data_7HGH
# 
_entry.id   7HGH 
# 
_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   7HGH         pdb_00007hgh 10.2210/pdb7hgh/pdb 
WWPDB D_1001407443 ?            ?                   
# 
_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                        7HGH 
_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 '(2S)-N-(5-ethyl-1,3,4-thiadiazol-2-yl)oxolane-2-carboxamide' 227.283   1   ? ?    ? ? 
5 water       nat water                                                         18.015    261 ? ?    ? ? 
# 
_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 '(2S)-N-(5-ethyl-1,3,4-thiadiazol-2-yl)oxolane-2-carboxamide' A1A4A 
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 
A1A4A non-polymer         . '(2S)-N-(5-ethyl-1,3,4-thiadiazol-2-yl)oxolane-2-carboxamide' ?                 'C9 H13 N3 O2 S' 
227.283 
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 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   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 ?  ?   ?   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        A1A4A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A4A 
_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 A1A4A 1   103 101 A1A4A LIG B . 
K 3 EDO   1   101 101 EDO   EDO C . 
L 2 SO4   1   102 5   SO4   SO4 C . 
M 5 HOH   1   201 362 HOH   HOH A . 
M 5 HOH   2   202 337 HOH   HOH A . 
M 5 HOH   3   203 307 HOH   HOH A . 
M 5 HOH   4   204 202 HOH   HOH A . 
M 5 HOH   5   205 336 HOH   HOH A . 
M 5 HOH   6   206 91  HOH   HOH A . 
M 5 HOH   7   207 87  HOH   HOH A . 
M 5 HOH   8   208 304 HOH   HOH A . 
M 5 HOH   9   209 66  HOH   HOH A . 
M 5 HOH   10  210 14  HOH   HOH A . 
M 5 HOH   11  211 293 HOH   HOH A . 
M 5 HOH   12  212 35  HOH   HOH A . 
M 5 HOH   13  213 71  HOH   HOH A . 
M 5 HOH   14  214 55  HOH   HOH A . 
M 5 HOH   15  215 292 HOH   HOH A . 
M 5 HOH   16  216 338 HOH   HOH A . 
M 5 HOH   17  217 259 HOH   HOH A . 
M 5 HOH   18  218 23  HOH   HOH A . 
M 5 HOH   19  219 27  HOH   HOH A . 
M 5 HOH   20  220 77  HOH   HOH A . 
M 5 HOH   21  221 8   HOH   HOH A . 
M 5 HOH   22  222 41  HOH   HOH A . 
M 5 HOH   23  223 99  HOH   HOH A . 
M 5 HOH   24  224 208 HOH   HOH A . 
M 5 HOH   25  225 12  HOH   HOH A . 
M 5 HOH   26  226 301 HOH   HOH A . 
M 5 HOH   27  227 58  HOH   HOH A . 
M 5 HOH   28  228 32  HOH   HOH A . 
M 5 HOH   29  229 289 HOH   HOH A . 
M 5 HOH   30  230 278 HOH   HOH A . 
M 5 HOH   31  231 86  HOH   HOH A . 
M 5 HOH   32  232 351 HOH   HOH A . 
M 5 HOH   33  233 1   HOH   HOH A . 
M 5 HOH   34  234 28  HOH   HOH A . 
M 5 HOH   35  235 7   HOH   HOH A . 
M 5 HOH   36  236 26  HOH   HOH A . 
M 5 HOH   37  237 290 HOH   HOH A . 
M 5 HOH   38  238 2   HOH   HOH A . 
M 5 HOH   39  239 167 HOH   HOH A . 
M 5 HOH   40  240 334 HOH   HOH A . 
M 5 HOH   41  241 34  HOH   HOH A . 
M 5 HOH   42  242 37  HOH   HOH A . 
M 5 HOH   43  243 327 HOH   HOH A . 
M 5 HOH   44  244 111 HOH   HOH A . 
M 5 HOH   45  245 190 HOH   HOH A . 
M 5 HOH   46  246 64  HOH   HOH A . 
M 5 HOH   47  247 97  HOH   HOH A . 
M 5 HOH   48  248 38  HOH   HOH A . 
M 5 HOH   49  249 139 HOH   HOH A . 
M 5 HOH   50  250 18  HOH   HOH A . 
M 5 HOH   51  251 188 HOH   HOH A . 
M 5 HOH   52  252 352 HOH   HOH A . 
M 5 HOH   53  253 267 HOH   HOH A . 
M 5 HOH   54  254 93  HOH   HOH A . 
M 5 HOH   55  255 22  HOH   HOH A . 
M 5 HOH   56  256 78  HOH   HOH A . 
M 5 HOH   57  257 165 HOH   HOH A . 
M 5 HOH   58  258 20  HOH   HOH A . 
M 5 HOH   59  259 60  HOH   HOH A . 
M 5 HOH   60  260 222 HOH   HOH A . 
M 5 HOH   61  261 42  HOH   HOH A . 
M 5 HOH   62  262 203 HOH   HOH A . 
M 5 HOH   63  263 300 HOH   HOH A . 
M 5 HOH   64  264 164 HOH   HOH A . 
M 5 HOH   65  265 109 HOH   HOH A . 
M 5 HOH   66  266 288 HOH   HOH A . 
M 5 HOH   67  267 274 HOH   HOH A . 
M 5 HOH   68  268 95  HOH   HOH A . 
M 5 HOH   69  269 94  HOH   HOH A . 
M 5 HOH   70  270 199 HOH   HOH A . 
M 5 HOH   71  271 131 HOH   HOH A . 
M 5 HOH   72  272 218 HOH   HOH A . 
M 5 HOH   73  273 47  HOH   HOH A . 
M 5 HOH   74  274 297 HOH   HOH A . 
M 5 HOH   75  275 115 HOH   HOH A . 
M 5 HOH   76  276 143 HOH   HOH A . 
M 5 HOH   77  277 260 HOH   HOH A . 
M 5 HOH   78  278 318 HOH   HOH A . 
M 5 HOH   79  279 113 HOH   HOH A . 
M 5 HOH   80  280 84  HOH   HOH A . 
M 5 HOH   81  281 19  HOH   HOH A . 
M 5 HOH   82  282 132 HOH   HOH A . 
M 5 HOH   83  283 21  HOH   HOH A . 
M 5 HOH   84  284 145 HOH   HOH A . 
M 5 HOH   85  285 299 HOH   HOH A . 
M 5 HOH   86  286 281 HOH   HOH A . 
M 5 HOH   87  287 9   HOH   HOH A . 
M 5 HOH   88  288 16  HOH   HOH A . 
M 5 HOH   89  289 151 HOH   HOH A . 
M 5 HOH   90  290 146 HOH   HOH A . 
M 5 HOH   91  291 179 HOH   HOH A . 
M 5 HOH   92  292 211 HOH   HOH A . 
M 5 HOH   93  293 296 HOH   HOH A . 
M 5 HOH   94  294 116 HOH   HOH A . 
M 5 HOH   95  295 31  HOH   HOH A . 
M 5 HOH   96  296 219 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  299 156 HOH   HOH A . 
M 5 HOH   100 300 343 HOH   HOH A . 
M 5 HOH   101 301 345 HOH   HOH A . 
M 5 HOH   102 302 270 HOH   HOH A . 
M 5 HOH   103 303 283 HOH   HOH A . 
M 5 HOH   104 304 83  HOH   HOH A . 
M 5 HOH   105 305 185 HOH   HOH A . 
M 5 HOH   106 306 73  HOH   HOH A . 
M 5 HOH   107 307 108 HOH   HOH A . 
M 5 HOH   108 308 344 HOH   HOH A . 
M 5 HOH   109 309 75  HOH   HOH A . 
M 5 HOH   110 310 57  HOH   HOH A . 
M 5 HOH   111 311 205 HOH   HOH A . 
M 5 HOH   112 312 125 HOH   HOH A . 
M 5 HOH   113 313 363 HOH   HOH A . 
M 5 HOH   114 314 332 HOH   HOH A . 
N 5 HOH   1   201 355 HOH   HOH B . 
N 5 HOH   2   202 258 HOH   HOH B . 
N 5 HOH   3   203 157 HOH   HOH B . 
N 5 HOH   4   204 354 HOH   HOH B . 
N 5 HOH   5   205 349 HOH   HOH B . 
N 5 HOH   6   206 169 HOH   HOH B . 
N 5 HOH   7   207 89  HOH   HOH B . 
N 5 HOH   8   208 123 HOH   HOH B . 
N 5 HOH   9   209 17  HOH   HOH B . 
N 5 HOH   10  210 359 HOH   HOH B . 
N 5 HOH   11  211 46  HOH   HOH B . 
N 5 HOH   12  212 316 HOH   HOH B . 
N 5 HOH   13  213 5   HOH   HOH B . 
N 5 HOH   14  214 10  HOH   HOH B . 
N 5 HOH   15  215 98  HOH   HOH B . 
N 5 HOH   16  216 261 HOH   HOH B . 
N 5 HOH   17  217 119 HOH   HOH B . 
N 5 HOH   18  218 153 HOH   HOH B . 
N 5 HOH   19  219 329 HOH   HOH B . 
N 5 HOH   20  220 242 HOH   HOH B . 
N 5 HOH   21  221 247 HOH   HOH B . 
N 5 HOH   22  222 353 HOH   HOH B . 
N 5 HOH   23  223 137 HOH   HOH B . 
N 5 HOH   24  224 333 HOH   HOH B . 
N 5 HOH   25  225 6   HOH   HOH B . 
N 5 HOH   26  226 315 HOH   HOH B . 
N 5 HOH   27  227 364 HOH   HOH B . 
N 5 HOH   28  228 224 HOH   HOH B . 
N 5 HOH   29  229 68  HOH   HOH B . 
N 5 HOH   30  230 303 HOH   HOH B . 
N 5 HOH   31  231 96  HOH   HOH B . 
N 5 HOH   32  232 54  HOH   HOH B . 
N 5 HOH   33  233 279 HOH   HOH B . 
N 5 HOH   34  234 101 HOH   HOH B . 
N 5 HOH   35  235 320 HOH   HOH B . 
N 5 HOH   36  236 69  HOH   HOH B . 
N 5 HOH   37  237 217 HOH   HOH B . 
N 5 HOH   38  238 197 HOH   HOH B . 
N 5 HOH   39  239 172 HOH   HOH B . 
N 5 HOH   40  240 280 HOH   HOH B . 
N 5 HOH   41  241 76  HOH   HOH B . 
N 5 HOH   42  242 175 HOH   HOH B . 
N 5 HOH   43  243 36  HOH   HOH B . 
N 5 HOH   44  244 24  HOH   HOH B . 
N 5 HOH   45  245 150 HOH   HOH B . 
N 5 HOH   46  246 59  HOH   HOH B . 
N 5 HOH   47  247 120 HOH   HOH B . 
N 5 HOH   48  248 25  HOH   HOH B . 
N 5 HOH   49  249 13  HOH   HOH B . 
N 5 HOH   50  250 214 HOH   HOH B . 
N 5 HOH   51  251 163 HOH   HOH B . 
N 5 HOH   52  252 182 HOH   HOH B . 
N 5 HOH   53  253 160 HOH   HOH B . 
N 5 HOH   54  254 74  HOH   HOH B . 
N 5 HOH   55  255 61  HOH   HOH B . 
N 5 HOH   56  256 272 HOH   HOH B . 
N 5 HOH   57  257 72  HOH   HOH B . 
N 5 HOH   58  258 44  HOH   HOH B . 
N 5 HOH   59  259 348 HOH   HOH B . 
N 5 HOH   60  260 249 HOH   HOH B . 
N 5 HOH   61  261 79  HOH   HOH B . 
N 5 HOH   62  262 201 HOH   HOH B . 
N 5 HOH   63  263 291 HOH   HOH B . 
N 5 HOH   64  264 104 HOH   HOH B . 
N 5 HOH   65  265 170 HOH   HOH B . 
N 5 HOH   66  266 309 HOH   HOH B . 
N 5 HOH   67  267 347 HOH   HOH B . 
N 5 HOH   68  268 322 HOH   HOH B . 
N 5 HOH   69  269 177 HOH   HOH B . 
N 5 HOH   70  270 92  HOH   HOH B . 
N 5 HOH   71  271 103 HOH   HOH B . 
N 5 HOH   72  272 356 HOH   HOH B . 
N 5 HOH   73  273 335 HOH   HOH B . 
N 5 HOH   74  274 314 HOH   HOH B . 
N 5 HOH   75  275 365 HOH   HOH B . 
N 5 HOH   76  276 312 HOH   HOH B . 
N 5 HOH   77  277 107 HOH   HOH B . 
N 5 HOH   78  278 313 HOH   HOH B . 
N 5 HOH   79  279 223 HOH   HOH B . 
O 5 HOH   1   201 357 HOH   HOH C . 
O 5 HOH   2   202 340 HOH   HOH C . 
O 5 HOH   3   203 15  HOH   HOH C . 
O 5 HOH   4   204 90  HOH   HOH C . 
O 5 HOH   5   205 350 HOH   HOH C . 
O 5 HOH   6   206 161 HOH   HOH C . 
O 5 HOH   7   207 126 HOH   HOH C . 
O 5 HOH   8   208 269 HOH   HOH C . 
O 5 HOH   9   209 326 HOH   HOH C . 
O 5 HOH   10  210 317 HOH   HOH C . 
O 5 HOH   11  211 254 HOH   HOH C . 
O 5 HOH   12  212 49  HOH   HOH C . 
O 5 HOH   13  213 321 HOH   HOH C . 
O 5 HOH   14  214 325 HOH   HOH C . 
O 5 HOH   15  215 342 HOH   HOH C . 
O 5 HOH   16  216 310 HOH   HOH C . 
O 5 HOH   17  217 135 HOH   HOH C . 
O 5 HOH   18  218 56  HOH   HOH C . 
O 5 HOH   19  219 85  HOH   HOH C . 
O 5 HOH   20  220 148 HOH   HOH C . 
O 5 HOH   21  221 45  HOH   HOH C . 
O 5 HOH   22  222 82  HOH   HOH C . 
O 5 HOH   23  223 302 HOH   HOH C . 
O 5 HOH   24  224 271 HOH   HOH C . 
O 5 HOH   25  225 189 HOH   HOH C . 
O 5 HOH   26  226 67  HOH   HOH C . 
O 5 HOH   27  227 122 HOH   HOH C . 
O 5 HOH   28  228 142 HOH   HOH C . 
O 5 HOH   29  229 284 HOH   HOH C . 
O 5 HOH   30  230 275 HOH   HOH C . 
O 5 HOH   31  231 4   HOH   HOH C . 
O 5 HOH   32  232 184 HOH   HOH C . 
O 5 HOH   33  233 102 HOH   HOH C . 
O 5 HOH   34  234 134 HOH   HOH C . 
O 5 HOH   35  235 330 HOH   HOH C . 
O 5 HOH   36  236 173 HOH   HOH C . 
O 5 HOH   37  237 118 HOH   HOH C . 
O 5 HOH   38  238 53  HOH   HOH C . 
O 5 HOH   39  239 198 HOH   HOH C . 
O 5 HOH   40  240 130 HOH   HOH C . 
O 5 HOH   41  241 305 HOH   HOH C . 
O 5 HOH   42  242 341 HOH   HOH C . 
O 5 HOH   43  243 294 HOH   HOH C . 
O 5 HOH   44  244 226 HOH   HOH C . 
O 5 HOH   45  245 287 HOH   HOH C . 
O 5 HOH   46  246 48  HOH   HOH C . 
O 5 HOH   47  247 43  HOH   HOH C . 
O 5 HOH   48  248 171 HOH   HOH C . 
O 5 HOH   49  249 246 HOH   HOH C . 
O 5 HOH   50  250 149 HOH   HOH C . 
O 5 HOH   51  251 241 HOH   HOH C . 
O 5 HOH   52  252 62  HOH   HOH C . 
O 5 HOH   53  253 168 HOH   HOH C . 
O 5 HOH   54  254 40  HOH   HOH C . 
O 5 HOH   55  255 328 HOH   HOH C . 
O 5 HOH   56  256 70  HOH   HOH C . 
O 5 HOH   57  257 65  HOH   HOH C . 
O 5 HOH   58  258 298 HOH   HOH C . 
O 5 HOH   59  259 324 HOH   HOH C . 
O 5 HOH   60  260 339 HOH   HOH C . 
O 5 HOH   61  261 361 HOH   HOH C . 
O 5 HOH   62  262 319 HOH   HOH C . 
O 5 HOH   63  263 209 HOH   HOH C . 
O 5 HOH   64  264 360 HOH   HOH C . 
O 5 HOH   65  265 346 HOH   HOH C . 
O 5 HOH   66  266 63  HOH   HOH C . 
O 5 HOH   67  267 295 HOH   HOH C . 
O 5 HOH   68  268 206 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 56 ? CD  ? A LYS 57 CD  
2  1 Y 1 A LYS 56 ? CE  ? A LYS 57 CE  
3  1 Y 1 A LYS 56 ? NZ  ? A LYS 57 NZ  
4  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
5  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
6  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
7  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
8  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
9  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
10 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
11 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
12 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
13 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
14 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
15 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
16 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
17 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
18 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
19 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
20 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
21 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
22 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
23 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
24 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
25 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
26 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
27 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
28 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
29 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
30 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
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 LYS 56 ? CG  ? C LYS 57 CG  
34 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
35 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
36 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
37 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
38 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
39 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
40 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
41 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
42 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
43 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
44 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
45 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
46 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
47 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           7HGH 
_cell.length_a           41.240 
_cell.length_b           41.930 
_cell.length_c           158.170 
_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                         7HGH 
_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          7HGH 
_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                     7HGH 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             52.72 
_reflns.d_resolution_high            1.74 
_reflns.number_obs                   26998 
_reflns.percent_possible_obs         92.9 
_reflns.pdbx_Rmerge_I_obs            0.061 
_reflns.pdbx_netI_over_sigmaI        12.3 
_reflns.pdbx_redundancy              5.0 
_reflns.pdbx_Rrim_I_all              0.067 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     136004 
_reflns.pdbx_chi_squared             0.97 
_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                  1.74 
_reflns_shell.d_res_low                   1.79 
_reflns_shell.number_measured_all         7861 
_reflns_shell.number_unique_obs           1789 
_reflns_shell.Rmerge_I_obs                1.467 
_reflns_shell.pdbx_chi_squared            0.67 
_reflns_shell.pdbx_redundancy             4.4 
_reflns_shell.percent_possible_obs        85.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.657 
_reflns_shell.pdbx_Rpim_I_all             0.745 
_reflns_shell.pdbx_CC_half                0.365 
_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                                 7HGH 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     25547 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.56 
_refine.ls_d_res_high                            1.74 
_refine.ls_percent_reflns_obs                    92.61 
_refine.ls_R_factor_obs                          0.21131 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20747 
_refine.ls_R_factor_R_free                       0.27970 
_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                  1390 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.929 
_refine.B_iso_mean                               41.690 
_refine.aniso_B[1][1]                            1.02 
_refine.aniso_B[2][2]                            -0.70 
_refine.aniso_B[3][3]                            -0.32 
_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                       0.149 
_refine.pdbx_overall_ESU_R_Free                  0.157 
_refine.overall_SU_ML                            0.147 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.851 
_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        2123 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.number_atoms_solvent             261 
_refine_hist.number_atoms_total               2437 
_refine_hist.d_res_high                       1.74 
_refine_hist.d_res_low                        40.56 
# 
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             0.009  0.012  ? 2280 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.819  1.834  ? 3101 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.597  5.000  ? 263  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       8.675  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.245 10.000 ? 302  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.129  0.200  ? 284  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1892 '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                  4.019  3.879  ? 1061 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.464  6.941  ? 1321 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.991  4.270  ? 1219 '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       10.076 56.73  ? 3457 '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                       1.740 
_refine_ls_shell.d_res_low                        1.785 
_refine_ls_shell.number_reflns_R_work             1686 
_refine_ls_shell.R_factor_R_work                  0.365 
_refine_ls_shell.percent_reflns_obs               84.88 
_refine_ls_shell.R_factor_R_free                  0.324 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             99 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGH 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z26823525' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGH 
_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 7HGH A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGH B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGH 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 7HGH GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGH SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGH GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGH SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGH GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGH 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 ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O ALA C 52 ? O ALA C 51 N ILE C 43 ? N ILE C 42 
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                   7HGH 
_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 201 ? ? O B HOH 214 ? ? 1.41 
2  1 O   B HOH 210 ? ? O B HOH 233 ? ? 1.64 
3  1 O   A HOH 212 ? ? O A HOH 303 ? ? 1.71 
4  1 O   B HOH 240 ? ? O B HOH 268 ? ? 1.73 
5  1 O   B PRO 19  ? ? O B HOH 201 ? ? 1.77 
6  1 O   A HOH 268 ? ? O A HOH 288 ? ? 1.83 
7  1 NH2 A ARG 74  ? ? O A HOH 201 ? ? 1.92 
8  1 OD1 A ASP 27  ? ? O A HOH 202 ? ? 2.01 
9  1 NE2 C HIS 89  ? ? O C HOH 201 ? ? 2.13 
10 1 O   A HOH 270 ? ? O A HOH 300 ? ? 2.16 
11 1 O2  A SO4 104 ? ? O A HOH 203 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     290 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     259 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_445 
_pdbx_validate_symm_contact.dist              1.75 
# 
_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                109.85 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            9.65 
_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 38 ? ? 55.96   13.90  
2 1 ASN A 87 ? ? -159.85 60.99  
3 1 ASN B 38 ? ? 90.57   -20.33 
4 1 ASN B 87 ? ? -163.78 61.65  
5 1 PRO C 37 ? ? -35.77  118.62 
6 1 ASN C 87 ? ? -149.07 52.00  
# 
_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            144.84 
# 
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 ASP 27 ? C ASP 28 
11 1 Y 1 C ILE 28 ? C ILE 29 
12 1 Y 1 C ALA 29 ? C ALA 30 
13 1 Y 1 C ASP 30 ? C ASP 31 
14 1 Y 1 C GLY 31 ? C GLY 32 
15 1 Y 1 C ALA 32 ? C ALA 33 
16 1 Y 1 C VAL 33 ? C VAL 34 
17 1 Y 1 C LYS 34 ? C LYS 35 
18 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 
A1A4A N1   N Y N 1   
A1A4A C4   C N N 2   
A1A4A C5   C N R 3   
A1A4A C6   C N N 4   
A1A4A C7   C N N 5   
A1A4A C8   C N N 6   
A1A4A O    O N N 7   
A1A4A O1   O N N 8   
A1A4A N2   N N N 9   
A1A4A C3   C Y N 10  
A1A4A N    N Y N 11  
A1A4A S    S Y N 12  
A1A4A C2   C Y N 13  
A1A4A C1   C N N 14  
A1A4A C    C N N 15  
A1A4A H6   H N N 16  
A1A4A H8   H N N 17  
A1A4A H7   H N N 18  
A1A4A H10  H N N 19  
A1A4A H9   H N N 20  
A1A4A H12  H N N 21  
A1A4A H11  H N N 22  
A1A4A H5   H N N 23  
A1A4A H3   H N N 24  
A1A4A H4   H N N 25  
A1A4A H    H N N 26  
A1A4A H1   H N N 27  
A1A4A H2   H N N 28  
ALA   N    N N N 29  
ALA   CA   C N S 30  
ALA   C    C N N 31  
ALA   O    O N N 32  
ALA   CB   C N N 33  
ALA   OXT  O N N 34  
ALA   H    H N N 35  
ALA   H2   H N N 36  
ALA   HA   H N N 37  
ALA   HB1  H N N 38  
ALA   HB2  H N N 39  
ALA   HB3  H N N 40  
ALA   HXT  H N N 41  
ARG   N    N N N 42  
ARG   CA   C N S 43  
ARG   C    C N N 44  
ARG   O    O N N 45  
ARG   CB   C N N 46  
ARG   CG   C N N 47  
ARG   CD   C N N 48  
ARG   NE   N N N 49  
ARG   CZ   C N N 50  
ARG   NH1  N N N 51  
ARG   NH2  N N N 52  
ARG   OXT  O N N 53  
ARG   H    H N N 54  
ARG   H2   H N N 55  
ARG   HA   H N N 56  
ARG   HB2  H N N 57  
ARG   HB3  H N N 58  
ARG   HG2  H N N 59  
ARG   HG3  H N N 60  
ARG   HD2  H N N 61  
ARG   HD3  H N N 62  
ARG   HE   H N N 63  
ARG   HH11 H N N 64  
ARG   HH12 H N N 65  
ARG   HH21 H N N 66  
ARG   HH22 H N N 67  
ARG   HXT  H N N 68  
ASN   N    N N N 69  
ASN   CA   C N S 70  
ASN   C    C N N 71  
ASN   O    O N N 72  
ASN   CB   C N N 73  
ASN   CG   C N N 74  
ASN   OD1  O N N 75  
ASN   ND2  N N N 76  
ASN   OXT  O N N 77  
ASN   H    H N N 78  
ASN   H2   H N N 79  
ASN   HA   H N N 80  
ASN   HB2  H N N 81  
ASN   HB3  H N N 82  
ASN   HD21 H N N 83  
ASN   HD22 H N N 84  
ASN   HXT  H N N 85  
ASP   N    N N N 86  
ASP   CA   C N S 87  
ASP   C    C N N 88  
ASP   O    O N N 89  
ASP   CB   C N N 90  
ASP   CG   C N N 91  
ASP   OD1  O N N 92  
ASP   OD2  O N N 93  
ASP   OXT  O N N 94  
ASP   H    H N N 95  
ASP   H2   H N N 96  
ASP   HA   H N N 97  
ASP   HB2  H N N 98  
ASP   HB3  H N N 99  
ASP   HD2  H N N 100 
ASP   HXT  H N N 101 
CYS   N    N N N 102 
CYS   CA   C N R 103 
CYS   C    C N N 104 
CYS   O    O N N 105 
CYS   CB   C N N 106 
CYS   SG   S N N 107 
CYS   OXT  O N N 108 
CYS   H    H N N 109 
CYS   H2   H N N 110 
CYS   HA   H N N 111 
CYS   HB2  H N N 112 
CYS   HB3  H N N 113 
CYS   HG   H N N 114 
CYS   HXT  H N N 115 
EDO   C1   C N N 116 
EDO   O1   O N N 117 
EDO   C2   C N N 118 
EDO   O2   O N N 119 
EDO   H11  H N N 120 
EDO   H12  H N N 121 
EDO   HO1  H N N 122 
EDO   H21  H N N 123 
EDO   H22  H N N 124 
EDO   HO2  H N N 125 
GLN   N    N N N 126 
GLN   CA   C N S 127 
GLN   C    C N N 128 
GLN   O    O N N 129 
GLN   CB   C N N 130 
GLN   CG   C N N 131 
GLN   CD   C N N 132 
GLN   OE1  O N N 133 
GLN   NE2  N N N 134 
GLN   OXT  O N N 135 
GLN   H    H N N 136 
GLN   H2   H N N 137 
GLN   HA   H N N 138 
GLN   HB2  H N N 139 
GLN   HB3  H N N 140 
GLN   HG2  H N N 141 
GLN   HG3  H N N 142 
GLN   HE21 H N N 143 
GLN   HE22 H N N 144 
GLN   HXT  H N N 145 
GLU   N    N N N 146 
GLU   CA   C N S 147 
GLU   C    C N N 148 
GLU   O    O N N 149 
GLU   CB   C N N 150 
GLU   CG   C N N 151 
GLU   CD   C N N 152 
GLU   OE1  O N N 153 
GLU   OE2  O N N 154 
GLU   OXT  O N N 155 
GLU   H    H N N 156 
GLU   H2   H N N 157 
GLU   HA   H N N 158 
GLU   HB2  H N N 159 
GLU   HB3  H N N 160 
GLU   HG2  H N N 161 
GLU   HG3  H N N 162 
GLU   HE2  H N N 163 
GLU   HXT  H N N 164 
GLY   N    N N N 165 
GLY   CA   C N N 166 
GLY   C    C N N 167 
GLY   O    O N N 168 
GLY   OXT  O N N 169 
GLY   H    H N N 170 
GLY   H2   H N N 171 
GLY   HA2  H N N 172 
GLY   HA3  H N N 173 
GLY   HXT  H N N 174 
HIS   N    N N N 175 
HIS   CA   C N S 176 
HIS   C    C N N 177 
HIS   O    O N N 178 
HIS   CB   C N N 179 
HIS   CG   C Y N 180 
HIS   ND1  N Y N 181 
HIS   CD2  C Y N 182 
HIS   CE1  C Y N 183 
HIS   NE2  N Y N 184 
HIS   OXT  O N N 185 
HIS   H    H N N 186 
HIS   H2   H N N 187 
HIS   HA   H N N 188 
HIS   HB2  H N N 189 
HIS   HB3  H N N 190 
HIS   HD1  H N N 191 
HIS   HD2  H N N 192 
HIS   HE1  H N N 193 
HIS   HE2  H N N 194 
HIS   HXT  H N N 195 
HOH   O    O N N 196 
HOH   H1   H N N 197 
HOH   H2   H N N 198 
ILE   N    N N N 199 
ILE   CA   C N S 200 
ILE   C    C N N 201 
ILE   O    O N N 202 
ILE   CB   C N S 203 
ILE   CG1  C N N 204 
ILE   CG2  C N N 205 
ILE   CD1  C N N 206 
ILE   OXT  O N N 207 
ILE   H    H N N 208 
ILE   H2   H N N 209 
ILE   HA   H N N 210 
ILE   HB   H N N 211 
ILE   HG12 H N N 212 
ILE   HG13 H N N 213 
ILE   HG21 H N N 214 
ILE   HG22 H N N 215 
ILE   HG23 H N N 216 
ILE   HD11 H N N 217 
ILE   HD12 H N N 218 
ILE   HD13 H N N 219 
ILE   HXT  H N N 220 
LEU   N    N N N 221 
LEU   CA   C N S 222 
LEU   C    C N N 223 
LEU   O    O N N 224 
LEU   CB   C N N 225 
LEU   CG   C N N 226 
LEU   CD1  C N N 227 
LEU   CD2  C N N 228 
LEU   OXT  O N N 229 
LEU   H    H N N 230 
LEU   H2   H N N 231 
LEU   HA   H N N 232 
LEU   HB2  H N N 233 
LEU   HB3  H N N 234 
LEU   HG   H N N 235 
LEU   HD11 H N N 236 
LEU   HD12 H N N 237 
LEU   HD13 H N N 238 
LEU   HD21 H N N 239 
LEU   HD22 H N N 240 
LEU   HD23 H N N 241 
LEU   HXT  H N N 242 
LYS   N    N N N 243 
LYS   CA   C N S 244 
LYS   C    C N N 245 
LYS   O    O N N 246 
LYS   CB   C N N 247 
LYS   CG   C N N 248 
LYS   CD   C N N 249 
LYS   CE   C N N 250 
LYS   NZ   N N N 251 
LYS   OXT  O N N 252 
LYS   H    H N N 253 
LYS   H2   H N N 254 
LYS   HA   H N N 255 
LYS   HB2  H N N 256 
LYS   HB3  H N N 257 
LYS   HG2  H N N 258 
LYS   HG3  H N N 259 
LYS   HD2  H N N 260 
LYS   HD3  H N N 261 
LYS   HE2  H N N 262 
LYS   HE3  H N N 263 
LYS   HZ1  H N N 264 
LYS   HZ2  H N N 265 
LYS   HZ3  H N N 266 
LYS   HXT  H N N 267 
MET   N    N N N 268 
MET   CA   C N S 269 
MET   C    C N N 270 
MET   O    O N N 271 
MET   CB   C N N 272 
MET   CG   C N N 273 
MET   SD   S N N 274 
MET   CE   C N N 275 
MET   OXT  O N N 276 
MET   H    H N N 277 
MET   H2   H N N 278 
MET   HA   H N N 279 
MET   HB2  H N N 280 
MET   HB3  H N N 281 
MET   HG2  H N N 282 
MET   HG3  H N N 283 
MET   HE1  H N N 284 
MET   HE2  H N N 285 
MET   HE3  H N N 286 
MET   HXT  H N N 287 
PHE   N    N N N 288 
PHE   CA   C N S 289 
PHE   C    C N N 290 
PHE   O    O N N 291 
PHE   CB   C N N 292 
PHE   CG   C Y N 293 
PHE   CD1  C Y N 294 
PHE   CD2  C Y N 295 
PHE   CE1  C Y N 296 
PHE   CE2  C Y N 297 
PHE   CZ   C Y N 298 
PHE   OXT  O N N 299 
PHE   H    H N N 300 
PHE   H2   H N N 301 
PHE   HA   H N N 302 
PHE   HB2  H N N 303 
PHE   HB3  H N N 304 
PHE   HD1  H N N 305 
PHE   HD2  H N N 306 
PHE   HE1  H N N 307 
PHE   HE2  H N N 308 
PHE   HZ   H N N 309 
PHE   HXT  H N N 310 
PRO   N    N N N 311 
PRO   CA   C N S 312 
PRO   C    C N N 313 
PRO   O    O N N 314 
PRO   CB   C N N 315 
PRO   CG   C N N 316 
PRO   CD   C N N 317 
PRO   OXT  O N N 318 
PRO   H    H N N 319 
PRO   HA   H N N 320 
PRO   HB2  H N N 321 
PRO   HB3  H N N 322 
PRO   HG2  H N N 323 
PRO   HG3  H N N 324 
PRO   HD2  H N N 325 
PRO   HD3  H N N 326 
PRO   HXT  H N N 327 
SER   N    N N N 328 
SER   CA   C N S 329 
SER   C    C N N 330 
SER   O    O N N 331 
SER   CB   C N N 332 
SER   OG   O N N 333 
SER   OXT  O N N 334 
SER   H    H N N 335 
SER   H2   H N N 336 
SER   HA   H N N 337 
SER   HB2  H N N 338 
SER   HB3  H N N 339 
SER   HG   H N N 340 
SER   HXT  H N N 341 
SO4   S    S N N 342 
SO4   O1   O N N 343 
SO4   O2   O N N 344 
SO4   O3   O N N 345 
SO4   O4   O N N 346 
THR   N    N N N 347 
THR   CA   C N S 348 
THR   C    C N N 349 
THR   O    O N N 350 
THR   CB   C N R 351 
THR   OG1  O N N 352 
THR   CG2  C N N 353 
THR   OXT  O N N 354 
THR   H    H N N 355 
THR   H2   H N N 356 
THR   HA   H N N 357 
THR   HB   H N N 358 
THR   HG1  H N N 359 
THR   HG21 H N N 360 
THR   HG22 H N N 361 
THR   HG23 H N N 362 
THR   HXT  H N N 363 
TRP   N    N N N 364 
TRP   CA   C N S 365 
TRP   C    C N N 366 
TRP   O    O N N 367 
TRP   CB   C N N 368 
TRP   CG   C Y N 369 
TRP   CD1  C Y N 370 
TRP   CD2  C Y N 371 
TRP   NE1  N Y N 372 
TRP   CE2  C Y N 373 
TRP   CE3  C Y N 374 
TRP   CZ2  C Y N 375 
TRP   CZ3  C Y N 376 
TRP   CH2  C Y N 377 
TRP   OXT  O N N 378 
TRP   H    H N N 379 
TRP   H2   H N N 380 
TRP   HA   H N N 381 
TRP   HB2  H N N 382 
TRP   HB3  H N N 383 
TRP   HD1  H N N 384 
TRP   HE1  H N N 385 
TRP   HE3  H N N 386 
TRP   HZ2  H N N 387 
TRP   HZ3  H N N 388 
TRP   HH2  H N N 389 
TRP   HXT  H N N 390 
TYR   N    N N N 391 
TYR   CA   C N S 392 
TYR   C    C N N 393 
TYR   O    O N N 394 
TYR   CB   C N N 395 
TYR   CG   C Y N 396 
TYR   CD1  C Y N 397 
TYR   CD2  C Y N 398 
TYR   CE1  C Y N 399 
TYR   CE2  C Y N 400 
TYR   CZ   C Y N 401 
TYR   OH   O N N 402 
TYR   OXT  O N N 403 
TYR   H    H N N 404 
TYR   H2   H N N 405 
TYR   HA   H N N 406 
TYR   HB2  H N N 407 
TYR   HB3  H N N 408 
TYR   HD1  H N N 409 
TYR   HD2  H N N 410 
TYR   HE1  H N N 411 
TYR   HE2  H N N 412 
TYR   HH   H N N 413 
TYR   HXT  H N N 414 
VAL   N    N N N 415 
VAL   CA   C N S 416 
VAL   C    C N N 417 
VAL   O    O N N 418 
VAL   CB   C N N 419 
VAL   CG1  C N N 420 
VAL   CG2  C N N 421 
VAL   OXT  O N N 422 
VAL   H    H N N 423 
VAL   H2   H N N 424 
VAL   HA   H N N 425 
VAL   HB   H N N 426 
VAL   HG11 H N N 427 
VAL   HG12 H N N 428 
VAL   HG13 H N N 429 
VAL   HG21 H N N 430 
VAL   HG22 H N N 431 
VAL   HG23 H N N 432 
VAL   HXT  H N N 433 
# 
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 
A1A4A C   C1   sing N N 1   
A1A4A C1  C2   sing N N 2   
A1A4A C2  N    doub Y N 3   
A1A4A N   N1   sing Y N 4   
A1A4A N1  C3   doub Y N 5   
A1A4A C3  N2   sing N N 6   
A1A4A N2  C4   sing N N 7   
A1A4A C4  O    doub N N 8   
A1A4A C5  C4   sing N N 9   
A1A4A C5  C6   sing N N 10  
A1A4A C6  C7   sing N N 11  
A1A4A C7  C8   sing N N 12  
A1A4A C8  O1   sing N N 13  
A1A4A O1  C5   sing N N 14  
A1A4A S   C3   sing Y N 15  
A1A4A C2  S    sing Y N 16  
A1A4A C5  H6   sing N N 17  
A1A4A C6  H8   sing N N 18  
A1A4A C6  H7   sing N N 19  
A1A4A C7  H10  sing N N 20  
A1A4A C7  H9   sing N N 21  
A1A4A C8  H12  sing N N 22  
A1A4A C8  H11  sing N N 23  
A1A4A N2  H5   sing N N 24  
A1A4A C1  H3   sing N N 25  
A1A4A C1  H4   sing N N 26  
A1A4A C   H    sing N N 27  
A1A4A C   H1   sing N N 28  
A1A4A C   H2   sing N N 29  
ALA   N   CA   sing N N 30  
ALA   N   H    sing N N 31  
ALA   N   H2   sing N N 32  
ALA   CA  C    sing N N 33  
ALA   CA  CB   sing N N 34  
ALA   CA  HA   sing N N 35  
ALA   C   O    doub N N 36  
ALA   C   OXT  sing N N 37  
ALA   CB  HB1  sing N N 38  
ALA   CB  HB2  sing N N 39  
ALA   CB  HB3  sing N N 40  
ALA   OXT HXT  sing N N 41  
ARG   N   CA   sing N N 42  
ARG   N   H    sing N N 43  
ARG   N   H2   sing N N 44  
ARG   CA  C    sing N N 45  
ARG   CA  CB   sing N N 46  
ARG   CA  HA   sing N N 47  
ARG   C   O    doub N N 48  
ARG   C   OXT  sing N N 49  
ARG   CB  CG   sing N N 50  
ARG   CB  HB2  sing N N 51  
ARG   CB  HB3  sing N N 52  
ARG   CG  CD   sing N N 53  
ARG   CG  HG2  sing N N 54  
ARG   CG  HG3  sing N N 55  
ARG   CD  NE   sing N N 56  
ARG   CD  HD2  sing N N 57  
ARG   CD  HD3  sing N N 58  
ARG   NE  CZ   sing N N 59  
ARG   NE  HE   sing N N 60  
ARG   CZ  NH1  sing N N 61  
ARG   CZ  NH2  doub N N 62  
ARG   NH1 HH11 sing N N 63  
ARG   NH1 HH12 sing N N 64  
ARG   NH2 HH21 sing N N 65  
ARG   NH2 HH22 sing N N 66  
ARG   OXT HXT  sing N N 67  
ASN   N   CA   sing N N 68  
ASN   N   H    sing N N 69  
ASN   N   H2   sing N N 70  
ASN   CA  C    sing N N 71  
ASN   CA  CB   sing N N 72  
ASN   CA  HA   sing N N 73  
ASN   C   O    doub N N 74  
ASN   C   OXT  sing N N 75  
ASN   CB  CG   sing N N 76  
ASN   CB  HB2  sing N N 77  
ASN   CB  HB3  sing N N 78  
ASN   CG  OD1  doub N N 79  
ASN   CG  ND2  sing N N 80  
ASN   ND2 HD21 sing N N 81  
ASN   ND2 HD22 sing N N 82  
ASN   OXT HXT  sing N N 83  
ASP   N   CA   sing N N 84  
ASP   N   H    sing N N 85  
ASP   N   H2   sing N N 86  
ASP   CA  C    sing N N 87  
ASP   CA  CB   sing N N 88  
ASP   CA  HA   sing N N 89  
ASP   C   O    doub N N 90  
ASP   C   OXT  sing N N 91  
ASP   CB  CG   sing N N 92  
ASP   CB  HB2  sing N N 93  
ASP   CB  HB3  sing N N 94  
ASP   CG  OD1  doub N N 95  
ASP   CG  OD2  sing N N 96  
ASP   OD2 HD2  sing N N 97  
ASP   OXT HXT  sing N N 98  
CYS   N   CA   sing N N 99  
CYS   N   H    sing N N 100 
CYS   N   H2   sing N N 101 
CYS   CA  C    sing N N 102 
CYS   CA  CB   sing N N 103 
CYS   CA  HA   sing N N 104 
CYS   C   O    doub N N 105 
CYS   C   OXT  sing N N 106 
CYS   CB  SG   sing N N 107 
CYS   CB  HB2  sing N N 108 
CYS   CB  HB3  sing N N 109 
CYS   SG  HG   sing N N 110 
CYS   OXT HXT  sing N N 111 
EDO   C1  O1   sing N N 112 
EDO   C1  C2   sing N N 113 
EDO   C1  H11  sing N N 114 
EDO   C1  H12  sing N N 115 
EDO   O1  HO1  sing N N 116 
EDO   C2  O2   sing N N 117 
EDO   C2  H21  sing N N 118 
EDO   C2  H22  sing N N 119 
EDO   O2  HO2  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
HOH   O   H1   sing N N 188 
HOH   O   H2   sing N N 189 
ILE   N   CA   sing N N 190 
ILE   N   H    sing N N 191 
