data_7HH1
# 
_entry.id   7HH1 
# 
_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   7HH1         pdb_00007hh1 10.2210/pdb7hh1/pdb 
WWPDB D_1001407463 ?            ?                   
# 
_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                        7HH1 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn 'N-(2-fluorophenyl)ethanesulfonamide'              203.234   1   ? ?    ? ? 
5 water       nat water                                              18.015    275 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                         SO4 
3 1,2-ETHANEDIOL                        EDO 
4 'N-(2-fluorophenyl)ethanesulfonamide' VVG 
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 
VVG non-polymer         . 'N-(2-fluorophenyl)ethanesulfonamide' ?                 'C8 H10 F N O2 S' 203.234 
# 
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 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        VVG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   VVG 
_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 VVG 1   103 101 VVG LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 84  HOH HOH A . 
M 5 HOH 3   203 337 HOH HOH A . 
M 5 HOH 4   204 202 HOH HOH A . 
M 5 HOH 5   205 259 HOH HOH A . 
M 5 HOH 6   206 139 HOH HOH A . 
M 5 HOH 7   207 362 HOH HOH A . 
M 5 HOH 8   208 304 HOH HOH A . 
M 5 HOH 9   209 361 HOH HOH A . 
M 5 HOH 10  210 66  HOH HOH A . 
M 5 HOH 11  211 346 HOH HOH A . 
M 5 HOH 12  212 341 HOH HOH A . 
M 5 HOH 13  213 86  HOH HOH A . 
M 5 HOH 14  214 71  HOH HOH A . 
M 5 HOH 15  215 87  HOH HOH A . 
M 5 HOH 16  216 95  HOH HOH A . 
M 5 HOH 17  217 37  HOH HOH A . 
M 5 HOH 18  218 55  HOH HOH A . 
M 5 HOH 19  219 26  HOH HOH A . 
M 5 HOH 20  220 199 HOH HOH A . 
M 5 HOH 21  221 289 HOH HOH A . 
M 5 HOH 22  222 334 HOH HOH A . 
M 5 HOH 23  223 208 HOH HOH A . 
M 5 HOH 24  224 343 HOH HOH A . 
M 5 HOH 25  225 28  HOH HOH A . 
M 5 HOH 26  226 91  HOH HOH A . 
M 5 HOH 27  227 8   HOH HOH A . 
M 5 HOH 28  228 260 HOH HOH A . 
M 5 HOH 29  229 293 HOH HOH A . 
M 5 HOH 30  230 179 HOH HOH A . 
M 5 HOH 31  231 7   HOH HOH A . 
M 5 HOH 32  232 32  HOH HOH A . 
M 5 HOH 33  233 167 HOH HOH A . 
M 5 HOH 34  234 23  HOH HOH A . 
M 5 HOH 35  235 34  HOH HOH A . 
M 5 HOH 36  236 97  HOH HOH A . 
M 5 HOH 37  237 188 HOH HOH A . 
M 5 HOH 38  238 77  HOH HOH A . 
M 5 HOH 39  239 218 HOH HOH A . 
M 5 HOH 40  240 58  HOH HOH A . 
M 5 HOH 41  241 290 HOH HOH A . 
M 5 HOH 42  242 111 HOH HOH A . 
M 5 HOH 43  243 292 HOH HOH A . 
M 5 HOH 44  244 335 HOH HOH A . 
M 5 HOH 45  245 27  HOH HOH A . 
M 5 HOH 46  246 2   HOH HOH A . 
M 5 HOH 47  247 41  HOH HOH A . 
M 5 HOH 48  248 47  HOH HOH A . 
M 5 HOH 49  249 267 HOH HOH A . 
M 5 HOH 50  250 278 HOH HOH A . 
M 5 HOH 51  251 12  HOH HOH A . 
M 5 HOH 52  252 1   HOH HOH A . 
M 5 HOH 53  253 274 HOH HOH A . 
M 5 HOH 54  254 60  HOH HOH A . 
M 5 HOH 55  255 145 HOH HOH A . 
M 5 HOH 56  256 203 HOH HOH A . 
M 5 HOH 57  257 190 HOH HOH A . 
M 5 HOH 58  258 288 HOH HOH A . 
M 5 HOH 59  259 99  HOH HOH A . 
M 5 HOH 60  260 300 HOH HOH A . 
M 5 HOH 61  261 109 HOH HOH A . 
M 5 HOH 62  262 299 HOH HOH A . 
M 5 HOH 63  263 164 HOH HOH A . 
M 5 HOH 64  264 78  HOH HOH A . 
M 5 HOH 65  265 42  HOH HOH A . 
M 5 HOH 66  266 21  HOH HOH A . 
M 5 HOH 67  267 94  HOH HOH A . 
M 5 HOH 68  268 38  HOH HOH A . 
M 5 HOH 69  269 20  HOH HOH A . 
M 5 HOH 70  270 364 HOH HOH A . 
M 5 HOH 71  271 18  HOH HOH A . 
M 5 HOH 72  272 222 HOH HOH A . 
M 5 HOH 73  273 143 HOH HOH A . 
M 5 HOH 74  274 115 HOH HOH A . 
M 5 HOH 75  275 93  HOH HOH A . 
M 5 HOH 76  276 14  HOH HOH A . 
M 5 HOH 77  277 116 HOH HOH A . 
M 5 HOH 78  278 9   HOH HOH A . 
