data_7HGC
# 
_entry.id   7HGC 
# 
_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   7HGC         pdb_00007hgc 10.2210/pdb7hgc/pdb 
WWPDB D_1001407438 ?            ?                   
# 
_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                        7HGC 
_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 '(1S)-1-(1-phenyl-1H-1,2,3-triazol-4-yl)ethan-1-amine' 188.229   1   ? ?    ? ? 
5 water       nat water                                                  18.015    278 ? ?    ? ? 
# 
_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 '(1S)-1-(1-phenyl-1H-1,2,3-triazol-4-yl)ethan-1-amine' A1AJ5 
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 
A1AJ5 non-polymer         . '(1S)-1-(1-phenyl-1H-1,2,3-triazol-4-yl)ethan-1-amine' ?                 'C10 H12 N4'     188.229 
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 ?  ?   ?   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 30 ASP ASP C . n 
C 1 32 GLY 32 31 31 GLY GLY C . n 
C 1 33 ALA 33 32 32 ALA ALA C . n 
C 1 34 VAL 34 33 33 VAL VAL C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AJ5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AJ5 
_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 A1AJ5 1   103 101 A1AJ5 LIG B . 
K 3 EDO   1   101 101 EDO   EDO C . 
L 2 SO4   1   102 5   SO4   SO4 C . 
M 5 HOH   1   201 307 HOH   HOH A . 
M 5 HOH   2   202 333 HOH   HOH A . 
M 5 HOH   3   203 259 HOH   HOH A . 
M 5 HOH   4   204 202 HOH   HOH A . 
M 5 HOH   5   205 66  HOH   HOH A . 
M 5 HOH   6   206 349 HOH   HOH A . 
M 5 HOH   7   207 95  HOH   HOH A . 
M 5 HOH   8   208 87  HOH   HOH A . 
M 5 HOH   9   209 84  HOH   HOH A . 
M 5 HOH   10  210 373 HOH   HOH A . 
M 5 HOH   11  211 364 HOH   HOH A . 
M 5 HOH   12  212 304 HOH   HOH A . 
M 5 HOH   13  213 337 HOH   HOH A . 
M 5 HOH   14  214 55  HOH   HOH A . 
M 5 HOH   15  215 91  HOH   HOH A . 
M 5 HOH   16  216 86  HOH   HOH A . 
M 5 HOH   17  217 139 HOH   HOH A . 
M 5 HOH   18  218 278 HOH   HOH A . 
M 5 HOH   19  219 26  HOH   HOH A . 
M 5 HOH   20  220 208 HOH   HOH A . 
M 5 HOH   21  221 28  HOH   HOH A . 
M 5 HOH   22  222 8   HOH   HOH A . 
M 5 HOH   23  223 199 HOH   HOH A . 
M 5 HOH   24  224 34  HOH   HOH A . 
M 5 HOH   25  225 37  HOH   HOH A . 
M 5 HOH   26  226 293 HOH   HOH A . 
M 5 HOH   27  227 71  HOH   HOH A . 
M 5 HOH   28  228 179 HOH   HOH A . 
M 5 HOH   29  229 260 HOH   HOH A . 
M 5 HOH   30  230 167 HOH   HOH A . 
M 5 HOH   31  231 289 HOH   HOH A . 
M 5 HOH   32  232 335 HOH   HOH A . 
M 5 HOH   33  233 32  HOH   HOH A . 
M 5 HOH   34  234 97  HOH   HOH A . 
M 5 HOH   35  235 78  HOH   HOH A . 
M 5 HOH   36  236 38  HOH   HOH A . 
M 5 HOH   37  237 42  HOH   HOH A . 
M 5 HOH   38  238 267 HOH   HOH A . 
M 5 HOH   39  239 211 HOH   HOH A . 
M 5 HOH   40  240 7   HOH   HOH A . 
M 5 HOH   41  241 2   HOH   HOH A . 
M 5 HOH   42  242 41  HOH   HOH A . 
M 5 HOH   43  243 290 HOH   HOH A . 
M 5 HOH   44  244 12  HOH   HOH A . 
M 5 HOH   45  245 203 HOH   HOH A . 
M 5 HOH   46  246 109 HOH   HOH A . 
M 5 HOH   47  247 23  HOH   HOH A . 
M 5 HOH   48  248 1   HOH   HOH A . 
M 5 HOH   49  249 27  HOH   HOH A . 
M 5 HOH   50  250 288 HOH   HOH A . 
M 5 HOH   51  251 274 HOH   HOH A . 
M 5 HOH   52  252 60  HOH   HOH A . 
M 5 HOH   53  253 77  HOH   HOH A . 
M 5 HOH   54  254 111 HOH   HOH A . 
M 5 HOH   55  255 299 HOH   HOH A . 
M 5 HOH   56  256 93  HOH   HOH A . 
M 5 HOH   57  257 115 HOH   HOH A . 
M 5 HOH   58  258 145 HOH   HOH A . 
M 5 HOH   59  259 292 HOH   HOH A . 
M 5 HOH   60  260 300 HOH   HOH A . 
M 5 HOH   61  261 367 HOH   HOH A . 
M 5 HOH   62  262 190 HOH   HOH A . 
M 5 HOH   63  263 218 HOH   HOH A . 
M 5 HOH   64  264 188 HOH   HOH A . 
M 5 HOH   65  265 18  HOH   HOH A . 
M 5 HOH   66  266 21  HOH   HOH A . 
M 5 HOH   67  267 99  HOH   HOH A . 
M 5 HOH   68  268 346 HOH   HOH A . 
M 5 HOH   69  269 94  HOH   HOH A . 
M 5 HOH   70  270 20  HOH   HOH A . 
M 5 HOH   71  271 164 HOH   HOH A . 
M 5 HOH   72  272 372 HOH   HOH A . 
M 5 HOH   73  273 131 HOH   HOH A . 
M 5 HOH   74  274 58  HOH   HOH A . 
M 5 HOH   75  275 116 HOH   HOH A . 
M 5 HOH   76  276 222 HOH   HOH A . 
M 5 HOH   77  277 73  HOH   HOH A . 
M 5 HOH   78  278 165 HOH   HOH A . 
M 5 HOH   79  279 47  HOH   HOH A . 
M 5 HOH   80  280 361 HOH   HOH A . 
M 5 HOH   81  281 301 HOH   HOH A . 
M 5 HOH   82  282 143 HOH   HOH A . 
M 5 HOH   83  283 358 HOH   HOH A . 
M 5 HOH   84  284 14  HOH   HOH A . 
M 5 HOH   85  285 281 HOH   HOH A . 
M 5 HOH   86  286 9   HOH   HOH A . 
M 5 HOH   87  287 354 HOH   HOH A . 
M 5 HOH   88  288 16  HOH   HOH A . 
M 5 HOH   89  289 318 HOH   HOH A . 
M 5 HOH   90  290 113 HOH   HOH A . 
M 5 HOH   91  291 31  HOH   HOH A . 
M 5 HOH   92  292 19  HOH   HOH A . 
M 5 HOH   93  293 152 HOH   HOH A . 
M 5 HOH   94  294 327 HOH   HOH A . 
M 5 HOH   95  295 22  HOH   HOH A . 
M 5 HOH   96  296 64  HOH   HOH A . 
M 5 HOH   97  297 35  HOH   HOH A . 
M 5 HOH   98  298 365 HOH   HOH A . 
M 5 HOH   99  299 146 HOH   HOH A . 
M 5 HOH   100 300 63  HOH   HOH A . 
M 5 HOH   101 301 296 HOH   HOH A . 
M 5 HOH   102 302 210 HOH   HOH A . 
M 5 HOH   103 303 75  HOH   HOH A . 
M 5 HOH   104 304 108 HOH   HOH A . 
M 5 HOH   105 305 185 HOH   HOH A . 
M 5 HOH   106 306 83  HOH   HOH A . 
M 5 HOH   107 307 219 HOH   HOH A . 
M 5 HOH   108 308 57  HOH   HOH A . 
M 5 HOH   109 309 347 HOH   HOH A . 
M 5 HOH   110 310 205 HOH   HOH A . 
M 5 HOH   111 311 332 HOH   HOH A . 
M 5 HOH   112 312 283 HOH   HOH A . 
M 5 HOH   113 313 156 HOH   HOH A . 
M 5 HOH   114 314 313 HOH   HOH A . 
M 5 HOH   115 315 125 HOH   HOH A . 
N 5 HOH   1   201 272 HOH   HOH B . 
N 5 HOH   2   202 184 HOH   HOH B . 
N 5 HOH   3   203 247 HOH   HOH B . 
N 5 HOH   4   204 98  HOH   HOH B . 
N 5 HOH   5   205 258 HOH   HOH B . 
N 5 HOH   6   206 89  HOH   HOH B . 
N 5 HOH   7   207 331 HOH   HOH B . 
N 5 HOH   8   208 172 HOH   HOH B . 
N 5 HOH   9   209 377 HOH   HOH B . 
N 5 HOH   10  210 329 HOH   HOH B . 
N 5 HOH   11  211 54  HOH   HOH B . 
N 5 HOH   12  212 69  HOH   HOH B . 
N 5 HOH   13  213 168 HOH   HOH B . 
N 5 HOH   14  214 215 HOH   HOH B . 
N 5 HOH   15  215 123 HOH   HOH B . 
N 5 HOH   16  216 96  HOH   HOH B . 
N 5 HOH   17  217 169 HOH   HOH B . 
N 5 HOH   18  218 249 HOH   HOH B . 
N 5 HOH   19  219 119 HOH   HOH B . 
N 5 HOH   20  220 153 HOH   HOH B . 
N 5 HOH   21  221 279 HOH   HOH B . 
N 5 HOH   22  222 10  HOH   HOH B . 
N 5 HOH   23  223 137 HOH   HOH B . 
N 5 HOH   24  224 6   HOH   HOH B . 
N 5 HOH   25  225 150 HOH   HOH B . 
N 5 HOH   26  226 117 HOH   HOH B . 
N 5 HOH   27  227 17  HOH   HOH B . 
N 5 HOH   28  228 5   HOH   HOH B . 
N 5 HOH   29  229 61  HOH   HOH B . 
N 5 HOH   30  230 59  HOH   HOH B . 
N 5 HOH   31  231 261 HOH   HOH B . 
N 5 HOH   32  232 340 HOH   HOH B . 
N 5 HOH   33  233 223 HOH   HOH B . 
N 5 HOH   34  234 320 HOH   HOH B . 
N 5 HOH   35  235 13  HOH   HOH B . 
N 5 HOH   36  236 120 HOH   HOH B . 
N 5 HOH   37  237 280 HOH   HOH B . 
N 5 HOH   38  238 25  HOH   HOH B . 
N 5 HOH   39  239 36  HOH   HOH B . 
N 5 HOH   40  240 24  HOH   HOH B . 
N 5 HOH   41  241 170 HOH   HOH B . 
N 5 HOH   42  242 68  HOH   HOH B . 
N 5 HOH   43  243 76  HOH   HOH B . 
N 5 HOH   44  244 74  HOH   HOH B . 
N 5 HOH   45  245 101 HOH   HOH B . 
N 5 HOH   46  246 224 HOH   HOH B . 
N 5 HOH   47  247 214 HOH   HOH B . 
N 5 HOH   48  248 217 HOH   HOH B . 
N 5 HOH   49  249 350 HOH   HOH B . 
N 5 HOH   50  250 79  HOH   HOH B . 
N 5 HOH   51  251 315 HOH   HOH B . 
N 5 HOH   52  252 197 HOH   HOH B . 
N 5 HOH   53  253 72  HOH   HOH B . 
N 5 HOH   54  254 175 HOH   HOH B . 
N 5 HOH   55  255 370 HOH   HOH B . 
N 5 HOH   56  256 319 HOH   HOH B . 
N 5 HOH   57  257 303 HOH   HOH B . 
N 5 HOH   58  258 322 HOH   HOH B . 
N 5 HOH   59  259 104 HOH   HOH B . 
N 5 HOH   60  260 374 HOH   HOH B . 
N 5 HOH   61  261 177 HOH   HOH B . 
N 5 HOH   62  262 46  HOH   HOH B . 
N 5 HOH   63  263 182 HOH   HOH B . 
N 5 HOH   64  264 356 HOH   HOH B . 
N 5 HOH   65  265 44  HOH   HOH B . 
N 5 HOH   66  266 160 HOH   HOH B . 
N 5 HOH   67  267 336 HOH   HOH B . 
N 5 HOH   68  268 291 HOH   HOH B . 
N 5 HOH   69  269 201 HOH   HOH B . 
N 5 HOH   70  270 341 HOH   HOH B . 
N 5 HOH   71  271 163 HOH   HOH B . 
N 5 HOH   72  272 348 HOH   HOH B . 
N 5 HOH   73  273 369 HOH   HOH B . 
N 5 HOH   74  274 375 HOH   HOH B . 
N 5 HOH   75  275 103 HOH   HOH B . 
N 5 HOH   76  276 316 HOH   HOH B . 
N 5 HOH   77  277 107 HOH   HOH B . 
N 5 HOH   78  278 314 HOH   HOH B . 
N 5 HOH   79  279 92  HOH   HOH B . 
N 5 HOH   80  280 312 HOH   HOH B . 
O 5 HOH   1   201 254 HOH   HOH C . 
O 5 HOH   2   202 323 HOH   HOH C . 
O 5 HOH   3   203 321 HOH   HOH C . 
O 5 HOH   4   204 360 HOH   HOH C . 
O 5 HOH   5   205 357 HOH   HOH C . 
O 5 HOH   6   206 368 HOH   HOH C . 
O 5 HOH   7   207 317 HOH   HOH C . 
O 5 HOH   8   208 161 HOH   HOH C . 
O 5 HOH   9   209 271 HOH   HOH C . 
O 5 HOH   10  210 151 HOH   HOH C . 
O 5 HOH   11  211 189 HOH   HOH C . 
O 5 HOH   12  212 344 HOH   HOH C . 
O 5 HOH   13  213 134 HOH   HOH C . 
O 5 HOH   14  214 173 HOH   HOH C . 
O 5 HOH   15  215 118 HOH   HOH C . 
O 5 HOH   16  216 226 HOH   HOH C . 
O 5 HOH   17  217 326 HOH   HOH C . 
O 5 HOH   18  218 284 HOH   HOH C . 
O 5 HOH   19  219 90  HOH   HOH C . 
O 5 HOH   20  220 85  HOH   HOH C . 
O 5 HOH   21  221 302 HOH   HOH C . 
O 5 HOH   22  222 142 HOH   HOH C . 
O 5 HOH   23  223 294 HOH   HOH C . 
O 5 HOH   24  224 342 HOH   HOH C . 
O 5 HOH   25  225 309 HOH   HOH C . 
O 5 HOH   26  226 82  HOH   HOH C . 
O 5 HOH   27  227 56  HOH   HOH C . 
O 5 HOH   28  228 353 HOH   HOH C . 
O 5 HOH   29  229 126 HOH   HOH C . 
O 5 HOH   30  230 269 HOH   HOH C . 
O 5 HOH   31  231 325 HOH   HOH C . 
O 5 HOH   32  232 15  HOH   HOH C . 
O 5 HOH   33  233 4   HOH   HOH C . 
O 5 HOH   34  234 242 HOH   HOH C . 
O 5 HOH   35  235 359 HOH   HOH C . 
O 5 HOH   36  236 49  HOH   HOH C . 
O 5 HOH   37  237 45  HOH   HOH C . 
O 5 HOH   38  238 132 HOH   HOH C . 
O 5 HOH   39  239 157 HOH   HOH C . 
O 5 HOH   40  240 122 HOH   HOH C . 
O 5 HOH   41  241 40  HOH   HOH C . 
O 5 HOH   42  242 102 HOH   HOH C . 
O 5 HOH   43  243 135 HOH   HOH C . 
O 5 HOH   44  244 43  HOH   HOH C . 
O 5 HOH   45  245 130 HOH   HOH C . 
O 5 HOH   46  246 345 HOH   HOH C . 
O 5 HOH   47  247 275 HOH   HOH C . 
O 5 HOH   48  248 149 HOH   HOH C . 
O 5 HOH   49  249 48  HOH   HOH C . 
O 5 HOH   50  250 328 HOH   HOH C . 
O 5 HOH   51  251 355 HOH   HOH C . 
O 5 HOH   52  252 343 HOH   HOH C . 
O 5 HOH   53  253 351 HOH   HOH C . 
O 5 HOH   54  254 62  HOH   HOH C . 
O 5 HOH   55  255 53  HOH   HOH C . 
O 5 HOH   56  256 338 HOH   HOH C . 
O 5 HOH   57  257 198 HOH   HOH C . 
O 5 HOH   58  258 298 HOH   HOH C . 
O 5 HOH   59  259 171 HOH   HOH C . 
O 5 HOH   60  260 287 HOH   HOH C . 
O 5 HOH   61  261 148 HOH   HOH C . 
O 5 HOH   62  262 209 HOH   HOH C . 
O 5 HOH   63  263 330 HOH   HOH C . 
O 5 HOH   64  264 295 HOH   HOH C . 
O 5 HOH   65  265 67  HOH   HOH C . 
O 5 HOH   66  266 376 HOH   HOH C . 
O 5 HOH   67  267 65  HOH   HOH C . 
O 5 HOH   68  268 371 HOH   HOH C . 
O 5 HOH   69  269 305 HOH   HOH C . 
O 5 HOH   70  270 246 HOH   HOH C . 
O 5 HOH   71  271 241 HOH   HOH C . 
O 5 HOH   72  272 378 HOH   HOH C . 
O 5 HOH   73  273 334 HOH   HOH C . 
O 5 HOH   74  274 270 HOH   HOH C . 
O 5 HOH   75  275 70  HOH   HOH C . 
O 5 HOH   76  276 363 HOH   HOH C . 
O 5 HOH   77  277 324 HOH   HOH C . 
O 5 HOH   78  278 339 HOH   HOH C . 
O 5 HOH   79  279 366 HOH   HOH C . 
O 5 HOH   80  280 206 HOH   HOH C . 
O 5 HOH   81  281 310 HOH   HOH C . 
O 5 HOH   82  282 362 HOH   HOH C . 
O 5 HOH   83  283 352 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
4  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
8  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
9  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
10 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
11 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
12 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
13 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
14 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
15 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
16 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
17 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
18 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
19 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
20 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
21 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
22 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
23 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
24 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
25 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
26 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
27 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
28 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
29 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
30 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
31 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
32 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 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           7HGC 
_cell.length_a           41.640 
_cell.length_b           42.100 
_cell.length_c           158.690 
_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                         7HGC 
_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          7HGC 
_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                     7HGC 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             42.10 
_reflns.d_resolution_high            1.51 
_reflns.number_obs                   44735 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.047 
_reflns.pdbx_netI_over_sigmaI        15.1 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.052 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     273905 
_reflns.pdbx_chi_squared             0.95 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.51 
_reflns_shell.d_res_low                   1.55 
_reflns_shell.number_measured_all         16314 
_reflns_shell.number_unique_obs           3234 
_reflns_shell.Rmerge_I_obs                1.533 
_reflns_shell.pdbx_chi_squared            0.84 
_reflns_shell.pdbx_redundancy             5.0 
_reflns_shell.percent_possible_obs        99.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             1.715 
_reflns_shell.pdbx_Rpim_I_all             0.757 
_reflns_shell.pdbx_CC_half                0.347 
_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                                 7HGC 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     42306 
_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                             40.73 
_refine.ls_d_res_high                            1.51 
_refine.ls_percent_reflns_obs                    99.59 
_refine.ls_R_factor_obs                          0.20744 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20507 
_refine.ls_R_factor_R_free                       0.24984 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  2371 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_refine.B_iso_mean                               37.525 
_refine.aniso_B[1][1]                            0.23 
_refine.aniso_B[2][2]                            0.10 
_refine.aniso_B[3][3]                            -0.33 
_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                       0.088 
_refine.pdbx_overall_ESU_R_Free                  0.093 
_refine.overall_SU_ML                            0.078 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.211 
_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        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.number_atoms_solvent             278 
_refine_hist.number_atoms_total               2478 
_refine_hist.d_res_high                       1.51 
_refine_hist.d_res_low                        40.73 
# 
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             0.010  0.012  ? 2303 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.895  1.831  ? 3132 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.097  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.797  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.498 10.000 ? 304  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.129  0.200  ? 288  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 1932 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.422  3.466  ? 1076 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.714  6.197  ? 1339 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.515  3.791  ? 1227 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.418  54.07  ? 3561 '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                       1.510 
_refine_ls_shell.d_res_low                        1.549 
_refine_ls_shell.number_reflns_R_work             3050 
_refine_ls_shell.R_factor_R_work                  0.344 
_refine_ls_shell.percent_reflns_obs               99.14 
_refine_ls_shell.R_factor_R_free                  0.340 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             174 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGC 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1428159350' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGC 
_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 7HGC A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGC B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGC 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 7HGC GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGC SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGC GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGC SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGC GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGC 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 TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 255 ? ? O C HOH 212 ? ? 1.49 
2  1 O   B HOH 237 ? ? O B HOH 258 ? ? 1.62 
3  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 1.84 
4  1 O   C HOH 205 ? ? O C HOH 274 ? ? 1.87 
5  1 O   B HOH 204 ? ? O B HOH 267 ? ? 1.93 
6  1 O   A HOH 206 ? ? O A HOH 295 ? ? 1.95 
7  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 1.97 
8  1 OD1 C ASP 9   ? ? O C HOH 202 ? ? 2.05 
9  1 CE  A LYS 39  ? ? O A HOH 287 ? ? 2.08 
10 1 O2  C SO4 102 ? ? O C HOH 203 ? ? 2.09 
11 1 OH  C TYR 40  ? ? O C HOH 204 ? ? 2.09 
12 1 O   B HOH 208 ? ? O B HOH 240 ? ? 2.13 
13 1 OE1 C GLN 85  ? ? O C HOH 205 ? ? 2.14 
14 1 OE1 A GLN 85  ? ? O A HOH 202 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 235 ? ? 1_555 O C HOH 276 ? ? 4_435 1.79 
2 1 O B HOH 249 ? ? 1_555 O C HOH 225 ? ? 2_644 2.10 
3 1 O A HOH 273 ? ? 1_555 O A HOH 280 ? ? 4_545 2.12 
4 1 O A HOH 249 ? ? 1_555 O C HOH 273 ? ? 4_445 2.13 
5 1 O A HOH 256 ? ? 1_555 O C HOH 252 ? ? 4_435 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -159.67 66.64 
2 1 ASN B 38 ? ? 78.54   -2.68 
3 1 ASN B 87 ? ? -161.41 61.92 
4 1 ASN C 87 ? ? -156.94 51.65 
# 
_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   A 
_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   A 
_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            149.20 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.100 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 ILE 28 ? B ILE 29 
4  1 Y 1 B ALA 29 ? B ALA 30 
5  1 Y 1 B ASP 30 ? B ASP 31 
6  1 Y 1 B GLY 31 ? B GLY 32 
7  1 Y 1 B ALA 32 ? B ALA 33 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C ASP 27 ? C ASP 28 
12 1 Y 1 C ILE 28 ? C ILE 29 
13 1 Y 1 C ALA 29 ? C ALA 30 
14 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 
A1AJ5 N1   N Y N 1   
A1AJ5 N3   N Y N 2   
A1AJ5 C4   C Y N 3   
A1AJ5 C5   C Y N 4   
A1AJ5 C6   C Y N 5   
A1AJ5 C7   C Y N 6   
A1AJ5 C8   C Y N 7   
A1AJ5 N    N N N 8   
A1AJ5 C1   C N S 9   
A1AJ5 C    C N N 10  
A1AJ5 C2   C Y N 11  
A1AJ5 N2   N Y N 12  
A1AJ5 C3   C Y N 13  
A1AJ5 C9   C Y N 14  
A1AJ5 H7   H N N 15  
A1AJ5 H8   H N N 16  
A1AJ5 H9   H N N 17  
A1AJ5 H10  H N N 18  
A1AJ5 H4   H N N 19  
A1AJ5 H12  H N N 20  
A1AJ5 H3   H N N 21  
A1AJ5 H2   H N N 22  
A1AJ5 H    H N N 23  
A1AJ5 H1   H N N 24  
A1AJ5 H6   H N N 25  
A1AJ5 H11  H N N 26  
ALA   N    N N N 27  
ALA   CA   C N S 28  
ALA   C    C N N 29  
ALA   O    O N N 30  
ALA   CB   C N N 31  
ALA   OXT  O N N 32  
ALA   H    H N N 33  
ALA   H2   H N N 34  
ALA   HA   H N N 35  
ALA   HB1  H N N 36  
ALA   HB2  H N N 37  
ALA   HB3  H N N 38  
ALA   HXT  H N N 39  
ARG   N    N N N 40  
ARG   CA   C N S 41  
ARG   C    C N N 42  
ARG   O    O N N 43  
ARG   CB   C N N 44  
ARG   CG   C N N 45  
ARG   CD   C N N 46  
ARG   NE   N N N 47  
ARG   CZ   C N N 48  
ARG   NH1  N N N 49  
ARG   NH2  N N N 50  
ARG   OXT  O N N 51  
ARG   H    H N N 52  
ARG   H2   H N N 53  
ARG   HA   H N N 54  
ARG   HB2  H N N 55  
ARG   HB3  H N N 56  
ARG   HG2  H N N 57  
ARG   HG3  H N N 58  
ARG   HD2  H N N 59  
ARG   HD3  H N N 60  
ARG   HE   H N N 61  
ARG   HH11 H N N 62  
ARG   HH12 H N N 63  
ARG   HH21 H N N 64  
ARG   HH22 H N N 65  
ARG   HXT  H N N 66  
ASN   N    N N N 67  
ASN   CA   C N S 68  
ASN   C    C N N 69  
ASN   O    O N N 70  
ASN   CB   C N N 71  
ASN   CG   C N N 72  
ASN   OD1  O N N 73  
ASN   ND2  N N N 74  
ASN   OXT  O N N 75  
ASN   H    H N N 76  
ASN   H2   H N N 77  
ASN   HA   H N N 78  
ASN   HB2  H N N 79  
ASN   HB3  H N N 80  
ASN   HD21 H N N 81  
ASN   HD22 H N N 82  
ASN   HXT  H N N 83  
ASP   N    N N N 84  
ASP   CA   C N S 85  
ASP   C    C N N 86  
ASP   O    O N N 87  
ASP   CB   C N N 88  
ASP   CG   C N N 89  
ASP   OD1  O N N 90  
ASP   OD2  O N N 91  
ASP   OXT  O N N 92  
ASP   H    H N N 93  
ASP   H2   H N N 94  
ASP   HA   H N N 95  
ASP   HB2  H N N 96  
ASP   HB3  H N N 97  
ASP   HD2  H N N 98  
ASP   HXT  H N N 99  
CYS   N    N N N 100 
CYS   CA   C N R 101 
CYS   C    C N N 102 
CYS   O    O N N 103 
CYS   CB   C N N 104 
CYS   SG   S N N 105 
CYS   OXT  O N N 106 
CYS   H    H N N 107 
CYS   H2   H N N 108 
CYS   HA   H N N 109 
CYS   HB2  H N N 110 
CYS   HB3  H N N 111 
CYS   HG   H N N 112 
CYS   HXT  H N N 113 
EDO   C1   C N N 114 
EDO   O1   O N N 115 
EDO   C2   C N N 116 
EDO   O2   O N N 117 
EDO   H11  H N N 118 
EDO   H12  H N N 119 
EDO   HO1  H N N 120 
EDO   H21  H N N 121 
EDO   H22  H N N 122 
EDO   HO2  H N N 123 
GLN   N    N N N 124 
GLN   CA   C N S 125 
GLN   C    C N N 126 
GLN   O    O N N 127 
GLN   CB   C N N 128 
GLN   CG   C N N 129 
GLN   CD   C N N 130 
GLN   OE1  O N N 131 
GLN   NE2  N N N 132 
GLN   OXT  O N N 133 
GLN   H    H N N 134 
GLN   H2   H N N 135 
GLN   HA   H N N 136 
GLN   HB2  H N N 137 
GLN   HB3  H N N 138 
GLN   HG2  H N N 139 
GLN   HG3  H N N 140 
GLN   HE21 H N N 141 
GLN   HE22 H N N 142 
GLN   HXT  H N N 143 
GLU   N    N N N 144 
GLU   CA   C N S 145 
GLU   C    C N N 146 
GLU   O    O N N 147 
GLU   CB   C N N 148 
GLU   CG   C N N 149 
GLU   CD   C N N 150 
GLU   OE1  O N N 151 
GLU   OE2  O N N 152 
GLU   OXT  O N N 153 
GLU   H    H N N 154 
GLU   H2   H N N 155 
GLU   HA   H N N 156 
GLU   HB2  H N N 157 
GLU   HB3  H N N 158 
GLU   HG2  H N N 159 
GLU   HG3  H N N 160 
GLU   HE2  H N N 161 
GLU   HXT  H N N 162 
GLY   N    N N N 163 
GLY   CA   C N N 164 
GLY   C    C N N 165 
GLY   O    O N N 166 
GLY   OXT  O N N 167 
GLY   H    H N N 168 
GLY   H2   H N N 169 
GLY   HA2  H N N 170 
GLY   HA3  H N N 171 
GLY   HXT  H N N 172 
HIS   N    N N N 173 
HIS   CA   C N S 174 
HIS   C    C N N 175 
HIS   O    O N N 176 
HIS   CB   C N N 177 
HIS   CG   C Y N 178 
HIS   ND1  N Y N 179 
HIS   CD2  C Y N 180 
HIS   CE1  C Y N 181 
HIS   NE2  N Y N 182 
HIS   OXT  O N N 183 
HIS   H    H N N 184 
HIS   H2   H N N 185 
HIS   HA   H N N 186 
HIS   HB2  H N N 187 
HIS   HB3  H N N 188 
HIS   HD1  H N N 189 
HIS   HD2  H N N 190 
HIS   HE1  H N N 191 
HIS   HE2  H N N 192 
HIS   HXT  H N N 193 
HOH   O    O N N 194 
HOH   H1   H N N 195 
HOH   H2   H N N 196 
ILE   N    N N N 197 
ILE   CA   C N S 198 
ILE   C    C N N 199 
ILE   O    O N N 200 
ILE   CB   C N S 201 
ILE   CG1  C N N 202 
ILE   CG2  C N N 203 
ILE   CD1  C N N 204 
ILE   OXT  O N N 205 
ILE   H    H N N 206 
ILE   H2   H N N 207 
ILE   HA   H N N 208 
ILE   HB   H N N 209 
ILE   HG12 H N N 210 
ILE   HG13 H N N 211 
ILE   HG21 H N N 212 
ILE   HG22 H N N 213 
ILE   HG23 H N N 214 
ILE   HD11 H N N 215 
ILE   HD12 H N N 216 
ILE   HD13 H N N 217 
ILE   HXT  H N N 218 
LEU   N    N N N 219 
LEU   CA   C N S 220 
LEU   C    C N N 221 
LEU   O    O N N 222 
LEU   CB   C N N 223 
LEU   CG   C N N 224 
LEU   CD1  C N N 225 
LEU   CD2  C N N 226 
LEU   OXT  O N N 227 
LEU   H    H N N 228 
LEU   H2   H N N 229 
LEU   HA   H N N 230 
LEU   HB2  H N N 231 
LEU   HB3  H N N 232 
LEU   HG   H N N 233 
LEU   HD11 H N N 234 
LEU   HD12 H N N 235 
LEU   HD13 H N N 236 
LEU   HD21 H N N 237 
LEU   HD22 H N N 238 
LEU   HD23 H N N 239 
LEU   HXT  H N N 240 
LYS   N    N N N 241 
LYS   CA   C N S 242 
LYS   C    C N N 243 
LYS   O    O N N 244 
LYS   CB   C N N 245 
LYS   CG   C N N 246 
LYS   CD   C N N 247 
LYS   CE   C N N 248 
LYS   NZ   N N N 249 
LYS   OXT  O N N 250 
LYS   H    H N N 251 
LYS   H2   H N N 252 
LYS   HA   H N N 253 
LYS   HB2  H N N 254 
LYS   HB3  H N N 255 
LYS   HG2  H N N 256 
LYS   HG3  H N N 257 
LYS   HD2  H N N 258 
LYS   HD3  H N N 259 
LYS   HE2  H N N 260 
LYS   HE3  H N N 261 
LYS   HZ1  H N N 262 
LYS   HZ2  H N N 263 
LYS   HZ3  H N N 264 
LYS   HXT  H N N 265 
MET   N    N N N 266 
MET   CA   C N S 267 
MET   C    C N N 268 
MET   O    O N N 269 
MET   CB   C N N 270 
MET   CG   C N N 271 
MET   SD   S N N 272 
MET   CE   C N N 273 
MET   OXT  O N N 274 
MET   H    H N N 275 
MET   H2   H N N 276 
MET   HA   H N N 277 
MET   HB2  H N N 278 
MET   HB3  H N N 279 
MET   HG2  H N N 280 
MET   HG3  H N N 281 
MET   HE1  H N N 282 
MET   HE2  H N N 283 
MET   HE3  H N N 284 
MET   HXT  H N N 285 
PHE   N    N N N 286 
PHE   CA   C N S 287 
PHE   C    C N N 288 
PHE   O    O N N 289 
PHE   CB   C N N 290 
PHE   CG   C Y N 291 
PHE   CD1  C Y N 292 
PHE   CD2  C Y N 293 
PHE   CE1  C Y N 294 
PHE   CE2  C Y N 295 
PHE   CZ   C Y N 296 
PHE   OXT  O N N 297 
PHE   H    H N N 298 
PHE   H2   H N N 299 
PHE   HA   H N N 300 
PHE   HB2  H N N 301 
PHE   HB3  H N N 302 
PHE   HD1  H N N 303 
PHE   HD2  H N N 304 
PHE   HE1  H N N 305 
PHE   HE2  H N N 306 
PHE   HZ   H N N 307 
PHE   HXT  H N N 308 
PRO   N    N N N 309 
PRO   CA   C N S 310 
PRO   C    C N N 311 
PRO   O    O N N 312 
PRO   CB   C N N 313 
PRO   CG   C N N 314 
PRO   CD   C N N 315 
PRO   OXT  O N N 316 
PRO   H    H N N 317 
PRO   HA   H N N 318 
PRO   HB2  H N N 319 
PRO   HB3  H N N 320 
PRO   HG2  H N N 321 
PRO   HG3  H N N 322 
PRO   HD2  H N N 323 
PRO   HD3  H N N 324 
PRO   HXT  H N N 325 
SER   N    N N N 326 
SER   CA   C N S 327 
SER   C    C N N 328 
SER   O    O N N 329 
SER   CB   C N N 330 
SER   OG   O N N 331 
SER   OXT  O N N 332 
SER   H    H N N 333 
SER   H2   H N N 334 
SER   HA   H N N 335 
SER   HB2  H N N 336 
SER   HB3  H N N 337 
SER   HG   H N N 338 
SER   HXT  H N N 339 
SO4   S    S N N 340 
SO4   O1   O N N 341 
SO4   O2   O N N 342 
SO4   O3   O N N 343 
SO4   O4   O N N 344 
THR   N    N N N 345 
THR   CA   C N S 346 
THR   C    C N N 347 
THR   O    O N N 348 
THR   CB   C N R 349 
THR   OG1  O N N 350 
THR   CG2  C N N 351 
THR   OXT  O N N 352 
THR   H    H N N 353 
THR   H2   H N N 354 
THR   HA   H N N 355 
THR   HB   H N N 356 
THR   HG1  H N N 357 
THR   HG21 H N N 358 
THR   HG22 H N N 359 
THR   HG23 H N N 360 
THR   HXT  H N N 361 
TRP   N    N N N 362 
TRP   CA   C N S 363 
TRP   C    C N N 364 
TRP   O    O N N 365 
TRP   CB   C N N 366 
TRP   CG   C Y N 367 
TRP   CD1  C Y N 368 
TRP   CD2  C Y N 369 
TRP   NE1  N Y N 370 
TRP   CE2  C Y N 371 
TRP   CE3  C Y N 372 
TRP   CZ2  C Y N 373 
TRP   CZ3  C Y N 374 
TRP   CH2  C Y N 375 
TRP   OXT  O N N 376 
TRP   H    H N N 377 
TRP   H2   H N N 378 
TRP   HA   H N N 379 
TRP   HB2  H N N 380 
TRP   HB3  H N N 381 
TRP   HD1  H N N 382 
TRP   HE1  H N N 383 
TRP   HE3  H N N 384 
TRP   HZ2  H N N 385 
TRP   HZ3  H N N 386 
TRP   HH2  H N N 387 
TRP   HXT  H N N 388 
TYR   N    N N N 389 
TYR   CA   C N S 390 
TYR   C    C N N 391 
TYR   O    O N N 392 
TYR   CB   C N N 393 
TYR   CG   C Y N 394 
TYR   CD1  C Y N 395 
TYR   CD2  C Y N 396 
TYR   CE1  C Y N 397 
TYR   CE2  C Y N 398 
TYR   CZ   C Y N 399 
TYR   OH   O N N 400 
TYR   OXT  O N N 401 
TYR   H    H N N 402 
TYR   H2   H N N 403 
TYR   HA   H N N 404 
TYR   HB2  H N N 405 
TYR   HB3  H N N 406 
TYR   HD1  H N N 407 
TYR   HD2  H N N 408 
TYR   HE1  H N N 409 
TYR   HE2  H N N 410 
TYR   HH   H N N 411 
TYR   HXT  H N N 412 
VAL   N    N N N 413 
VAL   CA   C N S 414 
VAL   C    C N N 415 
VAL   O    O N N 416 
VAL   CB   C N N 417 
VAL   CG1  C N N 418 
VAL   CG2  C N N 419 
VAL   OXT  O N N 420 
VAL   H    H N N 421 
VAL   H2   H N N 422 
VAL   HA   H N N 423 
VAL   HB   H N N 424 
VAL   HG11 H N N 425 
VAL   HG12 H N N 426 
VAL   HG13 H N N 427 
VAL   HG21 H N N 428 
VAL   HG22 H N N 429 
VAL   HG23 H N N 430 
VAL   HXT  H N N 431 
# 
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 
A1AJ5 C   C1   sing N N 1   
A1AJ5 C1  N    sing N N 2   
A1AJ5 C2  C1   sing N N 3   
A1AJ5 C2  C3   doub Y N 4   
A1AJ5 C3  N1   sing Y N 5   
A1AJ5 N1  N2   sing Y N 6   
A1AJ5 N2  N3   doub Y N 7   
A1AJ5 N3  C2   sing Y N 8   
A1AJ5 C4  N1   sing N N 9   
A1AJ5 C4  C5   doub Y N 10  
A1AJ5 C5  C6   sing Y N 11  
A1AJ5 C6  C7   doub Y N 12  
A1AJ5 C7  C8   sing Y N 13  
A1AJ5 C8  C9   doub Y N 14  
A1AJ5 C9  C4   sing Y N 15  
A1AJ5 C5  H7   sing N N 16  
A1AJ5 C6  H8   sing N N 17  
A1AJ5 C7  H9   sing N N 18  
A1AJ5 C8  H10  sing N N 19  
A1AJ5 N   H4   sing N N 20  
A1AJ5 N   H12  sing N N 21  
A1AJ5 C1  H3   sing N N 22  
A1AJ5 C   H2   sing N N 23  
A1AJ5 C   H    sing N N 24  
A1AJ5 C   H1   sing N N 25  
A1AJ5 C3  H6   sing N N 26  
A1AJ5 C9  H11  sing N N 27  
ALA   N   CA   sing N N 28  
ALA   N   H    sing N N 29  
ALA   N   H2   sing N N 30  
ALA   CA  C    sing N N 31  
ALA   CA  CB   sing N N 32  
ALA   CA  HA   sing N N 33  
ALA   C   O    doub N N 34  
ALA   C   OXT  sing N N 35  
ALA   CB  HB1  sing N N 36  
ALA   CB  HB2  sing N N 37  
ALA   CB  HB3  sing N N 38  
ALA   OXT HXT  sing N N 39  
ARG   N   CA   sing N N 40  
ARG   N   H    sing N N 41  
ARG   N   H2   sing N N 42  
ARG   CA  C    sing N N 43  
ARG   CA  CB   sing N N 44  
ARG   CA  HA   sing N N 45  
ARG   C   O    doub N N 46  
ARG   C   OXT  sing N N 47  
ARG   CB  CG   sing N N 48  
ARG   CB  HB2  sing N N 49  
ARG   CB  HB3  sing N N 50  
ARG   CG  CD   sing N N 51  
ARG   CG  HG2  sing N N 52  
ARG   CG  HG3  sing N N 53  
ARG   CD  NE   sing N N 54  
ARG   CD  HD2  sing N N 55  
ARG   CD  HD3  sing N N 56  
ARG   NE  CZ   sing N N 57  
ARG   NE  HE   sing N N 58  
ARG   CZ  NH1  sing N N 59  
ARG   CZ  NH2  doub N N 60  
ARG   NH1 HH11 sing N N 61  
ARG   NH1 HH12 sing N N 62  
ARG   NH2 HH21 sing N N 63  
ARG   NH2 HH22 sing N N 64  
ARG   OXT HXT  sing N N 65  
ASN   N   CA   sing N N 66  
ASN   N   H    sing N N 67  
ASN   N   H2   sing N N 68  
ASN   CA  C    sing N N 69  
ASN   CA  CB   sing N N 70  
ASN   CA  HA   sing N N 71  
ASN   C   O    doub N N 72  
ASN   C   OXT  sing N N 73  
ASN   CB  CG   sing N N 74  
ASN   CB  HB2  sing N N 75  
ASN   CB  HB3  sing N N 76  
ASN   CG  OD1  doub N N 77  
ASN   CG  ND2  sing N N 78  
ASN   ND2 HD21 sing N N 79  
ASN   ND2 HD22 sing N N 80  
ASN   OXT HXT  sing N N 81  
ASP   N   CA   sing N N 82  
ASP   N   H    sing N N 83  
ASP   N   H2   sing N N 84  
ASP   CA  C    sing N N 85  
ASP   CA  CB   sing N N 86  
ASP   CA  HA   sing N N 87  
ASP   C   O    doub N N 88  
ASP   C   OXT  sing N N 89  
ASP   CB  CG   sing N N 90  
ASP   CB  HB2  sing N N 91  
ASP   CB  HB3  sing N N 92  
ASP   CG  OD1  doub N N 93  
ASP   CG  OD2  sing N N 94  
ASP   OD2 HD2  sing N N 95  
ASP   OXT HXT  sing N N 96  
CYS   N   CA   sing N N 97  
CYS   N   H    sing N N 98  
CYS   N   H2   sing N N 99  
CYS   CA  C    sing N N 100 
CYS   CA  CB   sing N N 101 
CYS   CA  HA   sing N N 102 
CYS   C   O    doub N N 103 
CYS   C   OXT  sing N N 104 
CYS   CB  SG   sing N N 105 
CYS   CB  HB2  sing N N 106 
CYS   CB  HB3  sing N N 107 
CYS   SG  HG   sing N N 108 
CYS   OXT HXT  sing N N 109 
EDO   C1  O1   sing N N 110 
EDO   C1  C2   sing N N 111 
EDO   C1  H11  sing N N 112 
EDO   C1  H12  sing N N 113 
EDO   O1  HO1  sing N N 114 
EDO   C2  O2   sing N N 115 
EDO   C2  H21  sing N N 116 
EDO   C2  H22  sing N N 117 
EDO   O2  HO2  sing N N 118 
GLN   N   CA   sing N N 119 
GLN   N   H    sing N N 120 
GLN   N   H2   sing N N 121 
GLN   CA  C    sing N N 122 
GLN   CA  CB   sing N N 123 
GLN   CA  HA   sing N N 124 
GLN   C   O    doub N N 125 
GLN   C   OXT  sing N N 126 
