data_7HG5
# 
_entry.id   7HG5 
# 
_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   7HG5         pdb_00007hg5 10.2210/pdb7hg5/pdb 
WWPDB D_1001407431 ?            ?                   
# 
_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                        7HG5 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    1   ? ?    ? ? 
4 non-polymer syn 'N-ethyl-2-fluoro-4-(methylsulfonyl)aniline'       217.260   2   ? ?    ? ? 
5 water       nat water                                              18.015    273 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                SO4 
3 1,2-ETHANEDIOL                               EDO 
4 'N-ethyl-2-fluoro-4-(methylsulfonyl)aniline' WV4 
5 water                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                      ?                 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                     ?                 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                   ?                 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                              ?                 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                     ?                 'C3 H7 N O2 S'    121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                               'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
GLN 'L-peptide linking' y GLUTAMINE                                    ?                 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                              ?                 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                      ?                 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                    ?                 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                        ?                 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                   ?                 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                                      ?                 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                                       ?                 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                                   ?                 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                ?                 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                                      ?                 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                                       ?                 'C3 H7 N O3'      105.093 
SO4 non-polymer         . 'SULFATE ION'                                ?                 'O4 S -2'         96.063  
THR 'L-peptide linking' y THREONINE                                    ?                 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                   ?                 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                                     ?                 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                       ?                 'C5 H11 N O2'     117.146 
WV4 non-polymer         . 'N-ethyl-2-fluoro-4-(methylsulfonyl)aniline' ?                 'C9 H12 F N O2 S' 217.260 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 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        WV4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WV4 
_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 WV4 1   103 101 WV4 LIG B . 
K 2 SO4 1   101 5   SO4 SO4 C . 
L 4 WV4 1   102 101 WV4 LIG C . 
M 5 HOH 1   201 202 HOH HOH A . 
M 5 HOH 2   202 307 HOH HOH A . 
M 5 HOH 3   203 359 HOH HOH A . 
M 5 HOH 4   204 84  HOH HOH A . 
M 5 HOH 5   205 347 HOH HOH A . 
M 5 HOH 6   206 139 HOH HOH A . 
M 5 HOH 7   207 368 HOH HOH A . 
M 5 HOH 8   208 301 HOH HOH A . 
M 5 HOH 9   209 55  HOH HOH A . 
M 5 HOH 10  210 95  HOH HOH A . 
M 5 HOH 11  211 344 HOH HOH A . 
M 5 HOH 12  212 293 HOH HOH A . 
M 5 HOH 13  213 87  HOH HOH A . 
M 5 HOH 14  214 208 HOH HOH A . 
M 5 HOH 15  215 66  HOH HOH A . 
M 5 HOH 16  216 167 HOH HOH A . 
M 5 HOH 17  217 85  HOH HOH A . 
M 5 HOH 18  218 71  HOH HOH A . 
M 5 HOH 19  219 26  HOH HOH A . 
M 5 HOH 20  220 86  HOH HOH A . 
M 5 HOH 21  221 37  HOH HOH A . 
M 5 HOH 22  222 91  HOH HOH A . 
M 5 HOH 23  223 278 HOH HOH A . 
M 5 HOH 24  224 97  HOH HOH A . 
M 5 HOH 25  225 41  HOH HOH A . 
M 5 HOH 26  226 32  HOH HOH A . 
M 5 HOH 27  227 203 HOH HOH A . 
M 5 HOH 28  228 179 HOH HOH A . 
M 5 HOH 29  229 28  HOH HOH A . 
M 5 HOH 30  230 99  HOH HOH A . 
M 5 HOH 31  231 8   HOH HOH A . 
M 5 HOH 32  232 111 HOH HOH A . 
M 5 HOH 33  233 34  HOH HOH A . 
M 5 HOH 34  234 218 HOH HOH A . 
M 5 HOH 35  235 292 HOH HOH A . 
M 5 HOH 36  236 289 HOH HOH A . 
M 5 HOH 37  237 188 HOH HOH A . 
M 5 HOH 38  238 23  HOH HOH A . 
M 5 HOH 39  239 267 HOH HOH A . 
M 5 HOH 40  240 7   HOH HOH A . 
M 5 HOH 41  241 199 HOH HOH A . 
M 5 HOH 42  242 274 HOH HOH A . 
M 5 HOH 43  243 288 HOH HOH A . 
M 5 HOH 44  244 12  HOH HOH A . 
M 5 HOH 45  245 131 HOH HOH A . 
M 5 HOH 46  246 60  HOH HOH A . 
M 5 HOH 47  247 47  HOH HOH A . 
M 5 HOH 48  248 78  HOH HOH A . 
M 5 HOH 49  249 343 HOH HOH A . 
M 5 HOH 50  250 1   HOH HOH A . 
M 5 HOH 51  251 27  HOH HOH A . 
M 5 HOH 52  252 2   HOH HOH A . 
M 5 HOH 53  253 58  HOH HOH A . 
M 5 HOH 54  254 190 HOH HOH A . 
M 5 HOH 55  255 31  HOH HOH A . 
M 5 HOH 56  256 143 HOH HOH A . 
M 5 HOH 57  257 260 HOH HOH A . 
M 5 HOH 58  258 20  HOH HOH A . 
M 5 HOH 59  259 73  HOH HOH A . 
M 5 HOH 60  260 300 HOH HOH A . 
M 5 HOH 61  261 290 HOH HOH A . 
M 5 HOH 62  262 21  HOH HOH A . 
M 5 HOH 63  263 18  HOH HOH A . 
M 5 HOH 64  264 38  HOH HOH A . 
M 5 HOH 65  265 297 HOH HOH A . 
M 5 HOH 66  266 164 HOH HOH A . 
M 5 HOH 67  267 14  HOH HOH A . 
M 5 HOH 68  268 77  HOH HOH A . 
M 5 HOH 69  269 115 HOH HOH A . 
M 5 HOH 70  270 109 HOH HOH A . 
M 5 HOH 71  271 42  HOH HOH A . 
M 5 HOH 72  272 222 HOH HOH A . 
M 5 HOH 73  273 93  HOH HOH A . 
M 5 HOH 74  274 113 HOH HOH A . 
M 5 HOH 75  275 318 HOH HOH A . 
M 5 HOH 76  276 145 HOH HOH A . 
M 5 HOH 77  277 259 HOH HOH A . 
M 5 HOH 78  278 16  HOH HOH A . 
M 5 HOH 79  279 9   HOH HOH A . 
M 5 HOH 80  280 116 HOH HOH A . 
M 5 HOH 81  281 296 HOH HOH A . 
M 5 HOH 82  282 304 HOH HOH A . 
M 5 HOH 83  283 19  HOH HOH A . 
M 5 HOH 84  284 152 HOH HOH A . 
M 5 HOH 85  285 281 HOH HOH A . 
M 5 HOH 86  286 64  HOH HOH A . 
M 5 HOH 87  287 360 HOH HOH A . 
M 5 HOH 88  288 353 HOH HOH A . 
M 5 HOH 89  289 94  HOH HOH A . 
M 5 HOH 90  290 151 HOH HOH A . 
M 5 HOH 91  291 165 HOH HOH A . 
M 5 HOH 92  292 327 HOH HOH A . 
M 5 HOH 93  293 211 HOH HOH A . 
M 5 HOH 94  294 63  HOH HOH A . 
M 5 HOH 95  295 22  HOH HOH A . 
M 5 HOH 96  296 361 HOH HOH A . 
M 5 HOH 97  297 108 HOH HOH A . 
M 5 HOH 98  298 270 HOH HOH A . 
M 5 HOH 99  299 346 HOH HOH A . 
M 5 HOH 100 300 83  HOH HOH A . 
M 5 HOH 101 301 210 HOH HOH A . 
M 5 HOH 102 302 358 HOH HOH A . 
M 5 HOH 103 303 75  HOH HOH A . 
M 5 HOH 104 304 185 HOH HOH A . 
M 5 HOH 105 305 219 HOH HOH A . 
M 5 HOH 106 306 205 HOH HOH A . 
M 5 HOH 107 307 372 HOH HOH A . 
M 5 HOH 108 308 363 HOH HOH A . 
M 5 HOH 109 309 362 HOH HOH A . 
M 5 HOH 110 310 57  HOH HOH A . 
M 5 HOH 111 311 283 HOH HOH A . 
M 5 HOH 112 312 35  HOH HOH A . 
M 5 HOH 113 313 156 HOH HOH A . 
M 5 HOH 114 314 125 HOH HOH A . 
M 5 HOH 115 315 313 HOH HOH A . 
M 5 HOH 116 316 332 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 365 HOH HOH B . 
N 5 HOH 3   203 101 HOH HOH B . 
N 5 HOH 4   204 272 HOH HOH B . 
N 5 HOH 5   205 89  HOH HOH B . 
N 5 HOH 6   206 17  HOH HOH B . 
N 5 HOH 7   207 69  HOH HOH B . 
N 5 HOH 8   208 258 HOH HOH B . 
N 5 HOH 9   209 331 HOH HOH B . 
N 5 HOH 10  210 223 HOH HOH B . 
N 5 HOH 11  211 342 HOH HOH B . 
N 5 HOH 12  212 150 HOH HOH B . 
N 5 HOH 13  213 184 HOH HOH B . 
N 5 HOH 14  214 153 HOH HOH B . 
N 5 HOH 15  215 345 HOH HOH B . 
N 5 HOH 16  216 340 HOH HOH B . 
N 5 HOH 17  217 137 HOH HOH B . 
N 5 HOH 18  218 249 HOH HOH B . 
N 5 HOH 19  219 123 HOH HOH B . 
N 5 HOH 20  220 175 HOH HOH B . 
N 5 HOH 21  221 169 HOH HOH B . 
N 5 HOH 22  222 177 HOH HOH B . 
N 5 HOH 23  223 315 HOH HOH B . 
N 5 HOH 24  224 168 HOH HOH B . 
N 5 HOH 25  225 68  HOH HOH B . 
N 5 HOH 26  226 242 HOH HOH B . 
N 5 HOH 27  227 98  HOH HOH B . 
N 5 HOH 28  228 339 HOH HOH B . 
N 5 HOH 29  229 320 HOH HOH B . 
N 5 HOH 30  230 350 HOH HOH B . 
N 5 HOH 31  231 79  HOH HOH B . 
N 5 HOH 32  232 6   HOH HOH B . 
N 5 HOH 33  233 215 HOH HOH B . 
N 5 HOH 34  234 172 HOH HOH B . 
N 5 HOH 35  235 10  HOH HOH B . 
N 5 HOH 36  236 24  HOH HOH B . 
N 5 HOH 37  237 25  HOH HOH B . 
N 5 HOH 38  238 329 HOH HOH B . 
N 5 HOH 39  239 96  HOH HOH B . 
N 5 HOH 40  240 170 HOH HOH B . 
N 5 HOH 41  241 157 HOH HOH B . 
N 5 HOH 42  242 280 HOH HOH B . 
N 5 HOH 43  243 354 HOH HOH B . 
N 5 HOH 44  244 13  HOH HOH B . 
N 5 HOH 45  245 5   HOH HOH B . 
N 5 HOH 46  246 117 HOH HOH B . 
N 5 HOH 47  247 54  HOH HOH B . 
N 5 HOH 48  248 279 HOH HOH B . 
N 5 HOH 49  249 46  HOH HOH B . 
N 5 HOH 50  250 261 HOH HOH B . 
N 5 HOH 51  251 72  HOH HOH B . 
N 5 HOH 52  252 224 HOH HOH B . 
N 5 HOH 53  253 120 HOH HOH B . 
N 5 HOH 54  254 61  HOH HOH B . 
N 5 HOH 55  255 119 HOH HOH B . 
N 5 HOH 56  256 59  HOH HOH B . 
N 5 HOH 57  257 217 HOH HOH B . 
N 5 HOH 58  258 76  HOH HOH B . 
N 5 HOH 59  259 36  HOH HOH B . 
N 5 HOH 60  260 74  HOH HOH B . 
N 5 HOH 61  261 349 HOH HOH B . 
N 5 HOH 62  262 197 HOH HOH B . 
N 5 HOH 63  263 182 HOH HOH B . 
N 5 HOH 64  264 351 HOH HOH B . 
N 5 HOH 65  265 303 HOH HOH B . 
N 5 HOH 66  266 104 HOH HOH B . 
N 5 HOH 67  267 214 HOH HOH B . 
N 5 HOH 68  268 44  HOH HOH B . 
N 5 HOH 69  269 201 HOH HOH B . 
N 5 HOH 70  270 163 HOH HOH B . 
N 5 HOH 71  271 352 HOH HOH B . 
N 5 HOH 72  272 160 HOH HOH B . 
N 5 HOH 73  273 291 HOH HOH B . 
N 5 HOH 74  274 316 HOH HOH B . 
N 5 HOH 75  275 341 HOH HOH B . 
N 5 HOH 76  276 322 HOH HOH B . 
N 5 HOH 77  277 371 HOH HOH B . 
N 5 HOH 78  278 103 HOH HOH B . 
N 5 HOH 79  279 314 HOH HOH B . 
N 5 HOH 80  280 348 HOH HOH B . 
N 5 HOH 81  281 107 HOH HOH B . 
N 5 HOH 82  282 312 HOH HOH B . 
O 5 HOH 1   201 321 HOH HOH C . 
O 5 HOH 2   202 323 HOH HOH C . 
O 5 HOH 3   203 142 HOH HOH C . 
O 5 HOH 4   204 375 HOH HOH C . 
O 5 HOH 5   205 271 HOH HOH C . 
O 5 HOH 6   206 367 HOH HOH C . 
O 5 HOH 7   207 294 HOH HOH C . 
O 5 HOH 8   208 118 HOH HOH C . 
O 5 HOH 9   209 254 HOH HOH C . 
O 5 HOH 10  210 67  HOH HOH C . 
O 5 HOH 11  211 173 HOH HOH C . 
O 5 HOH 12  212 275 HOH HOH C . 
O 5 HOH 13  213 49  HOH HOH C . 
O 5 HOH 14  214 309 HOH HOH C . 
O 5 HOH 15  215 90  HOH HOH C . 
O 5 HOH 16  216 226 HOH HOH C . 
O 5 HOH 17  217 317 HOH HOH C . 
O 5 HOH 18  218 126 HOH HOH C . 
O 5 HOH 19  219 302 HOH HOH C . 
O 5 HOH 20  220 366 HOH HOH C . 
O 5 HOH 21  221 15  HOH HOH C . 
O 5 HOH 22  222 284 HOH HOH C . 
O 5 HOH 23  223 269 HOH HOH C . 
O 5 HOH 24  224 45  HOH HOH C . 
O 5 HOH 25  225 53  HOH HOH C . 
O 5 HOH 26  226 82  HOH HOH C . 
O 5 HOH 27  227 4   HOH HOH C . 
O 5 HOH 28  228 209 HOH HOH C . 
O 5 HOH 29  229 134 HOH HOH C . 
O 5 HOH 30  230 135 HOH HOH C . 
O 5 HOH 31  231 40  HOH HOH C . 
O 5 HOH 32  232 62  HOH HOH C . 
O 5 HOH 33  233 43  HOH HOH C . 
O 5 HOH 34  234 122 HOH HOH C . 
O 5 HOH 35  235 189 HOH HOH C . 
O 5 HOH 36  236 198 HOH HOH C . 
O 5 HOH 37  237 295 HOH HOH C . 
O 5 HOH 38  238 328 HOH HOH C . 
O 5 HOH 39  239 298 HOH HOH C . 
O 5 HOH 40  240 48  HOH HOH C . 
O 5 HOH 41  241 102 HOH HOH C . 
O 5 HOH 42  242 299 HOH HOH C . 
O 5 HOH 43  243 148 HOH HOH C . 
O 5 HOH 44  244 130 HOH HOH C . 
O 5 HOH 45  245 132 HOH HOH C . 
O 5 HOH 46  246 373 HOH HOH C . 
O 5 HOH 47  247 338 HOH HOH C . 
O 5 HOH 48  248 335 HOH HOH C . 
O 5 HOH 49  249 56  HOH HOH C . 
O 5 HOH 50  250 337 HOH HOH C . 
O 5 HOH 51  251 287 HOH HOH C . 
O 5 HOH 52  252 305 HOH HOH C . 
O 5 HOH 53  253 319 HOH HOH C . 
O 5 HOH 54  254 65  HOH HOH C . 
O 5 HOH 55  255 146 HOH HOH C . 
O 5 HOH 56  256 356 HOH HOH C . 
O 5 HOH 57  257 171 HOH HOH C . 
O 5 HOH 58  258 370 HOH HOH C . 
O 5 HOH 59  259 357 HOH HOH C . 
O 5 HOH 60  260 149 HOH HOH C . 
O 5 HOH 61  261 241 HOH HOH C . 
O 5 HOH 62  262 334 HOH HOH C . 
O 5 HOH 63  263 70  HOH HOH C . 
O 5 HOH 64  264 324 HOH HOH C . 
O 5 HOH 65  265 333 HOH HOH C . 
O 5 HOH 66  266 330 HOH HOH C . 
O 5 HOH 67  267 246 HOH HOH C . 
O 5 HOH 68  268 355 HOH HOH C . 
O 5 HOH 69  269 374 HOH HOH C . 
O 5 HOH 70  270 369 HOH HOH C . 
O 5 HOH 71  271 336 HOH HOH C . 
O 5 HOH 72  272 92  HOH HOH C . 
O 5 HOH 73  273 364 HOH HOH C . 
O 5 HOH 74  274 206 HOH HOH C . 
O 5 HOH 75  275 310 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A ASP 62 ? CG  ? A ASP 63 CG  
4  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
5  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
6  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
7  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
8  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
9  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
10 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
11 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
12 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
13 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
14 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
15 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
16 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
17 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
18 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
19 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
20 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
21 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
22 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
23 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
24 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
25 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
26 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
27 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
28 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
29 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
30 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
31 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
32 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
33 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
34 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
35 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
36 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
37 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
38 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
39 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
40 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
41 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
42 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
43 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
44 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
45 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
46 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
47 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
48 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
49 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
50 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
51 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
52 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
53 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
54 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
55 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
56 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           7HG5 
_cell.length_a           41.830 
_cell.length_b           42.420 
_cell.length_c           159.750 
_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                         7HG5 
_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          7HG5 
_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                     7HG5 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.25 
_reflns.d_resolution_high            1.57 
_reflns.number_obs                   40735 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.051 
_reflns.pdbx_netI_over_sigmaI        14.2 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.056 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     248821 
_reflns.pdbx_chi_squared             0.96 
_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                  1.57 
_reflns_shell.d_res_low                   1.61 
_reflns_shell.number_measured_all         15212 
_reflns_shell.number_unique_obs           2963 
_reflns_shell.Rmerge_I_obs                1.667 
_reflns_shell.pdbx_chi_squared            0.76 
_reflns_shell.pdbx_redundancy             5.1 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.860 
_reflns_shell.pdbx_Rpim_I_all             0.814 
_reflns_shell.pdbx_CC_half                0.305 
_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                                 7HG5 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     38516 
_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                             40.50 
_refine.ls_d_res_high                            1.57 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_R_factor_obs                          0.20720 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20518 
_refine.ls_R_factor_R_free                       0.24275 
_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                  2146 
_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          0.954 
_refine.B_iso_mean                               38.790 
_refine.aniso_B[1][1]                            0.89 
_refine.aniso_B[2][2]                            -0.23 
_refine.aniso_B[3][3]                            -0.67 
_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                       0.097 
_refine.pdbx_overall_ESU_R_Free                  0.099 
_refine.overall_SU_ML                            0.088 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.615 
_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        2151 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         62 
_refine_hist.number_atoms_solvent             273 
_refine_hist.number_atoms_total               2486 
_refine_hist.d_res_high                       1.57 
_refine_hist.d_res_low                        40.50 
# 
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  ? 2316 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.841  1.826  ? 3156 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.107  5.000  ? 268  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.028  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.125 10.000 ? 308  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.134  0.200  ? 291  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1958 '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                  3.627  3.623  ? 1081 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.929  6.488  ? 1348 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.496  3.910  ? 1235 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.124  55.95  ? 3498 '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                       1.570 
_refine_ls_shell.d_res_low                        1.611 
_refine_ls_shell.number_reflns_R_work             2776 
_refine_ls_shell.R_factor_R_work                  0.366 
_refine_ls_shell.percent_reflns_obs               99.90 
_refine_ls_shell.R_factor_R_free                  0.370 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             177 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HG5 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z2142244288' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HG5 
_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 2 ? 
L N N 4 ? 
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 7HG5 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HG5 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HG5 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 7HG5 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HG5 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HG5 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HG5 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HG5 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HG5 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 TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HG5 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 242 ? ? O B HOH 276 ? ? 1.58 
2  1 O   A HOH 208 ? ? O A HOH 288 ? ? 1.58 
3  1 O   C HOH 232 ? ? O C HOH 265 ? ? 1.60 
4  1 O   B HOH 265 ? ? O B HOH 276 ? ? 1.82 
5  1 O2  C SO4 101 ? ? O C HOH 201 ? ? 1.87 
6  1 OD1 C ASP 9   ? ? O C HOH 202 ? ? 2.01 
7  1 O   A HOH 211 ? ? O A HOH 295 ? ? 2.08 
8  1 O4  A SO4 104 ? ? O A HOH 201 ? ? 2.12 
9  1 O   C HOH 207 ? ? O C HOH 253 ? ? 2.17 
10 1 O2  A SO4 104 ? ? O A HOH 202 ? ? 2.17 
11 1 O   B HOH 221 ? ? O B HOH 270 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 235 ? ? 1_555 O A HOH 272 ? ? 4_545 1.90 
2 1 O A HOH 297 ? ? 1_555 O C HOH 204 ? ? 4_445 1.98 
3 1 O A HOH 311 ? ? 1_555 O A HOH 312 ? ? 4_445 2.18 
4 1 O A HOH 251 ? ? 1_555 O C HOH 268 ? ? 4_445 2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                113.37 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            13.17 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -155.04 63.17 
2 1 ASN B 38 ? ? 84.52   -0.33 
3 1 ASN B 87 ? ? -158.88 62.77 
4 1 ALA C 4  ? ? -171.56 87.85 
5 1 ASN C 87 ? ? -146.69 54.25 
# 
_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            149.76 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ALA 29 ? C ALA 30 
11 1 Y 1 C ASP 30 ? C ASP 31 
12 1 Y 1 C GLY 31 ? C GLY 32 
13 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
SO4 S    S N N 314 
SO4 O1   O N N 315 
SO4 O2   O N N 316 
SO4 O3   O N N 317 
SO4 O4   O N N 318 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TRP N    N N N 336 
TRP CA   C N S 337 
TRP C    C N N 338 
TRP O    O N N 339 
TRP CB   C N N 340 
TRP CG   C Y N 341 
TRP CD1  C Y N 342 
TRP CD2  C Y N 343 
TRP NE1  N Y N 344 
TRP CE2  C Y N 345 
TRP CE3  C Y N 346 
TRP CZ2  C Y N 347 
TRP CZ3  C Y N 348 
TRP CH2  C Y N 349 
TRP OXT  O N N 350 
TRP H    H N N 351 
TRP H2   H N N 352 
TRP HA   H N N 353 
TRP HB2  H N N 354 
TRP HB3  H N N 355 
TRP HD1  H N N 356 
TRP HE1  H N N 357 
TRP HE3  H N N 358 
TRP HZ2  H N N 359 
TRP HZ3  H N N 360 
TRP HH2  H N N 361 
TRP HXT  H N N 362 
TYR N    N N N 363 
TYR CA   C N S 364 
TYR C    C N N 365 
TYR O    O N N 366 
TYR CB   C N N 367 
TYR CG   C Y N 368 
TYR CD1  C Y N 369 
TYR CD2  C Y N 370 
TYR CE1  C Y N 371 
TYR CE2  C Y N 372 
TYR CZ   C Y N 373 
TYR OH   O N N 374 
TYR OXT  O N N 375 
TYR H    H N N 376 
TYR H2   H N N 377 
TYR HA   H N N 378 
TYR HB2  H N N 379 
TYR HB3  H N N 380 
TYR HD1  H N N 381 
TYR HD2  H N N 382 
TYR HE1  H N N 383 
TYR HE2  H N N 384 
TYR HH   H N N 385 
TYR HXT  H N N 386 
VAL N    N N N 387 
VAL CA   C N S 388 
VAL C    C N N 389 
VAL O    O N N 390 
VAL CB   C N N 391 
VAL CG1  C N N 392 
VAL CG2  C N N 393 
VAL OXT  O N N 394 
VAL H    H N N 395 
VAL H2   H N N 396 
VAL HA   H N N 397 
VAL HB   H N N 398 
VAL HG11 H N N 399 
VAL HG12 H N N 400 
VAL HG13 H N N 401 
VAL HG21 H N N 402 
VAL HG22 H N N 403 
VAL HG23 H N N 404 
VAL HXT  H N N 405 
WV4 C4   C Y N 406 
WV4 C5   C Y N 407 
WV4 C6   C Y N 408 
WV4 C7   C N N 409 
WV4 C8   C N N 410 
WV4 C9   C N N 411 
WV4 N1   N N N 412 
WV4 C3   C Y N 413 
WV4 C1   C Y N 414 
WV4 C2   C Y N 415 
WV4 F1   F N N 416 
WV4 O1   O N N 417 
WV4 O2   O N N 418 
WV4 S1   S N N 419 
WV4 H2   H N N 420 
WV4 H3   H N N 421 
WV4 H6   H N N 422 
WV4 H4   H N N 423 
WV4 H5   H N N 424 
WV4 H9   H N N 425 
WV4 H8   H N N 426 
WV4 H11  H N N 427 
WV4 H12  H N N 428 
WV4 H10  H N N 429 
WV4 H7   H N N 430 
WV4 H1   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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
WV4 C9  C8   sing N N 389 
WV4 F1  C1   sing N N 390 
WV4 N1  C8   sing N N 391 
WV4 N1  C6   sing N N 392 
WV4 C1  C6   doub Y N 393 
WV4 C1  C2   sing Y N 394 
WV4 C6  C5   sing Y N 395 
WV4 C2  C3   doub Y N 396 
WV4 C5  C4   doub Y N 397 
WV4 C3  C4   sing Y N 398 
WV4 C3  S1   sing N N 399 
WV4 O2  S1   doub N N 400 
WV4 S1  C7   sing N N 401 
WV4 S1  O1   doub N N 402 
WV4 C4  H2   sing N N 403 
WV4 C5  H3   sing N N 404 
WV4 C7  H6   sing N N 405 
WV4 C7  H4   sing N N 406 
WV4 C7  H5   sing N N 407 
WV4 C8  H9   sing N N 408 
WV4 C8  H8   sing N N 409 
WV4 C9  H11  sing N N 410 
WV4 C9  H12  sing N N 411 
WV4 C9  H10  sing N N 412 
WV4 N1  H7   sing N N 413 
WV4 C2  H1   sing N N 414 
# 
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                    7HG5 
_atom_sites.fract_transf_matrix[1][1]   0.023906 
_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]   0.023574 
_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]   0.006260 
_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 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 2  ? 1.300   4.264   2.438   1.00 49.65  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? 0.207   3.497   1.781   1.00 53.06  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.806   2.452   0.841   1.00 50.59  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.881   2.658   0.285   1.00 49.73  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -0.755  4.434   1.039   1.00 60.59  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -1.742  5.178   1.939   1.00 71.21  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.176  4.273   2.575   1.00 72.45  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -3.678  5.304   3.960   1.00 70.83  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? 0.150   1.276   0.665   1.00 39.17  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.664   0.208   -0.202  1.00 38.80  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.746   0.496   -1.701  1.00 38.36  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? 0.027   1.327   -2.247  1.00 38.13  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -0.365  -0.935  0.103   1.00 42.44  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -0.953  -0.581  1.469   1.00 37.63  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.108  0.918   1.347   1.00 41.12  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.669   -0.184  -2.368  1.00 38.89  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.828   -0.060  -3.809  1.00 38.66  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 1.278   -1.351  -4.388  1.00 33.42  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.830   -2.200  -3.619  1.00 35.08  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 3.309   0.149   -4.173  1.00 48.89  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.867   1.430   -3.635  1.00 61.22  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 4.145   1.636   -2.298  1.00 63.53  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.145   2.592   -4.253  1.00 64.36  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.589   2.876   -2.127  1.00 69.20  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.606   3.473   -3.302  1.00 66.20  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 1.257   -1.480  -5.721  1.00 31.51  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 1.062   -2.790  -6.330  1.00 28.78  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 2.219   -3.697  -5.947  1.00 28.66  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 3.288   -3.209  -5.549  1.00 31.45  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.997   -2.640  -7.846  1.00 35.33  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.982   -5.000  -6.080  1.00 26.24  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 3.004   -6.024  -5.907  1.00 28.76  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 4.144   -5.822  -6.919  1.00 32.74  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.890   -5.484  -8.093  1.00 31.59  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.465   -7.460  -5.992  1.00 28.10  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.674   -7.850  -4.739  1.00 28.98  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 2.344   -8.060  -3.522  1.00 26.50  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? 0.279   -7.968  -4.759  1.00 30.11  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.677   -8.388  -2.344  1.00 24.37  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.390  -8.334  -3.570  1.00 23.04  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? 0.298   -8.525  -2.384  1.00 25.40  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 5.377   -6.092  -6.464  1.00 25.08  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.559   -5.975  -7.320  1.00 25.99  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.474   -7.169  -7.029  1.00 25.80  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 7.429   -7.778  -5.949  1.00 25.32  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 7.223   -4.614  -7.056  1.00 29.27  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.890   -4.465  -5.693  1.00 33.55  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.585   -3.131  -5.383  1.00 41.46  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 9.078   -3.096  -3.932  1.00 39.40  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 8.010   -3.155  -2.918  1.00 39.04  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 8.348   -7.561  -7.967  1.00 26.11  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 9.320   -8.628  -7.700  1.00 25.32  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 10.081  -8.356  -6.404  1.00 24.15  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.553  -7.233  -6.180  1.00 25.86  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 10.232  -8.529  -8.965  1.00 27.29  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 9.276   -8.042  -10.032 1.00 30.20  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.444   -6.995  -9.337  1.00 30.40  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 10.279  -9.433  -5.627  1.00 23.10  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.995  -9.401  -4.369  1.00 23.81  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 10.057  -9.263  -3.173  1.00 22.52  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 10.460  -9.497  -2.040  1.00 23.69  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.808   -8.862  -3.420  1.00 22.49  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.881   -8.780  -2.290  1.00 20.87  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.620   -10.153 -1.660  1.00 19.00  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.489   -11.135 -2.382  1.00 21.16  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.562   -8.155  -2.718  1.00 21.62  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.560   -6.656  -2.924  1.00 24.72  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.490   -5.964  -2.457  1.00 28.55  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.556   -6.175  -3.506  1.00 25.78  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.555   -10.189 -0.308  1.00 20.17  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 7.347   -11.456 0.413   1.00 18.47  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.877   -11.554 0.811   1.00 19.77  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 5.280   -10.540 1.243   1.00 22.20  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 8.274   -11.470 1.653   1.00 21.07  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.760   -11.283 1.308   1.00 20.72  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.621  -11.388 2.631   1.00 25.02  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 10.242  -12.231 0.207   1.00 23.15  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 5.327   -12.790 0.725   1.00 21.41  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.875   -12.960 0.926   1.00 22.29  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.644   -14.333 1.547   1.00 22.24  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.547   -15.190 1.585   1.00 21.88  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 3.057   -12.895 -0.385  1.00 19.42  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 3.192   -11.533 -1.043  1.00 21.53  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.523   -13.971 -1.370  1.00 21.71  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 2.416   -14.526 2.050   1.00 20.58  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.893   -15.883 2.031   1.00 22.86  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.929   -15.956 0.849   1.00 23.25  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? 