ILE   N   H2   sing N N 192 
ILE   CA  C    sing N N 193 
ILE   CA  CB   sing N N 194 
ILE   CA  HA   sing N N 195 
ILE   C   O    doub N N 196 
ILE   C   OXT  sing N N 197 
ILE   CB  CG1  sing N N 198 
ILE   CB  CG2  sing N N 199 
ILE   CB  HB   sing N N 200 
ILE   CG1 CD1  sing N N 201 
ILE   CG1 HG12 sing N N 202 
ILE   CG1 HG13 sing N N 203 
ILE   CG2 HG21 sing N N 204 
ILE   CG2 HG22 sing N N 205 
ILE   CG2 HG23 sing N N 206 
ILE   CD1 HD11 sing N N 207 
ILE   CD1 HD12 sing N N 208 
ILE   CD1 HD13 sing N N 209 
ILE   OXT HXT  sing N N 210 
LEU   N   CA   sing N N 211 
LEU   N   H    sing N N 212 
LEU   N   H2   sing N N 213 
LEU   CA  C    sing N N 214 
LEU   CA  CB   sing N N 215 
LEU   CA  HA   sing N N 216 
LEU   C   O    doub N N 217 
LEU   C   OXT  sing N N 218 
LEU   CB  CG   sing N N 219 
LEU   CB  HB2  sing N N 220 
LEU   CB  HB3  sing N N 221 
LEU   CG  CD1  sing N N 222 
LEU   CG  CD2  sing N N 223 
LEU   CG  HG   sing N N 224 
LEU   CD1 HD11 sing N N 225 
LEU   CD1 HD12 sing N N 226 
LEU   CD1 HD13 sing N N 227 
LEU   CD2 HD21 sing N N 228 
LEU   CD2 HD22 sing N N 229 
LEU   CD2 HD23 sing N N 230 
LEU   OXT HXT  sing N N 231 
LYS   N   CA   sing N N 232 
LYS   N   H    sing N N 233 
LYS   N   H2   sing N N 234 
LYS   CA  C    sing N N 235 
LYS   CA  CB   sing N N 236 
LYS   CA  HA   sing N N 237 
LYS   C   O    doub N N 238 
LYS   C   OXT  sing N N 239 
LYS   CB  CG   sing N N 240 
LYS   CB  HB2  sing N N 241 
LYS   CB  HB3  sing N N 242 
LYS   CG  CD   sing N N 243 
LYS   CG  HG2  sing N N 244 
LYS   CG  HG3  sing N N 245 
LYS   CD  CE   sing N N 246 
LYS   CD  HD2  sing N N 247 
LYS   CD  HD3  sing N N 248 
LYS   CE  NZ   sing N N 249 
LYS   CE  HE2  sing N N 250 
LYS   CE  HE3  sing N N 251 
LYS   NZ  HZ1  sing N N 252 
LYS   NZ  HZ2  sing N N 253 
LYS   NZ  HZ3  sing N N 254 
LYS   OXT HXT  sing N N 255 
MET   N   CA   sing N N 256 
MET   N   H    sing N N 257 
MET   N   H2   sing N N 258 
MET   CA  C    sing N N 259 
MET   CA  CB   sing N N 260 
MET   CA  HA   sing N N 261 
MET   C   O    doub N N 262 
MET   C   OXT  sing N N 263 
MET   CB  CG   sing N N 264 
MET   CB  HB2  sing N N 265 
MET   CB  HB3  sing N N 266 
MET   CG  SD   sing N N 267 
MET   CG  HG2  sing N N 268 
MET   CG  HG3  sing N N 269 
MET   SD  CE   sing N N 270 
MET   CE  HE1  sing N N 271 
MET   CE  HE2  sing N N 272 
MET   CE  HE3  sing N N 273 
MET   OXT HXT  sing N N 274 
PHE   N   CA   sing N N 275 
PHE   N   H    sing N N 276 
PHE   N   H2   sing N N 277 
PHE   CA  C    sing N N 278 
PHE   CA  CB   sing N N 279 
PHE   CA  HA   sing N N 280 
PHE   C   O    doub N N 281 
PHE   C   OXT  sing N N 282 
PHE   CB  CG   sing N N 283 
PHE   CB  HB2  sing N N 284 
PHE   CB  HB3  sing N N 285 
PHE   CG  CD1  doub Y N 286 
PHE   CG  CD2  sing Y N 287 
PHE   CD1 CE1  sing Y N 288 
PHE   CD1 HD1  sing N N 289 
PHE   CD2 CE2  doub Y N 290 
PHE   CD2 HD2  sing N N 291 
PHE   CE1 CZ   doub Y N 292 
PHE   CE1 HE1  sing N N 293 
PHE   CE2 CZ   sing Y N 294 
PHE   CE2 HE2  sing N N 295 
PHE   CZ  HZ   sing N N 296 
PHE   OXT HXT  sing N N 297 
PRO   N   CA   sing N N 298 
PRO   N   CD   sing N N 299 
PRO   N   H    sing N N 300 
PRO   CA  C    sing N N 301 
PRO   CA  CB   sing N N 302 
PRO   CA  HA   sing N N 303 
PRO   C   O    doub N N 304 
PRO   C   OXT  sing N N 305 
PRO   CB  CG   sing N N 306 
PRO   CB  HB2  sing N N 307 
PRO   CB  HB3  sing N N 308 
PRO   CG  CD   sing N N 309 
PRO   CG  HG2  sing N N 310 
PRO   CG  HG3  sing N N 311 
PRO   CD  HD2  sing N N 312 
PRO   CD  HD3  sing N N 313 
PRO   OXT HXT  sing N N 314 
SER   N   CA   sing N N 315 
SER   N   H    sing N N 316 
SER   N   H2   sing N N 317 
SER   CA  C    sing N N 318 
SER   CA  CB   sing N N 319 
SER   CA  HA   sing N N 320 
SER   C   O    doub N N 321 
SER   C   OXT  sing N N 322 
SER   CB  OG   sing N N 323 
SER   CB  HB2  sing N N 324 
SER   CB  HB3  sing N N 325 
SER   OG  HG   sing N N 326 
SER   OXT HXT  sing N N 327 
SO4   S   O1   doub N N 328 
SO4   S   O2   doub N N 329 
SO4   S   O3   sing N N 330 
SO4   S   O4   sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TRP   N   CA   sing N N 348 
TRP   N   H    sing N N 349 
TRP   N   H2   sing N N 350 
TRP   CA  C    sing N N 351 
TRP   CA  CB   sing N N 352 
TRP   CA  HA   sing N N 353 
TRP   C   O    doub N N 354 
TRP   C   OXT  sing N N 355 
TRP   CB  CG   sing N N 356 
TRP   CB  HB2  sing N N 357 
TRP   CB  HB3  sing N N 358 
TRP   CG  CD1  doub Y N 359 
TRP   CG  CD2  sing Y N 360 
TRP   CD1 NE1  sing Y N 361 
TRP   CD1 HD1  sing N N 362 
TRP   CD2 CE2  doub Y N 363 
TRP   CD2 CE3  sing Y N 364 
TRP   NE1 CE2  sing Y N 365 
TRP   NE1 HE1  sing N N 366 
TRP   CE2 CZ2  sing Y N 367 
TRP   CE3 CZ3  doub Y N 368 
TRP   CE3 HE3  sing N N 369 
TRP   CZ2 CH2  doub Y N 370 
TRP   CZ2 HZ2  sing N N 371 
TRP   CZ3 CH2  sing Y N 372 
TRP   CZ3 HZ3  sing N N 373 
TRP   CH2 HH2  sing N N 374 
TRP   OXT HXT  sing N N 375 
TYR   N   CA   sing N N 376 
TYR   N   H    sing N N 377 
TYR   N   H2   sing N N 378 
TYR   CA  C    sing N N 379 
TYR   CA  CB   sing N N 380 
TYR   CA  HA   sing N N 381 
TYR   C   O    doub N N 382 
TYR   C   OXT  sing N N 383 
TYR   CB  CG   sing N N 384 
TYR   CB  HB2  sing N N 385 
TYR   CB  HB3  sing N N 386 
TYR   CG  CD1  doub Y N 387 
TYR   CG  CD2  sing Y N 388 
TYR   CD1 CE1  sing Y N 389 
TYR   CD1 HD1  sing N N 390 
TYR   CD2 CE2  doub Y N 391 
TYR   CD2 HD2  sing N N 392 
TYR   CE1 CZ   doub Y N 393 
TYR   CE1 HE1  sing N N 394 
TYR   CE2 CZ   sing Y N 395 
TYR   CE2 HE2  sing N N 396 
TYR   CZ  OH   sing N N 397 
TYR   OH  HH   sing N N 398 
TYR   OXT HXT  sing N N 399 
VAL   N   CA   sing N N 400 
VAL   N   H    sing N N 401 
VAL   N   H2   sing N N 402 
VAL   CA  C    sing N N 403 
VAL   CA  CB   sing N N 404 
VAL   CA  HA   sing N N 405 
VAL   C   O    doub N N 406 
VAL   C   OXT  sing N N 407 
VAL   CB  CG1  sing N N 408 
VAL   CB  CG2  sing N N 409 
VAL   CB  HB   sing N N 410 
VAL   CG1 HG11 sing N N 411 
VAL   CG1 HG12 sing N N 412 
VAL   CG1 HG13 sing N N 413 
VAL   CG2 HG21 sing N N 414 
VAL   CG2 HG22 sing N N 415 
VAL   CG2 HG23 sing N N 416 
VAL   OXT HXT  sing N N 417 
# 
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                    7HGH 
_atom_sites.fract_transf_matrix[1][1]   0.024248 
_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]   0.023849 
_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]   0.006322 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET   A 1 2  ? -0.050  4.313   2.578   1.00 52.67  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -1.099  3.603   1.798   1.00 60.31  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? -0.461  2.558   0.873   1.00 54.84  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 0.710   2.663   0.500   1.00 53.82  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -2.037  4.561   1.046   1.00 55.93  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -3.028  5.314   1.928   1.00 62.20  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -4.237  4.412   2.934   1.00 62.10  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -5.189  5.746   3.678   1.00 58.54  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -1.200  1.461   0.584   1.00 52.39  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? -0.767  0.411   -0.344  1.00 49.11  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? -0.504  0.890   -1.770  1.00 42.40  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -1.180  1.767   -2.274  1.00 41.89  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.977  -0.591  -0.309  1.00 47.27  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -2.607  -0.370  1.046   1.00 49.48  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -2.482  1.129   1.241   1.00 54.81  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 0.478   0.252   -2.402  1.00 43.98  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 0.696   0.351   -3.828  1.00 42.66  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.148   -0.944  -4.421  1.00 35.85  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? -0.267  -1.825  -3.684  1.00 36.22  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.202   0.489   -4.094  1.00 53.08  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 2.838   1.741   -3.562  1.00 75.73  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.034   1.984   -2.218  1.00 85.33  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 3.320   2.823   -4.203  1.00 82.25  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 3.612   3.171   -2.061  1.00 89.52  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 3.798   3.695   -3.256  1.00 87.80  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.172   -1.077  -5.749  1.00 31.68  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? -0.005  -2.383  -6.352  1.00 32.21  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.117   -3.356  -5.928  1.00 30.88  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.207   -2.967  -5.446  1.00 31.91  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? -0.097  -2.233  -7.858  1.00 37.88  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 0.846   -4.664  -6.063  1.00 28.61  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 1.904   -5.653  -5.894  1.00 25.55  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.073   -5.405  -6.864  1.00 32.91  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 2.866   -5.007  -8.013  1.00 31.68  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.362   -7.077  -6.047  1.00 27.55  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 0.584   -7.542  -4.819  1.00 28.00  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.235   -7.731  -3.594  1.00 30.00  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.799  -7.741  -4.868  1.00 27.79  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 0.519   -8.147  -2.464  1.00 31.39  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -1.491  -8.202  -3.743  1.00 25.48  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.855  -8.331  -2.541  1.00 28.35  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.312   -5.638  -6.389  1.00 27.08  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 5.452   -5.697  -7.301  1.00 29.93  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.317   -6.933  -7.002  1.00 27.70  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.323   -7.465  -5.887  1.00 27.31  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.144   -4.356  -7.054  1.00 35.57  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 6.813   -4.326  -5.677  1.00 37.39  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 7.377   -2.934  -5.347  1.00 40.95  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.078   -2.940  -4.003  1.00 42.65  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.196   -3.275  -2.866  1.00 43.52  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.176   -7.387  -7.944  1.00 27.82  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.107   -8.492  -7.680  1.00 25.38  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 8.883   -8.258  -6.387  1.00 24.55  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 9.318   -7.133  -6.131  1.00 30.91  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.041   -8.393  -8.928  1.00 29.96  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.137   -7.857  -10.003 1.00 29.99  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.272   -6.850  -9.311  1.00 30.37  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.032   -9.324  -5.586  1.00 23.87  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 9.772   -9.265  -4.320  1.00 22.10  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 8.797   -9.180  -3.134  1.00 23.23  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.149   -9.510  -2.005  1.00 27.61  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 7.568   -8.707  -3.352  1.00 22.05  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 6.629   -8.657  -2.233  1.00 20.77  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 6.359   -10.035 -1.654  1.00 24.27  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 6.208   -10.980 -2.406  1.00 22.48  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 5.288   -8.062  -2.643  1.00 24.51  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 5.347   -6.563  -2.852  1.00 28.88  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.380   -5.959  -2.485  1.00 28.58  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 4.423   -6.033  -3.414  1.00 30.76  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 6.274   -10.115 -0.306  1.00 20.50  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.073   -11.375 0.394   1.00 25.15  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 4.607   -11.428 0.806   1.00 22.42  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.055   -10.400 1.212   1.00 21.47  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 6.965   -11.561 1.624   1.00 22.20  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 8.462   -11.331 1.339   1.00 19.72  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 9.310   -11.583 2.565   1.00 27.48  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 8.998   -12.095 0.189   1.00 25.27  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.020   -12.640 0.724   1.00 19.49  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 2.580   -12.801 0.933   1.00 21.98  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 2.339   -14.196 1.515   1.00 24.22  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 3.213   -15.071 1.470   1.00 26.80  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 1.828   -12.667 -0.432  1.00 20.24  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.004   -11.301 -1.078  1.00 25.39  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.180   -13.795 -1.402  1.00 23.27  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.129   -14.419 2.041   1.00 22.93  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 0.515   -15.736 2.075   1.00 22.36  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? -0.484  -15.801 0.916   1.00 24.82  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -1.227  -14.858 0.641   1.00 26.93  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? -0.300  -16.006 3.356   1.00 22.23  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 0.645   -16.156 4.530   1.00 23.97  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.051   -15.059 5.263   1.00 26.34  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 1.108   -17.418 4.897   1.00 24.75  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 1.967   -15.202 6.294   1.00 32.31  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 1.996   -17.557 5.967   1.00 30.28  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 2.471   -16.453 6.619   1.00 30.40  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? -0.434  -16.909 0.176   1.00 22.89  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -1.208  -16.965 -1.048  1.00 24.32  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -2.203  -18.111 -0.874  1.00 26.99  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -1.859  -19.155 -0.304  1.00 27.38  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? -0.294  -17.173 -2.254  1.00 21.55  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -3.416  -17.901 -1.386  1.00 27.14  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -4.507  -18.836 -1.129  1.00 33.08  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -4.920  -19.519 -2.428  1.00 33.96  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -5.330  -18.850 -3.375  1.00 32.69  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -5.722  -18.112 -0.535  1.00 31.58  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -6.869  -19.104 -0.194  1.00 42.72  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -6.598  -19.811 1.132   1.00 42.95  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -7.689  -20.724 1.675   1.00 43.88  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -8.011  -21.782 0.716   1.00 36.21  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -4.795  -20.849 -2.435  1.00 33.37  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -5.352  -21.706 -3.477  1.00 37.08  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -6.464  -22.569 -2.873  1.00 39.13  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -6.346  -23.012 -1.740  1.00 33.77  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -4.280  -22.698 -3.947  1.00 40.00  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -2.988  -22.027 -4.335  1.00 40.66  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -2.662  -22.100 -6.104  1.00 41.84  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -4.208  -21.987 -7.015  1.00 53.03  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -7.533  -22.810 -3.644  1.00 46.06  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -8.638  -23.693 -3.285  1.00 51.36  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -8.088  -24.998 -2.725  1.00 48.80  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -7.286  -25.654 -3.384  1.00 46.15  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -9.264  -24.106 -4.623  1.00 60.76  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -10.666 -24.688 -4.594  1.00 69.41  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -11.757 -23.641 -4.796  1.00 73.02  ? 16  LYS   A CD  1 
ATOM   125  C CE  . LYS   A 1 17 ? -13.104 -24.222 -5.131  1.00 67.07  ? 16  LYS   A CE  1 
ATOM   126  N NZ  . LYS   A 1 17 ? -13.805 -24.879 -4.022  1.00 63.25  ? 16  LYS   A NZ  1 
ATOM   127  N N   . GLY   A 1 18 ? -8.466  -25.357 -1.488  1.00 44.43  ? 17  GLY   A N   1 
ATOM   128  C CA  . GLY   A 1 18 ? -8.101  -26.685 -1.020  1.00 42.06  ? 17  GLY   A CA  1 
ATOM   129  C C   . GLY   A 1 18 ? -6.769  -26.726 -0.275  1.00 44.78  ? 17  GLY   A C   1 
ATOM   130  O O   . GLY   A 1 18 ? -6.447  -27.737 0.328   1.00 46.98  ? 17  GLY   A O   1 
ATOM   131  N N   . TYR   A 1 19 ? -5.978  -25.641 -0.314  1.00 42.26  ? 18  TYR   A N   1 
ATOM   132  C CA  . TYR   A 1 19 ? -4.761  -25.578 0.482   1.00 41.09  ? 18  TYR   A CA  1 
ATOM   133  C C   . TYR   A 1 19 ? -4.943  -24.493 1.535   1.00 36.30  ? 18  TYR   A C   1 
ATOM   134  O O   . TYR   A 1 19 ? -5.723  -23.569 1.315   1.00 37.23  ? 18  TYR   A O   1 
ATOM   135  C CB  . TYR   A 1 19 ? -3.549  -25.240 -0.399  1.00 46.12  ? 18  TYR   A CB  1 
ATOM   136  C CG  . TYR   A 1 19 ? -3.184  -26.295 -1.431  1.00 47.98  ? 18  TYR   A CG  1 
ATOM   137  C CD1 . TYR   A 1 19 ? -2.247  -27.285 -1.148  1.00 59.58  ? 18  TYR   A CD1 1 
ATOM   138  C CD2 . TYR   A 1 19 ? -3.800  -26.312 -2.681  1.00 46.11  ? 18  TYR   A CD2 1 
ATOM   139  C CE1 . TYR   A 1 19 ? -1.928  -28.260 -2.083  1.00 64.41  ? 18  TYR   A CE1 1 
ATOM   140  C CE2 . TYR   A 1 19 ? -3.497  -27.286 -3.619  1.00 56.93  ? 18  TYR   A CE2 1 
ATOM   141  C CZ  . TYR   A 1 19 ? -2.563  -28.262 -3.316  1.00 65.97  ? 18  TYR   A CZ  1 
ATOM   142  O OH  . TYR   A 1 19 ? -2.279  -29.203 -4.266  1.00 72.71  ? 18  TYR   A OH  1 
ATOM   143  N N   . PRO   A 1 20 ? -4.182  -24.500 2.659   1.00 37.38  ? 19  PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 20 ? -4.208  -23.365 3.589   1.00 36.80  ? 19  PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 20 ? -3.352  -22.255 2.967   1.00 37.13  ? 19  PRO   A C   1 
ATOM   146  O O   . PRO   A 1 20 ? -2.577  -22.476 2.013   1.00 30.72  ? 19  PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 20 ? -3.563  -23.944 4.858   1.00 39.74  ? 19  PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 20 ? -2.534  -24.897 4.307   1.00 34.85  ? 19  PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 20 ? -3.201  -25.524 3.060   1.00 37.26  ? 19  PRO   A CD  1 
ATOM   150  N N   . HIS   A 1 21 ? -3.517  -21.064 3.523   1.00 33.52  ? 20  HIS   A N   1 
ATOM   151  C CA  . HIS   A 1 21 ? -2.773  -19.880 3.140   1.00 33.19  ? 20  HIS   A CA  1 
ATOM   152  C C   . HIS   A 1 21 ? -1.281  -20.198 3.287   1.00 28.27  ? 20  HIS   A C   1 
ATOM   153  O O   . HIS   A 1 21 ? -0.878  -20.603 4.370   1.00 28.94  ? 20  HIS   A O   1 
ATOM   154  C CB  . HIS   A 1 21 ? -3.232  -18.712 4.020   1.00 33.80  ? 20  HIS   A CB  1 
ATOM   155  C CG  . HIS   A 1 21 ? -4.660  -18.283 3.839   1.00 34.73  ? 20  HIS   A CG  1 
ATOM   156  N ND1 . HIS   A 1 21 ? -5.768  -18.902 4.411   1.00 31.46  ? 20  HIS   A ND1 1 
ATOM   157  C CD2 . HIS   A 1 21 ? -5.142  -17.184 3.218   1.00 32.85  ? 20  HIS   A CD2 1 
ATOM   158  C CE1 . HIS   A 1 21 ? -6.881  -18.274 4.036   1.00 28.95  ? 20  HIS   A CE1 1 
ATOM   159  N NE2 . HIS   A 1 21 ? -6.536  -17.193 3.356   1.00 36.26  ? 20  HIS   A NE2 1 
ATOM   160  N N   . TRP   A 1 22 ? -0.519  -20.032 2.176   1.00 29.27  ? 21  TRP   A N   1 
ATOM   161  C CA  . TRP   A 1 22 ? 0.812   -20.611 2.025   1.00 28.53  ? 21  TRP   A CA  1 
ATOM   162  C C   . TRP   A 1 22 ? 1.862   -19.503 1.884   1.00 30.35  ? 21  TRP   A C   1 
ATOM   163  O O   . TRP   A 1 22 ? 1.647   -18.578 1.123   1.00 27.42  ? 21  TRP   A O   1 
ATOM   164  C CB  . TRP   A 1 22 ? 0.832   -21.500 0.762   1.00 26.20  ? 21  TRP   A CB  1 
ATOM   165  C CG  . TRP   A 1 22 ? 1.907   -22.558 0.796   1.00 28.24  ? 21  TRP   A CG  1 
ATOM   166  C CD1 . TRP   A 1 22 ? 3.253   -22.379 0.614   1.00 28.18  ? 21  TRP   A CD1 1 
ATOM   167  C CD2 . TRP   A 1 22 ? 1.739   -23.957 1.129   1.00 32.66  ? 21  TRP   A CD2 1 
ATOM   168  N NE1 . TRP   A 1 22 ? 3.918   -23.578 0.742   1.00 35.16  ? 21  TRP   A NE1 1 
ATOM   169  C CE2 . TRP   A 1 22 ? 3.020   -24.563 1.068   1.00 32.34  ? 21  TRP   A CE2 1 
ATOM   170  C CE3 . TRP   A 1 22 ? 0.638   -24.765 1.437   1.00 33.55  ? 21  TRP   A CE3 1 
ATOM   171  C CZ2 . TRP   A 1 22 ? 3.220   -25.926 1.326   1.00 38.03  ? 21  TRP   A CZ2 1 
ATOM   172  C CZ3 . TRP   A 1 22 ? 0.838   -26.107 1.665   1.00 37.32  ? 21  TRP   A CZ3 1 
ATOM   173  C CH2 . TRP   A 1 22 ? 2.113   -26.679 1.657   1.00 38.46  ? 21  TRP   A CH2 1 
ATOM   174  N N   . PRO   A 1 23 ? 3.040   -19.558 2.588   1.00 27.23  ? 22  PRO   A N   1 
ATOM   175  C CA  . PRO   A 1 23 ? 4.065   -18.526 2.432   1.00 25.69  ? 22  PRO   A CA  1 
ATOM   176  C C   . PRO   A 1 23 ? 4.523   -18.483 0.973   1.00 23.09  ? 22  PRO   A C   1 
ATOM   177  O O   . PRO   A 1 23 ? 4.790   -19.530 0.415   1.00 25.11  ? 22  PRO   A O   1 
ATOM   178  C CB  . PRO   A 1 23 ? 5.192   -18.992 3.423   1.00 21.96  ? 22  PRO   A CB  1 
ATOM   179  C CG  . PRO   A 1 23 ? 4.903   -20.488 3.642   1.00 21.78  ? 22  PRO   A CG  1 
ATOM   180  C CD  . PRO   A 1 23 ? 3.386   -20.568 3.600   1.00 25.61  ? 22  PRO   A CD  1 
ATOM   181  N N   . ALA   A 1 24 ? 4.686   -17.270 0.423   1.00 22.24  ? 23  ALA   A N   1 
ATOM   182  C CA  . ALA   A 1 24 ? 4.941   -17.101 -1.012  1.00 23.31  ? 23  ALA   A CA  1 
ATOM   183  C C   . ALA   A 1 24 ? 5.510   -15.707 -1.323  1.00 20.51  ? 23  ALA   A C   1 
ATOM   184  O O   . ALA   A 1 24 ? 5.618   -14.863 -0.440  1.00 22.82  ? 23  ALA   A O   1 
ATOM   185  C CB  . ALA   A 1 24 ? 3.655   -17.401 -1.782  1.00 25.86  ? 23  ALA   A CB  1 
ATOM   186  N N   . ARG   A 1 25 ? 6.052   -15.525 -2.549  1.00 23.43  ? 24  ARG   A N   1 
ATOM   187  C CA  . ARG   A 1 25 ? 6.477   -14.218 -2.984  1.00 23.05  ? 24  ARG   A CA  1 
ATOM   188  C C   . ARG   A 1 25 ? 5.973   -14.017 -4.417  1.00 22.67  ? 24  ARG   A C   1 
ATOM   189  O O   . ARG   A 1 25 ? 5.721   -15.015 -5.119  1.00 23.15  ? 24  ARG   A O   1 
ATOM   190  C CB  . ARG   A 1 25 ? 8.021   -14.133 -3.002  1.00 22.03  ? 24  ARG   A CB  1 
ATOM   191  C CG  . ARG   A 1 25 ? 8.710   -15.150 -3.912  1.00 24.17  ? 24  ARG   A CG  1 
ATOM   192  C CD  . ARG   A 1 25 ? 10.206  -15.002 -3.835  1.00 24.00  ? 24  ARG   A CD  1 
ATOM   193  N NE  . ARG   A 1 25 ? 10.902  -15.821 -4.854  1.00 26.62  ? 24  ARG   A NE  1 
ATOM   194  C CZ  . ARG   A 1 25 ? 12.186  -16.176 -4.803  1.00 25.99  ? 24  ARG   A CZ  1 
ATOM   195  N NH1 . ARG   A 1 25 ? 12.909  -16.011 -3.699  1.00 25.97  ? 24  ARG   A NH1 1 
ATOM   196  N NH2 . ARG   A 1 25 ? 12.735  -16.710 -5.880  1.00 25.48  ? 24  ARG   A NH2 1 
ATOM   197  N N   . ILE   A 1 26 ? 5.799   -12.744 -4.804  1.00 22.80  ? 25  ILE   A N   1 
ATOM   198  C CA  . ILE   A 1 26 ? 5.627   -12.320 -6.190  1.00 21.25  ? 25  ILE   A CA  1 
ATOM   199  C C   . ILE   A 1 26 ? 6.994   -12.437 -6.888  1.00 23.67  ? 25  ILE   A C   1 
ATOM   200  O O   . ILE   A 1 26 ? 7.937   -11.778 -6.466  1.00 29.93  ? 25  ILE   A O   1 
ATOM   201  C CB  . ILE   A 1 26 ? 5.129   -10.860 -6.296  1.00 26.17  ? 25  ILE   A CB  1 
ATOM   202  C CG1 . ILE   A 1 26 ? 3.970   -10.508 -5.357  1.00 28.83  ? 25  ILE   A CG1 1 
ATOM   203  C CG2 . ILE   A 1 26 ? 4.818   -10.532 -7.768  1.00 25.19  ? 25  ILE   A CG2 1 
ATOM   204  C CD1 . ILE   A 1 26 ? 2.682   -11.234 -5.604  1.00 31.33  ? 25  ILE   A CD1 1 
ATOM   205  N N   . ASP   A 1 27 ? 7.087   -13.301 -7.916  1.00 26.84  ? 26  ASP   A N   1 
ATOM   206  C CA  . ASP   A 1 27 ? 8.318   -13.490 -8.686  1.00 29.60  ? 26  ASP   A CA  1 
ATOM   207  C C   . ASP   A 1 27 ? 8.409   -12.427 -9.777  1.00 30.46  ? 26  ASP   A C   1 
ATOM   208  O O   . ASP   A 1 27 ? 7.416   -11.776 -10.151 1.00 32.48  ? 26  ASP   A O   1 
ATOM   209  C CB  . ASP   A 1 27 ? 8.392   -14.892 -9.280  1.00 30.46  ? 26  ASP   A CB  1 
ATOM   210  C CG  . ASP   A 1 27 ? 9.261   -15.905 -8.560  1.00 30.52  ? 26  ASP   A CG  1 
ATOM   211  O OD1 . ASP   A 1 27 ? 9.852   -15.565 -7.515  1.00 32.60  ? 26  ASP   A OD1 1 
ATOM   212  O OD2 . ASP   A 1 27 ? 9.392   -17.012 -9.086  1.00 36.61  ? 26  ASP   A OD2 1 
ATOM   213  N N   . ASP   A 1 28 ? 9.651   -12.196 -10.211 1.00 35.58  ? 27  ASP   A N   1 
ATOM   214  C CA  . ASP   A 1 28 ? 9.905   -11.539 -11.477 1.00 36.00  ? 27  ASP   A CA  1 
ATOM   215  C C   . ASP   A 1 28 ? 9.590   -12.525 -12.594 1.00 37.69  ? 27  ASP   A C   1 
ATOM   216  O O   . ASP   A 1 28 ? 9.557   -13.729 -12.391 1.00 41.97  ? 27  ASP   A O   1 
ATOM   217  C CB  . ASP   A 1 28 ? 11.378  -11.165 -11.600 1.00 44.39  ? 27  ASP   A CB  1 
ATOM   218  C CG  . ASP   A 1 28 ? 11.893  -10.191 -10.548 1.00 47.43  ? 27  ASP   A CG  1 
ATOM   219  O OD1 . ASP   A 1 28 ? 11.673  -8.952  -10.721 1.00 45.23  ? 27  ASP   A OD1 1 
ATOM   220  O OD2 . ASP   A 1 28 ? 12.461  -10.681 -9.544  1.00 51.88  ? 27  ASP   A OD2 1 
ATOM   221  N N   . ILE   A 1 29 ? 9.410   -12.010 -13.795 1.00 42.04  ? 28  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 29 ? 9.443   -12.887 -14.952 1.00 38.72  ? 28  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 29 ? 10.831  -12.745 -15.570 1.00 42.35  ? 28  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 29 ? 11.231  -11.621 -15.823 1.00 37.99  ? 28  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 29 ? 8.346   -12.440 -15.913 1.00 41.66  ? 28  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 29 ? 6.982   -12.441 -15.193 1.00 44.91  ? 28  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 29 ? 8.365   -13.356 -17.140 1.00 38.84  ? 28  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 29 ? 6.112   -11.230 -15.494 1.00 39.68  ? 28  ILE   A CD1 1 
ATOM   229  N N   . ALA   A 1 30 ? 11.596  -13.846 -15.675 1.00 33.66  ? 29  ALA   A N   1 
ATOM   230  C CA  . ALA   A 1 30 ? 12.946  -13.802 -16.213 1.00 31.88  ? 29  ALA   A CA  1 
ATOM   231  C C   . ALA   A 1 30 ? 12.875  -13.498 -17.710 1.00 38.69  ? 29  ALA   A C   1 
ATOM   232  O O   . ALA   A 1 30 ? 11.896  -13.824 -18.373 1.00 30.81  ? 29  ALA   A O   1 
ATOM   233  C CB  . ALA   A 1 30 ? 13.649  -15.127 -16.003 1.00 34.99  ? 29  ALA   A CB  1 
ATOM   234  N N   . ASP   A 1 31 ? 13.924  -12.850 -18.243 1.00 37.73  ? 30  ASP   A N   1 
ATOM   235  C CA  . ASP   A 1 31 ? 13.976  -12.731 -19.699 1.00 37.13  ? 30  ASP   A CA  1 
ATOM   236  C C   . ASP   A 1 31 ? 13.663  -14.072 -20.338 1.00 28.10  ? 30  ASP   A C   1 
ATOM   237  O O   . ASP   A 1 31 ? 14.300  -15.078 -20.008 1.00 33.40  ? 30  ASP   A O   1 
ATOM   238  C CB  . ASP   A 1 31 ? 15.359  -12.300 -20.130 1.00 30.23  ? 30  ASP   A CB  1 
ATOM   239  C CG  . ASP   A 1 31 ? 15.560  -10.800 -20.038 1.00 35.93  ? 30  ASP   A CG  1 
ATOM   240  O OD1 . ASP   A 1 31 ? 14.538  -10.094 -20.041 1.00 40.65  ? 30  ASP   A OD1 1 
ATOM   241  O OD2 . ASP   A 1 31 ? 16.718  -10.362 -19.969 1.00 38.17  ? 30  ASP   A OD2 1 
ATOM   242  N N   . GLY   A 1 32 ? 12.736  -14.072 -21.306 1.00 32.71  ? 31  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 32 ? 12.542  -15.261 -22.126 1.00 34.85  ? 31  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 32 ? 11.556  -16.284 -21.550 1.00 42.44  ? 31  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 32 ? 11.257  -17.289 -22.200 1.00 38.04  ? 31  GLY   A O   1 
ATOM   246  N N   . ALA   A 1 33 ? 11.078  -16.030 -20.324 1.00 38.93  ? 32  ALA   A N   1 
ATOM   247  C CA  . ALA   A 1 33 ? 10.243  -16.958 -19.574 1.00 38.27  ? 32  ALA   A CA  1 
ATOM   248  C C   . ALA   A 1 33 ? 8.782   -16.722 -19.903 1.00 36.46  ? 32  ALA   A C   1 
ATOM   249  O O   . ALA   A 1 33 ? 8.402   -15.644 -20.352 1.00 34.13  ? 32  ALA   A O   1 
ATOM   250  C CB  . ALA   A 1 33 ? 10.476  -16.770 -18.074 1.00 37.80  ? 32  ALA   A CB  1 
ATOM   251  N N   . VAL   A 1 34 ? 7.968   -17.750 -19.650 1.00 40.96  ? 33  VAL   A N   1 
ATOM   252  C CA  . VAL   A 1 34 ? 6.547   -17.677 -19.932 1.00 37.73  ? 33  VAL   A CA  1 
ATOM   253  C C   . VAL   A 1 34 ? 5.950   -16.634 -19.004 1.00 37.93  ? 33  VAL   A C   1 
ATOM   254  O O   . VAL   A 1 34 ? 6.271   -16.634 -17.810 1.00 41.34  ? 33  VAL   A O   1 
ATOM   255  C CB  . VAL   A 1 34 ? 5.926   -19.072 -19.701 1.00 45.73  ? 33  VAL   A CB  1 
ATOM   256  C CG1 . VAL   A 1 34 ? 4.410   -19.037 -19.867 1.00 43.77  ? 33  VAL   A CG1 1 
ATOM   257  C CG2 . VAL   A 1 34 ? 6.564   -20.111 -20.631 1.00 41.94  ? 33  VAL   A CG2 1 
ATOM   258  N N   . LYS   A 1 35 ? 5.119   -15.758 -19.588 1.00 36.40  ? 34  LYS   A N   1 
ATOM   259  C CA  . LYS   A 1 35 ? 4.476   -14.645 -18.900 1.00 39.01  ? 34  LYS   A CA  1 
ATOM   260  C C   . LYS   A 1 35 ? 3.138   -15.124 -18.338 1.00 45.75  ? 34  LYS   A C   1 
ATOM   261  O O   . LYS   A 1 35 ? 2.565   -16.096 -18.828 1.00 37.45  ? 34  LYS   A O   1 
ATOM   262  C CB  . LYS   A 1 35 ? 4.160   -13.443 -19.792 1.00 38.53  ? 34  LYS   A CB  1 
ATOM   263  C CG  . LYS   A 1 35 ? 5.381   -12.711 -20.400 1.00 38.31  ? 34  LYS   A CG  1 
ATOM   264  C CD  . LYS   A 1 35 ? 4.987   -11.504 -21.245 1.00 44.21  ? 34  LYS   A CD  1 
ATOM   265  C CE  . LYS   A 1 35 ? 4.229   -11.871 -22.491 1.00 49.97  ? 34  LYS   A CE  1 
ATOM   266  N NZ  . LYS   A 1 35 ? 4.514   -10.863 -23.515 1.00 52.23  ? 34  LYS   A NZ  1 
ATOM   267  N N   . PRO   A 1 36 ? 2.632   -14.520 -17.243 1.00 40.32  ? 35  PRO   A N   1 
ATOM   268  C CA  . PRO   A 1 36 ? 1.295   -14.870 -16.757 1.00 39.37  ? 35  PRO   A CA  1 
ATOM   269  C C   . PRO   A 1 36 ? 0.194   -14.279 -17.630 1.00 35.73  ? 35  PRO   A C   1 
ATOM   270  O O   . PRO   A 1 36 ? 0.411   -13.346 -18.397 1.00 39.87  ? 35  PRO   A O   1 
ATOM   271  C CB  . PRO   A 1 36 ? 1.204   -14.340 -15.317 1.00 46.11  ? 35  PRO   A CB  1 
ATOM   272  C CG  . PRO   A 1 36 ? 2.422   -13.472 -15.150 1.00 44.77  ? 35  PRO   A CG  1 
ATOM   273  C CD  . PRO   A 1 36 ? 3.351   -13.595 -16.368 1.00 43.70  ? 35  PRO   A CD  1 
ATOM   274  N N   . PRO   A 1 37 ? -1.073  -14.698 -17.450 1.00 41.61  ? 36  PRO   A N   1 
ATOM   275  C CA  . PRO   A 1 37 ? -2.187  -13.970 -18.059 1.00 36.13  ? 36  PRO   A CA  1 
ATOM   276  C C   . PRO   A 1 37 ? -2.347  -12.558 -17.521 1.00 39.84  ? 36  PRO   A C   1 
ATOM   277  O O   . PRO   A 1 37 ? -1.876  -12.232 -16.434 1.00 36.06  ? 36  PRO   A O   1 
ATOM   278  C CB  . PRO   A 1 37 ? -3.435  -14.843 -17.671 1.00 39.90  ? 36  PRO   A CB  1 
ATOM   279  C CG  . PRO   A 1 37 ? -2.864  -16.186 -17.285 1.00 37.19  ? 36  PRO   A CG  1 
ATOM   280  C CD  . PRO   A 1 37 ? -1.484  -15.903 -16.706 1.00 37.87  ? 36  PRO   A CD  1 
ATOM   281  N N   . PRO   A 1 38 ? -3.123  -11.716 -18.229 1.00 37.24  ? 37  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 38 ? -3.573  -10.419 -17.701 1.00 40.06  ? 37  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 38 ? -4.166  -10.454 -16.292 1.00 38.42  ? 37  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 38 ? -4.852  -11.399 -15.914 1.00 35.93  ? 37  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 38 ? -4.600  -9.932  -18.740 1.00 41.49  ? 37  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 38 ? -4.927  -11.174 -19.579 1.00 42.69  ? 37  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 38 ? -3.647  -12.011 -19.583 1.00 43.78  ? 37  PRO   A CD  1 
ATOM   288  N N   . ASN   A 1 39 ? -3.861  -9.390  -15.541 1.00 35.00  ? 38  ASN   A N   1 
ATOM   289  C CA  . ASN   A 1 39 ? -4.199  -9.171  -14.144 1.00 43.28  ? 38  ASN   A CA  1 
ATOM   290  C C   . ASN   A 1 39 ? -3.721  -10.273 -13.200 1.00 41.92  ? 38  ASN   A C   1 
ATOM   291  O O   . ASN   A 1 39 ? -4.203  -10.283 -12.064 1.00 44.93  ? 38  ASN   A O   1 
ATOM   292  C CB  . ASN   A 1 39 ? -5.694  -8.982  -13.895 1.00 56.72  ? 38  ASN   A CB  1 
ATOM   293  C CG  . ASN   A 1 39 ? -6.285  -7.899  -14.759 1.00 56.64  ? 38  ASN   A CG  1 
ATOM   294  O OD1 . ASN   A 1 39 ? -5.645  -6.866  -14.997 1.00 59.46  ? 38  ASN   A OD1 1 