GLN   CB  CG   sing N N 127 
GLN   CB  HB2  sing N N 128 
GLN   CB  HB3  sing N N 129 
GLN   CG  CD   sing N N 130 
GLN   CG  HG2  sing N N 131 
GLN   CG  HG3  sing N N 132 
GLN   CD  OE1  doub N N 133 
GLN   CD  NE2  sing N N 134 
GLN   NE2 HE21 sing N N 135 
GLN   NE2 HE22 sing N N 136 
GLN   OXT HXT  sing N N 137 
GLU   N   CA   sing N N 138 
GLU   N   H    sing N N 139 
GLU   N   H2   sing N N 140 
GLU   CA  C    sing N N 141 
GLU   CA  CB   sing N N 142 
GLU   CA  HA   sing N N 143 
GLU   C   O    doub N N 144 
GLU   C   OXT  sing N N 145 
GLU   CB  CG   sing N N 146 
GLU   CB  HB2  sing N N 147 
GLU   CB  HB3  sing N N 148 
GLU   CG  CD   sing N N 149 
GLU   CG  HG2  sing N N 150 
GLU   CG  HG3  sing N N 151 
GLU   CD  OE1  doub N N 152 
GLU   CD  OE2  sing N N 153 
GLU   OE2 HE2  sing N N 154 
GLU   OXT HXT  sing N N 155 
GLY   N   CA   sing N N 156 
GLY   N   H    sing N N 157 
GLY   N   H2   sing N N 158 
GLY   CA  C    sing N N 159 
GLY   CA  HA2  sing N N 160 
GLY   CA  HA3  sing N N 161 
GLY   C   O    doub N N 162 
GLY   C   OXT  sing N N 163 
GLY   OXT HXT  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
SO4   S   O1   doub N N 326 
SO4   S   O2   doub N N 327 
SO4   S   O3   sing N N 328 
SO4   S   O4   sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HGC 
_atom_sites.fract_transf_matrix[1][1]   0.024015 
_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]   0.023753 
_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]   0.006302 
_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  ? 0.873   4.200   2.492   1.00 49.66  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.214  3.455   1.802   1.00 55.03  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.360   2.400   0.854   1.00 49.04  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.452   2.564   0.301   1.00 48.42  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.190  4.406   1.098   1.00 58.16  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.136  5.136   2.048   1.00 63.80  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.436  4.207   2.903   1.00 60.12  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -4.163  5.471   3.958   1.00 67.13  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.346  1.257   0.688   1.00 39.43  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.074   0.160   -0.192  1.00 37.36  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.295   0.556   -1.655  1.00 36.10  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.419  1.376   -2.221  1.00 37.51  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.176  -0.792  -0.048  1.00 36.82  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.638  -0.559  1.388   1.00 41.75  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.606  0.952   1.398   1.00 37.69  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.266   -0.094  -2.290  1.00 34.48  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.456   0.054   -3.714  1.00 35.27  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.914   -1.230  -4.335  1.00 30.70  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.426   -2.125  -3.628  1.00 31.82  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.959   0.192   -4.007  1.00 39.13  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.592   1.487   -3.567  1.00 54.58  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.837   1.810   -2.248  1.00 60.81  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.041   2.539   -4.280  1.00 61.08  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.390   3.016   -2.174  1.00 63.69  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.535   3.473   -3.395  1.00 58.17  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.932   -1.329  -5.652  1.00 27.78  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.698   -2.627  -6.252  1.00 26.57  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.833   -3.591  -5.910  1.00 26.98  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.947   -3.207  -5.494  1.00 28.26  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.596   -2.448  -7.760  1.00 30.05  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.517   -4.877  -6.051  1.00 25.69  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.511   -5.923  -5.872  1.00 24.17  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.660   -5.733  -6.863  1.00 25.80  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.452   -5.361  -8.023  1.00 29.18  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.999   -7.360  -5.987  1.00 25.24  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.213   -7.706  -4.732  1.00 26.10  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.893   -7.959  -3.536  1.00 23.67  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.175  -7.896  -4.796  1.00 24.45  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.183   -8.277  -2.359  1.00 22.28  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.856  -8.254  -3.628  1.00 23.61  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.202  -8.419  -2.431  1.00 24.97  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.891   -5.963  -6.357  1.00 22.36  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.043   -5.908  -7.255  1.00 24.51  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.975   -7.090  -6.966  1.00 24.37  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.954   -7.718  -5.905  1.00 22.01  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.801   -4.594  -7.013  1.00 27.28  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.405   -4.524  -5.634  1.00 29.11  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 7.906   -3.111  -5.298  1.00 34.67  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.603   -3.038  -3.964  1.00 35.96  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.679   -3.241  -2.850  1.00 36.61  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.871   -7.452  -7.902  1.00 24.54  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.805   -8.547  -7.653  1.00 24.41  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.621   -8.288  -6.385  1.00 21.89  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.071  -7.180  -6.098  1.00 24.20  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.704   -8.559  -8.932  1.00 25.70  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.796   -7.915  -10.004 1.00 30.13  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 8.020   -6.823  -9.238  1.00 26.61  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.774   -9.355  -5.589  1.00 22.29  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.484  -9.287  -4.325  1.00 19.54  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.537   -9.176  -3.133  1.00 22.74  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.928   -9.461  -1.997  1.00 23.62  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.310   -8.729  -3.377  1.00 20.17  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.399   -8.724  -2.234  1.00 19.60  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.164   -10.123 -1.633  1.00 17.91  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.013   -11.097 -2.350  1.00 20.34  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.049   -8.160  -2.668  1.00 20.46  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.054   -6.647  -2.862  1.00 21.98  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.992   -5.935  -2.372  1.00 25.01  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.059   -6.126  -3.460  1.00 25.03  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.026   -10.168 -0.286  1.00 20.08  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.843   -11.439 0.430   1.00 18.72  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.364   -11.527 0.845   1.00 18.70  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.788   -10.521 1.276   1.00 22.09  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.795   -11.482 1.646   1.00 19.98  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.275   -11.246 1.267   1.00 20.12  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.134  -11.364 2.540   1.00 23.15  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.694   -12.269 0.261   1.00 21.47  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.821   -12.737 0.684   1.00 19.33  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.384   -12.930 0.894   1.00 19.04  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.153   -14.297 1.511   1.00 21.37  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.016   -15.153 1.564   1.00 20.76  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.575   -12.843 -0.411  1.00 19.52  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.711   -11.444 -1.006  1.00 22.98  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.990   -13.893 -1.444  1.00 21.13  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.932   -14.497 2.060   1.00 19.73  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.370   -15.832 2.053   1.00 19.97  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.400   -15.903 0.873   1.00 22.47  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.404  -14.964 0.671   1.00 23.02  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.595   -16.182 3.352   1.00 21.45  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.551   -16.260 4.529   1.00 20.07  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.871   -15.101 5.228   1.00 22.94  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.046   -17.500 4.942   1.00 22.97  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.788   -15.211 6.281   1.00 26.13  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.977   -17.596 5.993   1.00 25.68  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.315   -16.451 6.658   1.00 26.41  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.527   -16.989 0.084   1.00 21.34  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.287  -17.099 -1.126  1.00 22.02  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.256  -18.272 -0.941  1.00 24.77  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.879  -19.332 -0.430  1.00 23.90  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.628   -17.341 -2.323  1.00 21.59  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.526  -18.075 -1.353  1.00 24.47  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.515  -19.115 -1.125  1.00 25.56  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.855  -19.828 -2.431  1.00 27.22  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.248  -19.177 -3.391  1.00 29.79  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.740  -18.486 -0.447  1.00 26.31  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.849  -19.527 -0.094  1.00 31.74  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.370  -20.427 1.055   1.00 33.84  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.480  -21.198 1.751   1.00 37.72  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.991  -22.173 0.776   1.00 36.53  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.829  -21.172 -2.335  1.00 26.15  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.222  -22.076 -3.408  1.00 32.28  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.322  -22.939 -2.808  1.00 34.97  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.278  -23.233 -1.627  1.00 29.48  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.067  -23.036 -3.728  1.00 35.30  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -1.755  -22.377 -4.154  1.00 35.68  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.919  -21.818 -5.861  1.00 36.31  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.449  -23.305 -6.680  1.00 33.39  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.307  -23.304 -3.633  1.00 42.35  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.395  -24.167 -3.197  1.00 42.40  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.809  -25.432 -2.592  1.00 34.70  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.885  -26.027 -3.143  1.00 36.59  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.187  -24.576 -4.443  1.00 46.40  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.517  -25.278 -4.134  1.00 52.34  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.467 -24.432 -3.280  1.00 56.06  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.312  -25.822 -1.403  1.00 38.28  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -6.917  -27.105 -0.853  1.00 36.50  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -5.568  -27.050 -0.148  1.00 40.57  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -5.097  -28.049 0.381   1.00 44.18  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -4.928  -25.869 -0.156  1.00 32.81  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -3.686  -25.766 0.573   1.00 33.13  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -3.785  -24.643 1.583   1.00 30.01  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -4.520  -23.660 1.381   1.00 31.16  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.576  -25.337 -0.390  1.00 34.17  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -2.150  -26.330 -1.463  1.00 35.82  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -0.995  -27.087 -1.290  1.00 47.04  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -2.824  -26.411 -2.681  1.00 37.88  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -0.553  -27.957 -2.278  1.00 47.41  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -2.389  -27.278 -3.683  1.00 43.85  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -1.247  -28.040 -3.473  1.00 51.42  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -0.794  -28.908 -4.433  1.00 71.89  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -2.991  -24.721 2.666   1.00 30.76  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -2.956  -23.645 3.662   1.00 29.69  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.292  -22.415 3.009   1.00 27.55  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -1.529  -22.586 2.055   1.00 28.15  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -2.115  -24.236 4.812   1.00 33.53  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.282  -25.330 4.158   1.00 33.12  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -2.057  -25.825 2.966   1.00 34.02  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -2.540  -21.248 3.576   1.00 26.45  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -1.873  -20.024 3.123   1.00 23.70  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.361  -20.270 3.224   1.00 26.96  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? 0.115   -20.684 4.289   1.00 25.68  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.313  -18.828 3.966   1.00 23.41  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -3.772  -18.419 3.819   1.00 25.48  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -4.826  -19.067 4.456   1.00 32.55  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.323  -17.400 3.102   1.00 25.60  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -5.984  -18.461 4.119   1.00 30.51  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -5.713  -17.447 3.294   1.00 30.47  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? 0.397   -20.011 2.128   1.00 24.05  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.713   -20.649 1.974   1.00 23.93  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.766   -19.560 1.838   1.00 23.35  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.584   -18.642 1.066   1.00 23.46  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.757   -21.510 0.709   1.00 24.05  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 2.835   -22.565 0.767   1.00 24.71  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 4.180   -22.393 0.567   1.00 26.61  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.636   -23.960 1.095   1.00 28.18  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 4.830   -23.603 0.709   1.00 26.01  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 3.908   -24.577 1.038   1.00 29.36  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.508   -24.739 1.405   1.00 29.31  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 4.097   -25.941 1.299   1.00 32.65  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.701   -26.091 1.663   1.00 30.33  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 2.974   -26.683 1.599   1.00 32.86  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 3.901   -19.624 2.585   1.00 23.24  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 4.935   -18.591 2.417   1.00 22.48  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.474   -18.551 0.979   1.00 20.27  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 5.808   -19.575 0.374   1.00 22.18  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 5.982   -19.047 3.467   1.00 22.35  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 5.811   -20.531 3.554   1.00 21.05  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 4.228   -20.659 3.572   1.00 22.00  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.543   -17.347 0.405   1.00 18.37  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 5.872   -17.226 -1.012  1.00 18.44  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.387   -15.816 -1.306  1.00 18.61  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.396   -14.920 -0.458  1.00 19.14  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.619   -17.555 -1.893  1.00 19.74  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 6.912   -15.654 -2.538  1.00 18.68  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 7.284   -14.326 -2.992  1.00 18.30  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 6.742   -14.041 -4.387  1.00 18.80  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.501   -15.010 -5.136  1.00 21.01  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 8.825   -14.178 -2.973  1.00 19.80  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.563   -15.083 -3.951  1.00 21.00  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 11.072  -14.850 -3.807  1.00 22.05  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 11.788  -15.639 -4.833  1.00 23.58  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 13.049  -16.094 -4.729  1.00 23.64  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.752  -15.939 -3.613  1.00 23.02  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.578  -16.702 -5.788  1.00 25.85  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.642   -12.746 -4.708  1.00 20.76  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.436   -12.355 -6.116  1.00 20.07  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 7.769   -12.475 -6.834  1.00 23.06  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.729   -11.817 -6.443  1.00 24.25  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 5.954   -10.905 -6.231  1.00 21.06  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 4.741   -10.609 -5.273  1.00 27.35  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.591   -10.623 -7.708  1.00 24.00  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.484   -11.390 -5.549  1.00 32.84  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 7.809   -13.302 -7.866  1.00 23.53  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 9.026   -13.467 -8.658  1.00 24.59  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 9.117   -12.444 -9.775  1.00 27.80  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 8.153   -11.829 -10.234 1.00 27.17  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 9.152   -14.844 -9.259  1.00 25.19  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 10.129  -15.776 -8.578  1.00 26.49  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.718  -15.366 -7.539  1.00 30.89  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 10.235  -16.931 -9.007  1.00 28.63  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.374  -12.290 -10.254 1.00 29.71  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.638  -11.613 -11.501 1.00 35.71  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.370  -12.621 -12.618 1.00 30.22  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.211  -13.819 -12.387 1.00 32.92  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 12.111  -11.224 -11.606 1.00 39.86  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.601  -10.008 -10.823 1.00 47.04  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 12.262  -8.862  -11.214 1.00 48.26  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 13.367  -10.218 -9.859  1.00 52.41  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 10.283  -12.104 -13.829 1.00 40.24  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 10.210  -12.955 -15.010 1.00 36.38  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.512  -12.646 -15.746 1.00 30.13  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 11.737  -11.477 -16.030 1.00 35.78  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 9.013   -12.504 -15.855 1.00 39.27  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.661   -12.584 -15.092 1.00 39.20  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 8.979   -13.291 -17.171 1.00 34.90  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.651   -11.558 -15.575 1.00 40.27  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 12.343  -13.672 -15.899 1.00 38.06  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.627  -13.564 -16.577 1.00 35.69  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.352  -13.316 -18.064 1.00 37.03  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.286  -13.658 -18.593 1.00 35.44  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.423  -14.824 -16.363 1.00 38.53  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.263  -12.578 -18.708 1.00 35.14  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.256  -12.538 -20.161 1.00 31.56  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 14.078  -13.954 -20.703 1.00 29.58  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 14.785  -14.848 -20.296 1.00 32.88  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.609  -11.995 -20.624 1.00 33.62  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 15.799  -10.492 -20.510 1.00 41.71  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 14.792  -9.792  -20.447 1.00 41.77  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 16.969  -10.037 -20.533 1.00 41.76  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.197  -14.113 -21.708 1.00 28.98  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 13.006  -15.386 -22.376 1.00 29.77  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 12.092  -16.355 -21.637 1.00 34.25  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 11.767  -17.408 -22.172 1.00 33.95  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.709  -15.997 -20.407 1.00 34.15  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 10.842  -16.850 -19.596 1.00 35.19  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.367   -16.671 -19.962 1.00 30.96  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 8.901   -15.633 -20.431 1.00 32.82  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 11.068  -16.550 -18.103 1.00 32.33  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.590   -17.723 -19.645 1.00 36.00  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 7.141   -17.697 -19.834 1.00 35.34  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.499   -16.642 -18.928 1.00 35.30  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 6.767   -16.637 -17.724 1.00 37.28  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.623   -19.116 -19.512 1.00 36.05  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 5.098   -19.164 -19.446 1.00 40.96  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 7.140   -20.120 -20.540 1.00 37.67  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.707   -15.740 -19.529 1.00 34.53  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 4.975   -14.666 -18.861 1.00 33.68  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.669   -15.197 -18.264 1.00 37.44  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 3.055   -16.137 -18.771 1.00 37.29  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.673   -13.405 -19.676 1.00 37.81  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 5.883   -12.685 -20.298 1.00 34.68  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.551   -11.549 -21.262 1.00 46.23  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.200   -12.016 -22.657 1.00 44.53  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 5.011   -10.872 -23.549 1.00 46.19  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 3.190   -14.593 -17.156 1.00 38.99  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 1.913   -15.008 -16.575 1.00 36.41  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 0.783   -14.471 -17.442 1.00 34.21  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 0.949   -13.513 -18.183 1.00 36.85  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 1.858   -14.360 -15.178 1.00 36.54  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 2.983   -13.336 -15.136 1.00 36.97  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 3.796   -13.456 -16.454 1.00 37.60  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.456  -14.957 -17.244 1.00 39.08  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.629  -14.327 -17.868 1.00 40.96  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.818  -12.891 -17.400 1.00 43.42  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.315  -12.514 -16.347 1.00 31.28  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -2.795  -15.178 -17.377 1.00 41.01  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -2.170  -16.460 -16.884 1.00 37.56  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -0.760  -16.148 -16.433 1.00 41.46  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.598  -12.042 -18.099 1.00 40.97  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -2.916  -10.712 -17.576 1.00 44.10  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.514  -10.766 -16.171 1.00 39.82  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -4.235  -11.700 -15.837 1.00 41.09  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -3.921  -10.150 -18.615 1.00 45.54  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -4.377  -11.377 -19.342 1.00 38.98  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -3.190  -12.300 -19.432 1.00 45.68  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -3.165  -9.753  -15.369 1.00 40.18  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.612  -9.549  -14.003 1.00 41.66  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -3.120  -10.655 -13.068 1.00 36.81  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.596  -10.693 -11.929 1.00 34.86  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -5.127  -9.404  -13.895 1.00 45.94  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.630  -8.267  -14.753 1.00 48.21  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.454  -7.091  -14.403 1.00 47.82  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -6.218  -8.610  -15.885 1.00 50.73  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -2.179  -11.512 -13.523 1.00 31.47  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.654  -12.589 -12.680 1.00 25.72  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? -0.160  -12.289 -12.460 1.00 25.40  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.490   -11.517 -13.204 1.00 28.63  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -1.778  -14.027 -13.198 1.00 29.00  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -3.161  -14.616 -13.602 1.00 33.61  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -4.086  -14.532 -12.404 1.00 34.20  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -5.536  -14.943 -12.703 1.00 39.59  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -5.799  -16.385 -12.677 1.00 49.01  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? 0.323   -12.710 -11.290 1.00 22.30  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.731   -12.585 -10.898 1.00 23.83  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.363   -13.960 -10.844 1.00 22.27  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.753   -14.941 -10.418 1.00 23.14  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 1.822   -11.962 -9.467  1.00 23.18  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.331   -10.526 -9.437  1.00 24.51  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? -0.034  -10.258 -9.276  1.00 27.12  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 2.171   -9.442  -9.668  1.00 27.20  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.526  -8.969  -9.369  1.00 29.16  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.691   -8.138  -9.691  1.00 27.24  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.331   -7.911  -9.567  1.00 34.36  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? -0.237  -6.684  -9.712  1.00 32.55  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.692   -14.082 -11.096 1.00 23.55  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 4.373   -15.348 -10.865 1.00 21.33  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.743   -15.489 -9.395  1.00 21.39  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 5.402   -14.589 -8.872  1.00 24.32  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.670   -15.188 -11.760 1.00 22.58  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 5.870   -13.738 -11.864 1.00 24.31  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.543   -12.991 -11.577 1.00 26.35  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 4.193   -16.529 -8.776  1.00 22.48  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 4.390   -16.718 -7.337  1.00 21.21  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 5.339   -17.886 -7.149  1.00 24.10  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 5.011   -19.036 -7.559  1.00 26.09  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 3.057   -16.985 -6.633  1.00 21.94  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 2.054   -15.826 -6.930  1.00 23.66  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 3.304   -17.173 -5.124  1.00 21.18  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.572   -14.460 -6.515  1.00 21.87  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.445   -17.609 -6.416  1.00 21.23  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 7.313   -18.698 -6.038  1.00 23.52  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 6.986   -19.095 -4.609  1.00 20.91  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 7.046   -18.278 -3.692  1.00 21.93  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 8.754   -18.199 -6.218  1.00 22.15  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 9.815   -19.203 -5.769  1.00 24.27  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 10.179  -20.229 -6.650  1.00 28.51  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 10.407  -19.152 -4.496  1.00 26.57  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 11.131  -21.168 -6.284  1.00 29.78  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 11.351  -20.126 -4.141  1.00 27.85  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.737  -21.088 -5.051  1.00 26.68  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.711   -20.372 -4.432  1.00 22.37  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 6.352   -20.880 -3.128  1.00 21.98  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.605   -21.414 -2.456  1.00 24.98  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 8.326   -22.276 -3.007  1.00 23.48  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 5.367   -22.033 -3.388  1.00 25.82  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 3.990   -21.554 -3.795  1.00 22.72  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.642   -21.371 -5.125  1.00 28.10  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 3.034   -21.359 -2.804  1.00 24.72  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 2.367   -20.907 -5.438  1.00 30.93  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 1.772   -20.901 -3.127  1.00 27.84  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 1.455   -20.684 -4.434  1.00 28.40  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 7.853   -20.882 -1.263  1.00 23.10  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 9.037   -21.344 -0.549  1.00 22.27  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 8.822   -22.780 -0.075  1.00 24.81  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.702   -23.271 0.069   1.00 25.84  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 9.284   -20.432 0.666   1.00 22.89  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 9.755   -19.037 0.290   1.00 20.69  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 11.022  -18.840 -0.266  1.00 20.65  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 9.011   -17.879 0.562   1.00 22.35  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 11.453  -17.578 -0.607  1.00 20.58  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 9.462   -16.609 0.246   1.00 21.97  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.715  -16.449 -0.350  1.00 21.46  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 9.948   -23.466 0.122   1.00 25.02  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 9.906   -24.835 0.615   1.00 24.90  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.642   -25.806 -0.551  1.00 30.50  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 10.461  -26.652 -0.859  1.00 31.28  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 8.490   -25.713 -1.233  1.00 28.85  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 8.273   -26.595 -2.380  1.00 30.04  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 9.089   -26.152 -3.589  1.00 29.66  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 9.374   -26.945 -4.500  1.00 31.39  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 6.779   -26.679 -2.713  1.00 29.61  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 6.405   -25.381 -3.193  1.00 30.37  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 5.911   -27.121 -1.557  1.00 31.63  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 9.349   -24.830 -3.674  1.00 26.21  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 10.041  -24.210 -4.791  1.00 26.03  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 9.253   -24.358 -6.092  1.00 26.90  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 9.854   -24.353 -7.161  1.00 30.29  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 11.514  -24.669 -4.931  1.00 26.98  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 12.243  -24.686 -3.624  1.00 29.54  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 13.034  -25.759 -3.264  1.00 32.01  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 12.317  -23.804 -2.604  1.00 27.10  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 13.540  -25.530 -2.059  1.00 34.50  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 13.126  -24.333 -1.642  1.00 29.56  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 7.927   -24.439 -5.991  1.00 28.44  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 7.060   -24.477 -7.164  1.00 30.45  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.549   -23.072 -7.496  1.00 29.37  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 6.677   -22.141 -6.683  1.00 27.10  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 5.860   -25.394 -6.934  1.00 34.31  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 6.307   -26.842 -6.713  1.00 42.61  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 5.248   -27.742 -6.114  1.00 52.63  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 4.054   -27.367 -6.066  1.00 49.12  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 5.660   -28.832 -5.656  1.00 59.81  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 6.091   -22.899 -8.746  1.00 26.18  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.623   -21.601 -9.219  1.00 26.13  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 4.167   -21.781 -9.634  1.00 28.04  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 3.852   -22.793 -10.286 1.00 30.75  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 6.442   -21.043 -10.391 1.00 29.38  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 7.750   -20.700 -9.913  1.00 30.36  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 5.828   -19.799 -11.013 1.00 33.92  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 3.287   -20.838 -9.249  1.00 25.38  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 1.962   -20.770 -9.863  1.00 24.58  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.667   -19.316 -10.182 1.00 24.70  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 2.354   -18.404 -9.709  1.00 26.29  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 0.911   -21.305 -8.919  1.00 25.29  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.602   -19.066 -10.954 1.00 24.65  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? 