0.073   -15.081 0.665   1.00 22.36  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 1.100   -16.300 3.297   1.00 22.41  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 2.014   -16.331 4.507   1.00 22.15  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 2.335   -15.156 5.180   1.00 24.73  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.579   -17.544 4.913   1.00 27.57  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 3.224   -15.193 6.254   1.00 32.21  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.482   -17.577 5.978   1.00 28.48  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.791   -16.407 6.638   1.00 31.18  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 1.001   -17.062 0.094   1.00 23.27  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? 0.204   -17.233 -1.122  1.00 21.17  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -0.778  -18.380 -0.909  1.00 25.66  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.384  -19.407 -0.346  1.00 26.25  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 1.090   -17.474 -2.346  1.00 23.09  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.051  -18.166 -1.319  1.00 24.56  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.106  -19.167 -1.074  1.00 24.68  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.449  -19.881 -2.371  1.00 28.21  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -3.800  -19.263 -3.349  1.00 29.80  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.315  -18.475 -0.417  1.00 26.01  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.434  -19.453 0.082   1.00 32.06  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -4.947  -20.484 1.105   1.00 30.72  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.111  -21.208 1.772   1.00 35.45  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.536  -22.337 0.939   1.00 35.08  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.468  -21.214 -2.304  1.00 29.82  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.076  -22.010 -3.350  1.00 33.86  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.055  -22.975 -2.687  1.00 40.31  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -4.816  -23.426 -1.569  1.00 35.00  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -2.955  -22.731 -4.088  1.00 35.18  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -2.152  -21.724 -4.942  1.00 41.81  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.246  -22.602 -6.207  1.00 44.01  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -0.350  -23.804 -5.207  1.00 43.05  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.160  -23.246 -3.387  1.00 44.75  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.225  -24.102 -2.870  1.00 43.48  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.629  -25.448 -2.457  1.00 40.37  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.763  -26.011 -3.129  1.00 38.60  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.326  -24.138 -3.945  1.00 53.04  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.541  -25.033 -3.721  1.00 57.39  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.810 -24.429 -4.318  1.00 55.98  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.028  -25.931 -1.275  1.00 43.61  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -6.529  -27.208 -0.817  1.00 40.56  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.184  -27.098 -0.113  1.00 44.69  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -4.644  -28.089 0.356   1.00 44.13  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -4.614  -25.889 -0.043  1.00 42.36  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.304  -25.792 0.578   1.00 35.50  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.368  -24.678 1.602   1.00 31.32  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.128  -23.742 1.425   1.00 31.16  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.217  -25.395 -0.431  1.00 36.20  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -1.840  -26.359 -1.555  1.00 40.76  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -0.732  -27.193 -1.447  1.00 52.06  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.567  -26.398 -2.746  1.00 44.04  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.372  -28.059 -2.477  1.00 54.13  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.229  -27.278 -3.773  1.00 48.09  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.118  -28.096 -3.646  1.00 52.84  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -0.787  -28.963 -4.664  1.00 59.68  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -2.598  -24.776 2.704   1.00 31.43  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -2.505  -23.705 3.705   1.00 30.09  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -1.820  -22.488 3.068   1.00 29.67  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.036  -22.690 2.150   1.00 31.58  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -1.620  -24.365 4.799   1.00 36.28  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -0.800  -25.427 4.054   1.00 37.49  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -1.739  -25.942 2.985   1.00 37.45  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.123  -21.280 3.554   1.00 28.30  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.391  -20.074 3.148   1.00 26.48  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? 0.111   -20.355 3.236   1.00 27.75  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.595   -20.757 4.303   1.00 25.84  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -1.818  -18.901 4.033   1.00 29.13  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.279  -18.503 3.827   1.00 27.59  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.310  -19.226 4.413   1.00 31.30  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -3.860  -17.510 3.145   1.00 31.94  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -5.468  -18.639 4.120   1.00 30.62  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.234  -17.594 3.344   1.00 33.69  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.847   -20.108 2.119   1.00 26.01  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 2.179   -20.704 1.967   1.00 24.20  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 3.267   -19.629 1.833   1.00 23.96  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 3.107   -18.714 1.033   1.00 24.63  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 2.203   -21.602 0.726   1.00 24.86  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 3.326   -22.606 0.763   1.00 26.69  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.669   -22.435 0.536   1.00 24.66  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 3.131   -24.004 1.037   1.00 28.71  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 5.330   -23.643 0.656   1.00 26.59  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 4.396   -24.614 0.968   1.00 29.47  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.990   -24.772 1.324   1.00 35.89  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.564   -25.989 1.191   1.00 38.09  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 2.158   -26.126 1.540   1.00 35.47  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 3.431   -26.721 1.478   1.00 37.73  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 4.423   -19.703 2.550   1.00 24.48  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 5.476   -18.689 2.388   1.00 20.97  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.987   -18.637 0.946   1.00 21.07  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 6.315   -19.673 0.345   1.00 22.56  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 6.573   -19.129 3.385   1.00 22.69  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 6.336   -20.642 3.547   1.00 23.06  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.805   -20.778 3.497   1.00 25.10  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 6.028   -17.421 0.374   1.00 20.36  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 6.342   -17.279 -1.056  1.00 20.36  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.880   -15.887 -1.352  1.00 20.01  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.897   -15.045 -0.476  1.00 20.54  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 5.093   -17.593 -1.896  1.00 21.23  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 7.423   -15.692 -2.563  1.00 19.55  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.824   -14.365 -3.002  1.00 20.02  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 7.308   -14.120 -4.415  1.00 21.66  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 7.047   -15.072 -5.160  1.00 22.86  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 9.353   -14.241 -2.952  1.00 21.94  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 10.046  -15.088 -4.003  1.00 23.07  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.586  -14.957 -3.813  1.00 22.62  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 12.254  -15.730 -4.897  1.00 23.33  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 13.535  -16.151 -4.795  1.00 25.75  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 14.218  -16.001 -3.640  1.00 24.35  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 14.071  -16.808 -5.843  1.00 27.18  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 7.142   -12.846 -4.773  1.00 21.74  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.928   -12.491 -6.174  1.00 19.84  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 8.264   -12.565 -6.910  1.00 24.98  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 9.236   -11.923 -6.500  1.00 23.67  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 6.437   -11.038 -6.234  1.00 20.98  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 5.312   -10.690 -5.244  1.00 28.99  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 6.061   -10.640 -7.693  1.00 22.15  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.968   -11.339 -5.512  1.00 30.17  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 8.303   -13.391 -7.944  1.00 25.04  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 9.507   -13.544 -8.741  1.00 26.96  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.581   -12.509 -9.856  1.00 29.78  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.605   -11.836 -10.227 1.00 28.03  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.613   -14.951 -9.304  1.00 26.58  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.584  -15.896 -8.615  1.00 29.22  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 11.222  -15.495 -7.595  1.00 33.18  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.696  -17.009 -9.103  1.00 29.86  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.823  -12.328 -10.348 1.00 32.60  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 11.064  -11.640 -11.600 1.00 35.60  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.776  -12.624 -12.727 1.00 32.30  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.587  -13.812 -12.504 1.00 33.55  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.522  -11.195 -11.684 1.00 41.53  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.863  -9.839  -11.080 1.00 48.27  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.424  -8.810  -11.648 1.00 55.08  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.570  -9.820  -10.051 1.00 54.04  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.711  -12.112 -13.955 1.00 33.63  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.632  -13.021 -15.099 1.00 32.93  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.942  -12.793 -15.865 1.00 29.23  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 12.231  -11.642 -16.154 1.00 32.59  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.415   -12.604 -15.950 1.00 35.55  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 8.071   -12.763 -15.180 1.00 34.93  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.391   -13.352 -17.290 1.00 35.39  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 7.043   -11.747 -15.619 1.00 38.50  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.733  -13.864 -16.050 1.00 33.55  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.977  -13.838 -16.805 1.00 33.85  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.703  -13.504 -18.274 1.00 32.67  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.659  -13.803 -18.831 1.00 29.79  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.662  -15.191 -16.674 1.00 35.05  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.673  -12.835 -18.904 1.00 35.07  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.661  -12.709 -20.359 1.00 31.27  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.386  -14.063 -20.983 1.00 27.26  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.977  -15.059 -20.582 1.00 31.29  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 16.012  -12.182 -20.813 1.00 33.85  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 16.283  -10.717 -20.549 1.00 36.02  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 15.309  -9.992  -20.338 1.00 35.08  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 17.490  -10.305 -20.562 1.00 36.71  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.446  -14.075 -21.939 1.00 29.56  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.123  -15.247 -22.744 1.00 30.94  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.289  -16.315 -22.038 1.00 34.80  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 12.005  -17.352 -22.623 1.00 35.51  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.970  -16.094 -20.758 1.00 34.25  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 11.155  -17.044 -20.008 1.00 34.04  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.664   -16.770 -20.254 1.00 30.38  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 9.237   -15.679 -20.661 1.00 30.83  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.512  -16.943 -18.528 1.00 35.42  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.858   -17.812 -19.966 1.00 32.37  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.409   -17.750 -20.079 1.00 33.24  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.829   -16.728 -19.098 1.00 33.11  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 7.105   -16.788 -17.902 1.00 34.66  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.888   -19.161 -19.732 1.00 34.36  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.364   -19.172 -19.665 1.00 34.17  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.378   -20.188 -20.765 1.00 37.07  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 6.013   -15.826 -19.636 1.00 34.13  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.376   -14.760 -18.875 1.00 34.53  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 4.062   -15.257 -18.267 1.00 34.54  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.427   -16.180 -18.776 1.00 34.83  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 5.070   -13.584 -19.799 1.00 37.06  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 6.308   -12.835 -20.272 1.00 36.98  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.985   -11.600 -21.111 1.00 43.34  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.505   -12.041 -22.468 1.00 42.23  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.385   -10.912 -23.389 1.00 44.49  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.572   -14.631 -17.177 1.00 36.47  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 2.308   -15.071 -16.574 1.00 33.16  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 1.177   -14.562 -17.458 1.00 32.76  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.349   -13.600 -18.203 1.00 37.04  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 2.215   -14.373 -15.208 1.00 34.15  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.207   -13.210 -15.325 1.00 41.20  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 4.104   -13.399 -16.576 1.00 35.30  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.048  -15.087 -17.271 1.00 36.81  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.225  -14.480 -17.883 1.00 37.40  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.451  -13.059 -17.390 1.00 38.41  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -0.949  -12.685 -16.324 1.00 31.72  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.336  -15.404 -17.409 1.00 36.70  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -1.670  -16.713 -17.077 1.00 36.39  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.342  -16.309 -16.501 1.00 35.76  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.261  -12.228 -18.096 1.00 37.53  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.653  -10.919 -17.575 1.00 39.98  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.233  -10.937 -16.168 1.00 37.12  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -3.914  -11.890 -15.783 1.00 39.54  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.646  -10.315 -18.588 1.00 48.62  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -3.851  -11.402 -19.598 1.00 42.55  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -2.826  -12.509 -19.437 1.00 44.66  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -2.907  -9.873  -15.420 1.00 37.23  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.330  -9.639  -14.058 1.00 38.92  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -2.807  -10.721 -13.115 1.00 34.09  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.267  -10.761 -11.974 1.00 32.98  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -4.857  -9.614  -13.957 1.00 45.65  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.449  -8.616  -14.927 1.00 52.12  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.337  -7.404  -14.716 1.00 57.16  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.048  -9.101  -16.001 1.00 56.26  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -1.893  -11.599 -13.579 1.00 30.13  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.283  -12.594 -12.677 1.00 28.19  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? 0.215   -12.290 -12.433 1.00 25.21  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.874   -11.510 -13.169 1.00 26.78  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.451  -14.047 -13.117 1.00 31.85  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -2.860  -14.556 -13.464 1.00 33.10  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -3.808  -14.378 -12.284 1.00 38.04  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.223  -14.855 -12.575 1.00 45.42  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.131  -16.259 -12.971 1.00 47.63  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.731   -12.841 -11.309 1.00 25.05  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 2.113   -12.664 -10.887 1.00 26.40  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.815   -14.016 -10.805 1.00 25.04  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 2.222   -15.032 -10.477 1.00 23.67  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 2.190   -12.068 -9.459  1.00 25.94  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.736   -10.617 -9.481  1.00 27.18  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? 0.391   -10.329 -9.320  1.00 27.36  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.615   -9.567  -9.673  1.00 28.67  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.067  -9.023  -9.430  1.00 30.68  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 2.173   -8.239  -9.736  1.00 30.67  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.817   -7.985  -9.616  1.00 32.68  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? 0.287   -6.717  -9.744  1.00 35.08  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 4.133   -14.113 -11.094 1.00 23.65  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.834   -15.388 -10.907 1.00 24.23  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 5.149   -15.541 -9.429  1.00 22.64  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.815   -14.676 -8.881  1.00 24.69  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 6.121   -15.270 -11.720 1.00 24.23  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 6.221   -13.813 -11.999 1.00 27.53  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.943   -13.038 -11.688 1.00 26.45  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.601   -16.571 -8.794  1.00 23.36  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.805   -16.788 -7.363  1.00 23.33  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.766   -17.971 -7.187  1.00 26.33  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 5.470   -19.127 -7.609  1.00 27.64  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 3.459   -17.053 -6.673  1.00 23.42  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 2.455   -15.914 -6.898  1.00 23.12  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.697   -17.322 -5.167  1.00 24.96  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.972   -14.514 -6.550  1.00 25.08  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.867   -17.712 -6.463  1.00 22.93  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.809   -18.755 -6.103  1.00 25.49  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 7.526   -19.177 -4.663  1.00 24.57  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 7.600   -18.358 -3.735  1.00 23.31  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 9.259   -18.228 -6.262  1.00 23.17  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 10.287  -19.261 -5.836  1.00 25.03  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.687  -20.274 -6.722  1.00 29.81  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.861  -19.218 -4.553  1.00 25.94  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.601  -21.245 -6.304  1.00 29.16  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.807  -20.174 -4.154  1.00 30.08  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 12.182  -21.176 -5.046  1.00 29.29  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 7.202   -20.467 -4.467  1.00 21.99  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.859   -20.969 -3.147  1.00 21.13  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 8.105   -21.510 -2.453  1.00 26.51  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.828   -22.362 -3.014  1.00 26.57  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.891   -22.145 -3.443  1.00 25.04  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 4.468   -21.685 -3.809  1.00 23.35  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 4.087   -21.491 -5.138  1.00 28.46  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 3.513   -21.459 -2.813  1.00 28.16  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.808   -20.998 -5.453  1.00 29.16  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 2.224   -21.026 -3.133  1.00 27.78  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.877   -20.784 -4.440  1.00 27.45  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 8.422   -20.930 -1.274  1.00 24.65  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 9.569   -21.434 -0.512  1.00 22.45  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 9.327   -22.887 -0.102  1.00 25.52  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 8.180   -23.329 -0.004  1.00 26.30  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.831   -20.496 0.675   1.00 24.22  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 10.282  -19.098 0.287   1.00 23.86  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 11.529  -18.895 -0.285  1.00 22.76  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 9.489   -17.976 0.550   1.00 23.29  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.973  -17.628 -0.601  1.00 22.01  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.910   -16.705 0.225   1.00 20.85  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 11.145  -16.527 -0.368  1.00 22.89  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 10.420  -23.623 0.033   1.00 25.34  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 10.373  -24.998 0.538   1.00 25.40  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 10.195  -25.967 -0.636  1.00 31.55  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 11.076  -26.782 -0.922  1.00 35.05  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 9.051   -25.883 -1.316  1.00 32.47  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.776   -26.720 -2.478  1.00 33.67  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 9.556   -26.217 -3.695  1.00 33.42  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.831   -26.980 -4.618  1.00 30.50  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 7.276   -26.780 -2.794  1.00 35.00  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.884   -25.492 -3.267  1.00 30.90  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 6.388   -27.256 -1.662  1.00 33.81  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.845   -24.904 -3.748  1.00 27.94  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 10.526  -24.237 -4.847  1.00 28.12  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.690   -24.326 -6.134  1.00 29.42  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 10.261  -24.296 -7.217  1.00 33.07  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.986  -24.732 -5.032  1.00 27.98  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.702  -24.840 -3.730  1.00 32.95  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 13.450  -25.919 -3.310  1.00 34.03  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.763  -23.935 -2.723  1.00 33.04  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.922  -25.671 -2.097  1.00 42.05  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 13.526  -24.470 -1.722  1.00 34.18  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 8.360   -24.422 -5.999  1.00 30.70  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 7.462   -24.463 -7.148  1.00 34.04  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 7.020   -23.053 -7.548  1.00 31.13  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 7.107   -22.089 -6.761  1.00 30.62  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 6.235   -25.330 -6.879  1.00 36.43  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.574   -26.813 -6.780  1.00 44.90  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.434   -27.677 -6.269  1.00 54.19  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 4.295   -27.198 -6.105  1.00 57.79  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.724   -28.862 -5.993  1.00 62.75  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.621   -22.918 -8.813  1.00 28.25  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 6.123   -21.639 -9.305  1.00 27.69  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.687   -21.824 -9.759  1.00 30.57  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 4.372   -22.774 -10.480 1.00 31.34  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.956   -21.033 -10.435 1.00 32.34  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 8.272   -20.716 -10.012 1.00 31.43  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 6.272   -19.814 -11.042 1.00 30.87  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.801   -20.929 -9.311  1.00 30.33  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 2.458   -20.858 -9.875  1.00 28.11  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 2.102   -19.398 -10.137 1.00 28.70  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.823   -18.466 -9.728  1.00 27.30  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 1.461   -21.543 -8.973  1.00 27.85  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 1.066   -19.189 -10.953 1.00 27.36  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.666   -17.856 -11.365 1.00 27.13  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -0.594  -17.479 -10.599 1.00 29.50  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -1.608  -18.188 -10.669 1.00 34.27  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? 