ATOM   295  N ND2 . ASN   A 1 39 ? -7.484  -8.146  -15.261 1.00 54.18  ? 38  ASN   A ND2 1 
ATOM   296  N N   . LYS   A 1 40 ? -2.814  -11.180 -13.635 1.00 34.38  ? 39  LYS   A N   1 
ATOM   297  C CA  . LYS   A 1 40 ? -2.303  -12.226 -12.742 1.00 32.43  ? 39  LYS   A CA  1 
ATOM   298  C C   . LYS   A 1 40 ? -0.805  -12.007 -12.493 1.00 29.59  ? 39  LYS   A C   1 
ATOM   299  O O   . LYS   A 1 40 ? -0.135  -11.444 -13.355 1.00 34.66  ? 39  LYS   A O   1 
ATOM   300  C CB  . LYS   A 1 40 ? -2.505  -13.658 -13.257 1.00 32.61  ? 39  LYS   A CB  1 
ATOM   301  C CG  . LYS   A 1 40 ? -3.927  -13.997 -13.768 1.00 35.16  ? 39  LYS   A CG  1 
ATOM   302  C CD  . LYS   A 1 40 ? -4.921  -13.776 -12.640 1.00 34.02  ? 39  LYS   A CD  1 
ATOM   303  C CE  . LYS   A 1 40 ? -6.350  -14.208 -12.937 1.00 41.07  ? 39  LYS   A CE  1 
ATOM   304  N NZ  . LYS   A 1 40 ? -6.469  -15.657 -12.741 1.00 44.58  ? 39  LYS   A NZ  1 
ATOM   305  N N   . TYR   A 1 41 ? -0.305  -12.535 -11.351 1.00 24.84  ? 40  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 41 ? 1.095   -12.505 -10.968 1.00 23.08  ? 40  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 41 ? 1.685   -13.904 -10.901 1.00 24.27  ? 40  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 41 ? 1.021   -14.866 -10.540 1.00 26.12  ? 40  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 41 ? 1.103   -11.929 -9.550  1.00 23.63  ? 40  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 41 ? 0.659   -10.476 -9.523  1.00 25.16  ? 40  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 41 ? -0.691  -10.133 -9.417  1.00 30.45  ? 40  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 41 ? 1.570   -9.439  -9.699  1.00 27.18  ? 40  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 41 ? -1.111  -8.807  -9.401  1.00 28.37  ? 40  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 41 ? 1.160   -8.109  -9.732  1.00 30.66  ? 40  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 41 ? -0.192  -7.798  -9.591  1.00 31.63  ? 40  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 41 ? -0.604  -6.479  -9.612  1.00 35.39  ? 40  TYR   A OH  1 
ATOM   317  N N   . PRO   A 1 42 ? 3.012   -14.059 -11.137 1.00 22.39  ? 41  PRO   A N   1 
ATOM   318  C CA  . PRO   A 1 42 ? 3.654   -15.355 -10.949 1.00 20.44  ? 41  PRO   A CA  1 
ATOM   319  C C   . PRO   A 1 42 ? 3.963   -15.498 -9.458  1.00 22.28  ? 41  PRO   A C   1 
ATOM   320  O O   . PRO   A 1 42 ? 4.642   -14.637 -8.879  1.00 28.28  ? 41  PRO   A O   1 
ATOM   321  C CB  . PRO   A 1 42 ? 4.942   -15.230 -11.781 1.00 22.56  ? 41  PRO   A CB  1 
ATOM   322  C CG  . PRO   A 1 42 ? 5.186   -13.746 -11.924 1.00 27.37  ? 41  PRO   A CG  1 
ATOM   323  C CD  . PRO   A 1 42 ? 3.922   -12.971 -11.534 1.00 26.62  ? 41  PRO   A CD  1 
ATOM   324  N N   . ILE   A 1 43 ? 3.330   -16.480 -8.808  1.00 21.27  ? 42  ILE   A N   1 
ATOM   325  C CA  . ILE   A 1 43 ? 3.527   -16.698 -7.360  1.00 21.54  ? 42  ILE   A CA  1 
ATOM   326  C C   . ILE   A 1 43 ? 4.475   -17.867 -7.168  1.00 25.23  ? 42  ILE   A C   1 
ATOM   327  O O   . ILE   A 1 43 ? 4.184   -18.979 -7.605  1.00 26.88  ? 42  ILE   A O   1 
ATOM   328  C CB  . ILE   A 1 43 ? 2.164   -16.966 -6.686  1.00 21.27  ? 42  ILE   A CB  1 
ATOM   329  C CG1 . ILE   A 1 43 ? 1.185   -15.866 -7.063  1.00 21.47  ? 42  ILE   A CG1 1 
ATOM   330  C CG2 . ILE   A 1 43 ? 2.269   -17.152 -5.151  1.00 22.05  ? 42  ILE   A CG2 1 
ATOM   331  C CD1 . ILE   A 1 43 ? 1.579   -14.465 -6.593  1.00 25.27  ? 42  ILE   A CD1 1 
ATOM   332  N N   . PHE   A 1 44 ? 5.626   -17.619 -6.491  1.00 25.35  ? 43  PHE   A N   1 
ATOM   333  C CA  . PHE   A 1 44 ? 6.497   -18.705 -6.081  1.00 26.86  ? 43  PHE   A CA  1 
ATOM   334  C C   . PHE   A 1 44 ? 6.142   -19.084 -4.645  1.00 25.48  ? 43  PHE   A C   1 
ATOM   335  O O   . PHE   A 1 44 ? 6.206   -18.232 -3.764  1.00 24.36  ? 43  PHE   A O   1 
ATOM   336  C CB  . PHE   A 1 44 ? 7.977   -18.269 -6.159  1.00 23.24  ? 43  PHE   A CB  1 
ATOM   337  C CG  . PHE   A 1 44 ? 8.979   -19.340 -5.729  1.00 27.61  ? 43  PHE   A CG  1 
ATOM   338  C CD1 . PHE   A 1 44 ? 9.351   -20.370 -6.609  1.00 31.84  ? 43  PHE   A CD1 1 
ATOM   339  C CD2 . PHE   A 1 44 ? 9.548   -19.330 -4.454  1.00 31.89  ? 43  PHE   A CD2 1 
ATOM   340  C CE1 . PHE   A 1 44 ? 10.282  -21.322 -6.239  1.00 34.28  ? 43  PHE   A CE1 1 
ATOM   341  C CE2 . PHE   A 1 44 ? 10.475  -20.293 -4.085  1.00 32.98  ? 43  PHE   A CE2 1 
ATOM   342  C CZ  . PHE   A 1 44 ? 10.846  -21.281 -4.977  1.00 30.72  ? 43  PHE   A CZ  1 
ATOM   343  N N   . PHE   A 1 45 ? 5.827   -20.384 -4.408  1.00 24.03  ? 44  PHE   A N   1 
ATOM   344  C CA  . PHE   A 1 45 ? 5.418   -20.917 -3.104  1.00 22.46  ? 44  PHE   A CA  1 
ATOM   345  C C   . PHE   A 1 45 ? 6.666   -21.459 -2.414  1.00 23.74  ? 44  PHE   A C   1 
ATOM   346  O O   . PHE   A 1 45 ? 7.406   -22.278 -3.019  1.00 28.08  ? 44  PHE   A O   1 
ATOM   347  C CB  . PHE   A 1 45 ? 4.403   -22.074 -3.272  1.00 26.63  ? 44  PHE   A CB  1 
ATOM   348  C CG  . PHE   A 1 45 ? 3.035   -21.580 -3.715  1.00 27.29  ? 44  PHE   A CG  1 
ATOM   349  C CD1 . PHE   A 1 45 ? 2.782   -21.296 -5.066  1.00 30.29  ? 44  PHE   A CD1 1 
ATOM   350  C CD2 . PHE   A 1 45 ? 2.030   -21.339 -2.774  1.00 28.87  ? 44  PHE   A CD2 1 
ATOM   351  C CE1 . PHE   A 1 45 ? 1.563   -20.724 -5.446  1.00 28.96  ? 44  PHE   A CE1 1 
ATOM   352  C CE2 . PHE   A 1 45 ? 0.801   -20.775 -3.166  1.00 31.31  ? 44  PHE   A CE2 1 
ATOM   353  C CZ  . PHE   A 1 45 ? 0.553   -20.522 -4.499  1.00 30.41  ? 44  PHE   A CZ  1 
ATOM   354  N N   . PHE   A 1 46 ? 6.950   -20.971 -1.189  1.00 29.19  ? 45  PHE   A N   1 
ATOM   355  C CA  . PHE   A 1 46 ? 8.093   -21.439 -0.421  1.00 28.58  ? 45  PHE   A CA  1 
ATOM   356  C C   . PHE   A 1 46 ? 7.815   -22.885 -0.026  1.00 31.12  ? 45  PHE   A C   1 
ATOM   357  O O   . PHE   A 1 46 ? 6.651   -23.321 0.043   1.00 26.92  ? 45  PHE   A O   1 
ATOM   358  C CB  . PHE   A 1 46 ? 8.503   -20.532 0.754   1.00 24.63  ? 45  PHE   A CB  1 
ATOM   359  C CG  . PHE   A 1 46 ? 8.940   -19.112 0.368   1.00 27.59  ? 45  PHE   A CG  1 
ATOM   360  C CD1 . PHE   A 1 46 ? 10.198  -18.872 -0.219  1.00 23.96  ? 45  PHE   A CD1 1 
ATOM   361  C CD2 . PHE   A 1 46 ? 8.122   -18.011 0.623   1.00 21.76  ? 45  PHE   A CD2 1 
ATOM   362  C CE1 . PHE   A 1 46 ? 10.582  -17.568 -0.567  1.00 26.85  ? 45  PHE   A CE1 1 
ATOM   363  C CE2 . PHE   A 1 46 ? 8.521   -16.699 0.309   1.00 23.29  ? 45  PHE   A CE2 1 
ATOM   364  C CZ  . PHE   A 1 46 ? 9.772   -16.468 -0.295  1.00 22.96  ? 45  PHE   A CZ  1 
ATOM   365  N N   . GLY   A 1 47 ? 8.898   -23.628 0.218   1.00 30.13  ? 46  GLY   A N   1 
ATOM   366  C CA  . GLY   A 1 47 ? 8.738   -25.005 0.655   1.00 35.67  ? 46  GLY   A CA  1 
ATOM   367  C C   . GLY   A 1 47 ? 8.607   -25.945 -0.537  1.00 40.44  ? 46  GLY   A C   1 
ATOM   368  O O   . GLY   A 1 47 ? 9.516   -26.744 -0.772  1.00 42.83  ? 46  GLY   A O   1 
ATOM   369  N N   . THR   A 1 48 ? 7.515   -25.797 -1.302  1.00 38.85  ? 47  THR   A N   1 
ATOM   370  C CA  . THR   A 1 48 ? 7.206   -26.622 -2.469  1.00 37.31  ? 47  THR   A CA  1 
ATOM   371  C C   . THR   A 1 48 ? 8.012   -26.180 -3.688  1.00 40.83  ? 47  THR   A C   1 
ATOM   372  O O   . THR   A 1 48 ? 8.291   -26.978 -4.610  1.00 38.90  ? 47  THR   A O   1 
ATOM   373  C CB  . THR   A 1 48 ? 5.699   -26.589 -2.759  1.00 36.66  ? 47  THR   A CB  1 
ATOM   374  O OG1 . THR   A 1 48 ? 5.373   -25.263 -3.142  1.00 40.37  ? 47  THR   A OG1 1 
ATOM   375  C CG2 . THR   A 1 48 ? 4.840   -26.893 -1.548  1.00 36.39  ? 47  THR   A CG2 1 
ATOM   376  N N   . HIS   A 1 49 ? 8.366   -24.890 -3.693  1.00 31.62  ? 48  HIS   A N   1 
ATOM   377  C CA  . HIS   A 1 49 ? 9.074   -24.267 -4.785  1.00 31.28  ? 48  HIS   A CA  1 
ATOM   378  C C   . HIS   A 1 49 ? 8.258   -24.322 -6.095  1.00 28.23  ? 48  HIS   A C   1 
ATOM   379  O O   . HIS   A 1 49 ? 8.830   -24.210 -7.172  1.00 31.10  ? 48  HIS   A O   1 
ATOM   380  C CB  . HIS   A 1 49 ? 10.489  -24.859 -4.863  1.00 32.33  ? 48  HIS   A CB  1 
ATOM   381  C CG  . HIS   A 1 49 ? 11.175  -24.867 -3.530  1.00 35.62  ? 48  HIS   A CG  1 
ATOM   382  N ND1 . HIS   A 1 49 ? 12.064  -25.849 -3.167  1.00 35.85  ? 48  HIS   A ND1 1 
ATOM   383  C CD2 . HIS   A 1 49 ? 11.162  -23.982 -2.498  1.00 34.99  ? 48  HIS   A CD2 1 
ATOM   384  C CE1 . HIS   A 1 49 ? 12.535  -25.595 -1.940  1.00 41.79  ? 48  HIS   A CE1 1 
ATOM   385  N NE2 . HIS   A 1 49 ? 12.055  -24.441 -1.540  1.00 36.28  ? 48  HIS   A NE2 1 
ATOM   386  N N   . GLU   A 1 50 ? 6.946   -24.568 -6.015  1.00 35.38  ? 49  GLU   A N   1 
ATOM   387  C CA  . GLU   A 1 50 ? 6.059   -24.592 -7.182  1.00 37.12  ? 49  GLU   A CA  1 
ATOM   388  C C   . GLU   A 1 50 ? 5.636   -23.164 -7.511  1.00 32.52  ? 49  GLU   A C   1 
ATOM   389  O O   . GLU   A 1 50 ? 5.716   -22.324 -6.632  1.00 31.46  ? 49  GLU   A O   1 
ATOM   390  C CB  . GLU   A 1 50 ? 4.719   -25.248 -6.845  1.00 39.92  ? 49  GLU   A CB  1 
ATOM   391  C CG  . GLU   A 1 50 ? 4.737   -26.767 -6.683  1.00 51.99  ? 49  GLU   A CG  1 
ATOM   392  C CD  . GLU   A 1 50 ? 3.436   -27.224 -6.020  1.00 63.74  ? 49  GLU   A CD  1 
ATOM   393  O OE1 . GLU   A 1 50 ? 2.511   -26.389 -5.821  1.00 56.40  ? 49  GLU   A OE1 1 
ATOM   394  O OE2 . GLU   A 1 50 ? 3.359   -28.419 -5.656  1.00 71.46  ? 49  GLU   A OE2 1 
ATOM   395  N N   . THR   A 1 51 ? 5.272   -22.879 -8.777  1.00 34.71  ? 50  THR   A N   1 
ATOM   396  C CA  . THR   A 1 51 ? 4.759   -21.582 -9.226  1.00 32.94  ? 50  THR   A CA  1 
ATOM   397  C C   . THR   A 1 51 ? 3.289   -21.746 -9.624  1.00 36.02  ? 50  THR   A C   1 
ATOM   398  O O   . THR   A 1 51 ? 2.936   -22.778 -10.183 1.00 37.52  ? 50  THR   A O   1 
ATOM   399  C CB  . THR   A 1 51 ? 5.582   -20.992 -10.388 1.00 36.15  ? 50  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 51 ? 6.903   -20.659 -9.937  1.00 36.79  ? 50  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 51 ? 4.947   -19.746 -10.998 1.00 31.25  ? 50  THR   A CG2 1 
ATOM   402  N N   . ALA   A 1 52 ? 2.449   -20.740 -9.335  1.00 27.38  ? 51  ALA   A N   1 
ATOM   403  C CA  . ALA   A 1 52 ? 1.127   -20.624 -9.955  1.00 28.70  ? 51  ALA   A CA  1 
ATOM   404  C C   . ALA   A 1 52 ? 0.820   -19.149 -10.214 1.00 29.45  ? 51  ALA   A C   1 
ATOM   405  O O   . ALA   A 1 52 ? 1.536   -18.259 -9.733  1.00 28.27  ? 51  ALA   A O   1 
ATOM   406  C CB  . ALA   A 1 52 ? 0.007   -21.326 -9.146  1.00 28.48  ? 51  ALA   A CB  1 
ATOM   407  N N   . PHE   A 1 53 ? -0.183  -18.903 -11.079 1.00 22.40  ? 52  PHE   A N   1 
ATOM   408  C CA  . PHE   A 1 53 ? -0.566  -17.555 -11.419 1.00 26.01  ? 52  PHE   A CA  1 
ATOM   409  C C   . PHE   A 1 53 ? -1.844  -17.221 -10.670 1.00 30.82  ? 52  PHE   A C   1 
ATOM   410  O O   . PHE   A 1 53 ? -2.866  -17.855 -10.884 1.00 31.91  ? 52  PHE   A O   1 
ATOM   411  C CB  . PHE   A 1 53 ? -0.848  -17.560 -12.922 1.00 25.02  ? 52  PHE   A CB  1 
ATOM   412  C CG  . PHE   A 1 53 ? 0.381   -17.853 -13.784 1.00 30.70  ? 52  PHE   A CG  1 
ATOM   413  C CD1 . PHE   A 1 53 ? 1.603   -17.231 -13.529 1.00 32.74  ? 52  PHE   A CD1 1 
ATOM   414  C CD2 . PHE   A 1 53 ? 0.284   -18.661 -14.920 1.00 35.15  ? 52  PHE   A CD2 1 
ATOM   415  C CE1 . PHE   A 1 53 ? 2.697   -17.456 -14.361 1.00 43.19  ? 52  PHE   A CE1 1 
ATOM   416  C CE2 . PHE   A 1 53 ? 1.388   -18.907 -15.728 1.00 36.37  ? 52  PHE   A CE2 1 
ATOM   417  C CZ  . PHE   A 1 53 ? 2.588   -18.301 -15.454 1.00 39.16  ? 52  PHE   A CZ  1 
ATOM   418  N N   . LEU   A 1 54 ? -1.775  -16.193 -9.816  1.00 28.13  ? 53  LEU   A N   1 
ATOM   419  C CA  . LEU   A 1 54 ? -2.909  -15.809 -9.003  1.00 23.33  ? 53  LEU   A CA  1 
ATOM   420  C C   . LEU   A 1 54 ? -3.180  -14.320 -9.144  1.00 28.70  ? 53  LEU   A C   1 
ATOM   421  O O   . LEU   A 1 54 ? -2.289  -13.541 -9.432  1.00 26.11  ? 53  LEU   A O   1 
ATOM   422  C CB  . LEU   A 1 54 ? -2.574  -16.114 -7.540  1.00 23.44  ? 53  LEU   A CB  1 
ATOM   423  C CG  . LEU   A 1 54 ? -2.512  -17.601 -7.211  1.00 28.65  ? 53  LEU   A CG  1 
ATOM   424  C CD1 . LEU   A 1 54 ? -2.088  -17.686 -5.747  1.00 31.13  ? 53  LEU   A CD1 1 
ATOM   425  C CD2 . LEU   A 1 54 ? -3.980  -18.002 -7.395  1.00 33.48  ? 53  LEU   A CD2 1 
ATOM   426  N N   . GLY   A 1 55 ? -4.426  -13.917 -8.882  1.00 24.23  ? 54  GLY   A N   1 
ATOM   427  C CA  . GLY   A 1 55 ? -4.696  -12.481 -8.824  1.00 23.41  ? 54  GLY   A CA  1 
ATOM   428  C C   . GLY   A 1 55 ? -4.798  -12.013 -7.368  1.00 23.27  ? 54  GLY   A C   1 
ATOM   429  O O   . GLY   A 1 55 ? -4.697  -12.809 -6.432  1.00 23.81  ? 54  GLY   A O   1 
ATOM   430  N N   . PRO   A 1 56 ? -4.802  -10.686 -7.142  1.00 25.78  ? 55  PRO   A N   1 
ATOM   431  C CA  . PRO   A 1 56 ? -4.750  -10.095 -5.802  1.00 25.11  ? 55  PRO   A CA  1 
ATOM   432  C C   . PRO   A 1 56 ? -5.746  -10.530 -4.750  1.00 25.76  ? 55  PRO   A C   1 
ATOM   433  O O   . PRO   A 1 56 ? -5.450  -10.525 -3.564  1.00 24.01  ? 55  PRO   A O   1 
ATOM   434  C CB  . PRO   A 1 56 ? -4.979  -8.633  -6.128  1.00 24.01  ? 55  PRO   A CB  1 
ATOM   435  C CG  . PRO   A 1 56 ? -4.280  -8.426  -7.494  1.00 24.51  ? 55  PRO   A CG  1 
ATOM   436  C CD  . PRO   A 1 56 ? -4.771  -9.670  -8.196  1.00 25.09  ? 55  PRO   A CD  1 
ATOM   437  N N   . LYS   A 1 57 ? -6.931  -10.948 -5.197  1.00 29.55  ? 56  LYS   A N   1 
ATOM   438  C CA  . LYS   A 1 57 ? -7.863  -11.496 -4.207  1.00 26.66  ? 56  LYS   A CA  1 
ATOM   439  C C   . LYS   A 1 57 ? -7.304  -12.738 -3.467  1.00 30.39  ? 56  LYS   A C   1 
ATOM   440  O O   . LYS   A 1 57 ? -7.792  -13.071 -2.387  1.00 27.96  ? 56  LYS   A O   1 
ATOM   441  C CB  . LYS   A 1 57 ? -9.187  -11.883 -4.891  1.00 33.70  ? 56  LYS   A CB  1 
ATOM   442  C CG  . LYS   A 1 57 ? -9.050  -13.204 -5.643  1.00 33.35  ? 56  LYS   A CG  1 
ATOM   443  N N   . ASP   A 1 58 ? -6.241  -13.393 -3.979  1.00 25.29  ? 57  ASP   A N   1 
ATOM   444  C CA  . ASP   A 1 58 ? -5.694  -14.577 -3.329  1.00 26.49  ? 57  ASP   A CA  1 
ATOM   445  C C   . ASP   A 1 58 ? -4.361  -14.336 -2.590  1.00 23.08  ? 57  ASP   A C   1 
ATOM   446  O O   . ASP   A 1 58 ? -3.767  -15.313 -2.108  1.00 26.31  ? 57  ASP   A O   1 
ATOM   447  C CB  . ASP   A 1 58 ? -5.623  -15.714 -4.325  1.00 29.81  ? 57  ASP   A CB  1 
ATOM   448  C CG  . ASP   A 1 58 ? -7.018  -16.231 -4.658  1.00 34.95  ? 57  ASP   A CG  1 
ATOM   449  O OD1 . ASP   A 1 58 ? -7.860  -16.200 -3.739  1.00 34.23  ? 57  ASP   A OD1 1 
ATOM   450  O OD2 . ASP   A 1 58 ? -7.277  -16.553 -5.829  1.00 31.70  ? 57  ASP   A OD2 1 
ATOM   451  N N   . LEU   A 1 59 ? -3.976  -13.053 -2.471  1.00 24.96  ? 58  LEU   A N   1 
ATOM   452  C CA  . LEU   A 1 59 ? -2.650  -12.619 -2.026  1.00 23.67  ? 58  LEU   A CA  1 
ATOM   453  C C   . LEU   A 1 59 ? -2.816  -11.771 -0.768  1.00 20.27  ? 58  LEU   A C   1 
ATOM   454  O O   . LEU   A 1 59 ? -3.416  -10.698 -0.792  1.00 23.92  ? 58  LEU   A O   1 
ATOM   455  C CB  . LEU   A 1 59 ? -1.919  -11.855 -3.143  1.00 23.85  ? 58  LEU   A CB  1 
ATOM   456  C CG  . LEU   A 1 59 ? -1.819  -12.599 -4.478  1.00 26.39  ? 58  LEU   A CG  1 
ATOM   457  C CD1 . LEU   A 1 59 ? -1.010  -11.825 -5.502  1.00 24.79  ? 58  LEU   A CD1 1 
ATOM   458  C CD2 . LEU   A 1 59 ? -1.148  -13.926 -4.257  1.00 23.75  ? 58  LEU   A CD2 1 
ATOM   459  N N   . PHE   A 1 60 ? -2.236  -12.247 0.339   1.00 22.77  ? 59  PHE   A N   1 
ATOM   460  C CA  . PHE   A 1 60 ? -2.350  -11.583 1.629   1.00 25.26  ? 59  PHE   A CA  1 
ATOM   461  C C   . PHE   A 1 60 ? -0.954  -11.131 2.050   1.00 23.57  ? 59  PHE   A C   1 
ATOM   462  O O   . PHE   A 1 60 ? -0.100  -11.983 2.320   1.00 24.22  ? 59  PHE   A O   1 
ATOM   463  C CB  . PHE   A 1 60 ? -2.838  -12.638 2.611   1.00 25.01  ? 59  PHE   A CB  1 
ATOM   464  C CG  . PHE   A 1 60 ? -4.276  -13.025 2.341   1.00 27.19  ? 59  PHE   A CG  1 
ATOM   465  C CD1 . PHE   A 1 60 ? -4.603  -13.837 1.267   1.00 30.23  ? 59  PHE   A CD1 1 
ATOM   466  C CD2 . PHE   A 1 60 ? -5.285  -12.635 3.218   1.00 34.48  ? 59  PHE   A CD2 1 
ATOM   467  C CE1 . PHE   A 1 60 ? -5.949  -14.187 1.045   1.00 34.78  ? 59  PHE   A CE1 1 
ATOM   468  C CE2 . PHE   A 1 60 ? -6.612  -12.980 2.987   1.00 31.36  ? 59  PHE   A CE2 1 
ATOM   469  C CZ  . PHE   A 1 60 ? -6.935  -13.765 1.928   1.00 26.30  ? 59  PHE   A CZ  1 
ATOM   470  N N   . PRO   A 1 61 ? -0.672  -9.811  2.052   1.00 25.73  ? 60  PRO   A N   1 
ATOM   471  C CA  . PRO   A 1 61 ? 0.667   -9.322  2.424   1.00 25.69  ? 60  PRO   A CA  1 
ATOM   472  C C   . PRO   A 1 61 ? 1.192   -9.866  3.756   1.00 31.38  ? 60  PRO   A C   1 
ATOM   473  O O   . PRO   A 1 61 ? 0.459   -9.933  4.751   1.00 28.18  ? 60  PRO   A O   1 
ATOM   474  C CB  . PRO   A 1 61 ? 0.439   -7.769  2.488   1.00 28.20  ? 60  PRO   A CB  1 
ATOM   475  C CG  . PRO   A 1 61 ? -0.641  -7.511  1.451   1.00 30.83  ? 60  PRO   A CG  1 
ATOM   476  C CD  . PRO   A 1 61 ? -1.579  -8.738  1.599   1.00 30.89  ? 60  PRO   A CD  1 
ATOM   477  N N   . TYR   A 1 62 ? 2.477   -10.239 3.770   1.00 29.05  ? 61  TYR   A N   1 
ATOM   478  C CA  . TYR   A 1 62 ? 3.057   -11.080 4.809   1.00 25.93  ? 61  TYR   A CA  1 
ATOM   479  C C   . TYR   A 1 62 ? 3.069   -10.376 6.173   1.00 24.29  ? 61  TYR   A C   1 
ATOM   480  O O   . TYR   A 1 62 ? 2.698   -11.004 7.150   1.00 28.72  ? 61  TYR   A O   1 
ATOM   481  C CB  . TYR   A 1 62 ? 4.472   -11.510 4.384   1.00 24.08  ? 61  TYR   A CB  1 
ATOM   482  C CG  . TYR   A 1 62 ? 5.188   -12.276 5.472   1.00 26.27  ? 61  TYR   A CG  1 
ATOM   483  C CD1 . TYR   A 1 62 ? 4.890   -13.629 5.697   1.00 30.56  ? 61  TYR   A CD1 1 
ATOM   484  C CD2 . TYR   A 1 62 ? 6.225   -11.678 6.180   1.00 31.07  ? 61  TYR   A CD2 1 
ATOM   485  C CE1 . TYR   A 1 62 ? 5.560   -14.336 6.678   1.00 35.66  ? 61  TYR   A CE1 1 
ATOM   486  C CE2 . TYR   A 1 62 ? 6.916   -12.394 7.148   1.00 32.80  ? 61  TYR   A CE2 1 
ATOM   487  C CZ  . TYR   A 1 62 ? 6.598   -13.721 7.357   1.00 31.17  ? 61  TYR   A CZ  1 
ATOM   488  O OH  . TYR   A 1 62 ? 7.254   -14.409 8.333   1.00 38.43  ? 61  TYR   A OH  1 
ATOM   489  N N   . ASP   A 1 63 ? 3.399   -9.069  6.233   1.00 26.43  ? 62  ASP   A N   1 
ATOM   490  C CA  . ASP   A 1 63 ? 3.588   -8.473  7.555   1.00 30.26  ? 62  ASP   A CA  1 
ATOM   491  C C   . ASP   A 1 63 ? 2.246   -8.443  8.292   1.00 32.76  ? 62  ASP   A C   1 
ATOM   492  O O   . ASP   A 1 63 ? 2.161   -8.761  9.485   1.00 31.81  ? 62  ASP   A O   1 
ATOM   493  C CB  . ASP   A 1 63 ? 4.230   -7.099  7.488   1.00 35.97  ? 62  ASP   A CB  1 
ATOM   494  C CG  . ASP   A 1 63 ? 5.619   -7.042  6.882   1.00 46.56  ? 62  ASP   A CG  1 
ATOM   495  O OD1 . ASP   A 1 63 ? 6.583   -7.472  7.549   1.00 51.29  ? 62  ASP   A OD1 1 
ATOM   496  O OD2 . ASP   A 1 63 ? 5.720   -6.565  5.742   1.00 65.67  ? 62  ASP   A OD2 1 
ATOM   497  N N   . LYS   A 1 64 ? 1.172   -8.116  7.542   1.00 32.50  ? 63  LYS   A N   1 
ATOM   498  C CA  . LYS   A 1 64 ? -0.178  -8.016  8.106   1.00 32.47  ? 63  LYS   A CA  1 
ATOM   499  C C   . LYS   A 1 64 ? -0.749  -9.370  8.533   1.00 31.37  ? 63  LYS   A C   1 
ATOM   500  O O   . LYS   A 1 64 ? -1.528  -9.421  9.485   1.00 37.16  ? 63  LYS   A O   1 
ATOM   501  C CB  . LYS   A 1 64 ? -1.112  -7.228  7.173   1.00 31.02  ? 63  LYS   A CB  1 
ATOM   502  C CG  . LYS   A 1 64 ? -2.567  -7.131  7.685   1.00 35.17  ? 63  LYS   A CG  1 
ATOM   503  C CD  . LYS   A 1 64 ? -3.475  -6.370  6.729   1.00 31.31  ? 63  LYS   A CD  1 
ATOM   504  C CE  . LYS   A 1 64 ? -4.737  -5.850  7.438   1.00 37.42  ? 63  LYS   A CE  1 
ATOM   505  N NZ  . LYS   A 1 64 ? -5.738  -6.871  7.735   1.00 44.40  ? 63  LYS   A NZ  1 
ATOM   506  N N   . SER   A 1 65 ? -0.372  -10.478 7.889   1.00 30.67  ? 64  SER   A N   1 
ATOM   507  C CA  . SER   A 1 65 ? -1.093  -11.746 8.037   1.00 31.28  ? 64  SER   A CA  1 
ATOM   508  C C   . SER   A 1 65 ? -0.302  -12.863 8.730   1.00 33.23  ? 64  SER   A C   1 
ATOM   509  O O   . SER   A 1 65 ? -0.836  -13.967 8.932   1.00 31.32  ? 64  SER   A O   1 
ATOM   510  C CB  . SER   A 1 65 ? -1.505  -12.249 6.666   1.00 38.69  ? 64  SER   A CB  1 
ATOM   511  O OG  . SER   A 1 65 ? -2.301  -11.274 6.011   1.00 45.79  ? 64  SER   A OG  1 
ATOM   512  N N   . LYS   A 1 66 ? 0.978   -12.621 9.045   1.00 33.42  ? 65  LYS   A N   1 
ATOM   513  C CA  . LYS   A 1 66 ? 1.804   -13.686 9.607   1.00 32.45  ? 65  LYS   A CA  1 
ATOM   514  C C   . LYS   A 1 66 ? 1.358   -14.109 11.002  1.00 31.89  ? 65  LYS   A C   1 
ATOM   515  O O   . LYS   A 1 66 ? 1.564   -15.275 11.354  1.00 36.30  ? 65  LYS   A O   1 
ATOM   516  C CB  . LYS   A 1 66 ? 3.307   -13.379 9.721   1.00 34.12  ? 65  LYS   A CB  1 
ATOM   517  C CG  . LYS   A 1 66 ? 3.698   -12.138 10.494  1.00 34.53  ? 65  LYS   A CG  1 
ATOM   518  C CD  . LYS   A 1 66 ? 5.220   -12.123 10.494  1.00 48.06  ? 65  LYS   A CD  1 
ATOM   519  C CE  . LYS   A 1 66 ? 5.739   -11.015 11.326  1.00 56.75  ? 65  LYS   A CE  1 
ATOM   520  N NZ  . LYS   A 1 66 ? 5.084   -9.763  10.945  1.00 66.36  ? 65  LYS   A NZ  1 
ATOM   521  N N   A ASP   A 1 67 ? 0.782   -13.175 11.775  0.50 35.32  ? 66  ASP   A N   1 
ATOM   522  N N   B ASP   A 1 67 ? 0.757   -13.203 11.779  0.50 35.49  ? 66  ASP   A N   1 
ATOM   523  C CA  A ASP   A 1 67 ? 0.244   -13.484 13.101  0.50 40.97  ? 66  ASP   A CA  1 
ATOM   524  C CA  B ASP   A 1 67 ? 0.275   -13.603 13.099  0.50 40.55  ? 66  ASP   A CA  1 
ATOM   525  C C   A ASP   A 1 67 ? -0.814  -14.585 12.985  0.50 42.10  ? 66  ASP   A C   1 
ATOM   526  C C   B ASP   A 1 67 ? -0.793  -14.679 12.951  0.50 41.74  ? 66  ASP   A C   1 
ATOM   527  O O   A ASP   A 1 67 ? -0.872  -15.491 13.815  0.50 37.79  ? 66  ASP   A O   1 
ATOM   528  O O   B ASP   A 1 67 ? -0.858  -15.627 13.732  0.50 36.08  ? 66  ASP   A O   1 
ATOM   529  C CB  A ASP   A 1 67 ? -0.338  -12.268 13.818  0.50 44.98  ? 66  ASP   A CB  1 
ATOM   530  C CB  B ASP   A 1 67 ? -0.388  -12.480 13.875  0.50 45.12  ? 66  ASP   A CB  1 
ATOM   531  C CG  A ASP   A 1 67 ? 0.610   -11.299 14.529  0.50 49.77  ? 66  ASP   A CG  1 
ATOM   532  C CG  B ASP   A 1 67 ? -0.682  -12.820 15.329  0.50 49.52  ? 66  ASP   A CG  1 
ATOM   533  O OD1 A ASP   A 1 67 ? 1.839   -11.353 14.283  0.50 48.98  ? 66  ASP   A OD1 1 
ATOM   534  O OD1 B ASP   A 1 67 ? 0.272   -12.808 16.130  0.50 51.18  ? 66  ASP   A OD1 1 
ATOM   535  O OD2 A ASP   A 1 67 ? 0.106   -10.489 15.351  0.50 45.14  ? 66  ASP   A OD2 1 
ATOM   536  O OD2 B ASP   A 1 67 ? -1.851  -13.137 15.642  0.50 60.95  ? 66  ASP   A OD2 1 
ATOM   537  N N   . LYS   A 1 68 ? -1.627  -14.519 11.922  1.00 37.94  ? 67  LYS   A N   1 
ATOM   538  C CA  . LYS   A 1 68 ? -2.709  -15.460 11.711  1.00 35.86  ? 67  LYS   A CA  1 
ATOM   539  C C   . LYS   A 1 68 ? -2.263  -16.726 10.991  1.00 35.86  ? 67  LYS   A C   1 
ATOM   540  O O   . LYS   A 1 68 ? -2.689  -17.812 11.363  1.00 33.59  ? 67  LYS   A O   1 
ATOM   541  C CB  . LYS   A 1 68 ? -3.768  -14.814 10.827  1.00 36.26  ? 67  LYS   A CB  1 
ATOM   542  C CG  . LYS   A 1 68 ? -5.040  -15.638 10.665  1.00 39.05  ? 67  LYS   A CG  1 
ATOM   543  C CD  . LYS   A 1 68 ? -6.095  -14.631 10.176  1.00 47.81  ? 67  LYS   A CD  1 
ATOM   544  C CE  . LYS   A 1 68 ? -7.348  -15.213 9.630   1.00 52.01  ? 67  LYS   A CE  1 
ATOM   545  N NZ  . LYS   A 1 68 ? -8.318  -14.181 9.242   1.00 47.98  ? 67  LYS   A NZ  1 
ATOM   546  N N   . TYR   A 1 69 ? -1.516  -16.578 9.882   1.00 32.92  ? 68  TYR   A N   1 
ATOM   547  C CA  . TYR   A 1 69 ? -1.234  -17.703 9.005   1.00 32.92  ? 68  TYR   A CA  1 
ATOM   548  C C   . TYR   A 1 69 ? 0.161   -18.282 9.244   1.00 30.44  ? 68  TYR   A C   1 
ATOM   549  O O   . TYR   A 1 69 ? 0.466   -19.361 8.739   1.00 35.04  ? 68  TYR   A O   1 
ATOM   550  C CB  . TYR   A 1 69 ? -1.374  -17.263 7.532   1.00 26.36  ? 68  TYR   A CB  1 
ATOM   551  C CG  . TYR   A 1 69 ? -2.764  -16.812 7.140   1.00 37.72  ? 68  TYR   A CG  1 
ATOM   552  C CD1 . TYR   A 1 69 ? -3.900  -17.568 7.451   1.00 40.44  ? 68  TYR   A CD1 1 
ATOM   553  C CD2 . TYR   A 1 69 ? -2.938  -15.612 6.450   1.00 39.15  ? 68  TYR   A CD2 1 
ATOM   554  C CE1 . TYR   A 1 69 ? -5.165  -17.123 7.085   1.00 34.34  ? 68  TYR   A CE1 1 
ATOM   555  C CE2 . TYR   A 1 69 ? -4.197  -15.177 6.063   1.00 38.33  ? 68  TYR   A CE2 1 
ATOM   556  C CZ  . TYR   A 1 69 ? -5.313  -15.913 6.421   1.00 36.21  ? 68  TYR   A CZ  1 
ATOM   557  O OH  . TYR   A 1 69 ? -6.547  -15.480 5.996   1.00 34.13  ? 68  TYR   A OH  1 
ATOM   558  N N   . GLY   A 1 70 ? 1.014   -17.586 9.996   1.00 37.33  ? 69  GLY   A N   1 
ATOM   559  C CA  . GLY   A 1 70 ? 2.401   -18.016 10.112  1.00 33.58  ? 69  GLY   A CA  1 
ATOM   560  C C   . GLY   A 1 70 ? 2.592   -19.063 11.212  1.00 41.45  ? 69  GLY   A C   1 
ATOM   561  O O   . GLY   A 1 70 ? 3.289   -18.816 12.188  1.00 45.97  ? 69  GLY   A O   1 
ATOM   562  N N   . LYS   A 1 71 ? 1.968   -20.233 11.044  1.00 42.44  ? 70  LYS   A N   1 
ATOM   563  C CA  . LYS   A 1 71 ? 1.953   -21.266 12.070  1.00 41.70  ? 70  LYS   A CA  1 
ATOM   564  C C   . LYS   A 1 71 ? 2.188   -22.629 11.424  1.00 36.31  ? 70  LYS   A C   1 
ATOM   565  O O   . LYS   A 1 71 ? 1.826   -22.833 10.267  1.00 33.77  ? 70  LYS   A O   1 
ATOM   566  C CB  . LYS   A 1 71 ? 0.662   -21.158 12.897  1.00 42.38  ? 70  LYS   A CB  1 
ATOM   567  C CG  . LYS   A 1 71 ? 0.787   -20.180 14.058  1.00 44.81  ? 70  LYS   A CG  1 
ATOM   568  C CD  . LYS   A 1 71 ? -0.480  -19.909 14.864  1.00 54.63  ? 70  LYS   A CD  1 
ATOM   569  N N   . PRO   A 1 72 ? 2.778   -23.609 12.149  1.00 39.29  ? 71  PRO   A N   1 
ATOM   570  C CA  . PRO   A 1 72 ? 3.151   -24.893 11.548  1.00 39.15  ? 71  PRO   A CA  1 
ATOM   571  C C   . PRO   A 1 72 ? 1.948   -25.640 11.001  1.00 39.70  ? 71  PRO   A C   1 
ATOM   572  O O   . PRO   A 1 72 ? 0.864   -25.508 11.552  1.00 43.53  ? 71  PRO   A O   1 
ATOM   573  C CB  . PRO   A 1 72 ? 3.756   -25.592 12.754  1.00 40.37  ? 71  PRO   A CB  1 
ATOM   574  C CG  . PRO   A 1 72 ? 4.357   -24.453 13.540  1.00 44.73  ? 71  PRO   A CG  1 
ATOM   575  C CD  . PRO   A 1 72 ? 3.156   -23.515 13.568  1.00 44.87  ? 71  PRO   A CD  1 
ATOM   576  N N   . ASN   A 1 73 ? 2.172   -26.391 9.915   1.00 44.71  ? 72  ASN   A N   1 
ATOM   577  C CA  . ASN   A 1 73 ? 1.126   -27.135 9.229   1.00 49.71  ? 72  ASN   A CA  1 
ATOM   578  C C   . ASN   A 1 73 ? 1.674   -28.500 8.816   1.00 54.30  ? 72  ASN   A C   1 
ATOM   579  O O   . ASN   A 1 73 ? 2.856   -28.639 8.468   1.00 46.80  ? 72  ASN   A O   1 
ATOM   580  C CB  . ASN   A 1 73 ? 0.590   -26.368 8.023   1.00 49.10  ? 72  ASN   A CB  1 
ATOM   581  C CG  . ASN   A 1 73 ? -0.775  -26.819 7.555   1.00 50.54  ? 72  ASN   A CG  1 
ATOM   582  O OD1 . ASN   A 1 73 ? -0.879  -27.642 6.641   1.00 53.95  ? 72  ASN   A OD1 1 
ATOM   583  N ND2 . ASN   A 1 73 ? -1.834  -26.255 8.116   1.00 57.15  ? 72  ASN   A ND2 1 
ATOM   584  N N   . LYS   A 1 74 ? 0.757   -29.476 8.792   1.00 49.30  ? 73  LYS   A N   1 
ATOM   585  C CA  . LYS   A 1 74 ? 1.029   -30.869 8.500   1.00 55.21  ? 73  LYS   A CA  1 
ATOM   586  C C   . LYS   A 1 74 ? 1.422   -31.089 7.031   1.00 52.00  ? 73  LYS   A C   1 
ATOM   587  O O   . LYS   A 1 74 ? 2.115   -32.062 6.720   1.00 52.58  ? 73  LYS   A O   1 
ATOM   588  C CB  . LYS   A 1 74 ? -0.153  -31.676 9.067   1.00 64.21  ? 73  LYS   A CB  1 
ATOM   589  C CG  . LYS   A 1 74 ? -1.481  -31.670 8.303   1.00 67.09  ? 73  LYS   A CG  1 
ATOM   590  N N   . ARG   A 1 75 ? 1.045   -30.183 6.119   1.00 44.00  ? 74  ARG   A N   1 
ATOM   591  C CA  . ARG   A 1 75 ? 1.233   -30.431 4.683   1.00 41.26  ? 74  ARG   A CA  1 
ATOM   592  C C   . ARG   A 1 75 ? 2.704   -30.353 4.248   1.00 43.81  ? 74  ARG   A C   1 
ATOM   593  O O   . ARG   A 1 75 ? 3.508   -29.615 4.835   1.00 39.13  ? 74  ARG   A O   1 
ATOM   594  C CB  . ARG   A 1 75 ? 0.446   -29.403 3.863   1.00 45.05  ? 74  ARG   A CB  1 
ATOM   595  C CG  . ARG   A 1 75 ? -0.984  -29.338 4.366   1.00 50.48  ? 74  ARG   A CG  1 
ATOM   596  C CD  . ARG   A 1 75 ? -1.790  -30.480 3.757   1.00 53.52  ? 74  ARG   A CD  1 
ATOM   597  N NE  . ARG   A 1 75 ? -2.547  -30.143 2.546   1.00 61.51  ? 74  ARG   A NE  1 
ATOM   598  C CZ  . ARG   A 1 75 ? -3.700  -29.471 2.580   1.00 60.19  ? 74  ARG   A CZ  1 
ATOM   599  N NH1 . ARG   A 1 75 ? -4.354  -29.225 1.463   1.00 54.89  ? 74  ARG   A NH1 1 
ATOM   600  N NH2 . ARG   A 1 75 ? -4.206  -29.073 3.738   1.00 58.36  ? 74  ARG   A NH2 1 
ATOM   601  N N   . LYS   A 1 76 ? 3.012   -31.078 3.163   1.00 44.11  ? 75  LYS   A N   1 
ATOM   602  C CA  . LYS   A 1 76 ? 4.352   -31.217 2.612   1.00 50.54  ? 75  LYS   A CA  1 
ATOM   603  C C   . LYS   A 1 76 ? 4.882   -29.838 2.223   1.00 44.45  ? 75  LYS   A C   1 
ATOM   604  O O   . LYS   A 1 76 ? 4.232   -29.123 1.464   1.00 43.47  ? 75  LYS   A O   1 
ATOM   605  C CB  . LYS   A 1 76 ? 4.339   -32.143 1.385   1.00 47.04  ? 75  LYS   A CB  1 
ATOM   606  C CG  . LYS   A 1 76 ? 5.693   -32.546 0.799   1.00 51.84  ? 75  LYS   A CG  1 
ATOM   607  C CD  . LYS   A 1 76 ? 5.636   -33.726 -0.173  1.00 54.33  ? 75  LYS   A CD  1 
ATOM   608  C CE  . LYS   A 1 76 ? 6.979   -34.094 -0.716  1.00 63.13  ? 75  LYS   A CE  1 
ATOM   609  N N   . GLY   A 1 77 ? 6.064   -29.488 2.747   1.00 46.90  ? 76  GLY   A N   1 
ATOM   610  C CA  . GLY   A 1 77 ? 6.761   -28.294 2.303   1.00 39.67  ? 76  GLY   A CA  1 
ATOM   611  C C   . GLY   A 1 77 ? 6.367   -27.042 3.085   1.00 34.12  ? 76  GLY   A C   1 
ATOM   612  O O   . GLY   A 1 77 ? 7.089   -26.031 3.027   1.00 38.27  ? 76  GLY   A O   1 
ATOM   613  N N   . PHE   A 1 78 ? 5.286   -27.133 3.871   1.00 32.06  ? 77  PHE   A N   1 
ATOM   614  C CA  . PHE   A 1 78 ? 4.784   -25.948 4.555   1.00 31.68  ? 77  PHE   A CA  1 
ATOM   615  C C   . PHE   A 1 78 ? 5.823   -25.378 5.530   1.00 35.21  ? 77  PHE   A C   1 
ATOM   616  O O   . PHE   A 1 78 ? 6.045   -24.154 5.562   1.00 34.84  ? 77  PHE   A O   1 
ATOM   617  C CB  . PHE   A 1 78 ? 3.456   -26.199 5.282   1.00 31.39  ? 77  PHE   A CB  1 
ATOM   618  C CG  . PHE   A 1 78 ? 2.709   -24.928 5.639   1.00 34.72  ? 77  PHE   A CG  1 
ATOM   619  C CD1 . PHE   A 1 78 ? 2.970   -24.258 6.832   1.00 33.61  ? 77  PHE   A CD1 1 
ATOM   620  C CD2 . PHE   A 1 78 ? 1.749   -24.391 4.763   1.00 34.43  ? 77  PHE   A CD2 1 
ATOM   621  C CE1 . PHE   A 1 78 ? 2.327   -23.051 7.132   1.00 34.58  ? 77  PHE   A CE1 1 
ATOM   622  C CE2 . PHE   A 1 78 ? 1.095   -23.206 5.070   1.00 24.73  ? 77  PHE   A CE2 1 
ATOM   623  C CZ  . PHE   A 1 78 ? 1.371   -22.542 6.269   1.00 28.00  ? 77  PHE   A CZ  1 
ATOM   624  N N   . ASN   A 1 79 ? 6.404   -26.235 6.395   1.00 31.86  ? 78  ASN   A N   1 
ATOM   625  C CA  . ASN   A 1 79 ? 7.231   -25.717 7.486   1.00 30.90  ? 78  ASN   A CA  1 
ATOM   626  C C   . ASN   A 1 79 ? 8.592   -25.308 6.922   1.00 30.71  ? 78  ASN   A C   1 
ATOM   627  O O   . ASN   A 1 79 ? 9.234   -24.367 7.429   1.00 37.07  ? 78  ASN   A O   1 
ATOM   628  C CB  . ASN   A 1 79 ? 7.318   -26.665 8.685   1.00 34.62  ? 78  ASN   A CB  1 
ATOM   629  C CG  . ASN   A 1 79 ? 5.976   -26.935 9.345   1.00 41.62  ? 78  ASN   A CG  1 
ATOM   630  O OD1 . ASN   A 1 79 ? 5.096   -26.066 9.340   1.00 37.94  ? 78  ASN   A OD1 1 
ATOM   631  N ND2 . ASN   A 1 79 ? 5.803   -28.117 9.945   1.00 36.75  ? 78  ASN   A ND2 1 
ATOM   632  N N   . GLU   A 1 80 ? 9.023   -26.013 5.870   1.00 30.38  ? 79  GLU   A N   1 
ATOM   633  C CA  . GLU   A 1 80 ? 10.179  -25.556 5.118   1.00 30.11  ? 79  GLU   A CA  1 
ATOM   634  C C   . GLU   A 1 80 ? 9.880   -24.158 4.586   1.00 32.84  ? 79  GLU   A C   1 
ATOM   635  O O   . GLU   A 1 80 ? 10.705  -23.255 4.662   1.00 28.25  ? 79  GLU   A O   1 
ATOM   636  C CB  . GLU   A 1 80 ? 10.590  -26.517 4.018   1.00 36.24  ? 79  GLU   A CB  1 
ATOM   637  C CG  . GLU   A 1 80 ? 11.846  -26.082 3.263   1.00 35.30  ? 79  GLU   A CG  1 
ATOM   638  C CD  . GLU   A 1 80 ? 12.260  -27.039 2.163   1.00 50.98  ? 79  GLU   A CD  1 
ATOM   639  O OE1 . GLU   A 1 80 ? 11.448  -27.906 1.767   1.00 57.42  ? 79  GLU   A OE1 1 
ATOM   640  O OE2 . GLU   A 1 80 ? 13.421  -26.928 1.713   1.00 53.33  ? 79  GLU   A OE2 1 
ATOM   641  N N   . GLY   A 1 81 ? 8.643   -23.960 4.127   1.00 33.91  ? 80  GLY   A N   1 
ATOM   642  C CA  . GLY   A 1 81 ? 8.288   -22.677 3.525   1.00 31.83  ? 80  GLY   A CA  1 
ATOM   643  C C   . GLY   A 1 81 ? 8.290   -21.515 4.509   1.00 27.05  ? 80  GLY   A C   1 
ATOM   644  O O   . GLY   A 1 81 ? 8.654   -20.394 4.137   1.00 26.46  ? 80  GLY   A O   1 
ATOM   645  N N   . LEU   A 1 82 ? 7.861   -21.780 5.749   1.00 26.74  ? 81  LEU   A N   1 
ATOM   646  C CA  . LEU   A 1 82 ? 7.889   -20.807 6.837   1.00 28.74  ? 81  LEU   A CA  1 
ATOM   647  C C   . LEU   A 1 82 ? 9.328   -20.358 7.130   1.00 27.05  ? 81  LEU   A C   1 
ATOM   648  O O   . LEU   A 1 82 ? 9.562   -19.165 7.331   1.00 25.60  ? 81  LEU   A O   1 
ATOM   649  C CB  . LEU   A 1 82 ? 7.167   -21.224 8.124   1.00 30.52  ? 81  LEU   A CB  1 
ATOM   650  C CG  . LEU   A 1 82 ? 5.687   -21.623 8.047   1.00 30.19  ? 81  LEU   A CG  1 
ATOM   651  C CD1 . LEU   A 1 82 ? 5.346   -21.977 9.458   1.00 29.57  ? 81  LEU   A CD1 1 
ATOM   652  C CD2 . LEU   A 1 82 ? 4.711   -20.502 7.683   1.00 30.06  ? 81  LEU   A CD2 1 
ATOM   653  N N   . TRP   A 1 83 ? 10.280  -21.290 7.084   1.00 30.55  ? 82  TRP   A N   1 
ATOM   654  C CA  . TRP   A 1 83 ? 11.669  -20.928 7.334   1.00 32.62  ? 82  TRP   A CA  1 