0.231   -17.705 -11.290 1.00 25.37  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -1.033  -17.377 -10.516 1.00 27.28  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -2.017  -18.116 -10.575 1.00 31.95  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? -0.048  -17.632 -12.798 1.00 27.03  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 1.156   -17.954 -13.658 1.00 29.54  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 2.304   -17.171 -13.590 1.00 34.82  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 1.095   -18.995 -14.582 1.00 37.90  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 3.406   -17.470 -14.398 1.00 45.39  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 2.196   -19.287 -15.376 1.00 40.42  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 3.337   -18.531 -15.292 1.00 38.97  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -0.982  -16.275 -9.763  1.00 23.39  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -2.102  -15.943 -8.898  1.00 23.15  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.394  -14.459 -9.002  1.00 21.95  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.545  -13.621 -9.320  1.00 22.97  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -1.723  -16.276 -7.452  1.00 24.26  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -1.671  -17.762 -7.129  1.00 24.74  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.296  -17.820 -5.637  1.00 25.75  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -3.075  -18.371 -7.292  1.00 30.55  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -3.667  -14.104 -8.705  1.00 21.11  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -3.935  -12.676 -8.642  1.00 22.15  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -3.989  -12.198 -7.177  1.00 19.51  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -3.973  -13.013 -6.251  1.00 20.38  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -4.083  -10.876 -6.985  1.00 22.20  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -4.032  -10.280 -5.651  1.00 20.79  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -5.025  -10.808 -4.630  1.00 20.84  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -4.748  -10.764 -3.445  1.00 21.16  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.304  -8.822  -5.905  1.00 22.14  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -3.703  -8.605  -7.312  1.00 23.32  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -4.108  -9.865  -8.059  1.00 23.31  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -6.186  -11.302 -5.111  1.00 23.17  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -7.150  -11.839 -4.136  1.00 23.90  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.581  -12.996 -3.280  1.00 22.45  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -7.037  -13.246 -2.169  1.00 22.94  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.449  -12.315 -4.828  1.00 27.62  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.251  -13.632 -5.562  1.00 29.33  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.562  -14.102 -6.222  1.00 36.18  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.409  -15.446 -6.878  1.00 35.92  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.425  -16.546 -5.902  1.00 45.53  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.530  -13.696 -3.784  1.00 20.78  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -4.948  -14.835 -3.136  1.00 21.34  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.596  -14.454 -2.499  1.00 21.01  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -2.904  -15.350 -2.043  1.00 23.17  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -4.858  -16.006 -4.120  1.00 24.01  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.262  -16.530 -4.432  1.00 28.15  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -7.095  -16.532 -3.506  1.00 30.65  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.504  -16.962 -5.562  1.00 31.83  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.283  -13.156 -2.458  1.00 20.29  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -1.957  -12.704 -1.974  1.00 19.55  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -2.090  -11.860 -0.695  1.00 18.41  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.664  -10.761 -0.710  1.00 19.59  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -1.215  -11.948 -3.094  1.00 19.58  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -1.064  -12.730 -4.385  1.00 20.43  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.324  -11.806 -5.369  1.00 23.97  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.284  -14.003 -4.246  1.00 20.44  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.471  -12.345 0.394   1.00 21.19  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.587  -11.704 1.721   1.00 21.48  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? -0.208  -11.185 2.109   1.00 22.36  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.709   -11.981 2.299   1.00 22.64  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -2.066  -12.737 2.742   1.00 21.63  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.505  -13.157 2.463   1.00 22.47  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -3.795  -14.055 1.459   1.00 23.95  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.526  -12.624 3.254   1.00 25.40  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -5.116  -14.416 1.183   1.00 26.39  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -5.832  -12.993 2.950   1.00 23.65  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -6.113  -13.889 1.966   1.00 24.10  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? 0.006   -9.875  2.242   1.00 24.26  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.367   -9.404  2.566   1.00 22.30  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 1.902   -10.098 3.809   1.00 22.16  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 1.243   -10.245 4.821   1.00 23.34  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 1.158   -7.881  2.689   1.00 23.86  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? 0.050   -7.591  1.589   1.00 26.69  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -0.917  -8.768  1.913   1.00 25.71  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 3.190   -10.509 3.797   1.00 23.36  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 3.733   -11.369 4.847   1.00 21.90  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 3.803   -10.676 6.218   1.00 22.54  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.438   -11.357 7.175   1.00 26.15  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 5.169   -11.704 4.360   1.00 23.35  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 5.966   -12.490 5.402   1.00 22.71  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.681   -13.822 5.666   1.00 22.76  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 7.043   -11.908 6.055   1.00 27.38  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.364   -14.596 6.620   1.00 25.55  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.722   -12.668 6.989   1.00 25.46  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.406   -13.978 7.273   1.00 26.38  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 8.158   -14.668 8.223   1.00 29.43  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 4.176   -9.376  6.243   1.00 25.26  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.361   -8.703  7.534   1.00 32.90  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 3.036   -8.662  8.300   1.00 27.45  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 2.984   -9.159  9.437   1.00 34.58  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 5.116   -7.387  7.400   1.00 31.92  ? 62  ASP   A CB  1 
ATOM   495  C CG  . ASP   A 1 63 ? 6.367   -7.348  8.261   1.00 59.02  ? 62  ASP   A CG  1 
ATOM   496  O OD1 . ASP   A 1 63 ? 6.212   -7.330  9.515   1.00 56.40  ? 62  ASP   A OD1 1 
ATOM   497  O OD2 . ASP   A 1 63 ? 7.478   -7.412  7.672   1.00 62.54  ? 62  ASP   A OD2 1 
ATOM   498  N N   . LYS   A 1 64 ? 1.978   -8.233  7.583   1.00 29.58  ? 63  LYS   A N   1 
ATOM   499  C CA  . LYS   A 1 64 ? 0.641   -8.152  8.184   1.00 29.51  ? 63  LYS   A CA  1 
ATOM   500  C C   . LYS   A 1 64 ? 0.153   -9.528  8.640   1.00 30.23  ? 63  LYS   A C   1 
ATOM   501  O O   . LYS   A 1 64 ? -0.594  -9.630  9.628   1.00 30.16  ? 63  LYS   A O   1 
ATOM   502  C CB  . LYS   A 1 64 ? -0.327  -7.461  7.204   1.00 30.21  ? 63  LYS   A CB  1 
ATOM   503  C CG  . LYS   A 1 64 ? -1.790  -7.312  7.705   1.00 32.72  ? 63  LYS   A CG  1 
ATOM   504  C CD  . LYS   A 1 64 ? -2.641  -6.622  6.649   1.00 36.53  ? 63  LYS   A CD  1 
ATOM   505  C CE  . LYS   A 1 64 ? -3.698  -5.784  7.264   1.00 45.99  ? 63  LYS   A CE  1 
ATOM   506  N NZ  . LYS   A 1 64 ? -4.728  -6.556  7.944   1.00 50.50  ? 63  LYS   A NZ  1 
ATOM   507  N N   . SER   A 1 65 ? 0.474   -10.607 7.903   1.00 26.64  ? 64  SER   A N   1 
ATOM   508  C CA  . SER   A 1 65 ? -0.207  -11.889 7.986   1.00 27.30  ? 64  SER   A CA  1 
ATOM   509  C C   . SER   A 1 65 ? 0.546   -12.976 8.750   1.00 28.31  ? 64  SER   A C   1 
ATOM   510  O O   . SER   A 1 65 ? 0.010   -14.068 8.930   1.00 28.53  ? 64  SER   A O   1 
ATOM   511  C CB  . SER   A 1 65 ? -0.538  -12.419 6.591   1.00 30.61  ? 64  SER   A CB  1 
ATOM   512  O OG  . SER   A 1 65 ? -1.314  -11.447 5.917   1.00 38.59  ? 64  SER   A OG  1 
ATOM   513  N N   . LYS   A 1 66 ? 1.811   -12.723 9.126   1.00 27.40  ? 65  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66 ? 2.638   -13.815 9.627   1.00 31.78  ? 65  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66 ? 2.194   -14.337 10.993  1.00 29.14  ? 65  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66 ? 2.344   -15.537 11.270  1.00 32.44  ? 65  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66 ? 4.117   -13.430 9.564   1.00 29.38  ? 65  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66 ? 4.508   -12.314 10.457  1.00 31.05  ? 65  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66 ? 6.015   -12.144 10.304  1.00 42.55  ? 65  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66 ? 6.505   -11.144 11.328  1.00 48.60  ? 65  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66 ? 6.120   -9.770  10.973  1.00 58.50  ? 65  LYS   A NZ  1 
ATOM   522  N N   A ASP   A 1 67 ? 1.608   -13.470 11.819  0.50 31.02  ? 66  ASP   A N   1 
ATOM   523  N N   B ASP   A 1 67 ? 1.631   -13.451 11.823  0.50 30.05  ? 66  ASP   A N   1 
ATOM   524  C CA  A ASP   A 1 67 ? 1.150   -13.930 13.127  0.50 34.40  ? 66  ASP   A CA  1 
ATOM   525  C CA  B ASP   A 1 67 ? 1.100   -13.884 13.113  0.50 32.62  ? 66  ASP   A CA  1 
ATOM   526  C C   A ASP   A 1 67 ? 0.016   -14.945 12.965  0.50 34.70  ? 66  ASP   A C   1 
ATOM   527  C C   B ASP   A 1 67 ? 0.110   -15.017 12.876  0.50 33.27  ? 66  ASP   A C   1 
ATOM   528  O O   A ASP   A 1 67 ? -0.132  -15.864 13.764  0.50 37.61  ? 66  ASP   A O   1 
ATOM   529  O O   B ASP   A 1 67 ? 0.174   -16.070 13.509  0.50 35.27  ? 66  ASP   A O   1 
ATOM   530  C CB  A ASP   A 1 67 ? 0.847   -12.766 14.059  0.50 37.95  ? 66  ASP   A CB  1 
ATOM   531  C CB  B ASP   A 1 67 ? 0.380   -12.764 13.850  0.50 34.02  ? 66  ASP   A CB  1 
ATOM   532  C CG  A ASP   A 1 67 ? 2.052   -11.996 14.583  0.50 41.10  ? 66  ASP   A CG  1 
ATOM   533  C CG  B ASP   A 1 67 ? -0.026  -13.072 15.285  0.50 35.52  ? 66  ASP   A CG  1 
ATOM   534  O OD1 A ASP   A 1 67 ? 3.166   -12.567 14.597  0.50 41.74  ? 66  ASP   A OD1 1 
ATOM   535  O OD1 B ASP   A 1 67 ? 0.884   -13.239 16.129  0.50 41.83  ? 66  ASP   A OD1 1 
ATOM   536  O OD2 A ASP   A 1 67 ? 1.885   -10.811 14.946  0.50 46.57  ? 66  ASP   A OD2 1 
ATOM   537  O OD2 B ASP   A 1 67 ? -1.247  -13.136 15.548  0.50 42.75  ? 66  ASP   A OD2 1 
ATOM   538  N N   . LYS   A 1 68 ? -0.784  -14.802 11.904  1.00 31.13  ? 67  LYS   A N   1 
ATOM   539  C CA  . LYS   A 1 68 ? -1.875  -15.717 11.665  1.00 31.01  ? 67  LYS   A CA  1 
ATOM   540  C C   . LYS   A 1 68 ? -1.434  -16.964 10.908  1.00 33.07  ? 67  LYS   A C   1 
ATOM   541  O O   . LYS   A 1 68 ? -1.905  -18.052 11.187  1.00 33.38  ? 67  LYS   A O   1 
ATOM   542  C CB  . LYS   A 1 68 ? -2.950  -14.938 10.911  1.00 31.68  ? 67  LYS   A CB  1 
ATOM   543  C CG  . LYS   A 1 68 ? -4.239  -15.712 10.758  1.00 31.98  ? 67  LYS   A CG  1 
ATOM   544  C CD  . LYS   A 1 68 ? -5.254  -14.766 10.092  1.00 37.44  ? 67  LYS   A CD  1 
ATOM   545  C CE  . LYS   A 1 68 ? -6.558  -15.434 9.733   1.00 43.18  ? 67  LYS   A CE  1 
ATOM   546  N NZ  . LYS   A 1 68 ? -7.492  -14.465 9.125   1.00 39.92  ? 67  LYS   A NZ  1 
ATOM   547  N N   . TYR   A 1 69 ? -0.587  -16.795 9.875   1.00 29.47  ? 68  TYR   A N   1 
ATOM   548  C CA  . TYR   A 1 69 ? -0.355  -17.872 8.922   1.00 28.91  ? 68  TYR   A CA  1 
ATOM   549  C C   . TYR   A 1 69 ? 1.024   -18.520 9.087   1.00 27.69  ? 68  TYR   A C   1 
ATOM   550  O O   . TYR   A 1 69 ? 1.240   -19.618 8.563   1.00 28.44  ? 68  TYR   A O   1 
ATOM   551  C CB  . TYR   A 1 69 ? -0.514  -17.353 7.479   1.00 26.66  ? 68  TYR   A CB  1 
ATOM   552  C CG  . TYR   A 1 69 ? -1.913  -16.932 7.072   1.00 29.49  ? 68  TYR   A CG  1 
ATOM   553  C CD1 . TYR   A 1 69 ? -3.021  -17.691 7.447   1.00 30.15  ? 68  TYR   A CD1 1 
ATOM   554  C CD2 . TYR   A 1 69 ? -2.094  -15.728 6.382   1.00 28.22  ? 68  TYR   A CD2 1 
ATOM   555  C CE1 . TYR   A 1 69 ? -4.298  -17.261 7.084   1.00 31.80  ? 68  TYR   A CE1 1 
ATOM   556  C CE2 . TYR   A 1 69 ? -3.356  -15.307 6.005   1.00 30.06  ? 68  TYR   A CE2 1 
ATOM   557  C CZ  . TYR   A 1 69 ? -4.452  -16.073 6.382   1.00 30.90  ? 68  TYR   A CZ  1 
ATOM   558  O OH  . TYR   A 1 69 ? -5.695  -15.659 6.003   1.00 32.59  ? 68  TYR   A OH  1 
ATOM   559  N N   . GLY   A 1 70 ? 1.884   -17.884 9.873   1.00 27.02  ? 69  GLY   A N   1 
ATOM   560  C CA  . GLY   A 1 70 ? 3.297   -18.278 9.952   1.00 26.44  ? 69  GLY   A CA  1 
ATOM   561  C C   . GLY   A 1 70 ? 3.540   -19.269 11.095  1.00 31.80  ? 69  GLY   A C   1 
ATOM   562  O O   . GLY   A 1 70 ? 4.285   -18.970 12.012  1.00 38.11  ? 69  GLY   A O   1 
ATOM   563  N N   . LYS   A 1 71 ? 2.834   -20.395 11.047  1.00 32.62  ? 70  LYS   A N   1 
ATOM   564  C CA  . LYS   A 1 71 ? 2.922   -21.436 12.062  1.00 35.91  ? 70  LYS   A CA  1 
ATOM   565  C C   . LYS   A 1 71 ? 3.183   -22.775 11.374  1.00 31.50  ? 70  LYS   A C   1 
ATOM   566  O O   . LYS   A 1 71 ? 2.741   -23.058 10.261  1.00 32.62  ? 70  LYS   A O   1 
ATOM   567  C CB  . LYS   A 1 71 ? 1.697   -21.425 12.999  1.00 39.26  ? 70  LYS   A CB  1 
ATOM   568  C CG  . LYS   A 1 71 ? 1.543   -20.163 13.841  1.00 40.98  ? 70  LYS   A CG  1 
ATOM   569  C CD  . LYS   A 1 71 ? 0.471   -20.272 14.919  1.00 56.17  ? 70  LYS   A CD  1 
ATOM   570  N N   . PRO   A 1 72 ? 3.899   -23.722 12.022  1.00 34.94  ? 71  PRO   A N   1 
ATOM   571  C CA  . PRO   A 1 72 ? 4.177   -24.997 11.357  1.00 33.32  ? 71  PRO   A CA  1 
ATOM   572  C C   . PRO   A 1 72 ? 2.951   -25.745 10.879  1.00 36.30  ? 71  PRO   A C   1 
ATOM   573  O O   . PRO   A 1 72 ? 1.881   -25.624 11.468  1.00 42.80  ? 71  PRO   A O   1 
ATOM   574  C CB  . PRO   A 1 72 ? 4.970   -25.784 12.417  1.00 41.32  ? 71  PRO   A CB  1 
ATOM   575  C CG  . PRO   A 1 72 ? 5.567   -24.691 13.265  1.00 42.18  ? 71  PRO   A CG  1 
ATOM   576  C CD  . PRO   A 1 72 ? 4.504   -23.592 13.354  1.00 42.58  ? 71  PRO   A CD  1 
ATOM   577  N N   . ASN   A 1 73 ? 3.146   -26.511 9.812   1.00 39.04  ? 72  ASN   A N   1 
ATOM   578  C CA  . ASN   A 1 73 ? 2.101   -27.251 9.150   1.00 41.65  ? 72  ASN   A CA  1 
ATOM   579  C C   . ASN   A 1 73 ? 2.735   -28.565 8.723   1.00 45.94  ? 72  ASN   A C   1 
ATOM   580  O O   . ASN   A 1 73 ? 3.923   -28.619 8.398   1.00 43.36  ? 72  ASN   A O   1 
ATOM   581  C CB  . ASN   A 1 73 ? 1.638   -26.475 7.917   1.00 42.02  ? 72  ASN   A CB  1 
ATOM   582  C CG  . ASN   A 1 73 ? 0.285   -26.905 7.406   1.00 49.82  ? 72  ASN   A CG  1 
ATOM   583  O OD1 . ASN   A 1 73 ? 0.202   -27.749 6.507   1.00 48.38  ? 72  ASN   A OD1 1 
ATOM   584  N ND2 . ASN   A 1 73 ? -0.780  -26.348 7.968   1.00 51.63  ? 72  ASN   A ND2 1 
ATOM   585  N N   . LYS   A 1 74 ? 1.923   -29.615 8.717   1.00 49.72  ? 73  LYS   A N   1 
ATOM   586  C CA  . LYS   A 1 74 ? 2.364   -30.947 8.361   1.00 49.03  ? 73  LYS   A CA  1 
ATOM   587  C C   . LYS   A 1 74 ? 2.652   -31.068 6.865   1.00 44.90  ? 73  LYS   A C   1 
ATOM   588  O O   . LYS   A 1 74 ? 3.281   -32.028 6.422   1.00 42.74  ? 73  LYS   A O   1 
ATOM   589  C CB  . LYS   A 1 74 ? 1.249   -31.898 8.829   1.00 51.07  ? 73  LYS   A CB  1 
ATOM   590  C CG  . LYS   A 1 74 ? -0.080  -31.822 8.070   1.00 56.13  ? 73  LYS   A CG  1 
ATOM   591  N N   . ARG   A 1 75 ? 2.166   -30.125 6.045   1.00 41.66  ? 74  ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 75 ? 2.250   -30.320 4.609   1.00 39.73  ? 74  ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 75 ? 3.700   -30.281 4.137   1.00 39.06  ? 74  ARG   A C   1 
ATOM   594  O O   . ARG   A 1 75 ? 4.487   -29.494 4.668   1.00 35.83  ? 74  ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 75 ? 1.378   -29.304 3.856   1.00 42.28  ? 74  ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 75 ? -0.095  -29.502 4.183   1.00 48.54  ? 74  ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 75 ? -0.692  -30.641 3.373   1.00 43.67  ? 74  ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 75 ? -1.540  -30.106 2.303   1.00 59.87  ? 74  ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 75 ? -2.703  -29.485 2.531   1.00 55.88  ? 74  ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 75 ? -3.422  -29.075 1.509   1.00 64.63  ? 74  ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 75 ? -3.156  -29.304 3.764   1.00 64.02  ? 74  ARG   A NH2 1 
ATOM   602  N N   . LYS   A 1 76 ? 3.992   -31.103 3.117   1.00 35.85  ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 76 ? 5.327   -31.269 2.558   1.00 37.53  ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 76 ? 5.887   -29.905 2.163   1.00 35.20  ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 76 ? 5.334   -29.230 1.298   1.00 34.05  ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 76 ? 5.307   -32.167 1.316   1.00 39.90  ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 76 ? 6.641   -32.532 0.687   1.00 45.71  ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 76 ? 6.540   -33.532 -0.461  1.00 46.63  ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 76 ? 7.870   -33.948 -1.026  1.00 53.82  ? 75  LYS   A CE  1 
ATOM   610  N N   . GLY   A 1 77 ? 7.018   -29.538 2.782   1.00 33.78  ? 76  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 77 ? 7.745   -28.378 2.304   1.00 31.97  ? 76  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 77 ? 7.370   -27.133 3.094   1.00 30.81  ? 76  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 77 ? 8.073   -26.149 2.985   1.00 28.99  ? 76  GLY   A O   1 
ATOM   614  N N   . PHE   A 1 78 ? 6.275   -27.160 3.857   1.00 28.96  ? 77  PHE   A N   1 
ATOM   615  C CA  . PHE   A 1 78 ? 5.804   -25.953 4.503   1.00 27.98  ? 77  PHE   A CA  1 
ATOM   616  C C   . PHE   A 1 78 ? 6.825   -25.376 5.490   1.00 31.85  ? 77  PHE   A C   1 
ATOM   617  O O   . PHE   A 1 78 ? 7.133   -24.182 5.489   1.00 28.87  ? 77  PHE   A O   1 
ATOM   618  C CB  . PHE   A 1 78 ? 4.428   -26.244 5.096   1.00 28.97  ? 77  PHE   A CB  1 
ATOM   619  C CG  . PHE   A 1 78 ? 3.718   -24.957 5.487   1.00 29.19  ? 77  PHE   A CG  1 
ATOM   620  C CD1 . PHE   A 1 78 ? 4.016   -24.301 6.677   1.00 29.14  ? 77  PHE   A CD1 1 
ATOM   621  C CD2 . PHE   A 1 78 ? 2.762   -24.396 4.633   1.00 31.34  ? 77  PHE   A CD2 1 
ATOM   622  C CE1 . PHE   A 1 78 ? 3.382   -23.111 7.040   1.00 28.73  ? 77  PHE   A CE1 1 
ATOM   623  C CE2 . PHE   A 1 78 ? 2.079   -23.246 5.013   1.00 27.72  ? 77  PHE   A CE2 1 
ATOM   624  C CZ  . PHE   A 1 78 ? 2.400   -22.586 6.199   1.00 26.95  ? 77  PHE   A CZ  1 
ATOM   625  N N   . ASN   A 1 79 ? 7.325   -26.208 6.402   1.00 27.35  ? 78  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 79 ? 8.217   -25.704 7.440   1.00 27.71  ? 78  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 79 ? 9.573   -25.240 6.861   1.00 25.66  ? 78  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 79 ? 10.143  -24.247 7.355   1.00 29.35  ? 78  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 79 ? 8.410   -26.792 8.503   1.00 29.51  ? 78  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 79 ? 7.080   -27.076 9.157   1.00 37.13  ? 78  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 79 ? 6.187   -26.218 9.133   1.00 31.40  ? 78  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 79 ? 6.921   -28.255 9.749   1.00 32.44  ? 78  ASN   A ND2 1 
ATOM   633  N N   . GLU   A 1 80 ? 10.064  -25.924 5.819   1.00 25.98  ? 79  GLU   A N   1 
ATOM   634  C CA  . GLU   A 1 80 ? 11.227  -25.431 5.091   1.00 27.16  ? 79  GLU   A CA  1 
ATOM   635  C C   . GLU   A 1 80 ? 10.879  -24.040 4.553   1.00 25.88  ? 79  GLU   A C   1 
ATOM   636  O O   . GLU   A 1 80 ? 11.695  -23.110 4.567   1.00 25.77  ? 79  GLU   A O   1 
ATOM   637  C CB  . GLU   A 1 80 ? 11.648  -26.371 3.955   1.00 27.94  ? 79  GLU   A CB  1 
ATOM   638  C CG  . GLU   A 1 80 ? 12.909  -25.921 3.209   1.00 28.89  ? 79  GLU   A CG  1 
ATOM   639  C CD  . GLU   A 1 80 ? 13.446  -26.889 2.143   1.00 35.43  ? 79  GLU   A CD  1 
ATOM   640  O OE1 . GLU   A 1 80 ? 12.761  -27.875 1.821   1.00 46.26  ? 79  GLU   A OE1 1 
ATOM   641  O OE2 . GLU   A 1 80 ? 14.566  -26.695 1.653   1.00 40.34  ? 79  GLU   A OE2 1 
ATOM   642  N N   . GLY   A 1 81 ? 9.643   -23.914 4.044   1.00 25.40  ? 80  GLY   A N   1 
ATOM   643  C CA  . GLY   A 1 81 ? 9.281   -22.627 3.447   1.00 24.18  ? 80  GLY   A CA  1 
ATOM   644  C C   . GLY   A 1 81 ? 9.222   -21.500 4.486   1.00 22.44  ? 80  GLY   A C   1 
ATOM   645  O O   . GLY   A 1 81 ? 9.500   -20.339 4.184   1.00 22.89  ? 80  GLY   A O   1 
ATOM   646  N N   . LEU   A 1 82 ? 8.766   -21.804 5.718   1.00 23.43  ? 81  LEU   A N   1 
ATOM   647  C CA  . LEU   A 1 82 ? 8.792   -20.797 6.765   1.00 23.54  ? 81  LEU   A CA  1 
ATOM   648  C C   . LEU   A 1 82 ? 10.221  -20.338 7.091   1.00 22.56  ? 81  LEU   A C   1 
ATOM   649  O O   . LEU   A 1 82 ? 10.439  -19.155 7.362   1.00 23.17  ? 81  LEU   A O   1 
ATOM   650  C CB  . LEU   A 1 82 ? 8.171   -21.351 8.051   1.00 26.08  ? 81  LEU   A CB  1 
ATOM   651  C CG  . LEU   A 1 82 ? 6.656   -21.624 7.976   1.00 28.20  ? 81  LEU   A CG  1 
ATOM   652  C CD1 . LEU   A 1 82 ? 6.235   -22.245 9.304   1.00 28.70  ? 81  LEU   A CD1 1 
ATOM   653  C CD2 . LEU   A 1 82 ? 5.848   -20.373 7.739   1.00 27.89  ? 81  LEU   A CD2 1 
ATOM   654  N N   . TRP   A 1 83 ? 11.194  -21.281 7.004   1.00 24.27  ? 82  TRP   A N   1 
ATOM   655  C CA  . TRP   A 1 83 ? 12.565  -20.885 7.295   1.00 25.38  ? 82  TRP   A CA  1 
ATOM   656  C C   . TRP   A 1 83 ? 13.036  -19.958 6.185   1.00 24.31  ? 82  TRP   A C   1 
ATOM   657  O O   . TRP   A 1 83 ? 13.695  -18.976 6.455   1.00 23.91  ? 82  TRP   A O   1 
ATOM   658  C CB  . TRP   A 1 83 ? 13.476  -22.132 7.395   1.00 23.99  ? 82  TRP   A CB  1 
ATOM   659  C CG  . TRP   A 1 83 ? 14.923  -21.765 7.660   1.00 22.28  ? 82  TRP   A CG  1 
ATOM   660  C CD1 . TRP   A 1 83 ? 15.541  -21.650 8.879   1.00 25.95  ? 82  TRP   A CD1 1 
ATOM   661  C CD2 . TRP   A 1 83 ? 15.907  -21.432 6.653   1.00 23.15  ? 82  TRP   A CD2 1 
ATOM   662  N NE1 . TRP   A 1 83 ? 16.851  -21.309 8.693   1.00 27.67  ? 82  TRP   A NE1 1 
ATOM   663  C CE2 . TRP   A 1 83 ? 17.094  -21.122 7.347   1.00 24.69  ? 82  TRP   A CE2 1 
ATOM   664  C CE3 . TRP   A 1 83 ? 15.887  -21.365 5.245   1.00 25.42  ? 82  TRP   A CE3 1 
ATOM   665  C CZ2 . TRP   A 1 83 ? 18.265  -20.766 6.669   1.00 25.48  ? 82  TRP   A CZ2 1 
ATOM   666  C CZ3 . TRP   A 1 83 ? 17.031  -20.975 4.571   1.00 26.48  ? 82  TRP   A CZ3 1 
ATOM   667  C CH2 . TRP   A 1 83 ? 18.197  -20.681 5.293   1.00 28.24  ? 82  TRP   A CH2 1 
ATOM   668  N N   . GLU   A 1 84 ? 12.711  -20.302 4.937   1.00 22.94  ? 83  GLU   A N   1 
ATOM   669  C CA  . GLU   A 1 84 ? 13.249  -19.561 3.821   1.00 21.08  ? 83  GLU   A CA  1 
ATOM   670  C C   . GLU   A 1 84 ? 12.713  -18.137 3.830   1.00 22.82  ? 83  GLU   A C   1 
ATOM   671  O O   . GLU   A 1 84 ? 13.434  -17.172 3.613   1.00 21.73  ? 83  GLU   A O   1 
ATOM   672  C CB  . GLU   A 1 84 ? 12.836  -20.199 2.517   1.00 22.51  ? 83  GLU   A CB  1 
ATOM   673  C CG  . GLU   A 1 84 ? 13.544  -21.533 2.351   1.00 23.05  ? 83  GLU   A CG  1 
ATOM   674  C CD  . GLU   A 1 84 ? 13.168  -22.273 1.076   1.00 25.29  ? 83  GLU   A CD  1 
ATOM   675  O OE1 . GLU   A 1 84 ? 12.227  -21.877 0.362   1.00 24.46  ? 83  GLU   A OE1 1 
ATOM   676  O OE2 . GLU   A 1 84 ? 13.805  -23.348 0.782   1.00 27.24  ? 83  GLU   A OE2 1 
ATOM   677  N N   . ILE   A 1 85 ? 11.380  -17.989 4.078   1.00 20.03  ? 84  ILE   A N   1 
ATOM   678  C CA  . ILE   A 1 85 ? 10.838  -16.633 3.973   1.00 20.03  ? 84  ILE   A CA  1 
ATOM   679  C C   . ILE   A 1 85 ? 11.378  -15.710 5.079   1.00 21.00  ? 84  ILE   A C   1 
ATOM   680  O O   . ILE   A 1 85 ? 11.507  -14.509 4.891   1.00 21.35  ? 84  ILE   A O   1 
ATOM   681  C CB  . ILE   A 1 85 ? 9.280   -16.697 3.970   1.00 20.12  ? 84  ILE   A CB  1 
ATOM   682  C CG1 . ILE   A 1 85 ? 8.674   -15.310 3.563   1.00 19.29  ? 84  ILE   A CG1 1 
ATOM   683  C CG2 . ILE   A 1 85 ? 8.708   -17.077 5.354   1.00 21.73  ? 84  ILE   A CG2 1 
ATOM   684  C CD1 . ILE   A 1 85 ? 7.217   -15.382 3.050   1.00 19.96  ? 84  ILE   A CD1 1 
ATOM   685  N N   . GLN   A 1 86 ? 11.657  -16.307 6.257   1.00 22.10  ? 85  GLN   A N   1 
ATOM   686  C CA  . GLN   A 1 86 ? 12.216  -15.528 7.385   1.00 23.10  ? 85  GLN   A CA  1 
ATOM   687  C C   . GLN   A 1 86 ? 13.717  -15.254 7.260   1.00 23.02  ? 85  GLN   A C   1 
ATOM   688  O O   . GLN   A 1 86 ? 14.152  -14.121 7.597   1.00 26.08  ? 85  GLN   A O   1 
ATOM   689  C CB  . GLN   A 1 86 ? 11.845  -16.292 8.666   1.00 26.21  ? 85  GLN   A CB  1 
ATOM   690  C CG  . GLN   A 1 86 ? 12.419  -15.679 9.948   1.00 31.83  ? 85  GLN   A CG  1 
ATOM   691  C CD  . GLN   A 1 86 ? 11.724  -16.177 11.210  1.00 37.60  ? 85  GLN   A CD  1 
ATOM   692  O OE1 . GLN   A 1 86 ? 11.386  -17.366 11.332  1.00 39.52  ? 85  GLN   A OE1 1 
ATOM   693  N NE2 . GLN   A 1 86 ? 11.463  -15.266 12.143  1.00 43.47  ? 85  GLN   A NE2 1 
ATOM   694  N N   . ASN   A 1 87 ? 14.455  -16.217 6.706   1.00 20.87  ? 86  ASN   A N   1 
ATOM   695  C CA  . ASN   A 1 87 ? 15.920  -16.200 6.812   1.00 21.75  ? 86  ASN   A CA  1 
ATOM   696  C C   . ASN   A 1 87 ? 16.648  -15.902 5.516   1.00 22.69  ? 86  ASN   A C   1 
ATOM   697  O O   . ASN   A 1 87 ? 17.760  -15.357 5.571   1.00 25.37  ? 86  ASN   A O   1 
ATOM   698  C CB  . ASN   A 1 87 ? 16.450  -17.492 7.429   1.00 22.55  ? 86  ASN   A CB  1 
ATOM   699  C CG  . ASN   A 1 87 ? 15.948  -17.615 8.857   1.00 27.84  ? 86  ASN   A CG  1 
ATOM   700  O OD1 . ASN   A 1 87 ? 16.261  -16.725 9.675   1.00 31.60  ? 86  ASN   A OD1 1 
ATOM   701  N ND2 . ASN   A 1 87 ? 15.016  -18.518 9.132   1.00 25.57  ? 86  ASN   A ND2 1 
ATOM   702  N N   . ASN   A 1 88 ? 16.059  -16.195 4.332   1.00 21.54  ? 87  ASN   A N   1 
ATOM   703  C CA  . ASN   A 1 88 ? 16.764  -15.851 3.107   1.00 20.25  ? 87  ASN   A CA  1 
ATOM   704  C C   . ASN   A 1 88 ? 15.713  -15.802 1.988   1.00 22.23  ? 87  ASN   A C   1 
ATOM   705  O O   . ASN   A 1 88 ? 15.763  -16.539 0.989   1.00 22.68  ? 87  ASN   A O   1 
ATOM   706  C CB  . ASN   A 1 88 ? 17.922  -16.804 2.778   1.00 24.44  ? 87  ASN   A CB  1 
ATOM   707  C CG  . ASN   A 1 88 ? 18.976  -16.183 1.880   1.00 25.30  ? 87  ASN   A CG  1 
ATOM   708  O OD1 . ASN   A 1 88 ? 18.767  -15.169 1.207   1.00 23.34  ? 87  ASN   A OD1 1 
ATOM   709  N ND2 . ASN   A 1 88 ? 20.197  -16.728 1.876   1.00 28.97  ? 87  ASN   A ND2 1 
ATOM   710  N N   . PRO   A 1 89 ? 14.800  -14.825 2.075   1.00 20.79  ? 88  PRO   A N   1 
ATOM   711  C CA  . PRO   A 1 89 ? 13.653  -14.809 1.171   1.00 20.99  ? 88  PRO   A CA  1 
ATOM   712  C C   . PRO   A 1 89 ? 14.027  -14.379 -0.239  1.00 22.07  ? 88  PRO   A C   1 
ATOM   713  O O   . PRO   A 1 89 ? 13.213  -14.604 -1.143  1.00 20.68  ? 88  PRO   A O   1 
ATOM   714  C CB  . PRO   A 1 89 ? 12.725  -13.810 1.828   1.00 20.16  ? 88  PRO   A CB  1 
ATOM   715  C CG  . PRO   A 1 89 ? 13.634  -12.885 2.564   1.00 20.56  ? 88  PRO   A CG  1 