0.376   -17.846 -12.871 1.00 28.26  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.604   -18.111 -13.731 1.00 31.37  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.750   -17.321 -13.620 1.00 37.65  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 1.590   -19.140 -14.684 1.00 37.74  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.863   -17.546 -14.433 1.00 42.27  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.705   -19.352 -15.494 1.00 38.77  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.828   -18.557 -15.377 1.00 39.61  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -0.522  -16.385 -9.824  1.00 24.77  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -1.625  -16.048 -8.927  1.00 23.40  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -1.913  -14.546 -9.012  1.00 24.63  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.032  -13.738 -9.343  1.00 25.77  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.253  -16.331 -7.469  1.00 24.96  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.238  -17.798 -7.063  1.00 26.66  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -0.847  -17.913 -5.575  1.00 28.26  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -2.628  -18.394 -7.359  1.00 32.64  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.186  -14.193 -8.712  1.00 25.17  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -3.600  -12.786 -8.658  1.00 24.09  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -3.612  -12.272 -7.199  1.00 21.79  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -3.540  -13.102 -6.258  1.00 23.22  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -3.696  -10.934 -6.999  1.00 23.59  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -3.612  -10.323 -5.657  1.00 23.04  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -4.594  -10.851 -4.614  1.00 23.73  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.303  -10.812 -3.421  1.00 22.94  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -3.949  -8.868  -5.960  1.00 24.14  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.327  -8.661  -7.327  1.00 26.67  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -3.726  -9.935  -8.088  1.00 23.02  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -5.748  -11.407 -5.075  1.00 25.25  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -6.715  -11.929 -4.103  1.00 24.73  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.138  -13.078 -3.251  1.00 25.61  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -6.613  -13.362 -2.146  1.00 25.03  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.004  -12.425 -4.773  1.00 26.79  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -7.799  -13.706 -5.596  1.00 31.31  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.136  -14.161 -6.209  1.00 37.92  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.096  -15.497 -6.939  1.00 38.59  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -8.818  -16.640 -6.060  1.00 44.08  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.131  -13.793 -3.791  1.00 23.09  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -4.513  -14.916 -3.120  1.00 24.81  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.162  -14.570 -2.487  1.00 24.63  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.467  -15.508 -2.108  1.00 24.10  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.392  -16.108 -4.058  1.00 26.04  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -5.769  -16.683 -4.398  1.00 30.68  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -6.601  -16.781 -3.444  1.00 31.01  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -5.991  -17.035 -5.568  1.00 30.46  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -2.819  -13.274 -2.423  1.00 22.75  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.490  -12.838 -1.979  1.00 20.34  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -1.647  -11.985 -0.717  1.00 18.79  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.230  -10.910 -0.759  1.00 22.34  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -0.775  -12.064 -3.098  1.00 20.94  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -0.609  -12.866 -4.384  1.00 22.27  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? 0.016   -11.987 -5.442  1.00 26.23  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? 0.260   -14.132 -4.174  1.00 21.60  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.020  -12.395 0.395   1.00 20.73  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.115  -11.736 1.703   1.00 20.00  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? 0.282   -11.242 2.102   1.00 23.95  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 1.187   -12.065 2.306   1.00 25.39  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -1.592  -12.806 2.709   1.00 22.68  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.043  -13.222 2.469   1.00 23.98  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.343  -14.158 1.473   1.00 26.99  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.076  -12.682 3.245   1.00 27.00  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -4.677  -14.513 1.220   1.00 30.38  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.385  -13.071 3.014   1.00 25.82  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -5.674  -13.956 2.004   1.00 24.36  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? 0.528   -9.922  2.201   1.00 24.06  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.862   -9.407  2.540   1.00 24.86  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 2.419   -10.056 3.812   1.00 25.66  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.716   -10.281 4.813   1.00 26.58  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.592   -7.902  2.678   1.00 25.59  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.556   -7.644  1.565   1.00 29.52  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.387  -8.812  1.858   1.00 25.24  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.720   -10.430 3.756   1.00 24.80  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 4.282   -11.331 4.767   1.00 25.61  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 4.285   -10.702 6.177   1.00 24.03  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.867   -11.366 7.129   1.00 28.12  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.687   -11.776 4.298   1.00 23.12  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 6.476   -12.561 5.341   1.00 24.27  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 6.191   -13.901 5.612   1.00 26.54  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 7.491   -11.944 6.073   1.00 30.83  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.891   -14.623 6.585   1.00 28.39  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 8.200   -12.678 7.016   1.00 29.83  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.886   -13.990 7.294   1.00 30.71  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.579   -14.729 8.242   1.00 32.03  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.704   -9.439  6.250   1.00 27.29  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.820   -8.756  7.545   1.00 30.82  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 3.476   -8.746  8.281   1.00 30.87  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 3.456   -9.196  9.423   1.00 37.60  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.467   -7.398  7.423   1.00 31.64  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 2.395   -8.344  7.576   1.00 32.16  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 1.059   -8.258  8.176   1.00 35.09  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? 0.564   -9.631  8.645   1.00 34.58  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.121  -9.729  9.669   1.00 31.60  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? 0.116   -7.549  7.193   1.00 33.02  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.355  -7.462  7.639   1.00 39.34  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.178  -6.736  6.578   1.00 40.45  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.371  -6.051  7.174   1.00 46.06  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.284  -7.040  7.727   1.00 48.25  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.908   -10.703 7.919   1.00 29.04  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? 0.241   -12.003 8.035   1.00 28.66  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 1.031   -13.078 8.797   1.00 30.03  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? 0.515   -14.182 8.964   1.00 31.52  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.098  -12.556 6.670   1.00 29.32  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.009  -11.673 6.022   1.00 40.37  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 2.292   -12.820 9.161   1.00 28.62  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 3.124   -13.933 9.620   1.00 32.30  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 2.686   -14.470 11.000  1.00 29.85  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.807   -15.669 11.280  1.00 33.56  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 4.601   -13.541 9.579   1.00 32.55  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.984   -12.395 10.453  1.00 37.80  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 6.490   -12.210 10.322  1.00 49.74  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.981   -11.159 11.273  1.00 58.96  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.239   -9.910  11.087  1.00 67.34  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 2.150   -13.572 11.831  0.50 34.45  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 2.171   -13.585 11.858  0.50 35.05  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 1.628   -13.972 13.133  0.50 38.53  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 1.607   -14.045 13.123  0.50 38.96  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? 0.521   -15.026 12.967  0.50 39.34  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? 0.616   -15.174 12.852  0.50 38.82  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? 0.399   -15.952 13.769  0.50 40.68  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? 0.660   -16.252 13.452  0.50 37.29  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 1.286   -12.753 13.986  0.50 40.38  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.896   -12.915 13.853  0.50 43.32  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 2.440   -11.957 14.600  0.50 40.14  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? 0.219   -13.281 15.170  0.50 48.48  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.613   -12.355 14.430  0.50 42.70  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 0.933   -13.733 16.095  0.50 53.65  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 2.163   -10.924 15.266  0.50 39.66  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.016  -13.100 15.267  0.50 50.72  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.278  -14.918 11.897  1.00 34.57  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -1.370  -15.840 11.658  1.00 32.02  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -0.900  -17.081 10.907  1.00 34.41  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -1.318  -18.194 11.212  1.00 38.30  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -2.406  -15.110 10.803  1.00 35.78  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -3.764  -15.757 10.765  1.00 35.14  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -4.766  -14.875 10.015  1.00 40.95  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.191  -15.308 10.218  1.00 48.96  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.123  -14.387 9.553   1.00 51.18  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.110  -16.898 9.837   1.00 30.34  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? 0.120   -18.017 8.940   1.00 27.31  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 1.506   -18.632 9.107   1.00 30.31  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.768   -19.691 8.562   1.00 34.78  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.033  -17.511 7.497   1.00 27.72  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -1.434  -17.052 7.146   1.00 30.44  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -2.571  -17.796 7.501   1.00 29.87  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -1.617  -15.870 6.440   1.00 31.13  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -3.842  -17.379 7.127   1.00 34.26  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -2.886  -15.444 6.071   1.00 30.96  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -3.997  -16.192 6.423   1.00 32.24  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.223  -15.724 6.037   1.00 32.80  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 2.394   -17.987 9.853   1.00 29.61  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.778   -18.445 9.944   1.00 32.24  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.970   -19.416 11.108  1.00 34.97  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.709   -19.094 12.023  1.00 40.37  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 3.254   -20.548 11.080  1.00 41.15  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 3.420   -21.620 12.058  1.00 39.35  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 3.689   -22.934 11.331  1.00 38.37  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 3.263   -23.120 10.191  1.00 40.30  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 2.211   -21.587 12.999  1.00 47.13  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 2.101   -20.308 13.822  1.00 44.48  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? 0.708   -20.153 14.412  1.00 53.68  ? 70  LYS A CD  1 
ATOM   567  C CE  . LYS A 1 71 ? 0.530   -18.903 15.205  1.00 60.38  ? 70  LYS A CE  1 
ATOM   568  N NZ  . LYS A 1 71 ? -0.885  -18.531 15.144  1.00 69.17  ? 70  LYS A NZ  1 
ATOM   569  N N   . PRO A 1 72 ? 4.431   -23.901 11.945  1.00 36.49  ? 71  PRO A N   1 
ATOM   570  C CA  . PRO A 1 72 ? 4.706   -25.189 11.296  1.00 38.06  ? 71  PRO A CA  1 
ATOM   571  C C   . PRO A 1 72 ? 3.449   -25.890 10.812  1.00 33.59  ? 71  PRO A C   1 
ATOM   572  O O   . PRO A 1 72 ? 2.404   -25.733 11.428  1.00 45.39  ? 71  PRO A O   1 
ATOM   573  C CB  . PRO A 1 72 ? 5.425   -26.002 12.393  1.00 39.94  ? 71  PRO A CB  1 
ATOM   574  C CG  . PRO A 1 72 ? 6.053   -24.944 13.272  1.00 44.77  ? 71  PRO A CG  1 
ATOM   575  C CD  . PRO A 1 72 ? 5.054   -23.771 13.271  1.00 41.69  ? 71  PRO A CD  1 
ATOM   576  N N   . ASN A 1 73 ? 3.600   -26.698 9.759   1.00 38.30  ? 72  ASN A N   1 
ATOM   577  C CA  . ASN A 1 73 ? 2.541   -27.386 9.056   1.00 44.59  ? 72  ASN A CA  1 
ATOM   578  C C   . ASN A 1 73 ? 3.139   -28.698 8.575   1.00 45.81  ? 72  ASN A C   1 
ATOM   579  O O   . ASN A 1 73 ? 4.297   -28.748 8.165   1.00 54.06  ? 72  ASN A O   1 
ATOM   580  C CB  . ASN A 1 73 ? 2.075   -26.562 7.855   1.00 45.76  ? 72  ASN A CB  1 
ATOM   581  C CG  . ASN A 1 73 ? 0.738   -26.996 7.294   1.00 56.23  ? 72  ASN A CG  1 
ATOM   582  O OD1 . ASN A 1 73 ? 0.656   -27.936 6.495   1.00 56.98  ? 72  ASN A OD1 1 
ATOM   583  N ND2 . ASN A 1 73 ? -0.330  -26.299 7.651   1.00 54.96  ? 72  ASN A ND2 1 
ATOM   584  N N   . LYS A 1 74 ? 2.336   -29.758 8.604   1.00 47.76  ? 73  LYS A N   1 
ATOM   585  C CA  . LYS A 1 74 ? 2.817   -31.079 8.253   1.00 51.75  ? 73  LYS A CA  1 
ATOM   586  C C   . LYS A 1 74 ? 3.084   -31.197 6.752   1.00 52.63  ? 73  LYS A C   1 
ATOM   587  O O   . LYS A 1 74 ? 3.737   -32.140 6.306   1.00 51.76  ? 73  LYS A O   1 
ATOM   588  C CB  . LYS A 1 74 ? 1.794   -32.108 8.755   1.00 60.43  ? 73  LYS A CB  1 
ATOM   589  C CG  . LYS A 1 74 ? 0.471   -32.186 7.990   1.00 67.46  ? 73  LYS A CG  1 
ATOM   590  N N   . ARG A 1 75 ? 2.596   -30.242 5.953   1.00 42.21  ? 74  ARG A N   1 
ATOM   591  C CA  . ARG A 1 75 ? 2.637   -30.437 4.512   1.00 45.34  ? 74  ARG A CA  1 
ATOM   592  C C   . ARG A 1 75 ? 4.083   -30.404 4.001   1.00 38.71  ? 74  ARG A C   1 
ATOM   593  O O   . ARG A 1 75 ? 4.902   -29.660 4.531   1.00 39.45  ? 74  ARG A O   1 
ATOM   594  C CB  . ARG A 1 75 ? 1.686   -29.412 3.880   1.00 45.69  ? 74  ARG A CB  1 
ATOM   595  C CG  . ARG A 1 75 ? 0.268   -29.833 4.233   1.00 51.59  ? 74  ARG A CG  1 
ATOM   596  C CD  . ARG A 1 75 ? -0.286  -30.797 3.206   1.00 46.92  ? 74  ARG A CD  1 
ATOM   597  N NE  . ARG A 1 75 ? -1.159  -30.137 2.226   1.00 58.10  ? 74  ARG A NE  1 
ATOM   598  C CZ  . ARG A 1 75 ? -2.371  -29.626 2.503   1.00 56.84  ? 74  ARG A CZ  1 
ATOM   599  N NH1 . ARG A 1 75 ? -3.179  -29.306 1.513   1.00 60.32  ? 74  ARG A NH1 1 
ATOM   600  N NH2 . ARG A 1 75 ? -2.816  -29.523 3.750   1.00 59.92  ? 74  ARG A NH2 1 
ATOM   601  N N   . LYS A 1 76 ? 4.365   -31.202 2.955   1.00 38.19  ? 75  LYS A N   1 
ATOM   602  C CA  . LYS A 1 76 ? 5.725   -31.379 2.448   1.00 39.28  ? 75  LYS A CA  1 
ATOM   603  C C   . LYS A 1 76 ? 6.324   -30.029 2.044   1.00 38.99  ? 75  LYS A C   1 
ATOM   604  O O   . LYS A 1 76 ? 5.752   -29.345 1.192   1.00 34.30  ? 75  LYS A O   1 
ATOM   605  C CB  . LYS A 1 76 ? 5.711   -32.277 1.204   1.00 41.20  ? 75  LYS A CB  1 
ATOM   606  C CG  . LYS A 1 76 ? 7.076   -32.684 0.715   1.00 43.40  ? 75  LYS A CG  1 
ATOM   607  C CD  . LYS A 1 76 ? 7.037   -33.790 -0.338  1.00 51.53  ? 75  LYS A CD  1 
ATOM   608  C CE  . LYS A 1 76 ? 8.403   -34.332 -0.635  1.00 60.15  ? 75  LYS A CE  1 
ATOM   609  N N   . GLY A 1 77 ? 7.488   -29.692 2.620   1.00 39.54  ? 76  GLY A N   1 
ATOM   610  C CA  . GLY A 1 77 ? 8.272   -28.532 2.218   1.00 33.17  ? 76  GLY A CA  1 
ATOM   611  C C   . GLY A 1 77 ? 7.926   -27.268 3.002   1.00 32.86  ? 76  GLY A C   1 
ATOM   612  O O   . GLY A 1 77 ? 8.668   -26.278 2.944   1.00 30.96  ? 76  GLY A O   1 
ATOM   613  N N   . PHE A 1 78 ? 6.833   -27.305 3.768   1.00 30.70  ? 77  PHE A N   1 
ATOM   614  C CA  . PHE A 1 78 ? 6.322   -26.097 4.408   1.00 28.56  ? 77  PHE A CA  1 
ATOM   615  C C   . PHE A 1 78 ? 7.299   -25.522 5.444   1.00 30.39  ? 77  PHE A C   1 
ATOM   616  O O   . PHE A 1 78 ? 7.580   -24.320 5.464   1.00 31.48  ? 77  PHE A O   1 
ATOM   617  C CB  . PHE A 1 78 ? 4.946   -26.400 4.997   1.00 30.75  ? 77  PHE A CB  1 
ATOM   618  C CG  . PHE A 1 78 ? 4.217   -25.132 5.416   1.00 34.72  ? 77  PHE A CG  1 
ATOM   619  C CD1 . PHE A 1 78 ? 4.482   -24.510 6.631   1.00 34.02  ? 77  PHE A CD1 1 
ATOM   620  C CD2 . PHE A 1 78 ? 3.288   -24.542 4.561   1.00 34.52  ? 77  PHE A CD2 1 
ATOM   621  C CE1 . PHE A 1 78 ? 3.823   -23.347 7.011   1.00 33.64  ? 77  PHE A CE1 1 
ATOM   622  C CE2 . PHE A 1 78 ? 2.600   -23.385 4.951   1.00 31.65  ? 77  PHE A CE2 1 
ATOM   623  C CZ  . PHE A 1 78 ? 2.874   -22.776 6.161   1.00 30.36  ? 77  PHE A CZ  1 
ATOM   624  N N   . ASN A 1 79 ? 7.813   -26.368 6.359   1.00 31.70  ? 78  ASN A N   1 
ATOM   625  C CA  . ASN A 1 79 ? 8.752   -25.907 7.380   1.00 32.82  ? 78  ASN A CA  1 
ATOM   626  C C   . ASN A 1 79 ? 10.079  -25.413 6.789   1.00 27.63  ? 78  ASN A C   1 
ATOM   627  O O   . ASN A 1 79 ? 10.654  -24.432 7.323   1.00 30.98  ? 78  ASN A O   1 
ATOM   628  C CB  . ASN A 1 79 ? 8.877   -26.954 8.501   1.00 31.97  ? 78  ASN A CB  1 
ATOM   629  C CG  . ASN A 1 79 ? 7.521   -27.245 9.106   1.00 36.88  ? 78  ASN A CG  1 
ATOM   630  O OD1 . ASN A 1 79 ? 6.600   -26.423 9.031   1.00 35.18  ? 78  ASN A OD1 1 
ATOM   631  N ND2 . ASN A 1 79 ? 7.383   -28.387 9.775   1.00 34.46  ? 78  ASN A ND2 1 
ATOM   632  N N   . GLU A 1 80 ? 10.582  -26.065 5.716   1.00 26.47  ? 79  GLU A N   1 
ATOM   633  C CA  . GLU A 1 80 ? 11.740  -25.578 5.000   1.00 29.30  ? 79  GLU A CA  1 
ATOM   634  C C   . GLU A 1 80 ? 11.386  -24.188 4.463   1.00 28.40  ? 79  GLU A C   1 
ATOM   635  O O   . GLU A 1 80 ? 12.189  -23.269 4.581   1.00 26.19  ? 79  GLU A O   1 
ATOM   636  C CB  . GLU A 1 80 ? 12.214  -26.518 3.894   1.00 29.36  ? 79  GLU A CB  1 
ATOM   637  C CG  . GLU A 1 80 ? 13.465  -26.034 3.171   1.00 30.61  ? 79  GLU A CG  1 
ATOM   638  C CD  . GLU A 1 80 ? 13.933  -26.991 2.070   1.00 44.65  ? 79  GLU A CD  1 
ATOM   639  O OE1 . GLU A 1 80 ? 13.195  -27.910 1.643   1.00 44.93  ? 79  GLU A OE1 1 
ATOM   640  O OE2 . GLU A 1 80 ? 15.084  -26.795 1.640   1.00 42.20  ? 79  GLU A OE2 1 
ATOM   641  N N   . GLY A 1 81 ? 10.202  -24.055 3.855   1.00 28.43  ? 80  GLY A N   1 
ATOM   642  C CA  . GLY A 1 81 ? 9.737   -22.743 3.389   1.00 29.97  ? 80  GLY A CA  1 
ATOM   643  C C   . GLY A 1 81 ? 9.735   -21.636 4.442   1.00 27.29  ? 80  GLY A C   1 
ATOM   644  O O   . GLY A 1 81 ? 10.121  -20.502 4.134   1.00 24.60  ? 80  GLY A O   1 
ATOM   645  N N   . LEU A 1 82 ? 9.324   -21.941 5.685   1.00 25.15  ? 81  LEU A N   1 
ATOM   646  C CA  . LEU A 1 82 ? 9.306   -20.963 6.749   1.00 26.46  ? 81  LEU A CA  1 
ATOM   647  C C   . LEU A 1 82 ? 10.732  -20.508 7.041   1.00 27.32  ? 81  LEU A C   1 
ATOM   648  O O   . LEU A 1 82 ? 10.969  -19.330 7.309   1.00 26.10  ? 81  LEU A O   1 
ATOM   649  C CB  . LEU A 1 82 ? 8.623   -21.467 8.028   1.00 29.22  ? 81  LEU A CB  1 
ATOM   650  C CG  . LEU A 1 82 ? 7.119   -21.736 7.902   1.00 28.12  ? 81  LEU A CG  1 
ATOM   651  C CD1 . LEU A 1 82 ? 6.738   -22.334 9.261   1.00 35.02  ? 81  LEU A CD1 1 
ATOM   652  C CD2 . LEU A 1 82 ? 6.292   -20.467 7.668   1.00 28.01  ? 81  LEU A CD2 1 
ATOM   653  N N   . TRP A 1 83 ? 11.701  -21.439 6.935   1.00 25.55  ? 82  TRP A N   1 
ATOM   654  C CA  . TRP A 1 83 ? 13.069  -21.034 7.235   1.00 26.32  ? 82  TRP A CA  1 
ATOM   655  C C   . TRP A 1 83 ? 13.582  -20.086 6.157   1.00 24.99  ? 82  TRP A C   1 
ATOM   656  O O   . TRP A 1 83 ? 14.219  -19.085 6.462   1.00 25.77  ? 82  TRP A O   1 
ATOM   657  C CB  . TRP A 1 83 ? 13.988  -22.276 7.393   1.00 28.31  ? 82  TRP A CB  1 
ATOM   658  C CG  . TRP A 1 83 ? 15.433  -21.931 7.674   1.00 27.80  ? 82  TRP A CG  1 
ATOM   659  C CD1 . TRP A 1 83 ? 16.058  -21.888 8.891   1.00 29.36  ? 82  TRP A CD1 1 
ATOM   660  C CD2 . TRP A 1 83 ? 16.428  -21.562 6.697   1.00 27.01  ? 82  TRP A CD2 1 
ATOM   661  N NE1 . TRP A 1 83 ? 17.362  -21.501 8.732   1.00 30.05  ? 82  TRP A NE1 1 
ATOM   662  C CE2 . TRP A 1 83 ? 17.623  -21.320 7.401   1.00 26.41  ? 82  TRP A CE2 1 
ATOM   663  C CE3 . TRP A 1 83 ? 16.438  -21.466 5.299   1.00 28.99  ? 82  TRP A CE3 1 
ATOM   664  C CZ2 . TRP A 1 83 ? 18.792  -20.957 6.749   1.00 28.22  ? 82  TRP A CZ2 1 
ATOM   665  C CZ3 . TRP A 1 83 ? 17.603  -21.123 4.646   1.00 29.72  ? 82  TRP A CZ3 1 
ATOM   666  C CH2 . TRP A 1 83 ? 18.764  -20.853 5.374   1.00 30.71  ? 82  TRP A CH2 1 
ATOM   667  N N   . GLU A 1 84 ? 13.278  -20.408 4.894   1.00 22.62  ? 83  GLU A N   1 
ATOM   668  C CA  . GLU A 1 84 ? 13.754  -19.652 3.760   1.00 21.85  ? 83  GLU A CA  1 
ATOM   669  C C   . GLU A 1 84 ? 13.220  -18.228 3.814   1.00 22.65  ? 83  GLU A C   1 
ATOM   670  O O   . GLU A 1 84 ? 13.994  -17.300 3.642   1.00 22.92  ? 83  GLU A O   1 
ATOM   671  C CB  . GLU A 1 84 ? 13.323  -20.358 2.477   1.00 25.12  ? 83  GLU A CB  1 
ATOM   672  C CG  . GLU A 1 84 ? 14.131  -21.654 2.307   1.00 24.00  ? 83  GLU A CG  1 
ATOM   673  C CD  . GLU A 1 84 ? 13.710  -22.394 1.036   1.00 28.36  ? 83  GLU A CD  1 
ATOM   674  O OE1 . GLU A 1 84 ? 12.805  -21.961 0.299   1.00 26.96  ? 83  GLU A OE1 1 
ATOM   675  O OE2 . GLU A 1 84 ? 14.281  -23.496 0.772   1.00 28.58  ? 83  GLU A OE2 1 
ATOM   676  N N   . ILE A 1 85 ? 11.925  -18.072 4.049   1.00 22.95  ? 84  ILE A N   1 
ATOM   677  C CA  . ILE A 1 85 ? 11.348  -16.716 3.949   1.00 22.72  ? 84  ILE A CA  1 
ATOM   678  C C   . ILE A 1 85 ? 11.893  -15.854 5.098   1.00 22.37  ? 84  ILE A C   1 
ATOM   679  O O   . ILE A 1 85 ? 12.055  -14.643 4.939   1.00 23.48  ? 84  ILE A O   1 
ATOM   680  C CB  . ILE A 1 85 ? 9.794   -16.764 3.930   1.00 19.85  ? 84  ILE A CB  1 
ATOM   681  C CG1 . ILE A 1 85 ? 9.253   -15.392 3.479   1.00 21.81  ? 84  ILE A CG1 1 
ATOM   682  C CG2 . ILE A 1 85 ? 9.232   -17.121 5.310   1.00 21.25  ? 84  ILE A CG2 1 
ATOM   683  C CD1 . ILE A 1 85 ? 7.787   -15.439 3.046   1.00 22.87  ? 84  ILE A CD1 1 
ATOM   684  N N   . GLN A 1 86 ? 12.183  -16.465 6.261   1.00 21.40  ? 85  GLN A N   1 
ATOM   685  C CA  . GLN A 1 86 ? 12.739  -15.754 7.427   1.00 25.07  ? 85  GLN A CA  1 
ATOM   686  C C   . GLN A 1 86 ? 14.228  -15.426 7.274   1.00 27.76  ? 85  GLN A C   1 
ATOM   687  O O   . GLN A 1 86 ? 14.661  -14.338 7.686   1.00 29.10  ? 85  GLN A O   1 
ATOM   688  C CB  . GLN A 1 86 ? 12.384  -16.491 8.731   1.00 27.70  ? 85  GLN A CB  1 
ATOM   689  C CG  . GLN A 1 86 ? 12.820  -15.777 10.002  1.00 34.77  ? 85  GLN A CG  1 
ATOM   690  C CD  . GLN A 1 86 ? 12.145  -16.383 11.226  1.00 39.94  ? 85  GLN A CD  1 
ATOM   691  O OE1 . GLN A 1 86 ? 12.078  -17.612 11.386  1.00 34.50  ? 85  GLN A OE1 1 
ATOM   692  N NE2 . GLN A 1 86 ? 11.590  -15.533 12.081  1.00 49.18  ? 85  GLN A NE2 1 
ATOM   693  N N   . ASN A 1 87 ? 15.018  -16.361 6.703   1.00 25.33  ? 86  ASN A N   1 
ATOM   694  C CA  . ASN A 1 87 ? 16.475  -16.325 6.808   1.00 23.18  ? 86  ASN A CA  1 
ATOM   695  C C   . ASN A 1 87 ? 17.198  -15.947 5.514   1.00 24.18  ? 86  ASN A C   1 
ATOM   696  O O   . ASN A 1 87 ? 18.323  -15.405 5.567   1.00 26.06  ? 86  ASN A O   1 
ATOM   697  C CB  . ASN A 1 87 ? 16.960  -17.651 7.386   1.00 24.79  ? 86  ASN A CB  1 
ATOM   698  C CG  . ASN A 1 87 ? 16.514  -17.771 8.825   1.00 28.71  ? 86  ASN A CG  1 
ATOM   699  O OD1 . ASN A 1 87 ? 16.902  -16.937 9.660   1.00 31.86  ? 86  ASN A OD1 1 
ATOM   700  N ND2 . ASN A 1 87 ? 15.569  -18.661 9.131   1.00 29.12  ? 86  ASN A ND2 1 
ATOM   701  N N   . ASN A 1 88 ? 16.638  -16.298 4.336   1.00 23.24  ? 87  ASN A N   1 
ATOM   702  C CA  . ASN A 1 88 ? 17.310  -15.956 3.092   1.00 24.52  ? 87  ASN A CA  1 
ATOM   703  C C   . ASN A 1 88 ? 16.274  -15.872 1.963   1.00 24.14  ? 87  ASN A C   1 
ATOM   704  O O   . ASN A 1 88 ? 16.282  -16.639 0.980   1.00 24.91  ? 87  ASN A O   1 
ATOM   705  C CB  . ASN A 1 88 ? 18.461  -16.912 2.765   1.00 23.42  ? 87  ASN A CB  1 
ATOM   706  C CG  . ASN A 1 88 ? 19.502  -16.300 1.858   1.00 28.22  ? 87  ASN A CG  1 
ATOM   707  O OD1 . ASN A 1 88 ? 19.273  -15.280 1.190   1.00 26.17  ? 87  ASN A OD1 1 
ATOM   708  N ND2 . ASN A 1 88 ? 20.703  -16.887 1.849   1.00 28.91  ? 87  ASN A ND2 1 
ATOM   709  N N   . PRO A 1 89 ? 15.322  -14.920 2.073   1.00 22.58  ? 88  PRO A N   1 
ATOM   710  C CA  . PRO A 1 89 ? 14.183  -14.892 1.144   1.00 21.26  ? 88  PRO A CA  1 
ATOM   711  C C   . PRO A 1 89 ? 14.527  -14.463 -0.267  1.00 24.29  ? 88  PRO A C   1 
ATOM   712  O O   . PRO A 1 89 ? 13.732  -14.725 -1.158  1.00 22.41  ? 88  PRO A O   1 
ATOM   713  C CB  . PRO A 1 89 ? 13.242  -13.909 1.804   1.00 20.97  ? 88  PRO A CB  1 
ATOM   714  C CG  . PRO A 1 89 ? 14.146  -12.978 2.564   1.00 20.74  ? 88  PRO A CG  1 
ATOM   715  C CD  . PRO A 1 89 ? 15.169  -13.945 3.157   1.00 21.39  ? 88  PRO A CD  1 
ATOM   716  N N   . HIS A 1 90 ? 15.720  -13.870 -0.468  1.00 22.03  ? 89  HIS A N   1 
ATOM   717  C CA  . HIS A 1 90 ? 16.082  -13.394 -1.800  1.00 20.31  ? 89  HIS A CA  1 
ATOM   718  C C   . HIS A 1 90 ? 17.201  -14.184 -2.485  1.00 23.18  ? 89  HIS A C   1 
ATOM   719  O O   . HIS A 1 90 ? 17.660  -13.763 -3.562  1.00 25.29  ? 89  HIS A O   1 
ATOM   720  C CB  . HIS A 1 90 ? 16.465  -11.904 -1.707  1.00 22.43  ? 89  HIS A CB  1 
ATOM   721  C CG  . HIS A 1 90 ? 15.378  -11.048 -1.111  1.00 23.57  ? 89  HIS A CG  1 
ATOM   722  N ND1 . HIS A 1 90 ? 14.120  -10.932 -1.706  1.00 21.45  ? 89  HIS A ND1 1 
ATOM   723  C CD2 . HIS A 1 90 ? 15.349  -10.296 -0.001  1.00 26.13  ? 89  HIS A CD2 1 
ATOM   724  C CE1 . HIS A 1 90 ? 13.390  -10.065 -0.992  1.00 21.44  ? 89  HIS A CE1 1 
ATOM   725  N NE2 . HIS A 1 90 ? 14.102  -9.662  0.085   1.00 23.90  ? 89  HIS A NE2 1 
ATOM   726  N N   . ALA A 1 91 ? 17.483  -15.383 -1.957  1.00 23.68  ? 90  ALA A N   1 
ATOM   727  C CA  . ALA A 1 91 ? 18.556  -16.189 -2.548  1.00 23.89  ? 90  ALA A CA  1 
ATOM   728  C C   . ALA A 1 91 ? 18.076  -16.888 -3.822  1.00 28.34  ? 90  ALA A C   1 
ATOM   729  O O   . ALA A 1 91 ? 16.879  -17.042 -4.091  1.00 27.41  ? 90  ALA A O   1 
ATOM   730  C CB  . ALA A 1 91 ? 19.020  -17.196 -1.505  1.00 24.44  ? 90  ALA A CB  1 
ATOM   731  N N   . SER A 1 92 ? 19.057  -17.417 -4.571  1.00 27.60  ? 91  SER A N   1 
ATOM   732  C CA  . SER A 1 92 ? 18.767  -18.367 -5.638  1.00 30.62  ? 91  SER A CA  1 
ATOM   733  C C   . SER A 1 92 ? 18.522  -19.764 -5.063  1.00 32.91  ? 91  SER A C   1 
ATOM   734  O O   . SER A 1 92 ? 19.364  -20.299 -4.333  1.00 33.94  ? 91  SER A O   1 
ATOM   735  C CB  . SER A 1 92 ? 19.917  -18.392 -6.614  1.00 37.12  ? 91  SER A CB  1 
ATOM   736  O OG  . SER A 1 92 ? 19.732  -19.513 -7.465  1.00 37.64  ? 91  SER A OG  1 
ATOM   737  N N   . TYR A 1 93 ? 17.377  -20.356 -5.431  1.00 29.54  ? 92  TYR A N   1 
ATOM   738  C CA  . TYR A 1 93 ? 16.968  -21.675 -4.988  1.00 32.17  ? 92  TYR A CA  1 
ATOM   739  C C   . TYR A 1 93 ? 16.958  -22.579 -6.222  1.00 41.78  ? 92  TYR A C   1 
ATOM   740  O O   . TYR A 1 93 ? 16.471  -23.695 -6.159  1.00 44.60  ? 92  TYR A O   1 
ATOM   741  C CB  . TYR A 1 93 ? 15.640  -21.653 -4.205  1.00 31.49  ? 92  TYR A CB  1 
ATOM   742  C CG  . TYR A 1 93 ? 15.778  -21.040 -2.816  1.00 26.46  ? 92  TYR A CG  1 
ATOM   743  C CD1 . TYR A 1 93 ? 16.186  -21.808 -1.727  1.00 26.35  ? 92  TYR A CD1 1 
ATOM   744  C CD2 . TYR A 1 93 ? 15.469  -19.698 -2.576  1.00 27.06  ? 92  TYR A CD2 1 
ATOM   745  C CE1 . TYR A 1 93 ? 16.335  -21.248 -0.463  1.00 30.61  ? 92  TYR A CE1 1 
ATOM   746  C CE2 . TYR A 1 93 ? 15.638  -19.122 -1.329  1.00 28.71  ? 92  TYR A CE2 1 
ATOM   747  C CZ  . TYR A 1 93 ? 16.027  -19.909 -0.255  1.00 29.06  ? 92  TYR A CZ  1 
ATOM   748  O OH  . TYR A 1 93 ? 16.265  -19.454 1.007   1.00 27.63  ? 92  TYR A OH  1 
ATOM   749  N N   . SER A 1 94 ? 17.548  -22.085 -7.320  1.00 46.04  ? 93  SER A N   1 
ATOM   750  C CA  . SER A 1 94 ? 17.741  -22.834 -8.557  1.00 57.80  ? 93  SER A CA  1 
ATOM   751  C C   . SER A 1 94 ? 18.714  -24.011 -8.368  1.00 65.80  ? 93  SER A C   1 
ATOM   752  O O   . SER A 1 94 ? 19.340  -24.092 -7.287  1.00 65.62  ? 93  SER A O   1 
ATOM   753  C CB  . SER A 1 94 ? 18.236  -21.919 -9.646  1.00 57.75  ? 93  SER A CB  1 
ATOM   754  O OG  . SER A 1 94 ? 17.157  -21.127 -10.116 1.00 65.88  ? 93  SER A OG  1 
ATOM   755  O OXT . SER A 1 94 ? 18.831  -24.807 -9.331  1.00 75.50  ? 93  SER A OXT 1 
ATOM   756  N N   . MET B 1 2  ? 38.952  -10.791 -42.540 1.00 67.48  ? 1   MET B N   1 
ATOM   757  C CA  . MET B 1 2  ? 38.642  -11.813 -43.578 1.00 56.66  ? 1   MET B CA  1 
ATOM   758  C C   . MET B 1 2  ? 37.137  -12.096 -43.552 1.00 54.69  ? 1   MET B C   1 
ATOM   759  O O   . MET B 1 2  ? 36.611  -12.471 -42.501 1.00 65.17  ? 1   MET B O   1 
ATOM   760  C CB  . MET B 1 2  ? 39.479  -13.085 -43.358 1.00 61.64  ? 1   MET B CB  1 
ATOM   761  C CG  . MET B 1 2  ? 39.460  -14.104 -44.506 1.00 71.90  ? 1   MET B CG  1 
ATOM   762  S SD  . MET B 1 2  ? 40.231  -13.647 -46.081 1.00 73.11  ? 1   MET B SD  1 
ATOM   763  C CE  . MET B 1 2  ? 41.716  -12.798 -45.524 1.00 61.21  ? 1   MET B CE  1 