M 5 HOH 79  279 287 HOH HOH A . 
M 5 HOH 80  280 327 HOH HOH A . 
M 5 HOH 81  281 131 HOH HOH A . 
M 5 HOH 82  282 113 HOH HOH A . 
M 5 HOH 83  283 19  HOH HOH A . 
M 5 HOH 84  284 281 HOH HOH A . 
M 5 HOH 85  285 16  HOH HOH A . 
M 5 HOH 86  286 152 HOH HOH A . 
M 5 HOH 87  287 64  HOH HOH A . 
M 5 HOH 88  288 165 HOH HOH A . 
M 5 HOH 89  289 301 HOH HOH A . 
M 5 HOH 90  290 318 HOH HOH A . 
M 5 HOH 91  291 73  HOH HOH A . 
M 5 HOH 92  292 349 HOH HOH A . 
M 5 HOH 93  293 211 HOH HOH A . 
M 5 HOH 94  294 375 HOH HOH A . 
M 5 HOH 95  295 63  HOH HOH A . 
M 5 HOH 96  296 31  HOH HOH A . 
M 5 HOH 97  297 296 HOH HOH A . 
M 5 HOH 98  298 22  HOH HOH A . 
M 5 HOH 99  299 210 HOH HOH A . 
M 5 HOH 100 300 108 HOH HOH A . 
M 5 HOH 101 301 363 HOH HOH A . 
M 5 HOH 102 302 270 HOH HOH A . 
M 5 HOH 103 303 185 HOH HOH A . 
M 5 HOH 104 304 83  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 75  HOH HOH A . 
M 5 HOH 108 308 357 HOH HOH A . 
M 5 HOH 109 309 336 HOH HOH A . 
M 5 HOH 110 310 57  HOH HOH A . 
M 5 HOH 111 311 35  HOH HOH A . 
M 5 HOH 112 312 283 HOH HOH A . 
M 5 HOH 113 313 342 HOH HOH A . 
M 5 HOH 114 314 156 HOH HOH A . 
M 5 HOH 115 315 313 HOH HOH A . 
M 5 HOH 116 316 125 HOH HOH A . 
M 5 HOH 117 317 332 HOH HOH A . 
M 5 HOH 118 318 368 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 331 HOH HOH B . 
N 5 HOH 3   203 224 HOH HOH B . 
N 5 HOH 4   204 272 HOH HOH B . 
N 5 HOH 5   205 98  HOH HOH B . 
N 5 HOH 6   206 172 HOH HOH B . 
N 5 HOH 7   207 153 HOH HOH B . 
N 5 HOH 8   208 184 HOH HOH B . 
N 5 HOH 9   209 69  HOH HOH B . 
N 5 HOH 10  210 258 HOH HOH B . 
N 5 HOH 11  211 360 HOH HOH B . 
N 5 HOH 12  212 17  HOH HOH B . 
N 5 HOH 13  213 89  HOH HOH B . 
N 5 HOH 14  214 150 HOH HOH B . 
N 5 HOH 15  215 329 HOH HOH B . 
N 5 HOH 16  216 177 HOH HOH B . 
N 5 HOH 17  217 249 HOH HOH B . 
N 5 HOH 18  218 168 HOH HOH B . 
N 5 HOH 19  219 320 HOH HOH B . 
N 5 HOH 20  220 123 HOH HOH B . 
N 5 HOH 21  221 137 HOH HOH B . 
N 5 HOH 22  222 223 HOH HOH B . 
N 5 HOH 23  223 373 HOH HOH B . 
N 5 HOH 24  224 279 HOH HOH B . 
N 5 HOH 25  225 72  HOH HOH B . 
N 5 HOH 26  226 6   HOH HOH B . 
N 5 HOH 27  227 280 HOH HOH B . 
N 5 HOH 28  228 54  HOH HOH B . 
N 5 HOH 29  229 358 HOH HOH B . 
N 5 HOH 30  230 59  HOH HOH B . 
N 5 HOH 31  231 10  HOH HOH B . 
N 5 HOH 32  232 169 HOH HOH B . 
N 5 HOH 33  233 96  HOH HOH B . 
N 5 HOH 34  234 242 HOH HOH B . 
N 5 HOH 35  235 333 HOH HOH B . 
N 5 HOH 36  236 68  HOH HOH B . 
N 5 HOH 37  237 5   HOH HOH B . 
N 5 HOH 38  238 315 HOH HOH B . 
N 5 HOH 39  239 352 HOH HOH B . 
N 5 HOH 40  240 117 HOH HOH B . 
N 5 HOH 41  241 215 HOH HOH B . 
N 5 HOH 42  242 261 HOH HOH B . 
N 5 HOH 43  243 170 HOH HOH B . 
N 5 HOH 44  244 25  HOH HOH B . 
N 5 HOH 45  245 119 HOH HOH B . 
N 5 HOH 46  246 24  HOH HOH B . 
N 5 HOH 47  247 61  HOH HOH B . 
N 5 HOH 48  248 175 HOH HOH B . 
N 5 HOH 49  249 74  HOH HOH B . 
N 5 HOH 50  250 76  HOH HOH B . 
N 5 HOH 51  251 13  HOH HOH B . 
N 5 HOH 52  252 101 HOH HOH B . 
N 5 HOH 53  253 217 HOH HOH B . 
N 5 HOH 54  254 355 HOH HOH B . 