ATOM   716  C CD  . PRO   A 1 89 ? 14.722  -13.789 3.122   1.00 20.86  ? 88  PRO   A CD  1 
ATOM   717  N N   . HIS   A 1 90 ? 15.233  -13.800 -0.454  1.00 18.95  ? 89  HIS   A N   1 
ATOM   718  C CA  . HIS   A 1 90 ? 15.590  -13.262 -1.781  1.00 20.04  ? 89  HIS   A CA  1 
ATOM   719  C C   . HIS   A 1 90 ? 16.692  -14.081 -2.468  1.00 20.40  ? 89  HIS   A C   1 
ATOM   720  O O   . HIS   A 1 90 ? 17.138  -13.665 -3.552  1.00 24.24  ? 89  HIS   A O   1 
ATOM   721  C CB  . HIS   A 1 90 ? 15.952  -11.759 -1.660  1.00 19.53  ? 89  HIS   A CB  1 
ATOM   722  C CG  . HIS   A 1 90 ? 14.860  -10.959 -1.052  1.00 19.07  ? 89  HIS   A CG  1 
ATOM   723  N ND1 . HIS   A 1 90 ? 13.620  -10.858 -1.689  1.00 20.51  ? 89  HIS   A ND1 1 
ATOM   724  C CD2 . HIS   A 1 90 ? 14.825  -10.211 0.019   1.00 21.56  ? 89  HIS   A CD2 1 
ATOM   725  C CE1 . HIS   A 1 90 ? 12.832  -10.072 -0.977  1.00 21.19  ? 89  HIS   A CE1 1 
ATOM   726  N NE2 . HIS   A 1 90 ? 13.544  -9.660  0.110   1.00 22.07  ? 89  HIS   A NE2 1 
ATOM   727  N N   . ALA   A 1 91 ? 16.972  -15.278 -1.939  1.00 20.90  ? 90  ALA   A N   1 
ATOM   728  C CA  . ALA   A 1 91 ? 18.020  -16.137 -2.511  1.00 22.35  ? 90  ALA   A CA  1 
ATOM   729  C C   . ALA   A 1 91 ? 17.545  -16.829 -3.782  1.00 25.75  ? 90  ALA   A C   1 
ATOM   730  O O   . ALA   A 1 91 ? 16.371  -16.971 -4.072  1.00 25.37  ? 90  ALA   A O   1 
ATOM   731  C CB  . ALA   A 1 91 ? 18.463  -17.160 -1.488  1.00 23.27  ? 90  ALA   A CB  1 
ATOM   732  N N   . SER   A 1 92 ? 18.514  -17.343 -4.556  1.00 24.58  ? 91  SER   A N   1 
ATOM   733  C CA  . SER   A 1 92 ? 18.230  -18.274 -5.618  1.00 29.34  ? 91  SER   A CA  1 
ATOM   734  C C   . SER   A 1 92 ? 18.023  -19.672 -5.038  1.00 29.48  ? 91  SER   A C   1 
ATOM   735  O O   . SER   A 1 92 ? 18.881  -20.191 -4.300  1.00 32.29  ? 91  SER   A O   1 
ATOM   736  C CB  . SER   A 1 92 ? 19.386  -18.182 -6.564  1.00 33.10  ? 91  SER   A CB  1 
ATOM   737  O OG  . SER   A 1 92 ? 19.399  -19.296 -7.427  1.00 40.58  ? 91  SER   A OG  1 
ATOM   738  N N   . TYR   A 1 93 ? 16.851  -20.257 -5.333  1.00 28.02  ? 92  TYR   A N   1 
ATOM   739  C CA  . TYR   A 1 93 ? 16.476  -21.596 -4.920  1.00 27.62  ? 92  TYR   A CA  1 
ATOM   740  C C   . TYR   A 1 93 ? 16.388  -22.542 -6.116  1.00 33.23  ? 92  TYR   A C   1 
ATOM   741  O O   . TYR   A 1 93 ? 15.911  -23.661 -5.956  1.00 40.80  ? 92  TYR   A O   1 
ATOM   742  C CB  . TYR   A 1 93 ? 15.123  -21.566 -4.183  1.00 27.94  ? 92  TYR   A CB  1 
ATOM   743  C CG  . TYR   A 1 93 ? 15.254  -20.969 -2.796  1.00 26.60  ? 92  TYR   A CG  1 
ATOM   744  C CD1 . TYR   A 1 93 ? 15.684  -21.728 -1.702  1.00 27.12  ? 92  TYR   A CD1 1 
ATOM   745  C CD2 . TYR   A 1 93 ? 14.954  -19.615 -2.583  1.00 26.59  ? 92  TYR   A CD2 1 
ATOM   746  C CE1 . TYR   A 1 93 ? 15.871  -21.151 -0.447  1.00 28.61  ? 92  TYR   A CE1 1 
ATOM   747  C CE2 . TYR   A 1 93 ? 15.098  -19.051 -1.331  1.00 26.86  ? 92  TYR   A CE2 1 
ATOM   748  C CZ  . TYR   A 1 93 ? 15.557  -19.810 -0.266  1.00 26.66  ? 92  TYR   A CZ  1 
ATOM   749  O OH  . TYR   A 1 93 ? 15.788  -19.315 0.982   1.00 27.98  ? 92  TYR   A OH  1 
ATOM   750  N N   . SER   A 1 94 ? 16.833  -22.084 -7.281  1.00 41.69  ? 93  SER   A N   1 
ATOM   751  C CA  . SER   A 1 94 ? 17.033  -22.910 -8.468  1.00 59.35  ? 93  SER   A CA  1 
ATOM   752  C C   . SER   A 1 94 ? 18.127  -23.960 -8.212  1.00 68.13  ? 93  SER   A C   1 
ATOM   753  O O   . SER   A 1 94 ? 19.130  -23.594 -7.561  1.00 71.82  ? 93  SER   A O   1 
ATOM   754  C CB  . SER   A 1 94 ? 17.413  -22.047 -9.642  1.00 55.30  ? 93  SER   A CB  1 
ATOM   755  O OG  . SER   A 1 94 ? 16.327  -21.205 -10.004 1.00 61.43  ? 93  SER   A OG  1 
ATOM   756  O OXT . SER   A 1 94 ? 17.958  -25.101 -8.701  1.00 82.47  ? 93  SER   A OXT 1 
ATOM   757  N N   . MET   B 1 2  ? 38.899  -11.253 -42.257 1.00 72.33  ? 1   MET   B N   1 
ATOM   758  C CA  . MET   B 1 2  ? 38.501  -12.247 -43.289 1.00 72.85  ? 1   MET   B CA  1 
ATOM   759  C C   . MET   B 1 2  ? 36.983  -12.410 -43.226 1.00 64.40  ? 1   MET   B C   1 
ATOM   760  O O   . MET   B 1 2  ? 36.452  -12.724 -42.160 1.00 67.06  ? 1   MET   B O   1 
ATOM   761  C CB  . MET   B 1 2  ? 39.206  -13.591 -43.051 1.00 79.57  ? 1   MET   B CB  1 
ATOM   762  C CG  . MET   B 1 2  ? 39.261  -14.531 -44.255 1.00 90.29  ? 1   MET   B CG  1 
ATOM   763  S SD  . MET   B 1 2  ? 40.304  -14.036 -45.648 1.00 91.78  ? 1   MET   B SD  1 
ATOM   764  C CE  . MET   B 1 2  ? 41.804  -13.421 -44.868 1.00 92.45  ? 1   MET   B CE  1 
ATOM   765  N N   . PRO   B 1 3  ? 36.245  -12.164 -44.340 1.00 54.74  ? 2   PRO   B N   1 
ATOM   766  C CA  . PRO   B 1 3  ? 34.785  -12.315 -44.354 1.00 53.24  ? 2   PRO   B CA  1 
ATOM   767  C C   . PRO   B 1 3  ? 34.418  -13.757 -44.016 1.00 53.56  ? 2   PRO   B C   1 
ATOM   768  O O   . PRO   B 1 3  ? 35.181  -14.666 -44.322 1.00 46.48  ? 2   PRO   B O   1 
ATOM   769  C CB  . PRO   B 1 3  ? 34.377  -11.910 -45.776 1.00 54.02  ? 2   PRO   B CB  1 
ATOM   770  C CG  . PRO   B 1 3  ? 35.548  -11.070 -46.261 1.00 50.82  ? 2   PRO   B CG  1 
ATOM   771  C CD  . PRO   B 1 3  ? 36.777  -11.699 -45.634 1.00 48.29  ? 2   PRO   B CD  1 
ATOM   772  N N   . HIS   B 1 4  ? 33.282  -13.942 -43.328 1.00 49.00  ? 3   HIS   B N   1 
ATOM   773  C CA  . HIS   B 1 4  ? 32.848  -15.272 -42.912 1.00 50.49  ? 3   HIS   B CA  1 
ATOM   774  C C   . HIS   B 1 4  ? 31.488  -15.575 -43.530 1.00 46.00  ? 3   HIS   B C   1 
ATOM   775  O O   . HIS   B 1 4  ? 30.881  -14.694 -44.152 1.00 46.11  ? 3   HIS   B O   1 
ATOM   776  C CB  . HIS   B 1 4  ? 32.921  -15.425 -41.390 1.00 57.38  ? 3   HIS   B CB  1 
ATOM   777  C CG  . HIS   B 1 4  ? 34.319  -15.646 -40.906 1.00 67.61  ? 3   HIS   B CG  1 
ATOM   778  N ND1 . HIS   B 1 4  ? 35.230  -16.402 -41.615 1.00 63.97  ? 3   HIS   B ND1 1 
ATOM   779  C CD2 . HIS   B 1 4  ? 34.960  -15.222 -39.799 1.00 66.65  ? 3   HIS   B CD2 1 
ATOM   780  C CE1 . HIS   B 1 4  ? 36.382  -16.424 -40.954 1.00 64.49  ? 3   HIS   B CE1 1 
ATOM   781  N NE2 . HIS   B 1 4  ? 36.237  -15.718 -39.848 1.00 67.04  ? 3   HIS   B NE2 1 
ATOM   782  N N   . ALA   B 1 5  ? 31.019  -16.830 -43.387 1.00 40.83  ? 4   ALA   B N   1 
ATOM   783  C CA  . ALA   B 1 5  ? 29.701  -17.168 -43.897 1.00 41.82  ? 4   ALA   B CA  1 
ATOM   784  C C   . ALA   B 1 5  ? 28.708  -16.114 -43.418 1.00 40.29  ? 4   ALA   B C   1 
ATOM   785  O O   . ALA   B 1 5  ? 27.930  -15.581 -44.212 1.00 43.26  ? 4   ALA   B O   1 
ATOM   786  C CB  . ALA   B 1 5  ? 29.269  -18.526 -43.403 1.00 44.00  ? 4   ALA   B CB  1 
ATOM   787  N N   . PHE   B 1 6  ? 28.747  -15.854 -42.111 1.00 43.62  ? 5   PHE   B N   1 
ATOM   788  C CA  . PHE   B 1 6  ? 27.967  -14.781 -41.510 1.00 43.40  ? 5   PHE   B CA  1 
ATOM   789  C C   . PHE   B 1 6  ? 28.855  -13.570 -41.203 1.00 41.54  ? 5   PHE   B C   1 
ATOM   790  O O   . PHE   B 1 6  ? 29.970  -13.686 -40.693 1.00 46.10  ? 5   PHE   B O   1 
ATOM   791  C CB  . PHE   B 1 6  ? 27.317  -15.214 -40.194 1.00 40.45  ? 5   PHE   B CB  1 
ATOM   792  C CG  . PHE   B 1 6  ? 26.202  -16.248 -40.301 1.00 35.45  ? 5   PHE   B CG  1 
ATOM   793  C CD1 . PHE   B 1 6  ? 24.898  -15.865 -40.607 1.00 33.57  ? 5   PHE   B CD1 1 
ATOM   794  C CD2 . PHE   B 1 6  ? 26.457  -17.603 -40.095 1.00 39.70  ? 5   PHE   B CD2 1 
ATOM   795  C CE1 . PHE   B 1 6  ? 23.880  -16.797 -40.690 1.00 34.02  ? 5   PHE   B CE1 1 
ATOM   796  C CE2 . PHE   B 1 6  ? 25.432  -18.531 -40.179 1.00 33.27  ? 5   PHE   B CE2 1 
ATOM   797  C CZ  . PHE   B 1 6  ? 24.140  -18.135 -40.440 1.00 32.82  ? 5   PHE   B CZ  1 
ATOM   798  N N   . LYS   B 1 7  ? 28.301  -12.397 -41.485 1.00 41.20  ? 6   LYS   B N   1 
ATOM   799  C CA  . LYS   B 1 7  ? 28.997  -11.137 -41.291 1.00 40.41  ? 6   LYS   B CA  1 
ATOM   800  C C   . LYS   B 1 7  ? 28.222  -10.288 -40.274 1.00 38.84  ? 6   LYS   B C   1 
ATOM   801  O O   . LYS   B 1 7  ? 26.983  -10.387 -40.180 1.00 34.92  ? 6   LYS   B O   1 
ATOM   802  C CB  . LYS   B 1 7  ? 29.096  -10.465 -42.659 1.00 43.56  ? 6   LYS   B CB  1 
ATOM   803  C CG  . LYS   B 1 7  ? 27.797  -10.003 -43.277 1.00 41.79  ? 6   LYS   B CG  1 
ATOM   804  C CD  . LYS   B 1 7  ? 28.022  -9.574  -44.726 1.00 51.45  ? 6   LYS   B CD  1 
ATOM   805  C CE  . LYS   B 1 7  ? 26.800  -9.098  -45.453 1.00 56.00  ? 6   LYS   B CE  1 
ATOM   806  N NZ  . LYS   B 1 7  ? 25.836  -10.178 -45.701 1.00 56.34  ? 6   LYS   B NZ  1 
ATOM   807  N N   . PRO   B 1 8  ? 28.905  -9.385  -39.526 1.00 44.35  ? 7   PRO   B N   1 
ATOM   808  C CA  . PRO   B 1 8  ? 28.227  -8.403  -38.669 1.00 37.67  ? 7   PRO   B CA  1 
ATOM   809  C C   . PRO   B 1 8  ? 27.065  -7.708  -39.360 1.00 34.69  ? 7   PRO   B C   1 
ATOM   810  O O   . PRO   B 1 8  ? 27.174  -7.278  -40.520 1.00 43.13  ? 7   PRO   B O   1 
ATOM   811  C CB  . PRO   B 1 8  ? 29.373  -7.444  -38.350 1.00 45.83  ? 7   PRO   B CB  1 
ATOM   812  C CG  . PRO   B 1 8  ? 30.598  -8.346  -38.276 1.00 44.19  ? 7   PRO   B CG  1 
ATOM   813  C CD  . PRO   B 1 8  ? 30.374  -9.215  -39.500 1.00 47.55  ? 7   PRO   B CD  1 
ATOM   814  N N   . GLY   B 1 9  ? 25.931  -7.621  -38.647 1.00 31.84  ? 8   GLY   B N   1 
ATOM   815  C CA  . GLY   B 1 9  ? 24.692  -7.061  -39.134 1.00 31.42  ? 8   GLY   B CA  1 
ATOM   816  C C   . GLY   B 1 9  ? 23.759  -8.050  -39.825 1.00 29.99  ? 8   GLY   B C   1 
ATOM   817  O O   . GLY   B 1 9  ? 22.644  -7.675  -40.172 1.00 33.79  ? 8   GLY   B O   1 
ATOM   818  N N   . ASP   B 1 10 ? 24.229  -9.295  -40.070 1.00 31.77  ? 9   ASP   B N   1 
ATOM   819  C CA  . ASP   B 1 10 ? 23.349  -10.329 -40.588 1.00 33.88  ? 9   ASP   B CA  1 
ATOM   820  C C   . ASP   B 1 10 ? 22.248  -10.615 -39.560 1.00 26.33  ? 9   ASP   B C   1 
ATOM   821  O O   . ASP   B 1 10 ? 22.541  -10.623 -38.372 1.00 30.63  ? 9   ASP   B O   1 
ATOM   822  C CB  . ASP   B 1 10 ? 24.085  -11.612 -40.932 1.00 35.06  ? 9   ASP   B CB  1 
ATOM   823  C CG  . ASP   B 1 10 ? 24.789  -11.658 -42.289 1.00 43.04  ? 9   ASP   B CG  1 
ATOM   824  O OD1 . ASP   B 1 10 ? 24.469  -10.793 -43.138 1.00 41.47  ? 9   ASP   B OD1 1 
ATOM   825  O OD2 . ASP   B 1 10 ? 25.652  -12.574 -42.466 1.00 38.97  ? 9   ASP   B OD2 1 
ATOM   826  N N   . LEU   B 1 11 ? 21.038  -10.747 -40.056 1.00 26.95  ? 10  LEU   B N   1 
ATOM   827  C CA  . LEU   B 1 11 ? 19.886  -10.955 -39.170 1.00 26.90  ? 10  LEU   B CA  1 
ATOM   828  C C   . LEU   B 1 11 ? 19.594  -12.452 -39.171 1.00 27.49  ? 10  LEU   B C   1 
ATOM   829  O O   . LEU   B 1 11 ? 19.641  -13.053 -40.251 1.00 30.29  ? 10  LEU   B O   1 
ATOM   830  C CB  . LEU   B 1 11 ? 18.686  -10.149 -39.664 1.00 30.54  ? 10  LEU   B CB  1 
ATOM   831  C CG  . LEU   B 1 11 ? 18.966  -8.638  -39.773 1.00 26.96  ? 10  LEU   B CG  1 
ATOM   832  C CD1 . LEU   B 1 11 ? 17.700  -7.929  -40.186 1.00 29.11  ? 10  LEU   B CD1 1 
ATOM   833  C CD2 . LEU   B 1 11 ? 19.600  -8.096  -38.483 1.00 29.78  ? 10  LEU   B CD2 1 
ATOM   834  N N   . VAL   B 1 12 ? 19.196  -13.023 -38.008 1.00 27.57  ? 11  VAL   B N   1 
ATOM   835  C CA  . VAL   B 1 12 ? 18.990  -14.476 -37.931 1.00 25.59  ? 11  VAL   B CA  1 
ATOM   836  C C   . VAL   B 1 12 ? 17.898  -14.732 -36.897 1.00 29.24  ? 11  VAL   B C   1 
ATOM   837  O O   . VAL   B 1 12 ? 17.528  -13.817 -36.164 1.00 27.48  ? 11  VAL   B O   1 
ATOM   838  C CB  . VAL   B 1 12 ? 20.294  -15.169 -37.473 1.00 25.62  ? 11  VAL   B CB  1 
ATOM   839  C CG1 . VAL   B 1 12 ? 21.430  -14.960 -38.490 1.00 29.44  ? 11  VAL   B CG1 1 
ATOM   840  C CG2 . VAL   B 1 12 ? 20.771  -14.819 -36.049 1.00 27.25  ? 11  VAL   B CG2 1 
ATOM   841  N N   . PHE   B 1 13 ? 17.452  -15.991 -36.823 1.00 25.82  ? 12  PHE   B N   1 
ATOM   842  C CA  . PHE   B 1 13 ? 16.918  -16.532 -35.594 1.00 26.63  ? 12  PHE   B CA  1 
ATOM   843  C C   . PHE   B 1 13 ? 18.014  -17.397 -35.004 1.00 27.90  ? 12  PHE   B C   1 
ATOM   844  O O   . PHE   B 1 13 ? 18.664  -18.163 -35.742 1.00 29.02  ? 12  PHE   B O   1 
ATOM   845  C CB  . PHE   B 1 13 ? 15.681  -17.384 -35.869 1.00 25.46  ? 12  PHE   B CB  1 
ATOM   846  C CG  . PHE   B 1 13 ? 14.471  -16.532 -36.258 1.00 25.76  ? 12  PHE   B CG  1 
ATOM   847  C CD1 . PHE   B 1 13 ? 14.255  -16.190 -37.586 1.00 30.61  ? 12  PHE   B CD1 1 
ATOM   848  C CD2 . PHE   B 1 13 ? 13.579  -16.059 -35.289 1.00 27.49  ? 12  PHE   B CD2 1 
ATOM   849  C CE1 . PHE   B 1 13 ? 13.155  -15.417 -37.925 1.00 31.25  ? 12  PHE   B CE1 1 
ATOM   850  C CE2 . PHE   B 1 13 ? 12.469  -15.305 -35.646 1.00 30.18  ? 12  PHE   B CE2 1 
ATOM   851  C CZ  . PHE   B 1 13 ? 12.269  -14.976 -36.971 1.00 36.44  ? 12  PHE   B CZ  1 
ATOM   852  N N   . ALA   B 1 14 ? 18.230  -17.255 -33.689 1.00 25.86  ? 13  ALA   B N   1 
ATOM   853  C CA  . ALA   B 1 14 ? 19.284  -17.967 -33.012 1.00 24.70  ? 13  ALA   B CA  1 
ATOM   854  C C   . ALA   B 1 14 ? 18.678  -18.897 -31.960 1.00 25.89  ? 13  ALA   B C   1 
ATOM   855  O O   . ALA   B 1 14 ? 17.750  -18.516 -31.250 1.00 26.93  ? 13  ALA   B O   1 
ATOM   856  C CB  . ALA   B 1 14 ? 20.276  -17.009 -32.378 1.00 26.30  ? 13  ALA   B CB  1 
ATOM   857  N N   . LYS   B 1 15 ? 19.173  -20.119 -31.901 1.00 25.32  ? 14  LYS   B N   1 
ATOM   858  C CA  . LYS   B 1 15 ? 18.556  -21.131 -31.034 1.00 25.68  ? 14  LYS   B CA  1 
ATOM   859  C C   . LYS   B 1 15 ? 19.427  -21.420 -29.816 1.00 27.12  ? 14  LYS   B C   1 
ATOM   860  O O   . LYS   B 1 15 ? 20.607  -21.748 -29.933 1.00 28.64  ? 14  LYS   B O   1 
ATOM   861  C CB  . LYS   B 1 15 ? 18.373  -22.422 -31.849 1.00 30.40  ? 14  LYS   B CB  1 
ATOM   862  C CG  . LYS   B 1 15 ? 17.701  -23.530 -31.025 1.00 27.00  ? 14  LYS   B CG  1 
ATOM   863  C CD  . LYS   B 1 15 ? 16.260  -23.126 -30.707 1.00 31.16  ? 14  LYS   B CD  1 
ATOM   864  C CE  . LYS   B 1 15 ? 15.414  -24.251 -30.038 1.00 32.81  ? 14  LYS   B CE  1 
ATOM   865  N NZ  . LYS   B 1 15 ? 15.993  -24.520 -28.723 1.00 33.98  ? 14  LYS   B NZ  1 
ATOM   866  N N   . MET   B 1 16 ? 18.821  -21.238 -28.637 1.00 28.66  ? 15  MET   B N   1 
ATOM   867  C CA  . MET   B 1 16 ? 19.442  -21.604 -27.370 1.00 29.76  ? 15  MET   B CA  1 
ATOM   868  C C   . MET   B 1 16 ? 18.617  -22.714 -26.726 1.00 30.32  ? 15  MET   B C   1 
ATOM   869  O O   . MET   B 1 16 ? 17.395  -22.745 -26.851 1.00 30.40  ? 15  MET   B O   1 
ATOM   870  C CB  . MET   B 1 16 ? 19.507  -20.411 -26.421 1.00 33.28  ? 15  MET   B CB  1 
ATOM   871  C CG  . MET   B 1 16 ? 20.213  -19.232 -27.022 1.00 34.38  ? 15  MET   B CG  1 
ATOM   872  S SD  . MET   B 1 16 ? 21.987  -19.362 -26.740 1.00 42.48  ? 15  MET   B SD  1 
ATOM   873  C CE  . MET   B 1 16 ? 22.019  -18.914 -24.999 1.00 39.31  ? 15  MET   B CE  1 
ATOM   874  N N   . LYS   B 1 17 ? 19.305  -23.635 -26.044 1.00 31.61  ? 16  LYS   B N   1 
ATOM   875  C CA  . LYS   B 1 17 ? 18.570  -24.641 -25.291 1.00 32.20  ? 16  LYS   B CA  1 
ATOM   876  C C   . LYS   B 1 17 ? 17.613  -23.974 -24.297 1.00 30.42  ? 16  LYS   B C   1 
ATOM   877  O O   . LYS   B 1 17 ? 17.996  -23.047 -23.577 1.00 35.65  ? 16  LYS   B O   1 
ATOM   878  C CB  . LYS   B 1 17 ? 19.647  -25.373 -24.472 1.00 40.99  ? 16  LYS   B CB  1 
ATOM   879  C CG  . LYS   B 1 17 ? 19.223  -26.746 -23.924 1.00 48.69  ? 16  LYS   B CG  1 
ATOM   880  C CD  . LYS   B 1 17 ? 20.190  -27.247 -22.861 1.00 45.35  ? 16  LYS   B CD  1 
ATOM   881  N N   . GLY   B 1 18 ? 16.342  -24.404 -24.319 1.00 34.79  ? 17  GLY   B N   1 
ATOM   882  C CA  . GLY   B 1 18 ? 15.326  -23.901 -23.400 1.00 33.50  ? 17  GLY   B CA  1 
ATOM   883  C C   . GLY   B 1 18 ? 14.472  -22.756 -23.955 1.00 35.10  ? 17  GLY   B C   1 
ATOM   884  O O   . GLY   B 1 18 ? 13.519  -22.319 -23.298 1.00 32.53  ? 17  GLY   B O   1 
ATOM   885  N N   . TYR   B 1 19 ? 14.809  -22.265 -25.164 1.00 32.05  ? 18  TYR   B N   1 
ATOM   886  C CA  . TYR   B 1 19 ? 14.121  -21.096 -25.712 1.00 30.30  ? 18  TYR   B CA  1 
ATOM   887  C C   . TYR   B 1 19 ? 13.747  -21.358 -27.165 1.00 27.95  ? 18  TYR   B C   1 
ATOM   888  O O   . TYR   B 1 19 ? 14.454  -22.068 -27.862 1.00 29.94  ? 18  TYR   B O   1 
ATOM   889  C CB  . TYR   B 1 19 ? 15.074  -19.896 -25.745 1.00 28.85  ? 18  TYR   B CB  1 
ATOM   890  C CG  . TYR   B 1 19 ? 15.527  -19.559 -24.328 1.00 32.44  ? 18  TYR   B CG  1 
ATOM   891  C CD1 . TYR   B 1 19 ? 14.739  -18.754 -23.512 1.00 33.72  ? 18  TYR   B CD1 1 
ATOM   892  C CD2 . TYR   B 1 19 ? 16.675  -20.135 -23.791 1.00 34.67  ? 18  TYR   B CD2 1 
ATOM   893  C CE1 . TYR   B 1 19 ? 15.119  -18.501 -22.197 1.00 34.80  ? 18  TYR   B CE1 1 
ATOM   894  C CE2 . TYR   B 1 19 ? 17.069  -19.873 -22.481 1.00 39.61  ? 18  TYR   B CE2 1 
ATOM   895  C CZ  . TYR   B 1 19 ? 16.277  -19.057 -21.689 1.00 34.42  ? 18  TYR   B CZ  1 
ATOM   896  O OH  . TYR   B 1 19 ? 16.655  -18.774 -20.407 1.00 41.47  ? 18  TYR   B OH  1 
ATOM   897  N N   . PRO   B 1 20 ? 12.686  -20.698 -27.669 1.00 28.42  ? 19  PRO   B N   1 
ATOM   898  C CA  . PRO   B 1 20 ? 12.359  -20.813 -29.090 1.00 25.42  ? 19  PRO   B CA  1 
ATOM   899  C C   . PRO   B 1 20 ? 13.405  -20.095 -29.951 1.00 26.23  ? 19  PRO   B C   1 
ATOM   900  O O   . PRO   B 1 20 ? 14.106  -19.255 -29.441 1.00 27.37  ? 19  PRO   B O   1 
ATOM   901  C CB  . PRO   B 1 20 ? 11.015  -20.184 -29.205 1.00 27.70  ? 19  PRO   B CB  1 
ATOM   902  C CG  . PRO   B 1 20 ? 10.981  -19.164 -28.065 1.00 29.19  ? 19  PRO   B CG  1 
ATOM   903  C CD  . PRO   B 1 20 ? 11.762  -19.834 -26.911 1.00 26.65  ? 19  PRO   B CD  1 
ATOM   904  N N   . HIS   B 1 21 ? 13.547  -20.528 -31.215 1.00 25.40  ? 20  HIS   B N   1 
ATOM   905  C CA  . HIS   B 1 21 ? 14.360  -19.764 -32.176 1.00 27.81  ? 20  HIS   B CA  1 
ATOM   906  C C   . HIS   B 1 21 ? 14.095  -18.253 -32.047 1.00 25.92  ? 20  HIS   B C   1 
ATOM   907  O O   . HIS   B 1 21 ? 12.960  -17.821 -32.090 1.00 27.04  ? 20  HIS   B O   1 
ATOM   908  C CB  . HIS   B 1 21 ? 13.985  -20.264 -33.579 1.00 26.67  ? 20  HIS   B CB  1 
ATOM   909  C CG  . HIS   B 1 21 ? 14.335  -21.709 -33.801 1.00 28.24  ? 20  HIS   B CG  1 
ATOM   910  N ND1 . HIS   B 1 21 ? 13.484  -22.712 -33.356 1.00 29.90  ? 20  HIS   B ND1 1 
ATOM   911  C CD2 . HIS   B 1 21 ? 15.376  -22.324 -34.372 1.00 28.79  ? 20  HIS   B CD2 1 
ATOM   912  C CE1 . HIS   B 1 21 ? 13.999  -23.896 -33.676 1.00 30.35  ? 20  HIS   B CE1 1 
ATOM   913  N NE2 . HIS   B 1 21 ? 15.147  -23.697 -34.306 1.00 28.64  ? 20  HIS   B NE2 1 
ATOM   914  N N   . TRP   B 1 22 ? 15.152  -17.465 -31.849 1.00 26.31  ? 21  TRP   B N   1 
ATOM   915  C CA  . TRP   B 1 22 ? 14.934  -16.128 -31.277 1.00 25.71  ? 21  TRP   B CA  1 
ATOM   916  C C   . TRP   B 1 22 ? 15.467  -15.069 -32.245 1.00 23.56  ? 21  TRP   B C   1 
ATOM   917  O O   . TRP   B 1 22 ? 16.597  -15.220 -32.711 1.00 24.81  ? 21  TRP   B O   1 
ATOM   918  C CB  . TRP   B 1 22 ? 15.639  -15.995 -29.920 1.00 26.64  ? 21  TRP   B CB  1 
ATOM   919  C CG  . TRP   B 1 22 ? 15.125  -14.848 -29.081 1.00 26.92  ? 21  TRP   B CG  1 
ATOM   920  C CD1 . TRP   B 1 22 ? 15.414  -13.514 -29.215 1.00 24.65  ? 21  TRP   B CD1 1 
ATOM   921  C CD2 . TRP   B 1 22 ? 14.215  -14.947 -27.955 1.00 27.87  ? 21  TRP   B CD2 1 
ATOM   922  N NE1 . TRP   B 1 22 ? 14.700  -12.767 -28.289 1.00 26.78  ? 21  TRP   B NE1 1 
ATOM   923  C CE2 . TRP   B 1 22 ? 13.971  -13.627 -27.501 1.00 27.93  ? 21  TRP   B CE2 1 
ATOM   924  C CE3 . TRP   B 1 22 ? 13.583  -16.037 -27.322 1.00 27.36  ? 21  TRP   B CE3 1 
ATOM   925  C CZ2 . TRP   B 1 22 ? 13.107  -13.337 -26.434 1.00 27.09  ? 21  TRP   B CZ2 1 
ATOM   926  C CZ3 . TRP   B 1 22 ? 12.739  -15.748 -26.262 1.00 27.25  ? 21  TRP   B CZ3 1 
ATOM   927  C CH2 . TRP   B 1 22 ? 12.501  -14.431 -25.858 1.00 27.66  ? 21  TRP   B CH2 1 
ATOM   928  N N   . PRO   B 1 23 ? 14.728  -13.955 -32.515 1.00 25.76  ? 22  PRO   B N   1 
ATOM   929  C CA  . PRO   B 1 23 ? 15.229  -12.925 -33.455 1.00 24.48  ? 22  PRO   B CA  1 
ATOM   930  C C   . PRO   B 1 23 ? 16.522  -12.334 -32.919 1.00 26.65  ? 22  PRO   B C   1 
ATOM   931  O O   . PRO   B 1 23 ? 16.645  -11.969 -31.753 1.00 26.46  ? 22  PRO   B O   1 
ATOM   932  C CB  . PRO   B 1 23 ? 14.071  -11.902 -33.520 1.00 25.67  ? 22  PRO   B CB  1 
ATOM   933  C CG  . PRO   B 1 23 ? 13.333  -12.102 -32.171 1.00 25.88  ? 22  PRO   B CG  1 
ATOM   934  C CD  . PRO   B 1 23 ? 13.393  -13.632 -31.995 1.00 26.65  ? 22  PRO   B CD  1 
ATOM   935  N N   . ALA   B 1 24 ? 17.553  -12.265 -33.769 1.00 26.16  ? 23  ALA   B N   1 
ATOM   936  C CA  . ALA   B 1 24 ? 18.857  -11.899 -33.280 1.00 24.00  ? 23  ALA   B CA  1 
ATOM   937  C C   . ALA   B 1 24 ? 19.671  -11.355 -34.458 1.00 23.99  ? 23  ALA   B C   1 
ATOM   938  O O   . ALA   B 1 24 ? 19.205  -11.431 -35.579 1.00 26.69  ? 23  ALA   B O   1 
ATOM   939  C CB  . ALA   B 1 24 ? 19.544  -13.091 -32.613 1.00 27.26  ? 23  ALA   B CB  1 
ATOM   940  N N   . ARG   B 1 25 ? 20.851  -10.849 -34.120 1.00 27.95  ? 24  ARG   B N   1 
ATOM   941  C CA  . ARG   B 1 25 ? 21.803  -10.365 -35.120 1.00 28.63  ? 24  ARG   B CA  1 
ATOM   942  C C   . ARG   B 1 25 ? 23.209  -10.816 -34.759 1.00 29.82  ? 24  ARG   B C   1 
ATOM   943  O O   . ARG   B 1 25 ? 23.545  -11.071 -33.624 1.00 28.93  ? 24  ARG   B O   1 
ATOM   944  C CB  . ARG   B 1 25 ? 21.782  -8.839  -35.232 1.00 29.37  ? 24  ARG   B CB  1 
ATOM   945  C CG  . ARG   B 1 25 ? 22.355  -8.107  -34.027 1.00 27.14  ? 24  ARG   B CG  1 
ATOM   946  C CD  . ARG   B 1 25 ? 22.182  -6.596  -34.246 1.00 28.37  ? 24  ARG   B CD  1 
ATOM   947  N NE  . ARG   B 1 25 ? 22.784  -5.916  -33.099 1.00 28.90  ? 24  ARG   B NE  1 
ATOM   948  C CZ  . ARG   B 1 25 ? 22.491  -4.643  -32.758 1.00 29.91  ? 24  ARG   B CZ  1 
ATOM   949  N NH1 . ARG   B 1 25 ? 21.538  -3.982  -33.413 1.00 29.23  ? 24  ARG   B NH1 1 
ATOM   950  N NH2 . ARG   B 1 25 ? 23.132  -4.065  -31.746 1.00 31.46  ? 24  ARG   B NH2 1 
ATOM   951  N N   . ILE   B 1 26 ? 24.075  -10.932 -35.784 1.00 29.31  ? 25  ILE   B N   1 
ATOM   952  C CA  . ILE   B 1 26 ? 25.495  -11.074 -35.568 1.00 30.44  ? 25  ILE   B CA  1 
ATOM   953  C C   . ILE   B 1 26 ? 26.020  -9.674  -35.263 1.00 33.36  ? 25  ILE   B C   1 
ATOM   954  O O   . ILE   B 1 26 ? 25.702  -8.744  -35.998 1.00 34.05  ? 25  ILE   B O   1 
ATOM   955  C CB  . ILE   B 1 26 ? 26.156  -11.528 -36.886 1.00 33.66  ? 25  ILE   B CB  1 
ATOM   956  C CG1 . ILE   B 1 26 ? 25.418  -12.702 -37.543 1.00 35.49  ? 25  ILE   B CG1 1 
ATOM   957  C CG2 . ILE   B 1 26 ? 27.648  -11.799 -36.692 1.00 36.17  ? 25  ILE   B CG2 1 
ATOM   958  C CD1 . ILE   B 1 26 ? 25.401  -13.965 -36.705 1.00 34.96  ? 25  ILE   B CD1 1 
ATOM   959  N N   . ASP   B 1 27 ? 26.770  -9.588  -34.175 1.00 33.13  ? 26  ASP   B N   1 
ATOM   960  C CA  . ASP   B 1 27 ? 27.418  -8.370  -33.712 1.00 37.99  ? 26  ASP   B CA  1 
ATOM   961  C C   . ASP   B 1 27 ? 28.866  -8.345  -34.209 1.00 43.54  ? 26  ASP   B C   1 
ATOM   962  O O   . ASP   B 1 27 ? 29.368  -9.354  -34.684 1.00 46.43  ? 26  ASP   B O   1 
ATOM   963  C CB  . ASP   B 1 27 ? 27.336  -8.295  -32.200 1.00 35.56  ? 26  ASP   B CB  1 
ATOM   964  C CG  . ASP   B 1 27 ? 26.105  -7.597  -31.646 1.00 38.02  ? 26  ASP   B CG  1 
ATOM   965  O OD1 . ASP   B 1 27 ? 25.306  -7.077  -32.455 1.00 39.11  ? 26  ASP   B OD1 1 
ATOM   966  O OD2 . ASP   B 1 27 ? 25.977  -7.550  -30.394 1.00 39.10  ? 26  ASP   B OD2 1 
ATOM   967  N N   A ASP   B 1 28 ? 29.524  -7.190  -34.050 0.50 50.82  ? 27  ASP   B N   1 
ATOM   968  N N   B ASP   B 1 28 ? 29.534  -7.194  -34.058 0.50 51.17  ? 27  ASP   B N   1 
ATOM   969  C CA  A ASP   B 1 28 ? 30.892  -6.967  -34.494 0.50 54.43  ? 27  ASP   B CA  1 
ATOM   970  C CA  B ASP   B 1 28 ? 30.947  -7.056  -34.385 0.50 55.11  ? 27  ASP   B CA  1 
ATOM   971  C C   A ASP   B 1 28 ? 31.880  -7.700  -33.575 0.50 51.86  ? 27  ASP   B C   1 
ATOM   972  C C   B ASP   B 1 28 ? 31.816  -7.599  -33.244 0.50 51.25  ? 27  ASP   B C   1 
ATOM   973  O O   A ASP   B 1 28 ? 31.851  -7.427  -32.359 0.50 54.91  ? 27  ASP   B O   1 
ATOM   974  O O   B ASP   B 1 28 ? 31.430  -7.376  -32.079 0.50 55.40  ? 27  ASP   B O   1 
ATOM   975  C CB  A ASP   B 1 28 ? 31.193  -5.480  -34.574 0.50 54.05  ? 27  ASP   B CB  1 
ATOM   976  C CB  B ASP   B 1 28 ? 31.302  -5.619  -34.731 0.50 56.11  ? 27  ASP   B CB  1 
ATOM   977  C CG  A ASP   B 1 28 ? 30.383  -4.716  -35.609 0.50 51.64  ? 27  ASP   B CG  1 
ATOM   978  C CG  B ASP   B 1 28 ? 31.226  -5.279  -36.209 0.50 57.26  ? 27  ASP   B CG  1 
ATOM   979  O OD1 A ASP   B 1 28 ? 30.698  -4.847  -36.812 0.50 59.78  ? 27  ASP   B OD1 1 
ATOM   980  O OD1 B ASP   B 1 28 ? 32.132  -5.718  -36.953 0.50 49.86  ? 27  ASP   B OD1 1 
ATOM   981  O OD2 A ASP   B 1 28 ? 29.436  -4.008  -35.209 0.50 48.04  ? 27  ASP   B OD2 1 
ATOM   982  O OD2 B ASP   B 1 28 ? 30.253  -4.595  -36.603 0.50 62.86  ? 27  ASP   B OD2 1 
ATOM   983  N N   . VAL   B 1 34 ? 37.147  -9.857  -25.727 1.00 68.51  ? 33  VAL   B N   1 
ATOM   984  C CA  . VAL   B 1 34 ? 36.894  -11.314 -25.501 1.00 71.87  ? 33  VAL   B CA  1 
ATOM   985  C C   . VAL   B 1 34 ? 36.305  -11.883 -26.785 1.00 72.79  ? 33  VAL   B C   1 
ATOM   986  O O   . VAL   B 1 34 ? 35.087  -11.875 -26.955 1.00 81.38  ? 33  VAL   B O   1 
ATOM   987  C CB  . VAL   B 1 34 ? 35.963  -11.581 -24.299 1.00 69.96  ? 33  VAL   B CB  1 
ATOM   988  C CG1 . VAL   B 1 34 ? 34.793  -10.602 -24.252 1.00 63.17  ? 33  VAL   B CG1 1 
ATOM   989  C CG2 . VAL   B 1 34 ? 35.470  -13.029 -24.267 1.00 64.02  ? 33  VAL   B CG2 1 
ATOM   990  N N   . LYS   B 1 35 ? 37.179  -12.371 -27.674 1.00 74.80  ? 34  LYS   B N   1 
ATOM   991  C CA  . LYS   B 1 35 ? 36.771  -12.854 -28.988 1.00 66.31  ? 34  LYS   B CA  1 
ATOM   992  C C   . LYS   B 1 35 ? 35.896  -14.103 -28.844 1.00 60.43  ? 34  LYS   B C   1 
ATOM   993  O O   . LYS   B 1 35 ? 35.985  -14.828 -27.850 1.00 57.79  ? 34  LYS   B O   1 
ATOM   994  C CB  . LYS   B 1 35 ? 38.010  -13.069 -29.866 1.00 69.03  ? 34  LYS   B CB  1 
ATOM   995  N N   . PRO   B 1 36 ? 34.992  -14.397 -29.812 1.00 57.69  ? 35  PRO   B N   1 
ATOM   996  C CA  . PRO   B 1 36 ? 34.225  -15.645 -29.774 1.00 55.59  ? 35  PRO   B CA  1 
ATOM   997  C C   . PRO   B 1 36 ? 35.165  -16.841 -29.703 1.00 50.61  ? 35  PRO   B C   1 
ATOM   998  O O   . PRO   B 1 36 ? 36.299  -16.760 -30.164 1.00 54.83  ? 35  PRO   B O   1 
ATOM   999  C CB  . PRO   B 1 36 ? 33.443  -15.615 -31.096 1.00 54.15  ? 35  PRO   B CB  1 
ATOM   1000 C CG  . PRO   B 1 36 ? 34.180  -14.601 -31.951 1.00 59.27  ? 35  PRO   B CG  1 
ATOM   1001 C CD  . PRO   B 1 36 ? 34.648  -13.550 -30.965 1.00 54.11  ? 35  PRO   B CD  1 
ATOM   1002 N N   . PRO   B 1 37 ? 34.746  -17.989 -29.129 1.00 50.38  ? 36  PRO   B N   1 
ATOM   1003 C CA  . PRO   B 1 37 ? 35.514  -19.216 -29.308 1.00 48.05  ? 36  PRO   B CA  1 
ATOM   1004 C C   . PRO   B 1 37 ? 35.595  -19.540 -30.802 1.00 53.66  ? 36  PRO   B C   1 
ATOM   1005 O O   . PRO   B 1 37 ? 34.867  -18.969 -31.626 1.00 49.72  ? 36  PRO   B O   1 
ATOM   1006 C CB  . PRO   B 1 37 ? 34.737  -20.277 -28.516 1.00 52.58  ? 36  PRO   B CB  1 
ATOM   1007 C CG  . PRO   B 1 37 ? 33.825  -19.477 -27.606 1.00 55.05  ? 36  PRO   B CG  1 
ATOM   1008 C CD  . PRO   B 1 37 ? 33.534  -18.169 -28.314 1.00 51.08  ? 36  PRO   B CD  1 
ATOM   1009 N N   . PRO   B 1 38 ? 36.494  -20.473 -31.197 1.00 52.62  ? 37  PRO   B N   1 
ATOM   1010 C CA  . PRO   B 1 38 ? 36.560  -20.968 -32.582 1.00 53.83  ? 37  PRO   B CA  1 
ATOM   1011 C C   . PRO   B 1 38 ? 35.200  -21.339 -33.183 1.00 45.52  ? 37  PRO   B C   1 
ATOM   1012 O O   . PRO   B 1 38 ? 34.420  -22.038 -32.539 1.00 48.33  ? 37  PRO   B O   1 
ATOM   1013 C CB  . PRO   B 1 38 ? 37.453  -22.232 -32.415 1.00 49.40  ? 37  PRO   B CB  1 
ATOM   1014 C CG  . PRO   B 1 38 ? 38.362  -21.920 -31.238 1.00 49.28  ? 37  PRO   B CG  1 
ATOM   1015 C CD  . PRO   B 1 38 ? 37.505  -21.080 -30.309 1.00 58.48  ? 37  PRO   B CD  1 
ATOM   1016 N N   . ASN   B 1 39 ? 34.926  -20.883 -34.413 1.00 47.39  ? 38  ASN   B N   1 
ATOM   1017 C CA  . ASN   B 1 39 ? 33.757  -21.338 -35.166 1.00 50.79  ? 38  ASN   B CA  1 
ATOM   1018 C C   . ASN   B 1 39 ? 32.452  -20.672 -34.720 1.00 46.41  ? 38  ASN   B C   1 
ATOM   1019 O O   . ASN   B 1 39 ? 31.404  -20.938 -35.306 1.00 44.95  ? 38  ASN   B O   1 
ATOM   1020 C CB  . ASN   B 1 39 ? 33.537  -22.848 -35.057 1.00 51.45  ? 38  ASN   B CB  1 
ATOM   1021 C CG  . ASN   B 1 39 ? 34.759  -23.653 -35.441 1.00 60.96  ? 38  ASN   B CG  1 
ATOM   1022 O OD1 . ASN   B 1 39 ? 35.100  -24.627 -34.757 1.00 69.08  ? 38  ASN   B OD1 1 
ATOM   1023 N ND2 . ASN   B 1 39 ? 35.420  -23.281 -36.530 1.00 52.01  ? 38  ASN   B ND2 1 
ATOM   1024 N N   . LYS   B 1 40 ? 32.502  -19.816 -33.688 1.00 41.78  ? 39  LYS   B N   1 
ATOM   1025 C CA  . LYS   B 1 40 ? 31.292  -19.196 -33.172 1.00 36.19  ? 39  LYS   B CA  1 
ATOM   1026 C C   . LYS   B 1 40 ? 31.233  -17.706 -33.495 1.00 35.39  ? 39  LYS   B C   1 
ATOM   1027 O O   . LYS   B 1 40 ? 32.246  -17.114 -33.846 1.00 40.13  ? 39  LYS   B O   1 
ATOM   1028 C CB  . LYS   B 1 40 ? 31.302  -19.459 -31.669 1.00 40.79  ? 39  LYS   B CB  1 
ATOM   1029 C CG  . LYS   B 1 40 ? 31.029  -20.916 -31.365 1.00 44.07  ? 39  LYS   B CG  1 
ATOM   1030 C CD  . LYS   B 1 40 ? 30.667  -20.986 -29.885 1.00 53.96  ? 39  LYS   B CD  1 
ATOM   1031 C CE  . LYS   B 1 40 ? 29.726  -22.075 -29.498 1.00 65.88  ? 39  LYS   B CE  1 
ATOM   1032 N NZ  . LYS   B 1 40 ? 30.355  -23.387 -29.637 1.00 67.71  ? 39  LYS   B NZ  1 
ATOM   1033 N N   . TYR   B 1 41 ? 30.043  -17.114 -33.308 1.00 35.08  ? 40  TYR   B N   1 
ATOM   1034 C CA  . TYR   B 1 41 ? 29.801  -15.708 -33.589 1.00 34.37  ? 40  TYR   B CA  1 
ATOM   1035 C C   . TYR   B 1 41 ? 29.227  -15.037 -32.350 1.00 38.94  ? 40  TYR   B C   1 
ATOM   1036 O O   . TYR   B 1 41 ? 28.462  -15.645 -31.599 1.00 34.59  ? 40  TYR   B O   1 
ATOM   1037 C CB  . TYR   B 1 41 ? 28.784  -15.542 -34.723 1.00 33.94  ? 40  TYR   B CB  1 
ATOM   1038 C CG  . TYR   B 1 41 ? 29.283  -16.014 -36.080 1.00 36.39  ? 40  TYR   B CG  1 
ATOM   1039 C CD1 . TYR   B 1 41 ? 29.946  -15.150 -36.935 1.00 35.07  ? 40  TYR   B CD1 1 
ATOM   1040 C CD2 . TYR   B 1 41 ? 29.056  -17.316 -36.506 1.00 34.18  ? 40  TYR   B CD2 1 
ATOM   1041 C CE1 . TYR   B 1 41 ? 30.394  -15.579 -38.175 1.00 39.86  ? 40  TYR   B CE1 1 
ATOM   1042 C CE2 . TYR   B 1 41 ? 29.490  -17.760 -37.747 1.00 39.27  ? 40  TYR   B CE2 1 
ATOM   1043 C CZ  . TYR   B 1 41 ? 30.179  -16.885 -38.574 1.00 42.41  ? 40  TYR   B CZ  1 
ATOM   1044 O OH  . TYR   B 1 41 ? 30.621  -17.279 -39.808 1.00 38.35  ? 40  TYR   B OH  1 
ATOM   1045 N N   . PRO   B 1 42 ? 29.499  -13.728 -32.147 1.00 39.84  ? 41  PRO   B N   1 
ATOM   1046 C CA  . PRO   B 1 42 ? 28.802  -12.989 -31.094 1.00 34.06  ? 41  PRO   B CA  1 
ATOM   1047 C C   . PRO   B 1 42 ? 27.383  -12.687 -31.553 1.00 28.96  ? 41  PRO   B C   1 
ATOM   1048 O O   . PRO   B 1 42 ? 27.197  -12.030 -32.596 1.00 33.64  ? 41  PRO   B O   1 
ATOM   1049 C CB  . PRO   B 1 42 ? 29.636  -11.697 -30.953 1.00 36.59  ? 41  PRO   B CB  1 
ATOM   1050 C CG  . PRO   B 1 42 ? 30.315  -11.504 -32.311 1.00 37.50  ? 41  PRO   B CG  1 
ATOM   1051 C CD  . PRO   B 1 42 ? 30.416  -12.896 -32.946 1.00 37.63  ? 41  PRO   B CD  1 
ATOM   1052 N N   . ILE   B 1 43 ? 26.390  -13.139 -30.757 1.00 31.02  ? 42  ILE   B N   1 
ATOM   1053 C CA  . ILE   B 1 43 ? 24.975  -12.941 -31.061 1.00 29.32  ? 42  ILE   B CA  1 
ATOM   1054 C C   . ILE   B 1 43 ? 24.354  -11.942 -30.082 1.00 29.07  ? 42  ILE   B C   1 
ATOM   1055 O O   . ILE   B 1 43 ? 24.608  -12.052 -28.898 1.00 33.57  ? 42  ILE   B O   1 
ATOM   1056 C CB  . ILE   B 1 43 ? 24.222  -14.279 -31.003 1.00 29.57  ? 42  ILE   B CB  1 
ATOM   1057 C CG1 . ILE   B 1 43 ? 24.944  -15.361 -31.868 1.00 30.38  ? 42  ILE   B CG1 1 
ATOM   1058 C CG2 . ILE   B 1 43 ? 22.753  -14.109 -31.416 1.00 32.40  ? 42  ILE   B CG2 1 
ATOM   1059 C CD1 . ILE   B 1 43 ? 25.200  -14.972 -33.308 1.00 30.26  ? 42  ILE   B CD1 1 
ATOM   1060 N N   . PHE   B 1 44 ? 23.546  -11.024 -30.619 1.00 28.09  ? 43  PHE   B N   1 
ATOM   1061 C CA  . PHE   B 1 44 ? 22.664  -10.174 -29.831 1.00 30.28  ? 43  PHE   B CA  1 
ATOM   1062 C C   . PHE   B 1 44 ? 21.223  -10.619 -30.056 1.00 29.82  ? 43  PHE   B C   1 
ATOM   1063 O O   . PHE   B 1 44 ? 20.744  -10.682 -31.189 1.00 28.89  ? 43  PHE   B O   1 
ATOM   1064 C CB  . PHE   B 1 44 ? 22.925  -8.698  -30.202 1.00 31.61  ? 43  PHE   B CB  1 
ATOM   1065 C CG  . PHE   B 1 44 ? 21.969  -7.690  -29.575 1.00 36.33  ? 43  PHE   B CG  1 
ATOM   1066 C CD1 . PHE   B 1 44 ? 20.814  -7.290  -30.244 1.00 34.06  ? 43  PHE   B CD1 1 
ATOM   1067 C CD2 . PHE   B 1 44 ? 22.262  -7.093  -28.356 1.00 48.37  ? 43  PHE   B CD2 1 
ATOM   1068 C CE1 . PHE   B 1 44 ? 19.929  -6.383  -29.678 1.00 38.48  ? 43  PHE   B CE1 1 
ATOM   1069 C CE2 . PHE   B 1 44 ? 21.404  -6.138  -27.815 1.00 43.52  ? 43  PHE   B CE2 1 
ATOM   1070 C CZ  . PHE   B 1 44 ? 20.237  -5.803  -28.472 1.00 50.30  ? 43  PHE   B CZ  1 
ATOM   1071 N N   . PHE   B 1 45 ? 20.484  -10.830 -28.952 1.00 29.18  ? 44  PHE   B N   1 
ATOM   1072 C CA  . PHE   B 1 45 ? 19.112  -11.262 -29.023 1.00 27.41  ? 44  PHE   B CA  1 
ATOM   1073 C C   . PHE   B 1 45 ? 18.221  -10.055 -28.865 1.00 27.59  ? 44  PHE   B C   1 
