  LEU   C N   1 
ATOM   1874 C CA  . LEU   C 1 59 ? 26.854  -28.735 22.100  1.00 40.98  ? 58  LEU   C CA  1 
ATOM   1875 C C   . LEU   C 1 59 ? 27.475  -27.451 21.570  1.00 42.45  ? 58  LEU   C C   1 
ATOM   1876 O O   . LEU   C 1 59 ? 28.652  -27.206 21.823  1.00 47.07  ? 58  LEU   C O   1 
ATOM   1877 C CB  . LEU   C 1 59 ? 26.500  -28.577 23.578  1.00 41.55  ? 58  LEU   C CB  1 
ATOM   1878 C CG  . LEU   C 1 59 ? 25.918  -29.823 24.257  1.00 38.06  ? 58  LEU   C CG  1 
ATOM   1879 C CD1 . LEU   C 1 59 ? 25.742  -29.592 25.740  1.00 36.54  ? 58  LEU   C CD1 1 
ATOM   1880 C CD2 . LEU   C 1 59 ? 24.593  -30.225 23.589  1.00 31.10  ? 58  LEU   C CD2 1 
ATOM   1881 N N   . PHE   C 1 60 ? 26.658  -26.639 20.890  1.00 43.43  ? 59  PHE   C N   1 
ATOM   1882 C CA  . PHE   C 1 60 ? 27.122  -25.454 20.174  1.00 42.84  ? 59  PHE   C CA  1 
ATOM   1883 C C   . PHE   C 1 60 ? 26.170  -24.294 20.468  1.00 41.58  ? 59  PHE   C C   1 
ATOM   1884 O O   . PHE   C 1 60 ? 24.973  -24.390 20.182  1.00 43.92  ? 59  PHE   C O   1 
ATOM   1885 C CB  . PHE   C 1 60 ? 27.339  -25.783 18.685  1.00 42.57  ? 59  PHE   C CB  1 
ATOM   1886 C CG  . PHE   C 1 60 ? 28.365  -26.882 18.424  1.00 42.96  ? 59  PHE   C CG  1 
ATOM   1887 C CD1 . PHE   C 1 60 ? 27.996  -28.223 18.405  1.00 37.25  ? 59  PHE   C CD1 1 
ATOM   1888 C CD2 . PHE   C 1 60 ? 29.709  -26.580 18.193  1.00 46.94  ? 59  PHE   C CD2 1 
ATOM   1889 C CE1 . PHE   C 1 60 ? 28.934  -29.233 18.232  1.00 42.86  ? 59  PHE   C CE1 1 
ATOM   1890 C CE2 . PHE   C 1 60 ? 30.647  -27.590 17.984  1.00 45.73  ? 59  PHE   C CE2 1 
ATOM   1891 C CZ  . PHE   C 1 60 ? 30.265  -28.917 17.996  1.00 46.66  ? 59  PHE   C CZ  1 
ATOM   1892 N N   . PRO   C 1 61 ? 26.646  -23.169 21.072  1.00 44.10  ? 60  PRO   C N   1 
ATOM   1893 C CA  . PRO   C 1 61 ? 25.769  -22.042 21.395  1.00 44.77  ? 60  PRO   C CA  1 
ATOM   1894 C C   . PRO   C 1 61 ? 25.046  -21.616 20.120  1.00 41.79  ? 60  PRO   C C   1 
ATOM   1895 O O   . PRO   C 1 61 ? 25.641  -21.548 19.041  1.00 46.30  ? 60  PRO   C O   1 
ATOM   1896 C CB  . PRO   C 1 61 ? 26.704  -20.937 21.969  1.00 45.15  ? 60  PRO   C CB  1 
ATOM   1897 C CG  . PRO   C 1 61 ? 27.991  -21.674 22.287  1.00 45.76  ? 60  PRO   C CG  1 
ATOM   1898 C CD  . PRO   C 1 61 ? 28.061  -22.893 21.388  1.00 48.97  ? 60  PRO   C CD  1 
ATOM   1899 N N   . TYR   C 1 62 ? 23.726  -21.425 20.249  1.00 49.90  ? 61  TYR   C N   1 
ATOM   1900 C CA  . TYR   C 1 62 ? 22.854  -21.240 19.102  1.00 53.06  ? 61  TYR   C CA  1 
ATOM   1901 C C   . TYR   C 1 62 ? 23.252  -19.995 18.318  1.00 62.43  ? 61  TYR   C C   1 
ATOM   1902 O O   . TYR   C 1 62 ? 23.431  -20.068 17.101  1.00 63.44  ? 61  TYR   C O   1 
ATOM   1903 C CB  . TYR   C 1 62 ? 21.397  -21.151 19.549  1.00 49.42  ? 61  TYR   C CB  1 
ATOM   1904 C CG  . TYR   C 1 62 ? 20.429  -20.771 18.439  1.00 49.89  ? 61  TYR   C CG  1 
ATOM   1905 C CD1 . TYR   C 1 62 ? 20.193  -21.634 17.374  1.00 50.14  ? 61  TYR   C CD1 1 
ATOM   1906 C CD2 . TYR   C 1 62 ? 19.721  -19.574 18.486  1.00 50.63  ? 61  TYR   C CD2 1 
ATOM   1907 C CE1 . TYR   C 1 62 ? 19.294  -21.304 16.371  1.00 50.65  ? 61  TYR   C CE1 1 
ATOM   1908 C CE2 . TYR   C 1 62 ? 18.824  -19.230 17.487  1.00 54.77  ? 61  TYR   C CE2 1 
ATOM   1909 C CZ  . TYR   C 1 62 ? 18.605  -20.102 16.430  1.00 47.89  ? 61  TYR   C CZ  1 
ATOM   1910 O OH  . TYR   C 1 62 ? 17.728  -19.773 15.438  1.00 45.99  ? 61  TYR   C OH  1 
ATOM   1911 N N   . ASP   C 1 63 ? 23.406  -18.873 19.032  1.00 58.54  ? 62  ASP   C N   1 
ATOM   1912 C CA  . ASP   C 1 63 ? 23.762  -17.617 18.391  1.00 62.27  ? 62  ASP   C CA  1 
ATOM   1913 C C   . ASP   C 1 63 ? 25.117  -17.712 17.704  1.00 53.68  ? 62  ASP   C C   1 
ATOM   1914 O O   . ASP   C 1 63 ? 25.266  -17.216 16.588  1.00 66.82  ? 62  ASP   C O   1 
ATOM   1915 C CB  . ASP   C 1 63 ? 23.504  -16.415 19.281  1.00 71.06  ? 62  ASP   C CB  1 
ATOM   1916 C CG  . ASP   C 1 63 ? 22.071  -15.913 19.182  1.00 86.12  ? 62  ASP   C CG  1 
ATOM   1917 O OD1 . ASP   C 1 63 ? 21.347  -15.993 20.202  1.00 78.76  ? 62  ASP   C OD1 1 
ATOM   1918 O OD2 . ASP   C 1 63 ? 21.683  -15.479 18.069  1.00 88.51  ? 62  ASP   C OD2 1 
ATOM   1919 N N   . LYS   C 1 64 ? 26.082  -18.377 18.340  1.00 46.34  ? 63  LYS   C N   1 
ATOM   1920 C CA  . LYS   C 1 64 ? 27.422  -18.458 17.778  1.00 48.32  ? 63  LYS   C CA  1 
ATOM   1921 C C   . LYS   C 1 64 ? 27.458  -19.342 16.529  1.00 50.03  ? 63  LYS   C C   1 
ATOM   1922 O O   . LYS   C 1 64 ? 28.295  -19.098 15.665  1.00 47.40  ? 63  LYS   C O   1 
ATOM   1923 C CB  . LYS   C 1 64 ? 28.501  -18.882 18.785  1.00 53.85  ? 63  LYS   C CB  1 
ATOM   1924 N N   . SER   C 1 65 ? 26.551  -20.342 16.408  1.00 44.57  ? 64  SER   C N   1 
ATOM   1925 C CA  . SER   C 1 65 ? 26.710  -21.338 15.348  1.00 39.90  ? 64  SER   C CA  1 
ATOM   1926 C C   . SER   C 1 65 ? 25.507  -21.435 14.396  1.00 38.49  ? 64  SER   C C   1 
ATOM   1927 O O   . SER   C 1 65 ? 25.532  -22.230 13.466  1.00 37.86  ? 64  SER   C O   1 
ATOM   1928 C CB  . SER   C 1 65 ? 27.105  -22.697 15.900  1.00 40.67  ? 64  SER   C CB  1 
ATOM   1929 O OG  . SER   C 1 65 ? 26.052  -23.201 16.709  1.00 43.86  ? 64  SER   C OG  1 
ATOM   1930 N N   . LYS   C 1 66 ? 24.470  -20.608 14.584  1.00 39.30  ? 65  LYS   C N   1 
ATOM   1931 C CA  . LYS   C 1 66 ? 23.316  -20.691 13.692  1.00 44.75  ? 65  LYS   C CA  1 
ATOM   1932 C C   . LYS   C 1 66 ? 23.696  -20.400 12.240  1.00 49.13  ? 65  LYS   C C   1 
ATOM   1933 O O   . LYS   C 1 66 ? 23.091  -20.964 11.332  1.00 41.68  ? 65  LYS   C O   1 
ATOM   1934 C CB  . LYS   C 1 66 ? 22.061  -19.918 14.116  1.00 43.97  ? 65  LYS   C CB  1 
ATOM   1935 C CG  . LYS   C 1 66 ? 22.258  -18.413 14.214  1.00 40.86  ? 65  LYS   C CG  1 
ATOM   1936 C CD  . LYS   C 1 66 ? 20.901  -17.759 14.438  1.00 53.56  ? 65  LYS   C CD  1 
ATOM   1937 C CE  . LYS   C 1 66 ? 21.057  -16.315 14.736  1.00 52.85  ? 65  LYS   C CE  1 
ATOM   1938 N NZ  . LYS   C 1 66 ? 19.757  -15.786 15.127  1.00 60.26  ? 65  LYS   C NZ  1 
ATOM   1939 N N   . ASP   C 1 67 ? 24.707  -19.555 12.000  1.00 47.55  ? 66  ASP   C N   1 
ATOM   1940 C CA  . ASP   C 1 67 ? 25.085  -19.288 10.612  1.00 51.17  ? 66  ASP   C CA  1 
ATOM   1941 C C   . ASP   C 1 67 ? 25.508  -20.585 9.908   1.00 49.12  ? 66  ASP   C C   1 
ATOM   1942 O O   . ASP   C 1 67 ? 25.217  -20.763 8.731   1.00 42.18  ? 66  ASP   C O   1 
ATOM   1943 C CB  . ASP   C 1 67 ? 25.955  -18.045 10.424  1.00 53.79  ? 66  ASP   C CB  1 
ATOM   1944 C CG  . ASP   C 1 67 ? 27.435  -18.104 10.801  1.00 63.85  ? 66  ASP   C CG  1 
ATOM   1945 O OD1 . ASP   C 1 67 ? 28.091  -19.139 10.516  1.00 56.49  ? 66  ASP   C OD1 1 
ATOM   1946 O OD2 . ASP   C 1 67 ? 27.952  -17.063 11.287  1.00 65.14  ? 66  ASP   C OD2 1 
ATOM   1947 N N   . LYS   C 1 68 ? 26.156  -21.504 10.642  1.00 41.38  ? 67  LYS   C N   1 
ATOM   1948 C CA  . LYS   C 1 68 ? 26.625  -22.776 10.102  1.00 41.82  ? 67  LYS   C CA  1 
ATOM   1949 C C   . LYS   C 1 68 ? 25.568  -23.904 10.187  1.00 41.40  ? 67  LYS   C C   1 
ATOM   1950 O O   . LYS   C 1 68 ? 25.400  -24.671 9.239   1.00 41.96  ? 67  LYS   C O   1 
ATOM   1951 C CB  . LYS   C 1 68 ? 27.922  -23.052 10.874  1.00 42.37  ? 67  LYS   C CB  1 