ATOM   764  N N   . PRO B 1 3  ? 36.391  -11.873 -44.674 1.00 50.53  ? 2   PRO B N   1 
ATOM   765  C CA  . PRO B 1 3  ? 34.956  -12.165 -44.731 1.00 47.82  ? 2   PRO B CA  1 
ATOM   766  C C   . PRO B 1 3  ? 34.659  -13.599 -44.311 1.00 47.85  ? 2   PRO B C   1 
ATOM   767  O O   . PRO B 1 3  ? 35.461  -14.486 -44.574 1.00 44.30  ? 2   PRO B O   1 
ATOM   768  C CB  . PRO B 1 3  ? 34.568  -11.917 -46.191 1.00 48.05  ? 2   PRO B CB  1 
ATOM   769  C CG  . PRO B 1 3  ? 35.602  -10.909 -46.685 1.00 42.57  ? 2   PRO B CG  1 
ATOM   770  C CD  . PRO B 1 3  ? 36.870  -11.253 -45.922 1.00 42.28  ? 2   PRO B CD  1 
ATOM   771  N N   . HIS B 1 4  ? 33.524  -13.786 -43.615 1.00 43.74  ? 3   HIS B N   1 
ATOM   772  C CA  . HIS B 1 4  ? 33.039  -15.109 -43.257 1.00 43.00  ? 3   HIS B CA  1 
ATOM   773  C C   . HIS B 1 4  ? 31.655  -15.306 -43.876 1.00 41.45  ? 3   HIS B C   1 
ATOM   774  O O   . HIS B 1 4  ? 31.086  -14.394 -44.475 1.00 41.98  ? 3   HIS B O   1 
ATOM   775  C CB  . HIS B 1 4  ? 33.100  -15.328 -41.741 1.00 48.99  ? 3   HIS B CB  1 
ATOM   776  C CG  . HIS B 1 4  ? 34.479  -15.280 -41.156 1.00 58.04  ? 3   HIS B CG  1 
ATOM   777  N ND1 . HIS B 1 4  ? 35.445  -16.235 -41.417 1.00 64.68  ? 3   HIS B ND1 1 
ATOM   778  C CD2 . HIS B 1 4  ? 35.053  -14.395 -40.324 1.00 54.41  ? 3   HIS B CD2 1 
ATOM   779  C CE1 . HIS B 1 4  ? 36.555  -15.929 -40.757 1.00 58.40  ? 3   HIS B CE1 1 
ATOM   780  N NE2 . HIS B 1 4  ? 36.339  -14.816 -40.087 1.00 61.85  ? 3   HIS B NE2 1 
ATOM   781  N N   . ALA B 1 5  ? 31.108  -16.516 -43.703 1.00 39.68  ? 4   ALA B N   1 
ATOM   782  C CA  . ALA B 1 5  ? 29.792  -16.880 -44.190 1.00 37.85  ? 4   ALA B CA  1 
ATOM   783  C C   . ALA B 1 5  ? 28.750  -15.850 -43.753 1.00 36.21  ? 4   ALA B C   1 
ATOM   784  O O   . ALA B 1 5  ? 27.872  -15.488 -44.531 1.00 38.86  ? 4   ALA B O   1 
ATOM   785  C CB  . ALA B 1 5  ? 29.462  -18.245 -43.636 1.00 37.49  ? 4   ALA B CB  1 
ATOM   786  N N   . PHE B 1 6  ? 28.830  -15.451 -42.483 1.00 41.84  ? 5   PHE B N   1 
ATOM   787  C CA  . PHE B 1 6  ? 27.973  -14.423 -41.919 1.00 39.26  ? 5   PHE B CA  1 
ATOM   788  C C   . PHE B 1 6  ? 28.814  -13.173 -41.657 1.00 39.01  ? 5   PHE B C   1 
ATOM   789  O O   . PHE B 1 6  ? 29.950  -13.276 -41.220 1.00 37.51  ? 5   PHE B O   1 
ATOM   790  C CB  . PHE B 1 6  ? 27.554  -14.920 -40.528 1.00 42.53  ? 5   PHE B CB  1 
ATOM   791  C CG  . PHE B 1 6  ? 26.520  -16.035 -40.548 1.00 34.50  ? 5   PHE B CG  1 
ATOM   792  C CD1 . PHE B 1 6  ? 25.172  -15.729 -40.718 1.00 31.66  ? 5   PHE B CD1 1 
ATOM   793  C CD2 . PHE B 1 6  ? 26.901  -17.369 -40.432 1.00 36.34  ? 5   PHE B CD2 1 
ATOM   794  C CE1 . PHE B 1 6  ? 24.203  -16.711 -40.787 1.00 37.05  ? 5   PHE B CE1 1 
ATOM   795  C CE2 . PHE B 1 6  ? 25.928  -18.359 -40.473 1.00 33.17  ? 5   PHE B CE2 1 
ATOM   796  C CZ  . PHE B 1 6  ? 24.591  -18.030 -40.633 1.00 32.60  ? 5   PHE B CZ  1 
ATOM   797  N N   . LYS B 1 7  ? 28.248  -11.996 -41.923 1.00 41.35  ? 6   LYS B N   1 
ATOM   798  C CA  . LYS B 1 7  ? 29.028  -10.784 -41.707 1.00 37.98  ? 6   LYS B CA  1 
ATOM   799  C C   . LYS B 1 7  ? 28.305  -9.954  -40.648 1.00 39.93  ? 6   LYS B C   1 
ATOM   800  O O   . LYS B 1 7  ? 27.081  -10.084 -40.501 1.00 36.00  ? 6   LYS B O   1 
ATOM   801  C CB  . LYS B 1 7  ? 29.117  -10.048 -43.052 1.00 42.78  ? 6   LYS B CB  1 
ATOM   802  C CG  . LYS B 1 7  ? 27.804  -9.699  -43.749 1.00 49.21  ? 6   LYS B CG  1 
ATOM   803  C CD  . LYS B 1 7  ? 27.928  -9.114  -45.158 1.00 49.14  ? 6   LYS B CD  1 
ATOM   804  C CE  . LYS B 1 7  ? 26.620  -8.681  -45.766 1.00 48.34  ? 6   LYS B CE  1 
ATOM   805  N NZ  . LYS B 1 7  ? 25.776  -9.827  -46.137 1.00 52.71  ? 6   LYS B NZ  1 
ATOM   806  N N   . PRO B 1 8  ? 29.000  -9.053  -39.918 1.00 43.33  ? 7   PRO B N   1 
ATOM   807  C CA  . PRO B 1 8  ? 28.333  -8.072  -39.051 1.00 35.81  ? 7   PRO B CA  1 
ATOM   808  C C   . PRO B 1 8  ? 27.158  -7.409  -39.744 1.00 33.38  ? 7   PRO B C   1 
ATOM   809  O O   . PRO B 1 8  ? 27.262  -6.959  -40.900 1.00 38.97  ? 7   PRO B O   1 
ATOM   810  C CB  . PRO B 1 8  ? 29.514  -7.122  -38.854 1.00 39.32  ? 7   PRO B CB  1 
ATOM   811  C CG  . PRO B 1 8  ? 30.653  -8.083  -38.631 1.00 44.90  ? 7   PRO B CG  1 
ATOM   812  C CD  . PRO B 1 8  ? 30.467  -8.916  -39.878 1.00 40.94  ? 7   PRO B CD  1 
ATOM   813  N N   . GLY B 1 9  ? 26.015  -7.371  -39.038 1.00 30.98  ? 8   GLY B N   1 
ATOM   814  C CA  . GLY B 1 9  ? 24.804  -6.751  -39.537 1.00 31.77  ? 8   GLY B CA  1 
ATOM   815  C C   . GLY B 1 9  ? 23.835  -7.737  -40.183 1.00 29.84  ? 8   GLY B C   1 
ATOM   816  O O   . GLY B 1 9  ? 22.699  -7.398  -40.460 1.00 31.24  ? 8   GLY B O   1 
ATOM   817  N N   . ASP B 1 10 ? 24.282  -8.985  -40.460 1.00 29.58  ? 9   ASP B N   1 
ATOM   818  C CA  . ASP B 1 10 ? 23.338  -9.937  -41.016 1.00 29.47  ? 9   ASP B CA  1 
ATOM   819  C C   . ASP B 1 10 ? 22.260  -10.267 -39.960 1.00 24.87  ? 9   ASP B C   1 
ATOM   820  O O   . ASP B 1 10 ? 22.562  -10.338 -38.774 1.00 30.49  ? 9   ASP B O   1 
ATOM   821  C CB  . ASP B 1 10 ? 24.021  -11.254 -41.371 1.00 29.30  ? 9   ASP B CB  1 
ATOM   822  C CG  . ASP B 1 10 ? 24.867  -11.302 -42.642 1.00 37.98  ? 9   ASP B CG  1 
ATOM   823  O OD1 . ASP B 1 10 ? 24.630  -10.455 -43.524 1.00 41.34  ? 9   ASP B OD1 1 
ATOM   824  O OD2 . ASP B 1 10 ? 25.718  -12.235 -42.746 1.00 39.81  ? 9   ASP B OD2 1 
ATOM   825  N N   . LEU B 1 11 ? 21.045  -10.422 -40.430 1.00 26.93  ? 10  LEU B N   1 
ATOM   826  C CA  . LEU B 1 11 ? 19.897  -10.672 -39.550 1.00 26.68  ? 10  LEU B CA  1 
ATOM   827  C C   . LEU B 1 11 ? 19.605  -12.172 -39.572 1.00 28.12  ? 10  LEU B C   1 
ATOM   828  O O   . LEU B 1 11 ? 19.664  -12.796 -40.645 1.00 27.93  ? 10  LEU B O   1 
ATOM   829  C CB  . LEU B 1 11 ? 18.719  -9.836  -40.040 1.00 28.57  ? 10  LEU B CB  1 
ATOM   830  C CG  . LEU B 1 11 ? 19.008  -8.330  -40.081 1.00 28.21  ? 10  LEU B CG  1 
ATOM   831  C CD1 . LEU B 1 11 ? 17.760  -7.626  -40.510 1.00 29.42  ? 10  LEU B CD1 1 
ATOM   832  C CD2 . LEU B 1 11 ? 19.566  -7.864  -38.739 1.00 28.69  ? 10  LEU B CD2 1 
ATOM   833  N N   . VAL B 1 12 ? 19.265  -12.717 -38.375 1.00 26.45  ? 11  VAL B N   1 
ATOM   834  C CA  . VAL B 1 12 ? 19.096  -14.166 -38.248 1.00 23.81  ? 11  VAL B CA  1 
ATOM   835  C C   . VAL B 1 12 ? 17.998  -14.457 -37.219 1.00 28.50  ? 11  VAL B C   1 
ATOM   836  O O   . VAL B 1 12 ? 17.600  -13.588 -36.446 1.00 26.43  ? 11  VAL B O   1 
ATOM   837  C CB  . VAL B 1 12 ? 20.383  -14.876 -37.782 1.00 25.52  ? 11  VAL B CB  1 
ATOM   838  C CG1 . VAL B 1 12 ? 21.520  -14.782 -38.812 1.00 26.85  ? 11  VAL B CG1 1 
ATOM   839  C CG2 . VAL B 1 12 ? 20.855  -14.476 -36.365 1.00 25.87  ? 11  VAL B CG2 1 
ATOM   840  N N   . PHE B 1 13 ? 17.553  -15.718 -37.163 1.00 25.64  ? 12  PHE B N   1 
ATOM   841  C CA  . PHE B 1 13 ? 17.017  -16.275 -35.918 1.00 25.33  ? 12  PHE B CA  1 
ATOM   842  C C   . PHE B 1 13 ? 18.111  -17.130 -35.292 1.00 24.58  ? 12  PHE B C   1 
ATOM   843  O O   . PHE B 1 13 ? 18.751  -17.920 -36.004 1.00 26.38  ? 12  PHE B O   1 
ATOM   844  C CB  . PHE B 1 13 ? 15.802  -17.160 -36.201 1.00 25.10  ? 12  PHE B CB  1 
ATOM   845  C CG  . PHE B 1 13 ? 14.583  -16.333 -36.580 1.00 26.47  ? 12  PHE B CG  1 
ATOM   846  C CD1 . PHE B 1 13 ? 14.341  -15.977 -37.917 1.00 29.06  ? 12  PHE B CD1 1 
ATOM   847  C CD2 . PHE B 1 13 ? 13.700  -15.907 -35.600 1.00 29.14  ? 12  PHE B CD2 1 
ATOM   848  C CE1 . PHE B 1 13 ? 13.259  -15.178 -38.245 1.00 31.13  ? 12  PHE B CE1 1 
ATOM   849  C CE2 . PHE B 1 13 ? 12.599  -15.116 -35.931 1.00 28.61  ? 12  PHE B CE2 1 
ATOM   850  C CZ  . PHE B 1 13 ? 12.370  -14.772 -37.258 1.00 30.31  ? 12  PHE B CZ  1 
ATOM   851  N N   . ALA B 1 14 ? 18.343  -16.961 -33.973 1.00 22.86  ? 13  ALA B N   1 
ATOM   852  C CA  . ALA B 1 14 ? 19.404  -17.654 -33.283 1.00 24.26  ? 13  ALA B CA  1 
ATOM   853  C C   . ALA B 1 14 ? 18.789  -18.614 -32.266 1.00 27.03  ? 13  ALA B C   1 
ATOM   854  O O   . ALA B 1 14 ? 17.858  -18.222 -31.555 1.00 25.71  ? 13  ALA B O   1 
ATOM   855  C CB  . ALA B 1 14 ? 20.319  -16.667 -32.575 1.00 26.46  ? 13  ALA B CB  1 
ATOM   856  N N   . LYS B 1 15 ? 19.322  -19.852 -32.218 1.00 24.35  ? 14  LYS B N   1 
ATOM   857  C CA  . LYS B 1 15 ? 18.731  -20.871 -31.344 1.00 27.34  ? 14  LYS B CA  1 
ATOM   858  C C   . LYS B 1 15 ? 19.648  -21.160 -30.158 1.00 27.75  ? 14  LYS B C   1 
ATOM   859  O O   . LYS B 1 15 ? 20.834  -21.488 -30.302 1.00 30.83  ? 14  LYS B O   1 
ATOM   860  C CB  . LYS B 1 15 ? 18.438  -22.103 -32.219 1.00 27.93  ? 14  LYS B CB  1 
ATOM   861  C CG  . LYS B 1 15 ? 17.820  -23.277 -31.393 1.00 30.16  ? 14  LYS B CG  1 
ATOM   862  C CD  . LYS B 1 15 ? 16.368  -22.905 -31.080 1.00 30.51  ? 14  LYS B CD  1 
ATOM   863  C CE  . LYS B 1 15 ? 15.550  -24.050 -30.443 1.00 39.19  ? 14  LYS B CE  1 
ATOM   864  N NZ  . LYS B 1 15 ? 16.062  -24.310 -29.101 1.00 32.26  ? 14  LYS B NZ  1 
ATOM   865  N N   . MET B 1 16 ? 19.074  -20.988 -28.956 1.00 28.54  ? 15  MET B N   1 
ATOM   866  C CA  . MET B 1 16 ? 19.703  -21.348 -27.689 1.00 31.58  ? 15  MET B CA  1 
ATOM   867  C C   . MET B 1 16 ? 18.849  -22.441 -27.038 1.00 30.79  ? 15  MET B C   1 
ATOM   868  O O   . MET B 1 16 ? 17.635  -22.407 -27.127 1.00 30.46  ? 15  MET B O   1 
ATOM   869  C CB  . MET B 1 16 ? 19.714  -20.143 -26.729 1.00 32.85  ? 15  MET B CB  1 
ATOM   870  C CG  . MET B 1 16 ? 20.424  -18.925 -27.250 1.00 44.73  ? 15  MET B CG  1 
ATOM   871  S SD  . MET B 1 16 ? 22.177  -18.920 -26.828 1.00 53.80  ? 15  MET B SD  1 
ATOM   872  C CE  . MET B 1 16 ? 21.959  -18.524 -25.083 1.00 55.64  ? 15  MET B CE  1 
ATOM   873  N N   . LYS B 1 17 ? 19.483  -23.371 -26.314 1.00 32.99  ? 16  LYS B N   1 
ATOM   874  C CA  . LYS B 1 17 ? 18.705  -24.456 -25.727 1.00 34.37  ? 16  LYS B CA  1 
ATOM   875  C C   . LYS B 1 17 ? 17.755  -23.863 -24.677 1.00 30.58  ? 16  LYS B C   1 
ATOM   876  O O   . LYS B 1 17 ? 18.155  -23.011 -23.898 1.00 35.66  ? 16  LYS B O   1 
ATOM   877  C CB  . LYS B 1 17 ? 19.736  -25.387 -25.078 1.00 37.00  ? 16  LYS B CB  1 
ATOM   878  C CG  . LYS B 1 17 ? 19.131  -26.564 -24.290 1.00 48.60  ? 16  LYS B CG  1 
ATOM   879  C CD  . LYS B 1 17 ? 20.116  -27.295 -23.388 1.00 53.16  ? 16  LYS B CD  1 
ATOM   880  N N   . GLY B 1 18 ? 16.496  -24.298 -24.703 1.00 35.95  ? 17  GLY B N   1 
ATOM   881  C CA  . GLY B 1 18 ? 15.477  -23.845 -23.768 1.00 37.10  ? 17  GLY B CA  1 
ATOM   882  C C   . GLY B 1 18 ? 14.657  -22.673 -24.297 1.00 37.94  ? 17  GLY B C   1 
ATOM   883  O O   . GLY B 1 18 ? 13.771  -22.186 -23.603 1.00 32.52  ? 17  GLY B O   1 
ATOM   884  N N   . TYR B 1 19 ? 15.003  -22.161 -25.494 1.00 32.23  ? 18  TYR B N   1 
ATOM   885  C CA  . TYR B 1 19 ? 14.355  -20.945 -25.975 1.00 29.91  ? 18  TYR B CA  1 
ATOM   886  C C   . TYR B 1 19 ? 13.921  -21.184 -27.419 1.00 27.91  ? 18  TYR B C   1 
ATOM   887  O O   . TYR B 1 19 ? 14.615  -21.911 -28.137 1.00 28.94  ? 18  TYR B O   1 
ATOM   888  C CB  . TYR B 1 19 ? 15.311  -19.734 -25.988 1.00 29.45  ? 18  TYR B CB  1 
ATOM   889  C CG  . TYR B 1 19 ? 15.876  -19.336 -24.631 1.00 28.76  ? 18  TYR B CG  1 
ATOM   890  C CD1 . TYR B 1 19 ? 15.184  -18.481 -23.770 1.00 28.88  ? 18  TYR B CD1 1 
ATOM   891  C CD2 . TYR B 1 19 ? 17.036  -19.953 -24.160 1.00 29.31  ? 18  TYR B CD2 1 
ATOM   892  C CE1 . TYR B 1 19 ? 15.672  -18.204 -22.495 1.00 30.38  ? 18  TYR B CE1 1 
ATOM   893  C CE2 . TYR B 1 19 ? 17.532  -19.680 -22.887 1.00 35.73  ? 18  TYR B CE2 1 
ATOM   894  C CZ  . TYR B 1 19 ? 16.836  -18.819 -22.051 1.00 34.34  ? 18  TYR B CZ  1 
ATOM   895  O OH  . TYR B 1 19 ? 17.400  -18.555 -20.829 1.00 35.61  ? 18  TYR B OH  1 
ATOM   896  N N   . PRO B 1 20 ? 12.857  -20.544 -27.944 1.00 29.59  ? 19  PRO B N   1 
ATOM   897  C CA  . PRO B 1 20 ? 12.530  -20.655 -29.368 1.00 30.11  ? 19  PRO B CA  1 
ATOM   898  C C   . PRO B 1 20 ? 13.549  -19.900 -30.221 1.00 29.27  ? 19  PRO B C   1 
ATOM   899  O O   . PRO B 1 20 ? 14.240  -19.028 -29.708 1.00 28.23  ? 19  PRO B O   1 
ATOM   900  C CB  . PRO B 1 20 ? 11.154  -20.027 -29.481 1.00 29.39  ? 19  PRO B CB  1 
ATOM   901  C CG  . PRO B 1 20 ? 11.127  -19.002 -28.355 1.00 31.78  ? 19  PRO B CG  1 
ATOM   902  C CD  . PRO B 1 20 ? 11.922  -19.661 -27.234 1.00 30.98  ? 19  PRO B CD  1 
ATOM   903  N N   . HIS B 1 21 ? 13.652  -20.286 -31.491 1.00 27.96  ? 20  HIS B N   1 
ATOM   904  C CA  . HIS B 1 21 ? 14.486  -19.523 -32.435 1.00 25.44  ? 20  HIS B CA  1 
ATOM   905  C C   . HIS B 1 21 ? 14.207  -18.018 -32.284 1.00 23.43  ? 20  HIS B C   1 
ATOM   906  O O   . HIS B 1 21 ? 13.060  -17.595 -32.411 1.00 26.20  ? 20  HIS B O   1 
ATOM   907  C CB  . HIS B 1 21 ? 14.139  -19.981 -33.855 1.00 25.27  ? 20  HIS B CB  1 
ATOM   908  C CG  . HIS B 1 21 ? 14.411  -21.455 -34.067 1.00 25.91  ? 20  HIS B CG  1 
ATOM   909  N ND1 . HIS B 1 21 ? 13.565  -22.468 -33.627 1.00 29.92  ? 20  HIS B ND1 1 
ATOM   910  C CD2 . HIS B 1 21 ? 15.481  -22.080 -34.624 1.00 30.56  ? 20  HIS B CD2 1 
ATOM   911  C CE1 . HIS B 1 21 ? 14.103  -23.654 -33.906 1.00 30.48  ? 20  HIS B CE1 1 
ATOM   912  N NE2 . HIS B 1 21 ? 15.248  -23.470 -34.541 1.00 29.72  ? 20  HIS B NE2 1 
ATOM   913  N N   . TRP B 1 22 ? 15.267  -17.208 -32.119 1.00 24.69  ? 21  TRP B N   1 
ATOM   914  C CA  . TRP B 1 22 ? 15.031  -15.875 -31.562 1.00 23.24  ? 21  TRP B CA  1 
ATOM   915  C C   . TRP B 1 22 ? 15.549  -14.818 -32.541 1.00 25.80  ? 21  TRP B C   1 
ATOM   916  O O   . TRP B 1 22 ? 16.715  -14.962 -32.972 1.00 25.65  ? 21  TRP B O   1 
ATOM   917  C CB  . TRP B 1 22 ? 15.838  -15.749 -30.257 1.00 25.77  ? 21  TRP B CB  1 
ATOM   918  C CG  . TRP B 1 22 ? 15.305  -14.624 -29.404 1.00 24.42  ? 21  TRP B CG  1 
ATOM   919  C CD1 . TRP B 1 22 ? 15.578  -13.284 -29.507 1.00 24.94  ? 21  TRP B CD1 1 
ATOM   920  C CD2 . TRP B 1 22 ? 14.352  -14.746 -28.312 1.00 25.12  ? 21  TRP B CD2 1 
ATOM   921  N NE1 . TRP B 1 22 ? 14.869  -12.574 -28.542 1.00 27.47  ? 21  TRP B NE1 1 
ATOM   922  C CE2 . TRP B 1 22 ? 14.103  -13.445 -27.811 1.00 24.92  ? 21  TRP B CE2 1 
ATOM   923  C CE3 . TRP B 1 22 ? 13.667  -15.845 -27.745 1.00 28.97  ? 21  TRP B CE3 1 
ATOM   924  C CZ2 . TRP B 1 22 ? 13.202  -13.204 -26.761 1.00 27.55  ? 21  TRP B CZ2 1 
ATOM   925  C CZ3 . TRP B 1 22 ? 12.805  -15.602 -26.692 1.00 28.87  ? 21  TRP B CZ3 1 
ATOM   926  C CH2 . TRP B 1 22 ? 12.538  -14.302 -26.239 1.00 28.83  ? 21  TRP B CH2 1 
ATOM   927  N N   . PRO B 1 23 ? 14.795  -13.723 -32.821 1.00 24.79  ? 22  PRO B N   1 
ATOM   928  C CA  . PRO B 1 23 ? 15.275  -12.682 -33.753 1.00 23.46  ? 22  PRO B CA  1 
ATOM   929  C C   . PRO B 1 23 ? 16.565  -12.044 -33.238 1.00 23.55  ? 22  PRO B C   1 
ATOM   930  O O   . PRO B 1 23 ? 16.696  -11.683 -32.046 1.00 23.69  ? 22  PRO B O   1 
ATOM   931  C CB  . PRO B 1 23 ? 14.122  -11.658 -33.833 1.00 23.14  ? 22  PRO B CB  1 
ATOM   932  C CG  . PRO B 1 23 ? 13.426  -11.843 -32.465 1.00 24.69  ? 22  PRO B CG  1 
ATOM   933  C CD  . PRO B 1 23 ? 13.463  -13.396 -32.279 1.00 26.17  ? 22  PRO B CD  1 
ATOM   934  N N   . ALA B 1 24 ? 17.588  -11.930 -34.107 1.00 22.99  ? 23  ALA B N   1 
ATOM   935  C CA  . ALA B 1 24 ? 18.906  -11.560 -33.619 1.00 22.67  ? 23  ALA B CA  1 
ATOM   936  C C   . ALA B 1 24 ? 19.742  -11.023 -34.788 1.00 24.16  ? 23  ALA B C   1 
ATOM   937  O O   . ALA B 1 24 ? 19.268  -11.032 -35.917 1.00 25.32  ? 23  ALA B O   1 
ATOM   938  C CB  . ALA B 1 24 ? 19.646  -12.745 -32.929 1.00 26.26  ? 23  ALA B CB  1 
ATOM   939  N N   . ARG B 1 25 ? 20.934  -10.517 -34.450 1.00 26.33  ? 24  ARG B N   1 
ATOM   940  C CA  . ARG B 1 25 ? 21.848  -10.040 -35.493 1.00 25.40  ? 24  ARG B CA  1 
ATOM   941  C C   . ARG B 1 25 ? 23.252  -10.500 -35.147 1.00 25.78  ? 24  ARG B C   1 
ATOM   942  O O   . ARG B 1 25 ? 23.605  -10.775 -33.993 1.00 26.70  ? 24  ARG B O   1 
ATOM   943  C CB  . ARG B 1 25 ? 21.828  -8.518  -35.679 1.00 25.46  ? 24  ARG B CB  1 
ATOM   944  C CG  . ARG B 1 25 ? 22.391  -7.777  -34.477 1.00 27.52  ? 24  ARG B CG  1 
ATOM   945  C CD  . ARG B 1 25 ? 22.174  -6.235  -34.604 1.00 25.11  ? 24  ARG B CD  1 
ATOM   946  N NE  . ARG B 1 25 ? 22.818  -5.581  -33.473 1.00 27.60  ? 24  ARG B NE  1 
ATOM   947  C CZ  . ARG B 1 25 ? 22.520  -4.322  -33.012 1.00 28.27  ? 24  ARG B CZ  1 
ATOM   948  N NH1 . ARG B 1 25 ? 21.613  -3.613  -33.627 1.00 30.90  ? 24  ARG B NH1 1 
ATOM   949  N NH2 . ARG B 1 25 ? 23.196  -3.802  -32.017 1.00 30.03  ? 24  ARG B NH2 1 
ATOM   950  N N   . ILE B 1 26 ? 24.102  -10.555 -36.192 1.00 25.76  ? 25  ILE B N   1 
ATOM   951  C CA  . ILE B 1 26 ? 25.524  -10.760 -36.001 1.00 28.54  ? 25  ILE B CA  1 
ATOM   952  C C   . ILE B 1 26 ? 26.128  -9.398  -35.672 1.00 30.30  ? 25  ILE B C   1 
ATOM   953  O O   . ILE B 1 26 ? 25.881  -8.436  -36.405 1.00 34.44  ? 25  ILE B O   1 
ATOM   954  C CB  . ILE B 1 26 ? 26.153  -11.240 -37.315 1.00 29.21  ? 25  ILE B CB  1 
ATOM   955  C CG1 . ILE B 1 26 ? 25.519  -12.516 -37.887 1.00 32.22  ? 25  ILE B CG1 1 
ATOM   956  C CG2 . ILE B 1 26 ? 27.670  -11.368 -37.165 1.00 35.35  ? 25  ILE B CG2 1 
ATOM   957  C CD1 . ILE B 1 26 ? 25.520  -13.715 -36.948 1.00 35.02  ? 25  ILE B CD1 1 
ATOM   958  N N   . ASP B 1 27 ? 26.851  -9.345  -34.560 1.00 30.32  ? 26  ASP B N   1 
ATOM   959  C CA  . ASP B 1 27 ? 27.513  -8.114  -34.134 1.00 37.28  ? 26  ASP B CA  1 
ATOM   960  C C   . ASP B 1 27 ? 28.950  -8.049  -34.646 1.00 41.27  ? 26  ASP B C   1 
ATOM   961  O O   . ASP B 1 27 ? 29.487  -9.052  -35.113 1.00 43.04  ? 26  ASP B O   1 
ATOM   962  C CB  . ASP B 1 27 ? 27.515  -8.004  -32.624 1.00 36.05  ? 26  ASP B CB  1 
ATOM   963  C CG  . ASP B 1 27 ? 26.341  -7.254  -32.016 1.00 33.41  ? 26  ASP B CG  1 
ATOM   964  O OD1 . ASP B 1 27 ? 25.543  -6.680  -32.803 1.00 39.98  ? 26  ASP B OD1 1 
ATOM   965  O OD2 . ASP B 1 27 ? 26.273  -7.208  -30.745 1.00 34.99  ? 26  ASP B OD2 1 
ATOM   966  N N   A ASP B 1 28 ? 29.516  -6.833  -34.570 0.50 50.07  ? 27  ASP B N   1 
ATOM   967  N N   B ASP B 1 28 ? 29.551  -6.851  -34.577 0.50 51.92  ? 27  ASP B N   1 
ATOM   968  C CA  A ASP B 1 28 ? 30.929  -6.540  -34.741 0.50 55.72  ? 27  ASP B CA  1 
ATOM   969  C CA  B ASP B 1 28 ? 30.968  -6.674  -34.853 0.50 59.38  ? 27  ASP B CA  1 
ATOM   970  C C   A ASP B 1 28 ? 31.699  -7.021  -33.511 0.50 57.48  ? 27  ASP B C   1 
ATOM   971  C C   B ASP B 1 28 ? 31.721  -6.616  -33.526 0.50 63.31  ? 27  ASP B C   1 
ATOM   972  O O   A ASP B 1 28 ? 31.108  -7.495  -32.544 0.50 56.82  ? 27  ASP B O   1 
ATOM   973  O O   B ASP B 1 28 ? 31.124  -6.319  -32.492 0.50 69.06  ? 27  ASP B O   1 
ATOM   974  C CB  A ASP B 1 28 ? 31.149  -5.041  -34.912 0.50 49.34  ? 27  ASP B CB  1 
ATOM   975  C CB  B ASP B 1 28 ? 31.220  -5.456  -35.730 0.50 57.57  ? 27  ASP B CB  1 
ATOM   976  C CG  A ASP B 1 28 ? 30.442  -4.385  -36.093 0.50 50.07  ? 27  ASP B CG  1 
ATOM   977  C CG  B ASP B 1 28 ? 32.343  -5.623  -36.745 0.50 51.69  ? 27  ASP B CG  1 
ATOM   978  O OD1 A ASP B 1 28 ? 30.842  -4.653  -37.248 0.50 53.26  ? 27  ASP B OD1 1 
ATOM   979  O OD1 B ASP B 1 28 ? 33.068  -6.636  -36.649 0.50 48.50  ? 27  ASP B OD1 1 
ATOM   980  O OD2 A ASP B 1 28 ? 29.503  -3.605  -35.853 0.50 44.27  ? 27  ASP B OD2 1 
ATOM   981  O OD2 B ASP B 1 28 ? 32.456  -4.763  -37.645 0.50 48.37  ? 27  ASP B OD2 1 
ATOM   982  N N   . ILE B 1 29 ? 33.029  -6.908  -33.572 1.00 64.17  ? 28  ILE B N   1 
ATOM   983  C CA  . ILE B 1 29 ? 33.876  -6.912  -32.389 1.00 71.22  ? 28  ILE B CA  1 
ATOM   984  C C   . ILE B 1 29 ? 34.684  -5.600  -32.392 1.00 71.16  ? 28  ILE B C   1 
ATOM   985  O O   . ILE B 1 29 ? 35.143  -5.206  -31.303 1.00 85.25  ? 28  ILE B O   1 
ATOM   986  C CB  . ILE B 1 29 ? 34.788  -8.154  -32.345 1.00 68.57  ? 28  ILE B CB  1 
ATOM   987  N N   . VAL B 1 34 ? 37.102  -9.601  -25.467 1.00 76.57  ? 33  VAL B N   1 
ATOM   988  C CA  . VAL B 1 34 ? 36.992  -11.075 -25.705 1.00 82.67  ? 33  VAL B CA  1 
ATOM   989  C C   . VAL B 1 34 ? 36.723  -11.292 -27.190 1.00 85.79  ? 33  VAL B C   1 
ATOM   990  O O   . VAL B 1 34 ? 36.031  -10.491 -27.819 1.00 93.92  ? 33  VAL B O   1 
ATOM   991  C CB  . VAL B 1 34 ? 35.917  -11.761 -24.832 1.00 80.64  ? 33  VAL B CB  1 
ATOM   992  C CG1 . VAL B 1 34 ? 34.515  -11.202 -25.072 1.00 77.47  ? 33  VAL B CG1 1 
ATOM   993  C CG2 . VAL B 1 34 ? 35.929  -13.282 -24.983 1.00 70.81  ? 33  VAL B CG2 1 
ATOM   994  N N   . LYS B 1 35 ? 37.296  -12.370 -27.740 1.00 77.53  ? 34  LYS B N   1 
ATOM   995  C CA  . LYS B 1 35 ? 36.956  -12.821 -29.081 1.00 66.30  ? 34  LYS B CA  1 
ATOM   996  C C   . LYS B 1 35 ? 36.065  -14.062 -28.973 1.00 63.40  ? 34  LYS B C   1 
ATOM   997  O O   . LYS B 1 35 ? 36.111  -14.772 -27.962 1.00 58.61  ? 34  LYS B O   1 
ATOM   998  C CB  . LYS B 1 35 ? 38.243  -12.984 -29.900 1.00 62.12  ? 34  LYS B CB  1 
ATOM   999  N N   . PRO B 1 36 ? 35.197  -14.358 -29.978 1.00 53.18  ? 35  PRO B N   1 
ATOM   1000 C CA  . PRO B 1 36 ? 34.409  -15.598 -29.952 1.00 52.66  ? 35  PRO B CA  1 
ATOM   1001 C C   . PRO B 1 36 ? 35.344  -16.795 -29.809 1.00 50.40  ? 35  PRO B C   1 
ATOM   1002 O O   . PRO B 1 36 ? 36.505  -16.697 -30.186 1.00 51.26  ? 35  PRO B O   1 
ATOM   1003 C CB  . PRO B 1 36 ? 33.647  -15.620 -31.292 1.00 52.84  ? 35  PRO B CB  1 
ATOM   1004 C CG  . PRO B 1 36 ? 33.754  -14.199 -31.849 1.00 51.43  ? 35  PRO B CG  1 
ATOM   1005 C CD  . PRO B 1 36 ? 34.911  -13.503 -31.142 1.00 48.70  ? 35  PRO B CD  1 
ATOM   1006 N N   . PRO B 1 37 ? 34.912  -17.938 -29.226 1.00 47.64  ? 36  PRO B N   1 
ATOM   1007 C CA  . PRO B 1 37 ? 35.663  -19.181 -29.380 1.00 45.98  ? 36  PRO B CA  1 
ATOM   1008 C C   . PRO B 1 37 ? 35.691  -19.449 -30.877 1.00 54.66  ? 36  PRO B C   1 
ATOM   1009 O O   . PRO B 1 37 ? 34.851  -18.921 -31.609 1.00 50.42  ? 36  PRO B O   1 
ATOM   1010 C CB  . PRO B 1 37 ? 34.836  -20.250 -28.643 1.00 51.31  ? 36  PRO B CB  1 
ATOM   1011 C CG  . PRO B 1 37 ? 33.838  -19.488 -27.786 1.00 45.04  ? 36  PRO B CG  1 
ATOM   1012 C CD  . PRO B 1 37 ? 33.753  -18.076 -28.333 1.00 46.33  ? 36  PRO B CD  1 
ATOM   1013 N N   . PRO B 1 38 ? 36.636  -20.283 -31.376 1.00 54.47  ? 37  PRO B N   1 
ATOM   1014 C CA  . PRO B 1 38 ? 36.746  -20.530 -32.819 1.00 55.72  ? 37  PRO B CA  1 
ATOM   1015 C C   . PRO B 1 38 ? 35.402  -21.006 -33.390 1.00 44.83  ? 37  PRO B C   1 
ATOM   1016 O O   . PRO B 1 38 ? 34.685  -21.764 -32.730 1.00 48.17  ? 37  PRO B O   1 
ATOM   1017 C CB  . PRO B 1 38 ? 37.845  -21.630 -32.895 1.00 57.28  ? 37  PRO B CB  1 
ATOM   1018 C CG  . PRO B 1 38 ? 38.638  -21.471 -31.608 1.00 57.91  ? 37  PRO B CG  1 
ATOM   1019 C CD  . PRO B 1 38 ? 37.604  -21.054 -30.574 1.00 59.73  ? 37  PRO B CD  1 
ATOM   1020 N N   . ASN B 1 39 ? 35.060  -20.525 -34.594 1.00 46.06  ? 38  ASN B N   1 
ATOM   1021 C CA  . ASN B 1 39 ? 33.900  -21.013 -35.337 1.00 47.56  ? 38  ASN B CA  1 
ATOM   1022 C C   . ASN B 1 39 ? 32.593  -20.320 -34.918 1.00 43.09  ? 38  ASN B C   1 
ATOM   1023 O O   . ASN B 1 39 ? 31.548  -20.602 -35.475 1.00 37.85  ? 38  ASN B O   1 
ATOM   1024 C CB  . ASN B 1 39 ? 33.753  -22.527 -35.198 1.00 53.93  ? 38  ASN B CB  1 
ATOM   1025 C CG  . ASN B 1 39 ? 34.892  -23.245 -35.884 1.00 67.07  ? 38  ASN B CG  1 
ATOM   1026 O OD1 . ASN B 1 39 ? 35.409  -24.245 -35.366 1.00 72.82  ? 38  ASN B OD1 1 
ATOM   1027 N ND2 . ASN B 1 39 ? 35.279  -22.751 -37.055 1.00 59.91  ? 38  ASN B ND2 1 
ATOM   1028 N N   . LYS B 1 40 ? 32.650  -19.391 -33.957 1.00 41.36  ? 39  LYS B N   1 
ATOM   1029 C CA  . LYS B 1 40 ? 31.436  -18.817 -33.397 1.00 35.76  ? 39  LYS B CA  1 
ATOM   1030 C C   . LYS B 1 40 ? 31.376  -17.324 -33.682 1.00 36.13  ? 39  LYS B C   1 
ATOM   1031 O O   . LYS B 1 40 ? 32.378  -16.707 -34.039 1.00 43.04  ? 39  LYS B O   1 
ATOM   1032 C CB  . LYS B 1 40 ? 31.326  -19.128 -31.908 1.00 37.40  ? 39  LYS B CB  1 
ATOM   1033 C CG  . LYS B 1 40 ? 31.425  -20.643 -31.696 1.00 40.46  ? 39  LYS B CG  1 
ATOM   1034 C CD  . LYS B 1 40 ? 31.342  -21.210 -30.285 1.00 51.94  ? 39  LYS B CD  1 
ATOM   1035 C CE  . LYS B 1 40 ? 30.038  -21.875 -29.999 1.00 62.62  ? 39  LYS B CE  1 
ATOM   1036 N NZ  . LYS B 1 40 ? 30.096  -22.688 -28.776 1.00 55.76  ? 39  LYS B NZ  1 
ATOM   1037 N N   . TYR B 1 41 ? 30.159  -16.765 -33.602 1.00 32.83  ? 40  TYR B N   1 
ATOM   1038 C CA  . TYR B 1 41 ? 29.930  -15.371 -33.945 1.00 28.02  ? 40  TYR B CA  1 
ATOM   1039 C C   . TYR B 1 41 ? 29.375  -14.653 -32.714 1.00 31.63  ? 40  TYR B C   1 
ATOM   1040 O O   . TYR B 1 41 ? 28.655  -15.263 -31.899 1.00 27.82  ? 40  TYR B O   1 
ATOM   1041 C CB  . TYR B 1 41 ? 28.921  -15.230 -35.088 1.00 27.63  ? 40  TYR B CB  1 
ATOM   1042 C CG  . TYR B 1 41 ? 29.392  -15.725 -36.448 1.00 30.08  ? 40  TYR B CG  1 
ATOM   1043 C CD1 . TYR B 1 41 ? 29.908  -14.856 -37.396 1.00 33.62  ? 40  TYR B CD1 1 
ATOM   1044 C CD2 . TYR B 1 41 ? 29.251  -17.055 -36.789 1.00 30.93  ? 40  TYR B CD2 1 
ATOM   1045 C CE1 . TYR B 1 41 ? 30.339  -15.312 -38.636 1.00 39.47  ? 40  TYR B CE1 1 
ATOM   1046 C CE2 . TYR B 1 41 ? 29.702  -17.535 -38.003 1.00 33.81  ? 40  TYR B CE2 1 
ATOM   1047 C CZ  . TYR B 1 41 ? 30.229  -16.657 -38.945 1.00 38.10  ? 40  TYR B CZ  1 
ATOM   1048 O OH  . TYR B 1 41 ? 30.595  -17.119 -40.189 1.00 36.30  ? 40  TYR B OH  1 
ATOM   1049 N N   . PRO B 1 42 ? 29.609  -13.326 -32.540 1.00 34.34  ? 41  PRO B N   1 
ATOM   1050 C CA  . PRO B 1 42 ? 28.901  -12.611 -31.483 1.00 30.59  ? 41  PRO B CA  1 
ATOM   1051 C C   . PRO B 1 42 ? 27.484  -12.318 -31.959 1.00 31.39  ? 41  PRO B C   1 
ATOM   1052 O O   . PRO B 1 42 ? 27.279  -11.695 -33.008 1.00 30.32  ? 41  PRO B O   1 
ATOM   1053 C CB  . PRO B 1 42 ? 29.722  -11.313 -31.285 1.00 31.53  ? 41  PRO B CB  1 
ATOM   1054 C CG  . PRO B 1 42 ? 30.370  -11.074 -32.636 1.00 31.76  ? 41  PRO B CG  1 
ATOM   1055 C CD  . PRO B 1 42 ? 30.547  -12.457 -33.294 1.00 30.99  ? 41  PRO B CD  1 
ATOM   1056 N N   . ILE B 1 43 ? 26.502  -12.791 -31.166 1.00 30.87  ? 42  ILE B N   1 
ATOM   1057 C CA  . ILE B 1 43 ? 25.084  -12.586 -31.428 1.00 27.23  ? 42  ILE B CA  1 
ATOM   1058 C C   . ILE B 1 43 ? 24.531  -11.564 -30.433 1.00 27.34  ? 42  ILE B C   1 
ATOM   1059 O O   . ILE B 1 43 ? 24.892  -11.605 -29.280 1.00 31.29  ? 42  ILE B O   1 
ATOM   1060 C CB  . ILE B 1 43 ? 24.367  -13.943 -31.259 1.00 26.75  ? 42  ILE B CB  1 
ATOM   1061 C CG1 . ILE B 1 43 ? 25.138  -14.999 -32.128 1.00 29.10  ? 42  ILE B CG1 1 
ATOM   1062 C CG2 . ILE B 1 43 ? 22.892  -13.823 -31.669 1.00 26.81  ? 42  ILE B CG2 1 
ATOM   1063 C CD1 . ILE B 1 43 ? 25.232  -14.690 -33.610 1.00 27.11  ? 42  ILE B CD1 1 
ATOM   1064 N N   . PHE B 1 44 ? 23.742  -10.632 -30.965 1.00 27.54  ? 43  PHE B N   1 
ATOM   1065 C CA  . PHE B 1 44 ? 22.850  -9.748  -30.213 1.00 29.99  ? 43  PHE B CA  1 
ATOM   1066 C C   . PHE B 1 44 ? 21.410  -10.225 -30.409 1.00 27.64  ? 43  PHE B C   1 
ATOM   1067 O O   . PHE B 1 44 ? 20.900  -10.259 -31.543 1.00 24.78  ? 43  PHE B O   1 
ATOM   1068 C CB  . PHE B 1 44 ? 23.038  -8.317  -30.737 1.00 28.87  ? 43  PHE B CB  1 
ATOM   1069 C CG  . PHE B 1 44 ? 22.118  -7.315  -30.029 1.00 27.47  ? 43  PHE B CG  1 
ATOM   1070 C CD1 . PHE B 1 44 ? 20.944  -6.870  -30.629 1.00 30.44  ? 43  PHE B CD1 1 
ATOM   1071 C CD2 . PHE B 1 44 ? 22.444  -6.817  -28.772 1.00 35.99  ? 43  PHE B CD2 1 
ATOM   1072 C CE1 . PHE B 1 44 ? 20.083  -5.976  -29.986 1.00 30.33  ? 43  PHE B CE1 1 
ATOM   1073 C CE2 . PHE B 1 44 ? 21.600  -5.895  -28.141 1.00 32.43  ? 43  PHE B CE2 1 
ATOM   1074 C CZ  . PHE B 1 44 ? 20.446  -5.468  -28.767 1.00 32.10  ? 43  PHE B CZ  1 
ATOM   1075 N N   . PHE B 1 45 ? 20.689  -10.493 -29.282 1.00 26.52  ? 44  PHE B N   1 
ATOM   1076 C CA  . PHE B 1 45 ? 19.294  -10.883 -29.294 1.00 26.14  ? 44  PHE B CA  1 
ATOM   1077 C C   . PHE B 1 45 ? 18.396  -9.664  -29.173 1.00 25.55  ? 44  PHE B C   1 
ATOM   1078 O O   . PHE B 1 45 ? 18.491  -8.901  -28.180 1.00 26.85  ? 44  PHE B O   1 
ATOM   1079 C CB  . PHE B 1 45 ? 19.067  -11.892 -28.151 1.00 26.22  ? 44  PHE B CB  1 
ATOM   1080 C CG  . PHE B 1 45 ? 19.805  -13.217 -28.307 1.00 25.51  ? 44  PHE B CG  1 
ATOM   1081 C CD1 . PHE B 1 45 ? 21.123  -13.369 -27.945 1.00 27.36  ? 44  PHE B CD1 1 
ATOM   1082 C CD2 . PHE B 1 45 ? 19.115  -14.333 -28.814 1.00 24.04  ? 44  PHE B CD2 1 
ATOM   1083 C CE1 . PHE B 1 45 ? 21.780  -14.571 -28.130 1.00 28.54  ? 44  PHE B CE1 1 
ATOM   1084 C CE2 . PHE B 1 45 ? 19.764  -15.543 -28.972 1.00 25.94  ? 44  PHE B CE2 1 
ATOM   1085 C CZ  . PHE B 1 45 ? 21.087  -15.664 -28.626 1.00 25.92  ? 44  PHE B CZ  1 
ATOM   1086 N N   . PHE B 1 46 ? 17.578  -9.477  -30.226 1.00 26.11  ? 45  PHE B N   1 
ATOM   1087 C CA  . PHE B 1 46 ? 16.567  -8.421  -30.221 1.00 23.32  ? 45  PHE B CA  1 
ATOM   1088 C C   . PHE B 1 46 ? 15.603  -8.580  -29.025 1.00 26.61  ? 45  PHE B C   1 
ATOM   1089 O O   . PHE B 1 46 ? 15.292  -9.681  -28.592 1.00 27.26  ? 45  PHE B O   1 
ATOM   1090 C CB  . PHE B 1 46 ? 15.811  -8.168  -31.517 1.00 23.60  ? 45  PHE B CB  1 
ATOM   1091 C CG  . PHE B 1 46 ? 16.784  -7.676  -32.587 1.00 25.57  ? 45  PHE B CG  1 
ATOM   1092 C CD1 . PHE B 1 46 ? 17.346  -6.379  -32.509 1.00 26.51  ? 45  PHE B CD1 1 
ATOM   1093 C CD2 . PHE B 1 46 ? 17.071  -8.488  -33.693 1.00 24.53  ? 45  PHE B CD2 1 
ATOM   1094 C CE1 . PHE B 1 46 ? 18.237  -5.957  -33.505 1.00 27.27  ? 45  PHE B CE1 1 
ATOM   1095 C CE2 . PHE B 1 46 ? 17.902  -8.044  -34.726 1.00 25.37  ? 45  PHE B CE2 1 
ATOM   1096 C CZ  . PHE B 1 46 ? 18.468  -6.766  -34.626 1.00 28.22  ? 45  PHE B CZ  1 
ATOM   1097 N N   . GLY B 1 47 ? 15.081  -7.473  -28.511 1.00 26.13  ? 46  GLY B N   1 
ATOM   1098 C CA  . GLY B 1 47 ? 14.021  -7.536  -27.487 1.00 26.22  ? 46  GLY B CA  1 
ATOM   1099 C C   . GLY B 1 47 ? 14.619  -7.667  -26.081 1.00 29.58  ? 46  GLY B C   1 
ATOM   1100 O O   . GLY B 1 47 ? 14.426  -6.786  -25.227 1.00 34.21  ? 46  GLY B O   1 
ATOM   1101 N N   . THR B 1 48 ? 15.373  -8.742  -25.834 1.00 29.36  ? 47  THR B N   1 
ATOM   1102 C CA  . THR B 1 48 ? 16.044  -8.982  -24.563 1.00 30.96  ? 47  THR B CA  1 
ATOM   1103 C C   . THR B 1 48 ? 17.349  -8.188  -24.467 1.00 32.76  ? 47  THR B C   1 
ATOM   1104 O O   . THR B 1 48 ? 17.827  -7.861  -23.367 1.00 33.10  ? 47  THR B O   1 
ATOM   1105 C CB  . THR B 1 48 ? 16.294  -10.479 -24.360 1.00 32.21  ? 47  THR B CB  1 
ATOM   1106 O OG1 . THR B 1 48 ? 17.217  -10.803 -25.410 1.00 34.24  ? 47  THR B OG1 1 
ATOM   1107 C CG2 . THR B 1 48 ? 15.007  -11.300 -24.364 1.00 28.49  ? 47  THR B CG2 1 
ATOM   1108 N N   . HIS B 1 49 ? 17.939  -7.885  -25.632 1.00 30.50  ? 48  HIS B N   1 
ATOM   1109 C CA  . HIS B 1 49 ? 19.242  -7.242  -25.728 1.00 31.74  ? 48  HIS B CA  1 
ATOM   1110 C C   . HIS B 1 49 ? 20.346  -8.055  -25.057 1.00 28.39  ? 48  HIS B C   1 
ATOM   1111 O O   . HIS B 1 49 ? 21.381  -7.489  -24.675 1.00 35.67  ? 48  HIS B O   1 
ATOM   1112 C CB  . HIS B 1 49 ? 19.181  -5.750  -25.319 1.00 30.22  ? 48  HIS B CB  1 
ATOM   1113 C CG  . HIS B 1 49 ? 18.006  -5.033  -25.873 1.00 33.26  ? 48  HIS B CG  1 
ATOM   1114 N ND1 . HIS B 1 49 ? 17.305  -4.133  -25.097 1.00 37.19  ? 48  HIS B ND1 1 