ATOM   1074 O O   . PHE   B 1 45 ? 18.278  -9.348  -27.836 1.00 32.11  ? 44  PHE   B O   1 
ATOM   1075 C CB  . PHE   B 1 45 ? 18.840  -12.305 -27.925 1.00 28.86  ? 44  PHE   B CB  1 
ATOM   1076 C CG  . PHE   B 1 45 ? 19.619  -13.609 -28.052 1.00 26.75  ? 44  PHE   B CG  1 
ATOM   1077 C CD1 . PHE   B 1 45 ? 20.900  -13.724 -27.558 1.00 30.04  ? 44  PHE   B CD1 1 
ATOM   1078 C CD2 . PHE   B 1 45 ? 19.080  -14.706 -28.722 1.00 26.53  ? 44  PHE   B CD2 1 
ATOM   1079 C CE1 . PHE   B 1 45 ? 21.645  -14.893 -27.738 1.00 32.75  ? 44  PHE   B CE1 1 
ATOM   1080 C CE2 . PHE   B 1 45 ? 19.815  -15.886 -28.864 1.00 28.80  ? 44  PHE   B CE2 1 
ATOM   1081 C CZ  . PHE   B 1 45 ? 21.105  -15.984 -28.398 1.00 28.27  ? 44  PHE   B CZ  1 
ATOM   1082 N N   . PHE   B 1 46 ? 17.413  -9.800  -29.899 1.00 26.53  ? 45  PHE   B N   1 
ATOM   1083 C CA  . PHE   B 1 46 ? 16.535  -8.644  -29.857 1.00 26.82  ? 45  PHE   B CA  1 
ATOM   1084 C C   . PHE   B 1 46 ? 15.480  -8.823  -28.752 1.00 29.79  ? 45  PHE   B C   1 
ATOM   1085 O O   . PHE   B 1 46 ? 15.088  -9.934  -28.406 1.00 28.01  ? 45  PHE   B O   1 
ATOM   1086 C CB  . PHE   B 1 46 ? 15.842  -8.394  -31.199 1.00 26.32  ? 45  PHE   B CB  1 
ATOM   1087 C CG  . PHE   B 1 46 ? 16.787  -7.971  -32.311 1.00 28.34  ? 45  PHE   B CG  1 
ATOM   1088 C CD1 . PHE   B 1 46 ? 17.277  -6.664  -32.330 1.00 29.62  ? 45  PHE   B CD1 1 
ATOM   1089 C CD2 . PHE   B 1 46 ? 17.122  -8.851  -33.339 1.00 26.92  ? 45  PHE   B CD2 1 
ATOM   1090 C CE1 . PHE   B 1 46 ? 18.135  -6.242  -33.358 1.00 27.25  ? 45  PHE   B CE1 1 
ATOM   1091 C CE2 . PHE   B 1 46 ? 17.973  -8.428  -34.364 1.00 29.15  ? 45  PHE   B CE2 1 
ATOM   1092 C CZ  . PHE   B 1 46 ? 18.465  -7.121  -34.364 1.00 27.26  ? 45  PHE   B CZ  1 
ATOM   1093 N N   . GLY   B 1 47 ? 15.031  -7.700  -28.196 1.00 28.20  ? 46  GLY   B N   1 
ATOM   1094 C CA  . GLY   B 1 47 ? 14.007  -7.755  -27.149 1.00 28.37  ? 46  GLY   B CA  1 
ATOM   1095 C C   . GLY   B 1 47 ? 14.602  -7.886  -25.753 1.00 33.57  ? 46  GLY   B C   1 
ATOM   1096 O O   . GLY   B 1 47 ? 14.068  -7.301  -24.830 1.00 43.19  ? 46  GLY   B O   1 
ATOM   1097 N N   . THR   B 1 48 ? 15.645  -8.681  -25.581 1.00 31.63  ? 47  THR   B N   1 
ATOM   1098 C CA  . THR   B 1 48 ? 16.200  -9.038  -24.288 1.00 30.37  ? 47  THR   B CA  1 
ATOM   1099 C C   . THR   B 1 48 ? 17.467  -8.241  -24.065 1.00 34.64  ? 47  THR   B C   1 
ATOM   1100 O O   . THR   B 1 48 ? 18.032  -8.205  -22.961 1.00 33.27  ? 47  THR   B O   1 
ATOM   1101 C CB  . THR   B 1 48 ? 16.526  -10.535 -24.221 1.00 33.26  ? 47  THR   B CB  1 
ATOM   1102 O OG1 . THR   B 1 48 ? 17.623  -10.875 -25.077 1.00 32.21  ? 47  THR   B OG1 1 
ATOM   1103 C CG2 . THR   B 1 48 ? 15.310  -11.422 -24.417 1.00 36.09  ? 47  THR   B CG2 1 
ATOM   1104 N N   . HIS   B 1 49 ? 18.007  -7.855  -25.209 1.00 39.05  ? 48  HIS   B N   1 
ATOM   1105 C CA  . HIS   B 1 49 ? 19.357  -7.353  -25.356 1.00 48.30  ? 48  HIS   B CA  1 
ATOM   1106 C C   . HIS   B 1 49 ? 20.416  -8.262  -24.713 1.00 48.69  ? 48  HIS   B C   1 
ATOM   1107 O O   . HIS   B 1 49 ? 21.489  -7.763  -24.402 1.00 48.36  ? 48  HIS   B O   1 
ATOM   1108 C CB  . HIS   B 1 49 ? 19.320  -5.851  -25.052 1.00 43.72  ? 48  HIS   B CB  1 
ATOM   1109 C CG  . HIS   B 1 49 ? 18.095  -5.228  -25.648 1.00 42.26  ? 48  HIS   B CG  1 
ATOM   1110 N ND1 . HIS   B 1 49 ? 17.312  -4.355  -24.932 1.00 38.20  ? 48  HIS   B ND1 1 
ATOM   1111 C CD2 . HIS   B 1 49 ? 17.469  -5.374  -26.839 1.00 41.80  ? 48  HIS   B CD2 1 
ATOM   1112 C CE1 . HIS   B 1 49 ? 16.253  -3.994  -25.654 1.00 49.48  ? 48  HIS   B CE1 1 
ATOM   1113 N NE2 . HIS   B 1 49 ? 16.337  -4.584  -26.831 1.00 46.14  ? 48  HIS   B NE2 1 
ATOM   1114 N N   . GLU   B 1 50 ? 20.157  -9.577  -24.535 1.00 47.08  ? 49  GLU   B N   1 
ATOM   1115 C CA  . GLU   B 1 50 ? 21.171  -10.512 -24.047 1.00 41.72  ? 49  GLU   B CA  1 
ATOM   1116 C C   . GLU   B 1 50 ? 22.101  -10.944 -25.183 1.00 37.10  ? 49  GLU   B C   1 
ATOM   1117 O O   . GLU   B 1 50 ? 21.818  -10.677 -26.353 1.00 36.96  ? 49  GLU   B O   1 
ATOM   1118 C CB  . GLU   B 1 50 ? 20.598  -11.821 -23.524 1.00 42.77  ? 49  GLU   B CB  1 
ATOM   1119 C CG  . GLU   B 1 50 ? 19.823  -11.554 -22.242 1.00 48.12  ? 49  GLU   B CG  1 
ATOM   1120 C CD  . GLU   B 1 50 ? 19.321  -12.855 -21.672 1.00 49.66  ? 49  GLU   B CD  1 
ATOM   1121 O OE1 . GLU   B 1 50 ? 18.460  -13.445 -22.339 1.00 57.76  ? 49  GLU   B OE1 1 
ATOM   1122 O OE2 . GLU   B 1 50 ? 19.775  -13.271 -20.593 1.00 54.88  ? 49  GLU   B OE2 1 
ATOM   1123 N N   . THR   B 1 51 ? 23.245  -11.522 -24.804 1.00 33.19  ? 50  THR   B N   1 
ATOM   1124 C CA  . THR   B 1 51 ? 24.279  -11.903 -25.764 1.00 33.17  ? 50  THR   B CA  1 
ATOM   1125 C C   . THR   B 1 51 ? 24.784  -13.316 -25.461 1.00 36.02  ? 50  THR   B C   1 
ATOM   1126 O O   . THR   B 1 51 ? 24.651  -13.817 -24.347 1.00 35.97  ? 50  THR   B O   1 
ATOM   1127 C CB  . THR   B 1 51 ? 25.396  -10.859 -25.844 1.00 37.16  ? 50  THR   B CB  1 
ATOM   1128 O OG1 . THR   B 1 51 ? 25.959  -10.886 -24.540 1.00 39.91  ? 50  THR   B OG1 1 
ATOM   1129 C CG2 . THR   B 1 51 ? 24.926  -9.452  -26.193 1.00 34.27  ? 50  THR   B CG2 1 
ATOM   1130 N N   . ALA   B 1 52 ? 25.320  -14.003 -26.485 1.00 35.28  ? 51  ALA   B N   1 
ATOM   1131 C CA  . ALA   B 1 52 ? 25.930  -15.308 -26.304 1.00 36.54  ? 51  ALA   B CA  1 
ATOM   1132 C C   . ALA   B 1 52 ? 26.803  -15.567 -27.529 1.00 31.43  ? 51  ALA   B C   1 
ATOM   1133 O O   . ALA   B 1 52 ? 26.717  -14.820 -28.531 1.00 34.18  ? 51  ALA   B O   1 
ATOM   1134 C CB  . ALA   B 1 52 ? 24.872  -16.380 -26.130 1.00 35.21  ? 51  ALA   B CB  1 
ATOM   1135 N N   . PHE   B 1 53 ? 27.652  -16.596 -27.422 1.00 33.77  ? 52  PHE   B N   1 
ATOM   1136 C CA  . PHE   B 1 53 ? 28.400  -17.042 -28.587 1.00 36.42  ? 52  PHE   B CA  1 
ATOM   1137 C C   . PHE   B 1 53 ? 27.741  -18.320 -29.107 1.00 34.32  ? 52  PHE   B C   1 
ATOM   1138 O O   . PHE   B 1 53 ? 27.519  -19.246 -28.331 1.00 35.47  ? 52  PHE   B O   1 
ATOM   1139 C CB  . PHE   B 1 53 ? 29.868  -17.289 -28.215 1.00 34.11  ? 52  PHE   B CB  1 
ATOM   1140 C CG  . PHE   B 1 53 ? 30.636  -16.072 -27.722 1.00 41.17  ? 52  PHE   B CG  1 
ATOM   1141 C CD1 . PHE   B 1 53 ? 30.953  -15.045 -28.593 1.00 42.14  ? 52  PHE   B CD1 1 
ATOM   1142 C CD2 . PHE   B 1 53 ? 31.082  -15.998 -26.404 1.00 46.12  ? 52  PHE   B CD2 1 
ATOM   1143 C CE1 . PHE   B 1 53 ? 31.659  -13.936 -28.153 1.00 45.25  ? 52  PHE   B CE1 1 
ATOM   1144 C CE2 . PHE   B 1 53 ? 31.788  -14.890 -25.958 1.00 45.54  ? 52  PHE   B CE2 1 
ATOM   1145 C CZ  . PHE   B 1 53 ? 32.081  -13.868 -26.833 1.00 41.68  ? 52  PHE   B CZ  1 
ATOM   1146 N N   . LEU   B 1 54 ? 27.402  -18.348 -30.409 1.00 31.32  ? 53  LEU   B N   1 
ATOM   1147 C CA  . LEU   B 1 54 ? 26.766  -19.514 -31.009 1.00 30.89  ? 53  LEU   B CA  1 
ATOM   1148 C C   . LEU   B 1 54 ? 27.501  -19.889 -32.293 1.00 30.20  ? 53  LEU   B C   1 
ATOM   1149 O O   . LEU   B 1 54 ? 27.937  -18.995 -33.028 1.00 33.88  ? 53  LEU   B O   1 
ATOM   1150 C CB  . LEU   B 1 54 ? 25.302  -19.278 -31.371 1.00 30.94  ? 53  LEU   B CB  1 
ATOM   1151 C CG  . LEU   B 1 54 ? 24.319  -19.198 -30.196 1.00 31.09  ? 53  LEU   B CG  1 
ATOM   1152 C CD1 . LEU   B 1 54 ? 22.960  -18.749 -30.722 1.00 31.43  ? 53  LEU   B CD1 1 
ATOM   1153 C CD2 . LEU   B 1 54 ? 24.249  -20.569 -29.504 1.00 32.15  ? 53  LEU   B CD2 1 
ATOM   1154 N N   . GLY   B 1 55 ? 27.416  -21.175 -32.623 1.00 32.52  ? 54  GLY   B N   1 
ATOM   1155 C CA  . GLY   B 1 55 ? 27.928  -21.721 -33.877 1.00 29.72  ? 54  GLY   B CA  1 
ATOM   1156 C C   . GLY   B 1 55 ? 26.826  -21.774 -34.936 1.00 31.42  ? 54  GLY   B C   1 
ATOM   1157 O O   . GLY   B 1 55 ? 25.632  -21.695 -34.639 1.00 30.19  ? 54  GLY   B O   1 
ATOM   1158 N N   . PRO   B 1 56 ? 27.190  -21.897 -36.227 1.00 31.22  ? 55  PRO   B N   1 
ATOM   1159 C CA  . PRO   B 1 56 ? 26.212  -21.907 -37.302 1.00 28.94  ? 55  PRO   B CA  1 
ATOM   1160 C C   . PRO   B 1 56 ? 25.046  -22.878 -37.212 1.00 28.56  ? 55  PRO   B C   1 
ATOM   1161 O O   . PRO   B 1 56 ? 23.996  -22.599 -37.765 1.00 28.85  ? 55  PRO   B O   1 
ATOM   1162 C CB  . PRO   B 1 56 ? 27.106  -22.257 -38.519 1.00 31.53  ? 55  PRO   B CB  1 
ATOM   1163 C CG  . PRO   B 1 56 ? 28.487  -21.879 -38.158 1.00 36.33  ? 55  PRO   B CG  1 
ATOM   1164 C CD  . PRO   B 1 56 ? 28.576  -22.078 -36.683 1.00 34.83  ? 55  PRO   B CD  1 
ATOM   1165 N N   . LYS   B 1 57 ? 25.214  -24.019 -36.514 1.00 31.70  ? 56  LYS   B N   1 
ATOM   1166 C CA  . LYS   B 1 57 ? 24.133  -24.994 -36.458 1.00 31.58  ? 56  LYS   B CA  1 
ATOM   1167 C C   . LYS   B 1 57 ? 22.901  -24.391 -35.779 1.00 30.09  ? 56  LYS   B C   1 
ATOM   1168 O O   . LYS   B 1 57 ? 21.777  -24.866 -35.968 1.00 29.77  ? 56  LYS   B O   1 
ATOM   1169 C CB  . LYS   B 1 57 ? 24.578  -26.268 -35.715 1.00 34.15  ? 56  LYS   B CB  1 
ATOM   1170 C CG  . LYS   B 1 57 ? 24.671  -26.144 -34.210 1.00 38.00  ? 56  LYS   B CG  1 
ATOM   1171 C CD  . LYS   B 1 57 ? 24.698  -27.523 -33.549 1.00 44.13  ? 56  LYS   B CD  1 
ATOM   1172 C CE  . LYS   B 1 57 ? 25.135  -27.517 -32.098 1.00 45.63  ? 56  LYS   B CE  1 
ATOM   1173 N NZ  . LYS   B 1 57 ? 24.104  -26.995 -31.191 1.00 47.35  ? 56  LYS   B NZ  1 
ATOM   1174 N N   . ASP   B 1 58 ? 23.132  -23.313 -34.992 1.00 29.10  ? 57  ASP   B N   1 
ATOM   1175 C CA  . ASP   B 1 58 ? 22.088  -22.692 -34.194 1.00 30.14  ? 57  ASP   B CA  1 
ATOM   1176 C C   . ASP   B 1 58 ? 21.680  -21.330 -34.777 1.00 27.70  ? 57  ASP   B C   1 
ATOM   1177 O O   . ASP   B 1 58 ? 20.915  -20.592 -34.131 1.00 28.45  ? 57  ASP   B O   1 
ATOM   1178 C CB  . ASP   B 1 58 ? 22.545  -22.592 -32.745 1.00 32.85  ? 57  ASP   B CB  1 
ATOM   1179 C CG  . ASP   B 1 58 ? 22.576  -23.937 -32.018 1.00 36.41  ? 57  ASP   B CG  1 
ATOM   1180 O OD1 . ASP   B 1 58 ? 21.616  -24.710 -32.211 1.00 35.40  ? 57  ASP   B OD1 1 
ATOM   1181 O OD2 . ASP   B 1 58 ? 23.514  -24.177 -31.237 1.00 38.56  ? 57  ASP   B OD2 1 
ATOM   1182 N N   . LEU   B 1 59 ? 22.173  -21.029 -35.993 1.00 27.97  ? 58  LEU   B N   1 
ATOM   1183 C CA  . LEU   B 1 59 ? 21.929  -19.746 -36.643 1.00 26.54  ? 58  LEU   B CA  1 
ATOM   1184 C C   . LEU   B 1 59 ? 21.190  -19.923 -37.957 1.00 27.62  ? 58  LEU   B C   1 
ATOM   1185 O O   . LEU   B 1 59 ? 21.705  -20.574 -38.876 1.00 29.59  ? 58  LEU   B O   1 
ATOM   1186 C CB  . LEU   B 1 59 ? 23.254  -19.023 -36.840 1.00 27.07  ? 58  LEU   B CB  1 
ATOM   1187 C CG  . LEU   B 1 59 ? 24.047  -18.743 -35.568 1.00 26.33  ? 58  LEU   B CG  1 
ATOM   1188 C CD1 . LEU   B 1 59 ? 25.407  -18.132 -35.907 1.00 32.52  ? 58  LEU   B CD1 1 
ATOM   1189 C CD2 . LEU   B 1 59 ? 23.278  -17.857 -34.579 1.00 30.42  ? 58  LEU   B CD2 1 
ATOM   1190 N N   . PHE   B 1 60 ? 20.018  -19.328 -38.038 1.00 24.69  ? 59  PHE   B N   1 
ATOM   1191 C CA  . PHE   B 1 60 ? 19.093  -19.515 -39.149 1.00 25.29  ? 59  PHE   B CA  1 
ATOM   1192 C C   . PHE   B 1 60 ? 18.910  -18.160 -39.831 1.00 27.05  ? 59  PHE   B C   1 
ATOM   1193 O O   . PHE   B 1 60 ? 18.301  -17.245 -39.292 1.00 27.50  ? 59  PHE   B O   1 
ATOM   1194 C CB  . PHE   B 1 60 ? 17.749  -20.018 -38.603 1.00 25.82  ? 59  PHE   B CB  1 
ATOM   1195 C CG  . PHE   B 1 60 ? 17.832  -21.421 -37.980 1.00 25.52  ? 59  PHE   B CG  1 
ATOM   1196 C CD1 . PHE   B 1 60 ? 18.374  -21.590 -36.702 1.00 27.02  ? 59  PHE   B CD1 1 
ATOM   1197 C CD2 . PHE   B 1 60 ? 17.426  -22.533 -38.717 1.00 28.50  ? 59  PHE   B CD2 1 
ATOM   1198 C CE1 . PHE   B 1 60 ? 18.512  -22.871 -36.160 1.00 29.42  ? 59  PHE   B CE1 1 
ATOM   1199 C CE2 . PHE   B 1 60 ? 17.540  -23.807 -38.164 1.00 29.94  ? 59  PHE   B CE2 1 
ATOM   1200 C CZ  . PHE   B 1 60 ? 18.134  -23.970 -36.920 1.00 31.30  ? 59  PHE   B CZ  1 
ATOM   1201 N N   . PRO   B 1 61 ? 19.391  -17.960 -41.072 1.00 28.92  ? 60  PRO   B N   1 
ATOM   1202 C CA  . PRO   B 1 61 ? 19.152  -16.680 -41.758 1.00 30.82  ? 60  PRO   B CA  1 
ATOM   1203 C C   . PRO   B 1 61 ? 17.700  -16.192 -41.731 1.00 28.16  ? 60  PRO   B C   1 
ATOM   1204 O O   . PRO   B 1 61 ? 16.741  -16.930 -41.966 1.00 28.51  ? 60  PRO   B O   1 
ATOM   1205 C CB  . PRO   B 1 61 ? 19.730  -16.954 -43.162 1.00 30.20  ? 60  PRO   B CB  1 
ATOM   1206 C CG  . PRO   B 1 61 ? 20.807  -17.998 -42.936 1.00 37.12  ? 60  PRO   B CG  1 
ATOM   1207 C CD  . PRO   B 1 61 ? 20.214  -18.912 -41.851 1.00 31.08  ? 60  PRO   B CD  1 
ATOM   1208 N N   . TYR   B 1 62 ? 17.513  -14.883 -41.405 1.00 29.75  ? 61  TYR   B N   1 
ATOM   1209 C CA  . TYR   B 1 62 ? 16.222  -14.391 -41.001 1.00 29.24  ? 61  TYR   B CA  1 
ATOM   1210 C C   . TYR   B 1 62 ? 15.254  -14.402 -42.164 1.00 29.21  ? 61  TYR   B C   1 
ATOM   1211 O O   . TYR   B 1 62 ? 14.100  -14.778 -41.985 1.00 32.57  ? 61  TYR   B O   1 
ATOM   1212 C CB  . TYR   B 1 62 ? 16.417  -12.945 -40.504 1.00 33.79  ? 61  TYR   B CB  1 
ATOM   1213 C CG  . TYR   B 1 62 ? 15.102  -12.223 -40.272 1.00 34.92  ? 61  TYR   B CG  1 
ATOM   1214 C CD1 . TYR   B 1 62 ? 14.367  -12.467 -39.128 1.00 33.51  ? 61  TYR   B CD1 1 
ATOM   1215 C CD2 . TYR   B 1 62 ? 14.643  -11.260 -41.168 1.00 39.23  ? 61  TYR   B CD2 1 
ATOM   1216 C CE1 . TYR   B 1 62 ? 13.186  -11.792 -38.893 1.00 35.44  ? 61  TYR   B CE1 1 
ATOM   1217 C CE2 . TYR   B 1 62 ? 13.462  -10.572 -40.945 1.00 43.60  ? 61  TYR   B CE2 1 
ATOM   1218 C CZ  . TYR   B 1 62 ? 12.735  -10.858 -39.807 1.00 39.93  ? 61  TYR   B CZ  1 
ATOM   1219 O OH  . TYR   B 1 62 ? 11.586  -10.213 -39.549 1.00 40.69  ? 61  TYR   B OH  1 
ATOM   1220 N N   . ASP   B 1 63 ? 15.758  -13.995 -43.356 1.00 34.15  ? 62  ASP   B N   1 
ATOM   1221 C CA  . ASP   B 1 63 ? 14.896  -13.963 -44.539 1.00 40.72  ? 62  ASP   B CA  1 
ATOM   1222 C C   . ASP   B 1 63 ? 14.307  -15.340 -44.867 1.00 35.43  ? 62  ASP   B C   1 
ATOM   1223 O O   . ASP   B 1 63 ? 13.099  -15.494 -45.046 1.00 41.26  ? 62  ASP   B O   1 
ATOM   1224 C CB  . ASP   B 1 63 ? 15.613  -13.311 -45.709 1.00 46.51  ? 62  ASP   B CB  1 
ATOM   1225 C CG  . ASP   B 1 63 ? 15.289  -11.838 -45.898 1.00 61.03  ? 62  ASP   B CG  1 
ATOM   1226 O OD1 . ASP   B 1 63 ? 14.589  -11.270 -45.027 1.00 62.31  ? 62  ASP   B OD1 1 
ATOM   1227 O OD2 . ASP   B 1 63 ? 15.711  -11.278 -46.932 1.00 74.66  ? 62  ASP   B OD2 1 
ATOM   1228 N N   . LYS   B 1 64 ? 15.178  -16.341 -44.910 1.00 38.17  ? 63  LYS   B N   1 
ATOM   1229 C CA  . LYS   B 1 64 ? 14.777  -17.708 -45.196 1.00 37.89  ? 63  LYS   B CA  1 
ATOM   1230 C C   . LYS   B 1 64 ? 13.791  -18.225 -44.144 1.00 34.79  ? 63  LYS   B C   1 
ATOM   1231 O O   . LYS   B 1 64 ? 12.824  -18.921 -44.490 1.00 39.73  ? 63  LYS   B O   1 
ATOM   1232 C CB  . LYS   B 1 64 ? 16.014  -18.601 -45.285 1.00 43.06  ? 63  LYS   B CB  1 
ATOM   1233 C CG  . LYS   B 1 64 ? 15.700  -20.000 -45.805 1.00 40.18  ? 63  LYS   B CG  1 
ATOM   1234 C CD  . LYS   B 1 64 ? 16.916  -20.905 -45.741 1.00 48.28  ? 63  LYS   B CD  1 
ATOM   1235 C CE  . LYS   B 1 64 ? 16.708  -22.278 -46.352 1.00 50.18  ? 63  LYS   B CE  1 
ATOM   1236 N NZ  . LYS   B 1 64 ? 15.415  -22.888 -46.034 1.00 48.23  ? 63  LYS   B NZ  1 
ATOM   1237 N N   . SER   B 1 65 ? 14.018  -17.860 -42.869 1.00 36.11  ? 64  SER   B N   1 
ATOM   1238 C CA  . SER   B 1 65 ? 13.332  -18.589 -41.793 1.00 34.88  ? 64  SER   B CA  1 
ATOM   1239 C C   . SER   B 1 65 ? 12.203  -17.808 -41.095 1.00 34.46  ? 64  SER   B C   1 
ATOM   1240 O O   . SER   B 1 65 ? 11.569  -18.326 -40.185 1.00 34.09  ? 64  SER   B O   1 
ATOM   1241 C CB  . SER   B 1 65 ? 14.333  -19.118 -40.825 1.00 38.13  ? 64  SER   B CB  1 
ATOM   1242 O OG  . SER   B 1 65 ? 14.975  -18.051 -40.151 1.00 48.87  ? 64  SER   B OG  1 
ATOM   1243 N N   . LYS   B 1 66 ? 11.877  -16.595 -41.546 1.00 34.45  ? 65  LYS   B N   1 
ATOM   1244 C CA  . LYS   B 1 66 ? 10.957  -15.746 -40.794 1.00 34.95  ? 65  LYS   B CA  1 
ATOM   1245 C C   . LYS   B 1 66 ? 9.503   -16.225 -40.799 1.00 37.81  ? 65  LYS   B C   1 
ATOM   1246 O O   . LYS   B 1 66 ? 8.763   -15.959 -39.859 1.00 40.82  ? 65  LYS   B O   1 
ATOM   1247 C CB  . LYS   B 1 66 ? 11.104  -14.255 -41.124 1.00 36.90  ? 65  LYS   B CB  1 
ATOM   1248 C CG  . LYS   B 1 66 ? 10.702  -13.939 -42.571 1.00 39.31  ? 65  LYS   B CG  1 
ATOM   1249 N N   . ASP   B 1 67 ? 9.033   -16.925 -41.828 1.00 37.80  ? 66  ASP   B N   1 
ATOM   1250 C CA  . ASP   B 1 67 ? 7.636   -17.304 -41.710 1.00 42.10  ? 66  ASP   B CA  1 
ATOM   1251 C C   . ASP   B 1 67 ? 7.495   -18.575 -40.863 1.00 43.19  ? 66  ASP   B C   1 
ATOM   1252 O O   . ASP   B 1 67 ? 6.417   -18.851 -40.319 1.00 48.73  ? 66  ASP   B O   1 
ATOM   1253 C CB  . ASP   B 1 67 ? 6.893   -17.201 -43.033 1.00 59.04  ? 66  ASP   B CB  1 
ATOM   1254 C CG  . ASP   B 1 67 ? 7.300   -18.219 -44.080 1.00 70.58  ? 66  ASP   B CG  1 
ATOM   1255 O OD1 . ASP   B 1 67 ? 6.910   -18.038 -45.255 1.00 74.44  ? 66  ASP   B OD1 1 
ATOM   1256 O OD2 . ASP   B 1 67 ? 7.986   -19.188 -43.700 1.00 79.18  ? 66  ASP   B OD2 1 
ATOM   1257 N N   . LYS   B 1 68 ? 8.607   -19.297 -40.686 1.00 40.91  ? 67  LYS   B N   1 
ATOM   1258 C CA  . LYS   B 1 68 ? 8.620   -20.455 -39.805 1.00 34.18  ? 67  LYS   B CA  1 
ATOM   1259 C C   . LYS   B 1 68 ? 8.780   -20.034 -38.343 1.00 33.44  ? 67  LYS   B C   1 
ATOM   1260 O O   . LYS   B 1 68 ? 8.013   -20.510 -37.505 1.00 33.76  ? 67  LYS   B O   1 
ATOM   1261 C CB  . LYS   B 1 68 ? 9.698   -21.455 -40.230 1.00 37.48  ? 67  LYS   B CB  1 
ATOM   1262 C CG  . LYS   B 1 68 ? 9.739   -22.737 -39.394 1.00 42.74  ? 67  LYS   B CG  1 
ATOM   1263 C CD  . LYS   B 1 68 ? 10.821  -23.660 -39.947 1.00 46.43  ? 67  LYS   B CD  1 
ATOM   1264 C CE  . LYS   B 1 68 ? 10.959  -24.962 -39.205 1.00 52.49  ? 67  LYS   B CE  1 
ATOM   1265 N NZ  . LYS   B 1 68 ? 9.804   -25.825 -39.441 1.00 54.65  ? 67  LYS   B NZ  1 
ATOM   1266 N N   . TYR   B 1 69 ? 9.734   -19.131 -38.042 1.00 31.40  ? 68  TYR   B N   1 
ATOM   1267 C CA  . TYR   B 1 69 ? 10.109  -18.852 -36.651 1.00 28.11  ? 68  TYR   B CA  1 
ATOM   1268 C C   . TYR   B 1 69 ? 9.581   -17.508 -36.151 1.00 36.23  ? 68  TYR   B C   1 
ATOM   1269 O O   . TYR   B 1 69 ? 9.680   -17.243 -34.947 1.00 34.97  ? 68  TYR   B O   1 
ATOM   1270 C CB  . TYR   B 1 69 ? 11.634  -18.890 -36.475 1.00 28.45  ? 68  TYR   B CB  1 
ATOM   1271 C CG  . TYR   B 1 69 ? 12.242  -20.264 -36.741 1.00 29.95  ? 68  TYR   B CG  1 
ATOM   1272 C CD1 . TYR   B 1 69 ? 11.728  -21.421 -36.164 1.00 30.05  ? 68  TYR   B CD1 1 
ATOM   1273 C CD2 . TYR   B 1 69 ? 13.332  -20.398 -37.590 1.00 29.78  ? 68  TYR   B CD2 1 
ATOM   1274 C CE1 . TYR   B 1 69 ? 12.271  -22.678 -36.427 1.00 29.82  ? 68  TYR   B CE1 1 
ATOM   1275 C CE2 . TYR   B 1 69 ? 13.889  -21.641 -37.868 1.00 34.66  ? 68  TYR   B CE2 1 
ATOM   1276 C CZ  . TYR   B 1 69 ? 13.370  -22.780 -37.264 1.00 32.59  ? 68  TYR   B CZ  1 
ATOM   1277 O OH  . TYR   B 1 69 ? 13.915  -23.999 -37.580 1.00 36.07  ? 68  TYR   B OH  1 
ATOM   1278 N N   . GLY   B 1 70 ? 9.074   -16.647 -37.055 1.00 36.13  ? 69  GLY   B N   1 
ATOM   1279 C CA  . GLY   B 1 70 ? 8.840   -15.262 -36.662 1.00 38.88  ? 69  GLY   B CA  1 
ATOM   1280 C C   . GLY   B 1 70 ? 7.422   -15.011 -36.142 1.00 44.44  ? 69  GLY   B C   1 
ATOM   1281 O O   . GLY   B 1 70 ? 6.848   -13.957 -36.419 1.00 43.79  ? 69  GLY   B O   1 
ATOM   1282 N N   . LYS   B 1 71 ? 6.877   -15.975 -35.383 1.00 43.37  ? 70  LYS   B N   1 
ATOM   1283 C CA  . LYS   B 1 71 ? 5.517   -15.890 -34.880 1.00 48.39  ? 70  LYS   B CA  1 
ATOM   1284 C C   . LYS   B 1 71 ? 5.580   -15.430 -33.437 1.00 48.44  ? 70  LYS   B C   1 
ATOM   1285 O O   . LYS   B 1 71 ? 6.484   -15.848 -32.709 1.00 41.74  ? 70  LYS   B O   1 
ATOM   1286 C CB  . LYS   B 1 71 ? 4.813   -17.252 -34.784 1.00 49.79  ? 70  LYS   B CB  1 
ATOM   1287 C CG  . LYS   B 1 71 ? 3.919   -17.679 -35.958 1.00 63.74  ? 70  LYS   B CG  1 
ATOM   1288 C CD  . LYS   B 1 71 ? 4.616   -17.815 -37.306 1.00 60.16  ? 70  LYS   B CD  1 
ATOM   1289 C CE  . LYS   B 1 71 ? 3.694   -18.091 -38.471 1.00 62.36  ? 70  LYS   B CE  1 
ATOM   1290 N NZ  . LYS   B 1 71 ? 4.301   -17.607 -39.719 1.00 62.36  ? 70  LYS   B NZ  1 
ATOM   1291 N N   . PRO   B 1 72 ? 4.650   -14.554 -32.983 1.00 48.37  ? 71  PRO   B N   1 
ATOM   1292 C CA  . PRO   B 1 72 ? 4.607   -14.186 -31.569 1.00 47.06  ? 71  PRO   B CA  1 
ATOM   1293 C C   . PRO   B 1 72 ? 4.368   -15.375 -30.639 1.00 42.99  ? 71  PRO   B C   1 
ATOM   1294 O O   . PRO   B 1 72 ? 3.754   -16.372 -31.019 1.00 42.37  ? 71  PRO   B O   1 
ATOM   1295 C CB  . PRO   B 1 72 ? 3.519   -13.107 -31.466 1.00 45.93  ? 71  PRO   B CB  1 
ATOM   1296 C CG  . PRO   B 1 72 ? 3.360   -12.617 -32.890 1.00 50.69  ? 71  PRO   B CG  1 
ATOM   1297 C CD  . PRO   B 1 72 ? 3.687   -13.800 -33.805 1.00 47.44  ? 71  PRO   B CD  1 
ATOM   1298 N N   . ASN   B 1 73 ? 4.892   -15.253 -29.409 1.00 40.99  ? 72  ASN   B N   1 
ATOM   1299 C CA  . ASN   B 1 73 ? 4.681   -16.246 -28.366 1.00 38.72  ? 72  ASN   B CA  1 
ATOM   1300 C C   . ASN   B 1 73 ? 4.634   -15.497 -27.028 1.00 44.24  ? 72  ASN   B C   1 
ATOM   1301 O O   . ASN   B 1 73 ? 4.662   -14.262 -26.995 1.00 49.84  ? 72  ASN   B O   1 
ATOM   1302 C CB  . ASN   B 1 73 ? 5.732   -17.359 -28.391 1.00 40.34  ? 72  ASN   B CB  1 
ATOM   1303 C CG  . ASN   B 1 73 ? 7.140   -16.872 -28.123 1.00 36.68  ? 72  ASN   B CG  1 
ATOM   1304 O OD1 . ASN   B 1 73 ? 7.373   -16.140 -27.152 1.00 34.50  ? 72  ASN   B OD1 1 
ATOM   1305 N ND2 . ASN   B 1 73 ? 8.101   -17.268 -28.960 1.00 31.27  ? 72  ASN   B ND2 1 
ATOM   1306 N N   . LYS   B 1 74 ? 4.647   -16.240 -25.924 1.00 41.98  ? 73  LYS   B N   1 
ATOM   1307 C CA  . LYS   B 1 74 ? 4.516   -15.605 -24.616 1.00 48.47  ? 73  LYS   B CA  1 
ATOM   1308 C C   . LYS   B 1 74 ? 5.817   -15.626 -23.799 1.00 45.84  ? 73  LYS   B C   1 
ATOM   1309 O O   . LYS   B 1 74 ? 5.781   -15.502 -22.566 1.00 41.61  ? 73  LYS   B O   1 
ATOM   1310 C CB  . LYS   B 1 74 ? 3.420   -16.349 -23.846 1.00 47.61  ? 73  LYS   B CB  1 
ATOM   1311 C CG  . LYS   B 1 74 ? 3.757   -17.814 -23.584 1.00 59.20  ? 73  LYS   B CG  1 
ATOM   1312 C CD  . LYS   B 1 74 ? 2.601   -18.567 -22.931 1.00 69.61  ? 73  LYS   B CD  1 
ATOM   1313 C CE  . LYS   B 1 74 ? 1.409   -18.718 -23.818 1.00 73.24  ? 73  LYS   B CE  1 
ATOM   1314 N NZ  . LYS   B 1 74 ? 0.302   -19.376 -23.120 1.00 74.33  ? 73  LYS   B NZ  1 
ATOM   1315 N N   . ARG   B 1 75 ? 6.968   -15.795 -24.465 1.00 32.98  ? 74  ARG   B N   1 
ATOM   1316 C CA  . ARG   B 1 75 ? 8.251   -15.594 -23.794 1.00 32.50  ? 74  ARG   B CA  1 
ATOM   1317 C C   . ARG   B 1 75 ? 8.545   -14.090 -23.690 1.00 33.13  ? 74  ARG   B C   1 
ATOM   1318 O O   . ARG   B 1 75 ? 8.342   -13.307 -24.629 1.00 34.35  ? 74  ARG   B O   1 
ATOM   1319 C CB  . ARG   B 1 75 ? 9.414   -16.364 -24.453 1.00 32.03  ? 74  ARG   B CB  1 
ATOM   1320 C CG  . ARG   B 1 75 ? 9.274   -17.867 -24.652 1.00 29.20  ? 74  ARG   B CG  1 
ATOM   1321 C CD  . ARG   B 1 75 ? 9.061   -18.596 -23.324 1.00 32.56  ? 74  ARG   B CD  1 
ATOM   1322 N NE  . ARG   B 1 75 ? 9.335   -20.025 -23.553 1.00 32.13  ? 74  ARG   B NE  1 
ATOM   1323 C CZ  . ARG   B 1 75 ? 10.477  -20.651 -23.356 1.00 32.01  ? 74  ARG   B CZ  1 
ATOM   1324 N NH1 . ARG   B 1 75 ? 11.547  -19.996 -22.925 1.00 37.46  ? 74  ARG   B NH1 1 
ATOM   1325 N NH2 . ARG   B 1 75 ? 10.580  -21.934 -23.657 1.00 35.65  ? 74  ARG   B NH2 1 
ATOM   1326 N N   . LYS   B 1 76 ? 8.979   -13.654 -22.494 1.00 28.29  ? 75  LYS   B N   1 
ATOM   1327 C CA  . LYS   B 1 76 ? 9.286   -12.264 -22.245 1.00 26.68  ? 75  LYS   B CA  1 
ATOM   1328 C C   . LYS   B 1 76 ? 10.402  -11.778 -23.193 1.00 27.50  ? 75  LYS   B C   1 
ATOM   1329 O O   . LYS   B 1 76 ? 11.481  -12.365 -23.226 1.00 30.26  ? 75  LYS   B O   1 
ATOM   1330 C CB  . LYS   B 1 76 ? 9.719   -12.098 -20.774 1.00 31.11  ? 75  LYS   B CB  1 
ATOM   1331 C CG  . LYS   B 1 76 ? 10.102  -10.681 -20.411 1.00 32.80  ? 75  LYS   B CG  1 
ATOM   1332 C CD  . LYS   B 1 76 ? 10.658  -10.623 -18.996 1.00 35.10  ? 75  LYS   B CD  1 
ATOM   1333 C CE  . LYS   B 1 76 ? 10.949  -9.211  -18.572 1.00 41.40  ? 75  LYS   B CE  1 
ATOM   1334 N NZ  . LYS   B 1 76 ? 11.258  -9.150  -17.137 1.00 48.06  ? 75  LYS   B NZ  1 
ATOM   1335 N N   . GLY   B 1 77 ? 10.062  -10.692 -23.902 1.00 28.58  ? 76  GLY   B N   1 
ATOM   1336 C CA  . GLY   B 1 77 ? 11.010  -10.002 -24.783 1.00 27.28  ? 76  GLY   B CA  1 
ATOM   1337 C C   . GLY   B 1 77 ? 10.854  -10.476 -26.226 1.00 31.87  ? 76  GLY   B C   1 
ATOM   1338 O O   . GLY   B 1 77 ? 11.443  -9.883  -27.121 1.00 28.67  ? 76  GLY   B O   1 
ATOM   1339 N N   . PHE   B 1 78 ? 10.109  -11.557 -26.466 1.00 31.08  ? 77  PHE   B N   1 
ATOM   1340 C CA  . PHE   B 1 78 ? 10.029  -12.101 -27.834 1.00 28.67  ? 77  PHE   B CA  1 
ATOM   1341 C C   . PHE   B 1 78 ? 9.321   -11.156 -28.813 1.00 31.54  ? 77  PHE   B C   1 
ATOM   1342 O O   . PHE   B 1 78 ? 9.836   -10.893 -29.912 1.00 29.40  ? 77  PHE   B O   1 
ATOM   1343 C CB  . PHE   B 1 78 ? 9.323   -13.454 -27.890 1.00 29.02  ? 77  PHE   B CB  1 
ATOM   1344 C CG  . PHE   B 1 78 ? 9.610   -14.212 -29.172 1.00 27.81  ? 77  PHE   B CG  1 
ATOM   1345 C CD1 . PHE   B 1 78 ? 10.741  -15.016 -29.226 1.00 26.49  ? 77  PHE   B CD1 1 
ATOM   1346 C CD2 . PHE   B 1 78 ? 8.723   -14.158 -30.244 1.00 33.31  ? 77  PHE   B CD2 1 
ATOM   1347 C CE1 . PHE   B 1 78 ? 11.017  -15.743 -30.387 1.00 27.25  ? 77  PHE   B CE1 1 
ATOM   1348 C CE2 . PHE   B 1 78 ? 8.996   -14.892 -31.405 1.00 31.42  ? 77  PHE   B CE2 1 
ATOM   1349 C CZ  . PHE   B 1 78 ? 10.145  -15.683 -31.450 1.00 28.39  ? 77  PHE   B CZ  1 
ATOM   1350 N N   . ASN   B 1 79 ? 8.124   -10.660 -28.486 1.00 29.21  ? 78  ASN   B N   1 
ATOM   1351 C CA  . ASN   B 1 79 ? 7.402   -9.783  -29.397 1.00 32.53  ? 78  ASN   B CA  1 
ATOM   1352 C C   . ASN   B 1 79 ? 8.162   -8.461  -29.585 1.00 33.37  ? 78  ASN   B C   1 
ATOM   1353 O O   . ASN   B 1 79 ? 8.204   -7.929  -30.689 1.00 33.16  ? 78  ASN   B O   1 
ATOM   1354 C CB  . ASN   B 1 79 ? 5.924   -9.661  -29.031 1.00 35.59  ? 78  ASN   B CB  1 
ATOM   1355 C CG  . ASN   B 1 79 ? 5.247   -11.015 -29.005 1.00 42.01  ? 78  ASN   B CG  1 
ATOM   1356 O OD1 . ASN   B 1 79 ? 5.772   -12.000 -29.541 1.00 39.74  ? 78  ASN   B OD1 1 
ATOM   1357 N ND2 . ASN   B 1 79 ? 4.135   -11.112 -28.299 1.00 41.34  ? 78  ASN   B ND2 1 
ATOM   1358 N N   . GLU   B 1 80 ? 8.788   -7.952  -28.529 1.00 29.54  ? 79  GLU   B N   1 
ATOM   1359 C CA  . GLU   B 1 80 ? 9.596   -6.753  -28.670 1.00 33.25  ? 79  GLU   B CA  1 
ATOM   1360 C C   . GLU   B 1 80 ? 10.728  -7.047  -29.648 1.00 29.20  ? 79  GLU   B C   1 
ATOM   1361 O O   . GLU   B 1 80 ? 11.024  -6.194  -30.491 1.00 29.72  ? 79  GLU   B O   1 
ATOM   1362 C CB  . GLU   B 1 80 ? 10.223  -6.274  -27.366 1.00 35.69  ? 79  GLU   B CB  1 
ATOM   1363 C CG  . GLU   B 1 80 ? 9.212   -5.517  -26.512 1.00 47.97  ? 79  GLU   B CG  1 
ATOM   1364 N N   . GLY   B 1 81 ? 11.301  -8.255  -29.514 1.00 27.86  ? 80  GLY   B N   1 
ATOM   1365 C CA  . GLY   B 1 81 ? 12.416  -8.685  -30.356 1.00 27.89  ? 80  GLY   B CA  1 
ATOM   1366 C C   . GLY   B 1 81 ? 11.972  -8.769  -31.809 1.00 29.63  ? 80  GLY   B C   1 
ATOM   1367 O O   . GLY   B 1 81 ? 12.757  -8.413  -32.703 1.00 27.15  ? 80  GLY   B O   1 
ATOM   1368 N N   . LEU   B 1 82 ? 10.738  -9.211  -32.043 1.00 26.28  ? 81  LEU   B N   1 
ATOM   1369 C CA  . LEU   B 1 82 ? 10.236  -9.273  -33.408 1.00 30.06  ? 81  LEU   B CA  1 
ATOM   1370 C C   . LEU   B 1 82 ? 10.090  -7.857  -33.960 1.00 31.02  ? 81  LEU   B C   1 
ATOM   1371 O O   . LEU   B 1 82 ? 10.294  -7.646  -35.152 1.00 30.27  ? 81  LEU   B O   1 
ATOM   1372 C CB  . LEU   B 1 82 ? 8.903   -10.030 -33.502 1.00 29.34  ? 81  LEU   B CB  1 
ATOM   1373 C CG  . LEU   B 1 82 ? 8.960   -11.541 -33.282 1.00 27.77  ? 81  LEU   B CG  1 
ATOM   1374 C CD1 . LEU   B 1 82 ? 7.531   -12.103 -33.270 1.00 27.41  ? 81  LEU   B CD1 1 
ATOM   1375 C CD2 . LEU   B 1 82 ? 9.805   -12.214 -34.366 1.00 28.15  ? 81  LEU   B CD2 1 
ATOM   1376 N N   . TRP   B 1 83 ? 9.656   -6.916  -33.114 1.00 28.83  ? 82  TRP   B N   1 
ATOM   1377 C CA  . TRP   B 1 83 ? 9.520   -5.524  -33.515 1.00 32.89  ? 82  TRP   B CA  1 
ATOM   1378 C C   . TRP   B 1 83 ? 10.881  -4.953  -33.916 1.00 29.93  ? 82  TRP   B C   1 
ATOM   1379 O O   . TRP   B 1 83 ? 11.000  -4.377  -34.987 1.00 30.16  ? 82  TRP   B O   1 
ATOM   1380 C CB  . TRP   B 1 83 ? 8.854   -4.671  -32.420 1.00 33.30  ? 82  TRP   B CB  1 
ATOM   1381 C CG  . TRP   B 1 83 ? 8.547   -3.282  -32.923 1.00 33.34  ? 82  TRP   B CG  1 
ATOM   1382 C CD1 . TRP   B 1 83 ? 7.407   -2.841  -33.538 1.00 38.75  ? 82  TRP   B CD1 1 
ATOM   1383 C CD2 . TRP   B 1 83 ? 9.469   -2.172  -32.944 1.00 35.02  ? 82  TRP   B CD2 1 
ATOM   1384 N NE1 . TRP   B 1 83 ? 7.551   -1.524  -33.904 1.00 39.57  ? 82  TRP   B NE1 1 
ATOM   1385 C CE2 . TRP   B 1 83 ? 8.805   -1.092  -33.560 1.00 35.89  ? 82  TRP   B CE2 1 
ATOM   1386 C CE3 . TRP   B 1 83 ? 10.785  -1.984  -32.490 1.00 34.19  ? 82  TRP   B CE3 1 
ATOM   1387 C CZ2 . TRP   B 1 83 ? 9.420   0.160   -33.719 1.00 36.16  ? 82  TRP   B CZ2 1 
ATOM   1388 C CZ3 . TRP   B 1 83 ? 11.388  -0.749  -32.633 1.00 36.85  ? 82  TRP   B CZ3 1 
ATOM   1389 C CH2 . TRP   B 1 83 ? 10.712  0.308   -33.249 1.00 37.03  ? 82  TRP   B CH2 1 
ATOM   1390 N N   . GLU   B 1 84 ? 11.918  -5.232  -33.121 1.00 26.67  ? 83  GLU   B N   1 
ATOM   1391 C CA  . GLU   B 1 84 ? 13.241  -4.674  -33.360 1.00 29.36  ? 83  GLU   B CA  1 
ATOM   1392 C C   . GLU   B 1 84 ? 13.866  -5.202  -34.652 1.00 29.60  ? 83  GLU   B C   1 
ATOM   1393 O O   . GLU   B 1 84 ? 14.472  -4.432  -35.421 1.00 28.69  ? 83  GLU   B O   1 
ATOM   1394 C CB  . GLU   B 1 84 ? 14.141  -4.915  -32.172 1.00 26.10  ? 83  GLU   B CB  1 
ATOM   1395 C CG  . GLU   B 1 84 ? 13.587  -4.220  -30.927 1.00 29.44  ? 83  GLU   B CG  1 
ATOM   1396 C CD  . GLU   B 1 84 ? 14.424  -4.564  -29.745 1.00 30.20  ? 83  GLU   B CD  1 
ATOM   1397 O OE1 . GLU   B 1 84 ? 15.391  -5.360  -29.803 1.00 29.26  ? 83  GLU   B OE1 1 
ATOM   1398 O OE2 . GLU   B 1 84 ? 14.127  -3.924  -28.683 1.00 33.28  ? 83  GLU   B OE2 1 
ATOM   1399 N N   . ILE   B 1 85 ? 13.746  -6.516  -34.885 1.00 29.84  ? 84  ILE   B N   1 
ATOM   1400 C CA  . ILE   B 1 85 ? 14.447  -7.075  -36.042 1.00 25.05  ? 84  ILE   B CA  1 
ATOM   1401 C C   . ILE   B 1 85 ? 13.804  -6.534  -37.331 1.00 27.52  ? 84  ILE   B C   1 
ATOM   1402 O O   . ILE   B 1 85 ? 14.474  -6.388  -38.367 1.00 29.64  ? 84  ILE   B O   1 
ATOM   1403 C CB  . ILE   B 1 85 ? 14.478  -8.625  -35.993 1.00 23.73  ? 84  ILE   B CB  1 
ATOM   1404 C CG1 . ILE   B 1 85 ? 15.553  -9.196  -36.970 1.00 26.45  ? 84  ILE   B CG1 1 
ATOM   1405 C CG2 . ILE   B 1 85 ? 13.095  -9.212  -36.267 1.00 26.27  ? 84  ILE   B CG2 1 
ATOM   1406 C CD1 . ILE   B 1 85 ? 15.979  -10.617 -36.616 1.00 24.90  ? 84  ILE   B CD1 1 
ATOM   1407 N N   . GLN   B 1 86 ? 12.513  -6.234  -37.263 1.00 28.41  ? 85  GLN   B N   1 
ATOM   1408 C CA  . GLN   B 1 86 ? 11.737  -5.739  -38.382 1.00 31.70  ? 85  GLN   B CA  1 
ATOM   1409 C C   . GLN   B 1 86 ? 11.990  -4.241  -38.580 1.00 34.84  ? 85  GLN   B C   1 
ATOM   1410 O O   . GLN   B 1 86 ? 12.148  -3.798  -39.720 1.00 37.36  ? 85  GLN   B O   1 
ATOM   1411 C CB  . GLN   B 1 86 ? 10.264  -6.089  -38.163 1.00 35.09  ? 85  GLN   B CB  1 
ATOM   1412 N N   . ASN   B 1 87 ? 12.023  -3.451  -37.491 1.00 32.10  ? 86  ASN   B N   1 
ATOM   1413 C CA  . ASN   B 1 87 ? 11.904  -1.998  -37.638 1.00 31.05  ? 86  ASN   B CA  1 
ATOM   1414 C C   . ASN   B 1 87 ? 13.214  -1.268  -37.370 1.00 30.44  ? 86  ASN   B C   1 
ATOM   1415 O O   . ASN   B 1 87 ? 13.368  -0.110  -37.798 1.00 32.35  ? 86  ASN   B O   1 
ATOM   1416 C CB  . ASN   B 1 87 ? 10.823  -1.459  -36.693 1.00 36.50  ? 86  ASN   B CB  1 
ATOM   1417 C CG  . ASN   B 1 87 ? 9.452   -1.905  -37.147 1.00 39.97  ? 86  ASN   B CG  1 
ATOM   1418 O OD1 . ASN   B 1 87 ? 8.887   -1.287  -38.050 1.00 46.13  ? 86  ASN   B OD1 1 
ATOM   1419 N ND2 . ASN   B 1 87 ? 8.913   -2.997  -36.619 1.00 41.87  ? 86  ASN   B ND2 1 
ATOM   1420 N N   . ASN   B 1 88 ? 14.160  -1.860  -36.639 1.00 28.59  ? 87  ASN   B N   1 
ATOM   1421 C CA  . ASN   B 1 88 ? 15.398  -1.141  -36.403 1.00 28.75  ? 87  ASN   B CA  1 
ATOM   1422 C C   . ASN   B 1 88 ? 16.467  -2.128  -35.975 1.00 27.76  ? 87  ASN   B C   1 
ATOM   1423 O O   . ASN   B 1 88 ? 17.058  -2.036  -34.909 1.00 29.59  ? 87  ASN   B O   1 
ATOM   1424 C CB  . ASN   B 1 88 ? 15.229  0.055   -35.461 1.00 32.86  ? 87  ASN   B CB  1 
ATOM   1425 C CG  . ASN   B 1 88 ? 16.336  1.082   -35.603 1.00 33.36  ? 87  ASN   B CG  1 
ATOM   1426 O OD1 . ASN   B 1 88 ? 17.376  0.872   -36.256 1.00 30.79  ? 87  ASN   B OD1 1 
ATOM   1427 N ND2 . ASN   B 1 88 ? 16.103  2.238   -34.994 1.00 34.25  ? 87  ASN   B ND2 1 
ATOM   1428 N N   . PRO   B 1 89 ? 16.788  -3.087  -36.876 1.00 28.35  ? 88  PRO   B N   1 
ATOM   1429 C CA  . PRO   B 1 89 ? 17.722  -4.162  -36.537 1.00 25.81  ? 88  PRO   B CA  1 
ATOM   1430 C C   . PRO   B 1 89 ? 19.164  -3.773  -36.253 1.00 26.05  ? 88  PRO   B C   1 
ATOM   1431 O O   . PRO   B 1 89 ? 19.931  -4.509  -35.634 1.00 26.00  ? 88  PRO   B O   1 