N 5 HOH 55  255 36  HOH HOH B . 
N 5 HOH 56  256 157 HOH HOH B . 
N 5 HOH 57  257 339 HOH HOH B . 
N 5 HOH 58  258 104 HOH HOH B . 
N 5 HOH 59  259 79  HOH HOH B . 
N 5 HOH 60  260 46  HOH HOH B . 
N 5 HOH 61  261 120 HOH HOH B . 
N 5 HOH 62  262 365 HOH HOH B . 
N 5 HOH 63  263 44  HOH HOH B . 
N 5 HOH 64  264 197 HOH HOH B . 
N 5 HOH 65  265 182 HOH HOH B . 
N 5 HOH 66  266 214 HOH HOH B . 
N 5 HOH 67  267 303 HOH HOH B . 
N 5 HOH 68  268 370 HOH HOH B . 
N 5 HOH 69  269 322 HOH HOH B . 
N 5 HOH 70  270 291 HOH HOH B . 
N 5 HOH 71  271 316 HOH HOH B . 
N 5 HOH 72  272 201 HOH HOH B . 
N 5 HOH 73  273 356 HOH HOH B . 
N 5 HOH 74  274 160 HOH HOH B . 
N 5 HOH 75  275 372 HOH HOH B . 
N 5 HOH 76  276 163 HOH HOH B . 
N 5 HOH 77  277 345 HOH HOH B . 
N 5 HOH 78  278 366 HOH HOH B . 
N 5 HOH 79  279 103 HOH HOH B . 
N 5 HOH 80  280 338 HOH HOH B . 
N 5 HOH 81  281 314 HOH HOH B . 
N 5 HOH 82  282 107 HOH HOH B . 
N 5 HOH 83  283 312 HOH HOH B . 
O 5 HOH 1   201 321 HOH HOH C . 
O 5 HOH 2   202 254 HOH HOH C . 
O 5 HOH 3   203 347 HOH HOH C . 
O 5 HOH 4   204 323 HOH HOH C . 
O 5 HOH 5   205 353 HOH HOH C . 
O 5 HOH 6   206 325 HOH HOH C . 
O 5 HOH 7   207 271 HOH HOH C . 
O 5 HOH 8   208 317 HOH HOH C . 
O 5 HOH 9   209 90  HOH HOH C . 
O 5 HOH 10  210 302 HOH HOH C . 
O 5 HOH 11  211 118 HOH HOH C . 
O 5 HOH 12  212 134 HOH HOH C . 
O 5 HOH 13  213 294 HOH HOH C . 
O 5 HOH 14  214 351 HOH HOH C . 
O 5 HOH 15  215 226 HOH HOH C . 
O 5 HOH 16  216 142 HOH HOH C . 
O 5 HOH 17  217 15  HOH HOH C . 
O 5 HOH 18  218 85  HOH HOH C . 
O 5 HOH 19  219 173 HOH HOH C . 
O 5 HOH 20  220 53  HOH HOH C . 
O 5 HOH 21  221 189 HOH HOH C . 
O 5 HOH 22  222 269 HOH HOH C . 
O 5 HOH 23  223 326 HOH HOH C . 
O 5 HOH 24  224 82  HOH HOH C . 
O 5 HOH 25  225 126 HOH HOH C . 
O 5 HOH 26  226 132 HOH HOH C . 
O 5 HOH 27  227 275 HOH HOH C . 
O 5 HOH 28  228 49  HOH HOH C . 
O 5 HOH 29  229 40  HOH HOH C . 
O 5 HOH 30  230 45  HOH HOH C . 
O 5 HOH 31  231 309 HOH HOH C . 
O 5 HOH 32  232 284 HOH HOH C . 
O 5 HOH 33  233 374 HOH HOH C . 
O 5 HOH 34  234 295 HOH HOH C . 
O 5 HOH 35  235 122 HOH HOH C . 
O 5 HOH 36  236 48  HOH HOH C . 
O 5 HOH 37  237 102 HOH HOH C . 
O 5 HOH 38  238 4   HOH HOH C . 
O 5 HOH 39  239 148 HOH HOH C . 
O 5 HOH 40  240 161 HOH HOH C . 
O 5 HOH 41  241 56  HOH HOH C . 
O 5 HOH 42  242 43  HOH HOH C . 
O 5 HOH 43  243 151 HOH HOH C . 
O 5 HOH 44  244 135 HOH HOH C . 
O 5 HOH 45  245 328 HOH HOH C . 
O 5 HOH 46  246 198 HOH HOH C . 
O 5 HOH 47  247 62  HOH HOH C . 
O 5 HOH 48  248 209 HOH HOH C . 
O 5 HOH 49  249 130 HOH HOH C . 
O 5 HOH 50  250 67  HOH HOH C . 
O 5 HOH 51  251 298 HOH HOH C . 
O 5 HOH 52  252 344 HOH HOH C . 
O 5 HOH 53  253 348 HOH HOH C . 
O 5 HOH 54  254 65  HOH HOH C . 
O 5 HOH 55  255 171 HOH HOH C . 
O 5 HOH 56  256 149 HOH HOH C . 
O 5 HOH 57  257 305 HOH HOH C . 
O 5 HOH 58  258 146 HOH HOH C . 
O 5 HOH 59  259 241 HOH HOH C . 
O 5 HOH 60  260 70  HOH HOH C . 