ATOM   1115 C CD2 . HIS B 1 49 ? 17.373  -5.062  -27.063 1.00 32.01  ? 48  HIS B CD2 1 
ATOM   1116 C CE1 . HIS B 1 49 ? 16.294  -3.637  -25.800 1.00 41.94  ? 48  HIS B CE1 1 
ATOM   1117 N NE2 . HIS B 1 49 ? 16.316  -4.188  -27.013 1.00 35.48  ? 48  HIS B NE2 1 
ATOM   1118 N N   . GLU B 1 50 ? 20.178  -9.387  -24.964 1.00 27.99  ? 49  GLU B N   1 
ATOM   1119 C CA  . GLU B 1 50 ? 21.212  -10.297 -24.485 1.00 28.72  ? 49  GLU B CA  1 
ATOM   1120 C C   . GLU B 1 50 ? 22.266  -10.499 -25.595 1.00 27.55  ? 49  GLU B C   1 
ATOM   1121 O O   . GLU B 1 50 ? 21.998  -10.229 -26.787 1.00 28.97  ? 49  GLU B O   1 
ATOM   1122 C CB  . GLU B 1 50 ? 20.589  -11.644 -24.114 1.00 27.86  ? 49  GLU B CB  1 
ATOM   1123 C CG  . GLU B 1 50 ? 19.612  -11.582 -22.931 1.00 31.08  ? 49  GLU B CG  1 
ATOM   1124 C CD  . GLU B 1 50 ? 20.173  -11.962 -21.570 1.00 39.31  ? 49  GLU B CD  1 
ATOM   1125 O OE1 . GLU B 1 50 ? 19.398  -11.857 -20.590 1.00 38.98  ? 49  GLU B OE1 1 
ATOM   1126 O OE2 . GLU B 1 50 ? 21.344  -12.338 -21.440 1.00 39.57  ? 49  GLU B OE2 1 
ATOM   1127 N N   . THR B 1 51 ? 23.447  -10.958 -25.181 1.00 32.98  ? 50  THR B N   1 
ATOM   1128 C CA  . THR B 1 51 ? 24.513  -11.290 -26.120 1.00 32.05  ? 50  THR B CA  1 
ATOM   1129 C C   . THR B 1 51 ? 25.002  -12.692 -25.799 1.00 33.56  ? 50  THR B C   1 
ATOM   1130 O O   . THR B 1 51 ? 24.961  -13.143 -24.643 1.00 38.51  ? 50  THR B O   1 
ATOM   1131 C CB  . THR B 1 51 ? 25.650  -10.257 -26.145 1.00 34.94  ? 50  THR B CB  1 
ATOM   1132 O OG1 . THR B 1 51 ? 26.173  -10.242 -24.822 1.00 38.69  ? 50  THR B OG1 1 
ATOM   1133 C CG2 . THR B 1 51 ? 25.213  -8.879  -26.613 1.00 34.52  ? 50  THR B CG2 1 
ATOM   1134 N N   . ALA B 1 52 ? 25.387  -13.453 -26.835 1.00 34.45  ? 51  ALA B N   1 
ATOM   1135 C CA  . ALA B 1 52 ? 26.051  -14.726 -26.621 1.00 30.30  ? 51  ALA B CA  1 
ATOM   1136 C C   . ALA B 1 52 ? 26.915  -15.073 -27.839 1.00 30.98  ? 51  ALA B C   1 
ATOM   1137 O O   . ALA B 1 52 ? 26.840  -14.415 -28.871 1.00 30.84  ? 51  ALA B O   1 
ATOM   1138 C CB  . ALA B 1 52 ? 25.039  -15.848 -26.414 1.00 36.58  ? 51  ALA B CB  1 
ATOM   1139 N N   . PHE B 1 53 ? 27.757  -16.106 -27.709 1.00 32.81  ? 52  PHE B N   1 
ATOM   1140 C CA  . PHE B 1 53 ? 28.435  -16.600 -28.898 1.00 31.43  ? 52  PHE B CA  1 
ATOM   1141 C C   . PHE B 1 53 ? 27.768  -17.887 -29.391 1.00 32.39  ? 52  PHE B C   1 
ATOM   1142 O O   . PHE B 1 53 ? 27.542  -18.824 -28.616 1.00 34.10  ? 52  PHE B O   1 
ATOM   1143 C CB  . PHE B 1 53 ? 29.912  -16.876 -28.587 1.00 34.03  ? 52  PHE B CB  1 
ATOM   1144 C CG  . PHE B 1 53 ? 30.734  -15.686 -28.107 1.00 36.95  ? 52  PHE B CG  1 
ATOM   1145 C CD1 . PHE B 1 53 ? 31.030  -14.640 -28.965 1.00 38.49  ? 52  PHE B CD1 1 
ATOM   1146 C CD2 . PHE B 1 53 ? 31.234  -15.641 -26.812 1.00 41.81  ? 52  PHE B CD2 1 
ATOM   1147 C CE1 . PHE B 1 53 ? 31.792  -13.561 -28.544 1.00 42.78  ? 52  PHE B CE1 1 
ATOM   1148 C CE2 . PHE B 1 53 ? 31.987  -14.546 -26.385 1.00 40.87  ? 52  PHE B CE2 1 
ATOM   1149 C CZ  . PHE B 1 53 ? 32.267  -13.520 -27.249 1.00 46.20  ? 52  PHE B CZ  1 
ATOM   1150 N N   . LEU B 1 54 ? 27.429  -17.928 -30.687 1.00 31.37  ? 53  LEU B N   1 
ATOM   1151 C CA  . LEU B 1 54 ? 26.861  -19.143 -31.268 1.00 30.78  ? 53  LEU B CA  1 
ATOM   1152 C C   . LEU B 1 54 ? 27.621  -19.490 -32.552 1.00 31.81  ? 53  LEU B C   1 
ATOM   1153 O O   . LEU B 1 54 ? 28.126  -18.601 -33.239 1.00 32.37  ? 53  LEU B O   1 
ATOM   1154 C CB  . LEU B 1 54 ? 25.367  -19.016 -31.592 1.00 31.33  ? 53  LEU B CB  1 
ATOM   1155 C CG  . LEU B 1 54 ? 24.401  -18.824 -30.418 1.00 29.48  ? 53  LEU B CG  1 
ATOM   1156 C CD1 . LEU B 1 54 ? 22.978  -18.680 -30.911 1.00 28.07  ? 53  LEU B CD1 1 
ATOM   1157 C CD2 . LEU B 1 54 ? 24.525  -20.068 -29.571 1.00 34.64  ? 53  LEU B CD2 1 
ATOM   1158 N N   . GLY B 1 55 ? 27.595  -20.791 -32.888 1.00 31.07  ? 54  GLY B N   1 
ATOM   1159 C CA  . GLY B 1 55 ? 28.080  -21.343 -34.146 1.00 31.66  ? 54  GLY B CA  1 
ATOM   1160 C C   . GLY B 1 55 ? 26.987  -21.387 -35.214 1.00 27.14  ? 54  GLY B C   1 
ATOM   1161 O O   . GLY B 1 55 ? 25.801  -21.319 -34.918 1.00 29.40  ? 54  GLY B O   1 
ATOM   1162 N N   . PRO B 1 56 ? 27.355  -21.566 -36.512 1.00 30.32  ? 55  PRO B N   1 
ATOM   1163 C CA  . PRO B 1 56 ? 26.377  -21.609 -37.614 1.00 28.86  ? 55  PRO B CA  1 
ATOM   1164 C C   . PRO B 1 56 ? 25.242  -22.630 -37.544 1.00 26.12  ? 55  PRO B C   1 
ATOM   1165 O O   . PRO B 1 56 ? 24.186  -22.394 -38.102 1.00 26.33  ? 55  PRO B O   1 
ATOM   1166 C CB  . PRO B 1 56 ? 27.210  -21.813 -38.914 1.00 34.31  ? 55  PRO B CB  1 
ATOM   1167 C CG  . PRO B 1 56 ? 28.636  -21.964 -38.454 1.00 36.56  ? 55  PRO B CG  1 
ATOM   1168 C CD  . PRO B 1 56 ? 28.748  -21.703 -36.957 1.00 31.69  ? 55  PRO B CD  1 
ATOM   1169 N N   . LYS B 1 57 ? 25.424  -23.763 -36.838 1.00 26.50  ? 56  LYS B N   1 
ATOM   1170 C CA  . LYS B 1 57 ? 24.327  -24.720 -36.739 1.00 29.18  ? 56  LYS B CA  1 
ATOM   1171 C C   . LYS B 1 57 ? 23.111  -24.115 -36.038 1.00 29.08  ? 56  LYS B C   1 
ATOM   1172 O O   . LYS B 1 57 ? 21.988  -24.574 -36.253 1.00 29.09  ? 56  LYS B O   1 
ATOM   1173 C CB  . LYS B 1 57 ? 24.761  -25.999 -36.007 1.00 33.48  ? 56  LYS B CB  1 
ATOM   1174 C CG  . LYS B 1 57 ? 24.914  -25.825 -34.501 1.00 39.65  ? 56  LYS B CG  1 
ATOM   1175 C CD  . LYS B 1 57 ? 24.935  -27.213 -33.863 1.00 46.98  ? 56  LYS B CD  1 
ATOM   1176 C CE  . LYS B 1 57 ? 25.419  -27.193 -32.440 1.00 47.18  ? 56  LYS B CE  1 
ATOM   1177 N NZ  . LYS B 1 57 ? 24.481  -26.611 -31.478 1.00 51.39  ? 56  LYS B NZ  1 
ATOM   1178 N N   . ASP B 1 58 ? 23.350  -23.051 -35.245 1.00 27.16  ? 57  ASP B N   1 
ATOM   1179 C CA  . ASP B 1 58 ? 22.299  -22.408 -34.469 1.00 26.08  ? 57  ASP B CA  1 
ATOM   1180 C C   . ASP B 1 58 ? 21.863  -21.076 -35.102 1.00 28.40  ? 57  ASP B C   1 
ATOM   1181 O O   . ASP B 1 58 ? 21.106  -20.339 -34.469 1.00 27.51  ? 57  ASP B O   1 
ATOM   1182 C CB  . ASP B 1 58 ? 22.772  -22.260 -33.037 1.00 25.66  ? 57  ASP B CB  1 
ATOM   1183 C CG  . ASP B 1 58 ? 22.933  -23.594 -32.306 1.00 32.76  ? 57  ASP B CG  1 
ATOM   1184 O OD1 . ASP B 1 58 ? 22.023  -24.447 -32.442 1.00 34.69  ? 57  ASP B OD1 1 
ATOM   1185 O OD2 . ASP B 1 58 ? 23.928  -23.733 -31.589 1.00 33.90  ? 57  ASP B OD2 1 
ATOM   1186 N N   . LEU B 1 59 ? 22.340  -20.758 -36.322 1.00 26.64  ? 58  LEU B N   1 
ATOM   1187 C CA  . LEU B 1 59 ? 22.012  -19.453 -36.934 1.00 25.66  ? 58  LEU B CA  1 
ATOM   1188 C C   . LEU B 1 59 ? 21.245  -19.679 -38.225 1.00 25.67  ? 58  LEU B C   1 
ATOM   1189 O O   . LEU B 1 59 ? 21.733  -20.372 -39.139 1.00 28.43  ? 58  LEU B O   1 
ATOM   1190 C CB  . LEU B 1 59 ? 23.318  -18.708 -37.193 1.00 25.26  ? 58  LEU B CB  1 
ATOM   1191 C CG  . LEU B 1 59 ? 24.138  -18.404 -35.934 1.00 28.12  ? 58  LEU B CG  1 
ATOM   1192 C CD1 . LEU B 1 59 ? 25.487  -17.772 -36.255 1.00 29.78  ? 58  LEU B CD1 1 
ATOM   1193 C CD2 . LEU B 1 59 ? 23.359  -17.479 -34.918 1.00 29.18  ? 58  LEU B CD2 1 
ATOM   1194 N N   . PHE B 1 60 ? 20.059  -19.086 -38.313 1.00 25.71  ? 59  PHE B N   1 
ATOM   1195 C CA  . PHE B 1 60 ? 19.144  -19.274 -39.420 1.00 26.26  ? 59  PHE B CA  1 
ATOM   1196 C C   . PHE B 1 60 ? 18.937  -17.943 -40.124 1.00 28.04  ? 59  PHE B C   1 
ATOM   1197 O O   . PHE B 1 60 ? 18.381  -17.031 -39.549 1.00 28.53  ? 59  PHE B O   1 
ATOM   1198 C CB  . PHE B 1 60 ? 17.822  -19.772 -38.820 1.00 26.56  ? 59  PHE B CB  1 
ATOM   1199 C CG  . PHE B 1 60 ? 17.938  -21.179 -38.249 1.00 28.35  ? 59  PHE B CG  1 
ATOM   1200 C CD1 . PHE B 1 60 ? 18.481  -21.352 -36.973 1.00 28.23  ? 59  PHE B CD1 1 
ATOM   1201 C CD2 . PHE B 1 60 ? 17.492  -22.296 -38.971 1.00 27.96  ? 59  PHE B CD2 1 
ATOM   1202 C CE1 . PHE B 1 60 ? 18.613  -22.617 -36.428 1.00 30.34  ? 59  PHE B CE1 1 
ATOM   1203 C CE2 . PHE B 1 60 ? 17.649  -23.568 -38.425 1.00 28.53  ? 59  PHE B CE2 1 
ATOM   1204 C CZ  . PHE B 1 60 ? 18.218  -23.718 -37.171 1.00 26.89  ? 59  PHE B CZ  1 
ATOM   1205 N N   . PRO B 1 61 ? 19.446  -17.733 -41.362 1.00 28.71  ? 60  PRO B N   1 
ATOM   1206 C CA  . PRO B 1 61 ? 19.182  -16.448 -42.038 1.00 27.38  ? 60  PRO B CA  1 
ATOM   1207 C C   . PRO B 1 61 ? 17.729  -15.958 -41.973 1.00 26.65  ? 60  PRO B C   1 
ATOM   1208 O O   . PRO B 1 61 ? 16.746  -16.672 -42.240 1.00 30.81  ? 60  PRO B O   1 
ATOM   1209 C CB  . PRO B 1 61 ? 19.690  -16.772 -43.485 1.00 31.68  ? 60  PRO B CB  1 
ATOM   1210 C CG  . PRO B 1 61 ? 20.862  -17.693 -43.227 1.00 35.30  ? 60  PRO B CG  1 
ATOM   1211 C CD  . PRO B 1 61 ? 20.317  -18.652 -42.129 1.00 36.32  ? 60  PRO B CD  1 
ATOM   1212 N N   . TYR B 1 62 ? 17.566  -14.647 -41.635 1.00 29.07  ? 61  TYR B N   1 
ATOM   1213 C CA  . TYR B 1 62 ? 16.260  -14.113 -41.302 1.00 29.84  ? 61  TYR B CA  1 
ATOM   1214 C C   . TYR B 1 62 ? 15.243  -14.159 -42.439 1.00 30.64  ? 61  TYR B C   1 
ATOM   1215 O O   . TYR B 1 62 ? 14.111  -14.563 -42.206 1.00 32.81  ? 61  TYR B O   1 
ATOM   1216 C CB  . TYR B 1 62 ? 16.423  -12.689 -40.741 1.00 30.79  ? 61  TYR B CB  1 
ATOM   1217 C CG  . TYR B 1 62 ? 15.116  -11.952 -40.513 1.00 33.74  ? 61  TYR B CG  1 
ATOM   1218 C CD1 . TYR B 1 62 ? 14.291  -12.246 -39.428 1.00 37.26  ? 61  TYR B CD1 1 
ATOM   1219 C CD2 . TYR B 1 62 ? 14.754  -10.884 -41.333 1.00 39.68  ? 61  TYR B CD2 1 
ATOM   1220 C CE1 . TYR B 1 62 ? 13.105  -11.564 -39.212 1.00 36.92  ? 61  TYR B CE1 1 
ATOM   1221 C CE2 . TYR B 1 62 ? 13.580  -10.179 -41.115 1.00 39.13  ? 61  TYR B CE2 1 
ATOM   1222 C CZ  . TYR B 1 62 ? 12.761  -10.515 -40.048 1.00 39.97  ? 61  TYR B CZ  1 
ATOM   1223 O OH  . TYR B 1 62 ? 11.602  -9.836  -39.859 1.00 41.47  ? 61  TYR B OH  1 
ATOM   1224 N N   . ASP B 1 63 ? 15.636  -13.714 -43.645 1.00 35.77  ? 62  ASP B N   1 
ATOM   1225 C CA  . ASP B 1 63 ? 14.729  -13.692 -44.792 1.00 46.78  ? 62  ASP B CA  1 
ATOM   1226 C C   . ASP B 1 63 ? 14.166  -15.075 -45.111 1.00 37.03  ? 62  ASP B C   1 
ATOM   1227 O O   . ASP B 1 63 ? 12.953  -15.231 -45.200 1.00 46.56  ? 62  ASP B O   1 
ATOM   1228 C CB  . ASP B 1 63 ? 15.362  -13.019 -45.995 1.00 49.31  ? 62  ASP B CB  1 
ATOM   1229 C CG  . ASP B 1 63 ? 14.805  -11.640 -46.290 1.00 63.90  ? 62  ASP B CG  1 
ATOM   1230 O OD1 . ASP B 1 63 ? 14.769  -10.799 -45.357 1.00 68.27  ? 62  ASP B OD1 1 
ATOM   1231 O OD2 . ASP B 1 63 ? 14.382  -11.439 -47.445 1.00 67.26  ? 62  ASP B OD2 1 
ATOM   1232 N N   . LYS B 1 64 ? 15.047  -16.056 -45.259 1.00 42.44  ? 63  LYS B N   1 
ATOM   1233 C CA  . LYS B 1 64 ? 14.666  -17.431 -45.545 1.00 42.51  ? 63  LYS B CA  1 
ATOM   1234 C C   . LYS B 1 64 ? 13.751  -17.969 -44.448 1.00 35.24  ? 63  LYS B C   1 
ATOM   1235 O O   . LYS B 1 64 ? 12.879  -18.784 -44.720 1.00 41.38  ? 63  LYS B O   1 
ATOM   1236 C CB  . LYS B 1 64 ? 15.930  -18.301 -45.591 1.00 43.26  ? 63  LYS B CB  1 
ATOM   1237 C CG  . LYS B 1 64 ? 15.682  -19.792 -45.818 1.00 44.97  ? 63  LYS B CG  1 
ATOM   1238 C CD  . LYS B 1 64 ? 16.951  -20.602 -46.012 1.00 43.97  ? 63  LYS B CD  1 
ATOM   1239 C CE  . LYS B 1 64 ? 16.726  -21.915 -46.744 1.00 46.88  ? 63  LYS B CE  1 
ATOM   1240 N NZ  . LYS B 1 64 ? 15.684  -22.789 -46.203 1.00 50.82  ? 63  LYS B NZ  1 
ATOM   1241 N N   . SER B 1 65 ? 13.938  -17.511 -43.209 1.00 34.43  ? 64  SER B N   1 
ATOM   1242 C CA  . SER B 1 65 ? 13.356  -18.240 -42.079 1.00 39.50  ? 64  SER B CA  1 
ATOM   1243 C C   . SER B 1 65 ? 12.245  -17.486 -41.341 1.00 39.13  ? 64  SER B C   1 
ATOM   1244 O O   . SER B 1 65 ? 11.577  -18.045 -40.463 1.00 37.22  ? 64  SER B O   1 
ATOM   1245 C CB  . SER B 1 65 ? 14.414  -18.825 -41.176 1.00 38.52  ? 64  SER B CB  1 
ATOM   1246 O OG  . SER B 1 65 ? 15.116  -17.796 -40.496 1.00 56.80  ? 64  SER B OG  1 
ATOM   1247 N N   . LYS B 1 66 ? 11.936  -16.254 -41.764 1.00 34.20  ? 65  LYS B N   1 
ATOM   1248 C CA  . LYS B 1 66 ? 11.014  -15.461 -40.961 1.00 37.43  ? 65  LYS B CA  1 
ATOM   1249 C C   . LYS B 1 66 ? 9.579   -15.993 -40.965 1.00 41.46  ? 65  LYS B C   1 
ATOM   1250 O O   . LYS B 1 66 ? 8.853   -15.855 -39.979 1.00 41.99  ? 65  LYS B O   1 
ATOM   1251 C CB  . LYS B 1 66 ? 11.070  -13.961 -41.270 1.00 36.28  ? 65  LYS B CB  1 
ATOM   1252 C CG  . LYS B 1 66 ? 10.549  -13.645 -42.662 1.00 42.70  ? 65  LYS B CG  1 
ATOM   1253 C CD  . LYS B 1 66 ? 10.584  -12.174 -43.059 1.00 52.67  ? 65  LYS B CD  1 
ATOM   1254 C CE  . LYS B 1 66 ? 10.318  -12.101 -44.537 1.00 56.14  ? 65  LYS B CE  1 
ATOM   1255 N NZ  . LYS B 1 66 ? 10.154  -10.718 -44.982 1.00 71.00  ? 65  LYS B NZ  1 
ATOM   1256 N N   . ASP B 1 67 ? 9.118   -16.585 -42.066 1.00 42.36  ? 66  ASP B N   1 
ATOM   1257 C CA  . ASP B 1 67 ? 7.725   -17.001 -42.026 1.00 44.91  ? 66  ASP B CA  1 
ATOM   1258 C C   . ASP B 1 67 ? 7.546   -18.150 -41.031 1.00 46.44  ? 66  ASP B C   1 
ATOM   1259 O O   . ASP B 1 67 ? 6.522   -18.233 -40.356 1.00 50.96  ? 66  ASP B O   1 
ATOM   1260 C CB  . ASP B 1 67 ? 7.105   -17.158 -43.407 1.00 52.92  ? 66  ASP B CB  1 
ATOM   1261 C CG  . ASP B 1 67 ? 7.550   -18.351 -44.234 1.00 61.21  ? 66  ASP B CG  1 
ATOM   1262 O OD1 . ASP B 1 67 ? 7.971   -18.125 -45.396 1.00 70.95  ? 66  ASP B OD1 1 
ATOM   1263 O OD2 . ASP B 1 67 ? 7.437   -19.493 -43.728 1.00 77.66  ? 66  ASP B OD2 1 
ATOM   1264 N N   . LYS B 1 68 ? 8.578   -18.993 -40.906 1.00 41.84  ? 67  LYS B N   1 
ATOM   1265 C CA  . LYS B 1 68 ? 8.515   -20.141 -40.012 1.00 37.38  ? 67  LYS B CA  1 
ATOM   1266 C C   . LYS B 1 68 ? 8.694   -19.737 -38.540 1.00 36.86  ? 67  LYS B C   1 
ATOM   1267 O O   . LYS B 1 68 ? 7.923   -20.171 -37.678 1.00 39.36  ? 67  LYS B O   1 
ATOM   1268 C CB  . LYS B 1 68 ? 9.589   -21.146 -40.443 1.00 36.88  ? 67  LYS B CB  1 
ATOM   1269 C CG  . LYS B 1 68 ? 9.686   -22.436 -39.642 1.00 41.49  ? 67  LYS B CG  1 
ATOM   1270 C CD  . LYS B 1 68 ? 10.680  -23.289 -40.426 1.00 54.36  ? 67  LYS B CD  1 
ATOM   1271 C CE  . LYS B 1 68 ? 11.101  -24.554 -39.741 1.00 50.22  ? 67  LYS B CE  1 
ATOM   1272 N NZ  . LYS B 1 68 ? 9.971   -25.461 -39.543 1.00 51.28  ? 67  LYS B NZ  1 
ATOM   1273 N N   . TYR B 1 69 ? 9.701   -18.906 -38.254 1.00 35.45  ? 68  TYR B N   1 
ATOM   1274 C CA  . TYR B 1 69 ? 10.112  -18.616 -36.885 1.00 31.30  ? 68  TYR B CA  1 
ATOM   1275 C C   . TYR B 1 69 ? 9.578   -17.268 -36.406 1.00 33.72  ? 68  TYR B C   1 
ATOM   1276 O O   . TYR B 1 69 ? 9.654   -16.993 -35.213 1.00 35.34  ? 68  TYR B O   1 
ATOM   1277 C CB  . TYR B 1 69 ? 11.626  -18.663 -36.674 1.00 32.23  ? 68  TYR B CB  1 
ATOM   1278 C CG  . TYR B 1 69 ? 12.280  -20.019 -36.952 1.00 34.29  ? 68  TYR B CG  1 
ATOM   1279 C CD1 . TYR B 1 69 ? 11.824  -21.191 -36.360 1.00 33.30  ? 68  TYR B CD1 1 
ATOM   1280 C CD2 . TYR B 1 69 ? 13.370  -20.112 -37.812 1.00 34.84  ? 68  TYR B CD2 1 
ATOM   1281 C CE1 . TYR B 1 69 ? 12.441  -22.411 -36.626 1.00 34.73  ? 68  TYR B CE1 1 
ATOM   1282 C CE2 . TYR B 1 69 ? 13.992  -21.324 -38.095 1.00 35.30  ? 68  TYR B CE2 1 
ATOM   1283 C CZ  . TYR B 1 69 ? 13.519  -22.481 -37.489 1.00 38.39  ? 68  TYR B CZ  1 
ATOM   1284 O OH  . TYR B 1 69 ? 14.097  -23.692 -37.724 1.00 37.42  ? 68  TYR B OH  1 
ATOM   1285 N N   . GLY B 1 70 ? 9.086   -16.420 -37.321 1.00 33.83  ? 69  GLY B N   1 
ATOM   1286 C CA  . GLY B 1 70 ? 8.806   -15.031 -36.965 1.00 42.26  ? 69  GLY B CA  1 
ATOM   1287 C C   . GLY B 1 70 ? 7.393   -14.801 -36.421 1.00 47.49  ? 69  GLY B C   1 
ATOM   1288 O O   . GLY B 1 70 ? 6.735   -13.805 -36.762 1.00 45.78  ? 69  GLY B O   1 
ATOM   1289 N N   . LYS B 1 71 ? 6.911   -15.741 -35.598 1.00 43.47  ? 70  LYS B N   1 
ATOM   1290 C CA  . LYS B 1 71 ? 5.544   -15.660 -35.109 1.00 47.37  ? 70  LYS B CA  1 
ATOM   1291 C C   . LYS B 1 71 ? 5.571   -15.213 -33.663 1.00 48.03  ? 70  LYS B C   1 
ATOM   1292 O O   . LYS B 1 71 ? 6.392   -15.705 -32.890 1.00 43.33  ? 70  LYS B O   1 
ATOM   1293 C CB  . LYS B 1 71 ? 4.859   -17.027 -35.009 1.00 50.00  ? 70  LYS B CB  1 
ATOM   1294 C CG  . LYS B 1 71 ? 3.881   -17.326 -36.133 1.00 61.49  ? 70  LYS B CG  1 
ATOM   1295 C CD  . LYS B 1 71 ? 4.524   -17.872 -37.401 1.00 64.88  ? 70  LYS B CD  1 
ATOM   1296 C CE  . LYS B 1 71 ? 3.477   -18.410 -38.337 1.00 74.67  ? 70  LYS B CE  1 
ATOM   1297 N NZ  . LYS B 1 71 ? 3.999   -19.407 -39.277 1.00 75.78  ? 70  LYS B NZ  1 
ATOM   1298 N N   . PRO B 1 72 ? 4.648   -14.323 -33.237 1.00 45.03  ? 71  PRO B N   1 
ATOM   1299 C CA  . PRO B 1 72 ? 4.571   -13.979 -31.815 1.00 44.67  ? 71  PRO B CA  1 
ATOM   1300 C C   . PRO B 1 72 ? 4.419   -15.180 -30.882 1.00 38.76  ? 71  PRO B C   1 
ATOM   1301 O O   . PRO B 1 72 ? 3.789   -16.180 -31.237 1.00 45.05  ? 71  PRO B O   1 
ATOM   1302 C CB  . PRO B 1 72 ? 3.435   -12.951 -31.703 1.00 45.95  ? 71  PRO B CB  1 
ATOM   1303 C CG  . PRO B 1 72 ? 3.269   -12.448 -33.119 1.00 49.01  ? 71  PRO B CG  1 
ATOM   1304 C CD  . PRO B 1 72 ? 3.738   -13.540 -34.090 1.00 40.96  ? 71  PRO B CD  1 
ATOM   1305 N N   . ASN B 1 73 ? 5.021   -15.066 -29.690 1.00 42.75  ? 72  ASN B N   1 
ATOM   1306 C CA  . ASN B 1 73 ? 4.784   -16.015 -28.607 1.00 37.72  ? 72  ASN B CA  1 
ATOM   1307 C C   . ASN B 1 73 ? 4.766   -15.255 -27.268 1.00 44.14  ? 72  ASN B C   1 
ATOM   1308 O O   . ASN B 1 73 ? 4.784   -14.019 -27.245 1.00 48.21  ? 72  ASN B O   1 
ATOM   1309 C CB  . ASN B 1 73 ? 5.782   -17.162 -28.597 1.00 41.01  ? 72  ASN B CB  1 
ATOM   1310 C CG  . ASN B 1 73 ? 7.206   -16.708 -28.329 1.00 39.24  ? 72  ASN B CG  1 
ATOM   1311 O OD1 . ASN B 1 73 ? 7.460   -16.010 -27.340 1.00 36.67  ? 72  ASN B OD1 1 
ATOM   1312 N ND2 . ASN B 1 73 ? 8.157   -17.104 -29.178 1.00 35.76  ? 72  ASN B ND2 1 
ATOM   1313 N N   . LYS B 1 74 ? 4.799   -16.008 -26.162 1.00 39.51  ? 73  LYS B N   1 
ATOM   1314 C CA  . LYS B 1 74 ? 4.664   -15.442 -24.823 1.00 42.40  ? 73  LYS B CA  1 
ATOM   1315 C C   . LYS B 1 74 ? 5.986   -15.470 -24.030 1.00 46.58  ? 73  LYS B C   1 
ATOM   1316 O O   . LYS B 1 74 ? 5.978   -15.419 -22.795 1.00 45.76  ? 73  LYS B O   1 
ATOM   1317 C CB  . LYS B 1 74 ? 3.560   -16.213 -24.075 1.00 45.16  ? 73  LYS B CB  1 
ATOM   1318 N N   . ARG B 1 75 ? 7.139   -15.574 -24.713 1.00 36.01  ? 74  ARG B N   1 
ATOM   1319 C CA  . ARG B 1 75 ? 8.408   -15.483 -24.006 1.00 34.64  ? 74  ARG B CA  1 
ATOM   1320 C C   . ARG B 1 75 ? 8.699   -13.994 -23.822 1.00 32.72  ? 74  ARG B C   1 
ATOM   1321 O O   . ARG B 1 75 ? 8.412   -13.185 -24.703 1.00 31.69  ? 74  ARG B O   1 
ATOM   1322 C CB  . ARG B 1 75 ? 9.573   -16.231 -24.675 1.00 31.92  ? 74  ARG B CB  1 
ATOM   1323 C CG  . ARG B 1 75 ? 9.446   -17.735 -24.943 1.00 32.67  ? 74  ARG B CG  1 
ATOM   1324 C CD  . ARG B 1 75 ? 9.230   -18.530 -23.648 1.00 35.46  ? 74  ARG B CD  1 
ATOM   1325 N NE  . ARG B 1 75 ? 9.400   -19.973 -23.853 1.00 32.92  ? 74  ARG B NE  1 
ATOM   1326 C CZ  . ARG B 1 75 ? 10.520  -20.629 -23.652 1.00 36.41  ? 74  ARG B CZ  1 
ATOM   1327 N NH1 . ARG B 1 75 ? 11.590  -20.021 -23.149 1.00 42.45  ? 74  ARG B NH1 1 
ATOM   1328 N NH2 . ARG B 1 75 ? 10.574  -21.911 -23.981 1.00 40.08  ? 74  ARG B NH2 1 
ATOM   1329 N N   . LYS B 1 76 ? 9.219   -13.635 -22.643 1.00 30.64  ? 75  LYS B N   1 
ATOM   1330 C CA  . LYS B 1 76 ? 9.579   -12.255 -22.337 1.00 26.22  ? 75  LYS B CA  1 
ATOM   1331 C C   . LYS B 1 76 ? 10.639  -11.730 -23.317 1.00 28.90  ? 75  LYS B C   1 
ATOM   1332 O O   . LYS B 1 76 ? 11.723  -12.323 -23.451 1.00 29.87  ? 75  LYS B O   1 
ATOM   1333 C CB  . LYS B 1 76 ? 10.132  -12.153 -20.909 1.00 28.36  ? 75  LYS B CB  1 
ATOM   1334 C CG  . LYS B 1 76 ? 10.583  -10.722 -20.562 1.00 30.10  ? 75  LYS B CG  1 
ATOM   1335 C CD  . LYS B 1 76 ? 11.159  -10.612 -19.157 1.00 36.32  ? 75  LYS B CD  1 
ATOM   1336 C CE  . LYS B 1 76 ? 11.368  -9.174  -18.752 1.00 41.80  ? 75  LYS B CE  1 
ATOM   1337 N NZ  . LYS B 1 76 ? 11.868  -9.055  -17.371 1.00 50.49  ? 75  LYS B NZ  1 
ATOM   1338 N N   . GLY B 1 77 ? 10.255  -10.642 -23.998 1.00 27.54  ? 76  GLY B N   1 
ATOM   1339 C CA  . GLY B 1 77 ? 11.133  -9.886  -24.902 1.00 28.51  ? 76  GLY B CA  1 
ATOM   1340 C C   . GLY B 1 77 ? 10.971  -10.269 -26.373 1.00 32.46  ? 76  GLY B C   1 
ATOM   1341 O O   . GLY B 1 77 ? 11.545  -9.626  -27.256 1.00 32.39  ? 76  GLY B O   1 
ATOM   1342 N N   . PHE B 1 78 ? 10.237  -11.338 -26.660 1.00 28.41  ? 77  PHE B N   1 
ATOM   1343 C CA  . PHE B 1 78 ? 10.186  -11.873 -28.019 1.00 26.46  ? 77  PHE B CA  1 
ATOM   1344 C C   . PHE B 1 78 ? 9.444   -10.921 -28.952 1.00 30.84  ? 77  PHE B C   1 
ATOM   1345 O O   . PHE B 1 78 ? 9.929   -10.597 -30.052 1.00 30.49  ? 77  PHE B O   1 
ATOM   1346 C CB  . PHE B 1 78 ? 9.470   -13.227 -28.040 1.00 28.01  ? 77  PHE B CB  1 
ATOM   1347 C CG  . PHE B 1 78 ? 9.703   -13.948 -29.354 1.00 26.77  ? 77  PHE B CG  1 
ATOM   1348 C CD1 . PHE B 1 78 ? 10.802  -14.801 -29.523 1.00 27.84  ? 77  PHE B CD1 1 
ATOM   1349 C CD2 . PHE B 1 78 ? 8.803   -13.793 -30.400 1.00 31.50  ? 77  PHE B CD2 1 
ATOM   1350 C CE1 . PHE B 1 78 ? 10.996  -15.472 -30.759 1.00 25.81  ? 77  PHE B CE1 1 
ATOM   1351 C CE2 . PHE B 1 78 ? 8.996   -14.478 -31.595 1.00 31.42  ? 77  PHE B CE2 1 
ATOM   1352 C CZ  . PHE B 1 78 ? 10.085  -15.310 -31.752 1.00 27.97  ? 77  PHE B CZ  1 
ATOM   1353 N N   . ASN B 1 79 ? 8.280   -10.424 -28.537 1.00 30.46  ? 78  ASN B N   1 
ATOM   1354 C CA  . ASN B 1 79 ? 7.488   -9.601  -29.442 1.00 33.25  ? 78  ASN B CA  1 
ATOM   1355 C C   . ASN B 1 79 ? 8.184   -8.253  -29.672 1.00 31.50  ? 78  ASN B C   1 
ATOM   1356 O O   . ASN B 1 79 ? 8.115   -7.682  -30.777 1.00 33.75  ? 78  ASN B O   1 
ATOM   1357 C CB  . ASN B 1 79 ? 6.034   -9.515  -28.979 1.00 39.09  ? 78  ASN B CB  1 
ATOM   1358 C CG  . ASN B 1 79 ? 5.244   -10.807 -29.102 1.00 44.86  ? 78  ASN B CG  1 
ATOM   1359 O OD1 . ASN B 1 79 ? 5.688   -11.808 -29.687 1.00 43.56  ? 78  ASN B OD1 1 
ATOM   1360 N ND2 . ASN B 1 79 ? 4.061   -10.827 -28.512 1.00 47.64  ? 78  ASN B ND2 1 
ATOM   1361 N N   . GLU B 1 80 ? 8.869   -7.758  -28.634 1.00 31.05  ? 79  GLU B N   1 
ATOM   1362 C CA  . GLU B 1 80 ? 9.658   -6.546  -28.771 1.00 32.67  ? 79  GLU B CA  1 
ATOM   1363 C C   . GLU B 1 80 ? 10.770  -6.818  -29.784 1.00 31.33  ? 79  GLU B C   1 
ATOM   1364 O O   . GLU B 1 80 ? 11.083  -5.918  -30.584 1.00 29.62  ? 79  GLU B O   1 
ATOM   1365 C CB  . GLU B 1 80 ? 10.285  -6.117  -27.443 1.00 34.59  ? 79  GLU B CB  1 
ATOM   1366 C CG  . GLU B 1 80 ? 9.295   -5.491  -26.460 1.00 44.04  ? 79  GLU B CG  1 
ATOM   1367 N N   . GLY B 1 81 ? 11.379  -8.024  -29.689 1.00 27.87  ? 80  GLY B N   1 
ATOM   1368 C CA  . GLY B 1 81 ? 12.504  -8.399  -30.555 1.00 29.45  ? 80  GLY B CA  1 
ATOM   1369 C C   . GLY B 1 81 ? 12.062  -8.455  -32.015 1.00 28.10  ? 80  GLY B C   1 
ATOM   1370 O O   . GLY B 1 81 ? 12.824  -8.076  -32.933 1.00 30.38  ? 80  GLY B O   1 
ATOM   1371 N N   . LEU B 1 82 ? 10.824  -8.925  -32.242 1.00 26.78  ? 81  LEU B N   1 
ATOM   1372 C CA  . LEU B 1 82 ? 10.257  -8.943  -33.590 1.00 31.03  ? 81  LEU B CA  1 
ATOM   1373 C C   . LEU B 1 82 ? 10.100  -7.511  -34.104 1.00 29.80  ? 81  LEU B C   1 
ATOM   1374 O O   . LEU B 1 82 ? 10.350  -7.253  -35.274 1.00 30.57  ? 81  LEU B O   1 
ATOM   1375 C CB  . LEU B 1 82 ? 8.916   -9.660  -33.683 1.00 32.32  ? 81  LEU B CB  1 
ATOM   1376 C CG  . LEU B 1 82 ? 8.939   -11.165 -33.416 1.00 30.42  ? 81  LEU B CG  1 
ATOM   1377 C CD1 . LEU B 1 82 ? 7.541   -11.781 -33.457 1.00 33.04  ? 81  LEU B CD1 1 
ATOM   1378 C CD2 . LEU B 1 82 ? 9.897   -11.845 -34.395 1.00 30.34  ? 81  LEU B CD2 1 
ATOM   1379 N N   . TRP B 1 83 ? 9.628   -6.606  -33.242 1.00 31.82  ? 82  TRP B N   1 
ATOM   1380 C CA  . TRP B 1 83 ? 9.489   -5.205  -33.619 1.00 32.29  ? 82  TRP B CA  1 
ATOM   1381 C C   . TRP B 1 83 ? 10.836  -4.634  -34.056 1.00 32.83  ? 82  TRP B C   1 
ATOM   1382 O O   . TRP B 1 83 ? 10.932  -4.012  -35.122 1.00 32.42  ? 82  TRP B O   1 
ATOM   1383 C CB  . TRP B 1 83 ? 8.894   -4.366  -32.469 1.00 34.70  ? 82  TRP B CB  1 
ATOM   1384 C CG  . TRP B 1 83 ? 8.597   -2.966  -32.941 1.00 32.13  ? 82  TRP B CG  1 
ATOM   1385 C CD1 . TRP B 1 83 ? 7.456   -2.552  -33.559 1.00 41.01  ? 82  TRP B CD1 1 
ATOM   1386 C CD2 . TRP B 1 83 ? 9.520   -1.858  -32.993 1.00 35.77  ? 82  TRP B CD2 1 
ATOM   1387 N NE1 . TRP B 1 83 ? 7.581   -1.239  -33.944 1.00 42.71  ? 82  TRP B NE1 1 
ATOM   1388 C CE2 . TRP B 1 83 ? 8.839   -0.797  -33.624 1.00 38.00  ? 82  TRP B CE2 1 
ATOM   1389 C CE3 . TRP B 1 83 ? 10.841  -1.656  -32.571 1.00 34.25  ? 82  TRP B CE3 1 
ATOM   1390 C CZ2 . TRP B 1 83 ? 9.438   0.446   -33.830 1.00 35.74  ? 82  TRP B CZ2 1 
ATOM   1391 C CZ3 . TRP B 1 83 ? 11.433  -0.428  -32.786 1.00 40.34  ? 82  TRP B CZ3 1 
ATOM   1392 C CH2 . TRP B 1 83 ? 10.736  0.607   -33.421 1.00 33.62  ? 82  TRP B CH2 1 
ATOM   1393 N N   . GLU B 1 84 ? 11.870  -4.888  -33.248 1.00 27.17  ? 83  GLU B N   1 
ATOM   1394 C CA  . GLU B 1 84 ? 13.201  -4.346  -33.492 1.00 26.91  ? 83  GLU B CA  1 
ATOM   1395 C C   . GLU B 1 84 ? 13.794  -4.859  -34.807 1.00 28.71  ? 83  GLU B C   1 
ATOM   1396 O O   . GLU B 1 84 ? 14.384  -4.112  -35.580 1.00 29.27  ? 83  GLU B O   1 
ATOM   1397 C CB  . GLU B 1 84 ? 14.146  -4.662  -32.347 1.00 26.82  ? 83  GLU B CB  1 
ATOM   1398 C CG  . GLU B 1 84 ? 13.757  -3.876  -31.086 1.00 29.34  ? 83  GLU B CG  1 
ATOM   1399 C CD  . GLU B 1 84 ? 14.567  -4.255  -29.877 1.00 29.81  ? 83  GLU B CD  1 
ATOM   1400 O OE1 . GLU B 1 84 ? 15.503  -5.105  -29.978 1.00 30.44  ? 83  GLU B OE1 1 
ATOM   1401 O OE2 . GLU B 1 84 ? 14.311  -3.662  -28.774 1.00 32.71  ? 83  GLU B OE2 1 
ATOM   1402 N N   . ILE B 1 85 ? 13.713  -6.167  -35.043 1.00 26.05  ? 84  ILE B N   1 
ATOM   1403 C CA  . ILE B 1 85 ? 14.342  -6.709  -36.248 1.00 27.65  ? 84  ILE B CA  1 
ATOM   1404 C C   . ILE B 1 85 ? 13.715  -6.175  -37.544 1.00 27.78  ? 84  ILE B C   1 
ATOM   1405 O O   . ILE B 1 85 ? 14.443  -6.003  -38.554 1.00 26.20  ? 84  ILE B O   1 
ATOM   1406 C CB  . ILE B 1 85 ? 14.412  -8.252  -36.222 1.00 26.33  ? 84  ILE B CB  1 
ATOM   1407 C CG1 . ILE B 1 85 ? 15.450  -8.792  -37.266 1.00 25.76  ? 84  ILE B CG1 1 
ATOM   1408 C CG2 . ILE B 1 85 ? 13.043  -8.881  -36.438 1.00 25.61  ? 84  ILE B CG2 1 
ATOM   1409 C CD1 . ILE B 1 85 ? 15.965  -10.198 -36.929 1.00 28.08  ? 84  ILE B CD1 1 
ATOM   1410 N N   . GLN B 1 86 ? 12.398  -5.894  -37.500 1.00 28.93  ? 85  GLN B N   1 
ATOM   1411 C CA  . GLN B 1 86 ? 11.595  -5.359  -38.595 1.00 29.06  ? 85  GLN B CA  1 
ATOM   1412 C C   . GLN B 1 86 ? 11.843  -3.853  -38.782 1.00 34.40  ? 85  GLN B C   1 
ATOM   1413 O O   . GLN B 1 86 ? 11.943  -3.361  -39.908 1.00 34.74  ? 85  GLN B O   1 
ATOM   1414 C CB  . GLN B 1 86 ? 10.142  -5.698  -38.245 1.00 38.00  ? 85  GLN B CB  1 
ATOM   1415 C CG  . GLN B 1 86 ? 9.706   -7.104  -38.675 1.00 50.06  ? 85  GLN B CG  1 
ATOM   1416 C CD  . GLN B 1 86 ? 8.651   -7.790  -37.819 1.00 52.01  ? 85  GLN B CD  1 
ATOM   1417 O OE1 . GLN B 1 86 ? 7.508   -7.328  -37.665 1.00 60.49  ? 85  GLN B OE1 1 
ATOM   1418 N NE2 . GLN B 1 86 ? 9.024   -8.952  -37.288 1.00 47.56  ? 85  GLN B NE2 1 
ATOM   1419 N N   . ASN B 1 87 ? 11.996  -3.119  -37.688 1.00 32.08  ? 86  ASN B N   1 
ATOM   1420 C CA  . ASN B 1 87 ? 11.880  -1.667  -37.806 1.00 28.73  ? 86  ASN B CA  1 
ATOM   1421 C C   . ASN B 1 87 ? 13.195  -0.929  -37.601 1.00 32.99  ? 86  ASN B C   1 
ATOM   1422 O O   . ASN B 1 87 ? 13.344  0.211   -38.072 1.00 32.90  ? 86  ASN B O   1 
ATOM   1423 C CB  . ASN B 1 87 ? 10.939  -1.111  -36.733 1.00 31.56  ? 86  ASN B CB  1 
ATOM   1424 C CG  . ASN B 1 87 ? 9.510   -1.445  -37.067 1.00 38.76  ? 86  ASN B CG  1 
ATOM   1425 O OD1 . ASN B 1 87 ? 8.888   -0.755  -37.880 1.00 47.55  ? 86  ASN B OD1 1 
ATOM   1426 N ND2 . ASN B 1 87 ? 8.996   -2.529  -36.510 1.00 37.98  ? 86  ASN B ND2 1 
ATOM   1427 N N   . ASN B 1 88 ? 14.130  -1.494  -36.850 1.00 30.28  ? 87  ASN B N   1 
ATOM   1428 C CA  . ASN B 1 88 ? 15.384  -0.787  -36.642 1.00 29.68  ? 87  ASN B CA  1 
ATOM   1429 C C   . ASN B 1 88 ? 16.466  -1.775  -36.228 1.00 28.02  ? 87  ASN B C   1 
ATOM   1430 O O   . ASN B 1 88 ? 17.080  -1.673  -35.149 1.00 29.06  ? 87  ASN B O   1 
ATOM   1431 C CB  . ASN B 1 88 ? 15.210  0.467   -35.771 1.00 35.26  ? 87  ASN B CB  1 
ATOM   1432 C CG  . ASN B 1 88 ? 16.366  1.451   -35.845 1.00 34.92  ? 87  ASN B CG  1 
ATOM   1433 O OD1 . ASN B 1 88 ? 17.405  1.209   -36.477 1.00 33.36  ? 87  ASN B OD1 1 
ATOM   1434 N ND2 . ASN B 1 88 ? 16.223  2.589   -35.173 1.00 39.64  ? 87  ASN B ND2 1 
ATOM   1435 N N   . PRO B 1 89 ? 16.789  -2.739  -37.132 1.00 29.00  ? 88  PRO B N   1 
ATOM   1436 C CA  . PRO B 1 89 ? 17.688  -3.835  -36.781 1.00 27.18  ? 88  PRO B CA  1 
ATOM   1437 C C   . PRO B 1 89 ? 19.114  -3.394  -36.498 1.00 24.54  ? 88  PRO B C   1 
ATOM   1438 O O   . PRO B 1 89 ? 19.883  -4.135  -35.878 1.00 27.73  ? 88  PRO B O   1 
ATOM   1439 C CB  . PRO B 1 89 ? 17.614  -4.811  -37.991 1.00 28.93  ? 88  PRO B CB  1 
ATOM   1440 C CG  . PRO B 1 89 ? 17.125  -3.934  -39.162 1.00 25.42  ? 88  PRO B CG  1 
ATOM   1441 C CD  . PRO B 1 89 ? 16.231  -2.881  -38.483 1.00 28.52  ? 88  PRO B CD  1 
ATOM   1442 N N   . HIS B 1 90 ? 19.515  -2.183  -37.021 1.00 25.87  ? 89  HIS B N   1 
ATOM   1443 C CA  . HIS B 1 90 ? 20.911  -1.785  -36.929 1.00 25.78  ? 89  HIS B CA  1 
ATOM   1444 C C   . HIS B 1 90 ? 21.191  -0.721  -35.846 1.00 26.51  ? 89  HIS B C   1 
ATOM   1445 O O   . HIS B 1 90 ? 22.318  -0.254  -35.766 1.00 31.46  ? 89  HIS B O   1 
ATOM   1446 C CB  . HIS B 1 90 ? 21.434  -1.329  -38.310 1.00 25.11  ? 89  HIS B CB  1 
ATOM   1447 C CG  . HIS B 1 90 ? 21.288  -2.414  -39.348 1.00 26.60  ? 89  HIS B CG  1 
ATOM   1448 N ND1 . HIS B 1 90 ? 21.896  -3.644  -39.197 1.00 25.97  ? 89  HIS B ND1 1 
ATOM   1449 C CD2 . HIS B 1 90 ? 20.645  -2.457  -40.504 1.00 27.44  ? 89  HIS B CD2 1 
ATOM   1450 C CE1 . HIS B 1 90 ? 21.590  -4.405  -40.236 1.00 25.76  ? 89  HIS B CE1 1 
ATOM   1451 N NE2 . HIS B 1 90 ? 20.811  -3.710  -41.041 1.00 28.87  ? 89  HIS B NE2 1 
ATOM   1452 N N   . ALA B 1 91 ? 20.181  -0.393  -35.038 1.00 29.11  ? 90  ALA B N   1 
ATOM   1453 C CA  . ALA B 1 91 ? 20.355  0.619   -33.995 1.00 27.75  ? 90  ALA B CA  1 
ATOM   1454 C C   . ALA B 1 91 ? 21.343  0.210   -32.900 1.00 34.30  ? 90  ALA B C   1 
ATOM   1455 O O   . ALA B 1 91 ? 21.617  -0.964  -32.654 1.00 33.16  ? 90  ALA B O   1 
ATOM   1456 C CB  . ALA B 1 91 ? 19.011  1.003   -33.418 1.00 27.54  ? 90  ALA B CB  1 
ATOM   1457 N N   . SER B 1 92 ? 21.874  1.227   -32.197 1.00 34.35  ? 91  SER B N   1 
ATOM   1458 C CA  . SER B 1 92 ? 22.466  1.044   -30.888 1.00 36.03  ? 91  SER B CA  1 
ATOM   1459 C C   . SER B 1 92 ? 21.374  0.773   -29.848 1.00 42.67  ? 91  SER B C   1 
ATOM   1460 O O   . SER B 1 92 ? 20.454  1.593   -29.654 1.00 40.98  ? 91  SER B O   1 
ATOM   1461 C CB  . SER B 1 92 ? 23.216  2.313   -30.485 1.00 40.88  ? 91  SER B CB  1 
ATOM   1462 O OG  . SER B 1 92 ? 23.551  2.188   -29.114 1.00 45.21  ? 91  SER B OG  1 
ATOM   1463 N N   . TYR B 1 93 ? 21.525  -0.356  -29.144 1.00 38.19  ? 92  TYR B N   1 
ATOM   1464 C CA  . TYR B 1 93 ? 20.687  -0.747  -28.019 1.00 43.05  ? 92  TYR B CA  1 
ATOM   1465 C C   . TYR B 1 93 ? 21.543  -0.701  -26.755 1.00 53.82  ? 92  TYR B C   1 