ATOM   1432 C CB  . PRO   B 1 89 ? 17.619  -5.092  -37.785 1.00 27.99  ? 88  PRO   B CB  1 
ATOM   1433 C CG  . PRO   B 1 89 ? 17.217  -4.158  -38.928 1.00 26.84  ? 88  PRO   B CG  1 
ATOM   1434 C CD  . PRO   B 1 89 ? 16.291  -3.148  -38.265 1.00 27.20  ? 88  PRO   B CD  1 
ATOM   1435 N N   . HIS   B 1 90 ? 19.558  -2.563  -36.738 1.00 27.37  ? 89  HIS   B N   1 
ATOM   1436 C CA  . HIS   B 1 90 ? 20.949  -2.152  -36.643 1.00 28.06  ? 89  HIS   B CA  1 
ATOM   1437 C C   . HIS   B 1 90 ? 21.201  -1.059  -35.590 1.00 30.05  ? 89  HIS   B C   1 
ATOM   1438 O O   . HIS   B 1 90 ? 22.329  -0.574  -35.465 1.00 31.30  ? 89  HIS   B O   1 
ATOM   1439 C CB  . HIS   B 1 90 ? 21.457  -1.706  -38.026 1.00 27.23  ? 89  HIS   B CB  1 
ATOM   1440 C CG  . HIS   B 1 90 ? 21.275  -2.785  -39.037 1.00 29.74  ? 89  HIS   B CG  1 
ATOM   1441 N ND1 . HIS   B 1 90 ? 21.898  -4.003  -38.899 1.00 29.30  ? 89  HIS   B ND1 1 
ATOM   1442 C CD2 . HIS   B 1 90 ? 20.637  -2.817  -40.229 1.00 27.99  ? 89  HIS   B CD2 1 
ATOM   1443 C CE1 . HIS   B 1 90 ? 21.597  -4.745  -39.982 1.00 26.75  ? 89  HIS   B CE1 1 
ATOM   1444 N NE2 . HIS   B 1 90 ? 20.797  -4.073  -40.748 1.00 28.42  ? 89  HIS   B NE2 1 
ATOM   1445 N N   . ALA   B 1 91 ? 20.198  -0.783  -34.749 1.00 28.17  ? 90  ALA   B N   1 
ATOM   1446 C CA  . ALA   B 1 91 ? 20.331  0.230   -33.704 1.00 29.78  ? 90  ALA   B CA  1 
ATOM   1447 C C   . ALA   B 1 91 ? 21.234  -0.208  -32.550 1.00 35.89  ? 90  ALA   B C   1 
ATOM   1448 O O   . ALA   B 1 91 ? 21.495  -1.390  -32.333 1.00 31.73  ? 90  ALA   B O   1 
ATOM   1449 C CB  . ALA   B 1 91 ? 18.921  0.596   -33.262 1.00 28.43  ? 90  ALA   B CB  1 
ATOM   1450 N N   . SER   B 1 92 ? 21.710  0.788   -31.773 1.00 35.36  ? 91  SER   B N   1 
ATOM   1451 C CA  . SER   B 1 92 ? 22.322  0.582   -30.480 1.00 42.39  ? 91  SER   B CA  1 
ATOM   1452 C C   . SER   B 1 92 ? 21.210  0.306   -29.466 1.00 44.37  ? 91  SER   B C   1 
ATOM   1453 O O   . SER   B 1 92 ? 20.266  1.095   -29.347 1.00 47.10  ? 91  SER   B O   1 
ATOM   1454 C CB  . SER   B 1 92 ? 23.128  1.822   -30.090 1.00 45.67  ? 91  SER   B CB  1 
ATOM   1455 O OG  . SER   B 1 92 ? 23.809  1.596   -28.867 1.00 57.53  ? 91  SER   B OG  1 
ATOM   1456 N N   . TYR   B 1 93 ? 21.325  -0.851  -28.795 1.00 39.57  ? 92  TYR   B N   1 
ATOM   1457 C CA  . TYR   B 1 93 ? 20.438  -1.302  -27.742 1.00 41.35  ? 92  TYR   B CA  1 
ATOM   1458 C C   . TYR   B 1 93 ? 21.242  -1.388  -26.445 1.00 46.00  ? 92  TYR   B C   1 
ATOM   1459 O O   . TYR   B 1 93 ? 20.873  -2.115  -25.530 1.00 54.10  ? 92  TYR   B O   1 
ATOM   1460 C CB  . TYR   B 1 93 ? 19.783  -2.628  -28.142 1.00 39.33  ? 92  TYR   B CB  1 
ATOM   1461 C CG  . TYR   B 1 93 ? 18.793  -2.487  -29.287 1.00 35.55  ? 92  TYR   B CG  1 
ATOM   1462 C CD1 . TYR   B 1 93 ? 17.495  -2.055  -29.052 1.00 35.40  ? 92  TYR   B CD1 1 
ATOM   1463 C CD2 . TYR   B 1 93 ? 19.125  -2.802  -30.616 1.00 33.65  ? 92  TYR   B CD2 1 
ATOM   1464 C CE1 . TYR   B 1 93 ? 16.579  -1.853  -30.070 1.00 32.87  ? 92  TYR   B CE1 1 
ATOM   1465 C CE2 . TYR   B 1 93 ? 18.214  -2.609  -31.645 1.00 31.41  ? 92  TYR   B CE2 1 
ATOM   1466 C CZ  . TYR   B 1 93 ? 16.928  -2.152  -31.387 1.00 32.41  ? 92  TYR   B CZ  1 
ATOM   1467 O OH  . TYR   B 1 93 ? 15.966  -1.956  -32.343 1.00 33.16  ? 92  TYR   B OH  1 
ATOM   1468 N N   . SER   B 1 94 ? 22.348  -0.639  -26.402 1.00 60.92  ? 93  SER   B N   1 
ATOM   1469 C CA  . SER   B 1 94 ? 23.256  -0.619  -25.265 1.00 76.02  ? 93  SER   B CA  1 
ATOM   1470 C C   . SER   B 1 94 ? 22.496  -0.241  -23.982 1.00 91.55  ? 93  SER   B C   1 
ATOM   1471 O O   . SER   B 1 94 ? 21.472  0.490   -24.096 1.00 84.86  ? 93  SER   B O   1 
ATOM   1472 C CB  . SER   B 1 94 ? 24.411  0.322   -25.512 1.00 80.86  ? 93  SER   B CB  1 
ATOM   1473 O OG  . SER   B 1 94 ? 25.203  -0.116  -26.607 1.00 79.25  ? 93  SER   B OG  1 
ATOM   1474 O OXT . SER   B 1 94 ? 22.951  -0.690  -22.906 1.00 107.16 ? 93  SER   B OXT 1 
ATOM   1475 N N   . HIS   C 1 4  ? 32.888  -23.380 27.286  1.00 79.88  ? 3   HIS   C N   1 
ATOM   1476 C CA  . HIS   C 1 4  ? 31.618  -22.625 27.480  1.00 81.65  ? 3   HIS   C CA  1 
ATOM   1477 C C   . HIS   C 1 4  ? 30.972  -23.088 28.791  1.00 78.55  ? 3   HIS   C C   1 
ATOM   1478 O O   . HIS   C 1 4  ? 31.620  -23.764 29.589  1.00 75.20  ? 3   HIS   C O   1 
ATOM   1479 C CB  . HIS   C 1 4  ? 30.766  -22.771 26.210  1.00 85.80  ? 3   HIS   C CB  1 
ATOM   1480 C CG  . HIS   C 1 4  ? 29.905  -21.591 25.898  1.00 87.04  ? 3   HIS   C CG  1 
ATOM   1481 N ND1 . HIS   C 1 4  ? 28.598  -21.463 26.323  1.00 90.15  ? 3   HIS   C ND1 1 
ATOM   1482 C CD2 . HIS   C 1 4  ? 30.175  -20.483 25.196  1.00 81.61  ? 3   HIS   C CD2 1 
ATOM   1483 C CE1 . HIS   C 1 4  ? 28.103  -20.311 25.887  1.00 88.13  ? 3   HIS   C CE1 1 
ATOM   1484 N NE2 . HIS   C 1 4  ? 29.047  -19.697 25.205  1.00 80.46  ? 3   HIS   C NE2 1 
ATOM   1485 N N   . ALA   C 1 5  ? 29.703  -22.708 29.014  1.00 75.53  ? 4   ALA   C N   1 
ATOM   1486 C CA  . ALA   C 1 5  ? 28.881  -23.221 30.104  1.00 69.35  ? 4   ALA   C CA  1 
ATOM   1487 C C   . ALA   C 1 5  ? 27.402  -22.993 29.803  1.00 72.02  ? 4   ALA   C C   1 
ATOM   1488 O O   . ALA   C 1 5  ? 27.045  -22.030 29.124  1.00 72.75  ? 4   ALA   C O   1 
ATOM   1489 C CB  . ALA   C 1 5  ? 29.255  -22.550 31.390  1.00 71.36  ? 4   ALA   C CB  1 
ATOM   1490 N N   . PHE   C 1 6  ? 26.548  -23.861 30.359  1.00 57.19  ? 5   PHE   C N   1 
ATOM   1491 C CA  . PHE   C 1 6  ? 25.173  -23.967 29.910  1.00 54.70  ? 5   PHE   C CA  1 
ATOM   1492 C C   . PHE   C 1 6  ? 24.246  -24.062 31.113  1.00 60.61  ? 5   PHE   C C   1 
ATOM   1493 O O   . PHE   C 1 6  ? 24.341  -25.003 31.900  1.00 76.90  ? 5   PHE   C O   1 
ATOM   1494 C CB  . PHE   C 1 6  ? 25.083  -25.203 28.995  1.00 46.34  ? 5   PHE   C CB  1 
ATOM   1495 C CG  . PHE   C 1 6  ? 25.772  -25.033 27.644  1.00 48.49  ? 5   PHE   C CG  1 
ATOM   1496 C CD1 . PHE   C 1 6  ? 26.868  -25.802 27.276  1.00 47.70  ? 5   PHE   C CD1 1 
ATOM   1497 C CD2 . PHE   C 1 6  ? 25.329  -24.061 26.745  1.00 56.19  ? 5   PHE   C CD2 1 
ATOM   1498 C CE1 . PHE   C 1 6  ? 27.460  -25.630 26.027  1.00 48.95  ? 5   PHE   C CE1 1 
ATOM   1499 C CE2 . PHE   C 1 6  ? 25.942  -23.886 25.511  1.00 52.48  ? 5   PHE   C CE2 1 
ATOM   1500 C CZ  . PHE   C 1 6  ? 26.996  -24.681 25.145  1.00 45.83  ? 5   PHE   C CZ  1 
ATOM   1501 N N   . LYS   C 1 7  ? 23.356  -23.077 31.252  1.00 59.44  ? 6   LYS   C N   1 
ATOM   1502 C CA  . LYS   C 1 7  ? 22.330  -23.128 32.281  1.00 62.81  ? 6   LYS   C CA  1 
ATOM   1503 C C   . LYS   C 1 7  ? 21.067  -23.644 31.605  1.00 53.40  ? 6   LYS   C C   1 
ATOM   1504 O O   . LYS   C 1 7  ? 21.001  -23.622 30.375  1.00 63.41  ? 6   LYS   C O   1 
ATOM   1505 C CB  . LYS   C 1 7  ? 22.160  -21.761 32.963  1.00 61.36  ? 6   LYS   C CB  1 
ATOM   1506 N N   . PRO   C 1 8  ? 20.047  -24.149 32.345  1.00 55.04  ? 7   PRO   C N   1 
ATOM   1507 C CA  . PRO   C 1 8  ? 18.771  -24.525 31.732  1.00 54.99  ? 7   PRO   C CA  1 
ATOM   1508 C C   . PRO   C 1 8  ? 18.198  -23.357 30.927  1.00 62.85  ? 7   PRO   C C   1 
ATOM   1509 O O   . PRO   C 1 8  ? 18.306  -22.201 31.333  1.00 70.62  ? 7   PRO   C O   1 
ATOM   1510 C CB  . PRO   C 1 8  ? 17.890  -24.939 32.927  1.00 57.95  ? 7   PRO   C CB  1 
ATOM   1511 C CG  . PRO   C 1 8  ? 18.897  -25.413 33.951  1.00 50.51  ? 7   PRO   C CG  1 
ATOM   1512 C CD  . PRO   C 1 8  ? 20.097  -24.477 33.784  1.00 49.25  ? 7   PRO   C CD  1 
ATOM   1513 N N   . GLY   C 1 9  ? 17.640  -23.663 29.753  1.00 59.43  ? 8   GLY   C N   1 
ATOM   1514 C CA  . GLY   C 1 9  ? 16.971  -22.659 28.941  1.00 53.77  ? 8   GLY   C CA  1 
ATOM   1515 C C   . GLY   C 1 9  ? 17.814  -22.175 27.760  1.00 51.48  ? 8   GLY   C C   1 
ATOM   1516 O O   . GLY   C 1 9  ? 17.234  -21.709 26.778  1.00 50.33  ? 8   GLY   C O   1 
ATOM   1517 N N   . ASP   C 1 10 ? 19.152  -22.289 27.872  1.00 47.99  ? 9   ASP   C N   1 
ATOM   1518 C CA  . ASP   C 1 10 ? 20.131  -21.941 26.852  1.00 42.12  ? 9   ASP   C CA  1 
ATOM   1519 C C   . ASP   C 1 10 ? 19.859  -22.667 25.530  1.00 44.17  ? 9   ASP   C C   1 
ATOM   1520 O O   . ASP   C 1 10 ? 19.511  -23.851 25.499  1.00 39.37  ? 9   ASP   C O   1 
ATOM   1521 C CB  . ASP   C 1 10 ? 21.572  -22.170 27.277  1.00 44.36  ? 9   ASP   C CB  1 
ATOM   1522 C CG  . ASP   C 1 10 ? 22.167  -21.195 28.296  1.00 53.76  ? 9   ASP   C CG  1 
ATOM   1523 O OD1 . ASP   C 1 10 ? 21.464  -20.237 28.685  1.00 65.26  ? 9   ASP   C OD1 1 
ATOM   1524 O OD2 . ASP   C 1 10 ? 23.336  -21.400 28.696  1.00 60.58  ? 9   ASP   C OD2 1 
ATOM   1525 N N   . LEU   C 1 11 ? 19.989  -21.912 24.432  1.00 43.97  ? 10  LEU   C N   1 
ATOM   1526 C CA  . LEU   C 1 11 ? 19.601  -22.424 23.130  1.00 38.88  ? 10  LEU   C CA  1 
ATOM   1527 C C   . LEU   C 1 11 ? 20.860  -22.882 22.431  1.00 34.15  ? 10  LEU   C C   1 
ATOM   1528 O O   . LEU   C 1 11 ? 21.854  -22.179 22.455  1.00 35.75  ? 10  LEU   C O   1 
ATOM   1529 C CB  . LEU   C 1 11 ? 18.820  -21.394 22.306  1.00 38.27  ? 10  LEU   C CB  1 
ATOM   1530 C CG  . LEU   C 1 11 ? 17.522  -20.917 22.951  1.00 37.43  ? 10  LEU   C CG  1 
ATOM   1531 C CD1 . LEU   C 1 11 ? 16.860  -19.867 22.062  1.00 42.09  ? 10  LEU   C CD1 1 
ATOM   1532 C CD2 . LEU   C 1 11 ? 16.559  -22.063 23.226  1.00 38.51  ? 10  LEU   C CD2 1 
ATOM   1533 N N   . VAL   C 1 12 ? 20.809  -24.076 21.792  1.00 34.08  ? 11  VAL   C N   1 
ATOM   1534 C CA  . VAL   C 1 12 ? 22.000  -24.671 21.215  1.00 32.47  ? 11  VAL   C CA  1 
ATOM   1535 C C   . VAL   C 1 12 ? 21.623  -25.456 19.943  1.00 30.57  ? 11  VAL   C C   1 
ATOM   1536 O O   . VAL   C 1 12 ? 20.430  -25.661 19.707  1.00 30.71  ? 11  VAL   C O   1 
ATOM   1537 C CB  . VAL   C 1 12 ? 22.623  -25.644 22.248  1.00 34.82  ? 11  VAL   C CB  1 
ATOM   1538 C CG1 . VAL   C 1 12 ? 22.944  -24.936 23.568  1.00 38.49  ? 11  VAL   C CG1 1 
ATOM   1539 C CG2 . VAL   C 1 12 ? 21.744  -26.871 22.521  1.00 33.82  ? 11  VAL   C CG2 1 
ATOM   1540 N N   . PHE   C 1 13 ? 22.657  -25.851 19.182  1.00 31.79  ? 12  PHE   C N   1 
ATOM   1541 C CA  . PHE   C 1 13 ? 22.660  -27.016 18.290  1.00 28.93  ? 12  PHE   C CA  1 
ATOM   1542 C C   . PHE   C 1 13 ? 23.372  -28.170 18.990  1.00 30.75  ? 12  PHE   C C   1 
ATOM   1543 O O   . PHE   C 1 13 ? 24.492  -28.023 19.523  1.00 31.53  ? 12  PHE   C O   1 
ATOM   1544 C CB  . PHE   C 1 13 ? 23.340  -26.787 16.924  1.00 33.04  ? 12  PHE   C CB  1 
ATOM   1545 C CG  . PHE   C 1 13 ? 22.537  -25.793 16.104  1.00 35.05  ? 12  PHE   C CG  1 
ATOM   1546 C CD1 . PHE   C 1 13 ? 21.512  -26.223 15.259  1.00 34.76  ? 12  PHE   C CD1 1 
ATOM   1547 C CD2 . PHE   C 1 13 ? 22.838  -24.431 16.170  1.00 37.97  ? 12  PHE   C CD2 1 
ATOM   1548 C CE1 . PHE   C 1 13 ? 20.773  -25.294 14.534  1.00 34.34  ? 12  PHE   C CE1 1 
ATOM   1549 C CE2 . PHE   C 1 13 ? 22.073  -23.514 15.477  1.00 38.28  ? 12  PHE   C CE2 1 
ATOM   1550 C CZ  . PHE   C 1 13 ? 21.076  -23.951 14.634  1.00 36.27  ? 12  PHE   C CZ  1 
ATOM   1551 N N   . ALA   C 1 14 ? 22.715  -29.341 18.995  1.00 30.35  ? 13  ALA   C N   1 
ATOM   1552 C CA  . ALA   C 1 14 ? 23.162  -30.516 19.733  1.00 27.60  ? 13  ALA   C CA  1 
ATOM   1553 C C   . ALA   C 1 14 ? 23.480  -31.618 18.731  1.00 30.90  ? 13  ALA   C C   1 
ATOM   1554 O O   . ALA   C 1 14 ? 22.650  -31.923 17.867  1.00 29.04  ? 13  ALA   C O   1 
ATOM   1555 C CB  . ALA   C 1 14 ? 22.081  -30.976 20.701  1.00 28.16  ? 13  ALA   C CB  1 
ATOM   1556 N N   . LYS   C 1 15 ? 24.678  -32.191 18.840  1.00 29.74  ? 14  LYS   C N   1 
ATOM   1557 C CA  . LYS   C 1 15 ? 25.079  -33.217 17.882  1.00 29.57  ? 14  LYS   C CA  1 
ATOM   1558 C C   . LYS   C 1 15 ? 25.079  -34.596 18.528  1.00 28.95  ? 14  LYS   C C   1 
ATOM   1559 O O   . LYS   C 1 15 ? 25.856  -34.861 19.449  1.00 31.23  ? 14  LYS   C O   1 
ATOM   1560 C CB  . LYS   C 1 15 ? 26.495  -32.912 17.378  1.00 29.94  ? 14  LYS   C CB  1 
ATOM   1561 C CG  . LYS   C 1 15 ? 27.045  -33.798 16.245  1.00 31.19  ? 14  LYS   C CG  1 
ATOM   1562 C CD  . LYS   C 1 15 ? 26.170  -33.723 14.985  1.00 29.93  ? 14  LYS   C CD  1 
ATOM   1563 C CE  . LYS   C 1 15 ? 26.639  -34.580 13.795  1.00 31.28  ? 14  LYS   C CE  1 
ATOM   1564 N NZ  . LYS   C 1 15 ? 26.469  -36.021 14.053  1.00 31.70  ? 14  LYS   C NZ  1 
ATOM   1565 N N   . MET   C 1 16 ? 24.305  -35.534 17.947  1.00 27.48  ? 15  MET   C N   1 
ATOM   1566 C CA  . MET   C 1 16 ? 24.319  -36.951 18.288  1.00 27.57  ? 15  MET   C CA  1 
ATOM   1567 C C   . MET   C 1 16 ? 24.805  -37.732 17.070  1.00 33.04  ? 15  MET   C C   1 
ATOM   1568 O O   . MET   C 1 16 ? 24.523  -37.358 15.923  1.00 28.26  ? 15  MET   C O   1 
ATOM   1569 C CB  . MET   C 1 16 ? 22.898  -37.445 18.606  1.00 31.70  ? 15  MET   C CB  1 
ATOM   1570 C CG  . MET   C 1 16 ? 22.289  -36.764 19.824  1.00 34.55  ? 15  MET   C CG  1 
ATOM   1571 S SD  . MET   C 1 16 ? 20.698  -37.505 20.236  1.00 38.03  ? 15  MET   C SD  1 
ATOM   1572 C CE  . MET   C 1 16 ? 19.674  -36.852 18.904  1.00 37.15  ? 15  MET   C CE  1 
ATOM   1573 N N   . LYS   C 1 17 ? 25.522  -38.840 17.324  1.00 31.00  ? 16  LYS   C N   1 
ATOM   1574 C CA  . LYS   C 1 17 ? 25.866  -39.754 16.244  1.00 33.34  ? 16  LYS   C CA  1 
ATOM   1575 C C   . LYS   C 1 17 ? 24.596  -40.173 15.512  1.00 26.16  ? 16  LYS   C C   1 
ATOM   1576 O O   . LYS   C 1 17 ? 23.644  -40.645 16.121  1.00 31.04  ? 16  LYS   C O   1 
ATOM   1577 C CB  . LYS   C 1 17 ? 26.585  -40.981 16.830  1.00 31.67  ? 16  LYS   C CB  1 
ATOM   1578 C CG  . LYS   C 1 17 ? 27.247  -41.962 15.848  1.00 36.29  ? 16  LYS   C CG  1 
ATOM   1579 C CD  . LYS   C 1 17 ? 28.320  -41.171 15.104  1.00 36.99  ? 16  LYS   C CD  1 
ATOM   1580 C CE  . LYS   C 1 17 ? 29.132  -42.122 14.261  1.00 47.78  ? 16  LYS   C CE  1 
ATOM   1581 N NZ  . LYS   C 1 17 ? 30.372  -41.508 13.786  1.00 43.10  ? 16  LYS   C NZ  1 
ATOM   1582 N N   . GLY   C 1 18 ? 24.680  -40.087 14.178  1.00 30.01  ? 17  GLY   C N   1 
ATOM   1583 C CA  . GLY   C 1 18 ? 23.585  -40.559 13.335  1.00 29.73  ? 17  GLY   C CA  1 
ATOM   1584 C C   . GLY   C 1 18 ? 22.656  -39.415 12.933  1.00 30.41  ? 17  GLY   C C   1 
ATOM   1585 O O   . GLY   C 1 18 ? 21.684  -39.671 12.230  1.00 29.12  ? 17  GLY   C O   1 
ATOM   1586 N N   . TYR   C 1 19 ? 22.934  -38.176 13.362  1.00 29.24  ? 18  TYR   C N   1 
ATOM   1587 C CA  . TYR   C 1 19 ? 21.957  -37.091 13.165  1.00 29.48  ? 18  TYR   C CA  1 
ATOM   1588 C C   . TYR   C 1 19 ? 22.684  -35.785 12.895  1.00 31.27  ? 18  TYR   C C   1 
ATOM   1589 O O   . TYR   C 1 19 ? 23.803  -35.585 13.386  1.00 28.13  ? 18  TYR   C O   1 
ATOM   1590 C CB  . TYR   C 1 19 ? 21.147  -36.789 14.438  1.00 27.08  ? 18  TYR   C CB  1 
ATOM   1591 C CG  . TYR   C 1 19 ? 20.298  -37.970 14.860  1.00 28.82  ? 18  TYR   C CG  1 
ATOM   1592 C CD1 . TYR   C 1 19 ? 20.822  -38.992 15.661  1.00 30.30  ? 18  TYR   C CD1 1 
ATOM   1593 C CD2 . TYR   C 1 19 ? 19.004  -38.094 14.386  1.00 32.54  ? 18  TYR   C CD2 1 
ATOM   1594 C CE1 . TYR   C 1 19 ? 20.060  -40.101 15.984  1.00 33.53  ? 18  TYR   C CE1 1 
ATOM   1595 C CE2 . TYR   C 1 19 ? 18.228  -39.187 14.733  1.00 37.37  ? 18  TYR   C CE2 1 
ATOM   1596 C CZ  . TYR   C 1 19 ? 18.753  -40.176 15.538  1.00 35.11  ? 18  TYR   C CZ  1 
ATOM   1597 O OH  . TYR   C 1 19 ? 17.929  -41.235 15.849  1.00 46.14  ? 18  TYR   C OH  1 
ATOM   1598 N N   . PRO   C 1 20 ? 22.111  -34.855 12.095  1.00 27.53  ? 19  PRO   C N   1 
ATOM   1599 C CA  . PRO   C 1 20 ? 22.738  -33.549 11.888  1.00 26.96  ? 19  PRO   C CA  1 
ATOM   1600 C C   . PRO   C 1 20 ? 22.682  -32.716 13.172  1.00 27.65  ? 19  PRO   C C   1 
ATOM   1601 O O   . PRO   C 1 20 ? 21.932  -33.006 14.095  1.00 26.34  ? 19  PRO   C O   1 
ATOM   1602 C CB  . PRO   C 1 20 ? 21.873  -32.975 10.731  1.00 33.76  ? 19  PRO   C CB  1 
ATOM   1603 C CG  . PRO   C 1 20 ? 20.519  -33.506 11.042  1.00 30.99  ? 19  PRO   C CG  1 
ATOM   1604 C CD  . PRO   C 1 20 ? 20.810  -34.977 11.413  1.00 27.83  ? 19  PRO   C CD  1 
ATOM   1605 N N   . HIS   C 1 21 ? 23.497  -31.670 13.191  1.00 25.69  ? 20  HIS   C N   1 
ATOM   1606 C CA  . HIS   C 1 21 ? 23.438  -30.739 14.314  1.00 26.23  ? 20  HIS   C CA  1 
ATOM   1607 C C   . HIS   C 1 21 ? 22.015  -30.222 14.475  1.00 29.13  ? 20  HIS   C C   1 
ATOM   1608 O O   . HIS   C 1 21 ? 21.432  -29.712 13.535  1.00 29.40  ? 20  HIS   C O   1 
ATOM   1609 C CB  . HIS   C 1 21 ? 24.414  -29.583 14.169  1.00 30.53  ? 20  HIS   C CB  1 
ATOM   1610 C CG  . HIS   C 1 21 ? 25.848  -30.033 14.215  1.00 31.81  ? 20  HIS   C CG  1 
ATOM   1611 N ND1 . HIS   C 1 21 ? 26.537  -30.632 13.186  1.00 35.29  ? 20  HIS   C ND1 1 
ATOM   1612 C CD2 . HIS   C 1 21 ? 26.737  -29.895 15.222  1.00 32.74  ? 20  HIS   C CD2 1 
ATOM   1613 C CE1 . HIS   C 1 21 ? 27.791  -30.864 13.563  1.00 37.20  ? 20  HIS   C CE1 1 
ATOM   1614 N NE2 . HIS   C 1 21 ? 27.937  -30.382 14.776  1.00 36.52  ? 20  HIS   C NE2 1 
ATOM   1615 N N   . TRP   C 1 22 ? 21.461  -30.362 15.681  1.00 25.42  ? 21  TRP   C N   1 
ATOM   1616 C CA  . TRP   C 1 22 ? 20.005  -30.292 15.817  1.00 24.93  ? 21  TRP   C CA  1 
ATOM   1617 C C   . TRP   C 1 22 ? 19.611  -29.121 16.709  1.00 27.26  ? 21  TRP   C C   1 
ATOM   1618 O O   . TRP   C 1 22 ? 20.197  -28.972 17.792  1.00 26.02  ? 21  TRP   C O   1 
ATOM   1619 C CB  . TRP   C 1 22 ? 19.448  -31.604 16.403  1.00 25.32  ? 21  TRP   C CB  1 
ATOM   1620 C CG  . TRP   C 1 22 ? 17.991  -31.788 16.048  1.00 25.69  ? 21  TRP   C CG  1 
ATOM   1621 C CD1 . TRP   C 1 22 ? 16.902  -31.193 16.619  1.00 28.94  ? 21  TRP   C CD1 1 
ATOM   1622 C CD2 . TRP   C 1 22 ? 17.495  -32.689 15.029  1.00 26.22  ? 21  TRP   C CD2 1 
ATOM   1623 N NE1 . TRP   C 1 22 ? 15.759  -31.662 16.008  1.00 29.32  ? 21  TRP   C NE1 1 
ATOM   1624 C CE2 . TRP   C 1 22 ? 16.089  -32.565 15.029  1.00 26.94  ? 21  TRP   C CE2 1 
ATOM   1625 C CE3 . TRP   C 1 22 ? 18.125  -33.566 14.134  1.00 28.54  ? 21  TRP   C CE3 1 
ATOM   1626 C CZ2 . TRP   C 1 22 ? 15.309  -33.315 14.126  1.00 25.92  ? 21  TRP   C CZ2 1 
ATOM   1627 C CZ3 . TRP   C 1 22 ? 17.366  -34.286 13.225  1.00 29.29  ? 21  TRP   C CZ3 1 
ATOM   1628 C CH2 . TRP   C 1 22 ? 15.977  -34.164 13.266  1.00 27.05  ? 21  TRP   C CH2 1 
ATOM   1629 N N   . PRO   C 1 23 ? 18.589  -28.292 16.364  1.00 27.53  ? 22  PRO   C N   1 
ATOM   1630 C CA  . PRO   C 1 23 ? 18.180  -27.187 17.242  1.00 26.47  ? 22  PRO   C CA  1 
ATOM   1631 C C   . PRO   C 1 23 ? 17.612  -27.753 18.550  1.00 25.44  ? 22  PRO   C C   1 
ATOM   1632 O O   . PRO   C 1 23 ? 16.781  -28.668 18.558  1.00 26.75  ? 22  PRO   C O   1 
ATOM   1633 C CB  . PRO   C 1 23 ? 17.132  -26.445 16.350  1.00 28.95  ? 22  PRO   C CB  1 
ATOM   1634 C CG  . PRO   C 1 23 ? 16.598  -27.521 15.462  1.00 26.71  ? 22  PRO   C CG  1 
ATOM   1635 C CD  . PRO   C 1 23 ? 17.837  -28.309 15.077  1.00 25.44  ? 22  PRO   C CD  1 
ATOM   1636 N N   . ALA   C 1 24 ? 18.115  -27.228 19.664  1.00 28.30  ? 23  ALA   C N   1 
ATOM   1637 C CA  . ALA   C 1 24 ? 17.764  -27.766 20.969  1.00 32.68  ? 23  ALA   C CA  1 
ATOM   1638 C C   . ALA   C 1 24 ? 17.882  -26.703 22.054  1.00 34.16  ? 23  ALA   C C   1 
ATOM   1639 O O   . ALA   C 1 24 ? 18.346  -25.579 21.827  1.00 32.27  ? 23  ALA   C O   1 
ATOM   1640 C CB  . ALA   C 1 24 ? 18.694  -28.930 21.306  1.00 30.76  ? 23  ALA   C CB  1 
ATOM   1641 N N   . ARG   C 1 25 ? 17.553  -27.124 23.282  1.00 33.29  ? 24  ARG   C N   1 
ATOM   1642 C CA  . ARG   C 1 25 ? 17.950  -26.305 24.415  1.00 32.78  ? 24  ARG   C CA  1 
ATOM   1643 C C   . ARG   C 1 25 ? 18.385  -27.222 25.567  1.00 34.28  ? 24  ARG   C C   1 
ATOM   1644 O O   . ARG   C 1 25 ? 18.018  -28.403 25.605  1.00 36.40  ? 24  ARG   C O   1 
ATOM   1645 C CB  . ARG   C 1 25 ? 16.747  -25.480 24.873  1.00 36.62  ? 24  ARG   C CB  1 
ATOM   1646 C CG  . ARG   C 1 25 ? 15.456  -26.228 25.149  1.00 41.30  ? 24  ARG   C CG  1 
ATOM   1647 C CD  . ARG   C 1 25 ? 14.426  -25.338 25.856  1.00 43.55  ? 24  ARG   C CD  1 
ATOM   1648 N NE  . ARG   C 1 25 ? 13.248  -26.177 26.104  1.00 45.49  ? 24  ARG   C NE  1 
ATOM   1649 C CZ  . ARG   C 1 25 ? 11.964  -25.969 25.881  1.00 53.27  ? 24  ARG   C CZ  1 
ATOM   1650 N NH1 . ARG   C 1 25 ? 11.534  -24.841 25.338  1.00 48.81  ? 24  ARG   C NH1 1 
ATOM   1651 N NH2 . ARG   C 1 25 ? 11.104  -26.922 26.206  1.00 53.16  ? 24  ARG   C NH2 1 
ATOM   1652 N N   . ILE   C 1 26 ? 19.112  -26.609 26.493  1.00 34.91  ? 25  ILE   C N   1 
ATOM   1653 C CA  . ILE   C 1 26 ? 19.465  -27.195 27.782  1.00 38.83  ? 25  ILE   C CA  1 
ATOM   1654 C C   . ILE   C 1 26 ? 18.233  -27.173 28.676  1.00 46.92  ? 25  ILE   C C   1 
ATOM   1655 O O   . ILE   C 1 26 ? 17.655  -26.118 28.900  1.00 49.98  ? 25  ILE   C O   1 
ATOM   1656 C CB  . ILE   C 1 26 ? 20.604  -26.371 28.405  1.00 40.81  ? 25  ILE   C CB  1 
ATOM   1657 C CG1 . ILE   C 1 26 ? 21.736  -26.113 27.440  1.00 43.36  ? 25  ILE   C CG1 1 
ATOM   1658 C CG2 . ILE   C 1 26 ? 21.103  -27.000 29.708  1.00 45.95  ? 25  ILE   C CG2 1 
ATOM   1659 C CD1 . ILE   C 1 26 ? 22.572  -27.313 27.059  1.00 42.87  ? 25  ILE   C CD1 1 
ATOM   1660 N N   . ASP   C 1 27 ? 17.839  -28.350 29.162  1.00 44.27  ? 26  ASP   C N   1 
ATOM   1661 C CA  . ASP   C 1 27 ? 16.797  -28.491 30.172  1.00 57.34  ? 26  ASP   C CA  1 
ATOM   1662 C C   . ASP   C 1 27 ? 17.352  -28.198 31.572  1.00 55.63  ? 26  ASP   C C   1 
ATOM   1663 O O   . ASP   C 1 27 ? 18.566  -28.450 31.776  1.00 56.40  ? 26  ASP   C O   1 
ATOM   1664 C CB  . ASP   C 1 27 ? 16.157  -29.868 30.126  1.00 56.17  ? 26  ASP   C CB  1 
ATOM   1665 C CG  . ASP   C 1 27 ? 14.863  -29.936 29.335  1.00 66.62  ? 26  ASP   C CG  1 
ATOM   1666 O OD1 . ASP   C 1 27 ? 14.558  -28.913 28.676  1.00 60.41  ? 26  ASP   C OD1 1 
ATOM   1667 O OD2 . ASP   C 1 27 ? 14.162  -30.986 29.430  1.00 60.23  ? 26  ASP   C OD2 1 
ATOM   1668 N N   . ASP   C 1 31 ? 14.926  -31.721 40.859  1.00 60.77  ? 30  ASP   C N   1 
ATOM   1669 C CA  . ASP   C 1 31 ? 15.378  -32.489 42.056  1.00 66.46  ? 30  ASP   C CA  1 
ATOM   1670 C C   . ASP   C 1 31 ? 14.487  -33.715 42.271  1.00 69.99  ? 30  ASP   C C   1 
ATOM   1671 O O   . ASP   C 1 31 ? 13.251  -33.638 42.249  1.00 65.41  ? 30  ASP   C O   1 
ATOM   1672 C CB  . ASP   C 1 31 ? 15.443  -31.624 43.303  1.00 64.26  ? 30  ASP   C CB  1 
ATOM   1673 C CG  . ASP   C 1 31 ? 16.456  -32.081 44.341  1.00 68.06  ? 30  ASP   C CG  1 
ATOM   1674 O OD1 . ASP   C 1 31 ? 17.662  -31.842 44.122  1.00 79.20  ? 30  ASP   C OD1 1 
ATOM   1675 O OD2 . ASP   C 1 31 ? 16.039  -32.700 45.341  1.00 64.67  ? 30  ASP   C OD2 1 
ATOM   1676 N N   . GLY   C 1 32 ? 15.140  -34.855 42.493  1.00 70.91  ? 31  GLY   C N   1 
ATOM   1677 C CA  . GLY   C 1 32 ? 14.427  -36.101 42.724  1.00 76.33  ? 31  GLY   C CA  1 
ATOM   1678 C C   . GLY   C 1 32 ? 14.487  -37.013 41.502  1.00 76.15  ? 31  GLY   C C   1 
ATOM   1679 O O   . GLY   C 1 32 ? 14.187  -38.203 41.609  1.00 68.16  ? 31  GLY   C O   1 
ATOM   1680 N N   . ALA   C 1 33 ? 14.868  -36.430 40.353  1.00 66.66  ? 32  ALA   C N   1 
ATOM   1681 C CA  . ALA   C 1 33 ? 15.009  -37.161 39.107  1.00 66.36  ? 32  ALA   C CA  1 
ATOM   1682 C C   . ALA   C 1 33 ? 16.307  -37.972 39.118  1.00 69.59  ? 32  ALA   C C   1 
ATOM   1683 O O   . ALA   C 1 33 ? 17.121  -37.860 40.038  1.00 62.47  ? 32  ALA   C O   1 
ATOM   1684 C CB  . ALA   C 1 33 ? 14.940  -36.197 37.941  1.00 59.60  ? 32  ALA   C CB  1 
ATOM   1685 N N   . VAL   C 1 34 ? 16.479  -38.831 38.105  1.00 77.39  ? 33  VAL   C N   1 
ATOM   1686 C CA  . VAL   C 1 34 ? 17.754  -39.510 37.925  1.00 82.57  ? 33  VAL   C CA  1 
ATOM   1687 C C   . VAL   C 1 34 ? 18.701  -38.539 37.221  1.00 77.39  ? 33  VAL   C C   1 
ATOM   1688 O O   . VAL   C 1 34 ? 18.337  -37.903 36.225  1.00 64.53  ? 33  VAL   C O   1 
ATOM   1689 C CB  . VAL   C 1 34 ? 17.763  -40.933 37.326  1.00 81.04  ? 33  VAL   C CB  1 
ATOM   1690 C CG1 . VAL   C 1 34 ? 19.062  -41.264 36.593  1.00 84.56  ? 33  VAL   C CG1 1 
ATOM   1691 C CG2 . VAL   C 1 34 ? 17.474  -41.975 38.400  1.00 85.23  ? 33  VAL   C CG2 1 
ATOM   1692 N N   . LYS   C 1 35 ? 19.894  -38.409 37.817  1.00 68.35  ? 34  LYS   C N   1 
ATOM   1693 C CA  . LYS   C 1 35 ? 20.874  -37.401 37.462  1.00 64.19  ? 34  LYS   C CA  1 
ATOM   1694 C C   . LYS   C 1 35 ? 21.507  -37.786 36.126  1.00 56.19  ? 34  LYS   C C   1 
ATOM   1695 O O   . LYS   C 1 35 ? 21.485  -38.951 35.721  1.00 53.99  ? 34  LYS   C O   1 
ATOM   1696 C CB  . LYS   C 1 35 ? 21.862  -37.250 38.625  1.00 64.38  ? 34  LYS   C CB  1 
ATOM   1697 N N   . PRO   C 1 36 ? 22.062  -36.812 35.376  1.00 54.64  ? 35  PRO   C N   1 
ATOM   1698 C CA  . PRO   C 1 36 ? 22.758  -37.142 34.136  1.00 50.25  ? 35  PRO   C CA  1 
ATOM   1699 C C   . PRO   C 1 36 ? 23.887  -38.125 34.460  1.00 53.67  ? 35  PRO   C C   1 
ATOM   1700 O O   . PRO   C 1 36 ? 24.277  -38.304 35.622  1.00 50.43  ? 35  PRO   C O   1 
ATOM   1701 C CB  . PRO   C 1 36 ? 23.273  -35.770 33.642  1.00 56.70  ? 35  PRO   C CB  1 
ATOM   1702 C CG  . PRO   C 1 36 ? 22.432  -34.736 34.367  1.00 57.18  ? 35  PRO   C CG  1 
ATOM   1703 C CD  . PRO   C 1 36 ? 22.069  -35.373 35.700  1.00 57.72  ? 35  PRO   C CD  1 
ATOM   1704 N N   . PRO   C 1 37 ? 24.450  -38.832 33.459  1.00 50.78  ? 36  PRO   C N   1 
ATOM   1705 C CA  . PRO   C 1 37 ? 25.790  -39.389 33.626  1.00 47.95  ? 36  PRO   C CA  1 
ATOM   1706 C C   . PRO   C 1 37 ? 26.701  -38.210 33.940  1.00 45.31  ? 36  PRO   C C   1 
ATOM   1707 O O   . PRO   C 1 37 ? 26.341  -37.051 33.692  1.00 38.29  ? 36  PRO   C O   1 
ATOM   1708 C CB  . PRO   C 1 37 ? 26.061  -40.000 32.241  1.00 44.77  ? 36  PRO   C CB  1 
ATOM   1709 C CG  . PRO   C 1 37 ? 24.676  -40.416 31.795  1.00 42.48  ? 36  PRO   C CG  1 
ATOM   1710 C CD  . PRO   C 1 37 ? 23.821  -39.220 32.182  1.00 43.19  ? 36  PRO   C CD  1 
ATOM   1711 N N   . PRO   C 1 38 ? 27.899  -38.477 34.510  1.00 45.09  ? 37  PRO   C N   1 
ATOM   1712 C CA  . PRO   C 1 38 ? 28.883  -37.428 34.780  1.00 45.20  ? 37  PRO   C CA  1 
ATOM   1713 C C   . PRO   C 1 38 ? 29.197  -36.556 33.571  1.00 40.48  ? 37  PRO   C C   1 
ATOM   1714 O O   . PRO   C 1 38 ? 29.494  -37.077 32.496  1.00 37.93  ? 37  PRO   C O   1 
ATOM   1715 C CB  . PRO   C 1 38 ? 30.122  -38.246 35.220  1.00 48.65  ? 37  PRO   C CB  1 
ATOM   1716 C CG  . PRO   C 1 38 ? 29.546  -39.522 35.784  1.00 48.37  ? 37  PRO   C CG  1 
ATOM   1717 C CD  . PRO   C 1 38 ? 28.344  -39.817 34.929  1.00 48.91  ? 37  PRO   C CD  1 
ATOM   1718 N N   . ASN   C 1 39 ? 29.111  -35.232 33.779  1.00 37.15  ? 38  ASN   C N   1 
ATOM   1719 C CA  . ASN   C 1 39 ? 29.538  -34.210 32.845  1.00 36.96  ? 38  ASN   C CA  1 
ATOM   1720 C C   . ASN   C 1 39 ? 28.619  -34.224 31.621  1.00 36.54  ? 38  ASN   C C   1 
ATOM   1721 O O   . ASN   C 1 39 ? 29.083  -33.943 30.517  1.00 42.86  ? 38  ASN   C O   1 
ATOM   1722 C CB  . ASN   C 1 39 ? 30.996  -34.383 32.420  1.00 40.81  ? 38  ASN   C CB  1 
ATOM   1723 C CG  . ASN   C 1 39 ? 31.597  -33.154 31.761  1.00 46.55  ? 38  ASN   C CG  1 
ATOM   1724 O OD1 . ASN   C 1 39 ? 31.135  -32.029 31.977  1.00 53.89  ? 38  ASN   C OD1 1 
ATOM   1725 N ND2 . ASN   C 1 39 ? 32.647  -33.329 30.964  1.00 49.65  ? 38  ASN   C ND2 1 
ATOM   1726 N N   . LYS   C 1 40 ? 27.354  -34.637 31.800  1.00 35.17  ? 39  LYS   C N   1 
ATOM   1727 C CA  . LYS   C 1 40 ? 26.393  -34.549 30.703  1.00 30.15  ? 39  LYS   C CA  1 
ATOM   1728 C C   . LYS   C 1 40 ? 25.237  -33.617 31.057  1.00 34.39  ? 39  LYS   C C   1 
ATOM   1729 O O   . LYS   C 1 40 ? 24.801  -33.527 32.193  1.00 37.25  ? 39  LYS   C O   1 
ATOM   1730 C CB  . LYS   C 1 40 ? 25.708  -35.884 30.397  1.00 32.91  ? 39  LYS   C CB  1 
ATOM   1731 C CG  . LYS   C 1 40 ? 26.657  -36.986 30.017  1.00 37.50  ? 39  LYS   C CG  1 
ATOM   1732 C CD  . LYS   C 1 40 ? 27.581  -36.802 28.824  1.00 43.60  ? 39  LYS   C CD  1 
ATOM   1733 C CE  . LYS   C 1 40 ? 28.314  -38.080 28.479  1.00 48.82  ? 39  LYS   C CE  1 
ATOM   1734 N NZ  . LYS   C 1 40 ? 29.171  -37.878 27.301  1.00 54.01  ? 39  LYS   C NZ  1 
ATOM   1735 N N   . TYR   C 1 41 ? 24.705  -32.930 30.035  1.00 31.68  ? 40  TYR   C N   1 
ATOM   1736 C CA  . TYR   C 1 41 ? 23.569  -32.042 30.216  1.00 33.18  ? 40  TYR   C CA  1 
ATOM   1737 C C   . TYR   C 1 41 ? 22.311  -32.696 29.662  1.00 34.83  ? 40  TYR   C C   1 
ATOM   1738 O O   . TYR   C 1 41 ? 22.379  -33.408 28.657  1.00 32.93  ? 40  TYR   C O   1 
ATOM   1739 C CB  . TYR   C 1 41 ? 23.694  -30.846 29.261  1.00 31.53  ? 40  TYR   C CB  1 
ATOM   1740 C CG  . TYR   C 1 41 ? 24.814  -29.915 29.683  1.00 32.04  ? 40  TYR   C CG  1 
ATOM   1741 C CD1 . TYR   C 1 41 ? 26.106  -30.098 29.209  1.00 34.10  ? 40  TYR   C CD1 1 
ATOM   1742 C CD2 . TYR   C 1 41 ? 24.580  -28.896 30.599  1.00 34.86  ? 40  TYR   C CD2 1 
ATOM   1743 C CE1 . TYR   C 1 41 ? 27.154  -29.281 29.606  1.00 46.43  ? 40  TYR   C CE1 1 
ATOM   1744 C CE2 . TYR   C 1 41 ? 25.616  -28.061 30.982  1.00 36.53  ? 40  TYR   C CE2 1 
ATOM   1745 C CZ  . TYR   C 1 41 ? 26.896  -28.259 30.502  1.00 42.56  ? 40  TYR   C CZ  1 
ATOM   1746 O OH  . TYR   C 1 41 ? 27.886  -27.421 30.913  1.00 54.01  ? 40  TYR   C OH  1 
ATOM   1747 N N   . PRO   C 1 42 ? 21.127  -32.385 30.246  1.00 35.90  ? 41  PRO   C N   1 
ATOM   1748 C CA  . PRO   C 1 42 ? 19.850  -32.832 29.695  1.00 32.95  ? 41  PRO   C CA  1 
ATOM   1749 C C   . PRO   C 1 42 ? 19.509  -31.887 28.552  1.00 32.31  ? 41  PRO   C C   1 
ATOM   1750 O O   . PRO   C 1 42 ? 19.538  -30.655 28.724  1.00 35.37  ? 41  PRO   C O   1 
ATOM   1751 C CB  . PRO   C 1 42 ? 18.848  -32.698 30.864  1.00 36.75  ? 41  PRO   C CB  1 
ATOM   1752 C CG  . PRO   C 1 42 ? 19.544  -31.815 31.854  1.00 38.86  ? 41  PRO   C CG  1 
ATOM   1753 C CD  . PRO   C 1 42 ? 20.968  -31.519 31.428  1.00 41.42  ? 41  PRO   C CD  1 
ATOM   1754 N N   . ILE   C 1 43 ? 19.238  -32.495 27.403  1.00 31.86  ? 42  ILE   C N   1 
ATOM   1755 C CA  . ILE   C 1 43 ? 18.944  -31.710 26.201  1.00 31.35  ? 42  ILE   C CA  1 
ATOM   1756 C C   . ILE   C 1 43 ? 17.517  -31.995 25.769  1.00 32.56  ? 42  ILE   C C   1 
ATOM   1757 O O   . ILE   C 1 43 ? 17.059  -33.143 25.753  1.00 35.35  ? 42  ILE   C O   1 
ATOM   1758 C CB  . ILE   C 1 43 ? 19.944  -32.082 25.091  1.00 30.82  ? 42  ILE   C CB  1 
ATOM   1759 C CG1 . ILE   C 1 43 ? 21.417  -31.865 25.510  1.00 33.04  ? 42  ILE   C CG1 1 
ATOM   1760 C CG2 . ILE   C 1 43 ? 19.590  -31.409 23.749  1.00 31.45  ? 42  ILE   C CG2 1 
ATOM   1761 C CD1 . ILE   C 1 43 ? 21.782  -30.448 25.903  1.00 33.90  ? 42  ILE   C CD1 1 
ATOM   1762 N N   . PHE   C 1 44 ? 16.826  -30.942 25.309  1.00 33.70  ? 43  PHE   C N   1 
ATOM   1763 C CA  . PHE   C 1 44 ? 15.534  -31.124 24.679  1.00 32.94  ? 43  PHE   C CA  1 
ATOM   1764 C C   . PHE   C 1 44 ? 15.644  -30.697 23.217  1.00 30.75  ? 43  PHE   C C   1 
ATOM   1765 O O   . PHE   C 1 44 ? 16.170  -29.612 22.940  1.00 32.71  ? 43  PHE   C O   1 
ATOM   1766 C CB  . PHE   C 1 44 ? 14.542  -30.187 25.387  1.00 36.93  ? 43  PHE   C CB  1 
ATOM   1767 C CG  . PHE   C 1 44 ? 13.178  -30.108 24.714  1.00 39.76  ? 43  PHE   C CG  1 
ATOM   1768 C CD1 . PHE   C 1 44 ? 12.188  -31.055 24.970  1.00 40.52  ? 43  PHE   C CD1 1 
ATOM   1769 C CD2 . PHE   C 1 44 ? 12.885  -29.076 23.821  1.00 40.24  ? 43  PHE   C CD2 1 
ATOM   1770 C CE1 . PHE   C 1 44 ? 10.936  -30.979 24.361  1.00 44.66  ? 43  PHE   C CE1 1 
ATOM   1771 C CE2 . PHE   C 1 44 ? 11.649  -29.017 23.188  1.00 38.70  ? 43  PHE   C CE2 1 
ATOM   1772 C CZ  . PHE   C 1 44 ? 10.675  -29.950 23.470  1.00 43.81  ? 43  PHE   C CZ  1 
ATOM   1773 N N   . PHE   C 1 45 ? 15.180  -31.582 22.326  1.00 30.41  ? 44  PHE   C N   1 
ATOM   1774 C CA  . PHE   C 1 45 ? 15.343  -31.386 20.892  1.00 32.82  ? 44  PHE   C CA  1 
ATOM   1775 C C   . PHE   C 1 45 ? 14.087  -30.721 20.353  1.00 32.37  ? 44  PHE   C C   1 
ATOM   1776 O O   . PHE   C 1 45 ? 12.977  -31.247 20.506  1.00 35.44  ? 44  PHE   C O   1 
ATOM   1777 C CB  . PHE   C 1 45 ? 15.676  -32.687 20.162  1.00 28.45  ? 44  PHE   C CB  1 
ATOM   1778 C CG  . PHE   C 1 45 ? 17.052  -33.222 20.511  1.00 28.36  ? 44  PHE   C CG  1 
ATOM   1779 C CD1 . PHE   C 1 45 ? 18.177  -32.838 19.786  1.00 27.70  ? 44  PHE   C CD1 1 
ATOM   1780 C CD2 . PHE   C 1 45 ? 17.190  -34.173 21.524  1.00 30.35  ? 44  PHE   C CD2 1 
ATOM   1781 C CE1 . PHE   C 1 45 ? 19.427  -33.358 20.106  1.00 33.38  ? 44  PHE   C CE1 1 
ATOM   1782 C CE2 . PHE   C 1 45 ? 18.438  -34.710 21.815  1.00 31.12  ? 44  PHE   C CE2 1 
ATOM   1783 C CZ  . PHE   C 1 45 ? 19.552  -34.305 21.122  1.00 29.49  ? 44  PHE   C CZ  1 
ATOM   1784 N N   . PHE   C 1 46 ? 14.269  -29.550 19.722  1.00 28.59  ? 45  PHE   C N   1 
ATOM   1785 C CA  . PHE   C 1 46 ? 13.104  -28.977 19.056  1.00 27.32  ? 45  PHE   C CA  1 
ATOM   1786 C C   . PHE   C 1 46 ? 12.595  -29.829 17.892  1.00 30.45  ? 45  PHE   C C   1 
ATOM   1787 O O   . PHE   C 1 46 ? 13.321  -30.609 17.266  1.00 29.26  ? 45  PHE   C O   1 
ATOM   1788 C CB  . PHE   C 1 46 ? 13.339  -27.512 18.665  1.00 27.46  ? 45  PHE   C CB  1 
ATOM   1789 C CG  . PHE   C 1 46 ? 13.606  -26.511 19.776  1.00 28.95  ? 45  PHE   C CG  1 