O 5 HOH 61  261 330 HOH HOH C . 
O 5 HOH 62  262 371 HOH HOH C . 
O 5 HOH 63  263 324 HOH HOH C . 
O 5 HOH 64  264 246 HOH HOH C . 
O 5 HOH 65  265 354 HOH HOH C . 
O 5 HOH 66  266 319 HOH HOH C . 
O 5 HOH 67  267 369 HOH HOH C . 
O 5 HOH 68  268 367 HOH HOH C . 
O 5 HOH 69  269 359 HOH HOH C . 
O 5 HOH 70  270 340 HOH HOH C . 
O 5 HOH 71  271 92  HOH HOH C . 
O 5 HOH 72  272 206 HOH HOH C . 
O 5 HOH 73  273 350 HOH HOH C . 
O 5 HOH 74  274 310 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 LYS 70 ? CE  ? A LYS 71 CE  
4  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
8  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
9  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
10 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
11 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
12 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
13 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
14 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
19 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
20 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
21 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
22 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
23 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
24 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
25 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
26 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
27 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
28 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
29 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
30 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
31 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
32 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
33 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
34 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
35 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
36 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
37 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
38 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
39 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
40 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
41 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
42 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
43 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
44 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
45 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
46 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
47 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
48 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
49 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
50 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
51 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
52 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
53 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
54 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
55 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           7HH1 
_cell.length_a           41.630 
_cell.length_b           42.280 
_cell.length_c           158.960 
_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                         7HH1 
_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          7HH1 
_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                     7HH1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.48 
_reflns.d_resolution_high            1.53 
_reflns.number_obs                   43442 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.076 
_reflns.pdbx_netI_over_sigmaI        10.5 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.083 
_reflns.pdbx_Rpim_I_all              0.033 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     265275 
_reflns.pdbx_chi_squared             0.97 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.53 
_reflns_shell.d_res_low                   1.57 
_reflns_shell.number_measured_all         16266 
_reflns_shell.number_unique_obs           3170 
_reflns_shell.Rmerge_I_obs                1.646 
_reflns_shell.pdbx_chi_squared            0.79 
_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             1.835 
_reflns_shell.pdbx_Rpim_I_all             0.801 
_reflns_shell.pdbx_CC_half                0.359 
_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                                 7HH1 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     41068 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             79.48 
_refine.ls_d_res_high                            1.53 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_R_factor_obs                          0.20623 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20439 
_refine.ls_R_factor_R_free                       0.23890 
_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                  2299 
_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          0.955 
_refine.B_iso_mean                               35.364 
_refine.aniso_B[1][1]                            0.87 
_refine.aniso_B[2][2]                            -0.39 
_refine.aniso_B[3][3]                            -0.48 
_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                       0.090 
_refine.pdbx_overall_ESU_R_Free                  0.091 
_refine.overall_SU_ML                            0.081 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.337 
_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        2132 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             275 
_refine_hist.number_atoms_total               2458 
_refine_hist.d_res_high                       1.53 
_refine_hist.d_res_low                        79.48 
# 
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  ? 2276 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.968  1.833  ? 3096 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.864  5.000  ? 263  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.140  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.007 10.000 ? 298  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.132  0.200  ? 285  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1886 '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                  3.297  3.252  ? 1064 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.651  5.809  ? 1324 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.592  3.560  ? 1212 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.930  49.76  ? 3569 '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                       1.530 
_refine_ls_shell.d_res_low                        1.570 
_refine_ls_shell.number_reflns_R_work             2992 
_refine_ls_shell.R_factor_R_work                  0.342 
_refine_ls_shell.percent_reflns_obs               99.84 
_refine_ls_shell.R_factor_R_free                  0.347 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             174 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH1 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z53825177' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH1 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HH1 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH1 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH1 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 7HH1 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH1 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH1 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH1 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH1 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH1 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HH1 
_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 227 ? ? O B HOH 269 ? ? 1.42 
2  1 O  A HOH 224 ? ? O A HOH 240 ? ? 1.93 
3  1 O2 A SO4 104 ? ? O A HOH 201 ? ? 1.94 
4  1 O  A HOH 302 ? ? O C HOH 205 ? ? 1.96 
5  1 O  B HOH 205 ? ? O B HOH 277 ? ? 1.96 
6  1 O  A HOH 209 ? ? O A HOH 272 ? ? 2.00 
7  1 O  A HOH 237 ? ? O A HOH 308 ? ? 2.02 
8  1 O  A HOH 207 ? ? O A HOH 298 ? ? 2.04 
9  1 O2 C SO4 102 ? ? O C HOH 201 ? ? 2.04 