ATOM   1466 O O   . TYR B 1 93 ? 21.329  -1.474  -25.824 1.00 58.33  ? 92  TYR B O   1 
ATOM   1467 C CB  . TYR B 1 93 ? 19.987  -2.102  -28.250 1.00 35.67  ? 92  TYR B CB  1 
ATOM   1468 C CG  . TYR B 1 93 ? 18.987  -2.048  -29.392 1.00 30.03  ? 92  TYR B CG  1 
ATOM   1469 C CD1 . TYR B 1 93 ? 17.716  -1.524  -29.213 1.00 37.41  ? 92  TYR B CD1 1 
ATOM   1470 C CD2 . TYR B 1 93 ? 19.327  -2.486  -30.684 1.00 34.80  ? 92  TYR B CD2 1 
ATOM   1471 C CE1 . TYR B 1 93 ? 16.818  -1.394  -30.252 1.00 36.06  ? 92  TYR B CE1 1 
ATOM   1472 C CE2 . TYR B 1 93 ? 18.422  -2.363  -31.731 1.00 30.02  ? 92  TYR B CE2 1 
ATOM   1473 C CZ  . TYR B 1 93 ? 17.162  -1.844  -31.513 1.00 30.88  ? 92  TYR B CZ  1 
ATOM   1474 O OH  . TYR B 1 93 ? 16.204  -1.705  -32.470 1.00 30.44  ? 92  TYR B OH  1 
ATOM   1475 N N   . SER B 1 94 ? 22.539  0.193   -26.760 1.00 61.16  ? 93  SER B N   1 
ATOM   1476 C CA  . SER B 1 94 ? 23.373  0.449   -25.594 1.00 69.42  ? 93  SER B CA  1 
ATOM   1477 C C   . SER B 1 94 ? 22.546  1.221   -24.555 1.00 72.65  ? 93  SER B C   1 
ATOM   1478 O O   . SER B 1 94 ? 22.066  2.322   -24.907 1.00 74.00  ? 93  SER B O   1 
ATOM   1479 C CB  . SER B 1 94 ? 24.637  1.205   -25.958 1.00 71.36  ? 93  SER B CB  1 
ATOM   1480 O OG  . SER B 1 94 ? 25.545  0.388   -26.683 1.00 77.16  ? 93  SER B OG  1 
ATOM   1481 O OXT . SER B 1 94 ? 22.401  0.686   -23.434 1.00 76.78  ? 93  SER B OXT 1 
ATOM   1482 N N   . HIS C 1 4  ? 33.251  -24.669 27.107  1.00 75.86  ? 3   HIS C N   1 
ATOM   1483 C CA  . HIS C 1 4  ? 32.228  -23.601 27.280  1.00 79.14  ? 3   HIS C CA  1 
ATOM   1484 C C   . HIS C 1 4  ? 31.647  -23.683 28.694  1.00 93.86  ? 3   HIS C C   1 
ATOM   1485 O O   . HIS C 1 4  ? 32.383  -23.934 29.650  1.00 87.82  ? 3   HIS C O   1 
ATOM   1486 C CB  . HIS C 1 4  ? 31.203  -23.660 26.141  1.00 77.47  ? 3   HIS C CB  1 
ATOM   1487 N N   . ALA C 1 5  ? 30.320  -23.501 28.802  1.00 96.10  ? 4   ALA C N   1 
ATOM   1488 C CA  . ALA C 1 5  ? 29.648  -23.237 30.065  1.00 90.63  ? 4   ALA C CA  1 
ATOM   1489 C C   . ALA C 1 5  ? 28.134  -23.289 29.871  1.00 91.46  ? 4   ALA C C   1 
ATOM   1490 O O   . ALA C 1 5  ? 27.501  -22.261 29.625  1.00 88.78  ? 4   ALA C O   1 
ATOM   1491 C CB  . ALA C 1 5  ? 30.048  -21.856 30.525  1.00 93.07  ? 4   ALA C CB  1 
ATOM   1492 N N   . PHE C 1 6  ? 27.550  -24.484 29.999  1.00 82.56  ? 5   PHE C N   1 
ATOM   1493 C CA  . PHE C 1 6  ? 26.142  -24.629 29.665  1.00 61.76  ? 5   PHE C CA  1 
ATOM   1494 C C   . PHE C 1 6  ? 25.327  -24.654 30.948  1.00 60.82  ? 5   PHE C C   1 
ATOM   1495 O O   . PHE C 1 6  ? 25.692  -25.337 31.900  1.00 67.28  ? 5   PHE C O   1 
ATOM   1496 C CB  . PHE C 1 6  ? 25.851  -25.804 28.722  1.00 54.89  ? 5   PHE C CB  1 
ATOM   1497 C CG  . PHE C 1 6  ? 26.618  -25.733 27.410  1.00 52.09  ? 5   PHE C CG  1 
ATOM   1498 C CD1 . PHE C 1 6  ? 27.790  -26.465 27.223  1.00 57.40  ? 5   PHE C CD1 1 
ATOM   1499 C CD2 . PHE C 1 6  ? 26.198  -24.896 26.380  1.00 55.41  ? 5   PHE C CD2 1 
ATOM   1500 C CE1 . PHE C 1 6  ? 28.504  -26.389 26.031  1.00 58.48  ? 5   PHE C CE1 1 
ATOM   1501 C CE2 . PHE C 1 6  ? 26.909  -24.833 25.186  1.00 50.06  ? 5   PHE C CE2 1 
ATOM   1502 C CZ  . PHE C 1 6  ? 28.057  -25.571 25.013  1.00 51.21  ? 5   PHE C CZ  1 
ATOM   1503 N N   . LYS C 1 7  ? 24.231  -23.892 30.943  1.00 56.74  ? 6   LYS C N   1 
ATOM   1504 C CA  . LYS C 1 7  ? 23.282  -23.814 32.041  1.00 62.33  ? 6   LYS C CA  1 
ATOM   1505 C C   . LYS C 1 7  ? 21.912  -24.121 31.455  1.00 61.96  ? 6   LYS C C   1 
ATOM   1506 O O   . LYS C 1 7  ? 21.749  -24.013 30.239  1.00 65.47  ? 6   LYS C O   1 
ATOM   1507 C CB  . LYS C 1 7  ? 23.324  -22.409 32.662  1.00 67.45  ? 6   LYS C CB  1 
ATOM   1508 N N   . PRO C 1 8  ? 20.901  -24.551 32.250  1.00 61.43  ? 7   PRO C N   1 
ATOM   1509 C CA  . PRO C 1 8  ? 19.571  -24.815 31.698  1.00 57.94  ? 7   PRO C CA  1 
ATOM   1510 C C   . PRO C 1 8  ? 19.051  -23.599 30.937  1.00 64.77  ? 7   PRO C C   1 
ATOM   1511 O O   . PRO C 1 8  ? 19.320  -22.460 31.323  1.00 67.78  ? 7   PRO C O   1 
ATOM   1512 C CB  . PRO C 1 8  ? 18.713  -25.163 32.920  1.00 58.03  ? 7   PRO C CB  1 
ATOM   1513 C CG  . PRO C 1 8  ? 19.716  -25.683 33.926  1.00 57.74  ? 7   PRO C CG  1 
ATOM   1514 C CD  . PRO C 1 8  ? 20.984  -24.854 33.693  1.00 60.65  ? 7   PRO C CD  1 
ATOM   1515 N N   . GLY C 1 9  ? 18.354  -23.866 29.827  1.00 58.07  ? 8   GLY C N   1 
ATOM   1516 C CA  . GLY C 1 9  ? 17.700  -22.829 29.045  1.00 55.25  ? 8   GLY C CA  1 
ATOM   1517 C C   . GLY C 1 9  ? 18.488  -22.457 27.794  1.00 51.86  ? 8   GLY C C   1 
ATOM   1518 O O   . GLY C 1 9  ? 17.890  -22.092 26.789  1.00 61.16  ? 8   GLY C O   1 
ATOM   1519 N N   . ASP C 1 10 ? 19.816  -22.582 27.873  1.00 45.76  ? 9   ASP C N   1 
ATOM   1520 C CA  . ASP C 1 10 ? 20.760  -22.264 26.817  1.00 45.03  ? 9   ASP C CA  1 
ATOM   1521 C C   . ASP C 1 10 ? 20.404  -23.037 25.540  1.00 48.68  ? 9   ASP C C   1 
ATOM   1522 O O   . ASP C 1 10 ? 20.117  -24.241 25.599  1.00 39.66  ? 9   ASP C O   1 
ATOM   1523 C CB  . ASP C 1 10 ? 22.184  -22.541 27.273  1.00 48.07  ? 9   ASP C CB  1 
ATOM   1524 C CG  . ASP C 1 10 ? 22.671  -21.719 28.464  1.00 55.14  ? 9   ASP C CG  1 
ATOM   1525 O OD1 . ASP C 1 10 ? 21.933  -20.821 28.888  1.00 58.40  ? 9   ASP C OD1 1 
ATOM   1526 O OD2 . ASP C 1 10 ? 23.780  -21.992 28.963  1.00 60.90  ? 9   ASP C OD2 1 
ATOM   1527 N N   . LEU C 1 11 ? 20.411  -22.314 24.406  1.00 45.73  ? 10  LEU C N   1 
ATOM   1528 C CA  . LEU C 1 11 ? 20.152  -22.880 23.084  1.00 42.01  ? 10  LEU C CA  1 
ATOM   1529 C C   . LEU C 1 11 ? 21.455  -23.360 22.437  1.00 45.15  ? 10  LEU C C   1 
ATOM   1530 O O   . LEU C 1 11 ? 22.465  -22.657 22.459  1.00 45.69  ? 10  LEU C O   1 
ATOM   1531 C CB  . LEU C 1 11 ? 19.400  -21.829 22.251  1.00 37.50  ? 10  LEU C CB  1 
ATOM   1532 C CG  . LEU C 1 11 ? 18.109  -21.273 22.871  1.00 40.20  ? 10  LEU C CG  1 
ATOM   1533 C CD1 . LEU C 1 11 ? 17.436  -20.251 21.954  1.00 41.52  ? 10  LEU C CD1 1 
ATOM   1534 C CD2 . LEU C 1 11 ? 17.099  -22.358 23.300  1.00 39.61  ? 10  LEU C CD2 1 
ATOM   1535 N N   . VAL C 1 12 ? 21.434  -24.566 21.823  1.00 35.74  ? 11  VAL C N   1 
ATOM   1536 C CA  . VAL C 1 12 ? 22.648  -25.169 21.316  1.00 36.30  ? 11  VAL C CA  1 
ATOM   1537 C C   . VAL C 1 12 ? 22.343  -25.873 19.980  1.00 33.11  ? 11  VAL C C   1 
ATOM   1538 O O   . VAL C 1 12 ? 21.179  -26.036 19.651  1.00 35.82  ? 11  VAL C O   1 
ATOM   1539 C CB  . VAL C 1 12 ? 23.139  -26.217 22.338  1.00 33.85  ? 11  VAL C CB  1 
ATOM   1540 C CG1 . VAL C 1 12 ? 23.610  -25.603 23.663  1.00 37.38  ? 11  VAL C CG1 1 
ATOM   1541 C CG2 . VAL C 1 12 ? 22.069  -27.265 22.596  1.00 35.26  ? 11  VAL C CG2 1 
ATOM   1542 N N   . PHE C 1 13 ? 23.398  -26.258 19.257  1.00 33.91  ? 12  PHE C N   1 
ATOM   1543 C CA  . PHE C 1 13 ? 23.310  -27.408 18.350  1.00 32.29  ? 12  PHE C CA  1 
ATOM   1544 C C   . PHE C 1 13 ? 23.896  -28.616 19.076  1.00 33.26  ? 12  PHE C C   1 
ATOM   1545 O O   . PHE C 1 13 ? 25.001  -28.539 19.636  1.00 34.07  ? 12  PHE C O   1 
ATOM   1546 C CB  . PHE C 1 13 ? 23.965  -27.116 16.989  1.00 39.30  ? 12  PHE C CB  1 
ATOM   1547 C CG  . PHE C 1 13 ? 23.104  -26.177 16.157  1.00 41.82  ? 12  PHE C CG  1 
ATOM   1548 C CD1 . PHE C 1 13 ? 22.147  -26.688 15.284  1.00 44.77  ? 12  PHE C CD1 1 
ATOM   1549 C CD2 . PHE C 1 13 ? 23.259  -24.789 16.232  1.00 41.65  ? 12  PHE C CD2 1 
ATOM   1550 C CE1 . PHE C 1 13 ? 21.341  -25.841 14.540  1.00 45.14  ? 12  PHE C CE1 1 
ATOM   1551 C CE2 . PHE C 1 13 ? 22.427  -23.947 15.499  1.00 41.48  ? 12  PHE C CE2 1 
ATOM   1552 C CZ  . PHE C 1 13 ? 21.492  -24.480 14.636  1.00 40.03  ? 12  PHE C CZ  1 
ATOM   1553 N N   . ALA C 1 14 ? 23.159  -29.741 19.079  1.00 31.09  ? 13  ALA C N   1 
ATOM   1554 C CA  . ALA C 1 14 ? 23.636  -30.917 19.784  1.00 29.23  ? 13  ALA C CA  1 
ATOM   1555 C C   . ALA C 1 14 ? 23.916  -32.020 18.769  1.00 34.16  ? 13  ALA C C   1 
ATOM   1556 O O   . ALA C 1 14 ? 23.056  -32.267 17.903  1.00 31.75  ? 13  ALA C O   1 
ATOM   1557 C CB  . ALA C 1 14 ? 22.591  -31.357 20.748  1.00 29.87  ? 13  ALA C CB  1 
ATOM   1558 N N   . LYS C 1 15 ? 25.084  -32.664 18.934  1.00 31.65  ? 14  LYS C N   1 
ATOM   1559 C CA  . LYS C 1 15 ? 25.534  -33.685 17.992  1.00 29.96  ? 14  LYS C CA  1 
ATOM   1560 C C   . LYS C 1 15 ? 25.474  -35.071 18.628  1.00 31.65  ? 14  LYS C C   1 
ATOM   1561 O O   . LYS C 1 15 ? 26.226  -35.391 19.557  1.00 32.47  ? 14  LYS C O   1 
ATOM   1562 C CB  . LYS C 1 15 ? 26.911  -33.327 17.405  1.00 33.90  ? 14  LYS C CB  1 
ATOM   1563 C CG  . LYS C 1 15 ? 27.385  -34.339 16.340  1.00 33.60  ? 14  LYS C CG  1 
ATOM   1564 C CD  . LYS C 1 15 ? 26.584  -34.269 15.050  1.00 34.40  ? 14  LYS C CD  1 
ATOM   1565 C CE  . LYS C 1 15 ? 27.148  -35.131 13.947  1.00 36.60  ? 14  LYS C CE  1 
ATOM   1566 N NZ  . LYS C 1 15 ? 26.949  -36.564 14.137  1.00 36.80  ? 14  LYS C NZ  1 
ATOM   1567 N N   . MET C 1 16 ? 24.598  -35.926 18.077  1.00 27.66  ? 15  MET C N   1 
ATOM   1568 C CA  . MET C 1 16 ? 24.547  -37.345 18.412  1.00 28.66  ? 15  MET C CA  1 
ATOM   1569 C C   . MET C 1 16 ? 25.043  -38.161 17.216  1.00 35.58  ? 15  MET C C   1 
ATOM   1570 O O   . MET C 1 16 ? 24.870  -37.772 16.055  1.00 31.09  ? 15  MET C O   1 
ATOM   1571 C CB  . MET C 1 16 ? 23.086  -37.746 18.644  1.00 31.96  ? 15  MET C CB  1 
ATOM   1572 C CG  . MET C 1 16 ? 22.467  -37.134 19.873  1.00 37.85  ? 15  MET C CG  1 
ATOM   1573 S SD  . MET C 1 16 ? 20.837  -37.822 20.228  1.00 48.46  ? 15  MET C SD  1 
ATOM   1574 C CE  . MET C 1 16 ? 20.510  -39.360 19.364  1.00 35.00  ? 15  MET C CE  1 
ATOM   1575 N N   . LYS C 1 17 ? 25.617  -39.335 17.513  1.00 32.60  ? 16  LYS C N   1 
ATOM   1576 C CA  . LYS C 1 17 ? 26.058  -40.223 16.447  1.00 37.15  ? 16  LYS C CA  1 
ATOM   1577 C C   . LYS C 1 17 ? 24.835  -40.600 15.614  1.00 32.05  ? 16  LYS C C   1 
ATOM   1578 O O   . LYS C 1 17 ? 23.820  -41.072 16.136  1.00 32.12  ? 16  LYS C O   1 
ATOM   1579 C CB  . LYS C 1 17 ? 26.785  -41.449 17.014  1.00 36.39  ? 16  LYS C CB  1 
ATOM   1580 C CG  . LYS C 1 17 ? 27.428  -42.385 15.969  1.00 36.67  ? 16  LYS C CG  1 
ATOM   1581 C CD  . LYS C 1 17 ? 28.633  -41.755 15.284  1.00 44.36  ? 16  LYS C CD  1 
ATOM   1582 C CE  . LYS C 1 17 ? 29.371  -42.752 14.429  1.00 52.89  ? 16  LYS C CE  1 
ATOM   1583 N NZ  . LYS C 1 17 ? 30.659  -42.174 14.021  1.00 46.66  ? 16  LYS C NZ  1 
ATOM   1584 N N   . GLY C 1 18 ? 24.969  -40.404 14.310  1.00 38.15  ? 17  GLY C N   1 
ATOM   1585 C CA  . GLY C 1 18 ? 23.945  -40.906 13.411  1.00 38.21  ? 17  GLY C CA  1 
ATOM   1586 C C   . GLY C 1 18 ? 23.013  -39.791 12.949  1.00 35.07  ? 17  GLY C C   1 
ATOM   1587 O O   . GLY C 1 18 ? 22.066  -40.074 12.217  1.00 31.55  ? 17  GLY C O   1 
ATOM   1588 N N   . TYR C 1 19 ? 23.259  -38.551 13.425  1.00 30.71  ? 18  TYR C N   1 
ATOM   1589 C CA  . TYR C 1 19 ? 22.358  -37.433 13.138  1.00 30.06  ? 18  TYR C CA  1 
ATOM   1590 C C   . TYR C 1 19 ? 23.167  -36.167 12.921  1.00 31.51  ? 18  TYR C C   1 
ATOM   1591 O O   . TYR C 1 19 ? 24.242  -36.011 13.503  1.00 30.88  ? 18  TYR C O   1 
ATOM   1592 C CB  . TYR C 1 19 ? 21.485  -37.105 14.360  1.00 27.64  ? 18  TYR C CB  1 
ATOM   1593 C CG  . TYR C 1 19 ? 20.612  -38.282 14.748  1.00 31.08  ? 18  TYR C CG  1 
ATOM   1594 C CD1 . TYR C 1 19 ? 21.097  -39.285 15.585  1.00 31.59  ? 18  TYR C CD1 1 
ATOM   1595 C CD2 . TYR C 1 19 ? 19.320  -38.380 14.266  1.00 29.96  ? 18  TYR C CD2 1 
ATOM   1596 C CE1 . TYR C 1 19 ? 20.297  -40.362 15.941  1.00 30.07  ? 18  TYR C CE1 1 
ATOM   1597 C CE2 . TYR C 1 19 ? 18.515  -39.456 14.609  1.00 32.16  ? 18  TYR C CE2 1 
ATOM   1598 C CZ  . TYR C 1 19 ? 19.007  -40.433 15.448  1.00 33.79  ? 18  TYR C CZ  1 
ATOM   1599 O OH  . TYR C 1 19 ? 18.172  -41.492 15.711  1.00 40.25  ? 18  TYR C OH  1 
ATOM   1600 N N   . PRO C 1 20 ? 22.644  -35.227 12.110  1.00 31.77  ? 19  PRO C N   1 
ATOM   1601 C CA  . PRO C 1 20 ? 23.302  -33.935 11.907  1.00 30.69  ? 19  PRO C CA  1 
ATOM   1602 C C   . PRO C 1 20 ? 23.219  -33.122 13.202  1.00 34.33  ? 19  PRO C C   1 
ATOM   1603 O O   . PRO C 1 20 ? 22.407  -33.417 14.101  1.00 30.28  ? 19  PRO C O   1 
ATOM   1604 C CB  . PRO C 1 20 ? 22.449  -33.339 10.765  1.00 34.67  ? 19  PRO C CB  1 
ATOM   1605 C CG  . PRO C 1 20 ? 21.063  -33.881 11.031  1.00 33.60  ? 19  PRO C CG  1 
ATOM   1606 C CD  . PRO C 1 20 ? 21.361  -35.341 11.375  1.00 32.23  ? 19  PRO C CD  1 
ATOM   1607 N N   . HIS C 1 21 ? 24.076  -32.101 13.279  1.00 37.12  ? 20  HIS C N   1 
ATOM   1608 C CA  . HIS C 1 21 ? 24.018  -31.160 14.396  1.00 36.56  ? 20  HIS C CA  1 
ATOM   1609 C C   . HIS C 1 21 ? 22.599  -30.627 14.474  1.00 37.87  ? 20  HIS C C   1 
ATOM   1610 O O   . HIS C 1 21 ? 22.093  -30.079 13.493  1.00 34.13  ? 20  HIS C O   1 
ATOM   1611 C CB  . HIS C 1 21 ? 25.029  -30.023 14.194  1.00 38.85  ? 20  HIS C CB  1 
ATOM   1612 C CG  . HIS C 1 21 ? 26.434  -30.473 14.308  1.00 35.78  ? 20  HIS C CG  1 
ATOM   1613 N ND1 . HIS C 1 21 ? 27.118  -31.097 13.286  1.00 39.65  ? 20  HIS C ND1 1 
ATOM   1614 C CD2 . HIS C 1 21 ? 27.296  -30.398 15.352  1.00 38.58  ? 20  HIS C CD2 1 
ATOM   1615 C CE1 . HIS C 1 21 ? 28.339  -31.403 13.704  1.00 46.54  ? 20  HIS C CE1 1 
ATOM   1616 N NE2 . HIS C 1 21 ? 28.476  -30.945 14.940  1.00 42.15  ? 20  HIS C NE2 1 
ATOM   1617 N N   . TRP C 1 22 ? 21.985  -30.738 15.661  1.00 32.15  ? 21  TRP C N   1 
ATOM   1618 C CA  . TRP C 1 22 ? 20.541  -30.602 15.756  1.00 29.70  ? 21  TRP C CA  1 
ATOM   1619 C C   . TRP C 1 22 ? 20.125  -29.451 16.671  1.00 30.04  ? 21  TRP C C   1 
ATOM   1620 O O   . TRP C 1 22 ? 20.685  -29.317 17.780  1.00 31.42  ? 21  TRP C O   1 
ATOM   1621 C CB  . TRP C 1 22 ? 19.963  -31.909 16.308  1.00 28.49  ? 21  TRP C CB  1 
ATOM   1622 C CG  . TRP C 1 22 ? 18.528  -32.127 15.933  1.00 30.05  ? 21  TRP C CG  1 
ATOM   1623 C CD1 . TRP C 1 22 ? 17.414  -31.568 16.491  1.00 27.37  ? 21  TRP C CD1 1 
ATOM   1624 C CD2 . TRP C 1 22 ? 18.071  -32.998 14.866  1.00 29.48  ? 21  TRP C CD2 1 
ATOM   1625 N NE1 . TRP C 1 22 ? 16.292  -32.042 15.838  1.00 30.56  ? 21  TRP C NE1 1 
ATOM   1626 C CE2 . TRP C 1 22 ? 16.666  -32.902 14.839  1.00 31.03  ? 21  TRP C CE2 1 
ATOM   1627 C CE3 . TRP C 1 22 ? 18.717  -33.845 13.952  1.00 29.86  ? 21  TRP C CE3 1 
ATOM   1628 C CZ2 . TRP C 1 22 ? 15.889  -33.636 13.931  1.00 31.65  ? 21  TRP C CZ2 1 
ATOM   1629 C CZ3 . TRP C 1 22 ? 17.960  -34.539 13.029  1.00 31.89  ? 21  TRP C CZ3 1 
ATOM   1630 C CH2 . TRP C 1 22 ? 16.556  -34.421 13.018  1.00 31.28  ? 21  TRP C CH2 1 
ATOM   1631 N N   . PRO C 1 23 ? 19.133  -28.599 16.310  1.00 35.29  ? 22  PRO C N   1 
ATOM   1632 C CA  . PRO C 1 23 ? 18.721  -27.525 17.221  1.00 31.49  ? 22  PRO C CA  1 
ATOM   1633 C C   . PRO C 1 23 ? 18.154  -28.073 18.524  1.00 31.12  ? 22  PRO C C   1 
ATOM   1634 O O   . PRO C 1 23 ? 17.276  -28.954 18.515  1.00 29.37  ? 22  PRO C O   1 
ATOM   1635 C CB  . PRO C 1 23 ? 17.660  -26.772 16.358  1.00 31.53  ? 22  PRO C CB  1 
ATOM   1636 C CG  . PRO C 1 23 ? 17.063  -27.844 15.469  1.00 30.12  ? 22  PRO C CG  1 
ATOM   1637 C CD  . PRO C 1 23 ? 18.324  -28.608 15.053  1.00 30.87  ? 22  PRO C CD  1 
ATOM   1638 N N   . ALA C 1 24 ? 18.683  -27.572 19.659  1.00 30.85  ? 23  ALA C N   1 
ATOM   1639 C CA  . ALA C 1 24 ? 18.309  -28.167 20.937  1.00 33.33  ? 23  ALA C CA  1 
ATOM   1640 C C   . ALA C 1 24 ? 18.409  -27.143 22.061  1.00 33.64  ? 23  ALA C C   1 
ATOM   1641 O O   . ALA C 1 24 ? 18.883  -26.022 21.841  1.00 36.17  ? 23  ALA C O   1 
ATOM   1642 C CB  . ALA C 1 24 ? 19.198  -29.386 21.205  1.00 33.56  ? 23  ALA C CB  1 
ATOM   1643 N N   . ARG C 1 25 ? 17.995  -27.539 23.274  1.00 35.74  ? 24  ARG C N   1 
ATOM   1644 C CA  . ARG C 1 25 ? 18.276  -26.709 24.439  1.00 37.02  ? 24  ARG C CA  1 
ATOM   1645 C C   . ARG C 1 25 ? 18.711  -27.575 25.629  1.00 38.38  ? 24  ARG C C   1 
ATOM   1646 O O   . ARG C 1 25 ? 18.266  -28.722 25.744  1.00 40.29  ? 24  ARG C O   1 
ATOM   1647 C CB  . ARG C 1 25 ? 17.033  -25.921 24.854  1.00 35.76  ? 24  ARG C CB  1 
ATOM   1648 C CG  . ARG C 1 25 ? 15.800  -26.699 25.284  1.00 43.13  ? 24  ARG C CG  1 
ATOM   1649 C CD  . ARG C 1 25 ? 14.750  -25.833 25.961  1.00 50.88  ? 24  ARG C CD  1 
ATOM   1650 N NE  . ARG C 1 25 ? 13.564  -26.668 26.194  1.00 56.85  ? 24  ARG C NE  1 
ATOM   1651 C CZ  . ARG C 1 25 ? 12.300  -26.361 25.942  1.00 53.30  ? 24  ARG C CZ  1 
ATOM   1652 N NH1 . ARG C 1 25 ? 11.976  -25.177 25.442  1.00 51.82  ? 24  ARG C NH1 1 
ATOM   1653 N NH2 . ARG C 1 25 ? 11.359  -27.250 26.212  1.00 56.93  ? 24  ARG C NH2 1 
ATOM   1654 N N   . ILE C 1 26 ? 19.522  -26.989 26.515  1.00 36.79  ? 25  ILE C N   1 
ATOM   1655 C CA  . ILE C 1 26 ? 19.887  -27.614 27.794  1.00 41.43  ? 25  ILE C CA  1 
ATOM   1656 C C   . ILE C 1 26 ? 18.652  -27.656 28.684  1.00 42.66  ? 25  ILE C C   1 
ATOM   1657 O O   . ILE C 1 26 ? 18.053  -26.616 28.956  1.00 49.41  ? 25  ILE C O   1 
ATOM   1658 C CB  . ILE C 1 26 ? 21.008  -26.825 28.509  1.00 38.67  ? 25  ILE C CB  1 
ATOM   1659 C CG1 . ILE C 1 26 ? 22.224  -26.538 27.647  1.00 38.61  ? 25  ILE C CG1 1 
ATOM   1660 C CG2 . ILE C 1 26 ? 21.372  -27.449 29.867  1.00 43.60  ? 25  ILE C CG2 1 
ATOM   1661 C CD1 . ILE C 1 26 ? 22.983  -27.760 27.161  1.00 41.38  ? 25  ILE C CD1 1 
ATOM   1662 N N   . ASP C 1 27 ? 18.293  -28.852 29.164  1.00 47.27  ? 26  ASP C N   1 
ATOM   1663 C CA  . ASP C 1 27 ? 17.178  -28.981 30.087  1.00 58.90  ? 26  ASP C CA  1 
ATOM   1664 C C   . ASP C 1 27 ? 17.670  -28.838 31.523  1.00 60.02  ? 26  ASP C C   1 
ATOM   1665 O O   . ASP C 1 27 ? 18.877  -28.762 31.775  1.00 53.37  ? 26  ASP C O   1 
ATOM   1666 C CB  . ASP C 1 27 ? 16.423  -30.288 29.908  1.00 57.95  ? 26  ASP C CB  1 
ATOM   1667 C CG  . ASP C 1 27 ? 15.090  -30.179 29.184  1.00 66.71  ? 26  ASP C CG  1 
ATOM   1668 O OD1 . ASP C 1 27 ? 14.897  -29.167 28.469  1.00 67.80  ? 26  ASP C OD1 1 
ATOM   1669 O OD2 . ASP C 1 27 ? 14.241  -31.083 29.388  1.00 63.78  ? 26  ASP C OD2 1 
ATOM   1670 N N   . ASP C 1 28 ? 16.701  -28.783 32.445  1.00 68.04  ? 27  ASP C N   1 
ATOM   1671 C CA  . ASP C 1 28 ? 16.963  -28.943 33.864  1.00 72.43  ? 27  ASP C CA  1 
ATOM   1672 C C   . ASP C 1 28 ? 16.418  -30.302 34.283  1.00 72.50  ? 27  ASP C C   1 
ATOM   1673 O O   . ASP C 1 28 ? 15.363  -30.709 33.809  1.00 81.12  ? 27  ASP C O   1 
ATOM   1674 C CB  . ASP C 1 28 ? 16.353  -27.814 34.678  1.00 81.96  ? 27  ASP C CB  1 
ATOM   1675 C CG  . ASP C 1 28 ? 16.823  -27.708 36.123  1.00 90.30  ? 27  ASP C CG  1 
ATOM   1676 O OD1 . ASP C 1 28 ? 17.809  -28.394 36.484  1.00 92.26  ? 27  ASP C OD1 1 
ATOM   1677 O OD2 . ASP C 1 28 ? 16.195  -26.943 36.883  1.00 96.14  ? 27  ASP C OD2 1 
ATOM   1678 N N   . ILE C 1 29 ? 17.162  -30.989 35.159  1.00 79.26  ? 28  ILE C N   1 
ATOM   1679 C CA  . ILE C 1 29 ? 16.771  -32.288 35.685  1.00 70.41  ? 28  ILE C CA  1 
ATOM   1680 C C   . ILE C 1 29 ? 15.886  -32.052 36.918  1.00 66.71  ? 28  ILE C C   1 
ATOM   1681 O O   . ILE C 1 29 ? 16.376  -31.333 37.819  1.00 60.54  ? 28  ILE C O   1 
ATOM   1682 C CB  . ILE C 1 29 ? 18.018  -33.127 36.029  1.00 71.35  ? 28  ILE C CB  1 
ATOM   1683 N N   . ALA C 1 33 ? 15.033  -36.867 40.270  1.00 63.83  ? 32  ALA C N   1 
ATOM   1684 C CA  . ALA C 1 33 ? 15.257  -37.559 38.977  1.00 62.36  ? 32  ALA C CA  1 
ATOM   1685 C C   . ALA C 1 33 ? 16.477  -38.472 39.089  1.00 67.42  ? 32  ALA C C   1 
ATOM   1686 O O   . ALA C 1 33 ? 17.257  -38.364 40.037  1.00 63.98  ? 32  ALA C O   1 
ATOM   1687 C CB  . ALA C 1 33 ? 15.430  -36.544 37.854  1.00 56.12  ? 32  ALA C CB  1 
ATOM   1688 N N   . VAL C 1 34 ? 16.611  -39.382 38.111  1.00 70.66  ? 33  VAL C N   1 
ATOM   1689 C CA  . VAL C 1 34 ? 17.853  -40.095 37.845  1.00 74.50  ? 33  VAL C CA  1 
ATOM   1690 C C   . VAL C 1 34 ? 18.880  -39.067 37.370  1.00 74.71  ? 33  VAL C C   1 
ATOM   1691 O O   . VAL C 1 34 ? 18.562  -38.171 36.577  1.00 60.87  ? 33  VAL C O   1 
ATOM   1692 C CB  . VAL C 1 34 ? 17.719  -41.264 36.842  1.00 79.85  ? 33  VAL C CB  1 
ATOM   1693 C CG1 . VAL C 1 34 ? 19.064  -41.750 36.302  1.00 83.71  ? 33  VAL C CG1 1 
ATOM   1694 C CG2 . VAL C 1 34 ? 16.943  -42.436 37.430  1.00 89.47  ? 33  VAL C CG2 1 
ATOM   1695 N N   . LYS C 1 35 ? 20.109  -39.213 37.886  1.00 65.45  ? 34  LYS C N   1 
ATOM   1696 C CA  . LYS C 1 35 ? 21.185  -38.285 37.593  1.00 58.84  ? 34  LYS C CA  1 
ATOM   1697 C C   . LYS C 1 35 ? 21.701  -38.580 36.187  1.00 51.46  ? 34  LYS C C   1 
ATOM   1698 O O   . LYS C 1 35 ? 21.591  -39.707 35.700  1.00 53.95  ? 34  LYS C O   1 
ATOM   1699 C CB  . LYS C 1 35 ? 22.269  -38.392 38.675  1.00 59.92  ? 34  LYS C CB  1 
ATOM   1700 N N   . PRO C 1 36 ? 22.271  -37.572 35.490  1.00 47.58  ? 35  PRO C N   1 
ATOM   1701 C CA  . PRO C 1 36 ? 22.949  -37.820 34.220  1.00 52.64  ? 35  PRO C CA  1 
ATOM   1702 C C   . PRO C 1 36 ? 24.099  -38.777 34.522  1.00 53.21  ? 35  PRO C C   1 
ATOM   1703 O O   . PRO C 1 36 ? 24.560  -38.861 35.672  1.00 49.53  ? 35  PRO C O   1 
ATOM   1704 C CB  . PRO C 1 36 ? 23.448  -36.424 33.767  1.00 48.01  ? 35  PRO C CB  1 
ATOM   1705 C CG  . PRO C 1 36 ? 22.632  -35.438 34.578  1.00 50.48  ? 35  PRO C CG  1 
ATOM   1706 C CD  . PRO C 1 36 ? 22.280  -36.147 35.878  1.00 50.85  ? 35  PRO C CD  1 
ATOM   1707 N N   . PRO C 1 37 ? 24.610  -39.508 33.505  1.00 50.03  ? 36  PRO C N   1 
ATOM   1708 C CA  . PRO C 1 37 ? 25.912  -40.150 33.642  1.00 48.31  ? 36  PRO C CA  1 
ATOM   1709 C C   . PRO C 1 37 ? 26.850  -38.993 33.973  1.00 42.92  ? 36  PRO C C   1 
ATOM   1710 O O   . PRO C 1 37 ? 26.534  -37.819 33.715  1.00 41.16  ? 36  PRO C O   1 
ATOM   1711 C CB  . PRO C 1 37 ? 26.127  -40.719 32.238  1.00 46.70  ? 36  PRO C CB  1 
ATOM   1712 C CG  . PRO C 1 37 ? 24.717  -41.011 31.804  1.00 51.44  ? 36  PRO C CG  1 
ATOM   1713 C CD  . PRO C 1 37 ? 24.012  -39.721 32.174  1.00 47.70  ? 36  PRO C CD  1 
ATOM   1714 N N   . PRO C 1 38 ? 28.024  -39.271 34.586  1.00 40.88  ? 37  PRO C N   1 
ATOM   1715 C CA  . PRO C 1 38 ? 28.946  -38.200 34.958  1.00 39.08  ? 37  PRO C CA  1 
ATOM   1716 C C   . PRO C 1 38 ? 29.270  -37.310 33.766  1.00 35.48  ? 37  PRO C C   1 
ATOM   1717 O O   . PRO C 1 38 ? 29.573  -37.793 32.671  1.00 41.31  ? 37  PRO C O   1 
ATOM   1718 C CB  . PRO C 1 38 ? 30.169  -39.008 35.421  1.00 40.90  ? 37  PRO C CB  1 
ATOM   1719 C CG  . PRO C 1 38 ? 29.545  -40.273 35.971  1.00 40.16  ? 37  PRO C CG  1 
ATOM   1720 C CD  . PRO C 1 38 ? 28.533  -40.620 34.898  1.00 39.92  ? 37  PRO C CD  1 
ATOM   1721 N N   . ASN C 1 39 ? 29.212  -36.002 34.029  1.00 40.72  ? 38  ASN C N   1 
ATOM   1722 C CA  . ASN C 1 39 ? 29.649  -34.945 33.131  1.00 38.99  ? 38  ASN C CA  1 
ATOM   1723 C C   . ASN C 1 39 ? 28.813  -34.944 31.848  1.00 41.66  ? 38  ASN C C   1 
ATOM   1724 O O   . ASN C 1 39 ? 29.339  -34.587 30.794  1.00 45.81  ? 38  ASN C O   1 
ATOM   1725 C CB  . ASN C 1 39 ? 31.128  -35.065 32.777  1.00 48.03  ? 38  ASN C CB  1 
ATOM   1726 C CG  . ASN C 1 39 ? 31.704  -33.827 32.124  1.00 54.48  ? 38  ASN C CG  1 
ATOM   1727 O OD1 . ASN C 1 39 ? 31.313  -32.707 32.466  1.00 59.71  ? 38  ASN C OD1 1 
ATOM   1728 N ND2 . ASN C 1 39 ? 32.628  -33.997 31.187  1.00 57.41  ? 38  ASN C ND2 1 
ATOM   1729 N N   . LYS C 1 40 ? 27.521  -35.300 31.949  1.00 35.20  ? 39  LYS C N   1 
ATOM   1730 C CA  . LYS C 1 40 ? 26.622  -35.158 30.806  1.00 32.12  ? 39  LYS C CA  1 
ATOM   1731 C C   . LYS C 1 40 ? 25.503  -34.180 31.149  1.00 33.05  ? 39  LYS C C   1 
ATOM   1732 O O   . LYS C 1 40 ? 25.085  -34.075 32.295  1.00 36.46  ? 39  LYS C O   1 
ATOM   1733 C CB  . LYS C 1 40 ? 25.901  -36.486 30.524  1.00 33.99  ? 39  LYS C CB  1 
ATOM   1734 C CG  . LYS C 1 40 ? 26.888  -37.562 30.217  1.00 35.48  ? 39  LYS C CG  1 
ATOM   1735 C CD  . LYS C 1 40 ? 27.225  -37.719 28.749  1.00 41.75  ? 39  LYS C CD  1 
ATOM   1736 C CE  . LYS C 1 40 ? 28.279  -38.790 28.549  1.00 43.71  ? 39  LYS C CE  1 
ATOM   1737 N NZ  . LYS C 1 40 ? 29.100  -38.505 27.368  1.00 50.04  ? 39  LYS C NZ  1 
ATOM   1738 N N   . TYR C 1 41 ? 24.979  -33.487 30.127  1.00 32.52  ? 40  TYR C N   1 
ATOM   1739 C CA  . TYR C 1 41 ? 23.869  -32.546 30.274  1.00 34.64  ? 40  TYR C CA  1 
ATOM   1740 C C   . TYR C 1 41 ? 22.596  -33.193 29.731  1.00 37.63  ? 40  TYR C C   1 
ATOM   1741 O O   . TYR C 1 41 ? 22.697  -33.929 28.752  1.00 35.24  ? 40  TYR C O   1 
ATOM   1742 C CB  . TYR C 1 41 ? 24.046  -31.315 29.375  1.00 32.09  ? 40  TYR C CB  1 
ATOM   1743 C CG  . TYR C 1 41 ? 25.199  -30.421 29.800  1.00 38.28  ? 40  TYR C CG  1 
ATOM   1744 C CD1 . TYR C 1 41 ? 26.500  -30.676 29.366  1.00 39.88  ? 40  TYR C CD1 1 
ATOM   1745 C CD2 . TYR C 1 41 ? 24.997  -29.339 30.659  1.00 41.34  ? 40  TYR C CD2 1 
ATOM   1746 C CE1 . TYR C 1 41 ? 27.577  -29.913 29.790  1.00 44.85  ? 40  TYR C CE1 1 
ATOM   1747 C CE2 . TYR C 1 41 ? 26.066  -28.560 31.070  1.00 40.85  ? 40  TYR C CE2 1 
ATOM   1748 C CZ  . TYR C 1 41 ? 27.350  -28.846 30.644  1.00 47.09  ? 40  TYR C CZ  1 
ATOM   1749 O OH  . TYR C 1 41 ? 28.397  -28.095 31.066  1.00 48.92  ? 40  TYR C OH  1 
ATOM   1750 N N   . PRO C 1 42 ? 21.393  -32.892 30.304  1.00 35.92  ? 41  PRO C N   1 
ATOM   1751 C CA  . PRO C 1 42 ? 20.100  -33.337 29.760  1.00 34.36  ? 41  PRO C CA  1 
ATOM   1752 C C   . PRO C 1 42 ? 19.765  -32.429 28.583  1.00 36.81  ? 41  PRO C C   1 
ATOM   1753 O O   . PRO C 1 42 ? 19.780  -31.212 28.730  1.00 37.01  ? 41  PRO C O   1 
ATOM   1754 C CB  . PRO C 1 42 ? 19.088  -33.150 30.909  1.00 37.99  ? 41  PRO C CB  1 
ATOM   1755 C CG  . PRO C 1 42 ? 19.768  -32.193 31.848  1.00 41.81  ? 41  PRO C CG  1 
ATOM   1756 C CD  . PRO C 1 42 ? 21.228  -32.015 31.484  1.00 43.16  ? 41  PRO C CD  1 
ATOM   1757 N N   . ILE C 1 43 ? 19.489  -33.040 27.422  1.00 32.09  ? 42  ILE C N   1 
ATOM   1758 C CA  . ILE C 1 43 ? 19.260  -32.222 26.227  1.00 30.85  ? 42  ILE C CA  1 
ATOM   1759 C C   . ILE C 1 43 ? 17.822  -32.465 25.768  1.00 33.61  ? 42  ILE C C   1 
ATOM   1760 O O   . ILE C 1 43 ? 17.343  -33.609 25.764  1.00 37.42  ? 42  ILE C O   1 
ATOM   1761 C CB  . ILE C 1 43 ? 20.279  -32.576 25.125  1.00 28.49  ? 42  ILE C CB  1 
ATOM   1762 C CG1 . ILE C 1 43 ? 21.755  -32.432 25.560  1.00 31.47  ? 42  ILE C CG1 1 
ATOM   1763 C CG2 . ILE C 1 43 ? 19.980  -31.805 23.816  1.00 31.26  ? 42  ILE C CG2 1 
ATOM   1764 C CD1 . ILE C 1 43 ? 22.181  -31.022 25.932  1.00 33.72  ? 42  ILE C CD1 1 
ATOM   1765 N N   . PHE C 1 44 ? 17.134  -31.394 25.310  1.00 33.23  ? 43  PHE C N   1 
ATOM   1766 C CA  . PHE C 1 44 ? 15.838  -31.560 24.662  1.00 32.50  ? 43  PHE C CA  1 
ATOM   1767 C C   . PHE C 1 44 ? 16.008  -31.088 23.217  1.00 32.83  ? 43  PHE C C   1 
ATOM   1768 O O   . PHE C 1 44 ? 16.660  -30.059 22.991  1.00 32.26  ? 43  PHE C O   1 
ATOM   1769 C CB  . PHE C 1 44 ? 14.847  -30.611 25.337  1.00 35.92  ? 43  PHE C CB  1 
ATOM   1770 C CG  . PHE C 1 44 ? 13.488  -30.502 24.655  1.00 39.98  ? 43  PHE C CG  1 
ATOM   1771 C CD1 . PHE C 1 44 ? 12.497  -31.454 24.882  1.00 41.39  ? 43  PHE C CD1 1 
ATOM   1772 C CD2 . PHE C 1 44 ? 13.210  -29.435 23.796  1.00 45.98  ? 43  PHE C CD2 1 
ATOM   1773 C CE1 . PHE C 1 44 ? 11.262  -31.360 24.250  1.00 43.54  ? 43  PHE C CE1 1 
ATOM   1774 C CE2 . PHE C 1 44 ? 11.969  -29.341 23.171  1.00 39.87  ? 43  PHE C CE2 1 
ATOM   1775 C CZ  . PHE C 1 44 ? 11.003  -30.300 23.401  1.00 45.94  ? 43  PHE C CZ  1 
ATOM   1776 N N   . PHE C 1 45 ? 15.542  -31.920 22.276  1.00 31.42  ? 44  PHE C N   1 
ATOM   1777 C CA  . PHE C 1 45 ? 15.805  -31.697 20.854  1.00 31.79  ? 44  PHE C CA  1 
ATOM   1778 C C   . PHE C 1 45 ? 14.530  -31.099 20.256  1.00 30.20  ? 44  PHE C C   1 
ATOM   1779 O O   . PHE C 1 45 ? 13.455  -31.663 20.374  1.00 36.24  ? 44  PHE C O   1 
ATOM   1780 C CB  . PHE C 1 45 ? 16.212  -32.980 20.131  1.00 32.26  ? 44  PHE C CB  1 
ATOM   1781 C CG  . PHE C 1 45 ? 17.569  -33.547 20.512  1.00 30.33  ? 44  PHE C CG  1 
ATOM   1782 C CD1 . PHE C 1 45 ? 18.703  -33.267 19.737  1.00 30.70  ? 44  PHE C CD1 1 
ATOM   1783 C CD2 . PHE C 1 45 ? 17.707  -34.389 21.625  1.00 29.74  ? 44  PHE C CD2 1 
ATOM   1784 C CE1 . PHE C 1 45 ? 19.959  -33.794 20.045  1.00 33.85  ? 44  PHE C CE1 1 
ATOM   1785 C CE2 . PHE C 1 45 ? 18.967  -34.897 21.944  1.00 35.16  ? 44  PHE C CE2 1 
ATOM   1786 C CZ  . PHE C 1 45 ? 20.085  -34.598 21.159  1.00 32.84  ? 44  PHE C CZ  1 
ATOM   1787 N N   . PHE C 1 46 ? 14.659  -29.894 19.664  1.00 35.96  ? 45  PHE C N   1 
ATOM   1788 C CA  . PHE C 1 46 ? 13.495  -29.284 19.037  1.00 33.71  ? 45  PHE C CA  1 
ATOM   1789 C C   . PHE C 1 46 ? 13.072  -30.088 17.814  1.00 34.47  ? 45  PHE C C   1 
ATOM   1790 O O   . PHE C 1 46 ? 13.878  -30.808 17.204  1.00 33.46  ? 45  PHE C O   1 
ATOM   1791 C CB  . PHE C 1 46 ? 13.831  -27.850 18.618  1.00 33.63  ? 45  PHE C CB  1 
ATOM   1792 C CG  . PHE C 1 46 ? 14.138  -26.877 19.747  1.00 33.73  ? 45  PHE C CG  1 
ATOM   1793 C CD1 . PHE C 1 46 ? 13.125  -26.363 20.561  1.00 40.90  ? 45  PHE C CD1 1 
ATOM   1794 C CD2 . PHE C 1 46 ? 15.436  -26.392 19.901  1.00 31.20  ? 45  PHE C CD2 1 
ATOM   1795 C CE1 . PHE C 1 46 ? 13.432  -25.431 21.558  1.00 35.01  ? 45  PHE C CE1 1 
ATOM   1796 C CE2 . PHE C 1 46 ? 15.735  -25.482 20.911  1.00 38.37  ? 45  PHE C CE2 1 
ATOM   1797 C CZ  . PHE C 1 46 ? 14.725  -24.987 21.718  1.00 32.90  ? 45  PHE C CZ  1 
ATOM   1798 N N   . GLY C 1 47 ? 11.800  -29.916 17.427  1.00 32.59  ? 46  GLY C N   1 
ATOM   1799 C CA  . GLY C 1 47 ? 11.262  -30.660 16.300  1.00 34.54  ? 46  GLY C CA  1 
ATOM   1800 C C   . GLY C 1 47 ? 10.838  -32.072 16.695  1.00 38.96  ? 46  GLY C C   1 
ATOM   1801 O O   . GLY C 1 47 ? 9.655   -32.391 16.640  1.00 42.64  ? 46  GLY C O   1 
ATOM   1802 N N   . THR C 1 48 ? 11.803  -32.925 17.086  1.00 35.51  ? 47  THR C N   1 
ATOM   1803 C CA  . THR C 1 48 ? 11.477  -34.283 17.503  1.00 33.69  ? 47  THR C CA  1 
ATOM   1804 C C   . THR C 1 48 ? 10.901  -34.287 18.923  1.00 34.98  ? 47  THR C C   1 
ATOM   1805 O O   . THR C 1 48 ? 10.128  -35.180 19.251  1.00 42.59  ? 47  THR C O   1 
ATOM   1806 C CB  . THR C 1 48 ? 12.696  -35.206 17.363  1.00 34.28  ? 47  THR C CB  1 
ATOM   1807 O OG1 . THR C 1 48 ? 13.664  -34.696 18.269  1.00 35.56  ? 47  THR C OG1 1 
ATOM   1808 C CG2 . THR C 1 48 ? 13.268  -35.268 15.959  1.00 34.74  ? 47  THR C CG2 1 
ATOM   1809 N N   . HIS C 1 49 ? 11.294  -33.328 19.764  1.00 37.23  ? 48  HIS C N   1 
ATOM   1810 C CA  . HIS C 1 49 ? 10.904  -33.230 21.175  1.00 40.13  ? 48  HIS C CA  1 
ATOM   1811 C C   . HIS C 1 49 ? 11.420  -34.421 21.992  1.00 40.59  ? 48  HIS C C   1 
ATOM   1812 O O   . HIS C 1 49 ? 10.874  -34.730 23.054  1.00 42.21  ? 48  HIS C O   1 
ATOM   1813 C CB  . HIS C 1 49 ? 9.397   -32.972 21.352  1.00 39.59  ? 48  HIS C CB  1 
ATOM   1814 C CG  . HIS C 1 49 ? 8.867   -31.898 20.457  1.00 49.17  ? 48  HIS C CG  1 
ATOM   1815 N ND1 . HIS C 1 49 ? 7.653   -32.013 19.805  1.00 52.04  ? 48  HIS C ND1 1 