ATOM   655  C C   . TRP   A 1 83 ? 12.153  -19.971 6.240   1.00 28.48  ? 82  TRP   A C   1 
ATOM   656  O O   . TRP   A 1 83 ? 12.743  -18.929 6.550   1.00 29.51  ? 82  TRP   A O   1 
ATOM   657  C CB  . TRP   A 1 83 ? 12.588  -22.156 7.525   1.00 32.28  ? 82  TRP   A CB  1 
ATOM   658  C CG  . TRP   A 1 83 ? 14.045  -21.797 7.738   1.00 29.19  ? 82  TRP   A CG  1 
ATOM   659  C CD1 . TRP   A 1 83 ? 14.707  -21.639 8.921   1.00 31.54  ? 82  TRP   A CD1 1 
ATOM   660  C CD2 . TRP   A 1 83 ? 14.987  -21.465 6.709   1.00 28.94  ? 82  TRP   A CD2 1 
ATOM   661  N NE1 . TRP   A 1 83 ? 16.013  -21.285 8.692   1.00 33.42  ? 82  TRP   A NE1 1 
ATOM   662  C CE2 . TRP   A 1 83 ? 16.208  -21.154 7.337   1.00 32.33  ? 82  TRP   A CE2 1 
ATOM   663  C CE3 . TRP   A 1 83 ? 14.901  -21.416 5.314   1.00 28.86  ? 82  TRP   A CE3 1 
ATOM   664  C CZ2 . TRP   A 1 83 ? 17.353  -20.796 6.617   1.00 30.87  ? 82  TRP   A CZ2 1 
ATOM   665  C CZ3 . TRP   A 1 83 ? 16.026  -21.070 4.600   1.00 27.62  ? 82  TRP   A CZ3 1 
ATOM   666  C CH2 . TRP   A 1 83 ? 17.236  -20.756 5.245   1.00 37.13  ? 82  TRP   A CH2 1 
ATOM   667  N N   . GLU   A 1 84 ? 11.855  -20.319 4.976   1.00 26.70  ? 83  GLU   A N   1 
ATOM   668  C CA  . GLU   A 1 84 ? 12.399  -19.601 3.836   1.00 28.65  ? 83  GLU   A CA  1 
ATOM   669  C C   . GLU   A 1 84 ? 11.864  -18.175 3.848   1.00 26.22  ? 83  GLU   A C   1 
ATOM   670  O O   . GLU   A 1 84 ? 12.591  -17.207 3.632   1.00 27.83  ? 83  GLU   A O   1 
ATOM   671  C CB  . GLU   A 1 84 ? 12.025  -20.274 2.525   1.00 25.19  ? 83  GLU   A CB  1 
ATOM   672  C CG  . GLU   A 1 84 ? 12.610  -21.689 2.417   1.00 27.34  ? 83  GLU   A CG  1 
ATOM   673  C CD  . GLU   A 1 84 ? 12.206  -22.362 1.111   1.00 29.13  ? 83  GLU   A CD  1 
ATOM   674  O OE1 . GLU   A 1 84 ? 11.282  -21.892 0.396   1.00 27.90  ? 83  GLU   A OE1 1 
ATOM   675  O OE2 . GLU   A 1 84 ? 12.830  -23.411 0.786   1.00 30.56  ? 83  GLU   A OE2 1 
ATOM   676  N N   . ILE   A 1 85 ? 10.562  -18.038 4.093   1.00 25.02  ? 84  ILE   A N   1 
ATOM   677  C CA  . ILE   A 1 85 ? 9.982   -16.701 4.023   1.00 27.43  ? 84  ILE   A CA  1 
ATOM   678  C C   . ILE   A 1 85 ? 10.519  -15.794 5.137   1.00 26.48  ? 84  ILE   A C   1 
ATOM   679  O O   . ILE   A 1 85 ? 10.607  -14.565 4.956   1.00 24.32  ? 84  ILE   A O   1 
ATOM   680  C CB  . ILE   A 1 85 ? 8.430   -16.732 3.970   1.00 27.00  ? 84  ILE   A CB  1 
ATOM   681  C CG1 . ILE   A 1 85 ? 7.889   -15.312 3.538   1.00 23.52  ? 84  ILE   A CG1 1 
ATOM   682  C CG2 . ILE   A 1 85 ? 7.841   -17.178 5.322   1.00 25.39  ? 84  ILE   A CG2 1 
ATOM   683  C CD1 . ILE   A 1 85 ? 6.433   -15.323 3.076   1.00 24.30  ? 84  ILE   A CD1 1 
ATOM   684  N N   . GLN   A 1 86 ? 10.833  -16.390 6.299   1.00 23.58  ? 85  GLN   A N   1 
ATOM   685  C CA  . GLN   A 1 86 ? 11.310  -15.633 7.453   1.00 27.47  ? 85  GLN   A CA  1 
ATOM   686  C C   . GLN   A 1 86 ? 12.823  -15.366 7.370   1.00 28.74  ? 85  GLN   A C   1 
ATOM   687  O O   . GLN   A 1 86 ? 13.246  -14.301 7.789   1.00 31.46  ? 85  GLN   A O   1 
ATOM   688  C CB  . GLN   A 1 86 ? 10.896  -16.266 8.784   1.00 31.11  ? 85  GLN   A CB  1 
ATOM   689  C CG  . GLN   A 1 86 ? 11.166  -15.422 10.029  1.00 42.82  ? 85  GLN   A CG  1 
ATOM   690  C CD  . GLN   A 1 86 ? 10.490  -15.976 11.273  1.00 47.97  ? 85  GLN   A CD  1 
ATOM   691  O OE1 . GLN   A 1 86 ? 10.070  -17.150 11.325  1.00 45.62  ? 85  GLN   A OE1 1 
ATOM   692  N NE2 . GLN   A 1 86 ? 10.408  -15.133 12.299  1.00 45.26  ? 85  GLN   A NE2 1 
ATOM   693  N N   . ASN   A 1 87 ? 13.605  -16.296 6.797   1.00 28.96  ? 86  ASN   A N   1 
ATOM   694  C CA  . ASN   A 1 87 ? 15.066  -16.307 6.883   1.00 25.70  ? 86  ASN   A CA  1 
ATOM   695  C C   . ASN   A 1 87 ? 15.815  -15.956 5.586   1.00 25.68  ? 86  ASN   A C   1 
ATOM   696  O O   . ASN   A 1 87 ? 16.956  -15.458 5.641   1.00 28.77  ? 86  ASN   A O   1 
ATOM   697  C CB  . ASN   A 1 87 ? 15.500  -17.624 7.493   1.00 29.20  ? 86  ASN   A CB  1 
ATOM   698  C CG  . ASN   A 1 87 ? 14.924  -17.736 8.889   1.00 35.61  ? 86  ASN   A CG  1 
ATOM   699  O OD1 . ASN   A 1 87 ? 15.294  -16.961 9.764   1.00 38.28  ? 86  ASN   A OD1 1 
ATOM   700  N ND2 . ASN   A 1 87 ? 13.998  -18.647 9.103   1.00 36.04  ? 86  ASN   A ND2 1 
ATOM   701  N N   . ASN   A 1 88 ? 15.247  -16.232 4.405   1.00 24.30  ? 87  ASN   A N   1 
ATOM   702  C CA  . ASN   A 1 88 ? 15.925  -15.973 3.137   1.00 23.91  ? 87  ASN   A CA  1 
ATOM   703  C C   . ASN   A 1 88 ? 14.859  -15.911 2.016   1.00 22.08  ? 87  ASN   A C   1 
ATOM   704  O O   . ASN   A 1 88 ? 14.886  -16.628 1.020   1.00 26.81  ? 87  ASN   A O   1 
ATOM   705  C CB  . ASN   A 1 88 ? 17.105  -16.925 2.828   1.00 31.99  ? 87  ASN   A CB  1 
ATOM   706  C CG  . ASN   A 1 88 ? 18.157  -16.309 1.912   1.00 28.61  ? 87  ASN   A CG  1 
ATOM   707  O OD1 . ASN   A 1 88 ? 17.911  -15.255 1.290   1.00 27.88  ? 87  ASN   A OD1 1 
ATOM   708  N ND2 . ASN   A 1 88 ? 19.393  -16.854 1.925   1.00 28.77  ? 87  ASN   A ND2 1 
ATOM   709  N N   . PRO   A 1 89 ? 13.906  -14.955 2.109   1.00 24.34  ? 88  PRO   A N   1 
ATOM   710  C CA  . PRO   A 1 89 ? 12.795  -14.870 1.147   1.00 22.30  ? 88  PRO   A CA  1 
ATOM   711  C C   . PRO   A 1 89 ? 13.125  -14.455 -0.284  1.00 26.63  ? 88  PRO   A C   1 
ATOM   712  O O   . PRO   A 1 89 ? 12.338  -14.694 -1.187  1.00 25.44  ? 88  PRO   A O   1 
ATOM   713  C CB  . PRO   A 1 89 ? 11.847  -13.919 1.861   1.00 24.33  ? 88  PRO   A CB  1 
ATOM   714  C CG  . PRO   A 1 89 ? 12.750  -12.989 2.655   1.00 26.42  ? 88  PRO   A CG  1 
ATOM   715  C CD  . PRO   A 1 89 ? 13.774  -13.988 3.209   1.00 24.55  ? 88  PRO   A CD  1 
ATOM   716  N N   . HIS   A 1 90 ? 14.341  -13.919 -0.509  1.00 25.30  ? 89  HIS   A N   1 
ATOM   717  C CA  . HIS   A 1 90 ? 14.696  -13.388 -1.821  1.00 24.31  ? 89  HIS   A CA  1 
ATOM   718  C C   . HIS   A 1 90 ? 15.834  -14.198 -2.458  1.00 26.97  ? 89  HIS   A C   1 
ATOM   719  O O   . HIS   A 1 90 ? 16.373  -13.771 -3.490  1.00 28.09  ? 89  HIS   A O   1 
ATOM   720  C CB  . HIS   A 1 90 ? 15.116  -11.916 -1.692  1.00 24.21  ? 89  HIS   A CB  1 
ATOM   721  C CG  . HIS   A 1 90 ? 14.061  -11.032 -1.078  1.00 24.29  ? 89  HIS   A CG  1 
ATOM   722  N ND1 . HIS   A 1 90 ? 12.783  -10.894 -1.626  1.00 24.56  ? 89  HIS   A ND1 1 
ATOM   723  C CD2 . HIS   A 1 90 ? 14.014  -10.408 0.102   1.00 25.69  ? 89  HIS   A CD2 1 
ATOM   724  C CE1 . HIS   A 1 90 ? 12.065  -10.087 -0.855  1.00 26.66  ? 89  HIS   A CE1 1 
ATOM   725  N NE2 . HIS   A 1 90 ? 12.782  -9.794  0.214   1.00 28.05  ? 89  HIS   A NE2 1 
ATOM   726  N N   . ALA   A 1 91 ? 16.159  -15.365 -1.875  1.00 27.31  ? 90  ALA   A N   1 
ATOM   727  C CA  . ALA   A 1 91 ? 17.172  -16.278 -2.429  1.00 29.32  ? 90  ALA   A CA  1 
ATOM   728  C C   . ALA   A 1 91 ? 16.732  -16.938 -3.741  1.00 28.44  ? 90  ALA   A C   1 
ATOM   729  O O   . ALA   A 1 91 ? 15.556  -17.011 -4.074  1.00 31.16  ? 90  ALA   A O   1 
ATOM   730  C CB  . ALA   A 1 91 ? 17.518  -17.351 -1.406  1.00 29.76  ? 90  ALA   A CB  1 
ATOM   731  N N   . SER   A 1 92 ? 17.718  -17.446 -4.493  1.00 30.25  ? 91  SER   A N   1 
ATOM   732  C CA  . SER   A 1 92 ? 17.427  -18.332 -5.611  1.00 30.39  ? 91  SER   A CA  1 
ATOM   733  C C   . SER   A 1 92 ? 17.147  -19.732 -5.103  1.00 29.19  ? 91  SER   A C   1 
ATOM   734  O O   . SER   A 1 92 ? 17.955  -20.318 -4.378  1.00 36.57  ? 91  SER   A O   1 
ATOM   735  C CB  . SER   A 1 92 ? 18.536  -18.324 -6.655  1.00 36.81  ? 91  SER   A CB  1 
ATOM   736  O OG  . SER   A 1 92 ? 18.388  -19.492 -7.453  1.00 44.94  ? 91  SER   A OG  1 
ATOM   737  N N   . TYR   A 1 93 ? 15.979  -20.272 -5.450  1.00 30.39  ? 92  TYR   A N   1 
ATOM   738  C CA  . TYR   A 1 93 ? 15.559  -21.589 -4.972  1.00 32.48  ? 92  TYR   A CA  1 
ATOM   739  C C   . TYR   A 1 93 ? 15.454  -22.555 -6.160  1.00 42.32  ? 92  TYR   A C   1 
ATOM   740  O O   . TYR   A 1 93 ? 14.795  -23.588 -6.065  1.00 44.86  ? 92  TYR   A O   1 
ATOM   741  C CB  . TYR   A 1 93 ? 14.206  -21.596 -4.234  1.00 33.00  ? 92  TYR   A CB  1 
ATOM   742  C CG  . TYR   A 1 93 ? 14.302  -21.024 -2.828  1.00 30.37  ? 92  TYR   A CG  1 
ATOM   743  C CD1 . TYR   A 1 93 ? 14.635  -21.819 -1.744  1.00 34.04  ? 92  TYR   A CD1 1 
ATOM   744  C CD2 . TYR   A 1 93 ? 14.123  -19.656 -2.604  1.00 31.23  ? 92  TYR   A CD2 1 
ATOM   745  C CE1 . TYR   A 1 93 ? 14.778  -21.278 -0.468  1.00 35.74  ? 92  TYR   A CE1 1 
ATOM   746  C CE2 . TYR   A 1 93 ? 14.255  -19.111 -1.332  1.00 31.10  ? 92  TYR   A CE2 1 
ATOM   747  C CZ  . TYR   A 1 93 ? 14.612  -19.916 -0.260  1.00 32.53  ? 92  TYR   A CZ  1 
ATOM   748  O OH  . TYR   A 1 93 ? 14.767  -19.351 0.988   1.00 36.38  ? 92  TYR   A OH  1 
ATOM   749  N N   . SER   A 1 94 ? 16.130  -22.205 -7.261  1.00 51.25  ? 93  SER   A N   1 
ATOM   750  C CA  . SER   A 1 94 ? 16.079  -22.918 -8.531  1.00 65.33  ? 93  SER   A CA  1 
ATOM   751  C C   . SER   A 1 94 ? 16.928  -24.202 -8.479  1.00 72.03  ? 93  SER   A C   1 
ATOM   752  O O   . SER   A 1 94 ? 17.529  -24.474 -7.411  1.00 77.72  ? 93  SER   A O   1 
ATOM   753  C CB  . SER   A 1 94 ? 16.545  -22.022 -9.659  1.00 65.87  ? 93  SER   A CB  1 
ATOM   754  O OG  . SER   A 1 94 ? 15.953  -20.731 -9.574  1.00 81.00  ? 93  SER   A OG  1 
ATOM   755  O OXT . SER   A 1 94 ? 16.972  -24.884 -9.526  1.00 74.73  ? 93  SER   A OXT 1 
ATOM   756  N N   . MET   B 1 2  ? 39.268  -11.636 -41.719 1.00 99.07  ? 1   MET   B N   1 
ATOM   757  C CA  . MET   B 1 2  ? 38.897  -12.664 -42.727 1.00 92.38  ? 1   MET   B CA  1 
ATOM   758  C C   . MET   B 1 2  ? 37.374  -12.802 -42.721 1.00 81.73  ? 1   MET   B C   1 
ATOM   759  O O   . MET   B 1 2  ? 36.807  -13.190 -41.702 1.00 80.94  ? 1   MET   B O   1 
ATOM   760  C CB  . MET   B 1 2  ? 39.592  -13.997 -42.402 1.00 98.18  ? 1   MET   B CB  1 
ATOM   761  C CG  . MET   B 1 2  ? 39.824  -14.929 -43.590 1.00 102.80 ? 1   MET   B CG  1 
ATOM   762  S SD  . MET   B 1 2  ? 40.819  -14.243 -44.935 1.00 93.22  ? 1   MET   B SD  1 
ATOM   763  C CE  . MET   B 1 2  ? 42.278  -13.677 -44.045 1.00 92.45  ? 1   MET   B CE  1 
ATOM   764  N N   . PRO   B 1 3  ? 36.662  -12.449 -43.825 1.00 71.80  ? 2   PRO   B N   1 
ATOM   765  C CA  . PRO   B 1 3  ? 35.212  -12.665 -43.902 1.00 69.71  ? 2   PRO   B CA  1 
ATOM   766  C C   . PRO   B 1 3  ? 34.778  -14.077 -43.502 1.00 71.18  ? 2   PRO   B C   1 
ATOM   767  O O   . PRO   B 1 3  ? 35.458  -15.057 -43.816 1.00 70.01  ? 2   PRO   B O   1 
ATOM   768  C CB  . PRO   B 1 3  ? 34.833  -12.313 -45.356 1.00 66.36  ? 2   PRO   B CB  1 
ATOM   769  C CG  . PRO   B 1 3  ? 35.952  -11.382 -45.806 1.00 65.18  ? 2   PRO   B CG  1 
ATOM   770  C CD  . PRO   B 1 3  ? 37.200  -11.790 -45.032 1.00 60.11  ? 2   PRO   B CD  1 
ATOM   771  N N   . HIS   B 1 4  ? 33.653  -14.145 -42.770 1.00 70.17  ? 3   HIS   B N   1 
ATOM   772  C CA  . HIS   B 1 4  ? 33.046  -15.389 -42.312 1.00 67.05  ? 3   HIS   B CA  1 
ATOM   773  C C   . HIS   B 1 4  ? 31.657  -15.559 -42.927 1.00 62.41  ? 3   HIS   B C   1 
ATOM   774  O O   . HIS   B 1 4  ? 31.124  -14.624 -43.533 1.00 61.18  ? 3   HIS   B O   1 
ATOM   775  C CB  . HIS   B 1 4  ? 32.992  -15.418 -40.783 1.00 73.18  ? 3   HIS   B CB  1 
ATOM   776  C CG  . HIS   B 1 4  ? 34.320  -15.674 -40.157 1.00 75.55  ? 3   HIS   B CG  1 
ATOM   777  N ND1 . HIS   B 1 4  ? 35.380  -16.209 -40.860 1.00 77.19  ? 3   HIS   B ND1 1 
ATOM   778  C CD2 . HIS   B 1 4  ? 34.751  -15.471 -38.909 1.00 66.50  ? 3   HIS   B CD2 1 
ATOM   779  C CE1 . HIS   B 1 4  ? 36.417  -16.320 -40.048 1.00 79.27  ? 3   HIS   B CE1 1 
ATOM   780  N NE2 . HIS   B 1 4  ? 36.052  -15.882 -38.858 1.00 76.44  ? 3   HIS   B NE2 1 
ATOM   781  N N   . ALA   B 1 5  ? 31.071  -16.759 -42.778 1.00 49.01  ? 4   ALA   B N   1 
ATOM   782  C CA  . ALA   B 1 5  ? 29.827  -17.039 -43.468 1.00 45.34  ? 4   ALA   B CA  1 
ATOM   783  C C   . ALA   B 1 5  ? 28.783  -16.044 -42.979 1.00 46.68  ? 4   ALA   B C   1 
ATOM   784  O O   . ALA   B 1 5  ? 28.082  -15.433 -43.782 1.00 50.03  ? 4   ALA   B O   1 
ATOM   785  C CB  . ALA   B 1 5  ? 29.400  -18.458 -43.203 1.00 54.36  ? 4   ALA   B CB  1 
ATOM   786  N N   . PHE   B 1 6  ? 28.709  -15.927 -41.649 1.00 45.44  ? 5   PHE   B N   1 
ATOM   787  C CA  . PHE   B 1 6  ? 27.954  -14.903 -40.954 1.00 52.19  ? 5   PHE   B CA  1 
ATOM   788  C C   . PHE   B 1 6  ? 28.884  -13.722 -40.665 1.00 48.40  ? 5   PHE   B C   1 
ATOM   789  O O   . PHE   B 1 6  ? 29.996  -13.925 -40.199 1.00 50.02  ? 5   PHE   B O   1 
ATOM   790  C CB  . PHE   B 1 6  ? 27.402  -15.575 -39.689 1.00 49.53  ? 5   PHE   B CB  1 
ATOM   791  C CG  . PHE   B 1 6  ? 26.205  -16.500 -39.887 1.00 43.19  ? 5   PHE   B CG  1 
ATOM   792  C CD1 . PHE   B 1 6  ? 24.930  -15.975 -40.133 1.00 33.65  ? 5   PHE   B CD1 1 
ATOM   793  C CD2 . PHE   B 1 6  ? 26.352  -17.881 -39.816 1.00 39.12  ? 5   PHE   B CD2 1 
ATOM   794  C CE1 . PHE   B 1 6  ? 23.826  -16.799 -40.275 1.00 36.38  ? 5   PHE   B CE1 1 
ATOM   795  C CE2 . PHE   B 1 6  ? 25.238  -18.708 -39.956 1.00 35.79  ? 5   PHE   B CE2 1 
ATOM   796  C CZ  . PHE   B 1 6  ? 23.980  -18.169 -40.180 1.00 40.42  ? 5   PHE   B CZ  1 
ATOM   797  N N   . LYS   B 1 7  ? 28.419  -12.498 -40.944 1.00 50.27  ? 6   LYS   B N   1 
ATOM   798  C CA  . LYS   B 1 7  ? 29.184  -11.287 -40.661 1.00 49.52  ? 6   LYS   B CA  1 
ATOM   799  C C   . LYS   B 1 7  ? 28.394  -10.369 -39.729 1.00 53.14  ? 6   LYS   B C   1 
ATOM   800  O O   . LYS   B 1 7  ? 27.165  -10.411 -39.726 1.00 46.68  ? 6   LYS   B O   1 
ATOM   801  C CB  . LYS   B 1 7  ? 29.468  -10.556 -41.972 1.00 45.68  ? 6   LYS   B CB  1 
ATOM   802  C CG  . LYS   B 1 7  ? 28.276  -10.176 -42.833 1.00 55.20  ? 6   LYS   B CG  1 
ATOM   803  C CD  . LYS   B 1 7  ? 28.660  -9.650  -44.214 1.00 62.00  ? 6   LYS   B CD  1 
ATOM   804  C CE  . LYS   B 1 7  ? 27.483  -9.044  -44.926 1.00 57.77  ? 6   LYS   B CE  1 
ATOM   805  N NZ  . LYS   B 1 7  ? 26.300  -9.898  -44.785 1.00 66.90  ? 6   LYS   B NZ  1 
ATOM   806  N N   . PRO   B 1 8  ? 29.065  -9.504  -38.931 1.00 54.31  ? 7   PRO   B N   1 
ATOM   807  C CA  . PRO   B 1 8  ? 28.372  -8.584  -38.024 1.00 48.72  ? 7   PRO   B CA  1 
ATOM   808  C C   . PRO   B 1 8  ? 27.274  -7.769  -38.695 1.00 46.04  ? 7   PRO   B C   1 
ATOM   809  O O   . PRO   B 1 8  ? 27.475  -7.115  -39.718 1.00 44.50  ? 7   PRO   B O   1 
ATOM   810  C CB  . PRO   B 1 8  ? 29.518  -7.747  -37.462 1.00 54.33  ? 7   PRO   B CB  1 
ATOM   811  C CG  . PRO   B 1 8  ? 30.687  -8.710  -37.473 1.00 52.65  ? 7   PRO   B CG  1 
ATOM   812  C CD  . PRO   B 1 8  ? 30.529  -9.368  -38.837 1.00 56.11  ? 7   PRO   B CD  1 
ATOM   813  N N   . GLY   B 1 9  ? 26.070  -7.881  -38.127 1.00 40.34  ? 8   GLY   B N   1 
ATOM   814  C CA  . GLY   B 1 9  ? 24.899  -7.211  -38.650 1.00 36.65  ? 8   GLY   B CA  1 
ATOM   815  C C   . GLY   B 1 9  ? 23.930  -8.176  -39.315 1.00 34.29  ? 8   GLY   B C   1 
ATOM   816  O O   . GLY   B 1 9  ? 22.821  -7.750  -39.619 1.00 34.63  ? 8   GLY   B O   1 
ATOM   817  N N   . ASP   B 1 10 ? 24.349  -9.439  -39.588 1.00 32.76  ? 9   ASP   B N   1 
ATOM   818  C CA  . ASP   B 1 10 ? 23.467  -10.449 -40.167 1.00 33.61  ? 9   ASP   B CA  1 
ATOM   819  C C   . ASP   B 1 10 ? 22.329  -10.768 -39.181 1.00 29.24  ? 9   ASP   B C   1 
ATOM   820  O O   . ASP   B 1 10 ? 22.581  -10.930 -37.983 1.00 30.64  ? 9   ASP   B O   1 
ATOM   821  C CB  . ASP   B 1 10 ? 24.221  -11.729 -40.540 1.00 35.37  ? 9   ASP   B CB  1 
ATOM   822  C CG  . ASP   B 1 10 ? 24.998  -11.691 -41.863 1.00 39.39  ? 9   ASP   B CG  1 
ATOM   823  O OD1 . ASP   B 1 10 ? 24.707  -10.817 -42.676 1.00 40.69  ? 9   ASP   B OD1 1 
ATOM   824  O OD2 . ASP   B 1 10 ? 25.858  -12.559 -42.079 1.00 41.96  ? 9   ASP   B OD2 1 
ATOM   825  N N   . LEU   B 1 11 ? 21.122  -10.872 -39.721 1.00 31.33  ? 10  LEU   B N   1 
ATOM   826  C CA  . LEU   B 1 11 ? 19.916  -11.095 -38.939 1.00 30.66  ? 10  LEU   B CA  1 
ATOM   827  C C   . LEU   B 1 11 ? 19.528  -12.575 -38.995 1.00 31.64  ? 10  LEU   B C   1 
ATOM   828  O O   . LEU   B 1 11 ? 19.625  -13.240 -40.032 1.00 28.78  ? 10  LEU   B O   1 
ATOM   829  C CB  . LEU   B 1 11 ? 18.796  -10.150 -39.371 1.00 30.50  ? 10  LEU   B CB  1 
ATOM   830  C CG  . LEU   B 1 11 ? 19.196  -8.664  -39.447 1.00 30.12  ? 10  LEU   B CG  1 
ATOM   831  C CD1 . LEU   B 1 11 ? 18.030  -7.848  -39.944 1.00 31.54  ? 10  LEU   B CD1 1 
ATOM   832  C CD2 . LEU   B 1 11 ? 19.839  -8.055  -38.150 1.00 26.11  ? 10  LEU   B CD2 1 
ATOM   833  N N   . VAL   B 1 12 ? 19.088  -13.097 -37.833 1.00 29.08  ? 11  VAL   B N   1 
ATOM   834  C CA  . VAL   B 1 12 ? 18.919  -14.535 -37.689 1.00 27.91  ? 11  VAL   B CA  1 
ATOM   835  C C   . VAL   B 1 12 ? 17.749  -14.771 -36.738 1.00 29.52  ? 11  VAL   B C   1 
ATOM   836  O O   . VAL   B 1 12 ? 17.324  -13.861 -36.012 1.00 30.98  ? 11  VAL   B O   1 
ATOM   837  C CB  . VAL   B 1 12 ? 20.191  -15.236 -37.173 1.00 26.90  ? 11  VAL   B CB  1 
ATOM   838  C CG1 . VAL   B 1 12 ? 21.375  -15.170 -38.152 1.00 32.38  ? 11  VAL   B CG1 1 
ATOM   839  C CG2 . VAL   B 1 12 ? 20.637  -14.789 -35.767 1.00 26.46  ? 11  VAL   B CG2 1 
ATOM   840  N N   . PHE   B 1 13 ? 17.210  -15.983 -36.779 1.00 27.57  ? 12  PHE   B N   1 
ATOM   841  C CA  . PHE   B 1 13 ? 16.711  -16.562 -35.533 1.00 30.89  ? 12  PHE   B CA  1 
ATOM   842  C C   . PHE   B 1 13 ? 17.763  -17.494 -34.941 1.00 30.45  ? 12  PHE   B C   1 
ATOM   843  O O   . PHE   B 1 13 ? 18.289  -18.348 -35.663 1.00 29.41  ? 12  PHE   B O   1 
ATOM   844  C CB  . PHE   B 1 13 ? 15.409  -17.315 -35.756 1.00 25.64  ? 12  PHE   B CB  1 
ATOM   845  C CG  . PHE   B 1 13 ? 14.213  -16.496 -36.189 1.00 29.97  ? 12  PHE   B CG  1 
ATOM   846  C CD1 . PHE   B 1 13 ? 13.917  -16.322 -37.547 1.00 30.70  ? 12  PHE   B CD1 1 
ATOM   847  C CD2 . PHE   B 1 13 ? 13.387  -15.897 -35.237 1.00 28.67  ? 12  PHE   B CD2 1 
ATOM   848  C CE1 . PHE   B 1 13 ? 12.802  -15.583 -37.921 1.00 37.64  ? 12  PHE   B CE1 1 
ATOM   849  C CE2 . PHE   B 1 13 ? 12.253  -15.188 -35.621 1.00 29.81  ? 12  PHE   B CE2 1 
ATOM   850  C CZ  . PHE   B 1 13 ? 11.962  -15.049 -36.956 1.00 31.03  ? 12  PHE   B CZ  1 
ATOM   851  N N   . ALA   B 1 14 ? 18.008  -17.364 -33.613 1.00 27.58  ? 13  ALA   B N   1 
ATOM   852  C CA  . ALA   B 1 14 ? 19.063  -18.037 -32.891 1.00 29.44  ? 13  ALA   B CA  1 
ATOM   853  C C   . ALA   B 1 14 ? 18.431  -18.975 -31.855 1.00 34.35  ? 13  ALA   B C   1 
ATOM   854  O O   . ALA   B 1 14 ? 17.545  -18.539 -31.119 1.00 32.62  ? 13  ALA   B O   1 
ATOM   855  C CB  . ALA   B 1 14 ? 19.961  -17.039 -32.216 1.00 33.52  ? 13  ALA   B CB  1 
ATOM   856  N N   . LYS   B 1 15 ? 18.847  -20.256 -31.831 1.00 32.11  ? 14  LYS   B N   1 
ATOM   857  C CA  . LYS   B 1 15 ? 18.167  -21.268 -31.005 1.00 33.44  ? 14  LYS   B CA  1 
ATOM   858  C C   . LYS   B 1 15 ? 19.000  -21.591 -29.775 1.00 37.67  ? 14  LYS   B C   1 
ATOM   859  O O   . LYS   B 1 15 ? 20.170  -21.990 -29.909 1.00 34.37  ? 14  LYS   B O   1 
ATOM   860  C CB  . LYS   B 1 15 ? 17.919  -22.582 -31.773 1.00 31.56  ? 14  LYS   B CB  1 
ATOM   861  C CG  . LYS   B 1 15 ? 17.241  -23.724 -30.966 1.00 31.18  ? 14  LYS   B CG  1 
ATOM   862  C CD  . LYS   B 1 15 ? 15.772  -23.427 -30.735 1.00 32.47  ? 14  LYS   B CD  1 
ATOM   863  C CE  . LYS   B 1 15 ? 14.915  -24.408 -29.928 1.00 35.13  ? 14  LYS   B CE  1 
ATOM   864  N NZ  . LYS   B 1 15 ? 15.530  -24.573 -28.607 1.00 35.00  ? 14  LYS   B NZ  1 
ATOM   865  N N   . MET   B 1 16 ? 18.349  -21.492 -28.597 1.00 39.79  ? 15  MET   B N   1 
ATOM   866  C CA  . MET   B 1 16 ? 18.959  -21.760 -27.297 1.00 41.57  ? 15  MET   B CA  1 
ATOM   867  C C   . MET   B 1 16 ? 18.132  -22.842 -26.613 1.00 39.62  ? 15  MET   B C   1 
ATOM   868  O O   . MET   B 1 16 ? 16.918  -22.890 -26.792 1.00 36.88  ? 15  MET   B O   1 
ATOM   869  C CB  . MET   B 1 16 ? 18.882  -20.546 -26.365 1.00 47.14  ? 15  MET   B CB  1 
ATOM   870  C CG  . MET   B 1 16 ? 19.695  -19.366 -26.827 1.00 60.40  ? 15  MET   B CG  1 
ATOM   871  S SD  . MET   B 1 16 ? 21.312  -19.441 -26.047 1.00 80.84  ? 15  MET   B SD  1 
ATOM   872  C CE  . MET   B 1 16 ? 20.904  -18.585 -24.516 1.00 74.14  ? 15  MET   B CE  1 
ATOM   873  N N   . LYS   B 1 17 ? 18.806  -23.701 -25.848 1.00 41.54  ? 16  LYS   B N   1 
ATOM   874  C CA  . LYS   B 1 17 ? 18.139  -24.717 -25.039 1.00 46.40  ? 16  LYS   B CA  1 
ATOM   875  C C   . LYS   B 1 17 ? 17.091  -24.058 -24.133 1.00 40.14  ? 16  LYS   B C   1 
ATOM   876  O O   . LYS   B 1 17 ? 17.404  -23.135 -23.389 1.00 44.96  ? 16  LYS   B O   1 
ATOM   877  C CB  . LYS   B 1 17 ? 19.234  -25.519 -24.319 1.00 57.00  ? 16  LYS   B CB  1 
ATOM   878  C CG  . LYS   B 1 17 ? 18.749  -26.808 -23.655 1.00 63.77  ? 16  LYS   B CG  1 
ATOM   879  C CD  . LYS   B 1 17 ? 19.808  -27.896 -23.497 1.00 72.63  ? 16  LYS   B CD  1 
ATOM   880  C CE  . LYS   B 1 17 ? 19.277  -29.086 -22.751 1.00 71.07  ? 16  LYS   B CE  1 
ATOM   881  N NZ  . LYS   B 1 17 ? 17.976  -29.527 -23.268 1.00 69.08  ? 16  LYS   B NZ  1 
ATOM   882  N N   . GLY   B 1 18 ? 15.829  -24.483 -24.278 1.00 37.97  ? 17  GLY   B N   1 
ATOM   883  C CA  . GLY   B 1 18 ? 14.734  -24.064 -23.414 1.00 38.06  ? 17  GLY   B CA  1 
ATOM   884  C C   . GLY   B 1 18 ? 13.947  -22.870 -23.960 1.00 42.52  ? 17  GLY   B C   1 
ATOM   885  O O   . GLY   B 1 18 ? 13.032  -22.407 -23.286 1.00 42.36  ? 17  GLY   B O   1 
ATOM   886  N N   . TYR   B 1 19 ? 14.300  -22.359 -25.164 1.00 38.27  ? 18  TYR   B N   1 
ATOM   887  C CA  . TYR   B 1 19 ? 13.638  -21.167 -25.694 1.00 35.72  ? 18  TYR   B CA  1 
ATOM   888  C C   . TYR   B 1 19 ? 13.240  -21.424 -27.146 1.00 32.08  ? 18  TYR   B C   1 
ATOM   889  O O   . TYR   B 1 19 ? 13.903  -22.208 -27.818 1.00 36.93  ? 18  TYR   B O   1 
ATOM   890  C CB  . TYR   B 1 19 ? 14.551  -19.932 -25.604 1.00 34.16  ? 18  TYR   B CB  1 
ATOM   891  C CG  . TYR   B 1 19 ? 14.944  -19.673 -24.155 1.00 37.72  ? 18  TYR   B CG  1 
ATOM   892  C CD1 . TYR   B 1 19 ? 14.127  -18.936 -23.305 1.00 41.45  ? 18  TYR   B CD1 1 
ATOM   893  C CD2 . TYR   B 1 19 ? 16.077  -20.274 -23.624 1.00 40.54  ? 18  TYR   B CD2 1 
ATOM   894  C CE1 . TYR   B 1 19 ? 14.455  -18.786 -21.964 1.00 43.73  ? 18  TYR   B CE1 1 
ATOM   895  C CE2 . TYR   B 1 19 ? 16.406  -20.142 -22.286 1.00 47.32  ? 18  TYR   B CE2 1 
ATOM   896  C CZ  . TYR   B 1 19 ? 15.588  -19.399 -21.457 1.00 46.21  ? 18  TYR   B CZ  1 
ATOM   897  O OH  . TYR   B 1 19 ? 15.964  -19.289 -20.147 1.00 53.79  ? 18  TYR   B OH  1 
ATOM   898  N N   . PRO   B 1 20 ? 12.137  -20.833 -27.650 1.00 29.02  ? 19  PRO   B N   1 
ATOM   899  C CA  . PRO   B 1 20 ? 11.831  -20.880 -29.080 1.00 27.07  ? 19  PRO   B CA  1 
ATOM   900  C C   . PRO   B 1 20 ? 12.931  -20.196 -29.920 1.00 28.75  ? 19  PRO   B C   1 
ATOM   901  O O   . PRO   B 1 20 ? 13.637  -19.327 -29.423 1.00 29.13  ? 19  PRO   B O   1 
ATOM   902  C CB  . PRO   B 1 20 ? 10.544  -20.121 -29.125 1.00 28.54  ? 19  PRO   B CB  1 
ATOM   903  C CG  . PRO   B 1 20 ? 10.583  -19.176 -27.927 1.00 27.77  ? 19  PRO   B CG  1 
ATOM   904  C CD  . PRO   B 1 20 ? 11.133  -20.097 -26.864 1.00 32.43  ? 19  PRO   B CD  1 
ATOM   905  N N   . HIS   B 1 21 ? 13.063  -20.562 -31.203 1.00 29.61  ? 20  HIS   B N   1 
ATOM   906  C CA  . HIS   B 1 21 ? 13.937  -19.844 -32.129 1.00 33.37  ? 20  HIS   B CA  1 
ATOM   907  C C   . HIS   B 1 21 ? 13.738  -18.332 -31.983 1.00 28.76  ? 20  HIS   B C   1 
ATOM   908  O O   . HIS   B 1 21 ? 12.644  -17.832 -32.129 1.00 29.14  ? 20  HIS   B O   1 
ATOM   909  C CB  . HIS   B 1 21 ? 13.578  -20.266 -33.564 1.00 26.97  ? 20  HIS   B CB  1 
ATOM   910  C CG  . HIS   B 1 21 ? 13.876  -21.717 -33.800 1.00 32.01  ? 20  HIS   B CG  1 
ATOM   911  N ND1 . HIS   B 1 21 ? 13.102  -22.764 -33.332 1.00 31.86  ? 20  HIS   B ND1 1 
ATOM   912  C CD2 . HIS   B 1 21 ? 14.923  -22.274 -34.411 1.00 31.45  ? 20  HIS   B CD2 1 
ATOM   913  C CE1 . HIS   B 1 21 ? 13.667  -23.913 -33.669 1.00 30.37  ? 20  HIS   B CE1 1 
ATOM   914  N NE2 . HIS   B 1 21 ? 14.779  -23.647 -34.316 1.00 33.33  ? 20  HIS   B NE2 1 
ATOM   915  N N   . TRP   B 1 22 ? 14.827  -17.583 -31.816 1.00 29.92  ? 21  TRP   B N   1 
ATOM   916  C CA  . TRP   B 1 22 ? 14.668  -16.253 -31.265 1.00 27.85  ? 21  TRP   B CA  1 
ATOM   917  C C   . TRP   B 1 22 ? 15.298  -15.164 -32.150 1.00 29.90  ? 21  TRP   B C   1 
ATOM   918  O O   . TRP   B 1 22 ? 16.450  -15.294 -32.538 1.00 32.11  ? 21  TRP   B O   1 
ATOM   919  C CB  . TRP   B 1 22 ? 15.257  -16.255 -29.848 1.00 27.47  ? 21  TRP   B CB  1 
ATOM   920  C CG  . TRP   B 1 22 ? 14.797  -15.083 -29.025 1.00 29.65  ? 21  TRP   B CG  1 
ATOM   921  C CD1 . TRP   B 1 22 ? 15.102  -13.755 -29.168 1.00 33.22  ? 21  TRP   B CD1 1 
ATOM   922  C CD2 . TRP   B 1 22 ? 13.850  -15.159 -27.929 1.00 33.90  ? 21  TRP   B CD2 1 
ATOM   923  N NE1 . TRP   B 1 22 ? 14.429  -13.003 -28.232 1.00 38.04  ? 21  TRP   B NE1 1 
ATOM   924  C CE2 . TRP   B 1 22 ? 13.654  -13.836 -27.454 1.00 32.14  ? 21  TRP   B CE2 1 
ATOM   925  C CE3 . TRP   B 1 22 ? 13.182  -16.216 -27.294 1.00 29.57  ? 21  TRP   B CE3 1 
ATOM   926  C CZ2 . TRP   B 1 22 ? 12.812  -13.551 -26.372 1.00 36.84  ? 21  TRP   B CZ2 1 
ATOM   927  C CZ3 . TRP   B 1 22 ? 12.343  -15.931 -26.235 1.00 32.75  ? 21  TRP   B CZ3 1 
ATOM   928  C CH2 . TRP   B 1 22 ? 12.152  -14.615 -25.790 1.00 36.51  ? 21  TRP   B CH2 1 
ATOM   929  N N   . PRO   B 1 23 ? 14.551  -14.066 -32.448 1.00 29.73  ? 22  PRO   B N   1 
ATOM   930  C CA  . PRO   B 1 23 ? 15.028  -12.963 -33.312 1.00 28.05  ? 22  PRO   B CA  1 
ATOM   931  C C   . PRO   B 1 23 ? 16.312  -12.343 -32.762 1.00 28.38  ? 22  PRO   B C   1 
ATOM   932  O O   . PRO   B 1 23 ? 16.440  -12.045 -31.570 1.00 26.08  ? 22  PRO   B O   1 
ATOM   933  C CB  . PRO   B 1 23 ? 13.799  -11.986 -33.341 1.00 33.37  ? 22  PRO   B CB  1 
ATOM   934  C CG  . PRO   B 1 23 ? 13.024  -12.319 -32.047 1.00 26.95  ? 22  PRO   B CG  1 
ATOM   935  C CD  . PRO   B 1 23 ? 13.142  -13.864 -32.032 1.00 26.82  ? 22  PRO   B CD  1 
ATOM   936  N N   . ALA   B 1 24 ? 17.328  -12.209 -33.619 1.00 28.11  ? 23  ALA   B N   1 
ATOM   937  C CA  . ALA   B 1 24 ? 18.666  -11.954 -33.111 1.00 24.85  ? 23  ALA   B CA  1 
ATOM   938  C C   . ALA   B 1 24 ? 19.576  -11.468 -34.245 1.00 27.89  ? 23  ALA   B C   1 
ATOM   939  O O   . ALA   B 1 24 ? 19.208  -11.568 -35.419 1.00 33.72  ? 23  ALA   B O   1 
ATOM   940  C CB  . ALA   B 1 24 ? 19.259  -13.185 -32.471 1.00 26.99  ? 23  ALA   B CB  1 
ATOM   941  N N   . ARG   B 1 25 ? 20.753  -10.957 -33.852 1.00 31.60  ? 24  ARG   B N   1 
ATOM   942  C CA  . ARG   B 1 25 ? 21.743  -10.533 -34.833 1.00 31.66  ? 24  ARG   B CA  1 
ATOM   943  C C   . ARG   B 1 25 ? 23.113  -11.010 -34.398 1.00 32.61  ? 24  ARG   B C   1 
ATOM   944  O O   . ARG   B 1 25 ? 23.336  -11.319 -33.215 1.00 32.14  ? 24  ARG   B O   1 
ATOM   945  C CB  . ARG   B 1 25 ? 21.695  -9.003  -34.947 1.00 32.77  ? 24  ARG   B CB  1 
ATOM   946  C CG  . ARG   B 1 25 ? 22.334  -8.205  -33.821 1.00 35.92  ? 24  ARG   B CG  1 
ATOM   947  C CD  . ARG   B 1 25 ? 21.889  -6.726  -33.863 1.00 37.12  ? 24  ARG   B CD  1 
ATOM   948  N NE  . ARG   B 1 25 ? 22.629  -5.954  -32.855 1.00 31.85  ? 24  ARG   B NE  1 
ATOM   949  C CZ  . ARG   B 1 25 ? 22.322  -4.717  -32.454 1.00 31.17  ? 24  ARG   B CZ  1 
ATOM   950  N NH1 . ARG   B 1 25 ? 21.341  -4.028  -33.024 1.00 28.54  ? 24  ARG   B NH1 1 
ATOM   951  N NH2 . ARG   B 1 25 ? 22.961  -4.204  -31.430 1.00 34.36  ? 24  ARG   B NH2 1 
ATOM   952  N N   . ILE   B 1 26 ? 24.029  -11.070 -35.382 1.00 34.99  ? 25  ILE   B N   1 
ATOM   953  C CA  . ILE   B 1 26 ? 25.461  -11.199 -35.161 1.00 38.09  ? 25  ILE   B CA  1 
ATOM   954  C C   . ILE   B 1 26 ? 26.039  -9.829  -34.783 1.00 39.32  ? 25  ILE   B C   1 
ATOM   955  O O   . ILE   B 1 26 ? 25.976  -8.905  -35.589 1.00 42.49  ? 25  ILE   B O   1 
ATOM   956  C CB  . ILE   B 1 26 ? 26.132  -11.654 -36.480 1.00 36.39  ? 25  ILE   B CB  1 
ATOM   957  C CG1 . ILE   B 1 26 ? 25.317  -12.742 -37.226 1.00 33.18  ? 25  ILE   B CG1 1 
ATOM   958  C CG2 . ILE   B 1 26 ? 27.609  -12.010 -36.261 1.00 36.60  ? 25  ILE   B CG2 1 
ATOM   959  C CD1 . ILE   B 1 26 ? 25.155  -14.055 -36.453 1.00 40.78  ? 25  ILE   B CD1 1 
ATOM   960  N N   . ASP   B 1 27 ? 26.707  -9.738  -33.629 1.00 43.09  ? 26  ASP   B N   1 
ATOM   961  C CA  . ASP   B 1 27 ? 27.470  -8.568  -33.212 1.00 49.14  ? 26  ASP   B CA  1 
ATOM   962  C C   . ASP   B 1 27 ? 28.967  -8.771  -33.500 1.00 54.72  ? 26  ASP   B C   1 
ATOM   963  O O   . ASP   B 1 27 ? 29.386  -9.878  -33.840 1.00 49.98  ? 26  ASP   B O   1 
ATOM   964  C CB  . ASP   B 1 27 ? 27.353  -8.402  -31.705 1.00 48.71  ? 26  ASP   B CB  1 
ATOM   965  C CG  . ASP   B 1 27 ? 26.110  -7.691  -31.194 1.00 50.88  ? 26  ASP   B CG  1 
ATOM   966  O OD1 . ASP   B 1 27 ? 25.281  -7.300  -32.034 1.00 43.34  ? 26  ASP   B OD1 1 
ATOM   967  O OD2 . ASP   B 1 27 ? 26.010  -7.505  -29.955 1.00 52.53  ? 26  ASP   B OD2 1 
ATOM   968  N N   A ASP   B 1 28 ? 29.757  -7.697  -33.320 0.50 51.00  ? 27  ASP   B N   1 
ATOM   969  N N   B ASP   B 1 28 ? 29.776  -7.714  -33.341 0.50 52.70  ? 27  ASP   B N   1 
ATOM   970  C CA  A ASP   B 1 28 ? 31.210  -7.744  -33.444 0.50 54.59  ? 27  ASP   B CA  1 
ATOM   971  C CA  B ASP   B 1 28 ? 31.216  -7.871  -33.498 0.50 56.79  ? 27  ASP   B CA  1 
ATOM   972  C C   A ASP   B 1 28 ? 31.809  -8.141  -32.097 0.50 57.76  ? 27  ASP   B C   1 
ATOM   973  C C   B ASP   B 1 28 ? 31.849  -8.061  -32.124 0.50 59.50  ? 27  ASP   B C   1 
ATOM   974  O O   A ASP   B 1 28 ? 31.158  -7.980  -31.065 0.50 58.70  ? 27  ASP   B O   1 
ATOM   975  O O   B ASP   B 1 28 ? 31.258  -7.687  -31.112 0.50 61.17  ? 27  ASP   B O   1 
ATOM   976  C CB  A ASP   B 1 28 ? 31.804  -6.411  -33.887 0.50 49.17  ? 27  ASP   B CB  1 
ATOM   977  C CB  B ASP   B 1 28 ? 31.857  -6.751  -34.306 0.50 53.77  ? 27  ASP   B CB  1 
ATOM   978  C CG  A ASP   B 1 28 ? 31.176  -5.730  -35.098 0.50 44.12  ? 27  ASP   B CG  1 
ATOM   979  C CG  B ASP   B 1 28 ? 33.238  -7.072  -34.865 0.50 52.34  ? 27  ASP   B CG  1 
ATOM   980  O OD1 A ASP   B 1 28 ? 31.789  -5.771  -36.187 0.50 39.46  ? 27  ASP   B OD1 1 
ATOM   981  O OD1 B ASP   B 1 28 ? 34.087  -7.573  -34.100 0.50 54.01  ? 27  ASP   B OD1 1 
ATOM   982  O OD2 A ASP   B 1 28 ? 30.104  -5.114  -34.936 0.50 45.65  ? 27  ASP   B OD2 1 
ATOM   983  O OD2 B ASP   B 1 28 ? 33.453  -6.830  -36.066 0.50 54.17  ? 27  ASP   B OD2 1 
ATOM   984  N N   . ILE   B 1 29 ? 33.055  -8.645  -32.123 1.00 62.92  ? 28  ILE   B N   1 
ATOM   985  C CA  . ILE   B 1 29 ? 33.758  -9.063  -30.920 1.00 56.55  ? 28  ILE   B CA  1 
ATOM   986  C C   . ILE   B 1 29 ? 34.258  -7.821  -30.165 1.00 65.59  ? 28  ILE   B C   1 
ATOM   987  O O   . ILE   B 1 29 ? 35.128  -7.121  -30.724 1.00 62.09  ? 28  ILE   B O   1 
ATOM   988  C CB  . ILE   B 1 29 ? 34.910  -10.032 -31.255 1.00 54.98  ? 28  ILE   B CB  1 
ATOM   989  N N   . VAL   B 1 34 ? 35.231  -10.627 -23.950 1.00 62.38  ? 33  VAL   B N   1 
ATOM   990  C CA  . VAL   B 1 34 ? 35.550  -12.091 -23.958 1.00 67.94  ? 33  VAL   B CA  1 
ATOM   991  C C   . VAL   B 1 34 ? 35.330  -12.633 -25.365 1.00 75.98  ? 33  VAL   B C   1 
ATOM   992  O O   . VAL   B 1 34 ? 34.198  -12.646 -25.841 1.00 77.58  ? 33  VAL   B O   1 
ATOM   993  C CB  . VAL   B 1 34 ? 34.759  -12.925 -22.929 1.00 71.79  ? 33  VAL   B CB  1 
ATOM   994  C CG1 . VAL   B 1 34 ? 33.398  -12.324 -22.592 1.00 66.57  ? 33  VAL   B CG1 1 
ATOM   995  C CG2 . VAL   B 1 34 ? 34.615  -14.382 -23.361 1.00 77.21  ? 33  VAL   B CG2 1 
ATOM   996  N N   . LYS   B 1 35 ? 36.415  -13.096 -26.000 1.00 77.30  ? 34  LYS   B N   1 
ATOM   997  C CA  . LYS   B 1 35 ? 36.376  -13.601 -27.366 1.00 81.98  ? 34  LYS   B CA  1 
ATOM   998  C C   . LYS   B 1 35 ? 35.541  -14.883 -27.435 1.00 83.62  ? 34  LYS   B C   1 
ATOM   999  O O   . LYS   B 1 35 ? 35.383  -15.581 -26.425 1.00 77.73  ? 34  LYS   B O   1 
ATOM   1000 C CB  . LYS   B 1 35 ? 37.790  -13.784 -27.934 1.00 85.25  ? 34  LYS   B CB  1 
ATOM   1001 N N   . PRO   B 1 36 ? 34.954  -15.205 -28.619 1.00 84.60  ? 35  PRO   B N   1 
ATOM   1002 C CA  . PRO   B 1 36 ? 34.053  -16.354 -28.760 1.00 71.17  ? 35  PRO   B CA  1 
ATOM   1003 C C   . PRO   B 1 36 ? 34.742  -17.713 -28.662 1.00 69.94  ? 35  PRO   B C   1 
ATOM   1004 O O   . PRO   B 1 36 ? 35.868  -17.871 -29.114 1.00 62.71  ? 35  PRO   B O   1 
ATOM   1005 C CB  . PRO   B 1 36 ? 33.354  -16.168 -30.125 1.00 73.62  ? 35  PRO   B CB  1 
ATOM   1006 C CG  . PRO   B 1 36 ? 33.834  -14.825 -30.646 1.00 78.40  ? 35  PRO   B CG  1 
ATOM   1007 C CD  . PRO   B 1 36 ? 35.082  -14.439 -29.872 1.00 81.80  ? 35  PRO   B CD  1 
ATOM   1008 N N   . PRO   B 1 37 ? 34.067  -18.752 -28.114 1.00 69.53  ? 36  PRO   B N   1 
ATOM   1009 C CA  . PRO   B 1 37 ? 34.608  -20.109 -28.125 1.00 64.93  ? 36  PRO   B CA  1 
ATOM   1010 C C   . PRO   B 1 37 ? 34.749  -20.541 -29.583 1.00 83.33  ? 36  PRO   B C   1 
ATOM   1011 O O   . PRO   B 1 37 ? 34.352  -19.807 -30.493 1.00 88.88  ? 36  PRO   B O   1 
ATOM   1012 C CB  . PRO   B 1 37 ? 33.601  -20.984 -27.340 1.00 68.38  ? 36  PRO   B CB  1 
ATOM   1013 C CG  . PRO   B 1 37 ? 32.525  -20.038 -26.851 1.00 64.98  ? 36  PRO   B CG  1 
ATOM   1014 C CD  . PRO   B 1 37 ? 32.730  -18.684 -27.507 1.00 65.99  ? 36  PRO   B CD  1 
ATOM   1015 N N   . PRO   B 1 38 ? 35.299  -21.745 -29.868 1.00 86.06  ? 37  PRO   B N   1 
ATOM   1016 C CA  . PRO   B 1 38 ? 35.720  -22.070 -31.231 1.00 82.15  ? 37  PRO   B CA  1 