10 1 O2 C SO4 102 ? ? O C HOH 202 ? ? 2.05 
11 1 O  C HOH 258 ? ? O C HOH 263 ? ? 2.06 
12 1 N  C PHE 5   ? ? O C HOH 203 ? ? 2.16 
13 1 O  B HOH 216 ? ? O B HOH 273 ? ? 2.16 
# 
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 311 ? ? 1_555 O A HOH 312 ? ? 4_545 2.18 
2 1 O A HOH 245 ? ? 1_555 O C HOH 265 ? ? 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             B 
_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             B 
_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             B 
_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                85.79 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -14.41 
_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 ? ? -153.93 64.34  
2 1 ASN B 38 ? ? 79.36   -3.49  
3 1 ASN B 87 ? ? -159.09 62.20  
4 1 ASN C 87 ? ? -151.88 49.38  
5 1 SER C 91 ? ? -64.79  -73.27 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 VAL A 11 ? ? PHE A 12 ? ? 149.10 
2 1 VAL B 11 ? ? PHE B 12 ? ? 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 ILE 28 ? C ILE 29 
11 1 Y 1 C ALA 29 ? C ALA 30 
12 1 Y 1 C ASP 30 ? C ASP 31 
13 1 Y 1 C GLY 31 ? C GLY 32 
14 1 Y 1 C ALA 32 ? C ALA 33 
15 1 Y 1 C VAL 33 ? C VAL 34 
16 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 
VVG N1   N N N 406 
VVG C4   C Y N 407 
VVG C5   C Y N 408 
VVG C6   C Y N 409 
VVG C7   C Y N 410 
VVG C8   C Y N 411 
VVG C1   C N N 412 
VVG C2   C N N 413 
VVG S1   S N N 414 
VVG O1   O N N 415 
VVG O2   O N N 416 
VVG C3   C Y N 417 
VVG F1   F N N 418 
VVG H6   H N N 419 
VVG H7   H N N 420 
VVG H8   H N N 421 
VVG H9   H N N 422 
VVG H10  H N N 423 
VVG H2   H N N 424 
VVG H1   H N N 425 
VVG H3   H N N 426 
VVG H4   H N N 427 
VVG H5   H N N 428 
# 
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 
VVG C1  C2   sing N N 389 
VVG C2  S1   sing N N 390 
VVG S1  O1   doub N N 391 
VVG S1  O2   doub N N 392 
VVG S1  N1   sing N N 393 
VVG N1  C3   sing N N 394 
VVG C3  C4   doub Y N 395 
VVG C4  C5   sing Y N 396 
VVG C5  C6   doub Y N 397 
VVG C6  C7   sing Y N 398 
VVG C7  C8   doub Y N 399 
VVG C8  F1   sing N N 400 
VVG C3  C8   sing Y N 401 
VVG N1  H6   sing N N 402 
VVG C4  H7   sing N N 403 
VVG C5  H8   sing N N 404 
VVG C6  H9   sing N N 405 
VVG C7  H10  sing N N 406 
VVG C1  H2   sing N N 407 
VVG C1  H1   sing N N 408 
VVG C1  H3   sing N N 409 
VVG C2  H4   sing N N 410 
VVG C2  H5   sing N N 411 
# 
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                    7HH1 
_atom_sites.fract_transf_matrix[1][1]   0.024021 
_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]   0.023652 
_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]   0.006291 
_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  ? 0.973   4.288   2.404   1.00 49.80  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.124  3.534   1.744   1.00 52.83  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.461   2.448   0.839   1.00 47.74  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.572   2.579   0.339   1.00 46.29  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.048  4.466   0.951   1.00 61.28  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.083  5.203   1.801   1.00 69.14  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.490  4.280   2.469   1.00 68.39  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -3.995  5.408   3.776   1.00 70.74  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.254  1.315   0.659   1.00 41.39  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.162   0.241   -0.247  1.00 40.69  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.399   0.592   -1.715  1.00 36.26  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.307  1.393   -2.326  1.00 40.74  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.083  -0.715  -0.088  1.00 39.42  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.475  -0.522  1.366   1.00 44.14  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.479  0.980   1.408   1.00 40.73  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.382   -0.093  -2.290  1.00 35.10  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.628   0.000   -3.709  1.00 36.40  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 1.059   -1.281  -4.305  1.00 32.07  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.545   -2.131  -3.572  1.00 30.41  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 3.138   0.149   -3.954  1.00 42.58  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.684   1.480   -3.512  1.00 54.91  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.765   1.881   -2.194  1.00 61.50  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.153   2.514   -4.233  1.00 64.05  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.259   3.111   -2.132  1.00 63.09  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.513   3.511   -3.358  1.00 58.35  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 1.108   -1.400  -5.628  1.00 27.91  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.868   -2.693  -6.241  1.00 27.17  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 2.020   -3.644  -5.927  1.00 26.01  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 3.117   -3.217  -5.514  1.00 27.10  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.664   -2.529  -7.739  1.00 31.26  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.699   -4.934  -6.040  1.00 23.69  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.697   -5.995  -5.924  1.00 25.13  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.850   -5.775  -6.905  1.00 29.77  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.636   -5.366  -8.049  1.00 27.21  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.160   -7.432  -5.940  1.00 24.96  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.391   -7.773  -4.671  1.00 25.25  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 2.046   -7.952  -3.448  1.00 22.17  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.002  -7.965  -4.720  1.00 24.39  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.363   -8.311  -2.282  1.00 21.32  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.673  -8.339  -3.553  1.00 22.73  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.020  -8.451  -2.354  1.00 23.21  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 5.081   -6.038  -6.419  1.00 22.04  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.231   -5.997  -7.329  1.00 24.01  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.152   -7.188  -7.027  1.00 22.96  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 7.123   -7.775  -5.946  1.00 21.92  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.972   -4.668  -7.102  1.00 27.35  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.626   -4.547  -5.753  1.00 29.48  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.307   -3.210  -5.404  1.00 35.99  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.952   -3.235  -4.023  1.00 33.97  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.935   -3.195  -2.955  1.00 33.86  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 8.058   -7.552  -7.954  1.00 24.35  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 9.007   -8.638  -7.705  1.00 23.76  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.784   -8.372  -6.421  1.00 21.42  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.259  -7.262  -6.173  1.00 24.01  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.915   -8.587  -8.976  1.00 25.71  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.970   -8.029  -10.013 1.00 25.19  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.185   -6.930  -9.294  1.00 25.11  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.954   -9.432  -5.609  1.00 21.44  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.693  -9.360  -4.370  1.00 20.96  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.746   -9.236  -3.181  1.00 21.21  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 10.126  -9.508  -2.045  1.00 21.85  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.487   -8.810  -3.419  1.00 18.98  