ATOM   1816 C CD2 . HIS C 1 49 ? 9.375   -30.709 20.097  1.00 48.84  ? 48  HIS C CD2 1 
ATOM   1817 C CE1 . HIS C 1 49 ? 7.449   -30.926 19.069  1.00 56.50  ? 48  HIS C CE1 1 
ATOM   1818 N NE2 . HIS C 1 49 ? 8.478   -30.115 19.230  1.00 47.57  ? 48  HIS C NE2 1 
ATOM   1819 N N   . GLU C 1 50 ? 12.494  -35.066 21.517  1.00 39.82  ? 49  GLU C N   1 
ATOM   1820 C CA  . GLU C 1 50 ? 13.151  -36.127 22.277  1.00 40.04  ? 49  GLU C CA  1 
ATOM   1821 C C   . GLU C 1 50 ? 14.156  -35.558 23.289  1.00 36.41  ? 49  GLU C C   1 
ATOM   1822 O O   . GLU C 1 50 ? 14.490  -34.370 23.292  1.00 34.59  ? 49  GLU C O   1 
ATOM   1823 C CB  . GLU C 1 50 ? 13.681  -37.151 21.272  1.00 49.14  ? 49  GLU C CB  1 
ATOM   1824 C CG  . GLU C 1 50 ? 12.549  -37.984 20.674  1.00 62.30  ? 49  GLU C CG  1 
ATOM   1825 C CD  . GLU C 1 50 ? 12.897  -38.877 19.502  1.00 73.91  ? 49  GLU C CD  1 
ATOM   1826 O OE1 . GLU C 1 50 ? 14.083  -38.936 19.131  1.00 90.46  ? 49  GLU C OE1 1 
ATOM   1827 O OE2 . GLU C 1 50 ? 11.969  -39.503 18.944  1.00 84.58  ? 49  GLU C OE2 1 
ATOM   1828 N N   . THR C 1 51 ? 14.565  -36.392 24.260  1.00 39.37  ? 50  THR C N   1 
ATOM   1829 C CA  . THR C 1 51 ? 15.580  -35.995 25.235  1.00 36.03  ? 50  THR C CA  1 
ATOM   1830 C C   . THR C 1 51 ? 16.680  -37.064 25.210  1.00 32.74  ? 50  THR C C   1 
ATOM   1831 O O   . THR C 1 51 ? 16.401  -38.229 24.926  1.00 38.87  ? 50  THR C O   1 
ATOM   1832 C CB  . THR C 1 51 ? 15.016  -35.879 26.658  1.00 38.74  ? 50  THR C CB  1 
ATOM   1833 O OG1 . THR C 1 51 ? 14.416  -37.155 26.885  1.00 43.95  ? 50  THR C OG1 1 
ATOM   1834 C CG2 . THR C 1 51 ? 14.061  -34.711 26.871  1.00 43.70  ? 50  THR C CG2 1 
ATOM   1835 N N   . ALA C 1 52 ? 17.925  -36.642 25.462  1.00 33.77  ? 51  ALA C N   1 
ATOM   1836 C CA  . ALA C 1 52 ? 19.071  -37.528 25.679  1.00 36.07  ? 51  ALA C CA  1 
ATOM   1837 C C   . ALA C 1 52 ? 20.075  -36.835 26.597  1.00 38.73  ? 51  ALA C C   1 
ATOM   1838 O O   . ALA C 1 52 ? 19.901  -35.673 26.952  1.00 37.97  ? 51  ALA C O   1 
ATOM   1839 C CB  . ALA C 1 52 ? 19.727  -37.948 24.381  1.00 36.61  ? 51  ALA C CB  1 
ATOM   1840 N N   . PHE C 1 53 ? 21.124  -37.563 27.004  1.00 37.27  ? 52  PHE C N   1 
ATOM   1841 C CA  . PHE C 1 53 ? 22.219  -36.926 27.725  1.00 38.23  ? 52  PHE C CA  1 
ATOM   1842 C C   . PHE C 1 53 ? 23.432  -36.843 26.816  1.00 37.39  ? 52  PHE C C   1 
ATOM   1843 O O   . PHE C 1 53 ? 23.802  -37.839 26.191  1.00 40.68  ? 52  PHE C O   1 
ATOM   1844 C CB  . PHE C 1 53 ? 22.652  -37.845 28.865  1.00 40.21  ? 52  PHE C CB  1 
ATOM   1845 C CG  . PHE C 1 53 ? 21.633  -37.902 29.987  1.00 37.90  ? 52  PHE C CG  1 
ATOM   1846 C CD1 . PHE C 1 53 ? 21.322  -36.761 30.722  1.00 39.83  ? 52  PHE C CD1 1 
ATOM   1847 C CD2 . PHE C 1 53 ? 21.007  -39.106 30.312  1.00 51.64  ? 52  PHE C CD2 1 
ATOM   1848 C CE1 . PHE C 1 53 ? 20.415  -36.818 31.771  1.00 44.08  ? 52  PHE C CE1 1 
ATOM   1849 C CE2 . PHE C 1 53 ? 20.101  -39.151 31.364  1.00 48.54  ? 52  PHE C CE2 1 
ATOM   1850 C CZ  . PHE C 1 53 ? 19.812  -38.005 32.084  1.00 43.94  ? 52  PHE C CZ  1 
ATOM   1851 N N   . LEU C 1 54 ? 24.082  -35.672 26.793  1.00 33.10  ? 53  LEU C N   1 
ATOM   1852 C CA  . LEU C 1 54 ? 25.252  -35.472 25.958  1.00 33.59  ? 53  LEU C CA  1 
ATOM   1853 C C   . LEU C 1 54 ? 26.328  -34.744 26.764  1.00 32.16  ? 53  LEU C C   1 
ATOM   1854 O O   . LEU C 1 54 ? 26.015  -33.977 27.688  1.00 33.03  ? 53  LEU C O   1 
ATOM   1855 C CB  . LEU C 1 54 ? 24.874  -34.692 24.695  1.00 33.49  ? 53  LEU C CB  1 
ATOM   1856 C CG  . LEU C 1 54 ? 24.074  -35.459 23.636  1.00 34.94  ? 53  LEU C CG  1 
ATOM   1857 C CD1 . LEU C 1 54 ? 23.888  -34.544 22.464  1.00 35.54  ? 53  LEU C CD1 1 
ATOM   1858 C CD2 . LEU C 1 54 ? 24.760  -36.784 23.197  1.00 37.66  ? 53  LEU C CD2 1 
ATOM   1859 N N   . GLY C 1 55 ? 27.588  -35.000 26.391  1.00 34.95  ? 54  GLY C N   1 
ATOM   1860 C CA  . GLY C 1 55 ? 28.732  -34.353 27.024  1.00 38.34  ? 54  GLY C CA  1 
ATOM   1861 C C   . GLY C 1 55 ? 29.071  -33.054 26.301  1.00 40.29  ? 54  GLY C C   1 
ATOM   1862 O O   . GLY C 1 55 ? 28.596  -32.816 25.177  1.00 36.94  ? 54  GLY C O   1 
ATOM   1863 N N   . PRO C 1 56 ? 29.854  -32.130 26.920  1.00 43.06  ? 55  PRO C N   1 
ATOM   1864 C CA  . PRO C 1 56 ? 30.010  -30.789 26.366  1.00 42.88  ? 55  PRO C CA  1 
ATOM   1865 C C   . PRO C 1 56 ? 30.687  -30.742 25.001  1.00 37.68  ? 55  PRO C C   1 
ATOM   1866 O O   . PRO C 1 56 ? 30.455  -29.791 24.263  1.00 48.58  ? 55  PRO C O   1 
ATOM   1867 C CB  . PRO C 1 56 ? 30.818  -30.040 27.465  1.00 41.74  ? 55  PRO C CB  1 
ATOM   1868 C CG  . PRO C 1 56 ? 31.624  -31.143 28.109  1.00 40.65  ? 55  PRO C CG  1 
ATOM   1869 C CD  . PRO C 1 56 ? 30.621  -32.300 28.174  1.00 45.71  ? 55  PRO C CD  1 
ATOM   1870 N N   . LYS C 1 57 ? 31.475  -31.770 24.651  1.00 42.62  ? 56  LYS C N   1 
ATOM   1871 C CA  . LYS C 1 57 ? 32.118  -31.759 23.339  1.00 47.25  ? 56  LYS C CA  1 
ATOM   1872 C C   . LYS C 1 57 ? 31.058  -31.813 22.237  1.00 53.04  ? 56  LYS C C   1 
ATOM   1873 O O   . LYS C 1 57 ? 31.300  -31.393 21.100  1.00 49.87  ? 56  LYS C O   1 
ATOM   1874 C CB  . LYS C 1 57 ? 33.056  -32.938 23.057  1.00 46.24  ? 56  LYS C CB  1 
ATOM   1875 N N   . ASP C 1 58 ? 29.883  -32.347 22.586  1.00 48.20  ? 57  ASP C N   1 
ATOM   1876 C CA  . ASP C 1 58 ? 28.853  -32.584 21.589  1.00 47.73  ? 57  ASP C CA  1 
ATOM   1877 C C   . ASP C 1 58 ? 27.936  -31.378 21.423  1.00 43.46  ? 57  ASP C C   1 
ATOM   1878 O O   . ASP C 1 58 ? 26.984  -31.481 20.658  1.00 36.28  ? 57  ASP C O   1 
ATOM   1879 C CB  . ASP C 1 58 ? 28.032  -33.825 21.898  1.00 44.16  ? 57  ASP C CB  1 
ATOM   1880 C CG  . ASP C 1 58 ? 28.860  -35.093 21.990  1.00 47.76  ? 57  ASP C CG  1 
ATOM   1881 O OD1 . ASP C 1 58 ? 29.810  -35.214 21.190  1.00 48.03  ? 57  ASP C OD1 1 
ATOM   1882 O OD2 . ASP C 1 58 ? 28.536  -35.927 22.845  1.00 47.82  ? 57  ASP C OD2 1 
ATOM   1883 N N   . LEU C 1 59 ? 28.236  -30.252 22.096  1.00 36.43  ? 58  LEU C N   1 
ATOM   1884 C CA  . LEU C 1 59 ? 27.311  -29.132 22.205  1.00 37.93  ? 58  LEU C CA  1 
ATOM   1885 C C   . LEU C 1 59 ? 27.941  -27.848 21.666  1.00 45.61  ? 58  LEU C C   1 
ATOM   1886 O O   . LEU C 1 59 ? 29.134  -27.624 21.879  1.00 50.99  ? 58  LEU C O   1 
ATOM   1887 C CB  . LEU C 1 59 ? 26.821  -28.951 23.648  1.00 35.67  ? 58  LEU C CB  1 
ATOM   1888 C CG  . LEU C 1 59 ? 26.280  -30.230 24.300  1.00 35.11  ? 58  LEU C CG  1 
ATOM   1889 C CD1 . LEU C 1 59 ? 26.017  -30.085 25.795  1.00 34.69  ? 58  LEU C CD1 1 
ATOM   1890 C CD2 . LEU C 1 59 ? 25.001  -30.696 23.599  1.00 31.59  ? 58  LEU C CD2 1 
ATOM   1891 N N   . PHE C 1 60 ? 27.126  -27.011 20.997  1.00 44.16  ? 59  PHE C N   1 
ATOM   1892 C CA  . PHE C 1 60 ? 27.587  -25.781 20.355  1.00 44.10  ? 59  PHE C CA  1 
ATOM   1893 C C   . PHE C 1 60 ? 26.580  -24.663 20.614  1.00 44.02  ? 59  PHE C C   1 
ATOM   1894 O O   . PHE C 1 60 ? 25.403  -24.793 20.287  1.00 45.05  ? 59  PHE C O   1 
ATOM   1895 C CB  . PHE C 1 60 ? 27.809  -26.002 18.851  1.00 44.43  ? 59  PHE C CB  1 
ATOM   1896 C CG  . PHE C 1 60 ? 28.768  -27.143 18.538  1.00 40.48  ? 59  PHE C CG  1 
ATOM   1897 C CD1 . PHE C 1 60 ? 28.345  -28.469 18.559  1.00 41.73  ? 59  PHE C CD1 1 
ATOM   1898 C CD2 . PHE C 1 60 ? 30.115  -26.900 18.280  1.00 47.20  ? 59  PHE C CD2 1 
ATOM   1899 C CE1 . PHE C 1 60 ? 29.241  -29.511 18.318  1.00 41.26  ? 59  PHE C CE1 1 
ATOM   1900 C CE2 . PHE C 1 60 ? 30.998  -27.947 18.014  1.00 46.10  ? 59  PHE C CE2 1 
ATOM   1901 C CZ  . PHE C 1 60 ? 30.561  -29.251 18.038  1.00 47.18  ? 59  PHE C CZ  1 
ATOM   1902 N N   . PRO C 1 61 ? 26.984  -23.503 21.196  1.00 42.69  ? 60  PRO C N   1 
ATOM   1903 C CA  . PRO C 1 61 ? 26.020  -22.441 21.498  1.00 43.86  ? 60  PRO C CA  1 
ATOM   1904 C C   . PRO C 1 61 ? 25.327  -22.007 20.204  1.00 40.14  ? 60  PRO C C   1 
ATOM   1905 O O   . PRO C 1 61 ? 25.963  -21.908 19.154  1.00 42.24  ? 60  PRO C O   1 
ATOM   1906 C CB  . PRO C 1 61 ? 26.841  -21.295 22.152  1.00 45.82  ? 60  PRO C CB  1 
ATOM   1907 C CG  . PRO C 1 61 ? 28.223  -21.894 22.348  1.00 41.30  ? 60  PRO C CG  1 
ATOM   1908 C CD  . PRO C 1 61 ? 28.379  -23.144 21.497  1.00 47.56  ? 60  PRO C CD  1 
ATOM   1909 N N   . TYR C 1 62 ? 24.003  -21.804 20.292  1.00 47.06  ? 61  TYR C N   1 
ATOM   1910 C CA  . TYR C 1 62 ? 23.164  -21.572 19.125  1.00 43.71  ? 61  TYR C CA  1 
ATOM   1911 C C   . TYR C 1 62 ? 23.649  -20.330 18.385  1.00 58.19  ? 61  TYR C C   1 
ATOM   1912 O O   . TYR C 1 62 ? 23.917  -20.382 17.180  1.00 62.08  ? 61  TYR C O   1 
ATOM   1913 C CB  . TYR C 1 62 ? 21.751  -21.201 19.567  1.00 42.63  ? 61  TYR C CB  1 
ATOM   1914 C CG  . TYR C 1 62 ? 20.790  -20.875 18.430  1.00 48.16  ? 61  TYR C CG  1 
ATOM   1915 C CD1 . TYR C 1 62 ? 20.582  -21.763 17.369  1.00 49.90  ? 61  TYR C CD1 1 
ATOM   1916 C CD2 . TYR C 1 62 ? 20.086  -19.678 18.420  1.00 50.11  ? 61  TYR C CD2 1 
ATOM   1917 C CE1 . TYR C 1 62 ? 19.690  -21.469 16.343  1.00 44.70  ? 61  TYR C CE1 1 
ATOM   1918 C CE2 . TYR C 1 62 ? 19.199  -19.372 17.399  1.00 50.14  ? 61  TYR C CE2 1 
ATOM   1919 C CZ  . TYR C 1 62 ? 18.997  -20.266 16.360  1.00 46.54  ? 61  TYR C CZ  1 
ATOM   1920 O OH  . TYR C 1 62 ? 18.097  -19.931 15.381  1.00 47.14  ? 61  TYR C OH  1 
ATOM   1921 N N   . ASP C 1 63 ? 23.752  -19.218 19.130  1.00 57.10  ? 62  ASP C N   1 
ATOM   1922 C CA  . ASP C 1 63 ? 24.103  -17.939 18.531  1.00 54.01  ? 62  ASP C CA  1 
ATOM   1923 C C   . ASP C 1 63 ? 25.401  -18.039 17.737  1.00 48.40  ? 62  ASP C C   1 
ATOM   1924 O O   . ASP C 1 63 ? 25.442  -17.620 16.579  1.00 56.69  ? 62  ASP C O   1 
ATOM   1925 C CB  . ASP C 1 63 ? 23.885  -16.771 19.480  1.00 61.00  ? 62  ASP C CB  1 
ATOM   1926 C CG  . ASP C 1 63 ? 22.559  -16.069 19.231  1.00 75.02  ? 62  ASP C CG  1 
ATOM   1927 O OD1 . ASP C 1 63 ? 21.691  -16.100 20.135  1.00 71.65  ? 62  ASP C OD1 1 
ATOM   1928 O OD2 . ASP C 1 63 ? 22.393  -15.532 18.108  1.00 83.83  ? 62  ASP C OD2 1 
ATOM   1929 N N   . LYS C 1 64 ? 26.429  -18.640 18.335  1.00 44.74  ? 63  LYS C N   1 
ATOM   1930 C CA  . LYS C 1 64 ? 27.754  -18.693 17.739  1.00 47.33  ? 63  LYS C CA  1 
ATOM   1931 C C   . LYS C 1 64 ? 27.765  -19.552 16.475  1.00 50.33  ? 63  LYS C C   1 
ATOM   1932 O O   . LYS C 1 64 ? 28.532  -19.265 15.557  1.00 44.68  ? 63  LYS C O   1 
ATOM   1933 C CB  . LYS C 1 64 ? 28.834  -19.165 18.726  1.00 54.50  ? 63  LYS C CB  1 
ATOM   1934 N N   . SER C 1 65 ? 26.898  -20.585 16.403  1.00 42.46  ? 64  SER C N   1 
ATOM   1935 C CA  . SER C 1 65 ? 27.070  -21.589 15.359  1.00 42.17  ? 64  SER C CA  1 
ATOM   1936 C C   . SER C 1 65 ? 25.892  -21.683 14.377  1.00 41.33  ? 64  SER C C   1 
ATOM   1937 O O   . SER C 1 65 ? 25.956  -22.476 13.444  1.00 45.27  ? 64  SER C O   1 
ATOM   1938 C CB  . SER C 1 65 ? 27.387  -22.930 15.953  1.00 45.83  ? 64  SER C CB  1 
ATOM   1939 O OG  . SER C 1 65 ? 26.238  -23.387 16.649  1.00 44.06  ? 64  SER C OG  1 
ATOM   1940 N N   . LYS C 1 66 ? 24.828  -20.904 14.560  1.00 41.28  ? 65  LYS C N   1 
ATOM   1941 C CA  . LYS C 1 66 ? 23.680  -21.038 13.662  1.00 44.41  ? 65  LYS C CA  1 
ATOM   1942 C C   . LYS C 1 66 ? 24.072  -20.765 12.209  1.00 53.74  ? 65  LYS C C   1 
ATOM   1943 O O   . LYS C 1 66 ? 23.507  -21.373 11.293  1.00 45.36  ? 65  LYS C O   1 
ATOM   1944 C CB  . LYS C 1 66 ? 22.434  -20.230 14.029  1.00 48.37  ? 65  LYS C CB  1 
ATOM   1945 C CG  . LYS C 1 66 ? 22.618  -18.726 14.104  1.00 41.08  ? 65  LYS C CG  1 
ATOM   1946 C CD  . LYS C 1 66 ? 21.363  -18.017 14.601  1.00 49.12  ? 65  LYS C CD  1 
ATOM   1947 C CE  . LYS C 1 66 ? 21.626  -16.591 14.935  1.00 50.43  ? 65  LYS C CE  1 
ATOM   1948 N NZ  . LYS C 1 66 ? 20.357  -15.896 15.104  1.00 54.06  ? 65  LYS C NZ  1 
ATOM   1949 N N   . ASP C 1 67 ? 25.038  -19.856 11.984  1.00 46.82  ? 66  ASP C N   1 
ATOM   1950 C CA  . ASP C 1 67 ? 25.359  -19.529 10.597  1.00 49.42  ? 66  ASP C CA  1 
ATOM   1951 C C   . ASP C 1 67 ? 25.752  -20.816 9.866   1.00 45.42  ? 66  ASP C C   1 
ATOM   1952 O O   . ASP C 1 67 ? 25.456  -20.972 8.689   1.00 42.41  ? 66  ASP C O   1 
ATOM   1953 C CB  . ASP C 1 67 ? 26.249  -18.293 10.438  1.00 49.66  ? 66  ASP C CB  1 
ATOM   1954 C CG  . ASP C 1 67 ? 27.739  -18.430 10.740  1.00 64.55  ? 66  ASP C CG  1 
ATOM   1955 O OD1 . ASP C 1 67 ? 28.226  -19.575 10.855  1.00 64.47  ? 66  ASP C OD1 1 
ATOM   1956 O OD2 . ASP C 1 67 ? 28.417  -17.376 10.874  1.00 63.42  ? 66  ASP C OD2 1 
ATOM   1957 N N   . LYS C 1 68 ? 26.325  -21.778 10.605  1.00 44.71  ? 67  LYS C N   1 
ATOM   1958 C CA  . LYS C 1 68 ? 26.858  -23.003 10.022  1.00 38.88  ? 67  LYS C CA  1 
ATOM   1959 C C   . LYS C 1 68 ? 25.847  -24.161 10.072  1.00 37.05  ? 67  LYS C C   1 
ATOM   1960 O O   . LYS C 1 68 ? 25.690  -24.905 9.100   1.00 42.50  ? 67  LYS C O   1 
ATOM   1961 C CB  . LYS C 1 68 ? 28.081  -23.361 10.872  1.00 34.60  ? 67  LYS C CB  1 
ATOM   1962 C CG  . LYS C 1 68 ? 28.875  -24.593 10.488  1.00 37.92  ? 67  LYS C CG  1 
ATOM   1963 C CD  . LYS C 1 68 ? 30.111  -24.506 11.391  1.00 49.18  ? 67  LYS C CD  1 
ATOM   1964 C CE  . LYS C 1 68 ? 30.981  -25.717 11.522  1.00 60.38  ? 67  LYS C CE  1 
ATOM   1965 N NZ  . LYS C 1 68 ? 31.434  -26.306 10.256  1.00 66.65  ? 67  LYS C NZ  1 
ATOM   1966 N N   . TYR C 1 69 ? 25.188  -24.345 11.226  1.00 38.53  ? 68  TYR C N   1 
ATOM   1967 C CA  . TYR C 1 69 ? 24.314  -25.501 11.419  1.00 37.82  ? 68  TYR C CA  1 
ATOM   1968 C C   . TYR C 1 69 ? 22.835  -25.149 11.215  1.00 36.06  ? 68  TYR C C   1 
ATOM   1969 O O   . TYR C 1 69 ? 22.005  -26.061 11.074  1.00 34.41  ? 68  TYR C O   1 
ATOM   1970 C CB  . TYR C 1 69 ? 24.543  -26.008 12.854  1.00 34.61  ? 68  TYR C CB  1 
ATOM   1971 C CG  . TYR C 1 69 ? 25.941  -26.548 13.135  1.00 34.19  ? 68  TYR C CG  1 
ATOM   1972 C CD1 . TYR C 1 69 ? 26.619  -27.378 12.246  1.00 41.65  ? 68  TYR C CD1 1 
ATOM   1973 C CD2 . TYR C 1 69 ? 26.566  -26.219 14.340  1.00 43.59  ? 68  TYR C CD2 1 
ATOM   1974 C CE1 . TYR C 1 69 ? 27.884  -27.875 12.545  1.00 43.35  ? 68  TYR C CE1 1 
ATOM   1975 C CE2 . TYR C 1 69 ? 27.827  -26.702 14.642  1.00 41.83  ? 68  TYR C CE2 1 
ATOM   1976 C CZ  . TYR C 1 69 ? 28.483  -27.524 13.747  1.00 46.03  ? 68  TYR C CZ  1 
ATOM   1977 O OH  . TYR C 1 69 ? 29.728  -27.950 14.121  1.00 51.98  ? 68  TYR C OH  1 
ATOM   1978 N N   . GLY C 1 70 ? 22.474  -23.847 11.220  1.00 36.09  ? 69  GLY C N   1 
ATOM   1979 C CA  . GLY C 1 70 ? 21.062  -23.488 11.183  1.00 36.23  ? 69  GLY C CA  1 
ATOM   1980 C C   . GLY C 1 70 ? 20.636  -23.340 9.722   1.00 40.04  ? 69  GLY C C   1 
ATOM   1981 O O   . GLY C 1 70 ? 20.643  -22.244 9.183   1.00 40.32  ? 69  GLY C O   1 
ATOM   1982 N N   . LYS C 1 71 ? 20.445  -24.473 9.067   1.00 36.43  ? 70  LYS C N   1 
ATOM   1983 C CA  . LYS C 1 71 ? 20.069  -24.522 7.663   1.00 36.96  ? 70  LYS C CA  1 
ATOM   1984 C C   . LYS C 1 71 ? 19.256  -25.789 7.494   1.00 41.33  ? 70  LYS C C   1 
ATOM   1985 O O   . LYS C 1 71 ? 19.361  -26.716 8.305   1.00 41.36  ? 70  LYS C O   1 
ATOM   1986 C CB  . LYS C 1 71 ? 21.284  -24.664 6.737   1.00 40.98  ? 70  LYS C CB  1 
ATOM   1987 C CG  . LYS C 1 71 ? 22.210  -25.786 7.093   1.00 43.66  ? 70  LYS C CG  1 
ATOM   1988 C CD  . LYS C 1 71 ? 23.379  -26.112 6.171   1.00 53.46  ? 70  LYS C CD  1 
ATOM   1989 C CE  . LYS C 1 71 ? 24.074  -27.348 6.672   1.00 55.34  ? 70  LYS C CE  1 
ATOM   1990 N N   . PRO C 1 72 ? 18.340  -25.821 6.517   1.00 35.36  ? 71  PRO C N   1 
ATOM   1991 C CA  . PRO C 1 72 ? 17.461  -26.972 6.411   1.00 32.88  ? 71  PRO C CA  1 
ATOM   1992 C C   . PRO C 1 72 ? 18.158  -28.271 6.020   1.00 31.55  ? 71  PRO C C   1 
ATOM   1993 O O   . PRO C 1 72 ? 19.171  -28.280 5.310   1.00 36.92  ? 71  PRO C O   1 
ATOM   1994 C CB  . PRO C 1 72 ? 16.403  -26.541 5.387   1.00 33.07  ? 71  PRO C CB  1 
ATOM   1995 C CG  . PRO C 1 72 ? 16.490  -25.032 5.420   1.00 31.87  ? 71  PRO C CG  1 
ATOM   1996 C CD  . PRO C 1 72 ? 17.929  -24.670 5.694   1.00 30.24  ? 71  PRO C CD  1 
ATOM   1997 N N   . ASN C 1 73 ? 17.523  -29.348 6.446   1.00 34.66  ? 72  ASN C N   1 
ATOM   1998 C CA  . ASN C 1 73 ? 17.769  -30.640 5.837   1.00 38.69  ? 72  ASN C CA  1 
ATOM   1999 C C   . ASN C 1 73 ? 16.543  -31.521 6.013   1.00 35.20  ? 72  ASN C C   1 
ATOM   2000 O O   . ASN C 1 73 ? 15.575  -31.182 6.681   1.00 38.58  ? 72  ASN C O   1 
ATOM   2001 C CB  . ASN C 1 73 ? 19.095  -31.299 6.224   1.00 41.57  ? 72  ASN C CB  1 
ATOM   2002 C CG  . ASN C 1 73 ? 19.075  -31.829 7.637   1.00 39.11  ? 72  ASN C CG  1 
ATOM   2003 O OD1 . ASN C 1 73 ? 18.202  -32.620 8.001   1.00 39.76  ? 72  ASN C OD1 1 
ATOM   2004 N ND2 . ASN C 1 73 ? 20.048  -31.420 8.433   1.00 40.55  ? 72  ASN C ND2 1 
ATOM   2005 N N   . LYS C 1 74 ? 16.600  -32.684 5.358   1.00 36.62  ? 73  LYS C N   1 
ATOM   2006 C CA  . LYS C 1 74 ? 15.376  -33.435 5.161   1.00 32.58  ? 73  LYS C CA  1 
ATOM   2007 C C   . LYS C 1 74 ? 15.190  -34.425 6.299   1.00 31.93  ? 73  LYS C C   1 
ATOM   2008 O O   . LYS C 1 74 ? 14.235  -35.195 6.282   1.00 38.20  ? 73  LYS C O   1 
ATOM   2009 C CB  . LYS C 1 74 ? 15.522  -34.176 3.825   1.00 39.75  ? 73  LYS C CB  1 
ATOM   2010 N N   . ARG C 1 75 ? 16.096  -34.412 7.284   1.00 30.43  ? 74  ARG C N   1 
ATOM   2011 C CA  . ARG C 1 75 ? 15.941  -35.382 8.365   1.00 32.92  ? 74  ARG C CA  1 
ATOM   2012 C C   . ARG C 1 75 ? 14.653  -35.109 9.151   1.00 34.41  ? 74  ARG C C   1 
ATOM   2013 O O   . ARG C 1 75 ? 14.239  -33.963 9.346   1.00 35.56  ? 74  ARG C O   1 
ATOM   2014 C CB  . ARG C 1 75 ? 17.205  -35.505 9.246   1.00 35.00  ? 74  ARG C CB  1 
ATOM   2015 C CG  . ARG C 1 75 ? 18.528  -35.854 8.554   1.00 38.48  ? 74  ARG C CG  1 
ATOM   2016 C CD  . ARG C 1 75 ? 18.708  -37.295 8.031   1.00 40.00  ? 74  ARG C CD  1 
ATOM   2017 N NE  . ARG C 1 75 ? 18.671  -38.175 9.193   1.00 41.29  ? 74  ARG C NE  1 
ATOM   2018 C CZ  . ARG C 1 75 ? 19.777  -38.604 9.824   1.00 34.39  ? 74  ARG C CZ  1 
ATOM   2019 N NH1 . ARG C 1 75 ? 19.655  -39.250 10.955  1.00 39.50  ? 74  ARG C NH1 1 
ATOM   2020 N NH2 . ARG C 1 75 ? 20.967  -38.320 9.339   1.00 36.75  ? 74  ARG C NH2 1 
ATOM   2021 N N   . LYS C 1 76 ? 14.026  -36.187 9.646   1.00 35.98  ? 75  LYS C N   1 
ATOM   2022 C CA  . LYS C 1 76 ? 12.722  -36.128 10.279  1.00 35.66  ? 75  LYS C CA  1 
ATOM   2023 C C   . LYS C 1 76 ? 12.739  -35.146 11.443  1.00 35.24  ? 75  LYS C C   1 
ATOM   2024 O O   . LYS C 1 76 ? 13.508  -35.323 12.389  1.00 37.21  ? 75  LYS C O   1 
ATOM   2025 C CB  . LYS C 1 76 ? 12.178  -37.479 10.781  1.00 41.57  ? 75  LYS C CB  1 
ATOM   2026 C CG  . LYS C 1 76 ? 10.660  -37.440 10.987  1.00 39.71  ? 75  LYS C CG  1 
ATOM   2027 C CD  . LYS C 1 76 ? 9.950   -38.544 11.759  1.00 50.00  ? 75  LYS C CD  1 
ATOM   2028 N N   . GLY C 1 77 ? 11.919  -34.081 11.312  1.00 36.47  ? 76  GLY C N   1 
ATOM   2029 C CA  . GLY C 1 77 ? 11.624  -33.177 12.421  1.00 32.70  ? 76  GLY C CA  1 
ATOM   2030 C C   . GLY C 1 77 ? 12.585  -31.977 12.453  1.00 30.35  ? 76  GLY C C   1 
ATOM   2031 O O   . GLY C 1 77 ? 12.426  -31.087 13.281  1.00 39.39  ? 76  GLY C O   1 
ATOM   2032 N N   . PHE C 1 78 ? 13.590  -31.980 11.564  1.00 32.90  ? 77  PHE C N   1 
ATOM   2033 C CA  . PHE C 1 78 ? 14.671  -31.021 11.622  1.00 31.16  ? 77  PHE C CA  1 
ATOM   2034 C C   . PHE C 1 78 ? 14.095  -29.627 11.372  1.00 34.26  ? 77  PHE C C   1 
ATOM   2035 O O   . PHE C 1 78 ? 14.365  -28.683 12.116  1.00 29.96  ? 77  PHE C O   1 
ATOM   2036 C CB  . PHE C 1 78 ? 15.785  -31.358 10.626  1.00 34.17  ? 77  PHE C CB  1 
ATOM   2037 C CG  . PHE C 1 78 ? 17.084  -30.606 10.894  1.00 33.10  ? 77  PHE C CG  1 
ATOM   2038 C CD1 . PHE C 1 78 ? 17.322  -29.340 10.345  1.00 32.71  ? 77  PHE C CD1 1 
ATOM   2039 C CD2 . PHE C 1 78 ? 18.073  -31.163 11.699  1.00 29.39  ? 77  PHE C CD2 1 
ATOM   2040 C CE1 . PHE C 1 78 ? 18.506  -28.658 10.627  1.00 36.10  ? 77  PHE C CE1 1 
ATOM   2041 C CE2 . PHE C 1 78 ? 19.255  -30.484 11.981  1.00 31.21  ? 77  PHE C CE2 1 
ATOM   2042 C CZ  . PHE C 1 78 ? 19.494  -29.242 11.421  1.00 33.88  ? 77  PHE C CZ  1 
ATOM   2043 N N   . ASN C 1 79 ? 13.355  -29.496 10.267  1.00 34.13  ? 78  ASN C N   1 
ATOM   2044 C CA  . ASN C 1 79 ? 12.979  -28.147 9.853   1.00 38.63  ? 78  ASN C CA  1 
ATOM   2045 C C   . ASN C 1 79 ? 11.986  -27.525 10.832  1.00 33.69  ? 78  ASN C C   1 
ATOM   2046 O O   . ASN C 1 79 ? 12.022  -26.315 11.125  1.00 34.24  ? 78  ASN C O   1 
ATOM   2047 C CB  . ASN C 1 79 ? 12.535  -28.086 8.396   1.00 34.60  ? 78  ASN C CB  1 
ATOM   2048 C CG  . ASN C 1 79 ? 13.684  -28.397 7.471   1.00 32.76  ? 78  ASN C CG  1 
ATOM   2049 O OD1 . ASN C 1 79 ? 14.827  -28.109 7.816   1.00 30.69  ? 78  ASN C OD1 1 
ATOM   2050 N ND2 . ASN C 1 79 ? 13.426  -29.053 6.343   1.00 30.41  ? 78  ASN C ND2 1 
ATOM   2051 N N   . GLU C 1 80 ? 11.098  -28.339 11.380  1.00 35.89  ? 79  GLU C N   1 
ATOM   2052 C CA  . GLU C 1 80 ? 10.280  -27.833 12.468  1.00 34.97  ? 79  GLU C CA  1 
ATOM   2053 C C   . GLU C 1 80 ? 11.150  -27.401 13.661  1.00 39.97  ? 79  GLU C C   1 
ATOM   2054 O O   . GLU C 1 80 ? 10.846  -26.402 14.319  1.00 36.14  ? 79  GLU C O   1 
ATOM   2055 C CB  . GLU C 1 80 ? 9.218   -28.878 12.806  1.00 40.59  ? 79  GLU C CB  1 
ATOM   2056 C CG  . GLU C 1 80 ? 8.233   -28.400 13.865  1.00 37.02  ? 79  GLU C CG  1 
ATOM   2057 C CD  . GLU C 1 80 ? 7.043   -29.324 14.039  1.00 47.21  ? 79  GLU C CD  1 
ATOM   2058 O OE1 . GLU C 1 80 ? 7.155   -30.496 13.634  1.00 55.42  ? 79  GLU C OE1 1 
ATOM   2059 O OE2 . GLU C 1 80 ? 5.986   -28.864 14.520  1.00 47.62  ? 79  GLU C OE2 1 
ATOM   2060 N N   . GLY C 1 81 ? 12.196  -28.192 13.987  1.00 34.21  ? 80  GLY C N   1 
ATOM   2061 C CA  . GLY C 1 81 ? 13.113  -27.811 15.056  1.00 34.83  ? 80  GLY C CA  1 
ATOM   2062 C C   . GLY C 1 81 ? 13.755  -26.438 14.824  1.00 35.59  ? 80  GLY C C   1 
ATOM   2063 O O   . GLY C 1 81 ? 13.891  -25.661 15.773  1.00 38.32  ? 80  GLY C O   1 
ATOM   2064 N N   . LEU C 1 82 ? 14.219  -26.177 13.581  1.00 34.67  ? 81  LEU C N   1 
ATOM   2065 C CA  . LEU C 1 82 ? 14.757  -24.876 13.187  1.00 36.67  ? 81  LEU C CA  1 
ATOM   2066 C C   . LEU C 1 82 ? 13.751  -23.759 13.489  1.00 33.35  ? 81  LEU C C   1 
ATOM   2067 O O   . LEU C 1 82 ? 14.155  -22.705 13.991  1.00 36.43  ? 81  LEU C O   1 
ATOM   2068 C CB  . LEU C 1 82 ? 15.189  -24.850 11.719  1.00 35.89  ? 81  LEU C CB  1 
ATOM   2069 C CG  . LEU C 1 82 ? 16.452  -25.637 11.366  1.00 32.35  ? 81  LEU C CG  1 
ATOM   2070 C CD1 . LEU C 1 82 ? 16.811  -25.438 9.888   1.00 32.99  ? 81  LEU C CD1 1 
ATOM   2071 C CD2 . LEU C 1 82 ? 17.649  -25.262 12.225  1.00 32.68  ? 81  LEU C CD2 1 
ATOM   2072 N N   . TRP C 1 83 ? 12.462  -24.001 13.223  1.00 34.67  ? 82  TRP C N   1 
ATOM   2073 C CA  . TRP C 1 83 ? 11.419  -22.999 13.460  1.00 39.99  ? 82  TRP C CA  1 
ATOM   2074 C C   . TRP C 1 83 ? 11.276  -22.741 14.972  1.00 41.58  ? 82  TRP C C   1 
ATOM   2075 O O   . TRP C 1 83 ? 11.233  -21.590 15.412  1.00 39.89  ? 82  TRP C O   1 
ATOM   2076 C CB  . TRP C 1 83 ? 10.066  -23.396 12.834  1.00 38.55  ? 82  TRP C CB  1 
ATOM   2077 C CG  . TRP C 1 83 ? 9.081   -22.256 12.937  1.00 40.39  ? 82  TRP C CG  1 
ATOM   2078 C CD1 . TRP C 1 83 ? 8.922   -21.246 12.029  1.00 40.54  ? 82  TRP C CD1 1 
ATOM   2079 C CD2 . TRP C 1 83 ? 8.238   -21.923 14.064  1.00 42.02  ? 82  TRP C CD2 1 
ATOM   2080 N NE1 . TRP C 1 83 ? 7.977   -20.352 12.468  1.00 41.89  ? 82  TRP C NE1 1 
ATOM   2081 C CE2 . TRP C 1 83 ? 7.546   -20.731 13.718  1.00 45.04  ? 82  TRP C CE2 1 
ATOM   2082 C CE3 . TRP C 1 83 ? 7.980   -22.517 15.312  1.00 40.58  ? 82  TRP C CE3 1 
ATOM   2083 C CZ2 . TRP C 1 83 ? 6.626   -20.131 14.577  1.00 50.72  ? 82  TRP C CZ2 1 
ATOM   2084 C CZ3 . TRP C 1 83 ? 7.073   -21.915 16.159  1.00 51.26  ? 82  TRP C CZ3 1 
ATOM   2085 C CH2 . TRP C 1 83 ? 6.411   -20.741 15.797  1.00 51.32  ? 82  TRP C CH2 1 
ATOM   2086 N N   . GLU C 1 84 ? 11.284  -23.816 15.776  1.00 40.07  ? 83  GLU C N   1 
ATOM   2087 C CA  . GLU C 1 84 ? 11.178  -23.697 17.229  1.00 42.38  ? 83  GLU C CA  1 
ATOM   2088 C C   . GLU C 1 84 ? 12.342  -22.911 17.854  1.00 37.74  ? 83  GLU C C   1 
ATOM   2089 O O   . GLU C 1 84 ? 12.124  -21.988 18.658  1.00 38.51  ? 83  GLU C O   1 
ATOM   2090 C CB  . GLU C 1 84 ? 11.023  -25.095 17.826  1.00 39.08  ? 83  GLU C CB  1 
ATOM   2091 C CG  . GLU C 1 84 ? 9.675   -25.728 17.502  1.00 42.08  ? 83  GLU C CG  1 
ATOM   2092 C CD  . GLU C 1 84 ? 9.578   -27.191 17.890  1.00 45.25  ? 83  GLU C CD  1 
ATOM   2093 O OE1 . GLU C 1 84 ? 10.569  -27.723 18.451  1.00 41.88  ? 83  GLU C OE1 1 
ATOM   2094 O OE2 . GLU C 1 84 ? 8.526   -27.791 17.609  1.00 50.74  ? 83  GLU C OE2 1 
ATOM   2095 N N   . ILE C 1 85 ? 13.590  -23.277 17.530  1.00 40.40  ? 84  ILE C N   1 
ATOM   2096 C CA  . ILE C 1 85 ? 14.747  -22.642 18.149  1.00 41.66  ? 84  ILE C CA  1 
ATOM   2097 C C   . ILE C 1 85 ? 14.745  -21.137 17.867  1.00 41.79  ? 84  ILE C C   1 
ATOM   2098 O O   . ILE C 1 85 ? 15.171  -20.347 18.698  1.00 39.22  ? 84  ILE C O   1 
ATOM   2099 C CB  . ILE C 1 85 ? 16.076  -23.350 17.797  1.00 37.44  ? 84  ILE C CB  1 
ATOM   2100 C CG1 . ILE C 1 85 ? 17.169  -23.076 18.830  1.00 36.56  ? 84  ILE C CG1 1 
ATOM   2101 C CG2 . ILE C 1 85 ? 16.561  -23.113 16.352  1.00 36.53  ? 84  ILE C CG2 1 
ATOM   2102 C CD1 . ILE C 1 85 ? 18.337  -24.054 18.789  1.00 39.66  ? 84  ILE C CD1 1 
ATOM   2103 N N   . GLN C 1 86 ? 14.263  -20.748 16.680  1.00 37.90  ? 85  GLN C N   1 
ATOM   2104 C CA  . GLN C 1 86 ? 14.369  -19.349 16.285  1.00 44.11  ? 85  GLN C CA  1 
ATOM   2105 C C   . GLN C 1 86 ? 13.166  -18.554 16.778  1.00 37.90  ? 85  GLN C C   1 
ATOM   2106 O O   . GLN C 1 86 ? 13.321  -17.375 17.085  1.00 43.96  ? 85  GLN C O   1 
ATOM   2107 C CB  . GLN C 1 86 ? 14.479  -19.162 14.768  1.00 40.64  ? 85  GLN C CB  1 
ATOM   2108 C CG  . GLN C 1 86 ? 14.795  -17.730 14.326  1.00 37.73  ? 85  GLN C CG  1 
ATOM   2109 C CD  . GLN C 1 86 ? 15.068  -17.651 12.838  1.00 41.74  ? 85  GLN C CD  1 
ATOM   2110 O OE1 . GLN C 1 86 ? 14.938  -18.654 12.117  1.00 38.99  ? 85  GLN C OE1 1 
ATOM   2111 N NE2 . GLN C 1 86 ? 15.499  -16.482 12.370  1.00 42.43  ? 85  GLN C NE2 1 
ATOM   2112 N N   . ASN C 1 87 ? 12.003  -19.195 16.878  1.00 43.63  ? 86  ASN C N   1 
ATOM   2113 C CA  . ASN C 1 87 ? 10.745  -18.476 17.025  1.00 45.41  ? 86  ASN C CA  1 
ATOM   2114 C C   . ASN C 1 87 ? 10.062  -18.736 18.371  1.00 48.33  ? 86  ASN C C   1 
ATOM   2115 O O   . ASN C 1 87 ? 9.363   -17.856 18.868  1.00 46.23  ? 86  ASN C O   1 
ATOM   2116 C CB  . ASN C 1 87 ? 9.809   -18.713 15.847  1.00 44.13  ? 86  ASN C CB  1 
ATOM   2117 C CG  . ASN C 1 87 ? 10.428  -18.135 14.599  1.00 51.50  ? 86  ASN C CG  1 
ATOM   2118 O OD1 . ASN C 1 87 ? 10.495  -16.909 14.458  1.00 52.14  ? 86  ASN C OD1 1 
ATOM   2119 N ND2 . ASN C 1 87 ? 10.972  -18.985 13.743  1.00 45.24  ? 86  ASN C ND2 1 
ATOM   2120 N N   . ASN C 1 88 ? 10.254  -19.931 18.948  1.00 48.18  ? 87  ASN C N   1 
ATOM   2121 C CA  . ASN C 1 88 ? 9.527   -20.309 20.159  1.00 45.38  ? 87  ASN C CA  1 
ATOM   2122 C C   . ASN C 1 88 ? 10.382  -21.203 21.061  1.00 48.50  ? 87  ASN C C   1 
ATOM   2123 O O   . ASN C 1 88 ? 9.947   -22.299 21.439  1.00 51.54  ? 87  ASN C O   1 
ATOM   2124 C CB  . ASN C 1 88 ? 8.208   -20.989 19.823  1.00 52.33  ? 87  ASN C CB  1 
ATOM   2125 C CG  . ASN C 1 88 ? 7.258   -20.914 20.996  1.00 60.73  ? 87  ASN C CG  1 
ATOM   2126 O OD1 . ASN C 1 88 ? 7.592   -20.310 22.025  1.00 62.49  ? 87  ASN C OD1 1 
ATOM   2127 N ND2 . ASN C 1 88 ? 6.076   -21.498 20.855  1.00 61.06  ? 87  ASN C ND2 1 
ATOM   2128 N N   . PRO C 1 89 ? 11.605  -20.768 21.435  1.00 41.45  ? 88  PRO C N   1 
ATOM   2129 C CA  . PRO C 1 89 ? 12.592  -21.669 22.040  1.00 47.33  ? 88  PRO C CA  1 
ATOM   2130 C C   . PRO C 1 89 ? 12.412  -22.066 23.503  1.00 51.98  ? 88  PRO C C   1 
ATOM   2131 O O   . PRO C 1 89 ? 13.074  -22.998 23.965  1.00 48.04  ? 88  PRO C O   1 
ATOM   2132 C CB  . PRO C 1 89 ? 13.930  -20.969 21.837  1.00 40.82  ? 88  PRO C CB  1 
ATOM   2133 C CG  . PRO C 1 89 ? 13.556  -19.499 21.716  1.00 45.78  ? 88  PRO C CG  1 
ATOM   2134 C CD  . PRO C 1 89 ? 12.129  -19.413 21.227  1.00 42.26  ? 88  PRO C CD  1 
ATOM   2135 N N   . HIS C 1 90 ? 11.548  -21.336 24.220  1.00 50.79  ? 89  HIS C N   1 
ATOM   2136 C CA  . HIS C 1 90 ? 11.377  -21.552 25.653  1.00 50.34  ? 89  HIS C CA  1 
ATOM   2137 C C   . HIS C 1 90 ? 9.970   -22.061 25.984  1.00 60.24  ? 89  HIS C C   1 
ATOM   2138 O O   . HIS C 1 90 ? 9.523   -21.963 27.125  1.00 66.25  ? 89  HIS C O   1 
ATOM   2139 C CB  . HIS C 1 90 ? 11.897  -20.344 26.442  1.00 42.35  ? 89  HIS C CB  1 
ATOM   2140 C CG  . HIS C 1 90 ? 13.361  -20.104 26.271  1.00 39.97  ? 89  HIS C CG  1 
ATOM   2141 N ND1 . HIS C 1 90 ? 13.912  -18.980 25.692  1.00 44.63  ? 89  HIS C ND1 1 
ATOM   2142 C CD2 . HIS C 1 90 ? 14.406  -20.875 26.654  1.00 44.14  ? 89  HIS C CD2 1 
ATOM   2143 C CE1 . HIS C 1 90 ? 15.234  -19.074 25.706  1.00 45.66  ? 89  HIS C CE1 1 
ATOM   2144 N NE2 . HIS C 1 90 ? 15.560  -20.217 26.299  1.00 46.53  ? 89  HIS C NE2 1 
ATOM   2145 N N   . ALA C 1 91 ? 9.285   -22.654 24.999  1.00 62.02  ? 90  ALA C N   1 
ATOM   2146 C CA  . ALA C 1 91 ? 7.949   -23.202 25.198  1.00 61.06  ? 90  ALA C CA  1 
ATOM   2147 C C   . ALA C 1 91 ? 8.024   -24.662 25.652  1.00 65.50  ? 90  ALA C C   1 
ATOM   2148 O O   . ALA C 1 91 ? 9.063   -25.310 25.531  1.00 72.54  ? 90  ALA C O   1 
ATOM   2149 C CB  . ALA C 1 91 ? 7.129   -23.048 23.935  1.00 64.30  ? 90  ALA C CB  1 
ATOM   2150 N N   . SER C 1 92 ? 6.883   -25.184 26.118  1.00 77.60  ? 91  SER C N   1 
ATOM   2151 C CA  . SER C 1 92 ? 6.784   -26.450 26.834  1.00 77.58  ? 91  SER C CA  1 
ATOM   2152 C C   . SER C 1 92 ? 6.907   -27.656 25.903  1.00 76.50  ? 91  SER C C   1 
ATOM   2153 O O   . SER C 1 92 ? 7.790   -28.489 26.094  1.00 84.94  ? 91  SER C O   1 
ATOM   2154 C CB  . SER C 1 92 ? 5.500   -26.509 27.630  1.00 79.20  ? 91  SER C CB  1 
ATOM   2155 O OG  . SER C 1 92 ? 5.462   -25.456 28.581  1.00 79.75  ? 91  SER C OG  1 
ATOM   2156 N N   . TYR C 1 93 ? 5.983   -27.758 24.937  1.00 75.60  ? 92  TYR C N   1 
ATOM   2157 C CA  . TYR C 1 93 ? 5.851   -28.886 24.018  1.00 81.55  ? 92  TYR C CA  1 
ATOM   2158 C C   . TYR C 1 93 ? 5.525   -30.183 24.789  1.00 82.33  ? 92  TYR C C   1 
ATOM   2159 O O   . TYR C 1 93 ? 5.173   -30.166 25.994  1.00 87.54  ? 92  TYR C O   1 
ATOM   2160 C CB  . TYR C 1 93 ? 7.047   -29.080 23.076  1.00 85.57  ? 92  TYR C CB  1 
ATOM   2161 C CG  . TYR C 1 93 ? 7.493   -27.833 22.321  1.00 77.14  ? 92  TYR C CG  1 
ATOM   2162 C CD1 . TYR C 1 93 ? 6.876   -27.453 21.129  1.00 71.54  ? 92  TYR C CD1 1 
ATOM   2163 C CD2 . TYR C 1 93 ? 8.533   -27.041 22.801  1.00 67.89  ? 92  TYR C CD2 1 
ATOM   2164 C CE1 . TYR C 1 93 ? 7.274   -26.318 20.441  1.00 67.15  ? 92  TYR C CE1 1 
ATOM   2165 C CE2 . TYR C 1 93 ? 8.938   -25.903 22.120  1.00 62.51  ? 92  TYR C CE2 1 
ATOM   2166 C CZ  . TYR C 1 93 ? 8.310   -25.544 20.939  1.00 64.33  ? 92  TYR C CZ  1 