ATOM   1017 C C   . PRO   B 1 38 ? 34.527  -22.471 -32.103 1.00 77.11  ? 37  PRO   B C   1 
ATOM   1018 O O   . PRO   B 1 38 ? 33.763  -23.357 -31.720 1.00 70.53  ? 37  PRO   B O   1 
ATOM   1019 C CB  . PRO   B 1 38 ? 36.751  -23.204 -31.023 1.00 76.99  ? 37  PRO   B CB  1 
ATOM   1020 C CG  . PRO   B 1 38 ? 36.706  -23.546 -29.533 1.00 77.10  ? 37  PRO   B CG  1 
ATOM   1021 C CD  . PRO   B 1 38 ? 35.502  -22.861 -28.926 1.00 83.53  ? 37  PRO   B CD  1 
ATOM   1022 N N   . ASN   B 1 39 ? 34.380  -21.790 -33.256 1.00 70.59  ? 38  ASN   B N   1 
ATOM   1023 C CA  . ASN   B 1 39 ? 33.338  -22.016 -34.258 1.00 62.91  ? 38  ASN   B CA  1 
ATOM   1024 C C   . ASN   B 1 39 ? 32.096  -21.162 -34.005 1.00 56.18  ? 38  ASN   B C   1 
ATOM   1025 O O   . ASN   B 1 39 ? 31.321  -20.942 -34.926 1.00 54.89  ? 38  ASN   B O   1 
ATOM   1026 C CB  . ASN   B 1 39 ? 32.917  -23.474 -34.407 1.00 68.86  ? 38  ASN   B CB  1 
ATOM   1027 C CG  . ASN   B 1 39 ? 33.911  -24.325 -35.164 1.00 84.17  ? 38  ASN   B CG  1 
ATOM   1028 O OD1 . ASN   B 1 39 ? 33.752  -25.552 -35.210 1.00 84.28  ? 38  ASN   B OD1 1 
ATOM   1029 N ND2 . ASN   B 1 39 ? 34.936  -23.716 -35.750 1.00 82.45  ? 38  ASN   B ND2 1 
ATOM   1030 N N   . LYS   B 1 40 ? 31.922  -20.678 -32.772 1.00 54.88  ? 39  LYS   B N   1 
ATOM   1031 C CA  . LYS   B 1 40 ? 30.743  -19.929 -32.357 1.00 54.45  ? 39  LYS   B CA  1 
ATOM   1032 C C   . LYS   B 1 40 ? 30.848  -18.441 -32.730 1.00 51.47  ? 39  LYS   B C   1 
ATOM   1033 O O   . LYS   B 1 40 ? 31.920  -17.941 -33.084 1.00 51.91  ? 39  LYS   B O   1 
ATOM   1034 C CB  . LYS   B 1 40 ? 30.588  -20.230 -30.860 1.00 58.06  ? 39  LYS   B CB  1 
ATOM   1035 C CG  . LYS   B 1 40 ? 30.237  -21.678 -30.527 1.00 55.21  ? 39  LYS   B CG  1 
ATOM   1036 C CD  . LYS   B 1 40 ? 30.026  -21.913 -29.038 1.00 59.65  ? 39  LYS   B CD  1 
ATOM   1037 C CE  . LYS   B 1 40 ? 29.153  -23.089 -28.731 1.00 66.37  ? 39  LYS   B CE  1 
ATOM   1038 N NZ  . LYS   B 1 40 ? 29.886  -24.352 -28.639 1.00 69.94  ? 39  LYS   B NZ  1 
ATOM   1039 N N   . TYR   B 1 41 ? 29.714  -17.728 -32.661 1.00 45.41  ? 40  TYR   B N   1 
ATOM   1040 C CA  . TYR   B 1 41 ? 29.678  -16.294 -32.904 1.00 42.59  ? 40  TYR   B CA  1 
ATOM   1041 C C   . TYR   B 1 41 ? 29.012  -15.571 -31.729 1.00 47.58  ? 40  TYR   B C   1 
ATOM   1042 O O   . TYR   B 1 41 ? 28.232  -16.188 -31.004 1.00 42.35  ? 40  TYR   B O   1 
ATOM   1043 C CB  . TYR   B 1 41 ? 28.822  -15.971 -34.134 1.00 46.06  ? 40  TYR   B CB  1 
ATOM   1044 C CG  . TYR   B 1 41 ? 29.342  -16.388 -35.502 1.00 44.95  ? 40  TYR   B CG  1 
ATOM   1045 C CD1 . TYR   B 1 41 ? 29.736  -15.440 -36.446 1.00 45.36  ? 40  TYR   B CD1 1 
ATOM   1046 C CD2 . TYR   B 1 41 ? 29.376  -17.733 -35.870 1.00 53.40  ? 40  TYR   B CD2 1 
ATOM   1047 C CE1 . TYR   B 1 41 ? 30.175  -15.825 -37.710 1.00 50.89  ? 40  TYR   B CE1 1 
ATOM   1048 C CE2 . TYR   B 1 41 ? 29.818  -18.127 -37.127 1.00 52.66  ? 40  TYR   B CE2 1 
ATOM   1049 C CZ  . TYR   B 1 41 ? 30.226  -17.172 -38.042 1.00 55.14  ? 40  TYR   B CZ  1 
ATOM   1050 O OH  . TYR   B 1 41 ? 30.648  -17.599 -39.267 1.00 57.45  ? 40  TYR   B OH  1 
ATOM   1051 N N   . PRO   B 1 42 ? 29.300  -14.252 -31.538 1.00 45.05  ? 41  PRO   B N   1 
ATOM   1052 C CA  . PRO   B 1 42 ? 28.566  -13.373 -30.614 1.00 41.64  ? 41  PRO   B CA  1 
ATOM   1053 C C   . PRO   B 1 42 ? 27.147  -13.047 -31.074 1.00 38.04  ? 41  PRO   B C   1 
ATOM   1054 O O   . PRO   B 1 42 ? 26.956  -12.451 -32.137 1.00 41.81  ? 41  PRO   B O   1 
ATOM   1055 C CB  . PRO   B 1 42 ? 29.412  -12.061 -30.570 1.00 46.63  ? 41  PRO   B CB  1 
ATOM   1056 C CG  . PRO   B 1 42 ? 30.250  -12.082 -31.845 1.00 46.67  ? 41  PRO   B CG  1 
ATOM   1057 C CD  . PRO   B 1 42 ? 30.371  -13.535 -32.249 1.00 50.76  ? 41  PRO   B CD  1 
ATOM   1058 N N   . ILE   B 1 43 ? 26.152  -13.420 -30.259 1.00 37.94  ? 42  ILE   B N   1 
ATOM   1059 C CA  . ILE   B 1 43 ? 24.753  -13.249 -30.640 1.00 31.57  ? 42  ILE   B CA  1 
ATOM   1060 C C   . ILE   B 1 43 ? 24.127  -12.240 -29.682 1.00 37.69  ? 42  ILE   B C   1 
ATOM   1061 O O   . ILE   B 1 43 ? 24.344  -12.335 -28.472 1.00 35.87  ? 42  ILE   B O   1 
ATOM   1062 C CB  . ILE   B 1 43 ? 23.993  -14.586 -30.622 1.00 37.78  ? 42  ILE   B CB  1 
ATOM   1063 C CG1 . ILE   B 1 43 ? 24.719  -15.695 -31.448 1.00 34.76  ? 42  ILE   B CG1 1 
ATOM   1064 C CG2 . ILE   B 1 43 ? 22.510  -14.417 -30.991 1.00 34.12  ? 42  ILE   B CG2 1 
ATOM   1065 C CD1 . ILE   B 1 43 ? 25.114  -15.318 -32.876 1.00 33.99  ? 42  ILE   B CD1 1 
ATOM   1066 N N   . PHE   B 1 44 ? 23.443  -11.242 -30.266 1.00 32.46  ? 43  PHE   B N   1 
ATOM   1067 C CA  . PHE   B 1 44 ? 22.627  -10.277 -29.541 1.00 30.20  ? 43  PHE   B CA  1 
ATOM   1068 C C   . PHE   B 1 44 ? 21.153  -10.596 -29.774 1.00 30.84  ? 43  PHE   B C   1 
ATOM   1069 O O   . PHE   B 1 44 ? 20.704  -10.586 -30.912 1.00 34.20  ? 43  PHE   B O   1 
ATOM   1070 C CB  . PHE   B 1 44 ? 23.000  -8.837  -29.938 1.00 31.92  ? 43  PHE   B CB  1 
ATOM   1071 C CG  . PHE   B 1 44 ? 22.071  -7.822  -29.291 1.00 30.60  ? 43  PHE   B CG  1 
ATOM   1072 C CD1 . PHE   B 1 44 ? 20.908  -7.424  -29.947 1.00 33.54  ? 43  PHE   B CD1 1 
ATOM   1073 C CD2 . PHE   B 1 44 ? 22.306  -7.367  -27.996 1.00 34.31  ? 43  PHE   B CD2 1 
ATOM   1074 C CE1 . PHE   B 1 44 ? 20.032  -6.512  -29.355 1.00 39.41  ? 43  PHE   B CE1 1 
ATOM   1075 C CE2 . PHE   B 1 44 ? 21.439  -6.434  -27.413 1.00 34.32  ? 43  PHE   B CE2 1 
ATOM   1076 C CZ  . PHE   B 1 44 ? 20.302  -6.027  -28.093 1.00 38.68  ? 43  PHE   B CZ  1 
ATOM   1077 N N   . PHE   B 1 45 ? 20.407  -10.916 -28.689 1.00 31.22  ? 44  PHE   B N   1 
ATOM   1078 C CA  . PHE   B 1 45 ? 18.984  -11.215 -28.809 1.00 27.61  ? 44  PHE   B CA  1 
ATOM   1079 C C   . PHE   B 1 45 ? 18.115  -9.961  -28.709 1.00 29.29  ? 44  PHE   B C   1 
ATOM   1080 O O   . PHE   B 1 45 ? 18.136  -9.234  -27.718 1.00 31.18  ? 44  PHE   B O   1 
ATOM   1081 C CB  . PHE   B 1 45 ? 18.542  -12.209 -27.728 1.00 27.19  ? 44  PHE   B CB  1 
ATOM   1082 C CG  . PHE   B 1 45 ? 19.261  -13.546 -27.857 1.00 27.28  ? 44  PHE   B CG  1 
ATOM   1083 C CD1 . PHE   B 1 45 ? 20.403  -13.820 -27.119 1.00 35.09  ? 44  PHE   B CD1 1 
ATOM   1084 C CD2 . PHE   B 1 45 ? 18.739  -14.551 -28.656 1.00 32.58  ? 44  PHE   B CD2 1 
ATOM   1085 C CE1 . PHE   B 1 45 ? 21.025  -15.065 -27.205 1.00 42.02  ? 44  PHE   B CE1 1 
ATOM   1086 C CE2 . PHE   B 1 45 ? 19.354  -15.796 -28.720 1.00 34.41  ? 44  PHE   B CE2 1 
ATOM   1087 C CZ  . PHE   B 1 45 ? 20.493  -16.046 -28.019 1.00 36.31  ? 44  PHE   B CZ  1 
ATOM   1088 N N   . PHE   B 1 46 ? 17.290  -9.743  -29.732 1.00 27.58  ? 45  PHE   B N   1 
ATOM   1089 C CA  . PHE   B 1 46 ? 16.327  -8.660  -29.686 1.00 31.00  ? 45  PHE   B CA  1 
ATOM   1090 C C   . PHE   B 1 46 ? 15.341  -8.915  -28.531 1.00 35.31  ? 45  PHE   B C   1 
ATOM   1091 O O   . PHE   B 1 46 ? 15.068  -10.060 -28.155 1.00 31.55  ? 45  PHE   B O   1 
ATOM   1092 C CB  . PHE   B 1 46 ? 15.597  -8.407  -30.992 1.00 29.31  ? 45  PHE   B CB  1 
ATOM   1093 C CG  . PHE   B 1 46 ? 16.538  -7.977  -32.128 1.00 35.23  ? 45  PHE   B CG  1 
ATOM   1094 C CD1 . PHE   B 1 46 ? 17.110  -6.698  -32.154 1.00 36.34  ? 45  PHE   B CD1 1 
ATOM   1095 C CD2 . PHE   B 1 46 ? 16.851  -8.845  -33.172 1.00 36.73  ? 45  PHE   B CD2 1 
ATOM   1096 C CE1 . PHE   B 1 46 ? 17.972  -6.286  -33.193 1.00 33.89  ? 45  PHE   B CE1 1 
ATOM   1097 C CE2 . PHE   B 1 46 ? 17.736  -8.448  -34.175 1.00 35.39  ? 45  PHE   B CE2 1 
ATOM   1098 C CZ  . PHE   B 1 46 ? 18.283  -7.165  -34.197 1.00 31.43  ? 45  PHE   B CZ  1 
ATOM   1099 N N   . GLY   B 1 47 ? 14.792  -7.833  -27.993 1.00 30.68  ? 46  GLY   B N   1 
ATOM   1100 C CA  . GLY   B 1 47 ? 13.743  -7.944  -26.981 1.00 34.22  ? 46  GLY   B CA  1 
ATOM   1101 C C   . GLY   B 1 47 ? 14.375  -7.994  -25.591 1.00 36.91  ? 46  GLY   B C   1 
ATOM   1102 O O   . GLY   B 1 47 ? 14.247  -7.047  -24.824 1.00 34.24  ? 46  GLY   B O   1 
ATOM   1103 N N   . THR   B 1 48 ? 15.083  -9.091  -25.293 1.00 34.65  ? 47  THR   B N   1 
ATOM   1104 C CA  . THR   B 1 48 ? 15.689  -9.325  -23.987 1.00 28.15  ? 47  THR   B CA  1 
ATOM   1105 C C   . THR   B 1 48 ? 16.969  -8.515  -23.897 1.00 36.65  ? 47  THR   B C   1 
ATOM   1106 O O   . THR   B 1 48 ? 17.442  -8.237  -22.789 1.00 33.32  ? 47  THR   B O   1 
ATOM   1107 C CB  . THR   B 1 48 ? 15.954  -10.819 -23.751 1.00 30.33  ? 47  THR   B CB  1 
ATOM   1108 O OG1 . THR   B 1 48 ? 16.864  -11.273 -24.751 1.00 31.01  ? 47  THR   B OG1 1 
ATOM   1109 C CG2 . THR   B 1 48 ? 14.685  -11.656 -23.822 1.00 32.15  ? 47  THR   B CG2 1 
ATOM   1110 N N   . HIS   B 1 49 ? 17.570  -8.239  -25.076 1.00 34.25  ? 48  HIS   B N   1 
ATOM   1111 C CA  . HIS   B 1 49 ? 18.888  -7.609  -25.177 1.00 33.91  ? 48  HIS   B CA  1 
ATOM   1112 C C   . HIS   B 1 49 ? 19.977  -8.388  -24.454 1.00 33.84  ? 48  HIS   B C   1 
ATOM   1113 O O   . HIS   B 1 49 ? 20.949  -7.791  -23.997 1.00 43.45  ? 48  HIS   B O   1 
ATOM   1114 C CB  . HIS   B 1 49 ? 18.870  -6.127  -24.762 1.00 34.55  ? 48  HIS   B CB  1 
ATOM   1115 C CG  . HIS   B 1 49 ? 17.708  -5.420  -25.371 1.00 34.55  ? 48  HIS   B CG  1 
ATOM   1116 N ND1 . HIS   B 1 49 ? 16.847  -4.609  -24.671 1.00 37.16  ? 48  HIS   B ND1 1 
ATOM   1117 C CD2 . HIS   B 1 49 ? 17.226  -5.486  -26.631 1.00 34.27  ? 48  HIS   B CD2 1 
ATOM   1118 C CE1 . HIS   B 1 49 ? 15.912  -4.167  -25.502 1.00 43.35  ? 48  HIS   B CE1 1 
ATOM   1119 N NE2 . HIS   B 1 49 ? 16.128  -4.681  -26.708 1.00 34.01  ? 48  HIS   B NE2 1 
ATOM   1120 N N   . GLU   B 1 50 ? 19.819  -9.705  -24.324 1.00 34.17  ? 49  GLU   B N   1 
ATOM   1121 C CA  . GLU   B 1 50 ? 20.908  -10.529 -23.835 1.00 34.17  ? 49  GLU   B CA  1 
ATOM   1122 C C   . GLU   B 1 50 ? 21.793  -10.961 -25.007 1.00 35.27  ? 49  GLU   B C   1 
ATOM   1123 O O   . GLU   B 1 50 ? 21.439  -10.713 -26.158 1.00 33.49  ? 49  GLU   B O   1 
ATOM   1124 C CB  . GLU   B 1 50 ? 20.353  -11.664 -22.985 1.00 42.81  ? 49  GLU   B CB  1 
ATOM   1125 C CG  . GLU   B 1 50 ? 19.621  -11.110 -21.769 1.00 46.03  ? 49  GLU   B CG  1 
ATOM   1126 C CD  . GLU   B 1 50 ? 19.688  -12.023 -20.572 1.00 55.95  ? 49  GLU   B CD  1 
ATOM   1127 O OE1 . GLU   B 1 50 ? 20.791  -12.557 -20.363 1.00 59.33  ? 49  GLU   B OE1 1 
ATOM   1128 O OE2 . GLU   B 1 50 ? 18.678  -12.185 -19.851 1.00 61.44  ? 49  GLU   B OE2 1 
ATOM   1129 N N   . THR   B 1 51 ? 22.970  -11.498 -24.671 1.00 38.19  ? 50  THR   B N   1 
ATOM   1130 C CA  . THR   B 1 51 ? 24.011  -11.941 -25.593 1.00 44.01  ? 50  THR   B CA  1 
ATOM   1131 C C   . THR   B 1 51 ? 24.361  -13.389 -25.236 1.00 37.54  ? 50  THR   B C   1 
ATOM   1132 O O   . THR   B 1 51 ? 24.128  -13.794 -24.120 1.00 36.36  ? 50  THR   B O   1 
ATOM   1133 C CB  . THR   B 1 51 ? 25.231  -11.015 -25.492 1.00 41.33  ? 50  THR   B CB  1 
ATOM   1134 O OG1 . THR   B 1 51 ? 25.719  -11.168 -24.167 1.00 46.14  ? 50  THR   B OG1 1 
ATOM   1135 C CG2 . THR   B 1 51 ? 24.920  -9.550  -25.739 1.00 43.52  ? 50  THR   B CG2 1 
ATOM   1136 N N   . ALA   B 1 52 ? 24.814  -14.193 -26.202 1.00 36.83  ? 51  ALA   B N   1 
ATOM   1137 C CA  . ALA   B 1 52 ? 25.443  -15.488 -25.929 1.00 37.50  ? 51  ALA   B CA  1 
ATOM   1138 C C   . ALA   B 1 52 ? 26.367  -15.846 -27.092 1.00 39.57  ? 51  ALA   B C   1 
ATOM   1139 O O   . ALA   B 1 52 ? 26.432  -15.110 -28.068 1.00 44.86  ? 51  ALA   B O   1 
ATOM   1140 C CB  . ALA   B 1 52 ? 24.379  -16.533 -25.781 1.00 37.82  ? 51  ALA   B CB  1 
ATOM   1141 N N   . PHE   B 1 53 ? 27.029  -17.002 -27.015 1.00 38.95  ? 52  PHE   B N   1 
ATOM   1142 C CA  . PHE   B 1 53 ? 27.818  -17.520 -28.124 1.00 43.19  ? 52  PHE   B CA  1 
ATOM   1143 C C   . PHE   B 1 53 ? 27.136  -18.751 -28.731 1.00 45.06  ? 52  PHE   B C   1 
ATOM   1144 O O   . PHE   B 1 53 ? 26.854  -19.705 -28.013 1.00 44.69  ? 52  PHE   B O   1 
ATOM   1145 C CB  . PHE   B 1 53 ? 29.166  -17.926 -27.529 1.00 46.32  ? 52  PHE   B CB  1 
ATOM   1146 C CG  . PHE   B 1 53 ? 30.025  -16.770 -27.034 1.00 48.52  ? 52  PHE   B CG  1 
ATOM   1147 C CD1 . PHE   B 1 53 ? 30.375  -15.727 -27.890 1.00 43.94  ? 52  PHE   B CD1 1 
ATOM   1148 C CD2 . PHE   B 1 53 ? 30.424  -16.704 -25.695 1.00 46.66  ? 52  PHE   B CD2 1 
ATOM   1149 C CE1 . PHE   B 1 53 ? 31.132  -14.667 -27.422 1.00 50.74  ? 52  PHE   B CE1 1 
ATOM   1150 C CE2 . PHE   B 1 53 ? 31.177  -15.631 -25.232 1.00 55.55  ? 52  PHE   B CE2 1 
ATOM   1151 C CZ  . PHE   B 1 53 ? 31.540  -14.621 -26.101 1.00 49.75  ? 52  PHE   B CZ  1 
ATOM   1152 N N   . LEU   B 1 54 ? 26.883  -18.739 -30.055 1.00 41.17  ? 53  LEU   B N   1 
ATOM   1153 C CA  . LEU   B 1 54 ? 26.211  -19.849 -30.712 1.00 39.23  ? 53  LEU   B CA  1 
ATOM   1154 C C   . LEU   B 1 54 ? 26.963  -20.256 -31.980 1.00 39.26  ? 53  LEU   B C   1 
ATOM   1155 O O   . LEU   B 1 54 ? 27.534  -19.389 -32.631 1.00 33.81  ? 53  LEU   B O   1 
ATOM   1156 C CB  . LEU   B 1 54 ? 24.763  -19.468 -31.022 1.00 38.88  ? 53  LEU   B CB  1 
ATOM   1157 C CG  . LEU   B 1 54 ? 23.790  -19.541 -29.835 1.00 39.11  ? 53  LEU   B CG  1 
ATOM   1158 C CD1 . LEU   B 1 54 ? 22.411  -19.180 -30.385 1.00 42.77  ? 53  LEU   B CD1 1 
ATOM   1159 C CD2 . LEU   B 1 54 ? 23.773  -20.947 -29.233 1.00 34.64  ? 53  LEU   B CD2 1 
ATOM   1160 N N   . GLY   B 1 55 ? 26.949  -21.567 -32.304 1.00 37.67  ? 54  GLY   B N   1 
ATOM   1161 C CA  . GLY   B 1 55 ? 27.465  -22.044 -33.580 1.00 36.24  ? 54  GLY   B CA  1 
ATOM   1162 C C   . GLY   B 1 55 ? 26.423  -21.980 -34.692 1.00 34.27  ? 54  GLY   B C   1 
ATOM   1163 O O   . GLY   B 1 55 ? 25.236  -21.770 -34.456 1.00 38.23  ? 54  GLY   B O   1 
ATOM   1164 N N   . PRO   B 1 56 ? 26.816  -22.161 -35.980 1.00 36.23  ? 55  PRO   B N   1 
ATOM   1165 C CA  . PRO   B 1 56 ? 25.867  -22.014 -37.080 1.00 31.76  ? 55  PRO   B CA  1 
ATOM   1166 C C   . PRO   B 1 56 ? 24.700  -22.998 -37.071 1.00 27.80  ? 55  PRO   B C   1 
ATOM   1167 O O   . PRO   B 1 56 ? 23.665  -22.691 -37.640 1.00 35.68  ? 55  PRO   B O   1 
ATOM   1168 C CB  . PRO   B 1 56 ? 26.744  -22.175 -38.338 1.00 33.24  ? 55  PRO   B CB  1 
ATOM   1169 C CG  . PRO   B 1 56 ? 28.147  -21.963 -37.858 1.00 30.28  ? 55  PRO   B CG  1 
ATOM   1170 C CD  . PRO   B 1 56 ? 28.170  -22.486 -36.420 1.00 34.61  ? 55  PRO   B CD  1 
ATOM   1171 N N   . LYS   B 1 57 ? 24.834  -24.175 -36.429 1.00 30.06  ? 56  LYS   B N   1 
ATOM   1172 C CA  . LYS   B 1 57 ? 23.728  -25.138 -36.389 1.00 32.24  ? 56  LYS   B CA  1 
ATOM   1173 C C   . LYS   B 1 57 ? 22.495  -24.527 -35.704 1.00 29.19  ? 56  LYS   B C   1 
ATOM   1174 O O   . LYS   B 1 57 ? 21.351  -24.877 -36.010 1.00 28.63  ? 56  LYS   B O   1 
ATOM   1175 C CB  . LYS   B 1 57 ? 24.136  -26.454 -35.708 1.00 32.90  ? 56  LYS   B CB  1 
ATOM   1176 C CG  . LYS   B 1 57 ? 24.138  -26.341 -34.177 1.00 34.99  ? 56  LYS   B CG  1 
ATOM   1177 C CD  . LYS   B 1 57 ? 24.715  -27.551 -33.438 1.00 44.29  ? 56  LYS   B CD  1 
ATOM   1178 C CE  . LYS   B 1 57 ? 24.692  -27.493 -31.931 1.00 47.35  ? 56  LYS   B CE  1 
ATOM   1179 N NZ  . LYS   B 1 57 ? 23.311  -27.398 -31.425 1.00 50.40  ? 56  LYS   B NZ  1 
ATOM   1180 N N   . ASP   B 1 58 ? 22.741  -23.577 -34.805 1.00 35.55  ? 57  ASP   B N   1 
ATOM   1181 C CA  . ASP   B 1 58 ? 21.647  -22.941 -34.076 1.00 36.76  ? 57  ASP   B CA  1 
ATOM   1182 C C   . ASP   B 1 58 ? 21.276  -21.579 -34.663 1.00 32.69  ? 57  ASP   B C   1 
ATOM   1183 O O   . ASP   B 1 58 ? 20.545  -20.801 -34.042 1.00 34.00  ? 57  ASP   B O   1 
ATOM   1184 C CB  . ASP   B 1 58 ? 21.944  -22.866 -32.587 1.00 33.47  ? 57  ASP   B CB  1 
ATOM   1185 C CG  . ASP   B 1 58 ? 22.002  -24.217 -31.896 1.00 40.18  ? 57  ASP   B CG  1 
ATOM   1186 O OD1 . ASP   B 1 58 ? 21.069  -25.001 -32.116 1.00 37.37  ? 57  ASP   B OD1 1 
ATOM   1187 O OD2 . ASP   B 1 58 ? 22.977  -24.463 -31.164 1.00 43.26  ? 57  ASP   B OD2 1 
ATOM   1188 N N   . LEU   B 1 59 ? 21.691  -21.307 -35.904 1.00 35.36  ? 58  LEU   B N   1 
ATOM   1189 C CA  . LEU   B 1 59 ? 21.605  -19.950 -36.427 1.00 32.73  ? 58  LEU   B CA  1 
ATOM   1190 C C   . LEU   B 1 59 ? 20.893  -19.983 -37.774 1.00 36.79  ? 58  LEU   B C   1 
ATOM   1191 O O   . LEU   B 1 59 ? 21.388  -20.573 -38.727 1.00 32.97  ? 58  LEU   B O   1 
ATOM   1192 C CB  . LEU   B 1 59 ? 22.991  -19.304 -36.544 1.00 33.02  ? 58  LEU   B CB  1 
ATOM   1193 C CG  . LEU   B 1 59 ? 23.779  -19.025 -35.260 1.00 37.54  ? 58  LEU   B CG  1 
ATOM   1194 C CD1 . LEU   B 1 59 ? 25.148  -18.403 -35.596 1.00 34.21  ? 58  LEU   B CD1 1 
ATOM   1195 C CD2 . LEU   B 1 59 ? 23.010  -18.072 -34.353 1.00 32.36  ? 58  LEU   B CD2 1 
ATOM   1196 N N   . PHE   B 1 60 ? 19.722  -19.356 -37.833 1.00 30.11  ? 59  PHE   B N   1 
ATOM   1197 C CA  . PHE   B 1 60 ? 18.805  -19.515 -38.953 1.00 32.74  ? 59  PHE   B CA  1 
ATOM   1198 C C   . PHE   B 1 60 ? 18.609  -18.164 -39.639 1.00 34.20  ? 59  PHE   B C   1 
ATOM   1199 O O   . PHE   B 1 60 ? 17.878  -17.307 -39.149 1.00 31.58  ? 59  PHE   B O   1 
ATOM   1200 C CB  . PHE   B 1 60 ? 17.438  -20.072 -38.529 1.00 30.67  ? 59  PHE   B CB  1 
ATOM   1201 C CG  . PHE   B 1 60 ? 17.488  -21.489 -37.967 1.00 31.08  ? 59  PHE   B CG  1 
ATOM   1202 C CD1 . PHE   B 1 60 ? 18.001  -21.750 -36.684 1.00 31.69  ? 59  PHE   B CD1 1 
ATOM   1203 C CD2 . PHE   B 1 60 ? 17.058  -22.567 -38.740 1.00 34.12  ? 59  PHE   B CD2 1 
ATOM   1204 C CE1 . PHE   B 1 60 ? 18.011  -23.049 -36.173 1.00 33.44  ? 59  PHE   B CE1 1 
ATOM   1205 C CE2 . PHE   B 1 60 ? 17.123  -23.881 -38.253 1.00 29.60  ? 59  PHE   B CE2 1 
ATOM   1206 C CZ  . PHE   B 1 60 ? 17.593  -24.107 -36.960 1.00 31.10  ? 59  PHE   B CZ  1 
ATOM   1207 N N   . PRO   B 1 61 ? 19.193  -17.965 -40.851 1.00 34.73  ? 60  PRO   B N   1 
ATOM   1208 C CA  . PRO   B 1 61 ? 18.996  -16.725 -41.617 1.00 33.65  ? 60  PRO   B CA  1 
ATOM   1209 C C   . PRO   B 1 61 ? 17.566  -16.179 -41.660 1.00 35.56  ? 60  PRO   B C   1 
ATOM   1210 O O   . PRO   B 1 61 ? 16.615  -16.868 -42.019 1.00 36.58  ? 60  PRO   B O   1 
ATOM   1211 C CB  . PRO   B 1 61 ? 19.621  -17.006 -43.018 1.00 34.87  ? 60  PRO   B CB  1 
ATOM   1212 C CG  . PRO   B 1 61 ? 20.591  -18.131 -42.746 1.00 41.73  ? 60  PRO   B CG  1 
ATOM   1213 C CD  . PRO   B 1 61 ? 20.096  -18.916 -41.521 1.00 33.10  ? 60  PRO   B CD  1 
ATOM   1214 N N   . TYR   B 1 62 ? 17.417  -14.911 -41.247 1.00 36.42  ? 61  TYR   B N   1 
ATOM   1215 C CA  . TYR   B 1 62 ? 16.111  -14.360 -40.935 1.00 32.61  ? 61  TYR   B CA  1 
ATOM   1216 C C   . TYR   B 1 62 ? 15.184  -14.415 -42.129 1.00 36.02  ? 61  TYR   B C   1 
ATOM   1217 O O   . TYR   B 1 62 ? 14.052  -14.869 -42.003 1.00 39.94  ? 61  TYR   B O   1 
ATOM   1218 C CB  . TYR   B 1 62 ? 16.240  -12.921 -40.448 1.00 38.14  ? 61  TYR   B CB  1 
ATOM   1219 C CG  . TYR   B 1 62 ? 14.938  -12.174 -40.195 1.00 40.22  ? 61  TYR   B CG  1 
ATOM   1220 C CD1 . TYR   B 1 62 ? 14.116  -12.466 -39.110 1.00 37.14  ? 61  TYR   B CD1 1 
ATOM   1221 C CD2 . TYR   B 1 62 ? 14.591  -11.101 -41.002 1.00 46.14  ? 61  TYR   B CD2 1 
ATOM   1222 C CE1 . TYR   B 1 62 ? 12.966  -11.727 -38.860 1.00 34.31  ? 61  TYR   B CE1 1 
ATOM   1223 C CE2 . TYR   B 1 62 ? 13.448  -10.362 -40.764 1.00 47.62  ? 61  TYR   B CE2 1 
ATOM   1224 C CZ  . TYR   B 1 62 ? 12.642  -10.664 -39.684 1.00 39.05  ? 61  TYR   B CZ  1 
ATOM   1225 O OH  . TYR   B 1 62 ? 11.537  -9.873  -39.536 1.00 40.94  ? 61  TYR   B OH  1 
ATOM   1226 N N   . ASP   B 1 63 ? 15.680  -13.980 -43.299 1.00 41.99  ? 62  ASP   B N   1 
ATOM   1227 C CA  . ASP   B 1 63 ? 14.783  -13.918 -44.447 1.00 43.83  ? 62  ASP   B CA  1 
ATOM   1228 C C   . ASP   B 1 63 ? 14.231  -15.303 -44.787 1.00 39.76  ? 62  ASP   B C   1 
ATOM   1229 O O   . ASP   B 1 63 ? 13.044  -15.443 -45.036 1.00 38.17  ? 62  ASP   B O   1 
ATOM   1230 C CB  . ASP   B 1 63 ? 15.378  -13.121 -45.594 1.00 53.95  ? 62  ASP   B CB  1 
ATOM   1231 C CG  . ASP   B 1 63 ? 15.348  -11.611 -45.370 1.00 64.54  ? 62  ASP   B CG  1 
ATOM   1232 O OD1 . ASP   B 1 63 ? 16.398  -10.962 -45.559 1.00 83.33  ? 62  ASP   B OD1 1 
ATOM   1233 O OD2 . ASP   B 1 63 ? 14.278  -11.082 -44.983 1.00 64.33  ? 62  ASP   B OD2 1 
ATOM   1234 N N   . LYS   B 1 64 ? 15.103  -16.315 -44.810 1.00 36.51  ? 63  LYS   B N   1 
ATOM   1235 C CA  . LYS   B 1 64 ? 14.710  -17.671 -45.145 1.00 38.79  ? 63  LYS   B CA  1 
ATOM   1236 C C   . LYS   B 1 64 ? 13.668  -18.234 -44.167 1.00 43.26  ? 63  LYS   B C   1 
ATOM   1237 O O   . LYS   B 1 64 ? 12.800  -18.979 -44.599 1.00 43.45  ? 63  LYS   B O   1 
ATOM   1238 C CB  . LYS   B 1 64 ? 15.942  -18.573 -45.170 1.00 40.74  ? 63  LYS   B CB  1 
ATOM   1239 C CG  . LYS   B 1 64 ? 15.661  -19.964 -45.707 1.00 39.77  ? 63  LYS   B CG  1 
ATOM   1240 C CD  . LYS   B 1 64 ? 16.918  -20.807 -45.734 1.00 44.50  ? 63  LYS   B CD  1 
ATOM   1241 C CE  . LYS   B 1 64 ? 16.753  -22.089 -46.480 1.00 53.01  ? 63  LYS   B CE  1 
ATOM   1242 N NZ  . LYS   B 1 64 ? 15.501  -22.794 -46.214 1.00 52.27  ? 63  LYS   B NZ  1 
ATOM   1243 N N   . SER   B 1 65 ? 13.775  -17.908 -42.866 1.00 41.94  ? 64  SER   B N   1 
ATOM   1244 C CA  . SER   B 1 65 ? 13.106  -18.669 -41.810 1.00 43.88  ? 64  SER   B CA  1 
ATOM   1245 C C   . SER   B 1 65 ? 12.031  -17.864 -41.071 1.00 40.34  ? 64  SER   B C   1 
ATOM   1246 O O   . SER   B 1 65 ? 11.498  -18.311 -40.061 1.00 44.70  ? 64  SER   B O   1 
ATOM   1247 C CB  . SER   B 1 65 ? 14.115  -19.267 -40.861 1.00 38.96  ? 64  SER   B CB  1 
ATOM   1248 O OG  . SER   B 1 65 ? 14.853  -18.210 -40.266 1.00 43.40  ? 64  SER   B OG  1 
ATOM   1249 N N   . LYS   B 1 66 ? 11.660  -16.699 -41.596 1.00 49.20  ? 65  LYS   B N   1 
ATOM   1250 C CA  . LYS   B 1 66 ? 10.838  -15.790 -40.814 1.00 44.39  ? 65  LYS   B CA  1 
ATOM   1251 C C   . LYS   B 1 66 ? 9.378   -16.210 -40.828 1.00 47.31  ? 65  LYS   B C   1 
ATOM   1252 O O   . LYS   B 1 66 ? 8.679   -16.020 -39.835 1.00 51.15  ? 65  LYS   B O   1 
ATOM   1253 C CB  . LYS   B 1 66 ? 11.080  -14.297 -41.057 1.00 44.13  ? 65  LYS   B CB  1 
ATOM   1254 C CG  . LYS   B 1 66 ? 10.716  -13.756 -42.423 1.00 43.49  ? 65  LYS   B CG  1 
ATOM   1255 N N   . ASP   B 1 67 ? 8.914   -16.834 -41.909 1.00 47.76  ? 66  ASP   B N   1 
ATOM   1256 C CA  . ASP   B 1 67 ? 7.527   -17.284 -41.894 1.00 49.71  ? 66  ASP   B CA  1 
ATOM   1257 C C   . ASP   B 1 67 ? 7.366   -18.463 -40.941 1.00 43.00  ? 66  ASP   B C   1 
ATOM   1258 O O   . ASP   B 1 67 ? 6.290   -18.661 -40.391 1.00 47.33  ? 66  ASP   B O   1 
ATOM   1259 C CB  . ASP   B 1 67 ? 6.897   -17.432 -43.275 1.00 61.82  ? 66  ASP   B CB  1 
ATOM   1260 C CG  . ASP   B 1 67 ? 7.590   -18.354 -44.267 1.00 76.35  ? 66  ASP   B CG  1 
ATOM   1261 O OD1 . ASP   B 1 67 ? 7.822   -17.904 -45.414 1.00 85.06  ? 66  ASP   B OD1 1 
ATOM   1262 O OD2 . ASP   B 1 67 ? 7.866   -19.518 -43.898 1.00 82.56  ? 66  ASP   B OD2 1 
ATOM   1263 N N   . LYS   B 1 68 ? 8.463   -19.193 -40.695 1.00 44.21  ? 67  LYS   B N   1 
ATOM   1264 C CA  . LYS   B 1 68 ? 8.443   -20.356 -39.825 1.00 38.01  ? 67  LYS   B CA  1 
ATOM   1265 C C   . LYS   B 1 68 ? 8.618   -19.944 -38.366 1.00 37.41  ? 67  LYS   B C   1 
ATOM   1266 O O   . LYS   B 1 68 ? 7.858   -20.395 -37.518 1.00 43.93  ? 67  LYS   B O   1 
ATOM   1267 C CB  . LYS   B 1 68 ? 9.484   -21.376 -40.288 1.00 53.70  ? 67  LYS   B CB  1 
ATOM   1268 C CG  . LYS   B 1 68 ? 9.506   -22.693 -39.525 1.00 52.82  ? 67  LYS   B CG  1 
ATOM   1269 C CD  . LYS   B 1 68 ? 10.424  -23.672 -40.249 1.00 68.07  ? 67  LYS   B CD  1 
ATOM   1270 C CE  . LYS   B 1 68 ? 10.522  -25.035 -39.624 1.00 74.28  ? 67  LYS   B CE  1 
ATOM   1271 N NZ  . LYS   B 1 68 ? 9.270   -25.800 -39.677 1.00 72.01  ? 67  LYS   B NZ  1 
ATOM   1272 N N   . TYR   B 1 69 ? 9.587   -19.066 -38.062 1.00 33.73  ? 68  TYR   B N   1 
ATOM   1273 C CA  . TYR   B 1 69 ? 9.924   -18.811 -36.667 1.00 33.29  ? 68  TYR   B CA  1 
ATOM   1274 C C   . TYR   B 1 69 ? 9.366   -17.478 -36.148 1.00 36.01  ? 68  TYR   B C   1 
ATOM   1275 O O   . TYR   B 1 69 ? 9.518   -17.180 -34.954 1.00 34.43  ? 68  TYR   B O   1 
ATOM   1276 C CB  . TYR   B 1 69 ? 11.451  -18.843 -36.540 1.00 31.15  ? 68  TYR   B CB  1 
ATOM   1277 C CG  . TYR   B 1 69 ? 11.989  -20.243 -36.809 1.00 34.24  ? 68  TYR   B CG  1 
ATOM   1278 C CD1 . TYR   B 1 69 ? 11.374  -21.353 -36.256 1.00 34.27  ? 68  TYR   B CD1 1 
ATOM   1279 C CD2 . TYR   B 1 69 ? 13.101  -20.445 -37.631 1.00 33.78  ? 68  TYR   B CD2 1 
ATOM   1280 C CE1 . TYR   B 1 69 ? 11.847  -22.643 -36.471 1.00 39.95  ? 68  TYR   B CE1 1 
ATOM   1281 C CE2 . TYR   B 1 69 ? 13.609  -21.714 -37.832 1.00 39.72  ? 68  TYR   B CE2 1 
ATOM   1282 C CZ  . TYR   B 1 69 ? 12.953  -22.813 -37.283 1.00 39.43  ? 68  TYR   B CZ  1 
ATOM   1283 O OH  . TYR   B 1 69 ? 13.415  -24.049 -37.528 1.00 41.89  ? 68  TYR   B OH  1 
ATOM   1284 N N   . GLY   B 1 70 ? 8.687   -16.726 -37.017 1.00 36.64  ? 69  GLY   B N   1 
ATOM   1285 C CA  . GLY   B 1 70 ? 8.332   -15.343 -36.721 1.00 45.90  ? 69  GLY   B CA  1 
ATOM   1286 C C   . GLY   B 1 70 ? 6.960   -15.133 -36.071 1.00 47.70  ? 69  GLY   B C   1 
ATOM   1287 O O   . GLY   B 1 70 ? 6.382   -14.067 -36.243 1.00 44.38  ? 69  GLY   B O   1 
ATOM   1288 N N   . LYS   B 1 71 ? 6.440   -16.108 -35.311 1.00 44.67  ? 70  LYS   B N   1 
ATOM   1289 C CA  . LYS   B 1 71 ? 5.127   -15.939 -34.710 1.00 50.02  ? 70  LYS   B CA  1 
ATOM   1290 C C   . LYS   B 1 71 ? 5.249   -15.395 -33.290 1.00 47.24  ? 70  LYS   B C   1 
ATOM   1291 O O   . LYS   B 1 71 ? 6.082   -15.864 -32.511 1.00 46.31  ? 70  LYS   B O   1 
ATOM   1292 C CB  . LYS   B 1 71 ? 4.362   -17.261 -34.566 1.00 52.64  ? 70  LYS   B CB  1 
ATOM   1293 C CG  . LYS   B 1 71 ? 3.337   -17.555 -35.647 1.00 60.05  ? 70  LYS   B CG  1 
ATOM   1294 C CD  . LYS   B 1 71 ? 3.875   -17.714 -37.064 1.00 65.26  ? 70  LYS   B CD  1 
ATOM   1295 C CE  . LYS   B 1 71 ? 3.031   -18.680 -37.838 1.00 73.26  ? 70  LYS   B CE  1 
ATOM   1296 N NZ  . LYS   B 1 71 ? 3.253   -18.539 -39.279 1.00 78.94  ? 70  LYS   B NZ  1 
ATOM   1297 N N   . PRO   B 1 72 ? 4.373   -14.445 -32.877 1.00 43.67  ? 71  PRO   B N   1 
ATOM   1298 C CA  . PRO   B 1 72 ? 4.256   -14.084 -31.458 1.00 41.02  ? 71  PRO   B CA  1 
ATOM   1299 C C   . PRO   B 1 72 ? 4.062   -15.298 -30.551 1.00 39.99  ? 71  PRO   B C   1 
ATOM   1300 O O   . PRO   B 1 72 ? 3.431   -16.284 -30.952 1.00 43.62  ? 71  PRO   B O   1 
ATOM   1301 C CB  . PRO   B 1 72 ? 3.067   -13.101 -31.407 1.00 42.73  ? 71  PRO   B CB  1 
ATOM   1302 C CG  . PRO   B 1 72 ? 3.000   -12.548 -32.811 1.00 49.93  ? 71  PRO   B CG  1 
ATOM   1303 C CD  . PRO   B 1 72 ? 3.424   -13.708 -33.733 1.00 47.48  ? 71  PRO   B CD  1 
ATOM   1304 N N   . ASN   B 1 73 ? 4.619   -15.213 -29.328 1.00 38.09  ? 72  ASN   B N   1 
ATOM   1305 C CA  . ASN   B 1 73 ? 4.378   -16.193 -28.282 1.00 41.94  ? 72  ASN   B CA  1 
ATOM   1306 C C   . ASN   B 1 73 ? 4.381   -15.495 -26.908 1.00 47.67  ? 72  ASN   B C   1 
ATOM   1307 O O   . ASN   B 1 73 ? 4.522   -14.263 -26.824 1.00 51.81  ? 72  ASN   B O   1 
ATOM   1308 C CB  . ASN   B 1 73 ? 5.331   -17.384 -28.382 1.00 38.53  ? 72  ASN   B CB  1 
ATOM   1309 C CG  . ASN   B 1 73 ? 6.777   -17.002 -28.164 1.00 42.16  ? 72  ASN   B CG  1 
ATOM   1310 O OD1 . ASN   B 1 73 ? 7.086   -16.311 -27.194 1.00 38.51  ? 72  ASN   B OD1 1 
ATOM   1311 N ND2 . ASN   B 1 73 ? 7.689   -17.412 -29.045 1.00 41.50  ? 72  ASN   B ND2 1 
ATOM   1312 N N   . LYS   B 1 74 ? 4.308   -16.300 -25.842 1.00 40.24  ? 73  LYS   B N   1 
ATOM   1313 C CA  . LYS   B 1 74 ? 4.064   -15.853 -24.467 1.00 41.64  ? 73  LYS   B CA  1 
ATOM   1314 C C   . LYS   B 1 74 ? 5.369   -15.717 -23.674 1.00 42.37  ? 73  LYS   B C   1 
ATOM   1315 O O   . LYS   B 1 74 ? 5.380   -15.586 -22.445 1.00 37.37  ? 73  LYS   B O   1 
ATOM   1316 C CB  . LYS   B 1 74 ? 3.159   -16.865 -23.754 1.00 46.52  ? 73  LYS   B CB  1 
ATOM   1317 N N   . ARG   B 1 75 ? 6.502   -15.767 -24.371 1.00 37.20  ? 74  ARG   B N   1 
ATOM   1318 C CA  . ARG   B 1 75 ? 7.762   -15.617 -23.672 1.00 36.88  ? 74  ARG   B CA  1 
ATOM   1319 C C   . ARG   B 1 75 ? 8.049   -14.115 -23.580 1.00 39.74  ? 74  ARG   B C   1 
ATOM   1320 O O   . ARG   B 1 75 ? 7.857   -13.390 -24.551 1.00 38.22  ? 74  ARG   B O   1 
ATOM   1321 C CB  . ARG   B 1 75 ? 8.912   -16.410 -24.302 1.00 35.73  ? 74  ARG   B CB  1 
ATOM   1322 C CG  . ARG   B 1 75 ? 8.820   -17.896 -24.622 1.00 37.84  ? 74  ARG   B CG  1 
ATOM   1323 C CD  . ARG   B 1 75 ? 8.430   -18.774 -23.418 1.00 40.28  ? 74  ARG   B CD  1 
ATOM   1324 N NE  . ARG   B 1 75 ? 8.782   -20.198 -23.550 1.00 42.01  ? 74  ARG   B NE  1 
ATOM   1325 C CZ  . ARG   B 1 75 ? 9.978   -20.755 -23.367 1.00 37.31  ? 74  ARG   B CZ  1 
ATOM   1326 N NH1 . ARG   B 1 75 ? 11.028  -20.043 -22.984 1.00 40.06  ? 74  ARG   B NH1 1 
ATOM   1327 N NH2 . ARG   B 1 75 ? 10.165  -22.040 -23.620 1.00 41.25  ? 74  ARG   B NH2 1 
ATOM   1328 N N   . LYS   B 1 76 ? 8.524   -13.681 -22.398 1.00 37.76  ? 75  LYS   B N   1 
ATOM   1329 C CA  . LYS   B 1 76 ? 8.891   -12.313 -22.093 1.00 33.99  ? 75  LYS   B CA  1 
ATOM   1330 C C   . LYS   B 1 76 ? 9.986   -11.835 -23.047 1.00 30.28  ? 75  LYS   B C   1 
ATOM   1331 O O   . LYS   B 1 76 ? 11.067  -12.418 -23.107 1.00 31.66  ? 75  LYS   B O   1 
ATOM   1332 C CB  . LYS   B 1 76 ? 9.505   -12.244 -20.689 1.00 36.32  ? 75  LYS   B CB  1 
ATOM   1333 C CG  . LYS   B 1 76 ? 9.789   -10.833 -20.176 1.00 35.27  ? 75  LYS   B CG  1 
ATOM   1334 C CD  . LYS   B 1 76 ? 10.622  -10.759 -18.901 1.00 40.80  ? 75  LYS   B CD  1 
ATOM   1335 C CE  . LYS   B 1 76 ? 11.002  -9.311  -18.631 1.00 48.02  ? 75  LYS   B CE  1 
ATOM   1336 N NZ  . LYS   B 1 76 ? 11.417  -9.054  -17.253 1.00 54.11  ? 75  LYS   B NZ  1 
ATOM   1337 N N   . GLY   B 1 77 ? 9.718   -10.736 -23.731 1.00 30.77  ? 76  GLY   B N   1 
ATOM   1338 C CA  . GLY   B 1 77 ? 10.780  -10.155 -24.561 1.00 35.93  ? 76  GLY   B CA  1 
ATOM   1339 C C   . GLY   B 1 77 ? 10.573  -10.470 -26.048 1.00 40.29  ? 76  GLY   B C   1 
ATOM   1340 O O   . GLY   B 1 77 ? 11.101  -9.761  -26.913 1.00 34.66  ? 76  GLY   B O   1 
ATOM   1341 N N   . PHE   B 1 78 ? 9.755   -11.496 -26.348 1.00 34.38  ? 77  PHE   B N   1 
ATOM   1342 C CA  . PHE   B 1 78 ? 9.751   -12.117 -27.668 1.00 35.22  ? 77  PHE   B CA  1 
ATOM   1343 C C   . PHE   B 1 78 ? 9.095   -11.217 -28.697 1.00 35.02  ? 77  PHE   B C   1 
ATOM   1344 O O   . PHE   B 1 78 ? 9.639   -11.029 -29.804 1.00 33.57  ? 77  PHE   B O   1 
ATOM   1345 C CB  . PHE   B 1 78 ? 9.049   -13.476 -27.702 1.00 30.97  ? 77  PHE   B CB  1 
ATOM   1346 C CG  . PHE   B 1 78 ? 9.256   -14.201 -29.019 1.00 34.89  ? 77  PHE   B CG  1 
ATOM   1347 C CD1 . PHE   B 1 78 ? 10.400  -14.986 -29.219 1.00 30.44  ? 77  PHE   B CD1 1 
ATOM   1348 C CD2 . PHE   B 1 78 ? 8.321   -14.065 -30.040 1.00 37.16  ? 77  PHE   B CD2 1 
ATOM   1349 C CE1 . PHE   B 1 78 ? 10.569  -15.666 -30.418 1.00 35.01  ? 77  PHE   B CE1 1 
ATOM   1350 C CE2 . PHE   B 1 78 ? 8.514   -14.729 -31.247 1.00 36.69  ? 77  PHE   B CE2 1 
ATOM   1351 C CZ  . PHE   B 1 78 ? 9.613   -15.562 -31.393 1.00 34.42  ? 77  PHE   B CZ  1 
ATOM   1352 N N   . ASN   B 1 79 ? 7.937   -10.653 -28.328 1.00 33.48  ? 78  ASN   B N   1 
ATOM   1353 C CA  . ASN   B 1 79 ? 7.204   -9.780  -29.232 1.00 33.95  ? 78  ASN   B CA  1 
ATOM   1354 C C   . ASN   B 1 79 ? 7.895   -8.433  -29.431 1.00 34.20  ? 78  ASN   B C   1 
ATOM   1355 O O   . ASN   B 1 79 ? 7.762   -7.837  -30.507 1.00 36.93  ? 78  ASN   B O   1 
ATOM   1356 C CB  . ASN   B 1 79 ? 5.752   -9.578  -28.833 1.00 34.75  ? 78  ASN   B CB  1 
ATOM   1357 C CG  . ASN   B 1 79 ? 4.938   -10.848 -28.926 1.00 42.59  ? 78  ASN   B CG  1 
ATOM   1358 O OD1 . ASN   B 1 79 ? 5.415   -11.885 -29.393 1.00 39.04  ? 78  ASN   B OD1 1 
ATOM   1359 N ND2 . ASN   B 1 79 ? 3.713   -10.803 -28.426 1.00 46.92  ? 78  ASN   B ND2 1 
ATOM   1360 N N   . GLU   B 1 80 ? 8.624   -7.951  -28.414 1.00 31.18  ? 79  GLU   B N   1 
ATOM   1361 C CA  . GLU   B 1 80 ? 9.385   -6.720  -28.607 1.00 37.65  ? 79  GLU   B CA  1 
ATOM   1362 C C   . GLU   B 1 80 ? 10.611  -7.031  -29.475 1.00 30.46  ? 79  GLU   B C   1 
ATOM   1363 O O   . GLU   B 1 80 ? 11.089  -6.157  -30.187 1.00 33.77  ? 79  GLU   B O   1 
ATOM   1364 C CB  . GLU   B 1 80 ? 9.928   -6.037  -27.359 1.00 31.88  ? 79  GLU   B CB  1 
ATOM   1365 C CG  . GLU   B 1 80 ? 8.846   -5.459  -26.450 1.00 48.27  ? 79  GLU   B CG  1 
ATOM   1366 N N   . GLY   B 1 81 ? 11.112  -8.270  -29.384 1.00 30.01  ? 80  GLY   B N   1 
ATOM   1367 C CA  . GLY   B 1 81 ? 12.233  -8.727  -30.192 1.00 26.55  ? 80  GLY   B CA  1 
ATOM   1368 C C   . GLY   B 1 81 ? 11.808  -8.759  -31.653 1.00 28.58  ? 80  GLY   B C   1 
ATOM   1369 O O   . GLY   B 1 81 ? 12.578  -8.368  -32.545 1.00 31.47  ? 80  GLY   B O   1 
ATOM   1370 N N   . LEU   B 1 82 ? 10.601  -9.258  -31.876 1.00 27.12  ? 81  LEU   B N   1 
ATOM   1371 C CA  . LEU   B 1 82 ? 10.040  -9.298  -33.225 1.00 33.18  ? 81  LEU   B CA  1 
ATOM   1372 C C   . LEU   B 1 82 ? 9.934   -7.878  -33.776 1.00 34.74  ? 81  LEU   B C   1 
ATOM   1373 O O   . LEU   B 1 82 ? 10.148  -7.669  -34.975 1.00 33.13  ? 81  LEU   B O   1 
ATOM   1374 C CB  . LEU   B 1 82 ? 8.699   -10.026 -33.357 1.00 30.34  ? 81  LEU   B CB  1 
ATOM   1375 C CG  . LEU   B 1 82 ? 8.680   -11.532 -33.064 1.00 30.95  ? 81  LEU   B CG  1 
ATOM   1376 C CD1 . LEU   B 1 82 ? 7.241   -12.037 -33.124 1.00 32.36  ? 81  LEU   B CD1 1 
ATOM   1377 C CD2 . LEU   B 1 82 ? 9.573   -12.293 -34.090 1.00 31.80  ? 81  LEU   B CD2 1 
ATOM   1378 N N   . TRP   B 1 83 ? 9.466   -6.944  -32.937 1.00 31.57  ? 82  TRP   B N   1 