ATOM   1952 C CG  . LYS   C 1 68 ? 28.622  -24.376 10.659  1.00 47.77  ? 67  LYS   C CG  1 
ATOM   1953 C CD  . LYS   C 1 68 ? 29.919  -24.381 11.472  1.00 52.77  ? 67  LYS   C CD  1 
ATOM   1954 C CE  . LYS   C 1 68 ? 30.688  -25.652 11.301  1.00 63.22  ? 67  LYS   C CE  1 
ATOM   1955 N NZ  . LYS   C 1 68 ? 30.934  -25.966 9.890   1.00 67.46  ? 67  LYS   C NZ  1 
ATOM   1956 N N   . TYR   C 1 69 ? 24.840  -24.030 11.307  1.00 36.20  ? 68  TYR   C N   1 
ATOM   1957 C CA  . TYR   C 1 69 ? 24.005  -25.222 11.480  1.00 36.49  ? 68  TYR   C CA  1 
ATOM   1958 C C   . TYR   C 1 69 ? 22.521  -24.941 11.229  1.00 36.62  ? 68  TYR   C C   1 
ATOM   1959 O O   . TYR   C 1 69 ? 21.755  -25.878 11.021  1.00 35.06  ? 68  TYR   C O   1 
ATOM   1960 C CB  . TYR   C 1 69 ? 24.196  -25.827 12.879  1.00 33.70  ? 68  TYR   C CB  1 
ATOM   1961 C CG  . TYR   C 1 69 ? 25.607  -26.319 13.169  1.00 33.10  ? 68  TYR   C CG  1 
ATOM   1962 C CD1 . TYR   C 1 69 ? 26.303  -27.139 12.278  1.00 38.66  ? 68  TYR   C CD1 1 
ATOM   1963 C CD2 . TYR   C 1 69 ? 26.244  -25.947 14.352  1.00 38.43  ? 68  TYR   C CD2 1 
ATOM   1964 C CE1 . TYR   C 1 69 ? 27.585  -27.597 12.565  1.00 37.31  ? 68  TYR   C CE1 1 
ATOM   1965 C CE2 . TYR   C 1 69 ? 27.520  -26.404 14.654  1.00 39.32  ? 68  TYR   C CE2 1 
ATOM   1966 C CZ  . TYR   C 1 69 ? 28.199  -27.204 13.749  1.00 42.36  ? 68  TYR   C CZ  1 
ATOM   1967 O OH  . TYR   C 1 69 ? 29.463  -27.596 14.115  1.00 44.44  ? 68  TYR   C OH  1 
ATOM   1968 N N   . GLY   C 1 70 ? 22.111  -23.668 11.311  1.00 31.60  ? 69  GLY   C N   1 
ATOM   1969 C CA  . GLY   C 1 70 ? 20.693  -23.339 11.194  1.00 37.76  ? 69  GLY   C CA  1 
ATOM   1970 C C   . GLY   C 1 70 ? 20.349  -23.183 9.720   1.00 39.25  ? 69  GLY   C C   1 
ATOM   1971 O O   . GLY   C 1 70 ? 20.365  -22.070 9.205   1.00 39.60  ? 69  GLY   C O   1 
ATOM   1972 N N   . LYS   C 1 71 ? 20.177  -24.325 9.045   1.00 36.37  ? 70  LYS   C N   1 
ATOM   1973 C CA  . LYS   C 1 71 ? 19.838  -24.401 7.630   1.00 40.38  ? 70  LYS   C CA  1 
ATOM   1974 C C   . LYS   C 1 71 ? 18.983  -25.644 7.462   1.00 40.07  ? 70  LYS   C C   1 
ATOM   1975 O O   . LYS   C 1 71 ? 19.181  -26.622 8.187   1.00 40.38  ? 70  LYS   C O   1 
ATOM   1976 C CB  . LYS   C 1 71 ? 21.061  -24.554 6.712   1.00 38.38  ? 70  LYS   C CB  1 
ATOM   1977 C CG  . LYS   C 1 71 ? 22.147  -25.465 7.249   1.00 40.18  ? 70  LYS   C CG  1 
ATOM   1978 C CD  . LYS   C 1 71 ? 23.219  -25.995 6.302   1.00 43.97  ? 70  LYS   C CD  1 
ATOM   1979 C CE  . LYS   C 1 71 ? 24.002  -27.129 6.927   1.00 48.20  ? 70  LYS   C CE  1 
ATOM   1980 N N   . PRO   C 1 72 ? 17.981  -25.637 6.551   1.00 37.33  ? 71  PRO   C N   1 
ATOM   1981 C CA  . PRO   C 1 72 ? 17.008  -26.728 6.522   1.00 31.09  ? 71  PRO   C CA  1 
ATOM   1982 C C   . PRO   C 1 72 ? 17.666  -28.060 6.192   1.00 35.71  ? 71  PRO   C C   1 
ATOM   1983 O O   . PRO   C 1 72 ? 18.733  -28.112 5.572   1.00 36.07  ? 71  PRO   C O   1 
ATOM   1984 C CB  . PRO   C 1 72 ? 16.039  -26.288 5.408   1.00 31.23  ? 71  PRO   C CB  1 
ATOM   1985 C CG  . PRO   C 1 72 ? 16.189  -24.787 5.409   1.00 32.11  ? 71  PRO   C CG  1 
ATOM   1986 C CD  . PRO   C 1 72 ? 17.679  -24.558 5.594   1.00 32.47  ? 71  PRO   C CD  1 
ATOM   1987 N N   . ASN   C 1 73 ? 16.981  -29.136 6.565   1.00 34.66  ? 72  ASN   C N   1 
ATOM   1988 C CA  . ASN   C 1 73 ? 17.319  -30.416 5.979   1.00 42.63  ? 72  ASN   C CA  1 
ATOM   1989 C C   . ASN   C 1 73 ? 16.118  -31.335 6.125   1.00 36.47  ? 72  ASN   C C   1 
ATOM   1990 O O   . ASN   C 1 73 ? 15.140  -30.986 6.780   1.00 35.50  ? 72  ASN   C O   1 
ATOM   1991 C CB  . ASN   C 1 73 ? 18.657  -30.988 6.446   1.00 45.89  ? 72  ASN   C CB  1 
ATOM   1992 C CG  . ASN   C 1 73 ? 18.584  -31.595 7.822   1.00 44.97  ? 72  ASN   C CG  1 
ATOM   1993 O OD1 . ASN   C 1 73 ? 17.808  -32.535 8.072   1.00 44.02  ? 72  ASN   C OD1 1 
ATOM   1994 N ND2 . ASN   C 1 73 ? 19.418  -31.086 8.709   1.00 45.48  ? 72  ASN   C ND2 1 
ATOM   1995 N N   . LYS   C 1 74 ? 16.218  -32.502 5.495   1.00 39.65  ? 73  LYS   C N   1 
ATOM   1996 C CA  . LYS   C 1 74 ? 15.031  -33.303 5.257   1.00 41.56  ? 73  LYS   C CA  1 
ATOM   1997 C C   . LYS   C 1 74 ? 14.776  -34.246 6.415   1.00 40.58  ? 73  LYS   C C   1 
ATOM   1998 O O   . LYS   C 1 74 ? 13.757  -34.946 6.422   1.00 41.71  ? 73  LYS   C O   1 
ATOM   1999 C CB  . LYS   C 1 74 ? 15.145  -34.018 3.908   1.00 50.13  ? 73  LYS   C CB  1 
ATOM   2000 C CG  . LYS   C 1 74 ? 14.838  -33.083 2.740   1.00 57.61  ? 73  LYS   C CG  1 
ATOM   2001 C CD  . LYS   C 1 74 ? 16.137  -32.733 2.023   1.00 62.26  ? 73  LYS   C CD  1 
ATOM   2002 N N   . ARG   C 1 75 ? 15.697  -34.277 7.390   1.00 36.68  ? 74  ARG   C N   1 
ATOM   2003 C CA  . ARG   C 1 75 ? 15.505  -35.202 8.505   1.00 36.34  ? 74  ARG   C CA  1 
ATOM   2004 C C   . ARG   C 1 75 ? 14.211  -34.871 9.246   1.00 37.99  ? 74  ARG   C C   1 
ATOM   2005 O O   . ARG   C 1 75 ? 13.837  -33.703 9.430   1.00 35.33  ? 74  ARG   C O   1 
ATOM   2006 C CB  . ARG   C 1 75 ? 16.691  -35.293 9.486   1.00 37.68  ? 74  ARG   C CB  1 
ATOM   2007 C CG  . ARG   C 1 75 ? 18.054  -35.477 8.830   1.00 39.20  ? 74  ARG   C CG  1 
ATOM   2008 C CD  . ARG   C 1 75 ? 18.374  -36.819 8.155   1.00 46.07  ? 74  ARG   C CD  1 
ATOM   2009 N NE  . ARG   C 1 75 ? 18.318  -37.841 9.199   1.00 41.94  ? 74  ARG   C NE  1 
ATOM   2010 C CZ  . ARG   C 1 75 ? 19.397  -38.296 9.834   1.00 40.27  ? 74  ARG   C CZ  1 
ATOM   2011 N NH1 . ARG   C 1 75 ? 19.236  -38.919 10.981  1.00 39.08  ? 74  ARG   C NH1 1 
ATOM   2012 N NH2 . ARG   C 1 75 ? 20.608  -38.020 9.378   1.00 38.49  ? 74  ARG   C NH2 1 
ATOM   2013 N N   . LYS   C 1 76 ? 13.536  -35.934 9.696   1.00 36.86  ? 75  LYS   C N   1 
ATOM   2014 C CA  . LYS   C 1 76 ? 12.221  -35.824 10.304  1.00 43.08  ? 75  LYS   C CA  1 
ATOM   2015 C C   . LYS   C 1 76 ? 12.256  -34.854 11.478  1.00 41.86  ? 75  LYS   C C   1 
ATOM   2016 O O   . LYS   C 1 76 ? 12.998  -35.066 12.444  1.00 38.04  ? 75  LYS   C O   1 
ATOM   2017 C CB  . LYS   C 1 76 ? 11.660  -37.172 10.785  1.00 40.64  ? 75  LYS   C CB  1 
ATOM   2018 C CG  . LYS   C 1 76 ? 10.142  -37.170 10.937  1.00 46.73  ? 75  LYS   C CG  1 
ATOM   2019 C CD  . LYS   C 1 76 ? 9.569   -38.465 11.502  1.00 57.82  ? 75  LYS   C CD  1 
ATOM   2020 N N   . GLY   C 1 77 ? 11.397  -33.831 11.410  1.00 40.41  ? 76  GLY   C N   1 
ATOM   2021 C CA  . GLY   C 1 77 ? 11.185  -32.965 12.560  1.00 35.70  ? 76  GLY   C CA  1 
ATOM   2022 C C   . GLY   C 1 77 ? 12.151  -31.783 12.577  1.00 31.73  ? 76  GLY   C C   1 
ATOM   2023 O O   . GLY   C 1 77 ? 12.004  -30.879 13.397  1.00 39.56  ? 76  GLY   C O   1 
ATOM   2024 N N   . PHE   C 1 78 ? 13.140  -31.789 11.672  1.00 34.09  ? 77  PHE   C N   1 
ATOM   2025 C CA  . PHE   C 1 78 ? 14.221  -30.831 11.743  1.00 31.50  ? 77  PHE   C CA  1 
ATOM   2026 C C   . PHE   C 1 78 ? 13.726  -29.403 11.464  1.00 36.17  ? 77  PHE   C C   1 
ATOM   2027 O O   . PHE   C 1 78 ? 14.099  -28.471 12.173  1.00 31.43  ? 77  PHE   C O   1 
ATOM   2028 C CB  . PHE   C 1 78 ? 15.338  -31.199 10.763  1.00 34.33  ? 77  PHE   C CB  1 