ATOM   1790 C CD1 . PHE   C 1 46 ? 12.570  -26.049 20.592  1.00 34.11  ? 45  PHE   C CD1 1 
ATOM   1791 C CD2 . PHE   C 1 46 ? 14.900  -26.036 20.000  1.00 31.10  ? 45  PHE   C CD2 1 
ATOM   1792 C CE1 . PHE   C 1 46 ? 12.862  -25.120 21.608  1.00 33.97  ? 45  PHE   C CE1 1 
ATOM   1793 C CE2 . PHE   C 1 46 ? 15.184  -25.110 21.001  1.00 33.80  ? 45  PHE   C CE2 1 
ATOM   1794 C CZ  . PHE   C 1 46 ? 14.168  -24.652 21.802  1.00 33.52  ? 45  PHE   C CZ  1 
ATOM   1795 N N   . GLY   C 1 47 ? 11.294  -29.691 17.582  1.00 28.74  ? 46  GLY   C N   1 
ATOM   1796 C CA  . GLY   C 1 47 ? 10.756  -30.399 16.425  1.00 32.94  ? 46  GLY   C CA  1 
ATOM   1797 C C   . GLY   C 1 47 ? 10.359  -31.834 16.774  1.00 34.55  ? 46  GLY   C C   1 
ATOM   1798 O O   . GLY   C 1 47 ? 9.182   -32.178 16.734  1.00 39.08  ? 46  GLY   C O   1 
ATOM   1799 N N   . THR   C 1 48 ? 11.336  -32.670 17.175  1.00 32.64  ? 47  THR   C N   1 
ATOM   1800 C CA  . THR   C 1 48 ? 10.988  -34.012 17.623  1.00 34.58  ? 47  THR   C CA  1 
ATOM   1801 C C   . THR   C 1 48 ? 10.488  -33.971 19.073  1.00 34.19  ? 47  THR   C C   1 
ATOM   1802 O O   . THR   C 1 48 ? 9.735   -34.861 19.491  1.00 39.52  ? 47  THR   C O   1 
ATOM   1803 C CB  . THR   C 1 48 ? 12.199  -34.936 17.541  1.00 29.31  ? 47  THR   C CB  1 
ATOM   1804 O OG1 . THR   C 1 48 ? 13.049  -34.377 18.547  1.00 33.95  ? 47  THR   C OG1 1 
ATOM   1805 C CG2 . THR   C 1 48 ? 12.816  -35.025 16.155  1.00 28.43  ? 47  THR   C CG2 1 
ATOM   1806 N N   . HIS   C 1 49 ? 10.908  -32.969 19.850  1.00 34.27  ? 48  HIS   C N   1 
ATOM   1807 C CA  . HIS   C 1 49 ? 10.585  -32.847 21.271  1.00 37.28  ? 48  HIS   C CA  1 
ATOM   1808 C C   . HIS   C 1 49 ? 11.045  -34.075 22.061  1.00 35.45  ? 48  HIS   C C   1 
ATOM   1809 O O   . HIS   C 1 49 ? 10.410  -34.437 23.054  1.00 42.09  ? 48  HIS   C O   1 
ATOM   1810 C CB  . HIS   C 1 49 ? 9.088   -32.584 21.508  1.00 39.53  ? 48  HIS   C CB  1 
ATOM   1811 C CG  . HIS   C 1 49 ? 8.517   -31.533 20.614  1.00 40.38  ? 48  HIS   C CG  1 
ATOM   1812 N ND1 . HIS   C 1 49 ? 7.350   -31.741 19.907  1.00 48.02  ? 48  HIS   C ND1 1 
ATOM   1813 C CD2 . HIS   C 1 49 ? 8.950   -30.325 20.275  1.00 40.67  ? 48  HIS   C CD2 1 
ATOM   1814 C CE1 . HIS   C 1 49 ? 7.099   -30.678 19.161  1.00 47.23  ? 48  HIS   C CE1 1 
ATOM   1815 N NE2 . HIS   C 1 49 ? 8.060   -29.806 19.365  1.00 45.57  ? 48  HIS   C NE2 1 
ATOM   1816 N N   . GLU   C 1 50 ? 12.141  -34.708 21.626  1.00 35.50  ? 49  GLU   C N   1 
ATOM   1817 C CA  . GLU   C 1 50 ? 12.756  -35.794 22.373  1.00 38.11  ? 49  GLU   C CA  1 
ATOM   1818 C C   . GLU   C 1 50 ? 13.856  -35.243 23.281  1.00 38.02  ? 49  GLU   C C   1 
ATOM   1819 O O   . GLU   C 1 50 ? 14.210  -34.068 23.219  1.00 35.43  ? 49  GLU   C O   1 
ATOM   1820 C CB  . GLU   C 1 50 ? 13.222  -36.872 21.404  1.00 39.20  ? 49  GLU   C CB  1 
ATOM   1821 C CG  . GLU   C 1 50 ? 12.066  -37.456 20.595  1.00 40.11  ? 49  GLU   C CG  1 
ATOM   1822 C CD  . GLU   C 1 50 ? 12.594  -38.356 19.503  1.00 47.77  ? 49  GLU   C CD  1 
ATOM   1823 O OE1 . GLU   C 1 50 ? 13.834  -38.510 19.391  1.00 51.83  ? 49  GLU   C OE1 1 
ATOM   1824 O OE2 . GLU   C 1 50 ? 11.770  -38.861 18.725  1.00 56.64  ? 49  GLU   C OE2 1 
ATOM   1825 N N   . THR   C 1 51 ? 14.317  -36.090 24.215  1.00 39.22  ? 50  THR   C N   1 
ATOM   1826 C CA  . THR   C 1 51 ? 15.377  -35.713 25.144  1.00 39.28  ? 50  THR   C CA  1 
ATOM   1827 C C   . THR   C 1 51 ? 16.502  -36.734 25.090  1.00 31.45  ? 50  THR   C C   1 
ATOM   1828 O O   . THR   C 1 51 ? 16.322  -37.880 24.666  1.00 34.85  ? 50  THR   C O   1 
ATOM   1829 C CB  . THR   C 1 51 ? 14.846  -35.581 26.573  1.00 41.82  ? 50  THR   C CB  1 
ATOM   1830 O OG1 . THR   C 1 51 ? 14.293  -36.868 26.858  1.00 41.64  ? 50  THR   C OG1 1 
ATOM   1831 C CG2 . THR   C 1 51 ? 13.896  -34.416 26.761  1.00 42.32  ? 50  THR   C CG2 1 
ATOM   1832 N N   . ALA   C 1 52 ? 17.698  -36.259 25.465  1.00 35.78  ? 51  ALA   C N   1 
ATOM   1833 C CA  . ALA   C 1 52 ? 18.895  -37.070 25.622  1.00 35.83  ? 51  ALA   C CA  1 
ATOM   1834 C C   . ALA   C 1 52 ? 19.865  -36.366 26.569  1.00 38.08  ? 51  ALA   C C   1 
ATOM   1835 O O   . ALA   C 1 52 ? 19.679  -35.208 26.947  1.00 40.40  ? 51  ALA   C O   1 
ATOM   1836 C CB  . ALA   C 1 52 ? 19.549  -37.337 24.287  1.00 36.07  ? 51  ALA   C CB  1 
ATOM   1837 N N   . PHE   C 1 53 ? 20.921  -37.085 26.973  1.00 35.62  ? 52  PHE   C N   1 
ATOM   1838 C CA  . PHE   C 1 53 ? 21.997  -36.478 27.738  1.00 34.35  ? 52  PHE   C CA  1 
ATOM   1839 C C   . PHE   C 1 53 ? 23.180  -36.350 26.806  1.00 35.71  ? 52  PHE   C C   1 
ATOM   1840 O O   . PHE   C 1 53 ? 23.534  -37.323 26.144  1.00 36.68  ? 52  PHE   C O   1 
ATOM   1841 C CB  . PHE   C 1 53 ? 22.405  -37.459 28.850  1.00 36.84  ? 52  PHE   C CB  1 
ATOM   1842 C CG  . PHE   C 1 53 ? 21.418  -37.413 29.997  1.00 32.96  ? 52  PHE   C CG  1 
ATOM   1843 C CD1 . PHE   C 1 53 ? 21.077  -36.210 30.598  1.00 34.90  ? 52  PHE   C CD1 1 
ATOM   1844 C CD2 . PHE   C 1 53 ? 20.781  -38.571 30.432  1.00 47.89  ? 52  PHE   C CD2 1 
ATOM   1845 C CE1 . PHE   C 1 53 ? 20.157  -36.158 31.643  1.00 41.67  ? 52  PHE   C CE1 1 
ATOM   1846 C CE2 . PHE   C 1 53 ? 19.850  -38.513 31.469  1.00 43.61  ? 52  PHE   C CE2 1 
ATOM   1847 C CZ  . PHE   C 1 53 ? 19.529  -37.307 32.064  1.00 43.56  ? 52  PHE   C CZ  1 
ATOM   1848 N N   . LEU   C 1 54 ? 23.806  -35.168 26.772  1.00 30.82  ? 53  LEU   C N   1 
ATOM   1849 C CA  . LEU   C 1 54 ? 24.968  -34.992 25.910  1.00 30.10  ? 53  LEU   C CA  1 
ATOM   1850 C C   . LEU   C 1 54 ? 26.048  -34.218 26.668  1.00 31.98  ? 53  LEU   C C   1 
ATOM   1851 O O   . LEU   C 1 54 ? 25.734  -33.404 27.515  1.00 34.06  ? 53  LEU   C O   1 
ATOM   1852 C CB  . LEU   C 1 54 ? 24.559  -34.236 24.639  1.00 31.55  ? 53  LEU   C CB  1 
ATOM   1853 C CG  . LEU   C 1 54 ? 23.695  -34.990 23.616  1.00 35.09  ? 53  LEU   C CG  1 
ATOM   1854 C CD1 . LEU   C 1 54 ? 23.389  -34.007 22.498  1.00 34.52  ? 53  LEU   C CD1 1 
ATOM   1855 C CD2 . LEU   C 1 54 ? 24.449  -36.193 23.037  1.00 44.39  ? 53  LEU   C CD2 1 
ATOM   1856 N N   . GLY   C 1 55 ? 27.306  -34.415 26.280  1.00 33.46  ? 54  GLY   C N   1 
ATOM   1857 C CA  . GLY   C 1 55 ? 28.402  -33.659 26.869  1.00 34.29  ? 54  GLY   C CA  1 
ATOM   1858 C C   . GLY   C 1 55 ? 28.654  -32.343 26.137  1.00 37.73  ? 54  GLY   C C   1 
ATOM   1859 O O   . GLY   C 1 55 ? 28.114  -32.066 25.053  1.00 33.28  ? 54  GLY   C O   1 
ATOM   1860 N N   . PRO   C 1 56 ? 29.493  -31.458 26.719  1.00 38.77  ? 55  PRO   C N   1 
ATOM   1861 C CA  . PRO   C 1 56 ? 29.576  -30.074 26.261  1.00 41.64  ? 55  PRO   C CA  1 
ATOM   1862 C C   . PRO   C 1 56 ? 30.221  -29.963 24.882  1.00 42.81  ? 55  PRO   C C   1 
ATOM   1863 O O   . PRO   C 1 56 ? 29.980  -28.991 24.156  1.00 46.62  ? 55  PRO   C O   1 
ATOM   1864 C CB  . PRO   C 1 56 ? 30.372  -29.329 27.397  1.00 42.41  ? 55  PRO   C CB  1 
ATOM   1865 C CG  . PRO   C 1 56 ? 31.060  -30.437 28.172  1.00 38.79  ? 55  PRO   C CG  1 
ATOM   1866 C CD  . PRO   C 1 56 ? 30.338  -31.738 27.896  1.00 39.14  ? 55  PRO   C CD  1 
ATOM   1867 N N   . LYS   C 1 57 ? 30.978  -30.996 24.507  1.00 39.97  ? 56  LYS   C N   1 
ATOM   1868 C CA  . LYS   C 1 57 ? 31.666  -31.039 23.232  1.00 41.11  ? 56  LYS   C CA  1 
ATOM   1869 C C   . LYS   C 1 57 ? 30.640  -31.154 22.110  1.00 42.32  ? 56  LYS   C C   1 
ATOM   1870 O O   . LYS   C 1 57 ? 30.969  -30.917 20.952  1.00 41.74  ? 56  LYS   C O   1 
ATOM   1871 C CB  . LYS   C 1 57 ? 32.455  -32.346 23.066  1.00 47.00  ? 56  LYS   C CB  1 
ATOM   1872 N N   . ASP   C 1 58 ? 29.424  -31.568 22.476  1.00 37.05  ? 57  ASP   C N   1 
ATOM   1873 C CA  . ASP   C 1 58 ? 28.418  -31.913 21.473  1.00 37.13  ? 57  ASP   C CA  1 
ATOM   1874 C C   . ASP   C 1 58 ? 27.422  -30.783 21.292  1.00 39.51  ? 57  ASP   C C   1 
ATOM   1875 O O   . ASP   C 1 58 ? 26.416  -30.949 20.586  1.00 35.55  ? 57  ASP   C O   1 
ATOM   1876 C CB  . ASP   C 1 58 ? 27.690  -33.190 21.841  1.00 38.39  ? 57  ASP   C CB  1 
ATOM   1877 C CG  . ASP   C 1 58 ? 28.530  -34.456 21.858  1.00 42.17  ? 57  ASP   C CG  1 
ATOM   1878 O OD1 . ASP   C 1 58 ? 29.438  -34.545 21.040  1.00 45.24  ? 57  ASP   C OD1 1 
ATOM   1879 O OD2 . ASP   C 1 58 ? 28.208  -35.368 22.638  1.00 50.75  ? 57  ASP   C OD2 1 
ATOM   1880 N N   . LEU   C 1 59 ? 27.665  -29.653 21.962  1.00 32.04  ? 58  LEU   C N   1 
ATOM   1881 C CA  . LEU   C 1 59 ? 26.723  -28.554 22.051  1.00 33.91  ? 58  LEU   C CA  1 
ATOM   1882 C C   . LEU   C 1 59 ? 27.357  -27.283 21.507  1.00 36.37  ? 58  LEU   C C   1 
ATOM   1883 O O   . LEU   C 1 59 ? 28.519  -27.020 21.814  1.00 41.01  ? 58  LEU   C O   1 
ATOM   1884 C CB  . LEU   C 1 59 ? 26.367  -28.385 23.522  1.00 34.11  ? 58  LEU   C CB  1 
ATOM   1885 C CG  . LEU   C 1 59 ? 25.831  -29.649 24.192  1.00 32.84  ? 58  LEU   C CG  1 
ATOM   1886 C CD1 . LEU   C 1 59 ? 25.623  -29.359 25.666  1.00 36.81  ? 58  LEU   C CD1 1 
ATOM   1887 C CD2 . LEU   C 1 59 ? 24.492  -30.041 23.551  1.00 27.87  ? 58  LEU   C CD2 1 
ATOM   1888 N N   . PHE   C 1 60 ? 26.565  -26.496 20.764  1.00 36.84  ? 59  PHE   C N   1 
ATOM   1889 C CA  . PHE   C 1 60 ? 27.036  -25.259 20.138  1.00 38.04  ? 59  PHE   C CA  1 
ATOM   1890 C C   . PHE   C 1 60 ? 26.037  -24.154 20.446  1.00 40.61  ? 59  PHE   C C   1 
ATOM   1891 O O   . PHE   C 1 60 ? 24.847  -24.329 20.242  1.00 37.24  ? 59  PHE   C O   1 
ATOM   1892 C CB  . PHE   C 1 60 ? 27.195  -25.507 18.630  1.00 37.97  ? 59  PHE   C CB  1 
ATOM   1893 C CG  . PHE   C 1 60 ? 28.147  -26.662 18.341  1.00 37.06  ? 59  PHE   C CG  1 
ATOM   1894 C CD1 . PHE   C 1 60 ? 27.703  -27.983 18.372  1.00 35.72  ? 59  PHE   C CD1 1 
ATOM   1895 C CD2 . PHE   C 1 60 ? 29.506  -26.438 18.105  1.00 43.92  ? 59  PHE   C CD2 1 
ATOM   1896 C CE1 . PHE   C 1 60 ? 28.576  -29.043 18.184  1.00 35.83  ? 59  PHE   C CE1 1 
ATOM   1897 C CE2 . PHE   C 1 60 ? 30.373  -27.503 17.876  1.00 40.71  ? 59  PHE   C CE2 1 
ATOM   1898 C CZ  . PHE   C 1 60 ? 29.910  -28.804 17.913  1.00 43.10  ? 59  PHE   C CZ  1 
ATOM   1899 N N   . PRO   C 1 61 ? 26.423  -22.979 21.011  1.00 40.83  ? 60  PRO   C N   1 
ATOM   1900 C CA  . PRO   C 1 61 ? 25.416  -21.954 21.298  1.00 37.66  ? 60  PRO   C CA  1 
ATOM   1901 C C   . PRO   C 1 61 ? 24.726  -21.473 20.026  1.00 35.69  ? 60  PRO   C C   1 
ATOM   1902 O O   . PRO   C 1 61 ? 25.369  -21.359 18.994  1.00 41.14  ? 60  PRO   C O   1 
ATOM   1903 C CB  . PRO   C 1 61 ? 26.116  -20.809 22.083  1.00 40.98  ? 60  PRO   C CB  1 
ATOM   1904 C CG  . PRO   C 1 61 ? 27.551  -21.307 22.232  1.00 41.97  ? 60  PRO   C CG  1 
ATOM   1905 C CD  . PRO   C 1 61 ? 27.781  -22.619 21.461  1.00 46.88  ? 60  PRO   C CD  1 
ATOM   1906 N N   . TYR   C 1 62 ? 23.392  -21.310 20.146  1.00 39.15  ? 61  TYR   C N   1 
ATOM   1907 C CA  . TYR   C 1 62 ? 22.469  -21.047 19.054  1.00 40.69  ? 61  TYR   C CA  1 
ATOM   1908 C C   . TYR   C 1 62 ? 22.894  -19.801 18.280  1.00 47.33  ? 61  TYR   C C   1 
ATOM   1909 O O   . TYR   C 1 62 ? 22.972  -19.841 17.055  1.00 44.54  ? 61  TYR   C O   1 
ATOM   1910 C CB  . TYR   C 1 62 ? 21.016  -20.968 19.525  1.00 44.85  ? 61  TYR   C CB  1 
ATOM   1911 C CG  . TYR   C 1 62 ? 20.072  -20.597 18.392  1.00 46.14  ? 61  TYR   C CG  1 
ATOM   1912 C CD1 . TYR   C 1 62 ? 19.871  -21.468 17.316  1.00 42.71  ? 61  TYR   C CD1 1 
ATOM   1913 C CD2 . TYR   C 1 62 ? 19.392  -19.385 18.396  1.00 48.09  ? 61  TYR   C CD2 1 
ATOM   1914 C CE1 . TYR   C 1 62 ? 19.020  -21.131 16.269  1.00 39.19  ? 61  TYR   C CE1 1 
ATOM   1915 C CE2 . TYR   C 1 62 ? 18.528  -19.049 17.365  1.00 47.04  ? 61  TYR   C CE2 1 
ATOM   1916 C CZ  . TYR   C 1 62 ? 18.354  -19.916 16.296  1.00 43.60  ? 61  TYR   C CZ  1 
ATOM   1917 O OH  . TYR   C 1 62 ? 17.507  -19.575 15.274  1.00 43.37  ? 61  TYR   C OH  1 
ATOM   1918 N N   . ASP   C 1 63 ? 23.213  -18.710 18.990  1.00 48.91  ? 62  ASP   C N   1 
ATOM   1919 C CA  . ASP   C 1 63 ? 23.480  -17.460 18.288  1.00 52.96  ? 62  ASP   C CA  1 
ATOM   1920 C C   . ASP   C 1 63 ? 24.773  -17.539 17.495  1.00 47.99  ? 62  ASP   C C   1 
ATOM   1921 O O   . ASP   C 1 63 ? 24.834  -17.046 16.368  1.00 55.52  ? 62  ASP   C O   1 
ATOM   1922 C CB  . ASP   C 1 63 ? 23.347  -16.240 19.184  1.00 57.76  ? 62  ASP   C CB  1 
ATOM   1923 C CG  . ASP   C 1 63 ? 21.940  -15.666 19.184  1.00 72.61  ? 62  ASP   C CG  1 
ATOM   1924 O OD1 . ASP   C 1 63 ? 21.303  -15.680 20.257  1.00 67.82  ? 62  ASP   C OD1 1 
ATOM   1925 O OD2 . ASP   C 1 63 ? 21.486  -15.235 18.096  1.00 84.39  ? 62  ASP   C OD2 1 
ATOM   1926 N N   . LYS   C 1 64 ? 25.783  -18.178 18.083  1.00 42.89  ? 63  LYS   C N   1 
ATOM   1927 C CA  . LYS   C 1 64 ? 27.124  -18.228 17.523  1.00 42.85  ? 63  LYS   C CA  1 
ATOM   1928 C C   . LYS   C 1 64 ? 27.203  -19.191 16.342  1.00 43.66  ? 63  LYS   C C   1 
ATOM   1929 O O   . LYS   C 1 64 ? 28.073  -19.031 15.497  1.00 41.49  ? 63  LYS   C O   1 
ATOM   1930 C CB  . LYS   C 1 64 ? 28.169  -18.642 18.568  1.00 50.01  ? 63  LYS   C CB  1 
ATOM   1931 N N   . SER   C 1 65 ? 26.293  -20.182 16.269  1.00 39.62  ? 64  SER   C N   1 
ATOM   1932 C CA  . SER   C 1 65 ? 26.510  -21.250 15.301  1.00 36.43  ? 64  SER   C CA  1 
ATOM   1933 C C   . SER   C 1 65 ? 25.357  -21.355 14.293  1.00 33.20  ? 64  SER   C C   1 
ATOM   1934 O O   . SER   C 1 65 ? 25.432  -22.165 13.386  1.00 34.29  ? 64  SER   C O   1 
ATOM   1935 C CB  . SER   C 1 65 ? 26.779  -22.589 15.981  1.00 38.27  ? 64  SER   C CB  1 
ATOM   1936 O OG  . SER   C 1 65 ? 25.632  -23.056 16.686  1.00 41.63  ? 64  SER   C OG  1 
ATOM   1937 N N   . LYS   C 1 66 ? 24.303  -20.562 14.478  1.00 33.63  ? 65  LYS   C N   1 
ATOM   1938 C CA  . LYS   C 1 66 ? 23.149  -20.725 13.600  1.00 37.11  ? 65  LYS   C CA  1 
ATOM   1939 C C   . LYS   C 1 66 ? 23.508  -20.429 12.148  1.00 36.77  ? 65  LYS   C C   1 
ATOM   1940 O O   . LYS   C 1 66 ? 22.916  -21.013 11.239  1.00 35.00  ? 65  LYS   C O   1 
ATOM   1941 C CB  . LYS   C 1 66 ? 21.934  -19.893 13.999  1.00 39.67  ? 65  LYS   C CB  1 
ATOM   1942 C CG  . LYS   C 1 66 ? 22.258  -18.409 14.093  1.00 35.48  ? 65  LYS   C CG  1 
ATOM   1943 C CD  . LYS   C 1 66 ? 20.971  -17.698 14.467  1.00 43.33  ? 65  LYS   C CD  1 
ATOM   1944 C CE  . LYS   C 1 66 ? 21.142  -16.246 14.715  1.00 46.90  ? 65  LYS   C CE  1 
ATOM   1945 N NZ  . LYS   C 1 66 ? 19.827  -15.854 15.209  1.00 51.12  ? 65  LYS   C NZ  1 
ATOM   1946 N N   . ASP   C 1 67 ? 24.467  -19.523 11.922  1.00 37.48  ? 66  ASP   C N   1 
ATOM   1947 C CA  . ASP   C 1 67 ? 24.877  -19.225 10.552  1.00 42.53  ? 66  ASP   C CA  1 
ATOM   1948 C C   . ASP   C 1 67 ? 25.300  -20.510 9.855   1.00 43.86  ? 66  ASP   C C   1 
ATOM   1949 O O   . ASP   C 1 67 ? 25.028  -20.701 8.673   1.00 41.19  ? 66  ASP   C O   1 
ATOM   1950 C CB  . ASP   C 1 67 ? 25.879  -18.074 10.449  1.00 45.01  ? 66  ASP   C CB  1 
ATOM   1951 C CG  . ASP   C 1 67 ? 27.294  -18.283 10.989  1.00 61.02  ? 66  ASP   C CG  1 
ATOM   1952 O OD1 . ASP   C 1 67 ? 27.536  -19.269 11.741  1.00 55.60  ? 66  ASP   C OD1 1 
ATOM   1953 O OD2 . ASP   C 1 67 ? 28.157  -17.424 10.681  1.00 63.09  ? 66  ASP   C OD2 1 
ATOM   1954 N N   . LYS   C 1 68 ? 25.895  -21.424 10.632  1.00 38.16  ? 67  LYS   C N   1 
ATOM   1955 C CA  . LYS   C 1 68 ? 26.405  -22.673 10.110  1.00 32.24  ? 67  LYS   C CA  1 
ATOM   1956 C C   . LYS   C 1 68 ? 25.398  -23.839 10.167  1.00 33.44  ? 67  LYS   C C   1 
ATOM   1957 O O   . LYS   C 1 68 ? 25.314  -24.627 9.231   1.00 36.42  ? 67  LYS   C O   1 
ATOM   1958 C CB  . LYS   C 1 68 ? 27.680  -22.980 10.892  1.00 36.86  ? 67  LYS   C CB  1 
ATOM   1959 C CG  . LYS   C 1 68 ? 28.392  -24.233 10.446  1.00 39.03  ? 67  LYS   C CG  1 
ATOM   1960 C CD  . LYS   C 1 68 ? 29.648  -24.407 11.311  1.00 50.71  ? 67  LYS   C CD  1 
ATOM   1961 C CE  . LYS   C 1 68 ? 30.271  -25.764 11.252  1.00 59.15  ? 67  LYS   C CE  1 
ATOM   1962 N NZ  . LYS   C 1 68 ? 30.644  -26.149 9.887   1.00 67.28  ? 67  LYS   C NZ  1 
ATOM   1963 N N   . TYR   C 1 69 ? 24.671  -24.003 11.284  1.00 31.95  ? 68  TYR   C N   1 
ATOM   1964 C CA  . TYR   C 1 69 ? 23.860  -25.207 11.435  1.00 30.44  ? 68  TYR   C CA  1 
ATOM   1965 C C   . TYR   C 1 69 ? 22.380  -24.904 11.212  1.00 33.49  ? 68  TYR   C C   1 
ATOM   1966 O O   . TYR   C 1 69 ? 21.572  -25.823 11.059  1.00 32.10  ? 68  TYR   C O   1 
ATOM   1967 C CB  . TYR   C 1 69 ? 24.024  -25.749 12.866  1.00 31.01  ? 68  TYR   C CB  1 
ATOM   1968 C CG  . TYR   C 1 69 ? 25.445  -26.216 13.144  1.00 29.00  ? 68  TYR   C CG  1 
ATOM   1969 C CD1 . TYR   C 1 69 ? 26.124  -27.022 12.234  1.00 31.74  ? 68  TYR   C CD1 1 
ATOM   1970 C CD2 . TYR   C 1 69 ? 26.087  -25.819 14.306  1.00 34.04  ? 68  TYR   C CD2 1 
ATOM   1971 C CE1 . TYR   C 1 69 ? 27.409  -27.479 12.497  1.00 34.44  ? 68  TYR   C CE1 1 
ATOM   1972 C CE2 . TYR   C 1 69 ? 27.374  -26.252 14.568  1.00 32.27  ? 68  TYR   C CE2 1 
ATOM   1973 C CZ  . TYR   C 1 69 ? 28.031  -27.069 13.661  1.00 34.48  ? 68  TYR   C CZ  1 
ATOM   1974 O OH  . TYR   C 1 69 ? 29.317  -27.467 13.973  1.00 39.63  ? 68  TYR   C OH  1 
ATOM   1975 N N   . GLY   C 1 70 ? 22.026  -23.622 11.196  1.00 29.79  ? 69  GLY   C N   1 
ATOM   1976 C CA  . GLY   C 1 70 ? 20.607  -23.287 11.134  1.00 32.44  ? 69  GLY   C CA  1 
ATOM   1977 C C   . GLY   C 1 70 ? 20.182  -23.168 9.677   1.00 32.99  ? 69  GLY   C C   1 
ATOM   1978 O O   . GLY   C 1 70 ? 20.051  -22.068 9.137   1.00 32.25  ? 69  GLY   C O   1 
ATOM   1979 N N   . LYS   C 1 71 ? 20.115  -24.318 9.025   1.00 31.38  ? 70  LYS   C N   1 
ATOM   1980 C CA  . LYS   C 1 71 ? 19.715  -24.361 7.628   1.00 33.32  ? 70  LYS   C CA  1 
ATOM   1981 C C   . LYS   C 1 71 ? 18.854  -25.591 7.489   1.00 33.64  ? 70  LYS   C C   1 
ATOM   1982 O O   . LYS   C 1 71 ? 18.981  -26.539 8.249   1.00 33.08  ? 70  LYS   C O   1 
ATOM   1983 C CB  . LYS   C 1 71 ? 20.932  -24.539 6.718   1.00 34.57  ? 70  LYS   C CB  1 
ATOM   1984 C CG  . LYS   C 1 71 ? 21.990  -25.441 7.316   1.00 37.28  ? 70  LYS   C CG  1 
ATOM   1985 C CD  . LYS   C 1 71 ? 23.100  -25.931 6.397   1.00 45.69  ? 70  LYS   C CD  1 
ATOM   1986 C CE  . LYS   C 1 71 ? 23.787  -27.035 7.141   1.00 49.60  ? 70  LYS   C CE  1 
ATOM   1987 N N   . PRO   C 1 72 ? 17.876  -25.603 6.568   1.00 28.78  ? 71  PRO   C N   1 
ATOM   1988 C CA  . PRO   C 1 72 ? 16.943  -26.729 6.539   1.00 26.18  ? 71  PRO   C CA  1 
ATOM   1989 C C   . PRO   C 1 72 ? 17.574  -28.066 6.190   1.00 30.84  ? 71  PRO   C C   1 
ATOM   1990 O O   . PRO   C 1 72 ? 18.582  -28.121 5.491   1.00 33.95  ? 71  PRO   C O   1 
ATOM   1991 C CB  . PRO   C 1 72 ? 16.022  -26.288 5.374   1.00 29.36  ? 71  PRO   C CB  1 
ATOM   1992 C CG  . PRO   C 1 72 ? 16.040  -24.799 5.502   1.00 31.11  ? 71  PRO   C CG  1 
ATOM   1993 C CD  . PRO   C 1 72 ? 17.523  -24.469 5.686   1.00 28.32  ? 71  PRO   C CD  1 
ATOM   1994 N N   . ASN   C 1 73 ? 16.898  -29.114 6.620   1.00 30.86  ? 72  ASN   C N   1 
ATOM   1995 C CA  . ASN   C 1 73 ? 17.166  -30.376 5.964   1.00 41.03  ? 72  ASN   C CA  1 
ATOM   1996 C C   . ASN   C 1 73 ? 15.953  -31.258 6.177   1.00 29.01  ? 72  ASN   C C   1 
ATOM   1997 O O   . ASN   C 1 73 ? 15.080  -30.938 6.973   1.00 32.53  ? 72  ASN   C O   1 
ATOM   1998 C CB  . ASN   C 1 73 ? 18.500  -30.999 6.357   1.00 46.27  ? 72  ASN   C CB  1 
ATOM   1999 C CG  . ASN   C 1 73 ? 18.417  -31.629 7.723   1.00 43.00  ? 72  ASN   C CG  1 
ATOM   2000 O OD1 . ASN   C 1 73 ? 17.965  -32.776 7.877   1.00 37.75  ? 72  ASN   C OD1 1 
ATOM   2001 N ND2 . ASN   C 1 73 ? 18.853  -30.871 8.708   1.00 49.56  ? 72  ASN   C ND2 1 
ATOM   2002 N N   . LYS   C 1 74 ? 15.981  -32.414 5.517   1.00 32.83  ? 73  LYS   C N   1 
ATOM   2003 C CA  . LYS   C 1 74 ? 14.742  -33.169 5.367   1.00 31.42  ? 73  LYS   C CA  1 
ATOM   2004 C C   . LYS   C 1 74 ? 14.550  -34.181 6.489   1.00 34.84  ? 73  LYS   C C   1 
ATOM   2005 O O   . LYS   C 1 74 ? 13.557  -34.910 6.521   1.00 36.20  ? 73  LYS   C O   1 
ATOM   2006 C CB  . LYS   C 1 74 ? 14.669  -33.922 4.028   1.00 34.83  ? 73  LYS   C CB  1 
ATOM   2007 N N   . ARG   C 1 75 ? 15.488  -34.253 7.442   1.00 29.77  ? 74  ARG   C N   1 
ATOM   2008 C CA  . ARG   C 1 75 ? 15.256  -35.187 8.532   1.00 27.90  ? 74  ARG   C CA  1 
ATOM   2009 C C   . ARG   C 1 75 ? 13.979  -34.892 9.321   1.00 31.31  ? 74  ARG   C C   1 
ATOM   2010 O O   . ARG   C 1 75 ? 13.578  -33.739 9.548   1.00 31.29  ? 74  ARG   C O   1 
ATOM   2011 C CB  . ARG   C 1 75 ? 16.485  -35.241 9.470   1.00 32.00  ? 74  ARG   C CB  1 
ATOM   2012 C CG  . ARG   C 1 75 ? 17.872  -35.445 8.858   1.00 39.01  ? 74  ARG   C CG  1 
ATOM   2013 C CD  . ARG   C 1 75 ? 18.248  -36.810 8.253   1.00 40.96  ? 74  ARG   C CD  1 
ATOM   2014 N NE  . ARG   C 1 75 ? 18.256  -37.819 9.317   1.00 36.53  ? 74  ARG   C NE  1 
ATOM   2015 C CZ  . ARG   C 1 75 ? 19.392  -38.242 9.881   1.00 34.55  ? 74  ARG   C CZ  1 
ATOM   2016 N NH1 . ARG   C 1 75 ? 19.315  -38.796 11.065  1.00 39.62  ? 74  ARG   C NH1 1 
ATOM   2017 N NH2 . ARG   C 1 75 ? 20.557  -37.936 9.314   1.00 35.55  ? 74  ARG   C NH2 1 
ATOM   2018 N N   . LYS   C 1 76 ? 13.358  -35.982 9.786   1.00 34.41  ? 75  LYS   C N   1 
ATOM   2019 C CA  . LYS   C 1 76 ? 12.068  -35.901 10.450  1.00 37.15  ? 75  LYS   C CA  1 
ATOM   2020 C C   . LYS   C 1 76 ? 12.097  -34.893 11.595  1.00 34.17  ? 75  LYS   C C   1 
ATOM   2021 O O   . LYS   C 1 76 ? 12.847  -35.019 12.574  1.00 31.35  ? 75  LYS   C O   1 
ATOM   2022 C CB  . LYS   C 1 76 ? 11.484  -37.242 10.906  1.00 37.30  ? 75  LYS   C CB  1 
ATOM   2023 C CG  . LYS   C 1 76 ? 9.969   -37.186 11.101  1.00 45.61  ? 75  LYS   C CG  1 
ATOM   2024 C CD  . LYS   C 1 76 ? 9.262   -38.288 11.893  1.00 53.57  ? 75  LYS   C CD  1 
ATOM   2025 N N   . GLY   C 1 77 ? 11.256  -33.863 11.456  1.00 35.86  ? 76  GLY   C N   1 
ATOM   2026 C CA  . GLY   C 1 77 ? 11.007  -32.958 12.566  1.00 29.02  ? 76  GLY   C CA  1 
ATOM   2027 C C   . GLY   C 1 77 ? 11.992  -31.778 12.575  1.00 26.66  ? 76  GLY   C C   1 
ATOM   2028 O O   . GLY   C 1 77 ? 11.816  -30.852 13.351  1.00 32.54  ? 76  GLY   C O   1 
ATOM   2029 N N   . PHE   C 1 78 ? 12.979  -31.770 11.686  1.00 27.69  ? 77  PHE   C N   1 
ATOM   2030 C CA  . PHE   C 1 78 ? 14.076  -30.823 11.788  1.00 26.81  ? 77  PHE   C CA  1 
ATOM   2031 C C   . PHE   C 1 78 ? 13.580  -29.397 11.524  1.00 30.72  ? 77  PHE   C C   1 
ATOM   2032 O O   . PHE   C 1 78 ? 13.917  -28.441 12.228  1.00 29.18  ? 77  PHE   C O   1 
ATOM   2033 C CB  . PHE   C 1 78 ? 15.186  -31.228 10.816  1.00 30.47  ? 77  PHE   C CB  1 
ATOM   2034 C CG  . PHE   C 1 78 ? 16.442  -30.415 11.057  1.00 28.08  ? 77  PHE   C CG  1 
ATOM   2035 C CD1 . PHE   C 1 78 ? 16.601  -29.166 10.488  1.00 30.85  ? 77  PHE   C CD1 1 
ATOM   2036 C CD2 . PHE   C 1 78 ? 17.475  -30.922 11.846  1.00 27.50  ? 77  PHE   C CD2 1 
ATOM   2037 C CE1 . PHE   C 1 78 ? 17.761  -28.432 10.711  1.00 27.78  ? 77  PHE   C CE1 1 
ATOM   2038 C CE2 . PHE   C 1 78 ? 18.627  -30.185 12.082  1.00 28.35  ? 77  PHE   C CE2 1 
ATOM   2039 C CZ  . PHE   C 1 78 ? 18.779  -28.941 11.514  1.00 26.91  ? 77  PHE   C CZ  1 
ATOM   2040 N N   . ASN   C 1 79 ? 12.786  -29.257 10.450  1.00 29.80  ? 78  ASN   C N   1 
ATOM   2041 C CA  . ASN   C 1 79 ? 12.485  -27.904 10.027  1.00 30.72  ? 78  ASN   C CA  1 
ATOM   2042 C C   . ASN   C 1 79 ? 11.466  -27.273 10.970  1.00 28.50  ? 78  ASN   C C   1 
ATOM   2043 O O   . ASN   C 1 79 ? 11.483  -26.060 11.253  1.00 28.93  ? 78  ASN   C O   1 
ATOM   2044 C CB  . ASN   C 1 79 ? 12.007  -27.915 8.582   1.00 28.02  ? 78  ASN   C CB  1 
ATOM   2045 C CG  . ASN   C 1 79 ? 13.118  -28.254 7.622   1.00 31.35  ? 78  ASN   C CG  1 
ATOM   2046 O OD1 . ASN   C 1 79 ? 14.275  -27.925 7.892   1.00 29.94  ? 78  ASN   C OD1 1 
ATOM   2047 N ND2 . ASN   C 1 79 ? 12.778  -28.794 6.464   1.00 28.66  ? 78  ASN   C ND2 1 
ATOM   2048 N N   . GLU   C 1 80 ? 10.574  -28.108 11.489  1.00 31.71  ? 79  GLU   C N   1 
ATOM   2049 C CA  . GLU   C 1 80 ? 9.713   -27.617 12.554  1.00 28.59  ? 79  GLU   C CA  1 
ATOM   2050 C C   . GLU   C 1 80 ? 10.571  -27.220 13.754  1.00 34.01  ? 79  GLU   C C   1 
ATOM   2051 O O   . GLU   C 1 80 ? 10.277  -26.225 14.410  1.00 30.66  ? 79  GLU   C O   1 
ATOM   2052 C CB  . GLU   C 1 80 ? 8.596   -28.621 12.859  1.00 35.61  ? 79  GLU   C CB  1 
ATOM   2053 C CG  . GLU   C 1 80 ? 7.673   -28.205 14.002  1.00 32.01  ? 79  GLU   C CG  1 
ATOM   2054 C CD  . GLU   C 1 80 ? 6.394   -29.008 14.121  1.00 45.70  ? 79  GLU   C CD  1 
ATOM   2055 O OE1 . GLU   C 1 80 ? 6.358   -30.143 13.598  1.00 45.32  ? 79  GLU   C OE1 1 
ATOM   2056 O OE2 . GLU   C 1 80 ? 5.409   -28.506 14.697  1.00 44.48  ? 79  GLU   C OE2 1 
ATOM   2057 N N   . GLY   C 1 81 ? 11.641  -28.008 14.037  1.00 28.83  ? 80  GLY   C N   1 
ATOM   2058 C CA  . GLY   C 1 81 ? 12.586  -27.609 15.079  1.00 29.60  ? 80  GLY   C CA  1 
ATOM   2059 C C   . GLY   C 1 81 ? 13.158  -26.206 14.871  1.00 30.03  ? 80  GLY   C C   1 
ATOM   2060 O O   . GLY   C 1 81 ? 13.331  -25.439 15.816  1.00 30.86  ? 80  GLY   C O   1 
ATOM   2061 N N   . LEU   C 1 82 ? 13.609  -25.936 13.634  1.00 29.84  ? 81  LEU   C N   1 
ATOM   2062 C CA  . LEU   C 1 82 ? 14.153  -24.626 13.305  1.00 30.06  ? 81  LEU   C CA  1 
ATOM   2063 C C   . LEU   C 1 82 ? 13.113  -23.534 13.550  1.00 27.24  ? 81  LEU   C C   1 
ATOM   2064 O O   . LEU   C 1 82 ? 13.474  -22.454 14.028  1.00 30.84  ? 81  LEU   C O   1 
ATOM   2065 C CB  . LEU   C 1 82 ? 14.619  -24.596 11.843  1.00 28.92  ? 81  LEU   C CB  1 
ATOM   2066 C CG  . LEU   C 1 82 ? 15.900  -25.346 11.441  1.00 29.40  ? 81  LEU   C CG  1 
ATOM   2067 C CD1 . LEU   C 1 82 ? 16.206  -25.279 9.947   1.00 29.29  ? 81  LEU   C CD1 1 
ATOM   2068 C CD2 . LEU   C 1 82 ? 17.153  -24.928 12.200  1.00 27.15  ? 81  LEU   C CD2 1 
ATOM   2069 N N   . TRP   C 1 83 ? 11.847  -23.815 13.236  1.00 27.97  ? 82  TRP   C N   1 
ATOM   2070 C CA  . TRP   C 1 83 ? 10.827  -22.796 13.467  1.00 31.84  ? 82  TRP   C CA  1 
ATOM   2071 C C   . TRP   C 1 83 ? 10.707  -22.516 14.973  1.00 33.95  ? 82  TRP   C C   1 
ATOM   2072 O O   . TRP   C 1 83 ? 10.724  -21.353 15.404  1.00 34.20  ? 82  TRP   C O   1 
ATOM   2073 C CB  . TRP   C 1 83 ? 9.479   -23.156 12.816  1.00 31.93  ? 82  TRP   C CB  1 
ATOM   2074 C CG  . TRP   C 1 83 ? 8.470   -22.049 13.008  1.00 35.92  ? 82  TRP   C CG  1 
ATOM   2075 C CD1 . TRP   C 1 83 ? 8.302   -20.968 12.180  1.00 36.96  ? 82  TRP   C CD1 1 
ATOM   2076 C CD2 . TRP   C 1 83 ? 7.564   -21.846 14.120  1.00 38.50  ? 82  TRP   C CD2 1 
ATOM   2077 N NE1 . TRP   C 1 83 ? 7.335   -20.135 12.674  1.00 36.23  ? 82  TRP   C NE1 1 
ATOM   2078 C CE2 . TRP   C 1 83 ? 6.860   -20.645 13.854  1.00 38.09  ? 82  TRP   C CE2 1 
ATOM   2079 C CE3 . TRP   C 1 83 ? 7.263   -22.578 15.283  1.00 35.59  ? 82  TRP   C CE3 1 
ATOM   2080 C CZ2 . TRP   C 1 83 ? 5.894   -20.155 14.732  1.00 43.94  ? 82  TRP   C CZ2 1 
ATOM   2081 C CZ3 . TRP   C 1 83 ? 6.312   -22.090 16.154  1.00 42.98  ? 82  TRP   C CZ3 1 
ATOM   2082 C CH2 . TRP   C 1 83 ? 5.665   -20.879 15.890  1.00 42.73  ? 82  TRP   C CH2 1 
ATOM   2083 N N   . GLU   C 1 84 ? 10.768  -23.596 15.780  1.00 30.81  ? 83  GLU   C N   1 
ATOM   2084 C CA  . GLU   C 1 84 ? 10.546  -23.459 17.217  1.00 37.09  ? 83  GLU   C CA  1 
ATOM   2085 C C   . GLU   C 1 84 ? 11.674  -22.680 17.895  1.00 36.19  ? 83  GLU   C C   1 
ATOM   2086 O O   . GLU   C 1 84 ? 11.419  -21.816 18.743  1.00 38.84  ? 83  GLU   C O   1 
ATOM   2087 C CB  . GLU   C 1 84 ? 10.396  -24.817 17.908  1.00 32.96  ? 83  GLU   C CB  1 
ATOM   2088 C CG  . GLU   C 1 84 ? 9.149   -25.562 17.459  1.00 34.33  ? 83  GLU   C CG  1 
ATOM   2089 C CD  . GLU   C 1 84 ? 9.033   -26.972 17.997  1.00 36.90  ? 83  GLU   C CD  1 
ATOM   2090 O OE1 . GLU   C 1 84 ? 9.994   -27.407 18.688  1.00 36.30  ? 83  GLU   C OE1 1 
ATOM   2091 O OE2 . GLU   C 1 84 ? 8.007   -27.624 17.705  1.00 39.08  ? 83  GLU   C OE2 1 
ATOM   2092 N N   . ILE   C 1 85 ? 12.922  -22.915 17.468  1.00 31.80  ? 84  ILE   C N   1 
ATOM   2093 C CA  . ILE   C 1 85 ? 14.073  -22.323 18.125  1.00 33.37  ? 84  ILE   C CA  1 
ATOM   2094 C C   . ILE   C 1 85 ? 14.174  -20.812 17.862  1.00 37.35  ? 84  ILE   C C   1 
ATOM   2095 O O   . ILE   C 1 85 ? 14.676  -20.057 18.692  1.00 33.65  ? 84  ILE   C O   1 
ATOM   2096 C CB  . ILE   C 1 85 ? 15.358  -23.072 17.779  1.00 32.19  ? 84  ILE   C CB  1 
ATOM   2097 C CG1 . ILE   C 1 85 ? 16.434  -22.682 18.791  1.00 32.06  ? 84  ILE   C CG1 1 
ATOM   2098 C CG2 . ILE   C 1 85 ? 15.803  -22.826 16.327  1.00 32.92  ? 84  ILE   C CG2 1 
ATOM   2099 C CD1 . ILE   C 1 85 ? 17.621  -23.631 18.918  1.00 31.89  ? 84  ILE   C CD1 1 
ATOM   2100 N N   . GLN   C 1 86 ? 13.716  -20.399 16.675  1.00 34.59  ? 85  GLN   C N   1 
ATOM   2101 C CA  . GLN   C 1 86 ? 13.680  -18.991 16.311  1.00 37.20  ? 85  GLN   C CA  1 
ATOM   2102 C C   . GLN   C 1 86 ? 12.431  -18.269 16.825  1.00 34.00  ? 85  GLN   C C   1 
ATOM   2103 O O   . GLN   C 1 86 ? 12.523  -17.088 17.160  1.00 39.96  ? 85  GLN   C O   1 
ATOM   2104 C CB  . GLN   C 1 86 ? 13.824  -18.919 14.789  1.00 34.56  ? 85  GLN   C CB  1 
ATOM   2105 C CG  . GLN   C 1 86 ? 13.988  -17.490 14.271  1.00 34.59  ? 85  GLN   C CG  1 
ATOM   2106 C CD  . GLN   C 1 86 ? 14.445  -17.458 12.829  1.00 33.86  ? 85  GLN   C CD  1 
ATOM   2107 O OE1 . GLN   C 1 86 ? 14.372  -18.457 12.105  1.00 35.35  ? 85  GLN   C OE1 1 
ATOM   2108 N NE2 . GLN   C 1 86 ? 15.011  -16.333 12.422  1.00 35.05  ? 85  GLN   C NE2 1 
ATOM   2109 N N   . ASN   C 1 87 ? 11.288  -18.942 16.890  1.00 36.30  ? 86  ASN   C N   1 
ATOM   2110 C CA  . ASN   C 1 87 ? 9.997   -18.288 17.039  1.00 42.97  ? 86  ASN   C CA  1 
ATOM   2111 C C   . ASN   C 1 87 ? 9.270   -18.653 18.338  1.00 45.62  ? 86  ASN   C C   1 
ATOM   2112 O O   . ASN   C 1 87 ? 8.330   -17.953 18.697  1.00 46.14  ? 86  ASN   C O   1 
ATOM   2113 C CB  . ASN   C 1 87 ? 9.082   -18.562 15.848  1.00 38.49  ? 86  ASN   C CB  1 
ATOM   2114 C CG  . ASN   C 1 87 ? 9.682   -17.973 14.596  1.00 41.71  ? 86  ASN   C CG  1 
ATOM   2115 O OD1 . ASN   C 1 87 ? 9.769   -16.747 14.491  1.00 39.60  ? 86  ASN   C OD1 1 
ATOM   2116 N ND2 . ASN   C 1 87 ? 10.152  -18.814 13.680  1.00 36.52  ? 86  ASN   C ND2 1 
ATOM   2117 N N   . ASN   C 1 88 ? 9.630   -19.756 19.011  1.00 45.34  ? 87  ASN   C N   1 
ATOM   2118 C CA  . ASN   C 1 88 ? 8.867   -20.165 20.197  1.00 41.90  ? 87  ASN   C CA  1 
ATOM   2119 C C   . ASN   C 1 88 ? 9.734   -21.042 21.099  1.00 43.92  ? 87  ASN   C C   1 
ATOM   2120 O O   . ASN   C 1 88 ? 9.315   -22.154 21.446  1.00 44.65  ? 87  ASN   C O   1 
ATOM   2121 C CB  . ASN   C 1 88 ? 7.610   -20.944 19.810  1.00 47.68  ? 87  ASN   C CB  1 
ATOM   2122 C CG  . ASN   C 1 88 ? 6.580   -20.982 20.920  1.00 52.22  ? 87  ASN   C CG  1 
ATOM   2123 O OD1 . ASN   C 1 88 ? 6.658   -20.203 21.877  1.00 55.03  ? 87  ASN   C OD1 1 
ATOM   2124 N ND2 . ASN   C 1 88 ? 5.602   -21.866 20.799  1.00 53.02  ? 87  ASN   C ND2 1 
ATOM   2125 N N   . PRO   C 1 89 ? 10.955  -20.583 21.453  1.00 38.71  ? 88  PRO   C N   1 
ATOM   2126 C CA  . PRO   C 1 89 ? 11.990  -21.444 22.044  1.00 42.76  ? 88  PRO   C CA  1 
ATOM   2127 C C   . PRO   C 1 89 ? 11.772  -21.892 23.485  1.00 47.50  ? 88  PRO   C C   1 
ATOM   2128 O O   . PRO   C 1 89 ? 12.530  -22.734 23.982  1.00 44.08  ? 88  PRO   C O   1 
ATOM   2129 C CB  . PRO   C 1 89 ? 13.273  -20.635 21.925  1.00 39.22  ? 88  PRO   C CB  1 
ATOM   2130 C CG  . PRO   C 1 89 ? 12.792  -19.199 21.923  1.00 40.46  ? 88  PRO   C CG  1 
ATOM   2131 C CD  . PRO   C 1 89 ? 11.466  -19.235 21.182  1.00 38.40  ? 88  PRO   C CD  1 
ATOM   2132 N N   . HIS   C 1 90 ? 10.757  -21.304 24.135  1.00 48.84  ? 89  HIS   C N   1 
ATOM   2133 C CA  . HIS   C 1 90 ? 10.483  -21.596 25.535  1.00 51.82  ? 89  HIS   C CA  1 
ATOM   2134 C C   . HIS   C 1 90 ? 9.029   -22.005 25.768  1.00 52.17  ? 89  HIS   C C   1 
ATOM   2135 O O   . HIS   C 1 90 ? 8.544   -21.926 26.895  1.00 58.46  ? 89  HIS   C O   1 
ATOM   2136 C CB  . HIS   C 1 90 ? 10.953  -20.462 26.455  1.00 45.86  ? 89  HIS   C CB  1 
ATOM   2137 C CG  . HIS   C 1 90 ? 12.348  -19.989 26.241  1.00 45.22  ? 89  HIS   C CG  1 
ATOM   2138 N ND1 . HIS   C 1 90 ? 13.480  -20.724 26.540  1.00 47.50  ? 89  HIS   C ND1 1 
ATOM   2139 C CD2 . HIS   C 1 90 ? 12.784  -18.823 25.758  1.00 43.89  ? 89  HIS   C CD2 1 
ATOM   2140 C CE1 . HIS   C 1 90 ? 14.561  -20.003 26.252  1.00 47.73  ? 89  HIS   C CE1 1 
ATOM   2141 N NE2 . HIS   C 1 90 ? 14.159  -18.842 25.769  1.00 43.58  ? 89  HIS   C NE2 1 
ATOM   2142 N N   . ALA   C 1 91 ? 8.334   -22.466 24.721  1.00 54.20  ? 90  ALA   C N   1 
ATOM   2143 C CA  . ALA   C 1 91 ? 7.054   -23.136 24.901  1.00 56.43  ? 90  ALA   C CA  1 
ATOM   2144 C C   . ALA   C 1 91 ? 7.297   -24.516 25.521  1.00 64.44  ? 90  ALA   C C   1 
ATOM   2145 O O   . ALA   C 1 91 ? 8.439   -24.974 25.587  1.00 65.51  ? 90  ALA   C O   1 
ATOM   2146 C CB  . ALA   C 1 91 ? 6.298   -23.219 23.587  1.00 54.03  ? 90  ALA   C CB  1 
ATOM   2147 N N   . SER   C 1 92 ? 6.211   -25.172 25.954  1.00 66.17  ? 91  SER   C N   1 