ATOM   1379 C CA  . TRP   B 1 83 ? 9.391   -5.545  -33.335 1.00 30.85  ? 82  TRP   B CA  1 
ATOM   1380 C C   . TRP   B 1 83 ? 10.757  -4.988  -33.738 1.00 30.51  ? 82  TRP   B C   1 
ATOM   1381 O O   . TRP   B 1 83 ? 10.854  -4.396  -34.803 1.00 36.83  ? 82  TRP   B O   1 
ATOM   1382 C CB  . TRP   B 1 83 ? 8.739   -4.656  -32.264 1.00 34.68  ? 82  TRP   B CB  1 
ATOM   1383 C CG  . TRP   B 1 83 ? 8.458   -3.270  -32.775 1.00 36.52  ? 82  TRP   B CG  1 
ATOM   1384 C CD1 . TRP   B 1 83 ? 7.313   -2.816  -33.364 1.00 39.76  ? 82  TRP   B CD1 1 
ATOM   1385 C CD2 . TRP   B 1 83 ? 9.403   -2.178  -32.810 1.00 40.77  ? 82  TRP   B CD2 1 
ATOM   1386 N NE1 . TRP   B 1 83 ? 7.474   -1.501  -33.723 1.00 44.65  ? 82  TRP   B NE1 1 
ATOM   1387 C CE2 . TRP   B 1 83 ? 8.743   -1.090  -33.410 1.00 42.17  ? 82  TRP   B CE2 1 
ATOM   1388 C CE3 . TRP   B 1 83 ? 10.729  -2.018  -32.372 1.00 38.22  ? 82  TRP   B CE3 1 
ATOM   1389 C CZ2 . TRP   B 1 83 ? 9.373   0.143   -33.595 1.00 49.01  ? 82  TRP   B CZ2 1 
ATOM   1390 C CZ3 . TRP   B 1 83 ? 11.345  -0.797  -32.551 1.00 44.53  ? 82  TRP   B CZ3 1 
ATOM   1391 C CH2 . TRP   B 1 83 ? 10.672  0.262   -33.160 1.00 46.80  ? 82  TRP   B CH2 1 
ATOM   1392 N N   . GLU   B 1 84 ? 11.773  -5.166  -32.880 1.00 28.09  ? 83  GLU   B N   1 
ATOM   1393 C CA  . GLU   B 1 84 ? 13.128  -4.677  -33.086 1.00 31.50  ? 83  GLU   B CA  1 
ATOM   1394 C C   . GLU   B 1 84 ? 13.721  -5.211  -34.401 1.00 33.78  ? 83  GLU   B C   1 
ATOM   1395 O O   . GLU   B 1 84 ? 14.405  -4.464  -35.134 1.00 33.48  ? 83  GLU   B O   1 
ATOM   1396 C CB  . GLU   B 1 84 ? 14.057  -4.999  -31.920 1.00 28.88  ? 83  GLU   B CB  1 
ATOM   1397 C CG  . GLU   B 1 84 ? 13.543  -4.483  -30.571 1.00 32.17  ? 83  GLU   B CG  1 
ATOM   1398 C CD  . GLU   B 1 84 ? 14.427  -4.630  -29.369 1.00 35.64  ? 83  GLU   B CD  1 
ATOM   1399 O OE1 . GLU   B 1 84 ? 15.397  -5.406  -29.401 1.00 33.93  ? 83  GLU   B OE1 1 
ATOM   1400 O OE2 . GLU   B 1 84 ? 14.118  -3.925  -28.360 1.00 40.80  ? 83  GLU   B OE2 1 
ATOM   1401 N N   . ILE   B 1 85 ? 13.483  -6.496  -34.697 1.00 34.79  ? 84  ILE   B N   1 
ATOM   1402 C CA  . ILE   B 1 85 ? 14.171  -7.128  -35.831 1.00 33.33  ? 84  ILE   B CA  1 
ATOM   1403 C C   . ILE   B 1 85 ? 13.573  -6.599  -37.140 1.00 32.01  ? 84  ILE   B C   1 
ATOM   1404 O O   . ILE   B 1 85 ? 14.292  -6.432  -38.143 1.00 32.14  ? 84  ILE   B O   1 
ATOM   1405 C CB  . ILE   B 1 85 ? 14.230  -8.670  -35.761 1.00 31.09  ? 84  ILE   B CB  1 
ATOM   1406 C CG1 . ILE   B 1 85 ? 15.322  -9.203  -36.757 1.00 34.84  ? 84  ILE   B CG1 1 
ATOM   1407 C CG2 . ILE   B 1 85 ? 12.847  -9.298  -36.035 1.00 32.20  ? 84  ILE   B CG2 1 
ATOM   1408 C CD1 . ILE   B 1 85 ? 15.816  -10.631 -36.511 1.00 33.48  ? 84  ILE   B CD1 1 
ATOM   1409 N N   . GLN   B 1 86 ? 12.268  -6.301  -37.118 1.00 33.39  ? 85  GLN   B N   1 
ATOM   1410 C CA  . GLN   B 1 86 ? 11.551  -5.726  -38.239 1.00 34.82  ? 85  GLN   B CA  1 
ATOM   1411 C C   . GLN   B 1 86 ? 11.748  -4.208  -38.372 1.00 38.50  ? 85  GLN   B C   1 
ATOM   1412 O O   . GLN   B 1 86 ? 11.705  -3.716  -39.498 1.00 38.81  ? 85  GLN   B O   1 
ATOM   1413 C CB  . GLN   B 1 86 ? 10.055  -6.048  -38.247 1.00 34.72  ? 85  GLN   B CB  1 
ATOM   1414 N N   . ASN   B 1 87 ? 11.974  -3.446  -37.288 1.00 30.91  ? 86  ASN   B N   1 
ATOM   1415 C CA  . ASN   B 1 87 ? 11.834  -1.992  -37.446 1.00 35.03  ? 86  ASN   B CA  1 
ATOM   1416 C C   . ASN   B 1 87 ? 13.139  -1.214  -37.251 1.00 34.74  ? 86  ASN   B C   1 
ATOM   1417 O O   . ASN   B 1 87 ? 13.256  -0.059  -37.685 1.00 36.87  ? 86  ASN   B O   1 
ATOM   1418 C CB  . ASN   B 1 87 ? 10.722  -1.399  -36.579 1.00 36.87  ? 86  ASN   B CB  1 
ATOM   1419 C CG  . ASN   B 1 87 ? 9.371   -1.885  -37.047 1.00 41.30  ? 86  ASN   B CG  1 
ATOM   1420 O OD1 . ASN   B 1 87 ? 8.895   -1.467  -38.108 1.00 43.01  ? 86  ASN   B OD1 1 
ATOM   1421 N ND2 . ASN   B 1 87 ? 8.752   -2.786  -36.297 1.00 42.44  ? 86  ASN   B ND2 1 
ATOM   1422 N N   . ASN   B 1 88 ? 14.103  -1.797  -36.544 1.00 31.83  ? 87  ASN   B N   1 
ATOM   1423 C CA  . ASN   B 1 88 ? 15.363  -1.102  -36.326 1.00 33.18  ? 87  ASN   B CA  1 
ATOM   1424 C C   . ASN   B 1 88 ? 16.390  -2.122  -35.862 1.00 33.61  ? 87  ASN   B C   1 
ATOM   1425 O O   . ASN   B 1 88 ? 16.880  -2.046  -34.735 1.00 33.83  ? 87  ASN   B O   1 
ATOM   1426 C CB  . ASN   B 1 88 ? 15.217  0.122   -35.400 1.00 38.39  ? 87  ASN   B CB  1 
ATOM   1427 C CG  . ASN   B 1 88 ? 16.327  1.137   -35.596 1.00 40.73  ? 87  ASN   B CG  1 
ATOM   1428 O OD1 . ASN   B 1 88 ? 17.354  0.817   -36.205 1.00 39.75  ? 87  ASN   B OD1 1 
ATOM   1429 N ND2 . ASN   B 1 88 ? 16.187  2.329   -35.033 1.00 35.64  ? 87  ASN   B ND2 1 
ATOM   1430 N N   . PRO   B 1 89 ? 16.694  -3.137  -36.710 1.00 30.38  ? 88  PRO   B N   1 
ATOM   1431 C CA  . PRO   B 1 89 ? 17.618  -4.205  -36.340 1.00 30.53  ? 88  PRO   B CA  1 
ATOM   1432 C C   . PRO   B 1 89 ? 19.036  -3.776  -36.001 1.00 30.14  ? 88  PRO   B C   1 
ATOM   1433 O O   . PRO   B 1 89 ? 19.765  -4.542  -35.371 1.00 31.39  ? 88  PRO   B O   1 
ATOM   1434 C CB  . PRO   B 1 89 ? 17.628  -5.098  -37.597 1.00 27.82  ? 88  PRO   B CB  1 
ATOM   1435 C CG  . PRO   B 1 89 ? 17.243  -4.142  -38.717 1.00 32.00  ? 88  PRO   B CG  1 
ATOM   1436 C CD  . PRO   B 1 89 ? 16.131  -3.303  -38.061 1.00 30.03  ? 88  PRO   B CD  1 
ATOM   1437 N N   . HIS   B 1 90 ? 19.461  -2.600  -36.503 1.00 34.16  ? 89  HIS   B N   1 
ATOM   1438 C CA  . HIS   B 1 90 ? 20.862  -2.189  -36.378 1.00 30.73  ? 89  HIS   B CA  1 
ATOM   1439 C C   . HIS   B 1 90 ? 21.062  -1.077  -35.344 1.00 36.80  ? 89  HIS   B C   1 
ATOM   1440 O O   . HIS   B 1 90 ? 22.178  -0.548  -35.232 1.00 38.22  ? 89  HIS   B O   1 
ATOM   1441 C CB  . HIS   B 1 90 ? 21.449  -1.850  -37.773 1.00 30.04  ? 89  HIS   B CB  1 
ATOM   1442 C CG  . HIS   B 1 90 ? 21.274  -2.932  -38.817 1.00 26.89  ? 89  HIS   B CG  1 
ATOM   1443 N ND1 . HIS   B 1 90 ? 21.858  -4.179  -38.668 1.00 27.21  ? 89  HIS   B ND1 1 
ATOM   1444 C CD2 . HIS   B 1 90 ? 20.559  -2.986  -39.966 1.00 30.20  ? 89  HIS   B CD2 1 
ATOM   1445 C CE1 . HIS   B 1 90 ? 21.535  -4.935  -39.708 1.00 27.80  ? 89  HIS   B CE1 1 
ATOM   1446 N NE2 . HIS   B 1 90 ? 20.736  -4.226  -40.517 1.00 29.35  ? 89  HIS   B NE2 1 
ATOM   1447 N N   . ALA   B 1 91 ? 20.020  -0.789  -34.538 1.00 34.63  ? 90  ALA   B N   1 
ATOM   1448 C CA  . ALA   B 1 91 ? 20.108  0.260   -33.524 1.00 34.13  ? 90  ALA   B CA  1 
ATOM   1449 C C   . ALA   B 1 91 ? 20.987  -0.160  -32.342 1.00 35.14  ? 90  ALA   B C   1 
ATOM   1450 O O   . ALA   B 1 91 ? 21.218  -1.349  -32.097 1.00 34.02  ? 90  ALA   B O   1 
ATOM   1451 C CB  . ALA   B 1 91 ? 18.722  0.687   -33.053 1.00 32.54  ? 90  ALA   B CB  1 
ATOM   1452 N N   . SER   B 1 92 ? 21.481  0.846   -31.597 1.00 33.39  ? 91  SER   B N   1 
ATOM   1453 C CA  . SER   B 1 92 ? 22.020  0.620   -30.263 1.00 40.94  ? 91  SER   B CA  1 
ATOM   1454 C C   . SER   B 1 92 ? 20.885  0.301   -29.288 1.00 39.14  ? 91  SER   B C   1 
ATOM   1455 O O   . SER   B 1 92 ? 19.919  1.039   -29.190 1.00 41.03  ? 91  SER   B O   1 
ATOM   1456 C CB  . SER   B 1 92 ? 22.872  1.751   -29.740 1.00 43.40  ? 91  SER   B CB  1 
ATOM   1457 O OG  . SER   B 1 92 ? 23.677  1.275   -28.661 1.00 45.62  ? 91  SER   B OG  1 
ATOM   1458 N N   . TYR   B 1 93 ? 21.008  -0.823  -28.585 1.00 36.28  ? 92  TYR   B N   1 
ATOM   1459 C CA  . TYR   B 1 93 ? 20.053  -1.143  -27.539 1.00 42.82  ? 92  TYR   B CA  1 
ATOM   1460 C C   . TYR   B 1 93 ? 20.759  -1.076  -26.187 1.00 50.72  ? 92  TYR   B C   1 
ATOM   1461 O O   . TYR   B 1 93 ? 20.156  -1.323  -25.144 1.00 54.82  ? 92  TYR   B O   1 
ATOM   1462 C CB  . TYR   B 1 93 ? 19.399  -2.474  -27.912 1.00 35.57  ? 92  TYR   B CB  1 
ATOM   1463 C CG  . TYR   B 1 93 ? 18.432  -2.334  -29.067 1.00 32.74  ? 92  TYR   B CG  1 
ATOM   1464 C CD1 . TYR   B 1 93 ? 17.160  -1.840  -28.884 1.00 29.51  ? 92  TYR   B CD1 1 
ATOM   1465 C CD2 . TYR   B 1 93 ? 18.810  -2.717  -30.355 1.00 34.60  ? 92  TYR   B CD2 1 
ATOM   1466 C CE1 . TYR   B 1 93 ? 16.276  -1.697  -29.942 1.00 32.46  ? 92  TYR   B CE1 1 
ATOM   1467 C CE2 . TYR   B 1 93 ? 17.928  -2.592  -31.413 1.00 30.92  ? 92  TYR   B CE2 1 
ATOM   1468 C CZ  . TYR   B 1 93 ? 16.661  -2.093  -31.208 1.00 30.83  ? 92  TYR   B CZ  1 
ATOM   1469 O OH  . TYR   B 1 93 ? 15.813  -1.959  -32.262 1.00 32.62  ? 92  TYR   B OH  1 
ATOM   1470 N N   . SER   B 1 94 ? 22.038  -0.695  -26.234 1.00 54.90  ? 93  SER   B N   1 
ATOM   1471 C CA  . SER   B 1 94 ? 22.830  -0.409  -25.049 1.00 69.96  ? 93  SER   B CA  1 
ATOM   1472 C C   . SER   B 1 94 ? 23.269  -1.732  -24.389 1.00 79.99  ? 93  SER   B C   1 
ATOM   1473 O O   . SER   B 1 94 ? 23.393  -1.759  -23.136 1.00 82.27  ? 93  SER   B O   1 
ATOM   1474 C CB  . SER   B 1 94 ? 22.074  0.531   -24.112 1.00 59.07  ? 93  SER   B CB  1 
ATOM   1475 O OG  . SER   B 1 94 ? 22.786  0.740   -22.902 1.00 65.25  ? 93  SER   B OG  1 
ATOM   1476 O OXT . SER   B 1 94 ? 23.485  -2.703  -25.161 1.00 89.23  ? 93  SER   B OXT 1 
ATOM   1477 N N   . HIS   C 1 4  ? 32.177  -23.867 27.056  1.00 86.82  ? 3   HIS   C N   1 
ATOM   1478 C CA  . HIS   C 1 4  ? 31.061  -22.898 27.257  1.00 93.73  ? 3   HIS   C CA  1 
ATOM   1479 C C   . HIS   C 1 4  ? 30.385  -23.206 28.601  1.00 100.28 ? 3   HIS   C C   1 
ATOM   1480 O O   . HIS   C 1 4  ? 30.951  -23.935 29.420  1.00 97.58  ? 3   HIS   C O   1 
ATOM   1481 C CB  . HIS   C 1 4  ? 30.189  -22.881 25.990  1.00 92.42  ? 3   HIS   C CB  1 
ATOM   1482 C CG  . HIS   C 1 4  ? 29.281  -21.696 25.852  1.00 98.66  ? 3   HIS   C CG  1 
ATOM   1483 N ND1 . HIS   C 1 4  ? 29.710  -20.468 25.390  1.00 91.09  ? 3   HIS   C ND1 1 
ATOM   1484 C CD2 . HIS   C 1 4  ? 27.973  -21.547 26.122  1.00 97.51  ? 3   HIS   C CD2 1 
ATOM   1485 C CE1 . HIS   C 1 4  ? 28.695  -19.616 25.392  1.00 87.62  ? 3   HIS   C CE1 1 
ATOM   1486 N NE2 . HIS   C 1 4  ? 27.628  -20.252 25.829  1.00 93.63  ? 3   HIS   C NE2 1 
ATOM   1487 N N   . ALA   C 1 5  ? 29.199  -22.615 28.836  1.00 92.12  ? 4   ALA   C N   1 
ATOM   1488 C CA  . ALA   C 1 5  ? 28.316  -22.975 29.941  1.00 82.94  ? 4   ALA   C CA  1 
ATOM   1489 C C   . ALA   C 1 5  ? 26.863  -22.603 29.636  1.00 64.60  ? 4   ALA   C C   1 
ATOM   1490 O O   . ALA   C 1 5  ? 26.598  -21.626 28.949  1.00 68.43  ? 4   ALA   C O   1 
ATOM   1491 C CB  . ALA   C 1 5  ? 28.775  -22.326 31.219  1.00 91.62  ? 4   ALA   C CB  1 
ATOM   1492 N N   . PHE   C 1 6  ? 25.937  -23.390 30.186  1.00 55.41  ? 5   PHE   C N   1 
ATOM   1493 C CA  . PHE   C 1 6  ? 24.528  -23.352 29.840  1.00 61.65  ? 5   PHE   C CA  1 
ATOM   1494 C C   . PHE   C 1 6  ? 23.725  -23.403 31.139  1.00 64.24  ? 5   PHE   C C   1 
ATOM   1495 O O   . PHE   C 1 6  ? 24.289  -23.629 32.207  1.00 83.73  ? 5   PHE   C O   1 
ATOM   1496 C CB  . PHE   C 1 6  ? 24.196  -24.519 28.897  1.00 64.28  ? 5   PHE   C CB  1 
ATOM   1497 C CG  . PHE   C 1 6  ? 25.073  -24.737 27.661  1.00 55.81  ? 5   PHE   C CG  1 
ATOM   1498 C CD1 . PHE   C 1 6  ? 26.172  -25.596 27.703  1.00 48.67  ? 5   PHE   C CD1 1 
ATOM   1499 C CD2 . PHE   C 1 6  ? 24.782  -24.110 26.449  1.00 57.70  ? 5   PHE   C CD2 1 
ATOM   1500 C CE1 . PHE   C 1 6  ? 26.962  -25.804 26.580  1.00 47.33  ? 5   PHE   C CE1 1 
ATOM   1501 C CE2 . PHE   C 1 6  ? 25.575  -24.323 25.321  1.00 51.21  ? 5   PHE   C CE2 1 
ATOM   1502 C CZ  . PHE   C 1 6  ? 26.658  -25.176 25.388  1.00 47.12  ? 5   PHE   C CZ  1 
ATOM   1503 N N   . LYS   C 1 7  ? 22.414  -23.184 31.033  1.00 49.55  ? 6   LYS   C N   1 
ATOM   1504 C CA  . LYS   C 1 7  ? 21.474  -23.276 32.142  1.00 51.15  ? 6   LYS   C CA  1 
ATOM   1505 C C   . LYS   C 1 7  ? 20.110  -23.507 31.506  1.00 49.95  ? 6   LYS   C C   1 
ATOM   1506 O O   . LYS   C 1 7  ? 19.964  -23.202 30.310  1.00 48.75  ? 6   LYS   C O   1 
ATOM   1507 C CB  . LYS   C 1 7  ? 21.493  -21.970 32.952  1.00 55.74  ? 6   LYS   C CB  1 
ATOM   1508 C CG  . LYS   C 1 7  ? 21.152  -20.697 32.172  1.00 52.55  ? 6   LYS   C CG  1 
ATOM   1509 C CD  . LYS   C 1 7  ? 21.438  -19.374 32.884  1.00 49.14  ? 6   LYS   C CD  1 
ATOM   1510 N N   . PRO   C 1 8  ? 19.080  -24.029 32.231  1.00 54.94  ? 7   PRO   C N   1 
ATOM   1511 C CA  . PRO   C 1 8  ? 17.801  -24.371 31.591  1.00 55.29  ? 7   PRO   C CA  1 
ATOM   1512 C C   . PRO   C 1 8  ? 17.178  -23.127 30.948  1.00 52.18  ? 7   PRO   C C   1 
ATOM   1513 O O   . PRO   C 1 8  ? 17.298  -22.020 31.482  1.00 53.26  ? 7   PRO   C O   1 
ATOM   1514 C CB  . PRO   C 1 8  ? 16.925  -25.021 32.697  1.00 55.14  ? 7   PRO   C CB  1 
ATOM   1515 C CG  . PRO   C 1 8  ? 17.904  -25.303 33.827  1.00 51.90  ? 7   PRO   C CG  1 
ATOM   1516 C CD  . PRO   C 1 8  ? 19.064  -24.311 33.682  1.00 53.23  ? 7   PRO   C CD  1 
ATOM   1517 N N   . GLY   C 1 9  ? 16.565  -23.307 29.768  1.00 53.97  ? 8   GLY   C N   1 
ATOM   1518 C CA  . GLY   C 1 9  ? 16.120  -22.165 28.982  1.00 47.33  ? 8   GLY   C CA  1 
ATOM   1519 C C   . GLY   C 1 9  ? 16.989  -21.923 27.751  1.00 48.08  ? 8   GLY   C C   1 
ATOM   1520 O O   . GLY   C 1 9  ? 16.438  -21.722 26.672  1.00 48.65  ? 8   GLY   C O   1 
ATOM   1521 N N   . ASP   C 1 10 ? 18.331  -21.938 27.924  1.00 43.90  ? 9   ASP   C N   1 
ATOM   1522 C CA  . ASP   C 1 10 ? 19.311  -21.674 26.879  1.00 43.32  ? 9   ASP   C CA  1 
ATOM   1523 C C   . ASP   C 1 10 ? 18.990  -22.398 25.567  1.00 42.77  ? 9   ASP   C C   1 
ATOM   1524 O O   . ASP   C 1 10 ? 18.502  -23.520 25.580  1.00 44.40  ? 9   ASP   C O   1 
ATOM   1525 C CB  . ASP   C 1 10 ? 20.723  -21.969 27.347  1.00 45.82  ? 9   ASP   C CB  1 
ATOM   1526 C CG  . ASP   C 1 10 ? 21.257  -20.957 28.352  1.00 52.77  ? 9   ASP   C CG  1 
ATOM   1527 O OD1 . ASP   C 1 10 ? 20.477  -20.048 28.764  1.00 54.43  ? 9   ASP   C OD1 1 
ATOM   1528 O OD2 . ASP   C 1 10 ? 22.441  -21.078 28.703  1.00 52.57  ? 9   ASP   C OD2 1 
ATOM   1529 N N   . LEU   C 1 11 ? 19.250  -21.723 24.429  1.00 40.98  ? 10  LEU   C N   1 
ATOM   1530 C CA  . LEU   C 1 11 ? 18.888  -22.257 23.121  1.00 43.21  ? 10  LEU   C CA  1 
ATOM   1531 C C   . LEU   C 1 11 ? 20.159  -22.730 22.420  1.00 41.36  ? 10  LEU   C C   1 
ATOM   1532 O O   . LEU   C 1 11 ? 21.154  -22.002 22.422  1.00 36.43  ? 10  LEU   C O   1 
ATOM   1533 C CB  . LEU   C 1 11 ? 18.083  -21.272 22.261  1.00 38.12  ? 10  LEU   C CB  1 
ATOM   1534 C CG  . LEU   C 1 11 ? 16.766  -20.738 22.840  1.00 36.55  ? 10  LEU   C CG  1 
ATOM   1535 C CD1 . LEU   C 1 11 ? 16.102  -19.791 21.842  1.00 34.79  ? 10  LEU   C CD1 1 
ATOM   1536 C CD2 . LEU   C 1 11 ? 15.805  -21.879 23.217  1.00 36.05  ? 10  LEU   C CD2 1 
ATOM   1537 N N   . VAL   C 1 12 ? 20.116  -23.953 21.849  1.00 35.73  ? 11  VAL   C N   1 
ATOM   1538 C CA  . VAL   C 1 12 ? 21.287  -24.614 21.268  1.00 37.39  ? 11  VAL   C CA  1 
ATOM   1539 C C   . VAL   C 1 12 ? 20.893  -25.361 19.984  1.00 34.47  ? 11  VAL   C C   1 
ATOM   1540 O O   . VAL   C 1 12 ? 19.707  -25.534 19.681  1.00 32.92  ? 11  VAL   C O   1 
ATOM   1541 C CB  . VAL   C 1 12 ? 21.950  -25.619 22.236  1.00 32.49  ? 11  VAL   C CB  1 
ATOM   1542 C CG1 . VAL   C 1 12 ? 22.428  -24.947 23.515  1.00 36.28  ? 11  VAL   C CG1 1 
ATOM   1543 C CG2 . VAL   C 1 12 ? 21.001  -26.780 22.566  1.00 30.66  ? 11  VAL   C CG2 1 
ATOM   1544 N N   . PHE   C 1 13 ? 21.916  -25.768 19.227  1.00 31.42  ? 12  PHE   C N   1 
ATOM   1545 C CA  . PHE   C 1 13 ? 21.847  -26.911 18.344  1.00 30.20  ? 12  PHE   C CA  1 
ATOM   1546 C C   . PHE   C 1 13 ? 22.533  -28.065 19.059  1.00 30.35  ? 12  PHE   C C   1 
ATOM   1547 O O   . PHE   C 1 13 ? 23.648  -27.897 19.575  1.00 35.62  ? 12  PHE   C O   1 
ATOM   1548 C CB  . PHE   C 1 13 ? 22.404  -26.705 16.922  1.00 32.43  ? 12  PHE   C CB  1 
ATOM   1549 C CG  . PHE   C 1 13 ? 21.550  -25.734 16.111  1.00 34.16  ? 12  PHE   C CG  1 
ATOM   1550 C CD1 . PHE   C 1 13 ? 20.495  -26.180 15.305  1.00 36.95  ? 12  PHE   C CD1 1 
ATOM   1551 C CD2 . PHE   C 1 13 ? 21.751  -24.353 16.226  1.00 40.48  ? 12  PHE   C CD2 1 
ATOM   1552 C CE1 . PHE   C 1 13 ? 19.692  -25.271 14.614  1.00 37.41  ? 12  PHE   C CE1 1 
ATOM   1553 C CE2 . PHE   C 1 13 ? 20.949  -23.446 15.525  1.00 37.95  ? 12  PHE   C CE2 1 
ATOM   1554 C CZ  . PHE   C 1 13 ? 19.934  -23.911 14.715  1.00 38.54  ? 12  PHE   C CZ  1 
ATOM   1555 N N   . ALA   C 1 14 ? 21.838  -29.206 19.080  1.00 30.72  ? 13  ALA   C N   1 
ATOM   1556 C CA  . ALA   C 1 14 ? 22.291  -30.390 19.799  1.00 36.77  ? 13  ALA   C CA  1 
ATOM   1557 C C   . ALA   C 1 14 ? 22.609  -31.511 18.809  1.00 32.81  ? 13  ALA   C C   1 
ATOM   1558 O O   . ALA   C 1 14 ? 21.785  -31.834 17.973  1.00 28.42  ? 13  ALA   C O   1 
ATOM   1559 C CB  . ALA   C 1 14 ? 21.236  -30.787 20.829  1.00 32.69  ? 13  ALA   C CB  1 
ATOM   1560 N N   . LYS   C 1 15 ? 23.813  -32.101 18.894  1.00 29.60  ? 14  LYS   C N   1 
ATOM   1561 C CA  . LYS   C 1 15 ? 24.191  -33.124 17.936  1.00 30.74  ? 14  LYS   C CA  1 
ATOM   1562 C C   . LYS   C 1 15 ? 24.173  -34.507 18.584  1.00 34.32  ? 14  LYS   C C   1 
ATOM   1563 O O   . LYS   C 1 15 ? 24.912  -34.769 19.536  1.00 31.42  ? 14  LYS   C O   1 
ATOM   1564 C CB  . LYS   C 1 15 ? 25.586  -32.807 17.362  1.00 29.94  ? 14  LYS   C CB  1 
ATOM   1565 C CG  . LYS   C 1 15 ? 26.103  -33.815 16.298  1.00 30.35  ? 14  LYS   C CG  1 
ATOM   1566 C CD  . LYS   C 1 15 ? 25.188  -33.899 15.083  1.00 29.94  ? 14  LYS   C CD  1 
ATOM   1567 C CE  . LYS   C 1 15 ? 25.752  -34.762 13.961  1.00 38.11  ? 14  LYS   C CE  1 
ATOM   1568 N NZ  . LYS   C 1 15 ? 25.586  -36.192 14.266  1.00 33.96  ? 14  LYS   C NZ  1 
ATOM   1569 N N   . MET   C 1 16 ? 23.359  -35.407 18.025  1.00 31.75  ? 15  MET   C N   1 
ATOM   1570 C CA  . MET   C 1 16 ? 23.380  -36.821 18.356  1.00 33.10  ? 15  MET   C CA  1 
ATOM   1571 C C   . MET   C 1 16 ? 23.856  -37.654 17.167  1.00 35.68  ? 15  MET   C C   1 
ATOM   1572 O O   . MET   C 1 16 ? 23.589  -37.301 16.009  1.00 33.54  ? 15  MET   C O   1 
ATOM   1573 C CB  . MET   C 1 16 ? 21.985  -37.343 18.707  1.00 33.35  ? 15  MET   C CB  1 
ATOM   1574 C CG  . MET   C 1 16 ? 21.476  -36.757 20.002  1.00 39.33  ? 15  MET   C CG  1 
ATOM   1575 S SD  . MET   C 1 16 ? 19.975  -37.585 20.555  1.00 45.27  ? 15  MET   C SD  1 
ATOM   1576 C CE  . MET   C 1 16 ? 18.942  -37.343 19.097  1.00 51.04  ? 15  MET   C CE  1 
ATOM   1577 N N   . LYS   C 1 17 ? 24.469  -38.817 17.485  1.00 36.45  ? 16  LYS   C N   1 
ATOM   1578 C CA  . LYS   C 1 17 ? 24.893  -39.779 16.472  1.00 36.36  ? 16  LYS   C CA  1 
ATOM   1579 C C   . LYS   C 1 17 ? 23.654  -40.212 15.689  1.00 29.84  ? 16  LYS   C C   1 
ATOM   1580 O O   . LYS   C 1 17 ? 22.637  -40.582 16.280  1.00 31.43  ? 16  LYS   C O   1 
ATOM   1581 C CB  . LYS   C 1 17 ? 25.650  -40.999 17.033  1.00 37.04  ? 16  LYS   C CB  1 
ATOM   1582 C CG  . LYS   C 1 17 ? 26.303  -41.958 15.987  1.00 35.70  ? 16  LYS   C CG  1 
ATOM   1583 C CD  . LYS   C 1 17 ? 27.336  -41.251 15.118  1.00 44.24  ? 16  LYS   C CD  1 
ATOM   1584 C CE  . LYS   C 1 17 ? 28.361  -42.122 14.426  1.00 46.18  ? 16  LYS   C CE  1 
ATOM   1585 N NZ  . LYS   C 1 17 ? 29.414  -41.318 13.792  1.00 43.50  ? 16  LYS   C NZ  1 
ATOM   1586 N N   . GLY   C 1 18 ? 23.751  -40.110 14.367  1.00 30.54  ? 17  GLY   C N   1 
ATOM   1587 C CA  . GLY   C 1 18 ? 22.627  -40.523 13.541  1.00 31.70  ? 17  GLY   C CA  1 
ATOM   1588 C C   . GLY   C 1 18 ? 21.686  -39.371 13.160  1.00 35.11  ? 17  GLY   C C   1 
ATOM   1589 O O   . GLY   C 1 18 ? 20.665  -39.649 12.515  1.00 36.19  ? 17  GLY   C O   1 
ATOM   1590 N N   . TYR   C 1 19 ? 22.009  -38.110 13.564  1.00 31.86  ? 18  TYR   C N   1 
ATOM   1591 C CA  . TYR   C 1 19 ? 21.090  -36.977 13.426  1.00 32.29  ? 18  TYR   C CA  1 
ATOM   1592 C C   . TYR   C 1 19 ? 21.827  -35.687 13.050  1.00 32.83  ? 18  TYR   C C   1 
ATOM   1593 O O   . TYR   C 1 19 ? 22.909  -35.418 13.555  1.00 31.95  ? 18  TYR   C O   1 
ATOM   1594 C CB  . TYR   C 1 19 ? 20.319  -36.761 14.734  1.00 29.25  ? 18  TYR   C CB  1 
ATOM   1595 C CG  . TYR   C 1 19 ? 19.415  -37.937 15.081  1.00 34.33  ? 18  TYR   C CG  1 
ATOM   1596 C CD1 . TYR   C 1 19 ? 19.886  -39.022 15.833  1.00 35.26  ? 18  TYR   C CD1 1 
ATOM   1597 C CD2 . TYR   C 1 19 ? 18.093  -37.978 14.636  1.00 40.23  ? 18  TYR   C CD2 1 
ATOM   1598 C CE1 . TYR   C 1 19 ? 19.061  -40.092 16.133  1.00 38.35  ? 18  TYR   C CE1 1 
ATOM   1599 C CE2 . TYR   C 1 19 ? 17.251  -39.029 14.965  1.00 42.80  ? 18  TYR   C CE2 1 
ATOM   1600 C CZ  . TYR   C 1 19 ? 17.749  -40.098 15.689  1.00 45.31  ? 18  TYR   C CZ  1 
ATOM   1601 O OH  . TYR   C 1 19 ? 16.930  -41.155 15.951  1.00 50.60  ? 18  TYR   C OH  1 
ATOM   1602 N N   . PRO   C 1 20 ? 21.229  -34.823 12.199  1.00 32.92  ? 19  PRO   C N   1 
ATOM   1603 C CA  . PRO   C 1 20 ? 21.811  -33.496 11.940  1.00 33.89  ? 19  PRO   C CA  1 
ATOM   1604 C C   . PRO   C 1 20 ? 21.800  -32.708 13.255  1.00 29.99  ? 19  PRO   C C   1 
ATOM   1605 O O   . PRO   C 1 20 ? 21.004  -33.035 14.131  1.00 30.43  ? 19  PRO   C O   1 
ATOM   1606 C CB  . PRO   C 1 20 ? 20.836  -32.884 10.908  1.00 35.14  ? 19  PRO   C CB  1 
ATOM   1607 C CG  . PRO   C 1 20 ? 19.524  -33.664 11.089  1.00 34.00  ? 19  PRO   C CG  1 
ATOM   1608 C CD  . PRO   C 1 20 ? 19.930  -35.069 11.510  1.00 30.62  ? 19  PRO   C CD  1 
ATOM   1609 N N   . HIS   C 1 21 ? 22.637  -31.666 13.355  1.00 33.11  ? 20  HIS   C N   1 
ATOM   1610 C CA  . HIS   C 1 21 ? 22.579  -30.683 14.435  1.00 33.31  ? 20  HIS   C CA  1 
ATOM   1611 C C   . HIS   C 1 21 ? 21.137  -30.161 14.517  1.00 35.74  ? 20  HIS   C C   1 
ATOM   1612 O O   . HIS   C 1 21 ? 20.579  -29.722 13.522  1.00 30.94  ? 20  HIS   C O   1 
ATOM   1613 C CB  . HIS   C 1 21 ? 23.564  -29.532 14.188  1.00 31.91  ? 20  HIS   C CB  1 
ATOM   1614 C CG  . HIS   C 1 21 ? 25.013  -29.979 14.217  1.00 34.33  ? 20  HIS   C CG  1 
ATOM   1615 N ND1 . HIS   C 1 21 ? 25.640  -30.583 13.150  1.00 39.47  ? 20  HIS   C ND1 1 
ATOM   1616 C CD2 . HIS   C 1 21 ? 25.914  -29.974 15.216  1.00 40.81  ? 20  HIS   C CD2 1 
ATOM   1617 C CE1 . HIS   C 1 21 ? 26.885  -30.924 13.493  1.00 37.95  ? 20  HIS   C CE1 1 
ATOM   1618 N NE2 . HIS   C 1 21 ? 27.083  -30.530 14.747  1.00 38.94  ? 20  HIS   C NE2 1 
ATOM   1619 N N   . TRP   C 1 22 ? 20.553  -30.170 15.719  1.00 31.89  ? 21  TRP   C N   1 
ATOM   1620 C CA  . TRP   C 1 22 ? 19.099  -30.108 15.864  1.00 33.19  ? 21  TRP   C CA  1 
ATOM   1621 C C   . TRP   C 1 22 ? 18.707  -28.933 16.760  1.00 28.37  ? 21  TRP   C C   1 
ATOM   1622 O O   . TRP   C 1 22 ? 19.349  -28.692 17.797  1.00 30.09  ? 21  TRP   C O   1 
ATOM   1623 C CB  . TRP   C 1 22 ? 18.591  -31.457 16.428  1.00 34.56  ? 21  TRP   C CB  1 
ATOM   1624 C CG  . TRP   C 1 22 ? 17.143  -31.764 16.130  1.00 33.28  ? 21  TRP   C CG  1 
ATOM   1625 C CD1 . TRP   C 1 22 ? 16.049  -31.241 16.755  1.00 33.94  ? 21  TRP   C CD1 1 
ATOM   1626 C CD2 . TRP   C 1 22 ? 16.627  -32.677 15.129  1.00 31.53  ? 21  TRP   C CD2 1 
ATOM   1627 N NE1 . TRP   C 1 22 ? 14.893  -31.735 16.192  1.00 33.89  ? 21  TRP   C NE1 1 
ATOM   1628 C CE2 . TRP   C 1 22 ? 15.213  -32.615 15.201  1.00 37.04  ? 21  TRP   C CE2 1 
ATOM   1629 C CE3 . TRP   C 1 22 ? 17.206  -33.527 14.174  1.00 30.06  ? 21  TRP   C CE3 1 
ATOM   1630 C CZ2 . TRP   C 1 22 ? 14.402  -33.394 14.363  1.00 35.96  ? 21  TRP   C CZ2 1 
ATOM   1631 C CZ3 . TRP   C 1 22 ? 16.415  -34.280 13.332  1.00 33.93  ? 21  TRP   C CZ3 1 
ATOM   1632 C CH2 . TRP   C 1 22 ? 15.023  -34.238 13.466  1.00 33.05  ? 21  TRP   C CH2 1 
ATOM   1633 N N   . PRO   C 1 23 ? 17.656  -28.151 16.425  1.00 30.27  ? 22  PRO   C N   1 
ATOM   1634 C CA  . PRO   C 1 23 ? 17.243  -27.050 17.297  1.00 31.82  ? 22  PRO   C CA  1 
ATOM   1635 C C   . PRO   C 1 23 ? 16.780  -27.616 18.639  1.00 32.94  ? 22  PRO   C C   1 
ATOM   1636 O O   . PRO   C 1 23 ? 16.018  -28.573 18.678  1.00 28.68  ? 22  PRO   C O   1 
ATOM   1637 C CB  . PRO   C 1 23 ? 16.104  -26.362 16.494  1.00 33.44  ? 22  PRO   C CB  1 
ATOM   1638 C CG  . PRO   C 1 23 ? 15.549  -27.481 15.670  1.00 28.69  ? 22  PRO   C CG  1 
ATOM   1639 C CD  . PRO   C 1 23 ? 16.813  -28.238 15.207  1.00 28.20  ? 22  PRO   C CD  1 
ATOM   1640 N N   . ALA   C 1 24 ? 17.270  -27.012 19.730  1.00 30.59  ? 23  ALA   C N   1 
ATOM   1641 C CA  . ALA   C 1 24 ? 16.958  -27.542 21.049  1.00 34.05  ? 23  ALA   C CA  1 
ATOM   1642 C C   . ALA   C 1 24 ? 17.138  -26.498 22.154  1.00 37.63  ? 23  ALA   C C   1 
ATOM   1643 O O   . ALA   C 1 24 ? 17.654  -25.389 21.928  1.00 34.43  ? 23  ALA   C O   1 
ATOM   1644 C CB  . ALA   C 1 24 ? 17.808  -28.802 21.305  1.00 32.72  ? 23  ALA   C CB  1 
ATOM   1645 N N   . ARG   C 1 25 ? 16.758  -26.896 23.389  1.00 39.85  ? 24  ARG   C N   1 
ATOM   1646 C CA  . ARG   C 1 25 ? 17.063  -26.099 24.570  1.00 38.86  ? 24  ARG   C CA  1 
ATOM   1647 C C   . ARG   C 1 25 ? 17.451  -26.981 25.763  1.00 41.86  ? 24  ARG   C C   1 
ATOM   1648 O O   . ARG   C 1 25 ? 17.149  -28.186 25.795  1.00 36.41  ? 24  ARG   C O   1 
ATOM   1649 C CB  . ARG   C 1 25 ? 15.836  -25.293 24.989  1.00 40.94  ? 24  ARG   C CB  1 
ATOM   1650 C CG  . ARG   C 1 25 ? 14.666  -26.105 25.507  1.00 38.24  ? 24  ARG   C CG  1 
ATOM   1651 C CD  . ARG   C 1 25 ? 13.629  -25.127 26.053  1.00 41.51  ? 24  ARG   C CD  1 
ATOM   1652 N NE  . ARG   C 1 25 ? 12.502  -25.921 26.558  1.00 43.95  ? 24  ARG   C NE  1 
ATOM   1653 C CZ  . ARG   C 1 25 ? 11.221  -25.763 26.276  1.00 52.20  ? 24  ARG   C CZ  1 
ATOM   1654 N NH1 . ARG   C 1 25 ? 10.809  -24.637 25.709  1.00 51.73  ? 24  ARG   C NH1 1 
ATOM   1655 N NH2 . ARG   C 1 25 ? 10.358  -26.726 26.588  1.00 51.18  ? 24  ARG   C NH2 1 
ATOM   1656 N N   . ILE   C 1 26 ? 18.083  -26.345 26.758  1.00 40.82  ? 25  ILE   C N   1 
ATOM   1657 C CA  . ILE   C 1 26 ? 18.373  -26.998 28.036  1.00 46.25  ? 25  ILE   C CA  1 
ATOM   1658 C C   . ILE   C 1 26 ? 17.079  -27.138 28.857  1.00 51.28  ? 25  ILE   C C   1 
ATOM   1659 O O   . ILE   C 1 26 ? 16.325  -26.180 29.020  1.00 50.66  ? 25  ILE   C O   1 
ATOM   1660 C CB  . ILE   C 1 26 ? 19.441  -26.208 28.812  1.00 50.00  ? 25  ILE   C CB  1 
ATOM   1661 C CG1 . ILE   C 1 26 ? 20.563  -25.645 27.922  1.00 40.22  ? 25  ILE   C CG1 1 
ATOM   1662 C CG2 . ILE   C 1 26 ? 19.984  -27.017 29.987  1.00 56.67  ? 25  ILE   C CG2 1 
ATOM   1663 C CD1 . ILE   C 1 26 ? 21.408  -26.681 27.204  1.00 37.72  ? 25  ILE   C CD1 1 
ATOM   1664 N N   . ASP   C 1 27 ? 16.829  -28.330 29.412  1.00 51.54  ? 26  ASP   C N   1 
ATOM   1665 C CA  . ASP   C 1 27 ? 15.580  -28.606 30.120  1.00 56.15  ? 26  ASP   C CA  1 
ATOM   1666 C C   . ASP   C 1 27 ? 15.664  -28.173 31.594  1.00 63.47  ? 26  ASP   C C   1 
ATOM   1667 O O   . ASP   C 1 27 ? 16.737  -28.402 32.207  1.00 70.70  ? 26  ASP   C O   1 
ATOM   1668 C CB  . ASP   C 1 27 ? 15.209  -30.076 30.034  1.00 57.83  ? 26  ASP   C CB  1 
ATOM   1669 C CG  . ASP   C 1 27 ? 13.754  -30.338 29.674  1.00 66.66  ? 26  ASP   C CG  1 
ATOM   1670 O OD1 . ASP   C 1 27 ? 13.298  -29.741 28.686  1.00 74.12  ? 26  ASP   C OD1 1 
ATOM   1671 O OD2 . ASP   C 1 27 ? 13.095  -31.144 30.362  1.00 63.79  ? 26  ASP   C OD2 1 
ATOM   1672 N N   . PRO   C 1 36 ? 21.202  -37.394 36.083  1.00 56.17  ? 35  PRO   C N   1 
ATOM   1673 C CA  . PRO   C 1 36 ? 21.959  -36.927 34.919  1.00 63.46  ? 35  PRO   C CA  1 
ATOM   1674 C C   . PRO   C 1 36 ? 23.377  -37.510 34.903  1.00 75.31  ? 35  PRO   C C   1 
ATOM   1675 O O   . PRO   C 1 36 ? 24.135  -37.330 35.860  1.00 61.58  ? 35  PRO   C O   1 
ATOM   1676 C CB  . PRO   C 1 36 ? 21.948  -35.390 35.041  1.00 64.57  ? 35  PRO   C CB  1 
ATOM   1677 C CG  . PRO   C 1 36 ? 21.796  -35.144 36.540  1.00 69.25  ? 35  PRO   C CG  1 
ATOM   1678 C CD  . PRO   C 1 36 ? 21.126  -36.388 37.147  1.00 64.06  ? 35  PRO   C CD  1 
ATOM   1679 N N   . PRO   C 1 37 ? 23.800  -38.238 33.836  1.00 78.28  ? 36  PRO   C N   1 
ATOM   1680 C CA  . PRO   C 1 37 ? 25.080  -38.941 33.867  1.00 75.54  ? 36  PRO   C CA  1 
ATOM   1681 C C   . PRO   C 1 37 ? 26.167  -37.878 34.005  1.00 71.88  ? 36  PRO   C C   1 
ATOM   1682 O O   . PRO   C 1 37 ? 25.986  -36.739 33.577  1.00 67.16  ? 36  PRO   C O   1 
ATOM   1683 C CB  . PRO   C 1 37 ? 25.171  -39.756 32.551  1.00 74.81  ? 36  PRO   C CB  1 
ATOM   1684 C CG  . PRO   C 1 37 ? 23.781  -39.645 31.942  1.00 75.61  ? 36  PRO   C CG  1 
ATOM   1685 C CD  . PRO   C 1 37 ? 23.116  -38.403 32.542  1.00 75.71  ? 36  PRO   C CD  1 
ATOM   1686 N N   . PRO   C 1 38 ? 27.294  -38.222 34.667  1.00 58.20  ? 37  PRO   C N   1 
ATOM   1687 C CA  . PRO   C 1 38 ? 28.434  -37.315 34.825  1.00 62.63  ? 37  PRO   C CA  1 
ATOM   1688 C C   . PRO   C 1 38 ? 28.672  -36.425 33.613  1.00 52.56  ? 37  PRO   C C   1 
ATOM   1689 O O   . PRO   C 1 38 ? 28.891  -36.929 32.514  1.00 47.38  ? 37  PRO   C O   1 
ATOM   1690 C CB  . PRO   C 1 38 ? 29.601  -38.305 35.033  1.00 63.93  ? 37  PRO   C CB  1 
ATOM   1691 C CG  . PRO   C 1 38 ? 28.967  -39.498 35.717  1.00 56.20  ? 37  PRO   C CG  1 
ATOM   1692 C CD  . PRO   C 1 38 ? 27.503  -39.524 35.324  1.00 57.85  ? 37  PRO   C CD  1 
ATOM   1693 N N   . ASN   C 1 39 ? 28.569  -35.113 33.846  1.00 52.06  ? 38  ASN   C N   1 
ATOM   1694 C CA  . ASN   C 1 39 ? 28.861  -34.055 32.887  1.00 55.24  ? 38  ASN   C CA  1 
ATOM   1695 C C   . ASN   C 1 39 ? 27.871  -34.043 31.714  1.00 48.08  ? 38  ASN   C C   1 
ATOM   1696 O O   . ASN   C 1 39 ? 28.237  -33.696 30.593  1.00 51.23  ? 38  ASN   C O   1 
ATOM   1697 C CB  . ASN   C 1 39 ? 30.321  -34.058 32.439  1.00 56.52  ? 38  ASN   C CB  1 
ATOM   1698 C CG  . ASN   C 1 39 ? 30.760  -32.682 31.978  1.00 70.10  ? 38  ASN   C CG  1 
ATOM   1699 O OD1 . ASN   C 1 39 ? 30.121  -31.671 32.312  1.00 56.02  ? 38  ASN   C OD1 1 
ATOM   1700 N ND2 . ASN   C 1 39 ? 31.860  -32.614 31.236  1.00 65.64  ? 38  ASN   C ND2 1 
ATOM   1701 N N   . LYS   C 1 40 ? 26.616  -34.417 31.963  1.00 44.75  ? 39  LYS   C N   1 
ATOM   1702 C CA  . LYS   C 1 40 ? 25.655  -34.358 30.871  1.00 44.31  ? 39  LYS   C CA  1 
ATOM   1703 C C   . LYS   C 1 40 ? 24.599  -33.298 31.172  1.00 44.06  ? 39  LYS   C C   1 
ATOM   1704 O O   . LYS   C 1 40 ? 24.259  -33.048 32.322  1.00 46.27  ? 39  LYS   C O   1 
ATOM   1705 C CB  . LYS   C 1 40 ? 25.050  -35.742 30.594  1.00 47.10  ? 39  LYS   C CB  1 
ATOM   1706 C CG  . LYS   C 1 40 ? 26.050  -36.863 30.291  1.00 51.18  ? 39  LYS   C CG  1 
ATOM   1707 C CD  . LYS   C 1 40 ? 26.737  -36.861 28.931  1.00 59.88  ? 39  LYS   C CD  1 
ATOM   1708 C CE  . LYS   C 1 40 ? 27.730  -37.984 28.832  1.00 62.47  ? 39  LYS   C CE  1 
ATOM   1709 N NZ  . LYS   C 1 40 ? 28.190  -38.238 27.462  1.00 61.82  ? 39  LYS   C NZ  1 
ATOM   1710 N N   . TYR   C 1 41 ? 24.059  -32.682 30.119  1.00 42.66  ? 40  TYR   C N   1 
ATOM   1711 C CA  . TYR   C 1 41 ? 22.907  -31.799 30.264  1.00 39.71  ? 40  TYR   C CA  1 
ATOM   1712 C C   . TYR   C 1 41 ? 21.636  -32.521 29.802  1.00 44.41  ? 40  TYR   C C   1 
ATOM   1713 O O   . TYR   C 1 41 ? 21.668  -33.376 28.904  1.00 40.87  ? 40  TYR   C O   1 
ATOM   1714 C CB  . TYR   C 1 41 ? 23.134  -30.573 29.368  1.00 39.81  ? 40  TYR   C CB  1 
ATOM   1715 C CG  . TYR   C 1 41 ? 24.177  -29.545 29.805  1.00 44.13  ? 40  TYR   C CG  1 
ATOM   1716 C CD1 . TYR   C 1 41 ? 25.521  -29.663 29.459  1.00 44.85  ? 40  TYR   C CD1 1 
ATOM   1717 C CD2 . TYR   C 1 41 ? 23.801  -28.449 30.572  1.00 51.39  ? 40  TYR   C CD2 1 
ATOM   1718 C CE1 . TYR   C 1 41 ? 26.453  -28.712 29.853  1.00 56.95  ? 40  TYR   C CE1 1 
ATOM   1719 C CE2 . TYR   C 1 41 ? 24.712  -27.478 30.944  1.00 54.93  ? 40  TYR   C CE2 1 
ATOM   1720 C CZ  . TYR   C 1 41 ? 26.040  -27.609 30.584  1.00 56.71  ? 40  TYR   C CZ  1 
ATOM   1721 O OH  . TYR   C 1 41 ? 26.907  -26.622 30.961  1.00 63.43  ? 40  TYR   C OH  1 
ATOM   1722 N N   . PRO   C 1 42 ? 20.466  -32.173 30.387  1.00 47.15  ? 41  PRO   C N   1 
ATOM   1723 C CA  . PRO   C 1 42 ? 19.182  -32.647 29.870  1.00 41.08  ? 41  PRO   C CA  1 
ATOM   1724 C C   . PRO   C 1 42 ? 18.749  -31.747 28.709  1.00 37.15  ? 41  PRO   C C   1 
ATOM   1725 O O   . PRO   C 1 42 ? 18.706  -30.537 28.856  1.00 39.89  ? 41  PRO   C O   1 
ATOM   1726 C CB  . PRO   C 1 42 ? 18.349  -32.462 31.158  1.00 40.76  ? 41  PRO   C CB  1 
ATOM   1727 C CG  . PRO   C 1 42 ? 18.845  -31.136 31.708  1.00 42.39  ? 41  PRO   C CG  1 
ATOM   1728 C CD  . PRO   C 1 42 ? 20.333  -31.333 31.600  1.00 40.52  ? 41  PRO   C CD  1 
ATOM   1729 N N   . ILE   C 1 43 ? 18.501  -32.340 27.540  1.00 36.56  ? 42  ILE   C N   1 
ATOM   1730 C CA  . ILE   C 1 43 ? 18.206  -31.607 26.316  1.00 34.84  ? 42  ILE   C CA  1 
ATOM   1731 C C   . ILE   C 1 43 ? 16.755  -31.880 25.896  1.00 37.29  ? 42  ILE   C C   1 
ATOM   1732 O O   . ILE   C 1 43 ? 16.285  -33.038 25.927  1.00 39.82  ? 42  ILE   C O   1 
ATOM   1733 C CB  . ILE   C 1 43 ? 19.259  -31.972 25.245  1.00 34.63  ? 42  ILE   C CB  1 
ATOM   1734 C CG1 . ILE   C 1 43 ? 20.690  -31.556 25.693  1.00 37.17  ? 42  ILE   C CG1 1 
ATOM   1735 C CG2 . ILE   C 1 43 ? 18.906  -31.424 23.856  1.00 28.87  ? 42  ILE   C CG2 1 
ATOM   1736 C CD1 . ILE   C 1 43 ? 20.830  -30.091 26.053  1.00 36.80  ? 42  ILE   C CD1 1 
ATOM   1737 N N   . PHE   C 1 44 ? 16.032  -30.808 25.488  1.00 33.77  ? 43  PHE   C N   1 
ATOM   1738 C CA  . PHE   C 1 44 ? 14.718  -30.954 24.858  1.00 34.63  ? 43  PHE   C CA  1 
ATOM   1739 C C   . PHE   C 1 44 ? 14.795  -30.539 23.391  1.00 29.99  ? 43  PHE   C C   1 
ATOM   1740 O O   . PHE   C 1 44 ? 15.106  -29.388 23.106  1.00 36.10  ? 43  PHE   C O   1 