ATOM   2029 C CG  . PHE   C 1 78 ? 16.627  -30.439 11.052  1.00 34.74  ? 77  PHE   C CG  1 
ATOM   2030 C CD1 . PHE   C 1 78 ? 16.839  -29.163 10.519  1.00 36.55  ? 77  PHE   C CD1 1 
ATOM   2031 C CD2 . PHE   C 1 78 ? 17.635  -30.995 11.835  1.00 30.61  ? 77  PHE   C CD2 1 
ATOM   2032 C CE1 . PHE   C 1 78 ? 18.005  -28.453 10.770  1.00 34.75  ? 77  PHE   C CE1 1 
ATOM   2033 C CE2 . PHE   C 1 78 ? 18.822  -30.289 12.060  1.00 30.22  ? 77  PHE   C CE2 1 
ATOM   2034 C CZ  . PHE   C 1 78 ? 19.013  -29.031 11.530  1.00 35.53  ? 77  PHE   C CZ  1 
ATOM   2035 N N   . ASN   C 1 79 ? 12.937  -29.225 10.395  1.00 35.38  ? 78  ASN   C N   1 
ATOM   2036 C CA  . ASN   C 1 79 ? 12.599  -27.871 9.969   1.00 36.65  ? 78  ASN   C CA  1 
ATOM   2037 C C   . ASN   C 1 79 ? 11.626  -27.248 10.964  1.00 35.15  ? 78  ASN   C C   1 
ATOM   2038 O O   . ASN   C 1 79 ? 11.714  -26.070 11.300  1.00 31.33  ? 78  ASN   C O   1 
ATOM   2039 C CB  . ASN   C 1 79 ? 12.197  -27.794 8.498   1.00 36.00  ? 78  ASN   C CB  1 
ATOM   2040 C CG  . ASN   C 1 79 ? 13.339  -28.233 7.604   1.00 35.81  ? 78  ASN   C CG  1 
ATOM   2041 O OD1 . ASN   C 1 79 ? 14.502  -28.006 7.941   1.00 35.22  ? 78  ASN   C OD1 1 
ATOM   2042 N ND2 . ASN   C 1 79 ? 13.049  -28.890 6.493   1.00 32.05  ? 78  ASN   C ND2 1 
ATOM   2043 N N   . GLU   C 1 80 ? 10.718  -28.057 11.490  1.00 33.52  ? 79  GLU   C N   1 
ATOM   2044 C CA  . GLU   C 1 80 ? 9.872   -27.558 12.566  1.00 35.74  ? 79  GLU   C CA  1 
ATOM   2045 C C   . GLU   C 1 80 ? 10.737  -27.149 13.755  1.00 40.87  ? 79  GLU   C C   1 
ATOM   2046 O O   . GLU   C 1 80 ? 10.456  -26.138 14.397  1.00 39.82  ? 79  GLU   C O   1 
ATOM   2047 C CB  . GLU   C 1 80 ? 8.846   -28.619 12.961  1.00 37.85  ? 79  GLU   C CB  1 
ATOM   2048 C CG  . GLU   C 1 80 ? 7.840   -28.093 13.975  1.00 37.49  ? 79  GLU   C CG  1 
ATOM   2049 C CD  . GLU   C 1 80 ? 6.664   -29.033 14.189  1.00 50.63  ? 79  GLU   C CD  1 
ATOM   2050 O OE1 . GLU   C 1 80 ? 6.737   -30.227 13.814  1.00 55.19  ? 79  GLU   C OE1 1 
ATOM   2051 O OE2 . GLU   C 1 80 ? 5.648   -28.552 14.717  1.00 48.34  ? 79  GLU   C OE2 1 
ATOM   2052 N N   . GLY   C 1 81 ? 11.783  -27.953 14.043  1.00 38.49  ? 80  GLY   C N   1 
ATOM   2053 C CA  . GLY   C 1 81 ? 12.747  -27.596 15.079  1.00 37.99  ? 80  GLY   C CA  1 
ATOM   2054 C C   . GLY   C 1 81 ? 13.390  -26.226 14.835  1.00 35.80  ? 80  GLY   C C   1 
ATOM   2055 O O   . GLY   C 1 81 ? 13.591  -25.452 15.770  1.00 33.51  ? 80  GLY   C O   1 
ATOM   2056 N N   . LEU   C 1 82 ? 13.798  -25.962 13.584  1.00 35.05  ? 81  LEU   C N   1 
ATOM   2057 C CA  . LEU   C 1 82 ? 14.395  -24.660 13.263  1.00 36.98  ? 81  LEU   C CA  1 
ATOM   2058 C C   . LEU   C 1 82 ? 13.386  -23.544 13.548  1.00 33.97  ? 81  LEU   C C   1 
ATOM   2059 O O   . LEU   C 1 82 ? 13.750  -22.486 14.050  1.00 35.79  ? 81  LEU   C O   1 
ATOM   2060 C CB  . LEU   C 1 82 ? 14.906  -24.560 11.824  1.00 36.22  ? 81  LEU   C CB  1 
ATOM   2061 C CG  . LEU   C 1 82 ? 16.101  -25.442 11.442  1.00 31.84  ? 81  LEU   C CG  1 
ATOM   2062 C CD1 . LEU   C 1 82 ? 16.386  -25.227 9.966   1.00 32.27  ? 81  LEU   C CD1 1 
ATOM   2063 C CD2 . LEU   C 1 82 ? 17.310  -25.053 12.235  1.00 27.30  ? 81  LEU   C CD2 1 
ATOM   2064 N N   . TRP   C 1 83 ? 12.120  -23.760 13.180  1.00 34.39  ? 82  TRP   C N   1 
ATOM   2065 C CA  . TRP   C 1 83 ? 11.099  -22.758 13.464  1.00 41.10  ? 82  TRP   C CA  1 
ATOM   2066 C C   . TRP   C 1 83 ? 11.009  -22.495 14.980  1.00 45.11  ? 82  TRP   C C   1 
ATOM   2067 O O   . TRP   C 1 83 ? 11.001  -21.342 15.413  1.00 42.09  ? 82  TRP   C O   1 
ATOM   2068 C CB  . TRP   C 1 83 ? 9.729   -23.152 12.877  1.00 38.92  ? 82  TRP   C CB  1 
ATOM   2069 C CG  . TRP   C 1 83 ? 8.742   -22.015 12.959  1.00 43.13  ? 82  TRP   C CG  1 
ATOM   2070 C CD1 . TRP   C 1 83 ? 8.553   -21.004 12.056  1.00 45.30  ? 82  TRP   C CD1 1 
ATOM   2071 C CD2 . TRP   C 1 83 ? 7.833   -21.741 14.049  1.00 48.75  ? 82  TRP   C CD2 1 
ATOM   2072 N NE1 . TRP   C 1 83 ? 7.582   -20.135 12.486  1.00 38.95  ? 82  TRP   C NE1 1 
ATOM   2073 C CE2 . TRP   C 1 83 ? 7.121   -20.563 13.704  1.00 42.90  ? 82  TRP   C CE2 1 
ATOM   2074 C CE3 . TRP   C 1 83 ? 7.551   -22.382 15.269  1.00 46.05  ? 82  TRP   C CE3 1 
ATOM   2075 C CZ2 . TRP   C 1 83 ? 6.147   -20.025 14.536  1.00 44.54  ? 82  TRP   C CZ2 1 
ATOM   2076 C CZ3 . TRP   C 1 83 ? 6.584   -21.844 16.093  1.00 52.13  ? 82  TRP   C CZ3 1 
ATOM   2077 C CH2 . TRP   C 1 83 ? 5.908   -20.674 15.732  1.00 54.82  ? 82  TRP   C CH2 1 
ATOM   2078 N N   . GLU   C 1 84 ? 10.983  -23.565 15.793  1.00 39.79  ? 83  GLU   C N   1 
ATOM   2079 C CA  . GLU   C 1 84 ? 10.823  -23.436 17.240  1.00 39.11  ? 83  GLU   C CA  1 
ATOM   2080 C C   . GLU   C 1 84 ? 11.965  -22.654 17.885  1.00 41.49  ? 83  GLU   C C   1 
ATOM   2081 O O   . GLU   C 1 84 ? 11.723  -21.754 18.695  1.00 45.54  ? 83  GLU   C O   1 
ATOM   2082 C CB  . GLU   C 1 84 ? 10.626  -24.773 17.950  1.00 34.59  ? 83  GLU   C CB  1 
ATOM   2083 C CG  . GLU   C 1 84 ? 9.353   -25.465 17.481  1.00 39.23  ? 83  GLU   C CG  1 
ATOM   2084 C CD  . GLU   C 1 84 ? 9.176   -26.859 18.018  1.00 46.24  ? 83  GLU   C CD  1 
ATOM   2085 O OE1 . GLU   C 1 84 ? 10.179  -27.394 18.568  1.00 42.96  ? 83  GLU   C OE1 1 
ATOM   2086 O OE2 . GLU   C 1 84 ? 8.043   -27.400 17.874  1.00 46.45  ? 83  GLU   C OE2 1 
ATOM   2087 N N   . ILE   C 1 85 ? 13.206  -22.983 17.516  1.00 38.62  ? 84  ILE   C N   1 
ATOM   2088 C CA  . ILE   C 1 85 ? 14.364  -22.389 18.159  1.00 38.26  ? 84  ILE   C CA  1 
ATOM   2089 C C   . ILE   C 1 85 ? 14.436  -20.889 17.868  1.00 41.23  ? 84  ILE   C C   1 
ATOM   2090 O O   . ILE   C 1 85 ? 14.932  -20.138 18.701  1.00 36.87  ? 84  ILE   C O   1 
ATOM   2091 C CB  . ILE   C 1 85 ? 15.651  -23.111 17.743  1.00 35.58  ? 84  ILE   C CB  1 
ATOM   2092 C CG1 . ILE   C 1 85 ? 16.796  -22.741 18.678  1.00 37.59  ? 84  ILE   C CG1 1 
ATOM   2093 C CG2 . ILE   C 1 85 ? 16.026  -22.848 16.277  1.00 32.06  ? 84  ILE   C CG2 1 
ATOM   2094 C CD1 . ILE   C 1 85 ? 17.882  -23.790 18.767  1.00 35.45  ? 84  ILE   C CD1 1 
ATOM   2095 N N   . GLN   C 1 86 ? 13.981  -20.482 16.669  1.00 37.84  ? 85  GLN   C N   1 
ATOM   2096 C CA  . GLN   C 1 86 ? 13.976  -19.080 16.257  1.00 43.01  ? 85  GLN   C CA  1 
ATOM   2097 C C   . GLN   C 1 86 ? 12.759  -18.326 16.807  1.00 40.77  ? 85  GLN   C C   1 
ATOM   2098 O O   . GLN   C 1 86 ? 12.869  -17.153 17.135  1.00 43.41  ? 85  GLN   C O   1 
ATOM   2099 C CB  . GLN   C 1 86 ? 14.038  -18.937 14.731  1.00 40.77  ? 85  GLN   C CB  1 
ATOM   2100 C CG  . GLN   C 1 86 ? 14.317  -17.519 14.227  1.00 39.59  ? 85  GLN   C CG  1 
ATOM   2101 C CD  . GLN   C 1 86 ? 14.708  -17.480 12.758  1.00 43.74  ? 85  GLN   C CD  1 
ATOM   2102 O OE1 . GLN   C 1 86 ? 14.668  -18.492 12.041  1.00 41.17  ? 85  GLN   C OE1 1 
ATOM   2103 N NE2 . GLN   C 1 86 ? 15.159  -16.317 12.305  1.00 43.37  ? 85  GLN   C NE2 1 
ATOM   2104 N N   . ASN   C 1 87 ? 11.607  -18.989 16.887  1.00 43.24  ? 86  ASN   C N   1 
ATOM   2105 C CA  . ASN   C 1 87 ? 10.347  -18.281 17.056  1.00 52.19  ? 86  ASN   C CA  1 
ATOM   2106 C C   . ASN   C 1 87 ? 9.699   -18.552 18.414  1.00 58.07  ? 86  ASN   C C   1 