ATOM   2167 O OH  . TYR C 1 93 ? 8.715   -24.422 20.277  1.00 69.05  ? 92  TYR C OH  1 
HETATM 2168 S S   . SO4 D 2 .  ? 1.647   -33.911 1.728   1.00 106.61 ? 101 SO4 A S   1 
HETATM 2169 O O1  . SO4 D 2 .  ? 2.626   -34.606 0.933   1.00 86.80  ? 101 SO4 A O1  1 
HETATM 2170 O O2  . SO4 D 2 .  ? 1.405   -32.608 1.167   1.00 101.77 ? 101 SO4 A O2  1 
HETATM 2171 O O3  . SO4 D 2 .  ? 0.418   -34.666 1.736   1.00 110.62 ? 101 SO4 A O3  1 
HETATM 2172 O O4  . SO4 D 2 .  ? 2.138   -33.769 3.074   1.00 100.62 ? 101 SO4 A O4  1 
HETATM 2173 S S   . SO4 E 2 .  ? -9.038  -24.838 1.501   1.00 89.49  ? 102 SO4 A S   1 
HETATM 2174 O O1  . SO4 E 2 .  ? -9.368  -24.252 0.226   1.00 80.41  ? 102 SO4 A O1  1 
HETATM 2175 O O2  . SO4 E 2 .  ? -9.346  -23.909 2.557   1.00 92.20  ? 102 SO4 A O2  1 
HETATM 2176 O O3  . SO4 E 2 .  ? -9.792  -26.052 1.690   1.00 93.21  ? 102 SO4 A O3  1 
HETATM 2177 O O4  . SO4 E 2 .  ? -7.635  -25.148 1.540   1.00 99.08  ? 102 SO4 A O4  1 
HETATM 2178 C C1  . EDO F 3 .  ? 14.475  -19.570 -7.304  1.00 39.09  ? 103 EDO A C1  1 
HETATM 2179 O O1  . EDO F 3 .  ? 15.719  -18.883 -7.275  1.00 35.08  ? 103 EDO A O1  1 
HETATM 2180 C C2  . EDO F 3 .  ? 13.671  -19.119 -8.479  1.00 40.52  ? 103 EDO A C2  1 
HETATM 2181 O O2  . EDO F 3 .  ? 13.037  -17.846 -8.271  1.00 37.76  ? 103 EDO A O2  1 
HETATM 2182 S S   . SO4 G 2 .  ? 9.502   -29.691 5.645   1.00 60.07  ? 104 SO4 A S   1 
HETATM 2183 O O1  . SO4 G 2 .  ? 10.370  -29.027 4.727   1.00 52.08  ? 104 SO4 A O1  1 
HETATM 2184 O O2  . SO4 G 2 .  ? 8.862   -30.802 4.964   1.00 59.38  ? 104 SO4 A O2  1 
HETATM 2185 O O3  . SO4 G 2 .  ? 10.271  -30.184 6.778   1.00 61.79  ? 104 SO4 A O3  1 
HETATM 2186 O O4  . SO4 G 2 .  ? 8.488   -28.776 6.100   1.00 71.35  ? 104 SO4 A O4  1 
HETATM 2187 S S   . SO4 H 2 .  ? 7.348   -8.512  -25.087 1.00 67.78  ? 101 SO4 B S   1 
HETATM 2188 O O1  . SO4 H 2 .  ? 8.518   -8.423  -25.947 1.00 42.38  ? 101 SO4 B O1  1 
HETATM 2189 O O2  . SO4 H 2 .  ? 6.354   -9.382  -25.666 1.00 53.67  ? 101 SO4 B O2  1 
HETATM 2190 O O3  . SO4 H 2 .  ? 7.715   -9.026  -23.770 1.00 48.68  ? 101 SO4 B O3  1 
HETATM 2191 O O4  . SO4 H 2 .  ? 6.824   -7.172  -24.972 1.00 69.61  ? 101 SO4 B O4  1 
HETATM 2192 S S   . SO4 I 2 .  ? 14.663  -26.721 -26.593 1.00 62.26  ? 102 SO4 B S   1 
HETATM 2193 O O1  . SO4 I 2 .  ? 16.097  -26.595 -26.545 1.00 68.29  ? 102 SO4 B O1  1 
HETATM 2194 O O2  . SO4 I 2 .  ? 14.303  -28.094 -26.858 1.00 73.42  ? 102 SO4 B O2  1 
HETATM 2195 O O3  . SO4 I 2 .  ? 14.124  -26.308 -25.321 1.00 67.05  ? 102 SO4 B O3  1 
HETATM 2196 O O4  . SO4 I 2 .  ? 14.123  -25.882 -27.631 1.00 57.65  ? 102 SO4 B O4  1 
HETATM 2197 C C4  . WV4 J 4 .  ? 18.468  -15.492 -22.717 0.78 33.12  ? 103 WV4 B C4  1 
HETATM 2198 C C5  . WV4 J 4 .  ? 19.593  -15.705 -21.937 0.78 36.43  ? 103 WV4 B C5  1 
HETATM 2199 C C6  . WV4 J 4 .  ? 20.871  -15.554 -22.478 0.78 35.41  ? 103 WV4 B C6  1 
HETATM 2200 C C7  . WV4 J 4 .  ? 16.880  -16.091 -26.063 0.78 26.67  ? 103 WV4 B C7  1 
HETATM 2201 C C8  . WV4 J 4 .  ? 21.941  -15.996 -20.226 0.78 51.25  ? 103 WV4 B C8  1 
HETATM 2202 C C9  . WV4 J 4 .  ? 22.734  -14.982 -19.426 0.78 57.69  ? 103 WV4 B C9  1 
HETATM 2203 N N1  . WV4 J 4 .  ? 21.990  -15.695 -21.697 0.78 43.71  ? 103 WV4 B N1  1 
HETATM 2204 C C3  . WV4 J 4 .  ? 18.613  -15.117 -24.049 0.78 30.21  ? 103 WV4 B C3  1 
HETATM 2205 C C1  . WV4 J 4 .  ? 20.961  -15.194 -23.819 0.78 33.70  ? 103 WV4 B C1  1 
HETATM 2206 C C2  . WV4 J 4 .  ? 19.869  -14.973 -24.617 0.78 30.15  ? 103 WV4 B C2  1 
HETATM 2207 F F1  . WV4 J 4 .  ? 22.207  -15.030 -24.353 0.78 34.12  ? 103 WV4 B F1  1 
HETATM 2208 O O1  . WV4 J 4 .  ? 16.064  -14.642 -24.073 0.78 32.19  ? 103 WV4 B O1  1 
HETATM 2209 O O2  . WV4 J 4 .  ? 17.433  -13.547 -25.785 0.78 27.79  ? 103 WV4 B O2  1 
HETATM 2210 S S1  . WV4 J 4 .  ? 17.170  -14.726 -24.987 0.78 28.12  ? 103 WV4 B S1  1 
HETATM 2211 S S   . SO4 K 2 .  ? 29.882  -38.896 12.446  1.00 102.66 ? 101 SO4 C S   1 
HETATM 2212 O O1  . SO4 K 2 .  ? 31.083  -38.103 12.496  1.00 109.22 ? 101 SO4 C O1  1 
HETATM 2213 O O2  . SO4 K 2 .  ? 29.043  -38.422 11.381  1.00 90.95  ? 101 SO4 C O2  1 
HETATM 2214 O O3  . SO4 K 2 .  ? 30.210  -40.277 12.211  1.00 88.25  ? 101 SO4 C O3  1 
HETATM 2215 O O4  . SO4 K 2 .  ? 29.191  -38.781 13.701  1.00 113.68 ? 101 SO4 C O4  1 
HETATM 2216 C C4  . WV4 L 4 .  ? 16.871  -39.037 17.772  0.60 38.60  ? 102 WV4 C C4  1 
HETATM 2217 C C5  . WV4 L 4 .  ? 16.868  -40.080 18.683  0.60 34.68  ? 102 WV4 C C5  1 
HETATM 2218 C C6  . WV4 L 4 .  ? 17.028  -39.829 20.048  0.60 37.82  ? 102 WV4 C C6  1 
HETATM 2219 C C7  . WV4 L 4 .  ? 18.736  -35.928 16.964  0.60 34.27  ? 102 WV4 C C7  1 
HETATM 2220 C C8  . WV4 L 4 .  ? 16.752  -42.198 20.731  0.60 45.78  ? 102 WV4 C C8  1 
HETATM 2221 C C9  . WV4 L 4 .  ? 15.378  -42.453 21.279  0.60 44.84  ? 102 WV4 C C9  1 
HETATM 2222 N N1  . WV4 L 4 .  ? 17.039  -40.815 21.011  0.60 38.59  ? 102 WV4 C N1  1 
HETATM 2223 C C3  . WV4 L 4 .  ? 17.044  -37.741 18.229  0.60 32.15  ? 102 WV4 C C3  1 
HETATM 2224 C C1  . WV4 L 4 .  ? 17.158  -38.513 20.448  0.60 35.71  ? 102 WV4 C C1  1 
HETATM 2225 C C2  . WV4 L 4 .  ? 17.182  -37.461 19.579  0.60 33.89  ? 102 WV4 C C2  1 
HETATM 2226 F F1  . WV4 L 4 .  ? 17.285  -38.272 21.768  0.60 38.20  ? 102 WV4 C F1  1 
HETATM 2227 O O1  . WV4 L 4 .  ? 16.325  -35.315 17.706  0.60 29.66  ? 102 WV4 C O1  1 
HETATM 2228 O O2  . WV4 L 4 .  ? 16.597  -36.876 15.815  0.60 30.91  ? 102 WV4 C O2  1 
HETATM 2229 S S1  . WV4 L 4 .  ? 17.049  -36.391 17.092  0.60 31.84  ? 102 WV4 C S1  1 
HETATM 2230 O O   . HOH M 5 .  ? 6.456   -29.183 6.563   1.00 54.77  ? 201 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 9.739   -32.359 3.728   1.00 53.55  ? 202 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 11.245  -19.425 10.338  1.00 63.58  ? 203 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? -5.422  -13.543 -16.706 1.00 48.34  ? 204 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? -6.770  -25.100 -5.177  1.00 51.07  ? 205 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 0.775   -10.459 -15.474 1.00 42.06  ? 206 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 4.791   -10.224 13.716  1.00 69.68  ? 207 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 17.548  -18.649 -9.711  1.00 52.55  ? 208 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 9.475   -18.190 -10.996 1.00 37.91  ? 209 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 13.169  -12.327 8.151   1.00 52.47  ? 210 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 10.936  -9.598  -13.578 1.00 67.74  ? 211 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? -3.352  -11.049 6.824   1.00 41.98  ? 212 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 7.520   -10.568 -12.179 1.00 38.03  ? 213 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 1.554   -24.859 13.690  1.00 60.88  ? 214 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 11.804  -29.839 2.644   1.00 46.54  ? 215 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 0.127   -29.630 9.953   1.00 60.21  ? 216 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 9.918   -22.686 -9.579  1.00 44.60  ? 217 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 0.115   -33.823 4.721   1.00 62.11  ? 218 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 11.652  -24.049 9.706   1.00 39.48  ? 219 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 16.407  -24.542 1.877   1.00 41.41  ? 220 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 5.141   -7.914  1.178   1.00 33.06  ? 221 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? -1.867  3.192   -2.107  1.00 42.65  ? 222 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 2.920   -24.934 -6.424  1.00 55.47  ? 223 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 11.309  -5.263  -7.828  1.00 39.18  ? 224 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 2.035   0.454   -7.431  1.00 40.25  ? 225 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? -7.586  -15.921 -1.082  1.00 38.12  ? 226 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 0.791   -23.415 9.115   1.00 47.02  ? 227 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 14.133  -27.880 -5.075  1.00 55.73  ? 228 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 4.863   -3.539  -3.287  1.00 36.20  ? 229 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 1.568   -18.184 -18.848 1.00 47.68  ? 230 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 20.401  -15.553 7.340   1.00 30.12  ? 231 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 3.748   -29.591 -0.671  1.00 41.03  ? 232 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? 10.121  -6.061  -1.671  1.00 35.00  ? 233 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? -0.199  -20.712 11.149  1.00 74.64  ? 234 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? 13.532  -9.411  -7.321  1.00 48.10  ? 235 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 14.376  -15.644 -9.275  1.00 44.12  ? 236 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? -3.619  -21.283 6.133   1.00 38.76  ? 237 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 11.941  -12.048 5.899   1.00 40.18  ? 238 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 13.794  -12.035 -4.229  1.00 24.48  ? 239 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -0.061  -21.138 6.971   1.00 34.64  ? 240 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 8.771   -17.925 -15.992 1.00 56.86  ? 241 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 11.966  -12.353 -6.203  1.00 29.88  ? 242 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 16.300  -12.085 -5.314  1.00 34.99  ? 243 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? -5.234  -16.051 -8.063  1.00 33.13  ? 244 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 15.412  -13.656 10.283  1.00 49.50  ? 245 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? -5.277  -19.818 -5.651  1.00 39.58  ? 246 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 9.969   -20.074 -18.735 1.00 48.41  ? 247 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? -7.378  -16.771 1.711   1.00 41.81  ? 248 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 11.890  -16.397 -15.139 1.00 43.59  ? 249 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 17.711  -12.930 1.363   1.00 22.77  ? 250 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 2.279   -4.624  -10.269 1.00 42.07  ? 251 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -1.307  -22.143 -0.683  1.00 30.10  ? 252 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? 8.613   -17.567 8.573   1.00 44.36  ? 253 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? 10.482  -13.067 9.577   1.00 39.08  ? 254 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? -5.571  -27.084 2.870   1.00 57.83  ? 255 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? 6.911   -5.958  0.354   1.00 54.09  ? 256 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -7.538  -17.350 6.573   1.00 41.35  ? 257 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 8.264   -7.857  1.241   1.00 34.63  ? 258 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? -10.548 -16.307 -3.770  1.00 64.69  ? 259 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? -0.917  -11.842 11.479  1.00 39.47  ? 260 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 2.917   -25.238 -10.014 1.00 40.43  ? 261 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? 9.145   -16.200 -13.325 1.00 38.29  ? 262 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? 2.149   -10.652 11.672  1.00 37.30  ? 263 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? -8.143  -21.214 -1.241  1.00 43.49  ? 264 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? 2.912   -6.416  5.425   1.00 36.35  ? 265 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? 13.358  -13.605 -8.294  1.00 45.11  ? 266 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 5.683   -7.774  4.036   1.00 37.06  ? 267 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 17.020  -11.999 -17.340 1.00 37.44  ? 268 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? 6.451   -16.166 -15.092 1.00 49.32  ? 269 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? 11.697  -5.952  -3.774  1.00 53.99  ? 270 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? -5.937  -11.907 -11.361 1.00 43.09  ? 271 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? -5.976  -12.918 6.704   1.00 43.72  ? 272 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? -4.059  -26.019 -5.587  1.00 67.97  ? 273 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? -7.704  -19.591 -3.515  1.00 59.22  ? 274 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? -3.781  -7.904  10.582  1.00 48.08  ? 275 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? -1.393  -7.504  11.276  1.00 47.32  ? 276 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? 4.804   -34.684 4.206   1.00 66.38  ? 277 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? -6.872  -11.623 -7.947  1.00 32.23  ? 278 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? 11.564  -7.916  0.401   1.00 27.24  ? 279 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? 3.475   -9.786  -13.252 1.00 48.57  ? 280 HOH A O   1 
HETATM 2310 O O   . HOH M 5 .  ? 0.996   -29.458 -7.184  1.00 62.51  ? 281 HOH A O   1 
HETATM 2311 O O   . HOH M 5 .  ? -2.237  -31.069 -2.863  1.00 44.89  ? 282 HOH A O   1 
HETATM 2312 O O   . HOH M 5 .  ? 21.989  -16.762 -3.642  1.00 34.76  ? 283 HOH A O   1 
HETATM 2313 O O   . HOH M 5 .  ? 9.441   -0.866  -1.281  1.00 71.20  ? 284 HOH A O   1 
HETATM 2314 O O   . HOH M 5 .  ? 22.825  -16.794 -0.491  1.00 40.08  ? 285 HOH A O   1 
HETATM 2315 O O   . HOH M 5 .  ? 10.590  -27.799 -7.584  1.00 59.75  ? 286 HOH A O   1 
HETATM 2316 O O   . HOH M 5 .  ? -5.280  -16.870 -16.078 1.00 48.51  ? 287 HOH A O   1 
HETATM 2317 O O   . HOH M 5 .  ? 18.620  -17.483 -9.751  1.00 64.50  ? 288 HOH A O   1 
HETATM 2318 O O   . HOH M 5 .  ? -7.363  -21.231 -5.674  1.00 53.74  ? 289 HOH A O   1 
HETATM 2319 O O   . HOH M 5 .  ? -9.633  -16.439 10.157  1.00 59.33  ? 290 HOH A O   1 
HETATM 2320 O O   . HOH M 5 .  ? 13.594  -15.368 -12.325 1.00 54.31  ? 291 HOH A O   1 
HETATM 2321 O O   . HOH M 5 .  ? -3.747  -26.698 7.354   1.00 68.12  ? 292 HOH A O   1 
HETATM 2322 O O   . HOH M 5 .  ? 15.264  -28.761 -1.226  1.00 54.56  ? 293 HOH A O   1 
HETATM 2323 O O   . HOH M 5 .  ? -5.154  -23.613 -6.704  1.00 45.47  ? 294 HOH A O   1 
HETATM 2324 O O   . HOH M 5 .  ? 8.969   -8.982  -13.843 1.00 38.39  ? 295 HOH A O   1 
HETATM 2325 O O   . HOH M 5 .  ? -8.661  -15.620 -13.040 1.00 58.00  ? 296 HOH A O   1 
HETATM 2326 O O   . HOH M 5 .  ? 5.285   -7.049  -11.045 1.00 43.40  ? 297 HOH A O   1 
HETATM 2327 O O   . HOH M 5 .  ? 12.612  -21.362 10.531  1.00 49.29  ? 298 HOH A O   1 
HETATM 2328 O O   . HOH M 5 .  ? -0.597  -3.312  -11.062 1.00 68.92  ? 299 HOH A O   1 
HETATM 2329 O O   . HOH M 5 .  ? -6.908  -14.209 -9.243  1.00 39.81  ? 300 HOH A O   1 
HETATM 2330 O O   . HOH M 5 .  ? -3.567  -11.255 9.463   1.00 55.64  ? 301 HOH A O   1 
HETATM 2331 O O   . HOH M 5 .  ? 8.821   -12.952 12.641  1.00 61.95  ? 302 HOH A O   1 
HETATM 2332 O O   . HOH M 5 .  ? 7.998   -30.658 -1.906  1.00 63.85  ? 303 HOH A O   1 
HETATM 2333 O O   . HOH M 5 .  ? -10.149 -28.527 -1.729  1.00 55.69  ? 304 HOH A O   1 
HETATM 2334 O O   . HOH M 5 .  ? -9.028  -19.157 1.834   1.00 51.47  ? 305 HOH A O   1 
HETATM 2335 O O   . HOH M 5 .  ? -5.387  -23.006 5.810   1.00 52.88  ? 306 HOH A O   1 
HETATM 2336 O O   . HOH M 5 .  ? 17.510  -30.328 1.637   1.00 60.21  ? 307 HOH A O   1 
HETATM 2337 O O   . HOH M 5 .  ? 5.391   2.986   3.236   1.00 74.82  ? 308 HOH A O   1 
HETATM 2338 O O   . HOH M 5 .  ? 12.532  -11.278 12.207  1.00 63.18  ? 309 HOH A O   1 
HETATM 2339 O O   . HOH M 5 .  ? 5.151   -9.357  -11.236 1.00 49.02  ? 310 HOH A O   1 
HETATM 2340 O O   . HOH M 5 .  ? -10.938 -13.536 -2.926  1.00 43.21  ? 311 HOH A O   1 
HETATM 2341 O O   . HOH M 5 .  ? 8.592   -8.328  4.477   1.00 39.16  ? 312 HOH A O   1 
HETATM 2342 O O   . HOH M 5 .  ? -7.074  -19.409 8.150   1.00 47.93  ? 313 HOH A O   1 
HETATM 2343 O O   . HOH M 5 .  ? -4.422  -21.155 -8.338  1.00 57.09  ? 314 HOH A O   1 
HETATM 2344 O O   . HOH M 5 .  ? 9.082   -22.512 -19.279 1.00 64.29  ? 315 HOH A O   1 
HETATM 2345 O O   . HOH M 5 .  ? 5.329   -3.488  1.691   1.00 74.89  ? 316 HOH A O   1 
HETATM 2346 O O   . HOH N 5 .  ? 30.757  -7.802  -30.372 1.00 52.01  ? 201 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 2.015   -16.277 -32.612 1.00 64.13  ? 202 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 7.210   -17.880 -32.079 1.00 51.53  ? 203 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 9.995   -10.986 -38.305 1.00 50.70  ? 204 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 6.809   -12.190 -26.317 1.00 44.55  ? 205 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 26.259  -22.884 -31.389 1.00 36.84  ? 206 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 30.435  -19.601 -40.550 1.00 38.10  ? 207 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 28.020  -8.022  -29.092 1.00 41.05  ? 208 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 20.457  -22.131 -23.272 1.00 63.46  ? 209 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 3.120   -8.732  -27.352 1.00 56.07  ? 210 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 16.438  -16.804 -19.207 1.00 45.65  ? 211 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 23.450  -2.051  -29.419 1.00 49.99  ? 212 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 30.590  -12.381 -46.019 1.00 71.07  ? 213 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 20.941  -25.516 -30.329 1.00 65.20  ? 214 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 11.274  -7.858  -41.531 1.00 52.27  ? 215 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 26.201  -11.756 -22.689 1.00 44.96  ? 216 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 20.616  -13.201 -43.055 1.00 40.47  ? 217 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 24.515  -1.587  -36.318 1.00 48.90  ? 218 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 26.083  -4.312  -33.860 1.00 46.09  ? 219 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 27.226  -10.353 -29.185 1.00 47.85  ? 220 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 13.472  -22.641 -20.975 1.00 57.84  ? 221 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 18.896  -0.328  -25.633 1.00 53.70  ? 222 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 7.161   -19.412 -35.197 1.00 51.58  ? 223 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 8.804   -27.710 -38.583 1.00 52.85  ? 224 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 10.188  -16.644 -44.565 1.00 47.26  ? 225 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 6.034   -7.053  -32.419 1.00 48.06  ? 226 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 25.222  -4.819  -29.953 1.00 37.94  ? 227 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 24.869  -15.141 -22.767 1.00 44.91  ? 228 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 17.730  -19.688 -42.303 1.00 46.62  ? 229 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 23.539  -5.755  -24.776 1.00 47.34  ? 230 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 17.879  -3.228  -22.542 1.00 55.49  ? 231 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 10.615  -18.743 -33.144 1.00 30.59  ? 232 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 34.683  -23.182 -30.317 1.00 66.07  ? 233 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 13.002  -4.468  -42.257 1.00 52.43  ? 234 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 17.026  -19.037 -28.993 1.00 27.96  ? 235 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 14.392  -6.274  -41.370 1.00 39.98  ? 236 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 23.802  -3.939  -37.105 1.00 30.13  ? 237 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 10.406  -19.149 -43.356 1.00 58.97  ? 238 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 20.082  -25.505 -34.246 1.00 42.13  ? 239 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 31.770  -12.167 -39.312 1.00 65.74  ? 240 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 7.686   -12.445 -39.092 1.00 54.01  ? 241 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 21.304  3.944   -32.933 1.00 36.85  ? 242 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 12.585  -4.581  -25.012 1.00 46.60  ? 243 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 10.860  -21.820 -32.871 1.00 39.27  ? 244 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 18.186  -0.315  -38.796 1.00 28.76  ? 245 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 28.068  -17.424 -25.160 1.00 47.27  ? 246 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 25.375  -5.612  -36.080 1.00 45.07  ? 247 HOH B O   1 
HETATM 2393 O O   . HOH N 5 .  ? 26.198  -0.076  -29.463 1.00 55.57  ? 248 HOH B O   1 
HETATM 2394 O O   . HOH N 5 .  ? 17.058  -9.355  -44.314 1.00 48.54  ? 249 HOH B O   1 
HETATM 2395 O O   . HOH N 5 .  ? 22.787  -23.172 -28.927 1.00 44.74  ? 250 HOH B O   1 
HETATM 2396 O O   . HOH N 5 .  ? 23.835  -11.022 -22.229 1.00 36.24  ? 251 HOH B O   1 
HETATM 2397 O O   . HOH N 5 .  ? 20.518  -2.512  -23.194 1.00 63.93  ? 252 HOH B O   1 
HETATM 2398 O O   . HOH N 5 .  ? 18.584  -25.824 -29.053 1.00 44.16  ? 253 HOH B O   1 
HETATM 2399 O O   . HOH N 5 .  ? 20.527  -10.027 -43.302 1.00 38.32  ? 254 HOH B O   1 
HETATM 2400 O O   . HOH N 5 .  ? 33.067  -18.564 -42.891 1.00 62.59  ? 255 HOH B O   1 
HETATM 2401 O O   . HOH N 5 .  ? 8.998   -8.671  -16.705 1.00 44.16  ? 256 HOH B O   1 
HETATM 2402 O O   . HOH N 5 .  ? 32.011  -21.063 -38.381 1.00 42.12  ? 257 HOH B O   1 
HETATM 2403 O O   . HOH N 5 .  ? 7.946   -8.021  -20.933 1.00 51.01  ? 258 HOH B O   1 
HETATM 2404 O O   . HOH N 5 .  ? 21.208  -6.308  -42.859 1.00 35.71  ? 259 HOH B O   1 
HETATM 2405 O O   . HOH N 5 .  ? 14.876  -24.413 -40.634 1.00 42.64  ? 260 HOH B O   1 
HETATM 2406 O O   . HOH N 5 .  ? 25.229  -7.758  -23.088 1.00 54.43  ? 261 HOH B O   1 
HETATM 2407 O O   . HOH N 5 .  ? 1.795   -13.110 -28.603 1.00 53.65  ? 262 HOH B O   1 
HETATM 2408 O O   . HOH N 5 .  ? 6.525   -20.555 -25.187 1.00 40.68  ? 263 HOH B O   1 
HETATM 2409 O O   . HOH N 5 .  ? 7.688   -14.638 -44.205 1.00 66.70  ? 264 HOH B O   1 
HETATM 2410 O O   . HOH N 5 .  ? 18.477  4.895   -34.509 1.00 40.08  ? 265 HOH B O   1 
HETATM 2411 O O   . HOH N 5 .  ? 28.185  -24.658 -35.273 1.00 39.46  ? 266 HOH B O   1 
HETATM 2412 O O   . HOH N 5 .  ? 18.247  -15.919 -46.090 1.00 54.73  ? 267 HOH B O   1 
HETATM 2413 O O   . HOH N 5 .  ? 24.836  -6.125  -43.026 1.00 46.80  ? 268 HOH B O   1 
HETATM 2414 O O   . HOH N 5 .  ? 15.207  -7.955  -43.343 1.00 42.97  ? 269 HOH B O   1 
HETATM 2415 O O   . HOH N 5 .  ? 14.080  -20.610 -20.414 1.00 56.28  ? 270 HOH B O   1 
HETATM 2416 O O   . HOH N 5 .  ? 18.946  -13.201 -44.940 1.00 49.70  ? 271 HOH B O   1 
HETATM 2417 O O   . HOH N 5 .  ? 17.389  -25.433 -21.139 1.00 56.34  ? 272 HOH B O   1 
HETATM 2418 O O   . HOH N 5 .  ? 9.630   -6.029  -41.357 1.00 54.97  ? 273 HOH B O   1 
HETATM 2419 O O   . HOH N 5 .  ? 40.030  -13.354 -39.842 1.00 76.02  ? 274 HOH B O   1 
HETATM 2420 O O   . HOH N 5 .  ? 29.068  -12.027 -26.778 1.00 58.45  ? 275 HOH B O   1 
HETATM 2421 O O   . HOH N 5 .  ? 19.900  4.377   -33.503 1.00 49.89  ? 276 HOH B O   1 
HETATM 2422 O O   . HOH N 5 .  ? 16.695  2.291   -30.871 1.00 58.74  ? 277 HOH B O   1 
HETATM 2423 O O   . HOH N 5 .  ? 11.406  -23.825 -30.054 1.00 53.24  ? 278 HOH B O   1 
HETATM 2424 O O   . HOH N 5 .  ? 15.176  -21.632 -42.222 1.00 53.40  ? 279 HOH B O   1 
HETATM 2425 O O   . HOH N 5 .  ? 28.977  -7.075  -26.733 1.00 48.12  ? 280 HOH B O   1 
HETATM 2426 O O   . HOH N 5 .  ? 7.488   -9.958  -18.764 1.00 41.02  ? 281 HOH B O   1 
HETATM 2427 O O   . HOH N 5 .  ? 22.812  -29.256 -35.784 1.00 43.47  ? 282 HOH B O   1 
HETATM 2428 O O   . HOH O 5 .  ? 27.493  -38.274 10.341  1.00 46.71  ? 201 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 20.551  -20.033 30.118  1.00 58.04  ? 202 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 25.915  -19.774 6.728   1.00 48.49  ? 203 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 26.833  -15.854 11.857  1.00 62.60  ? 204 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 19.769  -20.361 10.459  1.00 45.08  ? 205 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 27.755  -19.227 13.247  1.00 59.14  ? 206 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 28.226  -37.723 25.169  1.00 51.86  ? 207 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 17.580  -17.486 15.194  1.00 53.84  ? 208 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 27.028  -39.666 12.781  1.00 39.60  ? 209 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 26.683  -18.180 20.826  1.00 54.78  ? 210 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 6.322   -27.001 16.560  1.00 65.16  ? 211 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 25.973  -17.651 14.043  1.00 45.94  ? 212 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 28.343  -37.721 16.018  1.00 44.49  ? 213 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 33.764  -24.685 31.736  1.00 49.65  ? 214 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 13.357  -31.810 8.141   1.00 32.98  ? 215 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 8.356   -32.012 11.849  1.00 66.45  ? 216 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 12.278  -29.294 27.941  1.00 58.04  ? 217 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 16.119  -17.926 19.369  1.00 42.27  ? 218 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 32.084  -33.992 26.039  1.00 57.78  ? 219 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 23.968  -21.147 24.101  1.00 50.00  ? 220 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 20.511  -42.279 12.168  1.00 30.87  ? 221 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 30.861  -31.867 15.838  1.00 57.56  ? 222 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 15.807  -21.310 12.320  1.00 39.93  ? 223 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 22.671  -28.755 11.167  1.00 37.67  ? 224 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 23.898  -18.979 21.859  1.00 51.82  ? 225 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 25.894  -34.081 34.942  1.00 57.24  ? 226 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 22.571  -34.703 16.549  1.00 29.10  ? 227 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 28.959  -15.464 12.817  1.00 51.12  ? 228 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 23.316  -42.121 18.663  1.00 41.18  ? 229 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 31.409  -44.056 15.929  1.00 65.28  ? 230 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 7.286   -18.254 10.760  1.00 41.91  ? 231 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 26.040  -39.747 20.244  1.00 38.25  ? 232 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 21.021  -40.335 26.661  1.00 40.75  ? 233 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 21.454  -28.981 8.445   1.00 41.33  ? 234 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 15.216  -37.391 13.274  1.00 39.92  ? 235 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 21.679  -19.765 24.521  1.00 52.07  ? 236 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 19.941  -41.645 39.402  1.00 67.86  ? 237 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 14.941  -38.898 9.355   1.00 54.63  ? 238 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 30.886  -36.148 28.918  1.00 49.57  ? 239 HOH C O   1 
HETATM 2467 O O   . HOH O 5 .  ? 29.921  -40.456 31.592  1.00 45.85  ? 240 HOH C O   1 
HETATM 2468 O O   . HOH O 5 .  ? 25.786  -31.644 10.774  1.00 38.55  ? 241 HOH C O   1 
HETATM 2469 O O   . HOH O 5 .  ? 10.270  -30.628 9.772   1.00 37.13  ? 242 HOH C O   1 
HETATM 2470 O O   . HOH O 5 .  ? 9.617   -19.075 23.747  1.00 49.04  ? 243 HOH C O   1 
HETATM 2471 O O   . HOH O 5 .  ? 21.850  -29.435 4.657   1.00 64.81  ? 244 HOH C O   1 
HETATM 2472 O O   . HOH O 5 .  ? 19.721  -26.775 2.777   1.00 51.20  ? 245 HOH C O   1 
HETATM 2473 O O   . HOH O 5 .  ? 28.459  -37.258 18.767  1.00 50.98  ? 246 HOH C O   1 
HETATM 2474 O O   . HOH O 5 .  ? 13.164  -39.070 24.070  1.00 52.16  ? 247 HOH C O   1 
HETATM 2475 O O   . HOH O 5 .  ? 16.668  -38.587 11.485  1.00 52.06  ? 248 HOH C O   1 
HETATM 2476 O O   . HOH O 5 .  ? 31.519  -40.400 27.373  1.00 42.40  ? 249 HOH C O   1 
HETATM 2477 O O   . HOH O 5 .  ? 6.318   -34.749 19.323  1.00 61.88  ? 250 HOH C O   1 
HETATM 2478 O O   . HOH O 5 .  ? 15.076  -29.534 3.690   1.00 43.70  ? 251 HOH C O   1 
HETATM 2479 O O   . HOH O 5 .  ? 29.278  -25.526 32.714  1.00 46.86  ? 252 HOH C O   1 
HETATM 2480 O O   . HOH O 5 .  ? 28.787  -39.635 24.322  1.00 60.95  ? 253 HOH C O   1 
HETATM 2481 O O   . HOH O 5 .  ? 30.733  -33.294 18.481  1.00 50.02  ? 254 HOH C O   1 
HETATM 2482 O O   . HOH O 5 .  ? 21.069  -13.208 13.317  1.00 47.53  ? 255 HOH C O   1 
HETATM 2483 O O   . HOH O 5 .  ? 16.433  -19.733 29.488  1.00 55.23  ? 256 HOH C O   1 
HETATM 2484 O O   . HOH O 5 .  ? 2.656   -28.333 14.343  1.00 56.21  ? 257 HOH C O   1 
HETATM 2485 O O   . HOH O 5 .  ? 20.370  -37.094 40.606  1.00 62.92  ? 258 HOH C O   1 
HETATM 2486 O O   . HOH O 5 .  ? 7.554   -31.910 24.155  1.00 68.87  ? 259 HOH C O   1 
HETATM 2487 O O   . HOH O 5 .  ? 32.927  -43.983 12.047  1.00 57.40  ? 260 HOH C O   1 
HETATM 2488 O O   . HOH O 5 .  ? 17.448  -36.930 29.142  1.00 55.04  ? 261 HOH C O   1 
HETATM 2489 O O   . HOH O 5 .  ? 23.287  -39.729 23.245  1.00 56.16  ? 262 HOH C O   1 
HETATM 2490 O O   . HOH O 5 .  ? 29.482  -42.066 27.365  1.00 41.36  ? 263 HOH C O   1 
HETATM 2491 O O   . HOH O 5 .  ? 23.125  -14.111 13.655  1.00 51.07  ? 264 HOH C O   1 
HETATM 2492 O O   . HOH O 5 .  ? 24.909  -40.726 20.810  1.00 46.51  ? 265 HOH C O   1 
HETATM 2493 O O   . HOH O 5 .  ? 13.786  -23.345 28.124  1.00 56.54  ? 266 HOH C O   1 
HETATM 2494 O O   . HOH O 5 .  ? 5.229   -24.214 18.384  1.00 67.94  ? 267 HOH C O   1 
HETATM 2495 O O   . HOH O 5 .  ? 24.045  -16.031 12.199  1.00 53.49  ? 268 HOH C O   1 
HETATM 2496 O O   . HOH O 5 .  ? 31.031  -20.796 25.658  1.00 63.24  ? 269 HOH C O   1 
HETATM 2497 O O   . HOH O 5 .  ? 25.199  -18.731 31.336  1.00 58.77  ? 270 HOH C O   1 
HETATM 2498 O O   . HOH O 5 .  ? 9.303   -35.997 14.329  1.00 55.70  ? 271 HOH C O   1 
HETATM 2499 O O   . HOH O 5 .  ? 28.725  -42.044 29.932  1.00 41.05  ? 272 HOH C O   1 
HETATM 2500 O O   . HOH O 5 .  ? 17.366  -43.268 40.263  1.00 57.40  ? 273 HOH C O   1 
HETATM 2501 O O   . HOH O 5 .  ? 33.840  -45.095 15.471  1.00 41.66  ? 274 HOH C O   1 
HETATM 2502 O O   . HOH O 5 .  ? 37.628  -25.698 26.344  1.00 76.10  ? 275 HOH C O   1 
# 