ATOM   1741 C CB  . PHE   C 1 44 ? 13.663  -30.096 25.578  1.00 40.02  ? 43  PHE   C CB  1 
ATOM   1742 C CG  . PHE   C 1 44 ? 12.269  -29.986 24.961  1.00 48.35  ? 43  PHE   C CG  1 
ATOM   1743 C CD1 . PHE   C 1 44 ? 11.292  -30.955 25.211  1.00 49.67  ? 43  PHE   C CD1 1 
ATOM   1744 C CD2 . PHE   C 1 44 ? 11.915  -28.886 24.170  1.00 45.45  ? 43  PHE   C CD2 1 
ATOM   1745 C CE1 . PHE   C 1 44 ? 10.010  -30.843 24.672  1.00 53.42  ? 43  PHE   C CE1 1 
ATOM   1746 C CE2 . PHE   C 1 44 ? 10.639  -28.787 23.614  1.00 48.72  ? 43  PHE   C CE2 1 
ATOM   1747 C CZ  . PHE   C 1 44 ? 9.686   -29.764 23.873  1.00 53.83  ? 43  PHE   C CZ  1 
ATOM   1748 N N   . PHE   C 1 45 ? 14.427  -31.446 22.491  1.00 31.33  ? 44  PHE   C N   1 
ATOM   1749 C CA  . PHE   C 1 45 ? 14.521  -31.216 21.060  1.00 35.02  ? 44  PHE   C CA  1 
ATOM   1750 C C   . PHE   C 1 45 ? 13.225  -30.594 20.547  1.00 39.96  ? 44  PHE   C C   1 
ATOM   1751 O O   . PHE   C 1 45 ? 12.147  -31.178 20.702  1.00 38.37  ? 44  PHE   C O   1 
ATOM   1752 C CB  . PHE   C 1 45 ? 14.704  -32.586 20.400  1.00 35.69  ? 44  PHE   C CB  1 
ATOM   1753 C CG  . PHE   C 1 45 ? 16.092  -33.143 20.696  1.00 40.05  ? 44  PHE   C CG  1 
ATOM   1754 C CD1 . PHE   C 1 45 ? 17.180  -32.815 19.900  1.00 40.35  ? 44  PHE   C CD1 1 
ATOM   1755 C CD2 . PHE   C 1 45 ? 16.298  -33.966 21.798  1.00 36.41  ? 44  PHE   C CD2 1 
ATOM   1756 C CE1 . PHE   C 1 45 ? 18.442  -33.333 20.178  1.00 38.31  ? 44  PHE   C CE1 1 
ATOM   1757 C CE2 . PHE   C 1 45 ? 17.559  -34.469 22.074  1.00 37.46  ? 44  PHE   C CE2 1 
ATOM   1758 C CZ  . PHE   C 1 45 ? 18.619  -34.172 21.266  1.00 33.48  ? 44  PHE   C CZ  1 
ATOM   1759 N N   . PHE   C 1 46 ? 13.356  -29.434 19.881  1.00 35.34  ? 45  PHE   C N   1 
ATOM   1760 C CA  . PHE   C 1 46 ? 12.203  -28.836 19.221  1.00 35.25  ? 45  PHE   C CA  1 
ATOM   1761 C C   . PHE   C 1 46 ? 11.674  -29.756 18.113  1.00 36.51  ? 45  PHE   C C   1 
ATOM   1762 O O   . PHE   C 1 46 ? 12.428  -30.479 17.446  1.00 32.45  ? 45  PHE   C O   1 
ATOM   1763 C CB  . PHE   C 1 46 ? 12.503  -27.372 18.819  1.00 35.93  ? 45  PHE   C CB  1 
ATOM   1764 C CG  . PHE   C 1 46 ? 12.784  -26.381 19.940  1.00 37.35  ? 45  PHE   C CG  1 
ATOM   1765 C CD1 . PHE   C 1 46 ? 11.753  -25.920 20.758  1.00 37.73  ? 45  PHE   C CD1 1 
ATOM   1766 C CD2 . PHE   C 1 46 ? 14.080  -25.897 20.185  1.00 36.11  ? 45  PHE   C CD2 1 
ATOM   1767 C CE1 . PHE   C 1 46 ? 11.996  -25.012 21.777  1.00 37.05  ? 45  PHE   C CE1 1 
ATOM   1768 C CE2 . PHE   C 1 46 ? 14.319  -24.968 21.203  1.00 34.70  ? 45  PHE   C CE2 1 
ATOM   1769 C CZ  . PHE   C 1 46 ? 13.274  -24.518 21.996  1.00 35.47  ? 45  PHE   C CZ  1 
ATOM   1770 N N   . GLY   C 1 47 ? 10.360  -29.663 17.859  1.00 34.80  ? 46  GLY   C N   1 
ATOM   1771 C CA  . GLY   C 1 47 ? 9.743   -30.331 16.722  1.00 41.08  ? 46  GLY   C CA  1 
ATOM   1772 C C   . GLY   C 1 47 ? 9.282   -31.740 17.094  1.00 47.43  ? 46  GLY   C C   1 
ATOM   1773 O O   . GLY   C 1 47 ? 8.078   -32.010 17.086  1.00 41.78  ? 46  GLY   C O   1 
ATOM   1774 N N   . THR   C 1 48 ? 10.251  -32.603 17.460  1.00 47.05  ? 47  THR   C N   1 
ATOM   1775 C CA  . THR   C 1 48 ? 9.968   -33.956 17.933  1.00 43.41  ? 47  THR   C CA  1 
ATOM   1776 C C   . THR   C 1 48 ? 9.437   -33.908 19.364  1.00 36.10  ? 47  THR   C C   1 
ATOM   1777 O O   . THR   C 1 48 ? 8.643   -34.756 19.749  1.00 44.68  ? 47  THR   C O   1 
ATOM   1778 C CB  . THR   C 1 48 ? 11.193  -34.873 17.822  1.00 35.90  ? 47  THR   C CB  1 
ATOM   1779 O OG1 . THR   C 1 48 ? 12.156  -34.334 18.736  1.00 32.44  ? 47  THR   C OG1 1 
ATOM   1780 C CG2 . THR   C 1 48 ? 11.663  -35.018 16.388  1.00 37.70  ? 47  THR   C CG2 1 
ATOM   1781 N N   . HIS   C 1 49 ? 9.924   -32.962 20.173  1.00 42.79  ? 48  HIS   C N   1 
ATOM   1782 C CA  . HIS   C 1 49 ? 9.569   -32.826 21.585  1.00 41.95  ? 48  HIS   C CA  1 
ATOM   1783 C C   . HIS   C 1 49 ? 10.171  -33.916 22.479  1.00 41.94  ? 48  HIS   C C   1 
ATOM   1784 O O   . HIS   C 1 49 ? 9.681   -34.135 23.591  1.00 42.01  ? 48  HIS   C O   1 
ATOM   1785 C CB  . HIS   C 1 49 ? 8.050   -32.683 21.770  1.00 46.52  ? 48  HIS   C CB  1 
ATOM   1786 C CG  . HIS   C 1 49 ? 7.515   -31.580 20.921  1.00 52.59  ? 48  HIS   C CG  1 
ATOM   1787 N ND1 . HIS   C 1 49 ? 6.423   -31.748 20.094  1.00 53.51  ? 48  HIS   C ND1 1 
ATOM   1788 C CD2 . HIS   C 1 49 ? 7.974   -30.333 20.703  1.00 50.19  ? 48  HIS   C CD2 1 
ATOM   1789 C CE1 . HIS   C 1 49 ? 6.214   -30.614 19.425  1.00 62.39  ? 48  HIS   C CE1 1 
ATOM   1790 N NE2 . HIS   C 1 49 ? 7.135   -29.736 19.791  1.00 56.04  ? 48  HIS   C NE2 1 
ATOM   1791 N N   . GLU   C 1 50 ? 11.252  -34.559 22.023  1.00 45.19  ? 49  GLU   C N   1 
ATOM   1792 C CA  . GLU   C 1 50 ? 11.930  -35.613 22.779  1.00 46.82  ? 49  GLU   C CA  1 
ATOM   1793 C C   . GLU   C 1 50 ? 13.019  -35.051 23.700  1.00 45.91  ? 49  GLU   C C   1 
ATOM   1794 O O   . GLU   C 1 50 ? 13.341  -33.863 23.660  1.00 38.81  ? 49  GLU   C O   1 
ATOM   1795 C CB  . GLU   C 1 50 ? 12.465  -36.662 21.800  1.00 46.41  ? 49  GLU   C CB  1 
ATOM   1796 C CG  . GLU   C 1 50 ? 11.342  -37.431 21.108  1.00 51.69  ? 49  GLU   C CG  1 
ATOM   1797 C CD  . GLU   C 1 50 ? 11.768  -38.302 19.946  1.00 51.92  ? 49  GLU   C CD  1 
ATOM   1798 O OE1 . GLU   C 1 50 ? 12.949  -38.384 19.554  1.00 50.79  ? 49  GLU   C OE1 1 
ATOM   1799 O OE2 . GLU   C 1 50 ? 10.837  -38.898 19.392  1.00 64.32  ? 49  GLU   C OE2 1 
ATOM   1800 N N   . THR   C 1 51 ? 13.559  -35.919 24.574  1.00 45.30  ? 50  THR   C N   1 
ATOM   1801 C CA  . THR   C 1 51 ? 14.566  -35.543 25.569  1.00 45.60  ? 50  THR   C CA  1 
ATOM   1802 C C   . THR   C 1 51 ? 15.741  -36.531 25.535  1.00 42.95  ? 50  THR   C C   1 
ATOM   1803 O O   . THR   C 1 51 ? 15.556  -37.678 25.148  1.00 45.34  ? 50  THR   C O   1 
ATOM   1804 C CB  . THR   C 1 51 ? 13.973  -35.423 26.973  1.00 51.06  ? 50  THR   C CB  1 
ATOM   1805 O OG1 . THR   C 1 51 ? 13.524  -36.743 27.274  1.00 51.19  ? 50  THR   C OG1 1 
ATOM   1806 C CG2 . THR   C 1 51 ? 12.881  -34.368 27.080  1.00 41.74  ? 50  THR   C CG2 1 
ATOM   1807 N N   . ALA   C 1 52 ? 16.939  -36.038 25.888  1.00 41.42  ? 51  ALA   C N   1 
ATOM   1808 C CA  . ALA   C 1 52 ? 18.196  -36.772 25.837  1.00 42.52  ? 51  ALA   C CA  1 
ATOM   1809 C C   . ALA   C 1 52 ? 19.198  -36.134 26.793  1.00 40.69  ? 51  ALA   C C   1 
ATOM   1810 O O   . ALA   C 1 52 ? 18.995  -35.010 27.248  1.00 38.24  ? 51  ALA   C O   1 
ATOM   1811 C CB  . ALA   C 1 52 ? 18.736  -36.766 24.416  1.00 35.64  ? 51  ALA   C CB  1 
ATOM   1812 N N   . PHE   C 1 53 ? 20.260  -36.883 27.148  1.00 38.31  ? 52  PHE   C N   1 
ATOM   1813 C CA  . PHE   C 1 53 ? 21.387  -36.361 27.898  1.00 37.36  ? 52  PHE   C CA  1 
ATOM   1814 C C   . PHE   C 1 53 ? 22.554  -36.188 26.940  1.00 39.74  ? 52  PHE   C C   1 
ATOM   1815 O O   . PHE   C 1 53 ? 22.930  -37.140 26.266  1.00 40.30  ? 52  PHE   C O   1 
ATOM   1816 C CB  . PHE   C 1 53 ? 21.753  -37.426 28.942  1.00 40.18  ? 52  PHE   C CB  1 
ATOM   1817 C CG  . PHE   C 1 53 ? 20.866  -37.355 30.175  1.00 44.94  ? 52  PHE   C CG  1 
ATOM   1818 C CD1 . PHE   C 1 53 ? 20.655  -36.140 30.835  1.00 48.68  ? 52  PHE   C CD1 1 
ATOM   1819 C CD2 . PHE   C 1 53 ? 20.194  -38.482 30.646  1.00 50.96  ? 52  PHE   C CD2 1 
ATOM   1820 C CE1 . PHE   C 1 53 ? 19.820  -36.060 31.949  1.00 50.35  ? 52  PHE   C CE1 1 
ATOM   1821 C CE2 . PHE   C 1 53 ? 19.381  -38.404 31.778  1.00 52.63  ? 52  PHE   C CE2 1 
ATOM   1822 C CZ  . PHE   C 1 53 ? 19.194  -37.196 32.427  1.00 47.74  ? 52  PHE   C CZ  1 
ATOM   1823 N N   . LEU   C 1 54 ? 23.133  -34.976 26.882  1.00 37.09  ? 53  LEU   C N   1 
ATOM   1824 C CA  . LEU   C 1 54 ? 24.239  -34.684 25.979  1.00 38.70  ? 53  LEU   C CA  1 
ATOM   1825 C C   . LEU   C 1 54 ? 25.366  -33.970 26.733  1.00 37.46  ? 53  LEU   C C   1 
ATOM   1826 O O   . LEU   C 1 54 ? 25.107  -33.191 27.642  1.00 34.27  ? 53  LEU   C O   1 
ATOM   1827 C CB  . LEU   C 1 54 ? 23.715  -33.819 24.823  1.00 35.41  ? 53  LEU   C CB  1 
ATOM   1828 C CG  . LEU   C 1 54 ? 23.008  -34.542 23.673  1.00 39.60  ? 53  LEU   C CG  1 
ATOM   1829 C CD1 . LEU   C 1 54 ? 22.663  -33.610 22.518  1.00 34.01  ? 53  LEU   C CD1 1 
ATOM   1830 C CD2 . LEU   C 1 54 ? 23.802  -35.712 23.124  1.00 44.24  ? 53  LEU   C CD2 1 
ATOM   1831 N N   . GLY   C 1 55 ? 26.613  -34.240 26.332  1.00 42.53  ? 54  GLY   C N   1 
ATOM   1832 C CA  . GLY   C 1 55 ? 27.789  -33.554 26.853  1.00 38.70  ? 54  GLY   C CA  1 
ATOM   1833 C C   . GLY   C 1 55 ? 27.948  -32.206 26.148  1.00 46.80  ? 54  GLY   C C   1 
ATOM   1834 O O   . GLY   C 1 55 ? 27.447  -32.036 25.023  1.00 40.07  ? 54  GLY   C O   1 
ATOM   1835 N N   . PRO   C 1 56 ? 28.623  -31.202 26.770  1.00 40.85  ? 55  PRO   C N   1 
ATOM   1836 C CA  . PRO   C 1 56 ? 28.748  -29.883 26.144  1.00 41.11  ? 55  PRO   C CA  1 
ATOM   1837 C C   . PRO   C 1 56 ? 29.464  -29.856 24.793  1.00 41.12  ? 55  PRO   C C   1 
ATOM   1838 O O   . PRO   C 1 56 ? 29.348  -28.887 24.055  1.00 44.94  ? 55  PRO   C O   1 
ATOM   1839 C CB  . PRO   C 1 56 ? 29.473  -29.059 27.250  1.00 43.56  ? 55  PRO   C CB  1 
ATOM   1840 C CG  . PRO   C 1 56 ? 30.233  -30.115 28.048  1.00 42.63  ? 55  PRO   C CG  1 
ATOM   1841 C CD  . PRO   C 1 56 ? 29.230  -31.250 28.125  1.00 38.32  ? 55  PRO   C CD  1 
ATOM   1842 N N   . LYS   C 1 57 ? 30.208  -30.919 24.470  1.00 34.70  ? 56  LYS   C N   1 
ATOM   1843 C CA  . LYS   C 1 57 ? 30.910  -30.991 23.198  1.00 40.87  ? 56  LYS   C CA  1 
ATOM   1844 C C   . LYS   C 1 57 ? 29.887  -31.141 22.077  1.00 38.92  ? 56  LYS   C C   1 
ATOM   1845 O O   . LYS   C 1 57 ? 30.186  -30.833 20.927  1.00 39.03  ? 56  LYS   C O   1 
ATOM   1846 C CB  . LYS   C 1 57 ? 31.916  -32.144 23.069  1.00 40.36  ? 56  LYS   C CB  1 
ATOM   1847 N N   . ASP   C 1 58 ? 28.696  -31.621 22.443  1.00 41.72  ? 57  ASP   C N   1 
ATOM   1848 C CA  . ASP   C 1 58 ? 27.657  -31.875 21.460  1.00 41.52  ? 57  ASP   C CA  1 
ATOM   1849 C C   . ASP   C 1 58 ? 26.670  -30.714 21.382  1.00 39.57  ? 57  ASP   C C   1 
ATOM   1850 O O   . ASP   C 1 58 ? 25.609  -30.891 20.781  1.00 37.93  ? 57  ASP   C O   1 
ATOM   1851 C CB  . ASP   C 1 58 ? 26.947  -33.188 21.755  1.00 43.93  ? 57  ASP   C CB  1 
ATOM   1852 C CG  . ASP   C 1 58 ? 27.881  -34.384 21.845  1.00 50.78  ? 57  ASP   C CG  1 
ATOM   1853 O OD1 . ASP   C 1 58 ? 29.000  -34.274 21.313  1.00 54.38  ? 57  ASP   C OD1 1 
ATOM   1854 O OD2 . ASP   C 1 58 ? 27.482  -35.397 22.451  1.00 58.93  ? 57  ASP   C OD2 1 
ATOM   1855 N N   . LEU   C 1 59 ? 27.038  -29.538 21.931  1.00 39.05  ? 58  LEU   C N   1 
ATOM   1856 C CA  . LEU   C 1 59 ? 26.092  -28.452 22.137  1.00 40.33  ? 58  LEU   C CA  1 
ATOM   1857 C C   . LEU   C 1 59 ? 26.660  -27.134 21.611  1.00 47.12  ? 58  LEU   C C   1 
ATOM   1858 O O   . LEU   C 1 59 ? 27.827  -26.807 21.876  1.00 40.35  ? 58  LEU   C O   1 
ATOM   1859 C CB  . LEU   C 1 59 ? 25.745  -28.345 23.624  1.00 39.40  ? 58  LEU   C CB  1 
ATOM   1860 C CG  . LEU   C 1 59 ? 25.009  -29.535 24.255  1.00 36.89  ? 58  LEU   C CG  1 
ATOM   1861 C CD1 . LEU   C 1 59 ? 24.823  -29.217 25.721  1.00 38.91  ? 58  LEU   C CD1 1 
ATOM   1862 C CD2 . LEU   C 1 59 ? 23.667  -29.990 23.642  1.00 32.73  ? 58  LEU   C CD2 1 
ATOM   1863 N N   . PHE   C 1 60 ? 25.807  -26.365 20.905  1.00 39.86  ? 59  PHE   C N   1 
ATOM   1864 C CA  . PHE   C 1 60 ? 26.223  -25.135 20.233  1.00 43.02  ? 59  PHE   C CA  1 
ATOM   1865 C C   . PHE   C 1 60 ? 25.228  -24.007 20.516  1.00 44.12  ? 59  PHE   C C   1 
ATOM   1866 O O   . PHE   C 1 60 ? 24.038  -24.157 20.262  1.00 40.40  ? 59  PHE   C O   1 
ATOM   1867 C CB  . PHE   C 1 60 ? 26.454  -25.341 18.730  1.00 40.02  ? 59  PHE   C CB  1 
ATOM   1868 C CG  . PHE   C 1 60 ? 27.384  -26.515 18.428  1.00 43.00  ? 59  PHE   C CG  1 
ATOM   1869 C CD1 . PHE   C 1 60 ? 26.904  -27.826 18.426  1.00 34.64  ? 59  PHE   C CD1 1 
ATOM   1870 C CD2 . PHE   C 1 60 ? 28.736  -26.308 18.133  1.00 45.78  ? 59  PHE   C CD2 1 
ATOM   1871 C CE1 . PHE   C 1 60 ? 27.749  -28.904 18.188  1.00 34.42  ? 59  PHE   C CE1 1 
ATOM   1872 C CE2 . PHE   C 1 60 ? 29.583  -27.389 17.867  1.00 38.34  ? 59  PHE   C CE2 1 
ATOM   1873 C CZ  . PHE   C 1 60 ? 29.077  -28.677 17.880  1.00 40.15  ? 59  PHE   C CZ  1 
ATOM   1874 N N   . PRO   C 1 61 ? 25.658  -22.838 21.053  1.00 46.66  ? 60  PRO   C N   1 
ATOM   1875 C CA  . PRO   C 1 61 ? 24.724  -21.738 21.335  1.00 41.80  ? 60  PRO   C CA  1 
ATOM   1876 C C   . PRO   C 1 61 ? 23.997  -21.317 20.061  1.00 37.45  ? 60  PRO   C C   1 
ATOM   1877 O O   . PRO   C 1 61 ? 24.631  -21.174 19.020  1.00 42.66  ? 60  PRO   C O   1 
ATOM   1878 C CB  . PRO   C 1 61 ? 25.680  -20.643 21.864  1.00 46.62  ? 60  PRO   C CB  1 
ATOM   1879 C CG  . PRO   C 1 61 ? 26.829  -21.429 22.439  1.00 46.19  ? 60  PRO   C CG  1 
ATOM   1880 C CD  . PRO   C 1 61 ? 27.045  -22.535 21.438  1.00 46.65  ? 60  PRO   C CD  1 
ATOM   1881 N N   . TYR   C 1 62 ? 22.670  -21.143 20.164  1.00 40.01  ? 61  TYR   C N   1 
ATOM   1882 C CA  . TYR   C 1 62 ? 21.781  -20.899 19.039  1.00 40.97  ? 61  TYR   C CA  1 
ATOM   1883 C C   . TYR   C 1 62 ? 22.196  -19.651 18.265  1.00 48.87  ? 61  TYR   C C   1 
ATOM   1884 O O   . TYR   C 1 62 ? 22.366  -19.718 17.051  1.00 40.24  ? 61  TYR   C O   1 
ATOM   1885 C CB  . TYR   C 1 62 ? 20.320  -20.778 19.491  1.00 47.96  ? 61  TYR   C CB  1 
ATOM   1886 C CG  . TYR   C 1 62 ? 19.348  -20.403 18.380  1.00 43.00  ? 61  TYR   C CG  1 
ATOM   1887 C CD1 . TYR   C 1 62 ? 18.998  -21.345 17.407  1.00 47.39  ? 61  TYR   C CD1 1 
ATOM   1888 C CD2 . TYR   C 1 62 ? 18.782  -19.133 18.300  1.00 42.70  ? 61  TYR   C CD2 1 
ATOM   1889 C CE1 . TYR   C 1 62 ? 18.128  -21.035 16.375  1.00 42.11  ? 61  TYR   C CE1 1 
ATOM   1890 C CE2 . TYR   C 1 62 ? 17.887  -18.821 17.282  1.00 47.06  ? 61  TYR   C CE2 1 
ATOM   1891 C CZ  . TYR   C 1 62 ? 17.566  -19.769 16.317  1.00 39.35  ? 61  TYR   C CZ  1 
ATOM   1892 O OH  . TYR   C 1 62 ? 16.704  -19.513 15.292  1.00 43.40  ? 61  TYR   C OH  1 
ATOM   1893 N N   . ASP   C 1 63 ? 22.355  -18.516 18.965  1.00 54.55  ? 62  ASP   C N   1 
ATOM   1894 C CA  . ASP   C 1 63 ? 22.688  -17.258 18.300  1.00 52.50  ? 62  ASP   C CA  1 
ATOM   1895 C C   . ASP   C 1 63 ? 24.006  -17.379 17.545  1.00 46.05  ? 62  ASP   C C   1 
ATOM   1896 O O   . ASP   C 1 63 ? 24.095  -16.945 16.401  1.00 49.76  ? 62  ASP   C O   1 
ATOM   1897 C CB  . ASP   C 1 63 ? 22.704  -16.062 19.239  1.00 60.05  ? 62  ASP   C CB  1 
ATOM   1898 C CG  . ASP   C 1 63 ? 21.331  -15.514 19.596  1.00 75.18  ? 62  ASP   C CG  1 
ATOM   1899 O OD1 . ASP   C 1 63 ? 20.873  -15.776 20.732  1.00 75.14  ? 62  ASP   C OD1 1 
ATOM   1900 O OD2 . ASP   C 1 63 ? 20.738  -14.831 18.732  1.00 87.35  ? 62  ASP   C OD2 1 
ATOM   1901 N N   . LYS   C 1 64 ? 25.009  -17.998 18.178  1.00 48.84  ? 63  LYS   C N   1 
ATOM   1902 C CA  . LYS   C 1 64 ? 26.344  -18.149 17.598  1.00 39.89  ? 63  LYS   C CA  1 
ATOM   1903 C C   . LYS   C 1 64 ? 26.363  -19.127 16.416  1.00 38.52  ? 63  LYS   C C   1 
ATOM   1904 O O   . LYS   C 1 64 ? 27.194  -18.954 15.529  1.00 42.57  ? 63  LYS   C O   1 
ATOM   1905 C CB  . LYS   C 1 64 ? 27.399  -18.531 18.648  1.00 38.05  ? 63  LYS   C CB  1 
ATOM   1906 N N   . SER   C 1 65 ? 25.499  -20.174 16.385  1.00 37.68  ? 64  SER   C N   1 
ATOM   1907 C CA  . SER   C 1 65 ? 25.752  -21.240 15.411  1.00 37.25  ? 64  SER   C CA  1 
ATOM   1908 C C   . SER   C 1 65 ? 24.688  -21.376 14.311  1.00 40.70  ? 64  SER   C C   1 
ATOM   1909 O O   . SER   C 1 65 ? 24.854  -22.227 13.432  1.00 38.17  ? 64  SER   C O   1 
ATOM   1910 C CB  . SER   C 1 65 ? 26.025  -22.564 16.047  1.00 35.85  ? 64  SER   C CB  1 
ATOM   1911 O OG  . SER   C 1 65 ? 24.838  -23.018 16.669  1.00 38.97  ? 64  SER   C OG  1 
ATOM   1912 N N   . LYS   C 1 66 ? 23.618  -20.551 14.355  1.00 35.98  ? 65  LYS   C N   1 
ATOM   1913 C CA  . LYS   C 1 66 ? 22.423  -20.812 13.559  1.00 36.53  ? 65  LYS   C CA  1 
ATOM   1914 C C   . LYS   C 1 66 ? 22.652  -20.531 12.079  1.00 36.31  ? 65  LYS   C C   1 
ATOM   1915 O O   . LYS   C 1 66 ? 21.953  -21.107 11.248  1.00 34.41  ? 65  LYS   C O   1 
ATOM   1916 C CB  . LYS   C 1 66 ? 21.183  -20.028 14.015  1.00 40.47  ? 65  LYS   C CB  1 
ATOM   1917 C CG  . LYS   C 1 66 ? 21.321  -18.502 14.045  1.00 39.94  ? 65  LYS   C CG  1 
ATOM   1918 C CD  . LYS   C 1 66 ? 19.969  -17.799 13.992  1.00 52.03  ? 65  LYS   C CD  1 
ATOM   1919 C CE  . LYS   C 1 66 ? 20.076  -16.303 13.925  1.00 53.29  ? 65  LYS   C CE  1 
ATOM   1920 N NZ  . LYS   C 1 66 ? 20.151  -15.769 15.284  1.00 54.45  ? 65  LYS   C NZ  1 
ATOM   1921 N N   . ASP   C 1 67 ? 23.583  -19.613 11.770  1.00 36.55  ? 66  ASP   C N   1 
ATOM   1922 C CA  . ASP   C 1 67 ? 24.046  -19.372 10.407  1.00 42.53  ? 66  ASP   C CA  1 
ATOM   1923 C C   . ASP   C 1 67 ? 24.492  -20.680 9.761   1.00 41.74  ? 66  ASP   C C   1 
ATOM   1924 O O   . ASP   C 1 67 ? 24.159  -20.922 8.601   1.00 41.94  ? 66  ASP   C O   1 
ATOM   1925 C CB  . ASP   C 1 67 ? 25.102  -18.271 10.303  1.00 45.41  ? 66  ASP   C CB  1 
ATOM   1926 C CG  . ASP   C 1 67 ? 26.505  -18.609 10.809  1.00 55.17  ? 66  ASP   C CG  1 
ATOM   1927 O OD1 . ASP   C 1 67 ? 26.657  -18.930 12.014  1.00 51.31  ? 66  ASP   C OD1 1 
ATOM   1928 O OD2 . ASP   C 1 67 ? 27.454  -18.555 9.997   1.00 60.78  ? 66  ASP   C OD2 1 
ATOM   1929 N N   . LYS   C 1 68 ? 25.231  -21.515 10.515  1.00 37.23  ? 67  LYS   C N   1 
ATOM   1930 C CA  . LYS   C 1 68 ? 25.686  -22.814 10.040  1.00 38.02  ? 67  LYS   C CA  1 
ATOM   1931 C C   . LYS   C 1 68 ? 24.587  -23.894 10.095  1.00 39.33  ? 67  LYS   C C   1 
ATOM   1932 O O   . LYS   C 1 68 ? 24.425  -24.685 9.157   1.00 39.40  ? 67  LYS   C O   1 
ATOM   1933 C CB  . LYS   C 1 68 ? 26.946  -23.165 10.847  1.00 34.43  ? 67  LYS   C CB  1 
ATOM   1934 C CG  . LYS   C 1 68 ? 27.776  -24.311 10.291  1.00 45.06  ? 67  LYS   C CG  1 
ATOM   1935 C CD  . LYS   C 1 68 ? 28.963  -24.578 11.215  1.00 57.42  ? 67  LYS   C CD  1 
ATOM   1936 C CE  . LYS   C 1 68 ? 29.627  -25.909 11.029  1.00 64.20  ? 67  LYS   C CE  1 
ATOM   1937 N NZ  . LYS   C 1 68 ? 29.853  -26.256 9.621   1.00 73.91  ? 67  LYS   C NZ  1 
ATOM   1938 N N   . TYR   C 1 69 ? 23.873  -24.003 11.224  1.00 33.54  ? 68  TYR   C N   1 
ATOM   1939 C CA  . TYR   C 1 69 ? 23.024  -25.184 11.438  1.00 31.85  ? 68  TYR   C CA  1 
ATOM   1940 C C   . TYR   C 1 69 ? 21.522  -24.891 11.218  1.00 34.74  ? 68  TYR   C C   1 
ATOM   1941 O O   . TYR   C 1 69 ? 20.735  -25.824 11.071  1.00 35.98  ? 68  TYR   C O   1 
ATOM   1942 C CB  . TYR   C 1 69 ? 23.225  -25.808 12.830  1.00 35.10  ? 68  TYR   C CB  1 
ATOM   1943 C CG  . TYR   C 1 69 ? 24.643  -26.274 13.147  1.00 35.19  ? 68  TYR   C CG  1 
ATOM   1944 C CD1 . TYR   C 1 69 ? 25.397  -26.982 12.213  1.00 37.08  ? 68  TYR   C CD1 1 
ATOM   1945 C CD2 . TYR   C 1 69 ? 25.250  -25.953 14.357  1.00 39.12  ? 68  TYR   C CD2 1 
ATOM   1946 C CE1 . TYR   C 1 69 ? 26.682  -27.419 12.502  1.00 33.96  ? 68  TYR   C CE1 1 
ATOM   1947 C CE2 . TYR   C 1 69 ? 26.563  -26.336 14.623  1.00 39.04  ? 68  TYR   C CE2 1 
ATOM   1948 C CZ  . TYR   C 1 69 ? 27.273  -27.092 13.708  1.00 38.87  ? 68  TYR   C CZ  1 
ATOM   1949 O OH  . TYR   C 1 69 ? 28.592  -27.461 13.975  1.00 37.32  ? 68  TYR   C OH  1 
ATOM   1950 N N   . GLY   C 1 70 ? 21.109  -23.612 11.266  1.00 33.09  ? 69  GLY   C N   1 
ATOM   1951 C CA  . GLY   C 1 70 ? 19.700  -23.240 11.165  1.00 38.59  ? 69  GLY   C CA  1 
ATOM   1952 C C   . GLY   C 1 70 ? 19.232  -23.256 9.707   1.00 39.49  ? 69  GLY   C C   1 
ATOM   1953 O O   . GLY   C 1 70 ? 19.131  -22.227 9.052   1.00 39.74  ? 69  GLY   C O   1 
ATOM   1954 N N   . LYS   C 1 71 ? 18.976  -24.444 9.174   1.00 41.57  ? 70  LYS   C N   1 
ATOM   1955 C CA  . LYS   C 1 71 ? 18.687  -24.521 7.751   1.00 42.29  ? 70  LYS   C CA  1 
ATOM   1956 C C   . LYS   C 1 71 ? 17.795  -25.733 7.529   1.00 39.06  ? 70  LYS   C C   1 
ATOM   1957 O O   . LYS   C 1 71 ? 17.929  -26.766 8.205   1.00 42.90  ? 70  LYS   C O   1 
ATOM   1958 C CB  . LYS   C 1 71 ? 19.968  -24.513 6.898   1.00 46.60  ? 70  LYS   C CB  1 
ATOM   1959 C CG  . LYS   C 1 71 ? 20.854  -25.743 7.114   1.00 57.79  ? 70  LYS   C CG  1 
ATOM   1960 C CD  . LYS   C 1 71 ? 22.249  -25.778 6.498   1.00 60.24  ? 70  LYS   C CD  1 
ATOM   1961 C CE  . LYS   C 1 71 ? 23.049  -26.917 7.063   1.00 59.48  ? 70  LYS   C CE  1 
ATOM   1962 N N   . PRO   C 1 72 ? 16.788  -25.638 6.632   1.00 37.45  ? 71  PRO   C N   1 
ATOM   1963 C CA  . PRO   C 1 72 ? 15.772  -26.685 6.570   1.00 36.82  ? 71  PRO   C CA  1 
ATOM   1964 C C   . PRO   C 1 72 ? 16.437  -28.006 6.218   1.00 35.94  ? 71  PRO   C C   1 
ATOM   1965 O O   . PRO   C 1 72 ? 17.473  -28.072 5.534   1.00 41.71  ? 71  PRO   C O   1 
ATOM   1966 C CB  . PRO   C 1 72 ? 14.844  -26.174 5.474   1.00 31.61  ? 71  PRO   C CB  1 
ATOM   1967 C CG  . PRO   C 1 72 ? 15.010  -24.696 5.609   1.00 33.32  ? 71  PRO   C CG  1 
ATOM   1968 C CD  . PRO   C 1 72 ? 16.535  -24.526 5.702   1.00 32.99  ? 71  PRO   C CD  1 
ATOM   1969 N N   . ASN   C 1 73 ? 15.807  -29.062 6.675   1.00 36.38  ? 72  ASN   C N   1 
ATOM   1970 C CA  . ASN   C 1 73 ? 16.073  -30.365 6.109   1.00 39.83  ? 72  ASN   C CA  1 
ATOM   1971 C C   . ASN   C 1 73 ? 14.845  -31.222 6.355   1.00 41.28  ? 72  ASN   C C   1 
ATOM   1972 O O   . ASN   C 1 73 ? 13.940  -30.829 7.081   1.00 41.72  ? 72  ASN   C O   1 
ATOM   1973 C CB  . ASN   C 1 73 ? 17.429  -30.934 6.521   1.00 43.89  ? 72  ASN   C CB  1 
ATOM   1974 C CG  . ASN   C 1 73 ? 17.412  -31.389 7.958   1.00 39.85  ? 72  ASN   C CG  1 
ATOM   1975 O OD1 . ASN   C 1 73 ? 16.595  -32.240 8.324   1.00 42.53  ? 72  ASN   C OD1 1 
ATOM   1976 N ND2 . ASN   C 1 73 ? 18.289  -30.818 8.768   1.00 45.25  ? 72  ASN   C ND2 1 
ATOM   1977 N N   . LYS   C 1 74 ? 14.835  -32.390 5.716   1.00 43.91  ? 73  LYS   C N   1 
ATOM   1978 C CA  . LYS   C 1 74 ? 13.606  -33.138 5.538   1.00 39.05  ? 73  LYS   C CA  1 
ATOM   1979 C C   . LYS   C 1 74 ? 13.451  -34.170 6.640   1.00 41.15  ? 73  LYS   C C   1 
ATOM   1980 O O   . LYS   C 1 74 ? 12.481  -34.927 6.615   1.00 40.20  ? 73  LYS   C O   1 
ATOM   1981 C CB  . LYS   C 1 74 ? 13.573  -33.725 4.120   1.00 45.24  ? 73  LYS   C CB  1 
ATOM   1982 N N   . ARG   C 1 75 ? 14.406  -34.204 7.601   1.00 45.60  ? 74  ARG   C N   1 
ATOM   1983 C CA  . ARG   C 1 75 ? 14.338  -35.188 8.676   1.00 40.10  ? 74  ARG   C CA  1 
ATOM   1984 C C   . ARG   C 1 75 ? 13.071  -34.914 9.485   1.00 43.44  ? 74  ARG   C C   1 
ATOM   1985 O O   . ARG   C 1 75 ? 12.722  -33.749 9.684   1.00 36.46  ? 74  ARG   C O   1 
ATOM   1986 C CB  . ARG   C 1 75 ? 15.545  -35.190 9.633   1.00 41.30  ? 74  ARG   C CB  1 
ATOM   1987 C CG  . ARG   C 1 75 ? 16.889  -35.485 8.973   1.00 53.07  ? 74  ARG   C CG  1 
ATOM   1988 C CD  . ARG   C 1 75 ? 17.030  -36.929 8.471   1.00 48.21  ? 74  ARG   C CD  1 
ATOM   1989 N NE  . ARG   C 1 75 ? 16.857  -37.835 9.614   1.00 45.83  ? 74  ARG   C NE  1 
ATOM   1990 C CZ  . ARG   C 1 75 ? 17.873  -38.413 10.263  1.00 52.66  ? 74  ARG   C CZ  1 
ATOM   1991 N NH1 . ARG   C 1 75 ? 17.641  -39.097 11.376  1.00 55.10  ? 74  ARG   C NH1 1 
ATOM   1992 N NH2 . ARG   C 1 75 ? 19.115  -38.270 9.817   1.00 41.88  ? 74  ARG   C NH2 1 
ATOM   1993 N N   . LYS   C 1 76 ? 12.417  -35.986 9.953   1.00 43.77  ? 75  LYS   C N   1 
ATOM   1994 C CA  . LYS   C 1 76 ? 11.123  -35.897 10.622  1.00 45.64  ? 75  LYS   C CA  1 
ATOM   1995 C C   . LYS   C 1 76 ? 11.155  -34.898 11.781  1.00 45.33  ? 75  LYS   C C   1 
ATOM   1996 O O   . LYS   C 1 76 ? 11.904  -35.049 12.754  1.00 46.15  ? 75  LYS   C O   1 
ATOM   1997 C CB  . LYS   C 1 76 ? 10.525  -37.261 11.011  1.00 51.60  ? 75  LYS   C CB  1 
ATOM   1998 C CG  . LYS   C 1 76 ? 9.101   -37.256 11.612  1.00 46.22  ? 75  LYS   C CG  1 
ATOM   1999 C CD  . LYS   C 1 76 ? 8.216   -38.419 11.165  1.00 47.32  ? 75  LYS   C CD  1 
ATOM   2000 N N   . GLY   C 1 77 ? 10.290  -33.887 11.687  1.00 40.91  ? 76  GLY   C N   1 
ATOM   2001 C CA  . GLY   C 1 77 ? 10.095  -32.964 12.798  1.00 37.76  ? 76  GLY   C CA  1 
ATOM   2002 C C   . GLY   C 1 77 ? 11.081  -31.788 12.777  1.00 32.73  ? 76  GLY   C C   1 
ATOM   2003 O O   . GLY   C 1 77 ? 10.929  -30.849 13.549  1.00 36.16  ? 76  GLY   C O   1 
ATOM   2004 N N   . PHE   C 1 78 ? 12.091  -31.839 11.893  1.00 34.32  ? 77  PHE   C N   1 
ATOM   2005 C CA  . PHE   C 1 78 ? 13.150  -30.840 11.882  1.00 32.06  ? 77  PHE   C CA  1 
ATOM   2006 C C   . PHE   C 1 78 ? 12.580  -29.444 11.605  1.00 31.07  ? 77  PHE   C C   1 
ATOM   2007 O O   . PHE   C 1 78 ? 12.841  -28.482 12.342  1.00 33.40  ? 77  PHE   C O   1 
ATOM   2008 C CB  . PHE   C 1 78 ? 14.265  -31.244 10.898  1.00 34.43  ? 77  PHE   C CB  1 
ATOM   2009 C CG  . PHE   C 1 78 ? 15.525  -30.417 11.099  1.00 31.15  ? 77  PHE   C CG  1 
ATOM   2010 C CD1 . PHE   C 1 78 ? 15.643  -29.150 10.523  1.00 34.66  ? 77  PHE   C CD1 1 
ATOM   2011 C CD2 . PHE   C 1 78 ? 16.532  -30.868 11.952  1.00 31.02  ? 77  PHE   C CD2 1 
ATOM   2012 C CE1 . PHE   C 1 78 ? 16.765  -28.368 10.753  1.00 35.94  ? 77  PHE   C CE1 1 
ATOM   2013 C CE2 . PHE   C 1 78 ? 17.686  -30.100 12.127  1.00 33.39  ? 77  PHE   C CE2 1 
ATOM   2014 C CZ  . PHE   C 1 78 ? 17.800  -28.857 11.544  1.00 36.84  ? 77  PHE   C CZ  1 
ATOM   2015 N N   . ASN   C 1 79 ? 11.864  -29.301 10.490  1.00 33.34  ? 78  ASN   C N   1 
ATOM   2016 C CA  . ASN   C 1 79 ? 11.467  -27.969 10.044  1.00 39.02  ? 78  ASN   C CA  1 
ATOM   2017 C C   . ASN   C 1 79 ? 10.532  -27.321 11.073  1.00 34.24  ? 78  ASN   C C   1 
ATOM   2018 O O   . ASN   C 1 79 ? 10.641  -26.120 11.405  1.00 30.48  ? 78  ASN   C O   1 
ATOM   2019 C CB  . ASN   C 1 79 ? 10.970  -27.994 8.597   1.00 44.36  ? 78  ASN   C CB  1 
ATOM   2020 C CG  . ASN   C 1 79 ? 12.086  -28.309 7.621   1.00 45.20  ? 78  ASN   C CG  1 
ATOM   2021 O OD1 . ASN   C 1 79 ? 13.260  -28.093 7.939   1.00 33.77  ? 78  ASN   C OD1 1 
ATOM   2022 N ND2 . ASN   C 1 79 ? 11.755  -28.785 6.427   1.00 40.35  ? 78  ASN   C ND2 1 
ATOM   2023 N N   . GLU   C 1 80 ? 9.661   -28.145 11.653  1.00 36.65  ? 79  GLU   C N   1 
ATOM   2024 C CA  . GLU   C 1 80 ? 8.769   -27.637 12.672  1.00 32.67  ? 79  GLU   C CA  1 
ATOM   2025 C C   . GLU   C 1 80 ? 9.577   -27.190 13.886  1.00 37.33  ? 79  GLU   C C   1 
ATOM   2026 O O   . GLU   C 1 80 ? 9.232   -26.186 14.493  1.00 37.35  ? 79  GLU   C O   1 
ATOM   2027 C CB  . GLU   C 1 80 ? 7.686   -28.654 13.047  1.00 35.17  ? 79  GLU   C CB  1 
ATOM   2028 C CG  . GLU   C 1 80 ? 6.747   -28.149 14.144  1.00 31.37  ? 79  GLU   C CG  1 
ATOM   2029 C CD  . GLU   C 1 80 ? 5.580   -29.090 14.422  1.00 48.28  ? 79  GLU   C CD  1 
ATOM   2030 O OE1 . GLU   C 1 80 ? 5.498   -30.233 13.899  1.00 49.80  ? 79  GLU   C OE1 1 
ATOM   2031 O OE2 . GLU   C 1 80 ? 4.709   -28.629 15.176  1.00 50.36  ? 79  GLU   C OE2 1 
ATOM   2032 N N   . GLY   C 1 81 ? 10.664  -27.919 14.233  1.00 30.30  ? 80  GLY   C N   1 
ATOM   2033 C CA  . GLY   C 1 81 ? 11.477  -27.469 15.359  1.00 29.42  ? 80  GLY   C CA  1 
ATOM   2034 C C   . GLY   C 1 81 ? 12.230  -26.158 15.077  1.00 24.42  ? 80  GLY   C C   1 
ATOM   2035 O O   . GLY   C 1 81 ? 12.500  -25.368 15.992  1.00 26.36  ? 80  GLY   C O   1 
ATOM   2036 N N   . LEU   C 1 82 ? 12.617  -25.928 13.814  1.00 29.50  ? 81  LEU   C N   1 
ATOM   2037 C CA  . LEU   C 1 82 ? 13.193  -24.645 13.426  1.00 29.96  ? 81  LEU   C CA  1 
ATOM   2038 C C   . LEU   C 1 82 ? 12.163  -23.533 13.665  1.00 26.60  ? 81  LEU   C C   1 
ATOM   2039 O O   . LEU   C 1 82 ? 12.533  -22.451 14.115  1.00 29.97  ? 81  LEU   C O   1 
ATOM   2040 C CB  . LEU   C 1 82 ? 13.674  -24.611 11.971  1.00 32.87  ? 81  LEU   C CB  1 
ATOM   2041 C CG  . LEU   C 1 82 ? 14.899  -25.460 11.619  1.00 27.06  ? 81  LEU   C CG  1 
ATOM   2042 C CD1 . LEU   C 1 82 ? 15.011  -25.270 10.119  1.00 28.89  ? 81  LEU   C CD1 1 
ATOM   2043 C CD2 . LEU   C 1 82 ? 16.205  -24.972 12.250  1.00 26.88  ? 81  LEU   C CD2 1 
ATOM   2044 N N   . TRP   C 1 83 ? 10.889  -23.775 13.342  1.00 29.73  ? 82  TRP   C N   1 
ATOM   2045 C CA  . TRP   C 1 83 ? 9.883   -22.726 13.558  1.00 37.97  ? 82  TRP   C CA  1 
ATOM   2046 C C   . TRP   C 1 83 ? 9.759   -22.381 15.049  1.00 34.34  ? 82  TRP   C C   1 
ATOM   2047 O O   . TRP   C 1 83 ? 9.706   -21.205 15.414  1.00 30.52  ? 82  TRP   C O   1 
ATOM   2048 C CB  . TRP   C 1 83 ? 8.500   -23.125 13.010  1.00 37.34  ? 82  TRP   C CB  1 
ATOM   2049 C CG  . TRP   C 1 83 ? 7.521   -21.978 13.086  1.00 41.65  ? 82  TRP   C CG  1 
ATOM   2050 C CD1 . TRP   C 1 83 ? 7.329   -20.940 12.213  1.00 37.92  ? 82  TRP   C CD1 1 
ATOM   2051 C CD2 . TRP   C 1 83 ? 6.633   -21.713 14.189  1.00 38.92  ? 82  TRP   C CD2 1 
ATOM   2052 N NE1 . TRP   C 1 83 ? 6.364   -20.066 12.678  1.00 32.34  ? 82  TRP   C NE1 1 
ATOM   2053 C CE2 . TRP   C 1 83 ? 5.936   -20.508 13.892  1.00 34.71  ? 82  TRP   C CE2 1 
ATOM   2054 C CE3 . TRP   C 1 83 ? 6.377   -22.375 15.398  1.00 45.16  ? 82  TRP   C CE3 1 
ATOM   2055 C CZ2 . TRP   C 1 83 ? 4.987   -19.975 14.755  1.00 40.01  ? 82  TRP   C CZ2 1 
ATOM   2056 C CZ3 . TRP   C 1 83 ? 5.446   -21.833 16.252  1.00 44.32  ? 82  TRP   C CZ3 1 
ATOM   2057 C CH2 . TRP   C 1 83 ? 4.771   -20.655 15.932  1.00 41.80  ? 82  TRP   C CH2 1 
ATOM   2058 N N   . GLU   C 1 84 ? 9.770   -23.412 15.898  1.00 39.01  ? 83  GLU   C N   1 
ATOM   2059 C CA  . GLU   C 1 84 ? 9.617   -23.265 17.352  1.00 41.43  ? 83  GLU   C CA  1 
ATOM   2060 C C   . GLU   C 1 84 ? 10.766  -22.478 17.997  1.00 35.74  ? 83  GLU   C C   1 
ATOM   2061 O O   . GLU   C 1 84 ? 10.521  -21.614 18.851  1.00 35.25  ? 83  GLU   C O   1 
ATOM   2062 C CB  . GLU   C 1 84 ? 9.444   -24.570 18.145  1.00 37.19  ? 83  GLU   C CB  1 
ATOM   2063 C CG  . GLU   C 1 84 ? 8.243   -25.418 17.728  1.00 42.43  ? 83  GLU   C CG  1 
ATOM   2064 C CD  . GLU   C 1 84 ? 8.183   -26.852 18.252  1.00 46.16  ? 83  GLU   C CD  1 
ATOM   2065 O OE1 . GLU   C 1 84 ? 9.140   -27.284 18.947  1.00 38.44  ? 83  GLU   C OE1 1 
ATOM   2066 O OE2 . GLU   C 1 84 ? 7.165   -27.552 17.972  1.00 43.17  ? 83  GLU   C OE2 1 
ATOM   2067 N N   . ILE   C 1 85 ? 12.017  -22.763 17.591  1.00 34.51  ? 84  ILE   C N   1 
ATOM   2068 C CA  . ILE   C 1 85 ? 13.176  -22.155 18.229  1.00 32.65  ? 84  ILE   C CA  1 
ATOM   2069 C C   . ILE   C 1 85 ? 13.237  -20.649 17.960  1.00 35.04  ? 84  ILE   C C   1 
ATOM   2070 O O   . ILE   C 1 85 ? 13.702  -19.881 18.785  1.00 33.39  ? 84  ILE   C O   1 
ATOM   2071 C CB  . ILE   C 1 85 ? 14.486  -22.934 17.960  1.00 33.39  ? 84  ILE   C CB  1 
ATOM   2072 C CG1 . ILE   C 1 85 ? 15.603  -22.524 18.955  1.00 28.23  ? 84  ILE   C CG1 1 
ATOM   2073 C CG2 . ILE   C 1 85 ? 14.938  -22.867 16.489  1.00 35.54  ? 84  ILE   C CG2 1 
ATOM   2074 C CD1 . ILE   C 1 85 ? 16.861  -23.357 18.842  1.00 33.29  ? 84  ILE   C CD1 1 
ATOM   2075 N N   . GLN   C 1 86 ? 12.712  -20.225 16.807  1.00 34.09  ? 85  GLN   C N   1 
ATOM   2076 C CA  . GLN   C 1 86 ? 12.760  -18.820 16.411  1.00 36.56  ? 85  GLN   C CA  1 
ATOM   2077 C C   . GLN   C 1 86 ? 11.530  -18.090 16.946  1.00 31.68  ? 85  GLN   C C   1 
ATOM   2078 O O   . GLN   C 1 86 ? 11.639  -16.920 17.304  1.00 38.55  ? 85  GLN   C O   1 
ATOM   2079 C CB  . GLN   C 1 86 ? 12.765  -18.752 14.877  1.00 32.37  ? 85  GLN   C CB  1 
ATOM   2080 C CG  . GLN   C 1 86 ? 13.103  -17.388 14.298  1.00 35.60  ? 85  GLN   C CG  1 
ATOM   2081 C CD  . GLN   C 1 86 ? 13.542  -17.453 12.840  1.00 39.65  ? 85  GLN   C CD  1 
ATOM   2082 O OE1 . GLN   C 1 86 ? 13.533  -18.505 12.179  1.00 40.86  ? 85  GLN   C OE1 1 
ATOM   2083 N NE2 . GLN   C 1 86 ? 13.959  -16.313 12.324  1.00 41.54  ? 85  GLN   C NE2 1 
ATOM   2084 N N   . ASN   C 1 87 ? 10.384  -18.792 16.999  1.00 35.33  ? 86  ASN   C N   1 
ATOM   2085 C CA  . ASN   C 1 87 ? 9.064   -18.179 17.125  1.00 37.69  ? 86  ASN   C CA  1 
ATOM   2086 C C   . ASN   C 1 87 ? 8.385   -18.501 18.471  1.00 41.09  ? 86  ASN   C C   1 
ATOM   2087 O O   . ASN   C 1 87 ? 7.535   -17.740 18.916  1.00 41.01  ? 86  ASN   C O   1 
ATOM   2088 C CB  . ASN   C 1 87 ? 8.172   -18.514 15.929  1.00 33.04  ? 86  ASN   C CB  1 
ATOM   2089 C CG  . ASN   C 1 87 ? 8.762   -17.935 14.654  1.00 38.48  ? 86  ASN   C CG  1 
ATOM   2090 O OD1 . ASN   C 1 87 ? 8.853   -16.706 14.510  1.00 45.22  ? 86  ASN   C OD1 1 
ATOM   2091 N ND2 . ASN   C 1 87 ? 9.263   -18.779 13.768  1.00 33.81  ? 86  ASN   C ND2 1 
ATOM   2092 N N   . ASN   C 1 88 ? 8.671   -19.653 19.094  1.00 48.75  ? 87  ASN   C N   1 
ATOM   2093 C CA  . ASN   C 1 88 ? 7.947   -20.057 20.312  1.00 39.11  ? 87  ASN   C CA  1 
ATOM   2094 C C   . ASN   C 1 88 ? 8.875   -20.885 21.208  1.00 39.53  ? 87  ASN   C C   1 
ATOM   2095 O O   . ASN   C 1 88 ? 8.501   -22.010 21.559  1.00 41.47  ? 87  ASN   C O   1 
ATOM   2096 C CB  . ASN   C 1 88 ? 6.670   -20.822 19.950  1.00 43.38  ? 87  ASN   C CB  1 
ATOM   2097 C CG  . ASN   C 1 88 ? 5.641   -20.959 21.064  1.00 53.13  ? 87  ASN   C CG  1 
ATOM   2098 O OD1 . ASN   C 1 88 ? 5.736   -20.311 22.117  1.00 46.71  ? 87  ASN   C OD1 1 
ATOM   2099 N ND2 . ASN   C 1 88 ? 4.656   -21.833 20.867  1.00 46.93  ? 87  ASN   C ND2 1 
ATOM   2100 N N   . PRO   C 1 89 ? 10.108  -20.402 21.546  1.00 33.72  ? 88  PRO   C N   1 
ATOM   2101 C CA  . PRO   C 1 89 ? 11.162  -21.241 22.133  1.00 38.58  ? 88  PRO   C CA  1 
ATOM   2102 C C   . PRO   C 1 89 ? 10.951  -21.613 23.597  1.00 50.58  ? 88  PRO   C C   1 