ATOM   2107 O O   . ASN   C 1 87 ? 9.088   -17.652 18.983  1.00 59.72  ? 86  ASN   C O   1 
ATOM   2108 C CB  . ASN   C 1 87 ? 9.384   -18.557 15.909  1.00 44.45  ? 86  ASN   C CB  1 
ATOM   2109 C CG  . ASN   C 1 87 ? 9.943   -17.972 14.640  1.00 49.85  ? 86  ASN   C CG  1 
ATOM   2110 O OD1 . ASN   C 1 87 ? 9.986   -16.746 14.514  1.00 47.82  ? 86  ASN   C OD1 1 
ATOM   2111 N ND2 . ASN   C 1 87 ? 10.433  -18.811 13.737  1.00 42.35  ? 86  ASN   C ND2 1 
ATOM   2112 N N   . ASN   C 1 88 ? 9.794   -19.788 18.914  1.00 51.42  ? 87  ASN   C N   1 
ATOM   2113 C CA  . ASN   C 1 88 ? 9.111   -20.101 20.162  1.00 56.16  ? 87  ASN   C CA  1 
ATOM   2114 C C   . ASN   C 1 88 ? 9.990   -20.956 21.070  1.00 50.26  ? 87  ASN   C C   1 
ATOM   2115 O O   . ASN   C 1 88 ? 9.585   -22.058 21.460  1.00 51.50  ? 87  ASN   C O   1 
ATOM   2116 C CB  . ASN   C 1 88 ? 7.764   -20.775 19.919  1.00 63.09  ? 87  ASN   C CB  1 
ATOM   2117 C CG  . ASN   C 1 88 ? 6.865   -20.655 21.129  1.00 62.43  ? 87  ASN   C CG  1 
ATOM   2118 O OD1 . ASN   C 1 88 ? 7.200   -19.941 22.086  1.00 62.18  ? 87  ASN   C OD1 1 
ATOM   2119 N ND2 . ASN   C 1 88 ? 5.729   -21.331 21.095  1.00 58.02  ? 87  ASN   C ND2 1 
ATOM   2120 N N   . PRO   C 1 89 ? 11.201  -20.475 21.438  1.00 47.25  ? 88  PRO   C N   1 
ATOM   2121 C CA  . PRO   C 1 89 ? 12.207  -21.333 22.068  1.00 53.90  ? 88  PRO   C CA  1 
ATOM   2122 C C   . PRO   C 1 89 ? 11.996  -21.784 23.514  1.00 55.35  ? 88  PRO   C C   1 
ATOM   2123 O O   . PRO   C 1 89 ? 12.693  -22.693 23.964  1.00 53.78  ? 88  PRO   C O   1 
ATOM   2124 C CB  . PRO   C 1 89 ? 13.515  -20.534 21.882  1.00 51.20  ? 88  PRO   C CB  1 
ATOM   2125 C CG  . PRO   C 1 89 ? 13.058  -19.077 21.870  1.00 50.18  ? 88  PRO   C CG  1 
ATOM   2126 C CD  . PRO   C 1 89 ? 11.687  -19.102 21.212  1.00 47.08  ? 88  PRO   C CD  1 
ATOM   2127 N N   . HIS   C 1 90 ? 11.032  -21.167 24.221  1.00 57.50  ? 89  HIS   C N   1 
ATOM   2128 C CA  . HIS   C 1 90 ? 10.778  -21.493 25.622  1.00 51.50  ? 89  HIS   C CA  1 
ATOM   2129 C C   . HIS   C 1 90 ? 9.326   -21.891 25.877  1.00 57.26  ? 89  HIS   C C   1 
ATOM   2130 O O   . HIS   C 1 90 ? 8.878   -21.851 27.020  1.00 65.18  ? 89  HIS   C O   1 
ATOM   2131 C CB  . HIS   C 1 90 ? 11.228  -20.372 26.559  1.00 40.55  ? 89  HIS   C CB  1 
ATOM   2132 C CG  . HIS   C 1 90 ? 12.592  -19.858 26.277  1.00 45.33  ? 89  HIS   C CG  1 
ATOM   2133 N ND1 . HIS   C 1 90 ? 13.730  -20.585 26.557  1.00 49.33  ? 89  HIS   C ND1 1 
ATOM   2134 C CD2 . HIS   C 1 90 ? 13.011  -18.720 25.726  1.00 47.35  ? 89  HIS   C CD2 1 
ATOM   2135 C CE1 . HIS   C 1 90 ? 14.805  -19.881 26.215  1.00 49.25  ? 89  HIS   C CE1 1 
ATOM   2136 N NE2 . HIS   C 1 90 ? 14.390  -18.746 25.695  1.00 49.49  ? 89  HIS   C NE2 1 
ATOM   2137 N N   . ALA   C 1 91 ? 8.591   -22.303 24.835  1.00 64.57  ? 90  ALA   C N   1 
ATOM   2138 C CA  . ALA   C 1 91 ? 7.286   -22.917 25.047  1.00 61.84  ? 90  ALA   C CA  1 
ATOM   2139 C C   . ALA   C 1 91 ? 7.462   -24.315 25.645  1.00 70.65  ? 90  ALA   C C   1 
ATOM   2140 O O   . ALA   C 1 91 ? 8.567   -24.861 25.652  1.00 70.81  ? 90  ALA   C O   1 
ATOM   2141 C CB  . ALA   C 1 91 ? 6.473   -22.940 23.765  1.00 57.57  ? 90  ALA   C CB  1 
ATOM   2142 N N   . SER   C 1 92 ? 6.351   -24.898 26.114  1.00 78.69  ? 91  SER   C N   1 
ATOM   2143 C CA  . SER   C 1 92 ? 6.351   -26.084 26.962  1.00 80.73  ? 91  SER   C CA  1 
ATOM   2144 C C   . SER   C 1 92 ? 6.581   -27.357 26.149  1.00 79.33  ? 91  SER   C C   1 
ATOM   2145 O O   . SER   C 1 92 ? 7.330   -28.238 26.569  1.00 78.72  ? 91  SER   C O   1 
ATOM   2146 C CB  . SER   C 1 92 ? 5.052   -26.194 27.723  1.00 77.75  ? 91  SER   C CB  1 
ATOM   2147 O OG  . SER   C 1 92 ? 4.630   -24.926 28.200  1.00 83.51  ? 91  SER   C OG  1 
ATOM   2148 N N   . TYR   C 1 93 ? 5.871   -27.461 25.019  1.00 83.10  ? 92  TYR   C N   1 
ATOM   2149 C CA  . TYR   C 1 93 ? 5.851   -28.657 24.190  1.00 87.70  ? 92  TYR   C CA  1 
ATOM   2150 C C   . TYR   C 1 93 ? 5.523   -29.874 25.071  1.00 90.46  ? 92  TYR   C C   1 
ATOM   2151 O O   . TYR   C 1 93 ? 5.693   -31.018 24.600  1.00 102.68 ? 92  TYR   C O   1 
ATOM   2152 C CB  . TYR   C 1 93 ? 7.157   -28.755 23.390  1.00 86.55  ? 92  TYR   C CB  1 
ATOM   2153 C CG  . TYR   C 1 93 ? 7.470   -27.526 22.540  1.00 77.85  ? 92  TYR   C CG  1 
ATOM   2154 C CD1 . TYR   C 1 93 ? 6.758   -27.263 21.370  1.00 71.37  ? 92  TYR   C CD1 1 
ATOM   2155 C CD2 . TYR   C 1 93 ? 8.479   -26.633 22.900  1.00 70.58  ? 92  TYR   C CD2 1 
ATOM   2156 C CE1 . TYR   C 1 93 ? 7.026   -26.147 20.593  1.00 69.25  ? 92  TYR   C CE1 1 
ATOM   2157 C CE2 . TYR   C 1 93 ? 8.764   -25.519 22.122  1.00 63.88  ? 92  TYR   C CE2 1 
ATOM   2158 C CZ  . TYR   C 1 93 ? 8.036   -25.277 20.968  1.00 67.97  ? 92  TYR   C CZ  1 
ATOM   2159 O OH  . TYR   C 1 93 ? 8.299   -24.177 20.202  1.00 72.89  ? 92  TYR   C OH  1 
HETATM 2160 S S   . SO4   D 2 .  ? 1.402   -33.797 1.843   1.00 107.74 ? 101 SO4   A S   1 
HETATM 2161 O O1  . SO4   D 2 .  ? 2.351   -34.313 0.888   1.00 86.62  ? 101 SO4   A O1  1 
HETATM 2162 O O2  . SO4   D 2 .  ? 1.531   -32.363 1.934   1.00 86.44  ? 101 SO4   A O2  1 
HETATM 2163 O O3  . SO4   D 2 .  ? 0.063   -34.145 1.425   1.00 115.96 ? 101 SO4   A O3  1 
HETATM 2164 O O4  . SO4   D 2 .  ? 1.663   -34.379 3.131   1.00 109.13 ? 101 SO4   A O4  1 
HETATM 2165 S S   . SO4   E 2 .  ? -9.413  -24.633 1.281   1.00 98.91  ? 102 SO4   A S   1 
HETATM 2166 O O1  . SO4   E 2 .  ? -9.088  -24.100 -0.016  1.00 98.52  ? 102 SO4   A O1  1 
HETATM 2167 O O2  . SO4   E 2 .  ? -9.113  -23.654 2.295   1.00 90.05  ? 102 SO4   A O2  1 
HETATM 2168 O O3  . SO4   E 2 .  ? -10.814 -24.957 1.319   1.00 116.73 ? 102 SO4   A O3  1 
HETATM 2169 O O4  . SO4   E 2 .  ? -8.644  -25.826 1.525   1.00 96.98  ? 102 SO4   A O4  1 
HETATM 2170 C C1  . EDO   F 3 .  ? 14.192  -19.540 -7.442  1.00 39.07  ? 103 EDO   A C1  1 
HETATM 2171 O O1  . EDO   F 3 .  ? 15.416  -18.797 -7.262  1.00 34.09  ? 103 EDO   A O1  1 
HETATM 2172 C C2  . EDO   F 3 .  ? 13.302  -18.966 -8.498  1.00 39.02  ? 103 EDO   A C2  1 
HETATM 2173 O O2  . EDO   F 3 .  ? 12.843  -17.658 -8.222  1.00 35.97  ? 103 EDO   A O2  1 
HETATM 2174 S S   . SO4   G 2 .  ? 9.195   -29.465 5.784   1.00 64.01  ? 104 SO4   A S   1 
HETATM 2175 O O1  . SO4   G 2 .  ? 9.822   -28.546 4.893   1.00 62.57  ? 104 SO4   A O1  1 
HETATM 2176 O O2  . SO4   G 2 .  ? 8.784   -30.645 5.055   1.00 67.35  ? 104 SO4   A O2  1 
HETATM 2177 O O3  . SO4   G 2 .  ? 10.122  -29.838 6.823   1.00 66.86  ? 104 SO4   A O3  1 
HETATM 2178 O O4  . SO4   G 2 .  ? 8.023   -28.850 6.355   1.00 77.31  ? 104 SO4   A O4  1 
HETATM 2179 S S   . SO4   H 2 .  ? 7.356   -8.445  -25.087 1.00 75.49  ? 101 SO4   B S   1 
HETATM 2180 O O1  . SO4   H 2 .  ? 8.492   -8.506  -25.962 1.00 48.21  ? 101 SO4   B O1  1 
HETATM 2181 O O2  . SO4   H 2 .  ? 6.215   -9.083  -25.702 1.00 50.63  ? 101 SO4   B O2  1 
HETATM 2182 O O3  . SO4   H 2 .  ? 7.609   -9.145  -23.835 1.00 49.51  ? 101 SO4   B O3  1 
HETATM 2183 O O4  . SO4   H 2 .  ? 7.116   -7.035  -24.847 1.00 61.10  ? 101 SO4   B O4  1 
HETATM 2184 S S   . SO4   I 2 .  ? 14.548  -26.881 -26.555 1.00 58.41  ? 102 SO4   B S   1 