ATOM   2148 C CA  . SER   C 1 92 ? 6.273   -26.389 26.756  1.00 68.08  ? 91  SER   C CA  1 
ATOM   2149 C C   . SER   C 1 92 ? 6.571   -27.625 25.910  1.00 68.72  ? 91  SER   C C   1 
ATOM   2150 O O   . SER   C 1 92 ? 7.430   -28.425 26.272  1.00 73.72  ? 91  SER   C O   1 
ATOM   2151 C CB  . SER   C 1 92 ? 4.989   -26.588 27.519  1.00 70.22  ? 91  SER   C CB  1 
ATOM   2152 O OG  . SER   C 1 92 ? 4.710   -25.442 28.306  1.00 72.62  ? 91  SER   C OG  1 
ATOM   2153 N N   . TYR   C 1 93 ? 5.794   -27.805 24.834  1.00 68.80  ? 92  TYR   C N   1 
ATOM   2154 C CA  . TYR   C 1 93 ? 5.879   -28.954 23.941  1.00 70.82  ? 92  TYR   C CA  1 
ATOM   2155 C C   . TYR   C 1 93 ? 5.722   -30.262 24.736  1.00 73.02  ? 92  TYR   C C   1 
ATOM   2156 O O   . TYR   C 1 93 ? 4.655   -30.435 25.374  1.00 80.20  ? 92  TYR   C O   1 
ATOM   2157 C CB  . TYR   C 1 93 ? 7.157   -28.905 23.092  1.00 63.92  ? 92  TYR   C CB  1 
ATOM   2158 C CG  . TYR   C 1 93 ? 7.308   -27.629 22.269  1.00 54.65  ? 92  TYR   C CG  1 
ATOM   2159 C CD1 . TYR   C 1 93 ? 6.431   -27.346 21.226  1.00 50.62  ? 92  TYR   C CD1 1 
ATOM   2160 C CD2 . TYR   C 1 93 ? 8.341   -26.731 22.515  1.00 52.46  ? 92  TYR   C CD2 1 
ATOM   2161 C CE1 . TYR   C 1 93 ? 6.546   -26.190 20.473  1.00 49.03  ? 92  TYR   C CE1 1 
ATOM   2162 C CE2 . TYR   C 1 93 ? 8.487   -25.585 21.751  1.00 48.01  ? 92  TYR   C CE2 1 
ATOM   2163 C CZ  . TYR   C 1 93 ? 7.586   -25.315 20.737  1.00 51.32  ? 92  TYR   C CZ  1 
ATOM   2164 O OH  . TYR   C 1 93 ? 7.745   -24.163 20.027  1.00 49.70  ? 92  TYR   C OH  1 
HETATM 2165 S S   . SO4   D 2 .  ? 1.471   -33.799 1.708   1.00 81.73  ? 101 SO4   A S   1 
HETATM 2166 O O1  . SO4   D 2 .  ? 2.097   -34.281 0.502   1.00 64.64  ? 101 SO4   A O1  1 
HETATM 2167 O O2  . SO4   D 2 .  ? 1.399   -32.355 1.683   1.00 64.62  ? 101 SO4   A O2  1 
HETATM 2168 O O3  . SO4   D 2 .  ? 0.140   -34.349 1.801   1.00 86.72  ? 101 SO4   A O3  1 
HETATM 2169 O O4  . SO4   D 2 .  ? 2.240   -34.222 2.852   1.00 73.55  ? 101 SO4   A O4  1 
HETATM 2170 S S   . SO4   E 2 .  ? -9.350  -24.645 1.273   1.00 99.13  ? 102 SO4   A S   1 
HETATM 2171 O O1  . SO4   E 2 .  ? -9.434  -24.357 -0.132  1.00 85.56  ? 102 SO4   A O1  1 
HETATM 2172 O O2  . SO4   E 2 .  ? -9.912  -23.549 2.019   1.00 98.38  ? 102 SO4   A O2  1 
HETATM 2173 O O3  . SO4   E 2 .  ? -10.082 -25.852 1.556   1.00 106.94 ? 102 SO4   A O3  1 
HETATM 2174 O O4  . SO4   E 2 .  ? -7.975  -24.826 1.653   1.00 101.11 ? 102 SO4   A O4  1 
HETATM 2175 C C1  . EDO   F 3 .  ? 13.944  -19.419 -7.296  1.00 39.16  ? 103 EDO   A C1  1 
HETATM 2176 O O1  . EDO   F 3 .  ? 15.223  -18.802 -7.255  1.00 32.13  ? 103 EDO   A O1  1 
HETATM 2177 C C2  . EDO   F 3 .  ? 13.089  -18.993 -8.478  1.00 36.72  ? 103 EDO   A C2  1 
HETATM 2178 O O2  . EDO   F 3 .  ? 12.530  -17.710 -8.275  1.00 34.82  ? 103 EDO   A O2  1 
HETATM 2179 S S   . SO4   G 2 .  ? 9.128   -29.443 5.804   1.00 52.09  ? 104 SO4   A S   1 
HETATM 2180 O O1  . SO4   G 2 .  ? 9.972   -28.772 4.922   1.00 45.28  ? 104 SO4   A O1  1 
HETATM 2181 O O2  . SO4   G 2 .  ? 8.580   -30.603 5.112   1.00 58.37  ? 104 SO4   A O2  1 
HETATM 2182 O O3  . SO4   G 2 .  ? 9.875   -29.883 6.970   1.00 58.50  ? 104 SO4   A O3  1 
HETATM 2183 O O4  . SO4   G 2 .  ? 8.047   -28.582 6.198   1.00 68.40  ? 104 SO4   A O4  1 
HETATM 2184 S S   . SO4   H 2 .  ? 7.342   -8.663  -24.909 1.00 62.62  ? 101 SO4   B S   1 
HETATM 2185 O O1  . SO4   H 2 .  ? 8.508   -8.714  -25.771 1.00 41.63  ? 101 SO4   B O1  1 
HETATM 2186 O O2  . SO4   H 2 .  ? 6.222   -9.298  -25.541 1.00 46.96  ? 101 SO4   B O2  1 
HETATM 2187 O O3  . SO4   H 2 .  ? 7.572   -9.339  -23.638 1.00 48.32  ? 101 SO4   B O3  1 
HETATM 2188 O O4  . SO4   H 2 .  ? 7.083   -7.259  -24.678 1.00 63.98  ? 101 SO4   B O4  1 
HETATM 2189 S S   . SO4   I 2 .  ? 14.645  -27.021 -26.267 1.00 54.57  ? 102 SO4   B S   1 
HETATM 2190 O O1  . SO4   I 2 .  ? 15.986  -26.633 -25.941 1.00 57.60  ? 102 SO4   B O1  1 
HETATM 2191 O O2  . SO4   I 2 .  ? 14.673  -28.346 -26.831 1.00 64.36  ? 102 SO4   B O2  1 
HETATM 2192 O O3  . SO4   I 2 .  ? 13.846  -27.013 -25.074 1.00 62.09  ? 102 SO4   B O3  1 
HETATM 2193 O O4  . SO4   I 2 .  ? 14.079  -26.110 -27.231 1.00 55.56  ? 102 SO4   B O4  1 
HETATM 2194 N N1  . A1AJ5 J 4 .  ? 18.283  -16.244 -21.931 0.63 43.96  ? 103 A1AJ5 B N1  1 
HETATM 2195 N N3  . A1AJ5 J 4 .  ? 18.305  -15.880 -19.820 0.63 54.75  ? 103 A1AJ5 B N3  1 
HETATM 2196 C C4  . A1AJ5 J 4 .  ? 17.779  -16.146 -23.264 0.63 38.54  ? 103 A1AJ5 B C4  1 
HETATM 2197 C C5  . A1AJ5 J 4 .  ? 16.633  -15.414 -23.511 0.63 34.95  ? 103 A1AJ5 B C5  1 
HETATM 2198 C C6  . A1AJ5 J 4 .  ? 16.213  -15.220 -24.813 0.63 38.11  ? 103 A1AJ5 B C6  1 
HETATM 2199 C C7  . A1AJ5 J 4 .  ? 16.918  -15.761 -25.856 0.63 39.71  ? 103 A1AJ5 B C7  1 
HETATM 2200 C C8  . A1AJ5 J 4 .  ? 18.047  -16.509 -25.607 0.63 39.25  ? 103 A1AJ5 B C8  1 
HETATM 2201 N N   . A1AJ5 J 4 .  ? 21.850  -16.962 -19.629 0.63 54.26  ? 103 A1AJ5 B N   1 
HETATM 2202 C C1  . A1AJ5 J 4 .  ? 20.472  -16.947 -19.120 0.63 56.40  ? 103 A1AJ5 B C1  1 
HETATM 2203 C C   . A1AJ5 J 4 .  ? 20.344  -15.963 -17.960 0.63 53.71  ? 103 A1AJ5 B C   1 
HETATM 2204 C C2  . A1AJ5 J 4 .  ? 19.431  -16.583 -20.140 0.63 49.36  ? 103 A1AJ5 B C2  1 
HETATM 2205 N N2  . A1AJ5 J 4 .  ? 17.605  -15.671 -20.908 0.63 50.60  ? 103 A1AJ5 B N2  1 
HETATM 2206 C C3  . A1AJ5 J 4 .  ? 19.416  -16.826 -21.479 0.63 46.12  ? 103 A1AJ5 B C3  1 
HETATM 2207 C C9  . A1AJ5 J 4 .  ? 18.484  -16.705 -24.311 0.63 35.04  ? 103 A1AJ5 B C9  1 
HETATM 2208 C C1  . EDO   K 3 .  ? 16.759  -36.315 16.351  1.00 30.83  ? 101 EDO   C C1  1 
HETATM 2209 O O1  . EDO   K 3 .  ? 15.698  -37.015 15.700  1.00 35.79  ? 101 EDO   C O1  1 
HETATM 2210 C C2  . EDO   K 3 .  ? 16.347  -35.280 17.375  1.00 32.59  ? 101 EDO   C C2  1 
HETATM 2211 O O2  . EDO   K 3 .  ? 15.468  -35.814 18.355  1.00 33.03  ? 101 EDO   C O2  1 
HETATM 2212 S S   . SO4   L 2 .  ? 29.282  -38.363 12.376  1.00 90.90  ? 102 SO4   C S   1 
HETATM 2213 O O1  . SO4   L 2 .  ? 30.111  -37.410 11.677  1.00 87.26  ? 102 SO4   C O1  1 
HETATM 2214 O O2  . SO4   L 2 .  ? 27.895  -38.064 12.150  1.00 60.94  ? 102 SO4   C O2  1 
HETATM 2215 O O3  . SO4   L 2 .  ? 29.554  -39.689 11.892  1.00 71.87  ? 102 SO4   C O3  1 
HETATM 2216 O O4  . SO4   L 2 .  ? 29.561  -38.290 13.790  1.00 89.75  ? 102 SO4   C O4  1 
HETATM 2217 O O   . HOH   M 5 .  ? 8.678   -32.171 4.157   1.00 57.34  ? 201 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? 10.606  -19.068 10.216  1.00 66.42  ? 202 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 3.817   -34.592 4.395   1.00 53.14  ? 203 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 5.760   -29.045 6.709   1.00 53.80  ? 204 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 11.177  -29.660 3.007   1.00 46.57  ? 205 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 10.888  -8.814  -13.223 1.00 57.66  ? 206 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? 12.999  -11.999 8.029   1.00 53.82  ? 207 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 7.139   -10.503 -12.039 1.00 42.15  ? 208 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? -5.813  -13.487 -16.526 1.00 52.04  ? 209 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? -1.702  -33.870 0.174   1.00 50.69  ? 210 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 4.187   -10.432 13.697  1.00 55.05  ? 211 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? -2.447  -30.773 -3.856  1.00 56.79  ? 212 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? -2.646  -11.795 13.863  1.00 46.16  ? 213 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? 9.138   -18.133 -11.019 1.00 36.95  ? 214 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? -2.277  3.163   -1.964  1.00 43.17  ? 215 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 15.871  -24.477 1.983   1.00 42.36  ? 216 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 0.408   -10.569 -15.649 1.00 50.10  ? 217 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 2.509   -25.275 -6.491  1.00 45.90  ? 218 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? 11.147  -23.725 9.768   1.00 35.90  ? 219 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? 1.117   -24.900 13.922  1.00 48.66  ? 220 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 4.473   -3.520  -3.231  1.00 33.99  ? 221 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 19.811  -15.628 7.277   1.00 30.47  ? 222 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 8.285   -17.881 -15.883 1.00 52.22  ? 223 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 9.591   -5.955  -1.664  1.00 35.03  ? 224 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? 4.593   -7.834  1.166   1.00 36.71  ? 225 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? -3.805  -11.096 6.892   1.00 39.10  ? 226 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 0.410   -33.632 4.745   1.00 60.25  ? 227 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 13.283  -27.977 -4.787  1.00 50.35  ? 228 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? -7.803  -17.256 6.567   1.00 43.73  ? 229 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? -0.499  -29.397 9.915   1.00 57.50  ? 230 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? -6.758  -5.394  9.336   1.00 35.28  ? 231 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? 14.781  -17.257 -19.012 1.00 40.96  ? 232 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? -8.113  -15.723 -1.105  1.00 37.42  ? 233 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 10.805  -5.052  -7.663  1.00 36.77  ? 234 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? -7.782  -16.793 1.578   1.00 40.62  ? 235 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? -8.513  -21.168 -1.325  1.00 39.65  ? 236 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? -6.211  -11.373 -11.261 1.00 39.85  ? 237 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 13.307  -11.878 -4.261  1.00 22.72  ? 238 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 15.556  -28.019 -0.599  1.00 50.95  ? 239 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? -0.622  -20.991 6.994   1.00 35.14  ? 240 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? -1.716  -22.069 -0.687  1.00 28.76  ? 241 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 1.862   0.637   -7.413  1.00 38.02  ? 242 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 2.500   -25.230 -9.991  1.00 36.82  ? 243 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -5.709  -15.925 -8.090  1.00 30.08  ? 244 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 0.217   -23.352 9.074   1.00 42.99  ? 245 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 11.433  -5.991  -3.948  1.00 43.66  ? 246 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? 11.547  -11.878 5.890   1.00 35.57  ? 247 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? 17.180  -12.849 1.363   1.00 20.78  ? 248 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 1.838   -4.706  -10.237 1.00 37.82  ? 249 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 15.738  -12.000 -5.349  1.00 33.35  ? 250 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 11.489  -12.337 -6.158  1.00 28.84  ? 251 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? -5.778  -19.719 -5.701  1.00 36.64  ? 252 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 16.440  -11.528 -17.245 1.00 46.18  ? 253 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? 3.245   -29.633 -0.564  1.00 38.16  ? 254 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 9.670   -30.539 9.720   1.00 37.00  ? 255 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? -4.337  -25.910 -5.519  1.00 44.68  ? 256 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? 6.616   -15.992 -14.960 1.00 46.92  ? 257 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -1.326  -7.668  11.560  1.00 47.04  ? 258 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? 12.904  -9.554  -7.125  1.00 41.86  ? 259 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? -1.272  -11.838 11.317  1.00 36.85  ? 260 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? 2.464   -6.339  5.491   1.00 36.75  ? 261 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 10.055  -13.075 9.663   1.00 41.16  ? 262 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? -0.594  -20.612 11.181  1.00 60.41  ? 263 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? -4.116  -21.355 6.079   1.00 41.33  ? 264 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? 1.770   -10.533 11.697  1.00 36.53  ? 265 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? 8.962   -16.321 -13.204 1.00 42.37  ? 266 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 1.679   -18.723 -18.626 1.00 40.50  ? 267 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 11.787  -16.305 -14.730 1.00 49.71  ? 268 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? -7.246  -21.664 -5.880  1.00 51.28  ? 269 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 7.915   -7.832  1.280   1.00 31.75  ? 270 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? 12.622  -13.233 -8.580  1.00 41.22  ? 271 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? 0.027   -31.531 -3.331  1.00 49.33  ? 272 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 14.637  -13.240 10.383  1.00 47.59  ? 273 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 8.092   -17.596 8.677   1.00 44.84  ? 274 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? 3.011   -9.924  -13.223 1.00 42.40  ? 275 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? -6.046  -12.769 6.700   1.00 39.40  ? 276 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? -10.927 -15.981 -3.372  1.00 50.78  ? 277 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 12.099  -16.119 -11.965 1.00 59.10  ? 278 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 9.786   -20.175 -18.375 1.00 45.18  ? 279 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -4.180  -7.847  -11.089 1.00 66.90  ? 280 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 16.945  -18.111 -9.653  1.00 52.64  ? 281 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? 6.349   -5.869  0.599   1.00 49.06  ? 282 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 3.493   -5.941  -0.860  1.00 48.50  ? 283 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 5.124   -7.604  3.955   1.00 36.12  ? 284 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 22.182  -16.642 -0.455  1.00 38.73  ? 285 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? 10.977  -7.804  0.393   1.00 25.83  ? 286 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? -6.620  -13.592 -11.556 1.00 59.28  ? 287 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? -7.248  -11.498 -8.043  1.00 29.47  ? 288 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? -3.910  -7.990  10.619  1.00 47.14  ? 289 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? -8.148  -19.505 -3.386  1.00 47.67  ? 290 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? -5.997  -26.691 3.318   1.00 50.52  ? 291 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? 21.453  -16.625 -3.518  1.00 30.14  ? 292 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? 9.578   -2.399  -0.399  1.00 66.54  ? 293 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? -3.949  -26.806 7.348   1.00 56.51  ? 294 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? 9.038   -9.080  -13.788 1.00 45.11  ? 295 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? 10.954  -27.763 -7.271  1.00 55.54  ? 296 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? 8.044   -8.228  4.495   1.00 39.19  ? 297 HOH   A O   1 
HETATM 2314 O O   . HOH   M 5 .  ? -0.583  -3.550  -10.963 1.00 55.61  ? 298 HOH   A O   1 
HETATM 2315 O O   . HOH   M 5 .  ? -0.118  -8.165  -13.337 1.00 46.55  ? 299 HOH   A O   1 
HETATM 2316 O O   . HOH   M 5 .  ? -5.593  -23.514 -6.962  1.00 41.49  ? 300 HOH   A O   1 
HETATM 2317 O O   . HOH   M 5 .  ? 1.289   -29.125 -7.308  1.00 55.26  ? 301 HOH   A O   1 
HETATM 2318 O O   . HOH   M 5 .  ? -3.847  -10.982 9.614   1.00 49.60  ? 302 HOH   A O   1 
HETATM 2319 O O   . HOH   M 5 .  ? 7.827   -30.238 -3.218  1.00 59.88  ? 303 HOH   A O   1 
HETATM 2320 O O   . HOH   M 5 .  ? 4.915   -6.906  -10.901 1.00 48.99  ? 304 HOH   A O   1 
HETATM 2321 O O   . HOH   M 5 .  ? -10.213 -28.057 -1.686  1.00 63.32  ? 305 HOH   A O   1 
HETATM 2322 O O   . HOH   M 5 .  ? -7.364  -14.056 -9.186  1.00 39.86  ? 306 HOH   A O   1 
HETATM 2323 O O   . HOH   M 5 .  ? -9.349  -19.145 1.635   1.00 46.04  ? 307 HOH   A O   1 
HETATM 2324 O O   . HOH   M 5 .  ? 4.819   -9.736  -11.318 1.00 49.91  ? 308 HOH   A O   1 
HETATM 2325 O O   . HOH   M 5 .  ? 12.927  -18.762 -12.239 1.00 55.87  ? 309 HOH   A O   1 
HETATM 2326 O O   . HOH   M 5 .  ? -6.155  -22.979 5.617   1.00 57.61  ? 310 HOH   A O   1 
HETATM 2327 O O   . HOH   M 5 .  ? 5.796   -3.263  1.045   1.00 56.64  ? 311 HOH   A O   1 
HETATM 2328 O O   . HOH   M 5 .  ? -11.305 -13.493 -2.849  1.00 40.54  ? 312 HOH   A O   1 
HETATM 2329 O O   . HOH   M 5 .  ? -7.063  -19.229 8.442   1.00 49.61  ? 313 HOH   A O   1 
HETATM 2330 O O   . HOH   M 5 .  ? 8.639   -22.369 -19.428 1.00 58.50  ? 314 HOH   A O   1 
HETATM 2331 O O   . HOH   M 5 .  ? -5.091  -21.076 -8.080  1.00 53.64  ? 315 HOH   A O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 10.165  -11.357 -38.169 1.00 47.54  ? 201 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 30.050  -12.926 -45.347 1.00 67.12  ? 202 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 30.916  -8.361  -30.047 1.00 55.80  ? 203 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 24.946  -5.444  -29.810 1.00 41.52  ? 204 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 27.665  -8.272  -28.744 1.00 47.26  ? 205 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 6.593   -12.264 -26.126 1.00 44.34  ? 206 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 20.126  -21.754 -23.013 1.00 54.04  ? 207 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 13.168  -4.992  -41.751 1.00 57.14  ? 208 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 3.680   -18.868 -30.376 1.00 49.99  ? 209 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 10.391  -19.866 -43.055 1.00 46.20  ? 210 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 25.456  -6.172  -35.733 1.00 42.70  ? 211 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 30.276  -19.843 -40.176 1.00 39.29  ? 212 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 8.455   -27.866 -38.386 1.00 55.69  ? 213 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 34.733  -23.419 -30.259 1.00 57.76  ? 214 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 26.139  -4.740  -33.559 1.00 50.18  ? 215 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 19.836  -25.671 -34.032 1.00 43.40  ? 216 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 13.032  -21.794 -20.665 1.00 67.97  ? 217 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 24.611  -1.957  -36.048 1.00 45.73  ? 218 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 32.617  -18.708 -42.210 1.00 64.19  ? 219 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 21.234  -26.644 -30.311 1.00 57.41  ? 220 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 26.014  -0.517  -29.198 1.00 56.89  ? 221 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 16.769  -19.258 -28.768 1.00 26.48  ? 222 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 21.135  -13.597 -42.497 1.00 39.76  ? 223 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 10.515  -18.952 -32.958 1.00 31.38  ? 224 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 23.534  -2.479  -29.014 1.00 42.31  ? 225 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 27.711  -17.831 -24.948 1.00 46.90  ? 226 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 26.227  -23.184 -31.104 1.00 39.01  ? 227 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 18.294  -0.654  -38.438 1.00 30.42  ? 228 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 20.687  -10.338 -42.823 1.00 44.33  ? 229 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 8.563   -8.531  -16.584 1.00 47.12  ? 230 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 22.615  -23.374 -28.683 1.00 40.34  ? 231 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 17.082  -25.764 -34.337 1.00 41.30  ? 232 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 3.239   -8.698  -27.103 1.00 54.64  ? 233 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 17.493  -19.826 -42.084 1.00 52.02  ? 234 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 10.832  -22.005 -32.580 1.00 41.48  ? 235 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 18.476  -25.929 -28.679 1.00 43.96  ? 236 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 22.232  3.490   -32.565 1.00 48.50  ? 237 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 23.815  -4.343  -36.770 1.00 32.82  ? 238 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 21.152  -6.684  -42.447 1.00 39.45  ? 239 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 14.492  -6.583  -41.264 1.00 40.15  ? 240 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 31.702  -12.484 -38.672 1.00 66.55  ? 241 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 10.475  -16.893 -44.383 1.00 45.64  ? 242 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 7.285   -8.232  -20.928 1.00 57.07  ? 243 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 14.721  -24.393 -40.384 1.00 43.98  ? 244 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 7.757   -18.619 -31.554 1.00 42.35  ? 245 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 22.210  -4.458  -24.266 1.00 64.13  ? 246 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 18.023  -15.888 -45.681 1.00 40.49  ? 247 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 31.970  -21.415 -38.209 1.00 45.48  ? 248 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 27.845  -17.913 -46.096 1.00 65.36  ? 249 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 17.834  -3.588  -22.050 1.00 76.75  ? 250 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 7.211   -19.346 -34.825 1.00 50.63  ? 251 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 1.707   -13.020 -28.449 1.00 47.47  ? 252 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 23.699  -11.717 -21.737 1.00 44.18  ? 253 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 27.407  -10.609 -28.745 1.00 48.30  ? 254 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 18.371  -22.887 -20.445 1.00 54.57  ? 255 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 7.893   -23.557 -24.252 1.00 51.95  ? 256 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 18.465  4.314   -34.261 1.00 43.82  ? 257 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 20.636  3.655   -32.816 1.00 36.91  ? 258 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 27.933  -24.959 -35.026 1.00 38.22  ? 259 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 12.205  -4.648  -24.969 1.00 61.57  ? 260 HOH   B O   1 
HETATM 2392 O O   . HOH   N 5 .  ? 18.279  -0.139  -25.593 1.00 65.48  ? 261 HOH   B O   1 
HETATM 2393 O O   . HOH   N 5 .  ? 17.215  -9.654  -43.823 1.00 46.21  ? 262 HOH   B O   1 
HETATM 2394 O O   . HOH   N 5 .  ? 6.281   -20.520 -24.892 1.00 38.53  ? 263 HOH   B O   1 
HETATM 2395 O O   . HOH   N 5 .  ? 21.785  -15.382 -23.252 1.00 53.19  ? 264 HOH   B O   1 
HETATM 2396 O O   . HOH   N 5 .  ? 24.669  -6.490  -42.761 1.00 48.10  ? 265 HOH   B O   1 
HETATM 2397 O O   . HOH   N 5 .  ? 17.239  -25.362 -20.939 1.00 73.25  ? 266 HOH   B O   1 
HETATM 2398 O O   . HOH   N 5 .  ? 24.011  -4.685  -28.296 1.00 59.79  ? 267 HOH   B O   1 
HETATM 2399 O O   . HOH   N 5 .  ? 9.869   -6.242  -41.127 1.00 51.75  ? 268 HOH   B O   1 
HETATM 2400 O O   . HOH   N 5 .  ? 15.204  -8.229  -43.024 1.00 49.93  ? 269 HOH   B O   1 
HETATM 2401 O O   A HOH   N 5 .  ? 16.356  -0.802  -25.756 0.70 46.31  ? 270 HOH   B O   1 
HETATM 2402 O O   B HOH   N 5 .  ? 15.488  -0.922  -26.830 0.30 41.14  ? 270 HOH   B O   1 
HETATM 2403 O O   . HOH   N 5 .  ? 13.037  -19.794 -19.433 1.00 48.43  ? 271 HOH   B O   1 
HETATM 2404 O O   . HOH   N 5 .  ? 27.920  -24.952 -32.222 1.00 44.06  ? 272 HOH   B O   1 
HETATM 2405 O O   . HOH   N 5 .  ? 20.608  -19.275 -22.467 1.00 57.40  ? 273 HOH   B O   1 
HETATM 2406 O O   . HOH   N 5 .  ? 14.396  -31.280 -24.178 1.00 64.03  ? 274 HOH   B O   1 
HETATM 2407 O O   . HOH   N 5 .  ? 11.467  -24.137 -29.769 1.00 51.55  ? 275 HOH   B O   1 
HETATM 2408 O O   . HOH   N 5 .  ? 39.654  -13.348 -38.714 1.00 70.06  ? 276 HOH   B O   1 
HETATM 2409 O O   . HOH   N 5 .  ? 7.328   -9.757  -18.651 1.00 50.14  ? 277 HOH   B O   1 
HETATM 2410 O O   . HOH   N 5 .  ? 15.552  -21.949 -41.840 1.00 49.34  ? 278 HOH   B O   1 
HETATM 2411 O O   . HOH   N 5 .  ? 7.551   -21.640 -29.869 1.00 44.94  ? 279 HOH   B O   1 
HETATM 2412 O O   . HOH   N 5 .  ? 22.395  -29.464 -35.650 1.00 46.17  ? 280 HOH   B O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 26.418  -39.231 12.741  1.00 42.87  ? 201 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 19.839  -20.042 29.913  1.00 63.70  ? 202 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 27.106  -37.779 10.240  1.00 38.87  ? 203 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 29.950  -27.134 30.766  1.00 63.47  ? 204 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 13.167  -19.929 11.133  1.00 60.18  ? 205 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 16.109  -17.602 25.100  1.00 62.29  ? 206 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 12.282  -28.237 28.013  1.00 57.93  ? 207 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 8.972   -36.864 18.264  1.00 57.67  ? 208 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 19.198  -20.182 10.508  1.00 39.23  ? 209 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 30.358  -17.766 9.478   1.00 46.25  ? 210 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 14.289  -37.170 13.587  1.00 42.30  ? 211 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 9.165   -30.200 11.084  1.00 60.97  ? 212 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 23.203  -41.444 18.522  1.00 43.15  ? 213 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 5.810   -26.687 16.493  1.00 52.63  ? 214 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 17.509  -17.017 14.848  1.00 48.09  ? 215 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 7.713   -31.775 12.097  1.00 47.39  ? 216 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 16.306  -37.858 19.876  1.00 47.93  ? 217 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 30.270  -31.088 15.755  1.00 46.92  ? 218 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 12.851  -31.508 8.251   1.00 32.19  ? 219 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 30.317  -40.374 9.463   1.00 35.32  ? 220 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 31.796  -33.123 25.876  1.00 46.08  ? 221 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 25.658  -19.561 6.337   1.00 33.76  ? 222 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 27.867  -37.361 25.021  1.00 49.41  ? 223 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 23.569  -20.741 23.945  1.00 52.15  ? 224 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 33.286  -24.354 31.629  1.00 49.47  ? 225 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 25.698  -33.561 34.742  1.00 52.11  ? 226 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 31.149  -39.716 27.138  1.00 47.89  ? 227 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 29.514  -20.055 13.411  1.00 59.84  ? 228 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 15.348  -17.511 19.380  1.00 42.73  ? 229 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 15.154  -21.075 12.260  1.00 35.48  ? 230 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 15.063  -39.389 16.914  1.00 62.86  ? 231 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 20.029  -41.871 12.215  1.00 29.71  ? 232 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 22.098  -34.297 16.583  1.00 26.70  ? 233 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 14.715  -34.602 46.856  1.00 53.33  ? 234 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 30.704  -29.007 12.116  1.00 54.98  ? 235 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 28.215  -37.203 15.978  1.00 41.50  ? 236 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 22.188  -28.549 11.111  1.00 32.52  ? 237 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 19.160  -26.732 3.103   1.00 46.83  ? 238 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 13.132  -29.592 40.287  1.00 55.53  ? 239 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 20.828  -28.690 8.511   1.00 35.38  ? 240 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 6.981   -17.960 10.853  1.00 40.50  ? 241 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 25.198  -31.327 10.757  1.00 38.86  ? 242 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 31.376  -43.490 15.604  1.00 55.53  ? 243 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 20.880  -39.889 26.342  1.00 41.37  ? 244 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 20.998  -29.480 4.723   1.00 57.51  ? 245 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 9.478   -33.759 9.190   1.00 45.42  ? 246 HOH   C O   1 
HETATM 2459 O O   . HOH   O 5 .  ? 25.850  -17.456 13.695  1.00 45.56  ? 247 HOH   C O   1 
HETATM 2460 O O   . HOH   O 5 .  ? 31.714  -43.421 12.076  1.00 53.01  ? 248 HOH   C O   1 
HETATM 2461 O O   . HOH   O 5 .  ? 29.780  -39.737 31.379  1.00 38.16  ? 249 HOH   C O   1 
HETATM 2462 O O   . HOH   O 5 .  ? 14.145  -38.750 9.388   1.00 54.52  ? 250 HOH   C O   1 
HETATM 2463 O O   . HOH   O 5 .  ? 28.134  -36.530 18.654  1.00 44.04  ? 251 HOH   C O   1 
HETATM 2464 O O   . HOH   O 5 .  ? 14.449  -37.693 6.162   1.00 55.48  ? 252 HOH   C O   1 
HETATM 2465 O O   . HOH   O 5 .  ? 29.463  -26.346 25.363  1.00 53.97  ? 253 HOH   C O   1 
HETATM 2466 O O   . HOH   O 5 .  ? 25.646  -39.557 20.207  1.00 38.83  ? 254 HOH   C O   1 
HETATM 2467 O O   . HOH   O 5 .  ? 22.423  -18.360 21.880  1.00 53.97  ? 255 HOH   C O   1 
HETATM 2468 O O   . HOH   O 5 .  ? 17.576  -21.154 12.699  1.00 49.05  ? 256 HOH   C O   1 
HETATM 2469 O O   . HOH   O 5 .  ? 19.694  -18.938 24.896  1.00 44.26  ? 257 HOH   C O   1 
HETATM 2470 O O   . HOH   O 5 .  ? 30.735  -35.593 28.578  1.00 53.01  ? 258 HOH   C O   1 
HETATM 2471 O O   . HOH   O 5 .  ? 2.556   -28.775 13.630  1.00 50.84  ? 259 HOH   C O   1 
HETATM 2472 O O   . HOH   O 5 .  ? 14.480  -29.414 3.983   1.00 35.84  ? 260 HOH   C O   1 
HETATM 2473 O O   . HOH   O 5 .  ? 8.987   -18.836 23.657  1.00 51.02  ? 261 HOH   C O   1 
HETATM 2474 O O   . HOH   O 5 .  ? 28.055  -15.195 12.803  1.00 57.62  ? 262 HOH   C O   1 
HETATM 2475 O O   . HOH   O 5 .  ? 12.579  -23.427 27.902  1.00 79.33  ? 263 HOH   C O   1 
HETATM 2476 O O   . HOH   O 5 .  ? 20.384  -41.063 39.362  1.00 67.76  ? 264 HOH   C O   1 
HETATM 2477 O O   . HOH   O 5 .  ? 25.036  -17.711 21.310  1.00 65.38  ? 265 HOH   C O   1 
HETATM 2478 O O   . HOH   O 5 .  ? 12.720  -38.773 24.189  1.00 52.87  ? 266 HOH   C O   1 
HETATM 2479 O O   . HOH   O 5 .  ? 30.270  -32.444 18.301  1.00 46.68  ? 267 HOH   C O   1 
HETATM 2480 O O   . HOH   O 5 .  ? 33.886  -36.182 31.498  1.00 57.87  ? 268 HOH   C O   1 
HETATM 2481 O O   . HOH   O 5 .  ? 29.606  -25.345 32.834  1.00 57.21  ? 269 HOH   C O   1 
HETATM 2482 O O   . HOH   O 5 .  ? 4.839   -24.184 18.427  1.00 52.72  ? 270 HOH   C O   1 
HETATM 2483 O O   . HOH   O 5 .  ? 17.366  -36.404 29.346  1.00 63.37  ? 271 HOH   C O   1 
HETATM 2484 O O   . HOH   O 5 .  ? 28.928  -34.088 11.231  1.00 54.93  ? 272 HOH   C O   1 
HETATM 2485 O O   . HOH   O 5 .  ? 24.009  -15.910 11.830  1.00 42.14  ? 273 HOH   C O   1 
HETATM 2486 O O   . HOH   O 5 .  ? 11.951  -21.255 10.630  1.00 37.95  ? 274 HOH   C O   1 
HETATM 2487 O O   . HOH   O 5 .  ? 29.196  -41.532 27.106  1.00 45.35  ? 275 HOH   C O   1 
HETATM 2488 O O   . HOH   O 5 .  ? 29.936  -41.311 33.068  1.00 53.14  ? 276 HOH   C O   1 
HETATM 2489 O O   . HOH   O 5 .  ? 22.784  -13.923 13.355  1.00 49.05  ? 277 HOH   C O   1 
HETATM 2490 O O   . HOH   O 5 .  ? 28.552  -17.506 28.510  1.00 59.43  ? 278 HOH   C O   1 
HETATM 2491 O O   . HOH   O 5 .  ? 24.506  -29.130 9.389   1.00 43.79  ? 279 HOH   C O   1 
HETATM 2492 O O   . HOH   O 5 .  ? 33.395  -44.726 15.215  1.00 48.74  ? 280 HOH   C O   1 
HETATM 2493 O O   . HOH   O 5 .  ? 37.631  -24.318 26.566  1.00 66.36  ? 281 HOH   C O   1 
HETATM 2494 O O   . HOH   O 5 .  ? 1.692   -21.363 17.650  1.00 66.77  ? 282 HOH   C O   1 
HETATM 2495 O O   . HOH   O 5 .  ? 30.541  -23.079 17.946  1.00 57.55  ? 283 HOH   C O   1 
# 