ATOM   2103 O O   . PRO   C 1 89 ? 11.838  -22.248 24.170  1.00 47.12  ? 88  PRO   C O   1 
ATOM   2104 C CB  . PRO   C 1 89 ? 12.421  -20.401 22.007  1.00 36.76  ? 88  PRO   C CB  1 
ATOM   2105 C CG  . PRO   C 1 89 ? 11.898  -18.978 22.063  1.00 34.23  ? 88  PRO   C CG  1 
ATOM   2106 C CD  . PRO   C 1 89 ? 10.584  -19.036 21.332  1.00 35.75  ? 88  PRO   C CD  1 
ATOM   2107 N N   . HIS   C 1 90 ? 9.817   -21.186 24.191  1.00 49.24  ? 89  HIS   C N   1 
ATOM   2108 C CA  . HIS   C 1 90 ? 9.638   -21.369 25.628  1.00 52.35  ? 89  HIS   C CA  1 
ATOM   2109 C C   . HIS   C 1 90 ? 8.231   -21.814 26.012  1.00 57.18  ? 89  HIS   C C   1 
ATOM   2110 O O   . HIS   C 1 90 ? 7.874   -21.738 27.181  1.00 58.79  ? 89  HIS   C O   1 
ATOM   2111 C CB  . HIS   C 1 90 ? 9.992   -20.100 26.405  1.00 53.27  ? 89  HIS   C CB  1 
ATOM   2112 C CG  . HIS   C 1 90 ? 11.429  -19.704 26.294  1.00 56.01  ? 89  HIS   C CG  1 
ATOM   2113 N ND1 . HIS   C 1 90 ? 12.471  -20.563 26.583  1.00 56.42  ? 89  HIS   C ND1 1 
ATOM   2114 C CD2 . HIS   C 1 90 ? 11.988  -18.532 25.964  1.00 54.13  ? 89  HIS   C CD2 1 
ATOM   2115 C CE1 . HIS   C 1 90 ? 13.627  -19.924 26.408  1.00 57.47  ? 89  HIS   C CE1 1 
ATOM   2116 N NE2 . HIS   C 1 90 ? 13.356  -18.685 26.038  1.00 56.19  ? 89  HIS   C NE2 1 
ATOM   2117 N N   . ALA   C 1 91 ? 7.442   -22.290 25.046  1.00 64.05  ? 90  ALA   C N   1 
ATOM   2118 C CA  . ALA   C 1 91 ? 6.150   -22.879 25.380  1.00 75.27  ? 90  ALA   C CA  1 
ATOM   2119 C C   . ALA   C 1 91 ? 6.351   -24.304 25.895  1.00 78.51  ? 90  ALA   C C   1 
ATOM   2120 O O   . ALA   C 1 91 ? 7.442   -24.851 25.750  1.00 70.33  ? 90  ALA   C O   1 
ATOM   2121 C CB  . ALA   C 1 91 ? 5.208   -22.824 24.196  1.00 65.50  ? 90  ALA   C CB  1 
ATOM   2122 N N   . SER   C 1 92 ? 5.279   -24.899 26.451  1.00 79.84  ? 91  SER   C N   1 
ATOM   2123 C CA  . SER   C 1 92 ? 5.353   -26.042 27.354  1.00 76.59  ? 91  SER   C CA  1 
ATOM   2124 C C   . SER   C 1 92 ? 5.383   -27.398 26.640  1.00 80.30  ? 91  SER   C C   1 
ATOM   2125 O O   . SER   C 1 92 ? 5.884   -28.373 27.202  1.00 88.79  ? 91  SER   C O   1 
ATOM   2126 C CB  . SER   C 1 92 ? 4.280   -25.979 28.426  1.00 73.70  ? 91  SER   C CB  1 
ATOM   2127 O OG  . SER   C 1 92 ? 4.773   -25.332 29.596  1.00 73.78  ? 91  SER   C OG  1 
ATOM   2128 N N   . TYR   C 1 93 ? 4.849   -27.470 25.414  1.00 75.50  ? 92  TYR   C N   1 
ATOM   2129 C CA  . TYR   C 1 93 ? 4.839   -28.717 24.659  1.00 79.26  ? 92  TYR   C CA  1 
ATOM   2130 C C   . TYR   C 1 93 ? 4.900   -29.912 25.632  1.00 84.24  ? 92  TYR   C C   1 
ATOM   2131 O O   . TYR   C 1 93 ? 4.073   -30.855 25.549  1.00 95.36  ? 92  TYR   C O   1 
ATOM   2132 C CB  . TYR   C 1 93 ? 6.032   -28.820 23.703  1.00 78.94  ? 92  TYR   C CB  1 
ATOM   2133 C CG  . TYR   C 1 93 ? 6.367   -27.573 22.890  1.00 73.61  ? 92  TYR   C CG  1 
ATOM   2134 C CD1 . TYR   C 1 93 ? 5.716   -27.298 21.686  1.00 65.89  ? 92  TYR   C CD1 1 
ATOM   2135 C CD2 . TYR   C 1 93 ? 7.346   -26.673 23.325  1.00 64.49  ? 92  TYR   C CD2 1 
ATOM   2136 C CE1 . TYR   C 1 93 ? 6.030   -26.168 20.943  1.00 62.23  ? 92  TYR   C CE1 1 
ATOM   2137 C CE2 . TYR   C 1 93 ? 7.663   -25.535 22.593  1.00 57.37  ? 92  TYR   C CE2 1 
ATOM   2138 C CZ  . TYR   C 1 93 ? 7.007   -25.287 21.397  1.00 59.38  ? 92  TYR   C CZ  1 
ATOM   2139 O OH  . TYR   C 1 93 ? 7.316   -24.158 20.685  1.00 59.50  ? 92  TYR   C OH  1 
HETATM 2140 S S   . SO4   D 2 .  ? -0.033  -33.675 1.942   1.00 105.47 ? 101 SO4   A S   1 
HETATM 2141 O O1  . SO4   D 2 .  ? 0.407   -34.168 0.663   1.00 97.44  ? 101 SO4   A O1  1 
HETATM 2142 O O2  . SO4   D 2 .  ? 0.153   -32.250 2.002   1.00 101.53 ? 101 SO4   A O2  1 
HETATM 2143 O O3  . SO4   D 2 .  ? -1.429  -33.980 2.120   1.00 105.74 ? 101 SO4   A O3  1 
HETATM 2144 O O4  . SO4   D 2 .  ? 0.733   -34.302 2.984   1.00 99.97  ? 101 SO4   A O4  1 
HETATM 2145 S S   . SO4   E 2 .  ? -10.965 -24.482 0.758   1.00 103.40 ? 102 SO4   A S   1 
HETATM 2146 O O1  . SO4   E 2 .  ? -10.798 -24.138 -0.631  1.00 104.11 ? 102 SO4   A O1  1 
HETATM 2147 O O2  . SO4   E 2 .  ? -10.970 -23.285 1.557   1.00 100.89 ? 102 SO4   A O2  1 
HETATM 2148 O O3  . SO4   E 2 .  ? -12.212 -25.181 0.929   1.00 109.90 ? 102 SO4   A O3  1 
HETATM 2149 O O4  . SO4   E 2 .  ? -9.881  -25.326 1.178   1.00 106.44 ? 102 SO4   A O4  1 
HETATM 2150 C C1  . EDO   F 3 .  ? 13.233  -19.686 -7.573  1.00 43.16  ? 103 EDO   A C1  1 
HETATM 2151 O O1  . EDO   F 3 .  ? 14.394  -18.930 -7.213  1.00 35.78  ? 103 EDO   A O1  1 
HETATM 2152 C C2  . EDO   F 3 .  ? 12.349  -19.095 -8.632  1.00 40.85  ? 103 EDO   A C2  1 
HETATM 2153 O O2  . EDO   F 3 .  ? 11.772  -17.832 -8.312  1.00 37.34  ? 103 EDO   A O2  1 
HETATM 2154 S S   . SO4   G 2 .  ? 7.919   -29.491 5.841   1.00 62.42  ? 104 SO4   A S   1 
HETATM 2155 O O1  . SO4   G 2 .  ? 8.438   -28.423 5.042   1.00 66.12  ? 104 SO4   A O1  1 
HETATM 2156 O O2  . SO4   G 2 .  ? 7.597   -30.603 4.975   1.00 70.24  ? 104 SO4   A O2  1 
HETATM 2157 O O3  . SO4   G 2 .  ? 8.912   -29.886 6.802   1.00 62.69  ? 104 SO4   A O3  1 
HETATM 2158 O O4  . SO4   G 2 .  ? 6.715   -29.062 6.535   1.00 58.99  ? 104 SO4   A O4  1 
HETATM 2159 S S   . SO4   H 2 .  ? 7.164   -8.478  -24.657 1.00 71.71  ? 101 SO4   B S   1 
HETATM 2160 O O1  . SO4   H 2 .  ? 8.179   -8.444  -25.689 1.00 42.91  ? 101 SO4   B O1  1 
HETATM 2161 O O2  . SO4   H 2 .  ? 5.956   -9.028  -25.217 1.00 51.52  ? 101 SO4   B O2  1 
HETATM 2162 O O3  . SO4   H 2 .  ? 7.564   -9.296  -23.521 1.00 47.82  ? 101 SO4   B O3  1 
HETATM 2163 O O4  . SO4   H 2 .  ? 6.938   -7.124  -24.214 1.00 68.70  ? 101 SO4   B O4  1 
HETATM 2164 S S   . SO4   I 2 .  ? 14.043  -27.222 -26.259 1.00 75.20  ? 102 SO4   B S   1 
HETATM 2165 O O1  . SO4   I 2 .  ? 15.282  -26.823 -25.663 1.00 57.88  ? 102 SO4   B O1  1 
HETATM 2166 O O2  . SO4   I 2 .  ? 14.311  -28.227 -27.260 1.00 82.72  ? 102 SO4   B O2  1 
HETATM 2167 O O3  . SO4   I 2 .  ? 13.178  -27.757 -25.238 1.00 82.39  ? 102 SO4   B O3  1 
HETATM 2168 O O4  . SO4   I 2 .  ? 13.390  -26.107 -26.893 1.00 73.20  ? 102 SO4   B O4  1 
HETATM 2169 N N1  . A1A4A J 4 .  ? 17.066  -14.046 -22.316 0.80 48.66  ? 103 A1A4A B N1  1 
HETATM 2170 C C4  . A1A4A J 4 .  ? 18.133  -16.495 -19.899 0.80 53.83  ? 103 A1A4A B C4  1 
HETATM 2171 C C5  . A1A4A J 4 .  ? 18.266  -16.400 -18.386 0.80 54.67  ? 103 A1A4A B C5  1 
HETATM 2172 C C6  . A1A4A J 4 .  ? 19.511  -15.631 -17.962 0.80 52.94  ? 103 A1A4A B C6  1 
HETATM 2173 C C7  . A1A4A J 4 .  ? 18.991  -14.600 -16.982 0.80 53.12  ? 103 A1A4A B C7  1 
HETATM 2174 C C8  . A1A4A J 4 .  ? 17.495  -14.551 -17.195 0.80 53.07  ? 103 A1A4A B C8  1 
HETATM 2175 O O   . A1A4A J 4 .  ? 18.455  -17.515 -20.485 0.80 55.19  ? 103 A1A4A B O   1 
HETATM 2176 O O1  . A1A4A J 4 .  ? 17.113  -15.776 -17.810 0.80 55.45  ? 103 A1A4A B O1  1 
HETATM 2177 N N2  . A1A4A J 4 .  ? 17.683  -15.374 -20.505 0.80 49.19  ? 103 A1A4A B N2  1 
HETATM 2178 C C3  . A1A4A J 4 .  ? 17.373  -15.227 -21.844 0.80 49.14  ? 103 A1A4A B C3  1 
HETATM 2179 N N   . A1A4A J 4 .  ? 16.821  -14.071 -23.697 0.80 47.25  ? 103 A1A4A B N   1 
HETATM 2180 S S   . A1A4A J 4 .  ? 17.397  -16.507 -23.045 0.80 44.07  ? 103 A1A4A B S   1 
HETATM 2181 C C2  . A1A4A J 4 .  ? 16.923  -15.248 -24.210 0.80 46.93  ? 103 A1A4A B C2  1 
HETATM 2182 C C1  . A1A4A J 4 .  ? 16.570  -15.564 -25.635 0.80 38.83  ? 103 A1A4A B C1  1 
HETATM 2183 C C   . A1A4A J 4 .  ? 16.958  -16.930 -26.123 0.80 34.27  ? 103 A1A4A B C   1 
HETATM 2184 C C1  . EDO   K 3 .  ? 15.958  -36.455 16.789  1.00 49.22  ? 101 EDO   C C1  1 
HETATM 2185 O O1  . EDO   K 3 .  ? 14.768  -37.002 16.238  1.00 52.76  ? 101 EDO   C O1  1 
HETATM 2186 C C2  . EDO   K 3 .  ? 15.598  -35.334 17.656  1.00 43.96  ? 101 EDO   C C2  1 
HETATM 2187 O O2  . EDO   K 3 .  ? 14.593  -35.766 18.539  1.00 38.49  ? 101 EDO   C O2  1 
HETATM 2188 S S   . SO4   L 2 .  ? 28.382  -38.022 12.382  1.00 95.39  ? 102 SO4   C S   1 
HETATM 2189 O O1  . SO4   L 2 .  ? 29.745  -37.727 12.005  1.00 102.66 ? 102 SO4   C O1  1 
HETATM 2190 O O2  . SO4   L 2 .  ? 27.497  -37.042 11.803  1.00 81.53  ? 102 SO4   C O2  1 
HETATM 2191 O O3  . SO4   L 2 .  ? 28.017  -39.336 11.924  1.00 71.83  ? 102 SO4   C O3  1 
HETATM 2192 O O4  . SO4   L 2 .  ? 28.280  -37.983 13.817  1.00 115.48 ? 102 SO4   C O4  1 
HETATM 2193 O O   . HOH   M 5 .  ? -4.946  -28.625 5.453   1.00 49.73  ? 201 HOH   A O   1 
HETATM 2194 O O   . HOH   M 5 .  ? 10.577  -8.906  -12.403 1.00 45.24  ? 202 HOH   A O   1 
HETATM 2195 O O   . HOH   M 5 .  ? 7.214   -32.742 4.752   1.00 54.80  ? 203 HOH   A O   1 
HETATM 2196 O O   . HOH   M 5 .  ? 4.597   -29.532 6.927   1.00 55.43  ? 204 HOH   A O   1 
HETATM 2197 O O   . HOH   M 5 .  ? -2.590  -9.658  4.506   1.00 47.67  ? 205 HOH   A O   1 
HETATM 2198 O O   . HOH   M 5 .  ? -2.974  3.316   -2.120  1.00 48.05  ? 206 HOH   A O   1 
HETATM 2199 O O   . HOH   M 5 .  ? 6.442   -10.586 -12.044 1.00 48.50  ? 207 HOH   A O   1 
HETATM 2200 O O   . HOH   M 5 .  ? -3.966  -30.776 -3.453  1.00 83.39  ? 208 HOH   A O   1 
HETATM 2201 O O   . HOH   M 5 .  ? 10.093  -29.560 3.631   1.00 47.81  ? 209 HOH   A O   1 
HETATM 2202 O O   . HOH   M 5 .  ? 4.305   -7.368  3.900   1.00 34.95  ? 210 HOH   A O   1 
HETATM 2203 O O   . HOH   M 5 .  ? -4.645  -10.956 6.746   1.00 54.85  ? 211 HOH   A O   1 
HETATM 2204 O O   . HOH   M 5 .  ? 7.186   -8.171  4.555   1.00 45.70  ? 212 HOH   A O   1 
HETATM 2205 O O   . HOH   M 5 .  ? -0.330  -33.923 5.217   1.00 61.92  ? 213 HOH   A O   1 
HETATM 2206 O O   . HOH   M 5 .  ? 8.381   -18.083 -11.114 1.00 40.06  ? 214 HOH   A O   1 
HETATM 2207 O O   . HOH   M 5 .  ? 12.053  -9.728  -7.260  1.00 40.73  ? 215 HOH   A O   1 
HETATM 2208 O O   . HOH   M 5 .  ? 8.620   -18.568 9.811   1.00 48.42  ? 216 HOH   A O   1 
HETATM 2209 O O   . HOH   M 5 .  ? 3.111   -33.849 3.727   1.00 63.40  ? 217 HOH   A O   1 
HETATM 2210 O O   . HOH   M 5 .  ? 10.584  -12.216 5.978   1.00 47.26  ? 218 HOH   A O   1 
HETATM 2211 O O   . HOH   M 5 .  ? 1.247   -4.766  -10.204 1.00 34.37  ? 219 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? 15.695  -11.767 -16.692 1.00 44.52  ? 220 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? 18.971  -15.545 7.296   1.00 32.02  ? 221 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? 1.133   0.724   -7.394  1.00 49.82  ? 222 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? 1.031   -18.230 -18.780 1.00 46.93  ? 223 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? 0.214   -24.312 13.806  1.00 55.91  ? 224 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? -6.456  -15.706 -8.201  1.00 30.61  ? 225 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? 16.216  -18.103 -9.873  1.00 49.72  ? 226 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 7.156   -17.055 8.577   1.00 52.58  ? 227 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? -8.587  -15.705 -1.226  1.00 37.26  ? 228 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 13.094  -15.775 -9.382  1.00 40.68  ? 229 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 0.669   -24.465 -5.602  1.00 58.95  ? 230 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? 14.982  -24.401 2.042   1.00 43.71  ? 231 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 7.922   -9.287  9.010   1.00 53.22  ? 232 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 16.368  -13.019 1.412   1.00 22.86  ? 233 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 3.747   -3.376  -3.235  1.00 39.02  ? 234 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? -1.710  -20.726 6.967   1.00 35.77  ? 235 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 10.035  -23.563 9.914   1.00 40.24  ? 236 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 1.458   -25.076 -10.294 1.00 45.08  ? 237 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? -2.691  -21.824 -0.658  1.00 31.10  ? 238 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? -1.715  -28.928 9.892   1.00 77.16  ? 239 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 14.207  -17.574 -18.830 1.00 43.14  ? 240 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 9.016   -5.974  -1.649  1.00 42.84  ? 241 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 3.795   -7.648  1.129   1.00 38.74  ? 242 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? -4.565  -25.872 7.859   1.00 52.85  ? 243 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? 2.083   -29.626 -0.229  1.00 48.88  ? 244 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 9.245   -13.080 9.750   1.00 44.89  ? 245 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 8.888   -27.643 -7.249  1.00 64.75  ? 246 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 10.251  -5.293  -8.015  1.00 46.69  ? 247 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? -9.564  -20.712 -1.347  1.00 47.74  ? 248 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? 0.399   -10.623 -16.166 1.00 73.12  ? 249 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 0.798   -10.372 11.710  1.00 39.03  ? 250 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? -5.203  -21.196 5.961   1.00 51.27  ? 251 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 20.506  -19.637 -3.336  1.00 53.66  ? 252 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 12.473  -11.983 -4.233  1.00 24.33  ? 253 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? -5.378  -26.072 -5.455  1.00 54.89  ? 254 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 8.775   -9.211  -13.677 1.00 41.84  ? 255 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? -8.851  -16.474 1.810   1.00 51.13  ? 256 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? 12.118  -15.031 -12.229 1.00 48.67  ? 257 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 7.145   -7.827  1.240   1.00 33.24  ? 258 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? -6.523  -19.425 -5.950  1.00 44.02  ? 259 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? -7.047  -12.685 6.593   1.00 48.90  ? 260 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? -6.836  -11.244 -11.309 1.00 43.73  ? 261 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? -0.716  -23.840 9.288   1.00 53.35  ? 262 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? -2.473  -11.806 11.264  1.00 40.38  ? 263 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 11.952  -13.322 -8.402  1.00 44.91  ? 264 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 10.147  -5.746  -3.688  1.00 50.53  ? 265 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 14.896  -11.964 -5.280  1.00 43.74  ? 266 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 10.800  -12.417 -6.139  1.00 30.31  ? 267 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -8.044  -9.859  -7.707  1.00 48.19  ? 268 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? -8.389  -21.079 -5.896  1.00 52.40  ? 269 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 8.188   -17.564 -15.738 1.00 48.67  ? 270 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -4.465  -7.402  -11.369 1.00 50.72  ? 271 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? -1.687  -21.310 9.508   1.00 90.44  ? 272 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 8.899   -20.386 -18.543 1.00 59.02  ? 273 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 1.639   -6.016  5.425   1.00 36.68  ? 274 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 5.809   -15.543 -15.032 1.00 46.01  ? 275 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 5.814   -5.689  0.483   1.00 58.43  ? 276 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? -8.936  -17.303 6.495   1.00 49.20  ? 277 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? -4.786  -8.075  10.372  1.00 47.30  ? 278 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? -8.772  -20.018 -3.745  1.00 53.01  ? 279 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? -6.429  -13.925 -16.662 1.00 68.99  ? 280 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? 20.549  -16.790 -3.489  1.00 29.57  ? 281 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -0.661  4.719   -2.989  1.00 92.78  ? 282 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? 8.129   -16.336 -13.225 1.00 45.72  ? 283 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? -2.311  -7.031  11.387  1.00 48.02  ? 284 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? 8.427   -30.545 9.857   1.00 43.12  ? 285 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 21.474  -16.683 -0.481  1.00 36.84  ? 286 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? -10.302 -13.241 -0.429  1.00 31.20  ? 287 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? -8.063  -11.641 -8.112  1.00 33.47  ? 288 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? -10.202 -15.630 11.456  1.00 59.87  ? 289 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? -0.681  -8.177  -13.330 1.00 48.08  ? 290 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 12.491  -28.458 -5.163  1.00 64.02  ? 291 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 15.077  -28.466 -0.741  1.00 62.66  ? 292 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? -0.805  -29.015 -7.275  1.00 57.00  ? 293 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 2.970   -10.040 -13.191 1.00 60.52  ? 294 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? -7.358  -26.216 3.437   1.00 59.21  ? 295 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? 10.165  -1.473  -2.328  1.00 71.24  ? 296 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? -4.471  -11.379 10.031  1.00 56.55  ? 297 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 9.496   -2.779  -0.154  1.00 63.45  ? 298 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? -8.026  -19.652 7.165   1.00 70.68  ? 299 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? 6.586   -17.902 -14.335 1.00 58.09  ? 300 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? -0.918  -3.015  -10.977 1.00 63.29  ? 301 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 10.980  -20.891 10.735  1.00 41.86  ? 302 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 8.410   -7.929  3.388   1.00 47.94  ? 303 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -8.203  -14.343 -9.326  1.00 48.47  ? 304 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? -11.393 -27.941 -1.598  1.00 61.88  ? 305 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? 8.001   -5.007  2.915   1.00 64.43  ? 306 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 4.220   -6.855  -11.263 1.00 51.63  ? 307 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 20.697  -21.645 -9.904  1.00 54.75  ? 308 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 5.490   -30.464 -2.951  1.00 56.90  ? 309 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? 4.251   -9.515  -11.196 1.00 60.34  ? 310 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? -7.319  -22.232 6.066   1.00 49.37  ? 311 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? -6.352  -19.973 -8.869  1.00 54.69  ? 312 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? -7.349  -32.366 3.221   1.00 63.91  ? 313 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? 3.440   -3.121  2.010   1.00 58.21  ? 314 HOH   A O   1 
HETATM 2307 O O   . HOH   N 5 .  ? 15.355  -19.547 -29.042 1.00 43.78  ? 201 HOH   B O   1 
HETATM 2308 O O   . HOH   N 5 .  ? 27.496  -8.160  -28.344 1.00 55.90  ? 202 HOH   B O   1 
HETATM 2309 O O   . HOH   N 5 .  ? 6.430   -15.411 -39.524 1.00 58.84  ? 203 HOH   B O   1 
HETATM 2310 O O   . HOH   N 5 .  ? 22.671  2.869   -21.846 1.00 53.00  ? 204 HOH   B O   1 
HETATM 2311 O O   . HOH   N 5 .  ? 17.251  -7.816  -20.330 1.00 49.96  ? 205 HOH   B O   1 
HETATM 2312 O O   . HOH   N 5 .  ? 12.791  -22.628 -20.765 1.00 50.74  ? 206 HOH   B O   1 
HETATM 2313 O O   . HOH   N 5 .  ? 6.361   -11.885 -25.976 1.00 41.41  ? 207 HOH   B O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 25.618  -5.041  -33.215 1.00 51.41  ? 208 HOH   B O   1 
HETATM 2315 O O   . HOH   N 5 .  ? 25.793  -23.320 -30.820 1.00 41.42  ? 209 HOH   B O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 25.076  -0.809  -29.337 1.00 48.00  ? 210 HOH   B O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 17.795  -10.112 -43.518 1.00 45.44  ? 211 HOH   B O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 38.791  -11.526 -39.139 1.00 56.33  ? 212 HOH   B O   1 
HETATM 2319 O O   . HOH   N 5 .  ? 18.156  -0.665  -38.268 1.00 32.22  ? 213 HOH   B O   1 
HETATM 2320 O O   . HOH   N 5 .  ? 16.682  -19.411 -28.584 1.00 28.24  ? 214 HOH   B O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 24.671  -5.180  -29.628 1.00 49.17  ? 215 HOH   B O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 22.225  -24.417 -28.587 1.00 59.67  ? 216 HOH   B O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 32.596  -18.674 -41.641 1.00 62.43  ? 217 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 20.115  -26.653 -30.169 1.00 56.18  ? 218 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 10.408  -20.075 -43.082 1.00 62.28  ? 219 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 5.908   -7.053  -32.368 1.00 42.26  ? 220 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 34.470  -5.952  -28.325 1.00 83.27  ? 221 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 4.523   -19.057 -25.671 1.00 50.20  ? 222 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 20.852  -13.561 -42.496 1.00 41.30  ? 223 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 19.378  -20.090 -19.972 1.00 57.74  ? 224 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 10.151  -19.055 -32.953 1.00 37.98  ? 225 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 6.813   -18.912 -35.133 1.00 62.71  ? 226 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 16.094  -26.150 -34.531 1.00 47.44  ? 227 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 20.060  -3.041  -22.880 1.00 57.31  ? 228 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 10.519  -16.701 -44.258 1.00 68.37  ? 229 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 17.881  4.507   -34.301 1.00 43.36  ? 230 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 19.375  -26.010 -34.279 1.00 41.48  ? 231 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 25.224  -6.151  -35.361 1.00 58.57  ? 232 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 25.533  -0.721  -27.760 1.00 46.48  ? 233 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 7.426   -18.969 -31.467 1.00 55.03  ? 234 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 17.034  -19.740 -42.055 1.00 58.31  ? 235 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 10.208  0.326   -39.995 1.00 59.73  ? 236 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 31.961  -22.384 -37.384 1.00 60.95  ? 237 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 1.710   -12.865 -27.885 1.00 52.58  ? 238 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 13.604  -4.338  -41.636 1.00 117.05 ? 239 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 21.376  3.710   -32.337 1.00 36.68  ? 240 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 7.310   -8.415  -20.681 1.00 49.40  ? 241 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 26.949  -10.864 -28.400 1.00 44.04  ? 242 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 21.185  -6.547  -42.383 1.00 51.48  ? 243 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 14.520  -6.603  -41.143 1.00 42.38  ? 244 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 23.457  -2.628  -28.890 1.00 40.12  ? 245 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 8.521   -9.058  -16.354 1.00 58.27  ? 246 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 18.002  -26.339 -28.710 1.00 52.42  ? 247 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 23.890  -4.322  -36.397 1.00 35.12  ? 248 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 10.235  -21.951 -32.675 1.00 45.58  ? 249 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 17.996  -15.636 -45.619 1.00 44.64  ? 250 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 11.485  -20.470 -19.959 1.00 108.40 ? 251 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 6.014   -20.671 -24.946 1.00 41.79  ? 252 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 16.921  -28.127 -20.666 1.00 96.51  ? 253 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 14.257  -24.129 -40.559 1.00 50.19  ? 254 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 20.566  -10.031 -42.751 1.00 39.49  ? 255 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 9.635   -12.294 -38.491 1.00 69.89  ? 256 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 23.698  -11.385 -21.277 1.00 59.39  ? 257 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 24.911  -7.218  -42.098 1.00 56.01  ? 258 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 14.422  -27.458 -22.159 1.00 47.02  ? 259 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 25.071  -1.291  -36.729 1.00 59.54  ? 260 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 18.108  -3.629  -21.725 1.00 59.56  ? 261 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 14.494  -8.181  -43.112 1.00 69.79  ? 262 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 9.985   -6.413  -40.827 1.00 45.34  ? 263 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 27.717  -25.306 -34.710 1.00 45.39  ? 264 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 31.696  -12.098 -35.330 1.00 51.81  ? 265 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 28.946  -17.107 -46.814 1.00 68.82  ? 266 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 16.543  2.025   -30.005 1.00 51.42  ? 267 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 19.800  3.829   -33.050 1.00 47.46  ? 268 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 16.599  -0.172  -25.660 1.00 51.37  ? 269 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 7.280   -21.285 -29.789 1.00 49.43  ? 270 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 11.028  -24.506 -29.648 1.00 60.84  ? 271 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 8.807   -6.004  -16.766 1.00 50.29  ? 272 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 27.716  -15.279 -22.984 1.00 53.57  ? 273 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 13.655  -22.110 -42.172 1.00 70.90  ? 274 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 10.478  -12.256 -44.138 1.00 49.69  ? 275 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 21.858  -29.268 -35.508 1.00 47.92  ? 276 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 6.929   -9.940  -18.387 1.00 47.78  ? 277 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 8.521   -22.594 -19.077 1.00 61.32  ? 278 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 1.077   -6.492  -27.856 1.00 64.19  ? 279 HOH   B O   1 
HETATM 2386 O O   . HOH   O 5 .  ? 14.529  -16.906 26.041  1.00 71.07  ? 201 HOH   C O   1 
HETATM 2387 O O   . HOH   O 5 .  ? 29.012  -27.466 31.241  1.00 45.78  ? 202 HOH   C O   1 
HETATM 2388 O O   . HOH   O 5 .  ? 19.089  -41.378 12.366  1.00 36.75  ? 203 HOH   C O   1 
HETATM 2389 O O   . HOH   O 5 .  ? 11.938  -31.446 8.149   1.00 38.93  ? 204 HOH   C O   1 
HETATM 2390 O O   . HOH   O 5 .  ? 24.577  -20.220 29.191  1.00 62.72  ? 205 HOH   C O   1 
HETATM 2391 O O   . HOH   O 5 .  ? 8.093   -36.651 18.457  1.00 54.19  ? 206 HOH   C O   1 
HETATM 2392 O O   . HOH   O 5 .  ? 14.185  -17.621 19.299  1.00 50.48  ? 207 HOH   C O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 13.968  -20.868 12.127  1.00 42.35  ? 208 HOH   C O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 15.576  -37.457 20.046  1.00 50.10  ? 209 HOH   C O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 11.243  -28.383 28.924  1.00 58.59  ? 210 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 25.683  -38.947 12.699  1.00 38.25  ? 211 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 27.441  -37.115 16.035  1.00 47.86  ? 212 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 25.809  -37.463 9.952   1.00 54.58  ? 213 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 14.076  -39.268 17.197  1.00 54.25  ? 214 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 22.203  -20.291 24.013  1.00 46.73  ? 215 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 34.784  -23.998 27.265  1.00 88.53  ? 216 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 31.241  -42.131 15.499  1.00 61.30  ? 217 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 30.499  -39.470 26.999  1.00 56.22  ? 218 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 29.088  -40.105 9.610   1.00 36.43  ? 219 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 8.058   -19.210 23.811  1.00 48.83  ? 220 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 21.418  -28.412 11.089  1.00 32.02  ? 221 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 26.891  -34.493 35.839  1.00 56.40  ? 222 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 30.834  -33.046 26.002  1.00 58.14  ? 223 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 18.181  -20.209 10.580  1.00 38.12  ? 224 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 13.280  -37.130 13.811  1.00 50.26  ? 225 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 25.073  -17.808 20.884  1.00 52.10  ? 226 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 19.982  -28.519 8.543   1.00 39.32  ? 227 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 24.803  -19.755 6.229   1.00 40.35  ? 228 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 29.431  -31.428 15.809  1.00 49.61  ? 229 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 24.849  -17.640 13.600  1.00 43.47  ? 230 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 21.179  -34.309 16.801  1.00 32.32  ? 231 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 30.712  -29.090 31.593  1.00 49.68  ? 232 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 24.400  -31.166 10.764  1.00 44.90  ? 233 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 22.127  -41.314 18.885  1.00 40.75  ? 234 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 12.313  -23.071 27.913  1.00 49.73  ? 235 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 4.520   -26.377 16.916  1.00 50.18  ? 236 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 16.831  -16.766 14.491  1.00 64.69  ? 237 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 21.601  -18.295 21.897  1.00 41.74  ? 238 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 19.006  -18.889 24.905  1.00 37.64  ? 239 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 20.111  -28.738 4.557   1.00 53.35  ? 240 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 30.454  -25.302 31.922  1.00 77.67  ? 241 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 29.728  -29.225 11.971  1.00 50.40  ? 242 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 27.080  -37.213 24.983  1.00 54.61  ? 243 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 7.113   -31.044 11.600  1.00 62.87  ? 244 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 13.229  -29.512 4.007   1.00 48.37  ? 245 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 29.505  -39.576 31.403  1.00 47.54  ? 246 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 20.376  -39.719 26.188  1.00 50.82  ? 247 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 2.240   -28.858 13.458  1.00 62.35  ? 248 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 4.688   -24.216 18.986  1.00 68.01  ? 249 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 31.305  -42.730 11.841  1.00 55.83  ? 250 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 17.632  -36.844 29.310  1.00 68.06  ? 251 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 24.393  -39.648 20.471  1.00 37.76  ? 252 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 29.274  -33.052 36.056  1.00 59.91  ? 253 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 5.973   -17.437 10.940  1.00 56.44  ? 254 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 13.476  -39.037 9.896   1.00 52.75  ? 255 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 28.349  -41.464 27.271  1.00 49.28  ? 256 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 29.369  -32.480 18.124  1.00 41.38  ? 257 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 30.200  -35.459 28.473  1.00 52.03  ? 258 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 21.620  -13.276 13.431  1.00 50.61  ? 259 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 23.433  -16.121 11.925  1.00 41.21  ? 260 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 7.235   -33.663 9.977   1.00 49.45  ? 261 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 27.321  -39.679 24.196  1.00 59.10  ? 262 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 27.254  -15.331 12.923  1.00 46.22  ? 263 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 13.165  -32.349 2.261   1.00 64.77  ? 264 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 16.181  -16.306 24.434  1.00 47.47  ? 265 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 13.868  -39.712 7.611   1.00 63.63  ? 266 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 20.377  -40.409 39.422  1.00 59.75  ? 267 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 32.705  -44.298 14.936  1.00 51.04  ? 268 HOH   C O   1 
# 