HETATM 2185 O O1  . SO4   I 2 .  ? 15.778  -26.391 -25.986 1.00 64.91  ? 102 SO4   B O1  1 
HETATM 2186 O O2  . SO4   I 2 .  ? 14.777  -28.173 -27.156 1.00 73.61  ? 102 SO4   B O2  1 
HETATM 2187 O O3  . SO4   I 2 .  ? 13.560  -27.010 -25.524 1.00 70.41  ? 102 SO4   B O3  1 
HETATM 2188 O O4  . SO4   I 2 .  ? 14.073  -25.959 -27.552 1.00 55.40  ? 102 SO4   B O4  1 
HETATM 2189 N N1  . A1H9U J 4 .  ? 18.140  -15.630 -24.069 0.76 40.42  ? 103 A1H9U B N1  1 
HETATM 2190 C C4  . A1H9U J 4 .  ? 18.847  -15.299 -22.883 0.76 41.55  ? 103 A1H9U B C4  1 
HETATM 2191 C C5  . A1H9U J 4 .  ? 18.171  -15.170 -21.659 0.76 39.48  ? 103 A1H9U B C5  1 
HETATM 2192 C C6  . A1H9U J 4 .  ? 18.872  -14.778 -20.525 0.76 43.05  ? 103 A1H9U B C6  1 
HETATM 2193 C C7  . A1H9U J 4 .  ? 20.233  -14.530 -20.600 0.76 42.12  ? 103 A1H9U B C7  1 
HETATM 2194 C C8  . A1H9U J 4 .  ? 20.923  -14.654 -21.818 0.76 45.12  ? 103 A1H9U B C8  1 
HETATM 2195 C C10 . A1H9U J 4 .  ? 20.940  -15.159 -24.313 0.76 37.01  ? 103 A1H9U B C10 1 
HETATM 2196 C C1  . A1H9U J 4 .  ? 17.126  -16.545 -26.445 0.76 25.91  ? 103 A1H9U B C1  1 
HETATM 2197 C C2  . A1H9U J 4 .  ? 16.652  -15.154 -25.891 0.76 31.17  ? 103 A1H9U B C2  1 
HETATM 2198 C C3  . A1H9U J 4 .  ? 17.523  -14.656 -24.773 0.76 34.28  ? 103 A1H9U B C3  1 
HETATM 2199 C C9  . A1H9U J 4 .  ? 20.228  -15.044 -22.988 0.76 39.11  ? 103 A1H9U B C9  1 
HETATM 2200 N N2  . A1H9U J 4 .  ? 22.289  -14.383 -21.907 0.76 44.34  ? 103 A1H9U B N2  1 
HETATM 2201 O O1  . A1H9U J 4 .  ? 17.662  -13.472 -24.518 0.76 33.64  ? 103 A1H9U B O1  1 
HETATM 2202 C C1  . EDO   K 3 .  ? 16.870  -36.225 16.374  1.00 48.44  ? 101 EDO   C C1  1 
HETATM 2203 O O1  . EDO   K 3 .  ? 15.781  -37.027 15.939  1.00 51.25  ? 101 EDO   C O1  1 
HETATM 2204 C C2  . EDO   K 3 .  ? 16.573  -35.446 17.603  1.00 44.85  ? 101 EDO   C C2  1 
HETATM 2205 O O2  . EDO   K 3 .  ? 15.439  -35.885 18.309  1.00 37.94  ? 101 EDO   C O2  1 
HETATM 2206 S S   . SO4   L 2 .  ? 29.403  -38.517 12.427  1.00 99.93  ? 102 SO4   C S   1 
HETATM 2207 O O1  . SO4   L 2 .  ? 30.519  -37.624 12.224  1.00 104.68 ? 102 SO4   C O1  1 
HETATM 2208 O O2  . SO4   L 2 .  ? 28.308  -38.112 11.591  1.00 87.40  ? 102 SO4   C O2  1 
HETATM 2209 O O3  . SO4   L 2 .  ? 29.778  -39.865 12.088  1.00 79.23  ? 102 SO4   C O3  1 
HETATM 2210 O O4  . SO4   L 2 .  ? 29.003  -38.469 13.807  1.00 107.33 ? 102 SO4   C O4  1 
HETATM 2211 O O   . HOH   M 5 .  ? 9.179   -32.496 3.961   1.00 53.59  ? 201 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? 5.427   -29.136 6.772   1.00 59.08  ? 202 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? 15.667  -16.753 -19.205 1.00 42.97  ? 203 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? 0.625   -10.761 -15.338 1.00 49.85  ? 204 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? 4.149   -10.399 13.696  1.00 61.51  ? 205 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? -5.523  -13.288 -16.666 1.00 52.49  ? 206 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? 3.797   -34.679 4.085   1.00 67.39  ? 207 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? -1.988  -30.941 -3.737  1.00 55.74  ? 208 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 10.889  -9.589  -13.433 1.00 69.21  ? 209 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? -3.493  -10.773 6.648   1.00 44.64  ? 210 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 7.150   -10.571 -12.024 1.00 42.84  ? 211 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 14.012  -15.750 -9.341  1.00 36.28  ? 212 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? -7.156  -20.830 -3.799  1.00 64.82  ? 213 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 0.309   -33.617 5.131   1.00 55.87  ? 214 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 4.738   -7.963  0.980   1.00 37.24  ? 215 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? -2.075  3.093   -1.954  1.00 45.08  ? 216 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 13.216  -11.986 7.791   1.00 69.62  ? 217 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 1.518   -24.701 13.822  1.00 66.68  ? 218 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? -7.642  -15.765 -1.133  1.00 35.77  ? 219 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? 8.297   -17.835 -16.059 1.00 62.51  ? 220 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? 4.680   -3.592  -3.307  1.00 35.79  ? 221 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 10.000  -18.959 9.874   1.00 68.75  ? 222 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 9.290   -18.031 -11.059 1.00 35.18  ? 223 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 9.541   -22.783 -9.559  1.00 44.36  ? 224 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? -4.074  -21.145 6.107   1.00 44.51  ? 225 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? -8.298  -21.134 -1.218  1.00 46.19  ? 226 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 10.210  -13.389 9.679   1.00 50.55  ? 227 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 11.589  -12.063 5.829   1.00 40.27  ? 228 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 10.954  -5.189  -7.835  1.00 38.17  ? 229 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 9.747   -6.049  -1.580  1.00 41.62  ? 230 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? -0.437  -29.438 9.842   1.00 64.29  ? 231 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 3.431   -29.589 -0.435  1.00 48.77  ? 232 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 2.160   -4.708  -10.167 1.00 42.60  ? 233 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 1.949   0.542   -7.398  1.00 46.92  ? 234 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 16.289  -24.548 1.724   1.00 45.28  ? 235 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? 11.020  -29.668 2.754   1.00 47.91  ? 236 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? -0.482  -20.923 6.906   1.00 36.37  ? 237 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? -7.673  -17.061 6.744   1.00 41.36  ? 238 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? 11.625  -12.328 -6.194  1.00 29.51  ? 239 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 11.258  -23.677 9.827   1.00 40.75  ? 240 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 20.115  -15.457 7.294   1.00 32.79  ? 241 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 11.728  -16.284 -15.069 1.00 45.53  ? 242 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? 14.612  -29.428 3.834   1.00 45.00  ? 243 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 13.202  -9.427  -7.326  1.00 49.85  ? 244 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 17.434  -12.918 1.422   1.00 21.28  ? 245 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 0.505   -23.530 9.314   1.00 50.95  ? 246 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 13.531  -11.972 -4.158  1.00 22.47  ? 247 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 12.687  -13.258 -8.906  1.00 48.98  ? 248 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 1.253   -17.983 -18.733 1.00 52.73  ? 249 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? 2.599   -25.138 -10.085 1.00 45.85  ? 250 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 9.843   -30.564 9.476   1.00 40.31  ? 251 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 2.749   -6.504  5.397   1.00 38.14  ? 252 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -5.569  -19.702 -5.650  1.00 44.71  ? 253 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? 15.948  -11.950 -5.256  1.00 35.00  ? 254 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 9.546   -20.026 -18.591 1.00 47.30  ? 255 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? -1.520  -22.041 -0.704  1.00 31.62  ? 256 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? -5.490  -15.884 -8.103  1.00 30.51  ? 257 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 13.675  -28.227 -4.726  1.00 73.56  ? 258 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? -1.053  -7.422  11.327  1.00 47.09  ? 259 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? -7.817  -16.667 1.974   1.00 50.86  ? 260 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 16.740  -11.959 -17.217 1.00 44.42  ? 261 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? 11.522  -5.751  -4.064  1.00 49.75  ? 262 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? 8.174   -7.807  1.203   1.00 33.18  ? 263 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -6.028  -11.275 -11.291 1.00 45.16  ? 264 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? 1.932   -10.520 11.631  1.00 40.05  ? 265 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? 5.352   -7.591  4.070   1.00 40.17  ? 266 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? 8.813   -16.205 -13.256 1.00 39.85  ? 267 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 2.217   -24.977 -6.504  1.00 63.89  ? 268 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 6.814   -6.113  0.451   1.00 57.19  ? 269 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? 8.203   -17.502 8.576   1.00 48.16  ? 270 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? -6.761  -21.781 -6.138  1.00 70.09  ? 271 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? -6.116  -12.708 6.577   1.00 42.17  ? 272 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 6.470   -16.270 -14.937 1.00 55.56  ? 273 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? -1.369  -11.839 11.207  1.00 41.37  ? 274 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? -8.307  -19.268 -3.442  1.00 48.04  ? 275 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 3.593   -5.828  -0.981  1.00 55.84  ? 276 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? -4.132  -25.885 -5.774  1.00 50.01  ? 277 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? -6.985  -11.456 -7.988  1.00 32.24  ? 278 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 21.559  -16.681 -3.461  1.00 31.50  ? 279 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 22.531  -16.695 -0.398  1.00 44.71  ? 280 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? 0.799   -8.424  -12.978 1.00 61.43  ? 281 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? 11.255  -7.811  0.424   1.00 29.70  ? 282 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? 17.303  -18.166 -9.764  1.00 47.30  ? 283 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? -10.999 -16.063 -3.930  1.00 54.48  ? 284 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 15.429  -28.299 -0.961  1.00 57.52  ? 285 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? 8.299   -8.295  4.527   1.00 44.78  ? 286 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? -3.605  -7.686  10.596  1.00 51.92  ? 287 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? 10.717  -27.768 -7.300  1.00 58.73  ? 288 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 13.082  -15.141 -11.820 1.00 63.23  ? 289 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 15.169  -13.415 10.636  1.00 52.01  ? 290 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? -0.303  -20.878 10.961  1.00 61.45  ? 291 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? -6.026  -26.700 3.261   1.00 60.15  ? 292 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 8.840   -9.194  -13.853 1.00 40.95  ? 293 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 17.468  -13.854 10.678  1.00 49.28  ? 294 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? 0.802   -29.339 -7.202  1.00 61.73  ? 295 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? -3.933  -26.424 7.655   1.00 63.68  ? 296 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? -3.592  -10.825 9.642   1.00 54.08  ? 297 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? 10.001  -3.015  -0.150  1.00 73.45  ? 298 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? -5.654  -23.443 -7.018  1.00 46.77  ? 299 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? 11.777  -21.100 10.628  1.00 47.69  ? 300 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? -0.340  -3.270  -10.898 1.00 56.40  ? 301 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? -10.272 -27.875 -1.718  1.00 58.07  ? 302 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? -7.141  -14.076 -9.258  1.00 42.03  ? 303 HOH   A O   1 
HETATM 2314 O O   . HOH   M 5 .  ? 11.585  -2.011  -1.900  1.00 49.05  ? 304 HOH   A O   1 
HETATM 2315 O O   . HOH   M 5 .  ? -5.965  -22.747 5.832   1.00 59.42  ? 305 HOH   A O   1 
HETATM 2316 O O   . HOH   M 5 .  ? -8.672  -18.829 5.857   1.00 60.47  ? 306 HOH   A O   1 
HETATM 2317 O O   . HOH   M 5 .  ? 4.857   -9.709  -11.211 1.00 56.12  ? 307 HOH   A O   1 
HETATM 2318 O O   . HOH   M 5 .  ? 10.505  -11.533 10.224  1.00 50.93  ? 308 HOH   A O   1 
HETATM 2319 O O   . HOH   M 5 .  ? -11.041 -13.459 -3.095  1.00 44.78  ? 309 HOH   A O   1 
HETATM 2320 O O   . HOH   M 5 .  ? 7.473   -30.610 -2.402  1.00 61.89  ? 310 HOH   A O   1 
HETATM 2321 O O   . HOH   M 5 .  ? 8.459   -22.257 -19.548 1.00 64.69  ? 311 HOH   A O   1 
HETATM 2322 O O   . HOH   M 5 .  ? -6.974  -19.203 8.493   1.00 54.78  ? 312 HOH   A O   1 
HETATM 2323 O O   . HOH   M 5 .  ? -4.573  -21.163 -8.530  1.00 65.35  ? 313 HOH   A O   1 
HETATM 2324 O O   . HOH   M 5 .  ? -12.650 -28.556 -1.880  1.00 72.15  ? 314 HOH   A O   1 
HETATM 2325 O O   . HOH   M 5 .  ? 4.647   -3.216  2.140   1.00 74.39  ? 315 HOH   A O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 30.695  -8.114  -30.212 1.00 53.79  ? 201 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 6.642   -12.330 -26.286 1.00 45.53  ? 202 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 20.288  -22.047 -23.436 1.00 56.25  ? 203 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 18.825  -0.194  -25.498 1.00 62.35  ? 204 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 6.166   -7.505  -32.232 1.00 55.61  ? 205 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 27.718  -8.133  -29.080 1.00 44.35  ? 206 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 30.247  -19.681 -40.442 1.00 37.13  ? 207 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 10.012  -11.390 -38.254 1.00 62.46  ? 208 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 25.008  -5.034  -29.952 1.00 44.52  ? 209 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 10.317  -19.579 -43.110 1.00 58.43  ? 210 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 25.677  -4.429  -33.845 1.00 55.04  ? 211 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 26.104  -23.144 -31.337 1.00 44.53  ? 212 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 34.490  -23.081 -30.021 1.00 65.77  ? 213 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 23.705  -10.922 -22.123 1.00 41.73  ? 214 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 7.443   -8.164  -21.374 1.00 53.82  ? 215 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 17.624  -19.361 -42.279 1.00 66.72  ? 216 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 30.402  -12.650 -46.092 1.00 73.69  ? 217 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 25.421  -5.981  -35.934 1.00 49.17  ? 218 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 32.582  -18.638 -42.504 1.00 55.23  ? 219 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 32.343  -11.911 -41.828 1.00 50.56  ? 220 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 24.378  -1.724  -36.699 1.00 59.99  ? 221 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 27.606  -17.512 -25.134 1.00 50.29  ? 222 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 31.616  -12.378 -38.918 1.00 60.08  ? 223 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 7.358   -12.519 -38.901 1.00 62.08  ? 224 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 10.468  -18.775 -33.131 1.00 31.19  ? 225 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 10.386  -17.056 -44.234 1.00 59.03  ? 226 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 13.031  -4.636  -41.974 1.00 55.08  ? 227 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 16.733  -19.171 -29.009 1.00 26.81  ? 228 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 20.714  -13.245 -42.912 1.00 44.31  ? 229 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 18.138  -0.405  -38.592 1.00 32.12  ? 230 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 22.121  3.722   -32.744 1.00 58.26  ? 231 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 7.077   -19.183 -35.177 1.00 51.42  ? 232 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 13.171  -22.341 -20.754 1.00 65.91  ? 233 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 3.325   -8.567  -27.208 1.00 58.34  ? 234 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 8.389   -27.737 -38.464 1.00 60.55  ? 235 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 22.703  -23.284 -29.003 1.00 47.10  ? 236 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 23.741  -4.174  -37.008 1.00 32.51  ? 237 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 28.189  -17.571 -46.257 1.00 64.98  ? 238 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 23.473  -5.864  -24.606 1.00 58.79  ? 239 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 8.792   -8.646  -16.649 1.00 49.13  ? 240 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 20.157  -2.497  -23.143 1.00 64.37  ? 241 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 27.178  -10.447 -28.998 1.00 56.21  ? 242 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 14.306  -6.297  -41.358 1.00 44.50  ? 243 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 23.743  -2.283  -29.326 1.00 48.19  ? 244 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 10.596  -21.797 -32.811 1.00 38.76  ? 245 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 19.753  -25.674 -34.336 1.00 41.30  ? 246 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 7.419   -18.380 -31.779 1.00 47.90  ? 247 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 20.527  -10.244 -43.118 1.00 40.88  ? 248 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 26.038  -12.354 -22.315 1.00 59.48  ? 249 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 21.131  -26.522 -30.189 1.00 64.50  ? 250 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 6.644   -20.663 -24.955 1.00 45.61  ? 251 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 14.552  -24.536 -40.538 1.00 45.55  ? 252 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 31.985  -21.298 -38.247 1.00 47.51  ? 253 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 7.810   -23.189 -24.247 1.00 63.99  ? 254 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 21.262  -6.388  -42.748 1.00 43.26  ? 255 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 5.058   -19.257 -25.854 1.00 53.94  ? 256 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 26.329  -0.317  -29.443 1.00 52.90  ? 257 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 18.026  -15.771 -45.960 1.00 52.81  ? 258 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 18.503  -25.734 -28.984 1.00 47.14  ? 259 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 1.701   -12.982 -28.675 1.00 55.41  ? 260 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 34.351  -17.127 -46.010 1.00 64.41  ? 261 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 18.430  4.516   -34.523 1.00 42.42  ? 262 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 17.006  -9.487  -43.897 1.00 45.99  ? 263 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 13.463  -12.548 -47.684 1.00 64.97  ? 264 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 17.894  -3.587  -22.055 1.00 62.98  ? 265 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 38.891  -13.066 -39.840 1.00 70.90  ? 266 HOH   B O   1 
HETATM 2392 O O   . HOH   N 5 .  ? 24.854  -6.458  -42.747 1.00 49.64  ? 267 HOH   B O   1 
HETATM 2393 O O   . HOH   N 5 .  ? 28.269  -12.962 -24.478 1.00 55.03  ? 268 HOH   B O   1 
HETATM 2394 O O   . HOH   N 5 .  ? 27.907  -24.818 -35.110 1.00 44.33  ? 269 HOH   B O   1 
HETATM 2395 O O   . HOH   N 5 .  ? 9.270   -5.291  -40.747 1.00 85.51  ? 270 HOH   B O   1 
HETATM 2396 O O   . HOH   N 5 .  ? 25.009  -8.333  -22.514 1.00 58.86  ? 271 HOH   B O   1 
HETATM 2397 O O   . HOH   N 5 .  ? 20.466  3.989   -33.244 1.00 38.83  ? 272 HOH   B O   1 
HETATM 2398 O O   . HOH   N 5 .  ? 16.265  -26.051 -21.548 1.00 86.47  ? 273 HOH   B O   1 
HETATM 2399 O O   . HOH   N 5 .  ? 10.890  -2.599  -28.409 1.00 66.59  ? 274 HOH   B O   1 
HETATM 2400 O O   . HOH   N 5 .  ? 20.188  -7.306  -20.930 1.00 59.95  ? 275 HOH   B O   1 
HETATM 2401 O O   . HOH   N 5 .  ? 15.162  -7.971  -43.020 1.00 48.81  ? 276 HOH   B O   1 
HETATM 2402 O O   . HOH   N 5 .  ? 16.749  -0.572  -25.489 1.00 58.16  ? 277 HOH   B O   1 
HETATM 2403 O O   . HOH   N 5 .  ? 13.048  -19.860 -19.704 1.00 49.50  ? 278 HOH   B O   1 
HETATM 2404 O O   . HOH   N 5 .  ? 27.817  -24.879 -32.445 1.00 46.56  ? 279 HOH   B O   1 
HETATM 2405 O O   . HOH   N 5 .  ? 16.617  2.084   -30.629 1.00 63.15  ? 280 HOH   B O   1 
HETATM 2406 O O   . HOH   N 5 .  ? 11.525  -23.893 -30.187 1.00 51.51  ? 281 HOH   B O   1 
HETATM 2407 O O   . HOH   N 5 .  ? 24.473  -4.432  -28.007 1.00 64.92  ? 282 HOH   B O   1 
HETATM 2408 O O   . HOH   N 5 .  ? 15.295  -21.623 -42.119 1.00 56.05  ? 283 HOH   B O   1 
HETATM 2409 O O   . HOH   N 5 .  ? 7.481   -9.843  -18.709 1.00 46.60  ? 284 HOH   B O   1 
HETATM 2410 O O   . HOH   N 5 .  ? 19.151  -8.355  -43.790 1.00 47.51  ? 285 HOH   B O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 26.873  -37.905 10.214  1.00 45.00  ? 201 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 29.991  -27.339 30.220  1.00 66.73  ? 202 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 13.573  -20.086 11.176  1.00 64.56  ? 203 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 19.996  -20.052 29.886  1.00 58.79  ? 204 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 26.700  -39.168 12.760  1.00 45.98  ? 205 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 13.960  -22.517 27.815  1.00 81.36  ? 206 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 16.269  -17.488 25.112  1.00 68.94  ? 207 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 15.824  -41.241 15.163  1.00 55.96  ? 208 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 9.453   -30.116 11.157  1.00 64.11  ? 209 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 15.036  -39.170 16.870  1.00 62.38  ? 210 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 7.951   -31.675 12.234  1.00 55.95  ? 211 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 19.501  -20.177 10.586  1.00 47.65  ? 212 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 12.253  -28.242 28.118  1.00 61.96  ? 213 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 9.105   -19.021 23.440  1.00 50.53  ? 214 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 5.928   -26.572 16.781  1.00 51.45  ? 215 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 13.014  -31.580 8.042   1.00 37.32  ? 216 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 23.136  -41.500 18.418  1.00 46.01  ? 217 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 28.109  -37.310 15.980  1.00 52.21  ? 218 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 28.421  -15.174 12.956  1.00 65.30  ? 219 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 20.203  -41.808 12.168  1.00 32.54  ? 220 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 17.595  -17.194 15.277  1.00 51.80  ? 221 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 15.381  -21.255 12.445  1.00 43.92  ? 222 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 31.752  -33.410 25.854  1.00 46.17  ? 223 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 33.572  -24.644 31.351  1.00 49.48  ? 224 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 25.734  -33.845 34.803  1.00 58.79  ? 225 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 15.804  -17.711 19.344  1.00 49.24  ? 226 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 25.821  -19.643 6.391   1.00 42.43  ? 227 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 7.122   -18.150 10.746  1.00 41.78  ? 228 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 21.325  -19.660 24.512  1.00 57.84  ? 229 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 14.233  -37.235 13.465  1.00 48.77  ? 230 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 30.931  -34.443 35.667  1.00 52.37  ? 231 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 30.811  -29.071 12.278  1.00 57.63  ? 232 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 30.517  -31.343 15.805  1.00 57.56  ? 233 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 25.611  -31.420 10.747  1.00 40.08  ? 234 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 23.766  -20.971 24.053  1.00 51.15  ? 235 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 20.856  -39.884 26.544  1.00 37.60  ? 236 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 9.564   -37.336 18.143  1.00 62.23  ? 237 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 19.557  -26.685 3.402   1.00 52.40  ? 238 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 22.396  -28.567 11.189  1.00 40.06  ? 239 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 19.428  -41.286 39.000  1.00 69.25  ? 240 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 22.273  -34.397 16.547  1.00 29.36  ? 241 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 30.405  -35.718 28.837  1.00 52.71  ? 242 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 29.849  -39.862 31.476  1.00 42.58  ? 243 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 26.051  -17.653 13.922  1.00 50.28  ? 244 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 21.083  -28.689 8.475   1.00 39.04  ? 245 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 20.099  -13.417 13.583  1.00 50.03  ? 246 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 25.732  -39.666 20.220  1.00 39.18  ? 247 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 31.485  -43.541 15.877  1.00 54.02  ? 248 HOH   C O   1 
HETATM 2459 O O   . HOH   O 5 .  ? 16.524  -37.522 20.448  1.00 55.27  ? 249 HOH   C O   1 
HETATM 2460 O O   . HOH   O 5 .  ? 14.211  -38.692 9.087   1.00 58.02  ? 250 HOH   C O   1 
HETATM 2461 O O   . HOH   O 5 .  ? 27.916  -37.717 25.135  1.00 58.86  ? 251 HOH   C O   1 
HETATM 2462 O O   . HOH   O 5 .  ? 31.262  -39.945 27.228  1.00 43.93  ? 252 HOH   C O   1 
HETATM 2463 O O   . HOH   O 5 .  ? 23.219  -18.614 21.941  1.00 63.09  ? 253 HOH   C O   1 
HETATM 2464 O O   . HOH   O 5 .  ? 2.736   -28.254 14.330  1.00 61.37  ? 254 HOH   C O   1 
HETATM 2465 O O   . HOH   O 5 .  ? 30.482  -17.384 9.798   1.00 48.52  ? 255 HOH   C O   1 
HETATM 2466 O O   . HOH   O 5 .  ? 21.130  -29.661 4.792   1.00 59.98  ? 256 HOH   C O   1 
HETATM 2467 O O   . HOH   O 5 .  ? 25.568  -17.771 21.289  1.00 65.14  ? 257 HOH   C O   1 
HETATM 2468 O O   . HOH   O 5 .  ? 16.327  -33.580 28.833  1.00 58.09  ? 258 HOH   C O   1 
HETATM 2469 O O   . HOH   O 5 .  ? 31.778  -43.512 12.043  1.00 52.84  ? 259 HOH   C O   1 
HETATM 2470 O O   . HOH   O 5 .  ? 29.833  -25.481 32.417  1.00 57.05  ? 260 HOH   C O   1 
HETATM 2471 O O   . HOH   O 5 .  ? 30.425  -32.766 18.326  1.00 50.62  ? 261 HOH   C O   1 
HETATM 2472 O O   . HOH   O 5 .  ? 17.063  -38.069 28.664  1.00 61.81  ? 262 HOH   C O   1 
HETATM 2473 O O   . HOH   O 5 .  ? 4.877   -23.642 18.526  1.00 63.12  ? 263 HOH   C O   1 
HETATM 2474 O O   . HOH   O 5 .  ? 22.608  -14.341 13.519  1.00 59.11  ? 264 HOH   C O   1 
HETATM 2475 O O   . HOH   O 5 .  ? 25.364  -36.304 10.175  1.00 51.81  ? 265 HOH   C O   1 
HETATM 2476 O O   . HOH   O 5 .  ? 29.026  -18.061 28.853  1.00 59.44  ? 266 HOH   C O   1 
HETATM 2477 O O   . HOH   O 5 .  ? 24.058  -15.932 11.975  1.00 51.59  ? 267 HOH   C O   1 
HETATM 2478 O O   . HOH   O 5 .  ? 29.094  -41.627 27.400  1.00 42.00  ? 268 HOH   C O   1 
HETATM 2479 O O   . HOH   O 5 .  ? 25.942  -13.941 11.156  1.00 47.14  ? 269 HOH   C O   1 
HETATM 2480 O O   . HOH   O 5 .  ? 36.806  -23.931 27.754  1.00 76.70  ? 270 HOH   C O   1 
HETATM 2481 O O   . HOH   O 5 .  ? 15.291  -34.360 35.381  1.00 67.40  ? 271 HOH   C O   1 
HETATM 2482 O O   . HOH   O 5 .  ? 28.474  -41.680 29.730  1.00 45.25  ? 272 HOH   C O   1 
HETATM 2483 O O   . HOH   O 5 .  ? 11.006  -31.880 32.044  1.00 60.54  ? 273 HOH   C O   1 
HETATM 2484 O O   . HOH   O 5 .  ? 33.680  -44.547 15.446  1.00 42.73  ? 274 HOH   C O   1 
HETATM 2485 O O   . HOH   O 5 .  ? 7.812   -38.244 4.852   1.00 62.71  ? 275 HOH   C O   1 
# 