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.576   -8.770  -2.274  1.00 17.98  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.334   -10.154 -1.660  1.00 16.61  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.197   -11.140 -2.364  1.00 18.78  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.221   -8.149  -2.655  1.00 20.02  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.251   -6.651  -2.890  1.00 22.83  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.202   -5.975  -2.420  1.00 23.83  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.288   -6.151  -3.495  1.00 23.84  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.212   -10.189 -0.324  1.00 18.25  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 7.043   -11.419 0.434   1.00 16.29  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.574   -11.525 0.823   1.00 18.62  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.989   -10.518 1.274   1.00 20.63  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.964   -11.464 1.655   1.00 17.58  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.451   -11.310 1.291   1.00 18.93  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.273  -11.386 2.585   1.00 21.38  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.938   -12.330 0.241   1.00 21.69  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 5.054   -12.758 0.689   1.00 18.35  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.613   -12.980 0.896   1.00 18.72  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.363   -14.345 1.536   1.00 19.07  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.236   -15.207 1.590   1.00 19.84  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.773   -12.894 -0.393  1.00 18.95  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.874   -11.496 -1.011  1.00 20.08  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.254   -13.911 -1.436  1.00 19.89  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 2.119   -14.521 2.042   1.00 18.88  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.531   -15.849 2.049   1.00 19.55  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.576   -15.915 0.869   1.00 22.24  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.223  -14.988 0.671   1.00 21.72  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.777   -16.241 3.346   1.00 20.95  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.725   -16.306 4.529   1.00 20.59  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 2.039   -15.121 5.200   1.00 22.38  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.271   -17.519 4.952   1.00 24.15  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.938   -15.169 6.269   1.00 27.54  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.171   -17.555 6.019   1.00 24.16  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.498   -16.383 6.651   1.00 25.74  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.704   -17.007 0.093   1.00 20.27  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.094  -17.176 -1.115  1.00 20.28  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.077  -18.332 -0.901  1.00 22.62  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.708  -19.400 -0.385  1.00 24.66  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.787   -17.422 -2.334  1.00 20.01  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.337  -18.103 -1.310  1.00 21.64  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.369  -19.119 -1.067  1.00 22.68  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.772  -19.802 -2.372  1.00 25.33  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.206  -19.135 -3.304  1.00 28.01  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.583  -18.445 -0.405  1.00 24.66  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.721  -19.419 -0.027  1.00 28.67  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.227  -20.359 1.081   1.00 29.49  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.306  -21.157 1.792   1.00 32.55  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.765  -22.246 0.918   1.00 33.48  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.673  -21.151 -2.365  1.00 24.46  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.164  -22.050 -3.399  1.00 29.64  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.282  -22.884 -2.765  1.00 32.19  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.176  -23.270 -1.613  1.00 27.66  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.040  -23.034 -3.768  1.00 32.39  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -1.675  -22.411 -4.123  1.00 33.62  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.822  -21.772 -5.810  1.00 37.88  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.475  -23.290 -6.614  1.00 29.04  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.328  -23.188 -3.531  1.00 37.29  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.417  -24.022 -3.030  1.00 39.65  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.856  -25.356 -2.559  1.00 31.81  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.958  -25.938 -3.181  1.00 35.55  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.413  -24.249 -4.175  1.00 47.93  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.752  -24.833 -3.751  1.00 57.28  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.693 -23.794 -3.142  1.00 61.11  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.308  -25.809 -1.379  1.00 35.63  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -6.824  -27.090 -0.900  1.00 34.23  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.496  -27.022 -0.145  1.00 38.46  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.049  -28.009 0.423   1.00 41.70  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -4.840  -25.851 -0.119  1.00 32.49  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.605  -25.791 0.636   1.00 31.14  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.671  -24.654 1.642   1.00 27.65  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.385  -23.699 1.421   1.00 28.06  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.481  -25.397 -0.327  1.00 32.91  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.121  -26.367 -1.444  1.00 38.25  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.053  -27.240 -1.298  1.00 50.55  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.793  -26.350 -2.663  1.00 39.43  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.683  -28.101 -2.322  1.00 49.29  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.430  -27.207 -3.701  1.00 45.34  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.359  -28.071 -3.529  1.00 51.94  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -0.972  -28.945 -4.516  1.00 67.00  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -2.909  -24.724 2.748   1.00 28.77  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -2.856  -23.635 3.739   1.00 28.59  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.144  -22.440 3.079   1.00 25.75  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.415  -22.655 2.120   1.00 26.11  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.013  -24.253 4.883   1.00 32.30  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.183  -25.359 4.209   1.00 31.58  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.002  -25.862 3.054   1.00 31.72  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.417  -21.234 3.562   1.00 25.21  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.709  -20.024 3.145   1.00 22.80  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.201  -20.263 3.260   1.00 25.40  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.281   -20.688 4.312   1.00 24.49  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.136  -18.849 4.033   1.00 23.09  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.569  -18.412 3.861   1.00 23.96  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.596  -19.092 4.503   1.00 28.30  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.151  -17.429 3.142   1.00 27.27  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -5.761  -18.497 4.196   1.00 29.25  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.519  -17.471 3.401   1.00 28.91  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.557   -20.019 2.156   1.00 23.18  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.861   -20.662 2.020   1.00 22.57  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.934   -19.585 1.857   1.00 22.26  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.775   -18.679 1.048   1.00 22.17  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.882   -21.536 0.764   1.00 24.30  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.973   -22.583 0.811   1.00 24.25  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.327   -22.421 0.650   1.00 25.08  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.765   -23.981 1.109   1.00 26.13  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.966   -23.642 0.762   1.00 24.66  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 4.035   -24.604 1.050   1.00 27.35  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.634   -24.762 1.391   1.00 30.31  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.211   -25.971 1.286   1.00 33.19  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.811   -26.118 1.600   1.00 32.39  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 3.082   -26.703 1.569   1.00 36.65  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 4.060   -19.651 2.604   1.00 20.30  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 5.129   -18.658 2.429   1.00 19.65  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.622   -18.602 0.971   1.00 19.67  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.945   -19.635 0.359   1.00 20.71  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 6.233   -19.104 3.423   1.00 20.71  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 6.000   -20.599 3.596   1.00 20.41  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.434   -20.702 3.577   1.00 22.02  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.705   -17.389 0.407   1.00 17.44  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 6.027   -17.255 -1.010  1.00 18.69  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.562   -15.851 -1.327  1.00 18.21  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.576   -14.970 -0.492  1.00 18.65  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.758   -17.568 -1.840  1.00 20.00  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 7.074   -15.694 -2.549  1.00 17.41  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.495   -14.361 -2.995  1.00 17.89  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.961   -14.098 -4.401  1.00 18.57  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.694   -15.047 -5.139  1.00 20.57  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 9.012   -14.225 -2.951  1.00 18.95  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.718   -15.093 -3.973  1.00 18.60  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.278  -14.953 -3.792  1.00 18.71  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.941  -15.711 -4.879  1.00 20.78  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 13.217  -16.146 -4.773  1.00 21.11  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.907  -16.012 -3.625  1.00 21.24  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.752  -16.771 -5.828  1.00 24.52  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.826   -12.799 -4.718  1.00 18.78  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.613   -12.460 -6.135  1.00 19.05  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.937   -12.582 -6.860  1.00 22.87  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.903   -11.957 -6.465  1.00 21.57  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 6.106   -11.015 -6.256  1.00 21.14  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.945   -10.706 -5.280  1.00 26.80  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.789   -10.651 -7.731  1.00 21.64  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.624   -11.360 -5.585  1.00 30.91  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.969   -13.412 -7.896  1.00 22.15  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 9.205   -13.588 -8.637  1.00 24.28  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.323   -12.571 -9.767  1.00 27.12  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.364   -11.951 -10.203 1.00 25.02  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.330   -14.973 -9.230  1.00 22.60  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.311  -15.902 -8.545  1.00 27.48  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.899  -15.514 -7.483  1.00 29.55  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.443  -17.002 -9.034  1.00 26.43  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.569  -12.392 -10.244 1.00 28.24  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.766  -11.701 -11.502 1.00 32.82  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.477  -12.708 -12.616 1.00 30.39  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.377  -13.905 -12.388 1.00 29.91  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.223  -11.263 -11.644 1.00 38.33  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.652  -9.973  -10.949 1.00 46.41  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.239  -8.870  -11.400 1.00 47.54  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.428  -10.083 -9.977  1.00 52.49  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.386  -12.219 -13.845 1.00 31.84  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.353  -13.121 -14.995 1.00 31.92  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.694  -12.889 -15.697 1.00 28.19  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 12.009  -11.743 -15.969 1.00 31.57  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.191   -12.665 -15.888 1.00 34.07  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.844   -12.737 -15.123 1.00 36.31  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.164   -13.473 -17.188 1.00 29.79  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.825   -11.717 -15.586 1.00 36.70  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.487  -13.955 -15.851 1.00 31.99  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.767  -13.924 -16.559 1.00 27.46  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.555  -13.577 -18.042 1.00 29.26  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.512  -13.853 -18.630 1.00 29.69  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.465  -15.268 -16.432 1.00 32.80  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.523  -12.883 -18.643 1.00 29.10  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.511  -12.763 -20.104 1.00 27.90  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.265  -14.143 -20.706 1.00 25.80  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.846  -15.128 -20.286 1.00 29.15  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.856  -12.209 -20.569 1.00 30.51  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 16.079  -10.722 -20.389 1.00 32.26  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 15.098  -10.016 -20.223 1.00 31.67  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 17.261  -10.265 -20.425 1.00 34.46  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.374  -14.190 -21.706 1.00 26.06  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.057  -15.371 -22.492 1.00 26.58  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.178  -16.403 -21.789 1.00 30.19  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.903  -17.460 -22.345 1.00 33.20  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.762  -16.100 -20.560 1.00 30.25  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.971  -17.059 -19.800 1.00 29.89  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.480   -16.820 -20.058 1.00 28.80  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 9.040   -15.762 -20.500 1.00 29.67  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.278  -16.864 -18.312 1.00 30.65  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.680   -17.879 -19.808 1.00 32.82  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.229   -17.784 -19.960 1.00 32.04  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.624   -16.749 -18.997 1.00 32.47  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.883   -16.784 -17.794 1.00 32.26  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.634   -19.170 -19.634 1.00 33.13  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.115   -19.097 -19.546 1.00 36.40  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.055   -20.193 -20.683 1.00 32.74  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.801   -15.856 -19.551 1.00 31.94  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.169   -14.773 -18.804 1.00 31.93  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.839   -15.255 -18.235 1.00 36.96  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.197   -16.142 -18.785 1.00 34.53  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.837   -13.553 -19.660 1.00 31.34  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 6.062   -12.835 -20.241 1.00 34.03  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.789   -11.635 -21.150 1.00 44.63  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.317   -12.069 -22.508 1.00 41.91  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.215   -10.915 -23.409 1.00 43.11  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.348   -14.639 -17.142 1.00 36.71  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 2.073   -15.067 -16.567 1.00 34.98  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.947   -14.498 -17.425 1.00 34.86  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.119   -13.547 -18.194 1.00 34.67  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 2.065   -14.466 -15.147 1.00 32.26  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.020   -13.285 -15.222 1.00 39.81  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.908   -13.456 -16.482 1.00 35.24  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.283  -15.017 -17.239 1.00 36.58  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.461  -14.401 -17.856 1.00 41.77  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.655  -12.970 -17.375 1.00 41.63  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.172  -12.607 -16.299 1.00 34.34  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.611  -15.315 -17.387 1.00 36.88  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -1.951  -16.617 -16.985 1.00 35.08  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.587  -16.210 -16.432 1.00 37.55  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.438  -12.124 -18.087 1.00 37.24  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.789  -10.798 -17.579 1.00 38.03  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.375  -10.867 -16.169 1.00 32.82  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.050  -11.834 -15.825 1.00 38.39  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.799  -10.187 -18.603 1.00 41.46  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.087  -11.316 -19.551 1.00 39.08  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.072  -12.432 -19.391 1.00 43.03  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.052  -9.840  -15.378 1.00 35.42  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.522  -9.623  -14.027 1.00 36.35  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -2.980  -10.679 -13.065 1.00 32.04  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.409  -10.683 -11.905 1.00 32.18  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.045  -9.547  -13.979 1.00 43.34  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.538  -8.427  -14.870 1.00 48.84  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.344  -7.246  -14.552 1.00 49.94  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.120  -8.779  -16.003 1.00 51.47  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.061  -11.554 -13.535 1.00 27.09  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.512  -12.581 -12.640 1.00 22.95  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.012  -12.324 -12.428 1.00 23.52  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.636   -11.609 -13.198 1.00 25.97  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.648  -14.038 -13.077 1.00 27.63  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.032  -14.574 -13.498 1.00 32.61  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -3.979  -14.426 -12.310 1.00 36.90  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.463  -14.713 -12.513 1.00 43.13  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.714  -16.111 -12.864 1.00 46.50  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.484   -12.831 -11.285 1.00 21.89  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.871   -12.660 -10.885 1.00 21.56  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.511   -14.033 -10.807 1.00 19.91  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.900   -15.026 -10.433 1.00 20.90  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 2.012   -12.032 -9.474  1.00 21.78  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.532   -10.597 -9.457  1.00 23.42  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? 0.180   -10.324 -9.318  1.00 28.45  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.409   -9.538  -9.622  1.00 26.27  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.300  -9.032  -9.402  1.00 30.00  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.942   -8.222  -9.669  1.00 26.61  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.586   -7.983  -9.536  1.00 30.62  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? 0.080   -6.705  -9.662  1.00 32.48  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.844   -14.146 -11.073 1.00 20.36  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.521   -15.418 -10.847 1.00 21.08  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.862   -15.534 -9.373  1.00 21.15  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.558   -14.660 -8.849  1.00 23.38  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.792   -15.278 -11.708 1.00 21.80  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 6.012   -13.826 -11.874 1.00 22.61  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.691   -13.065 -11.613 1.00 24.42  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.282   -16.547 -8.733  1.00 19.65  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.497   -16.759 -7.306  1.00 18.66  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.444   -17.937 -7.117  1.00 22.25  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 5.123   -19.084 -7.519  1.00 23.87  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 3.135   -17.018 -6.636  1.00 20.41  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 2.190   -15.856 -6.922  1.00 20.92  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.361   -17.192 -5.119  1.00 21.95  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.723   -14.460 -6.549  1.00 22.63  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.554   -17.684 -6.389  1.00 19.88  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.465   -18.747 -6.054  1.00 21.06  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 7.175   -19.157 -4.613  1.00 21.45  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 7.252   -18.336 -3.694  1.00 21.23  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.912   -18.233 -6.255  1.00 22.72  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.937   -19.257 -5.808  1.00 21.92  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.328  -20.278 -6.698  1.00 24.47  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.507  -19.223 -4.518  1.00 25.98  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.265  -21.252 -6.302  1.00 24.27  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.453  -20.191 -4.144  1.00 28.00  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.825  -21.183 -5.039  1.00 25.75  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.809   -20.426 -4.437  1.00 20.42  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.493   -20.947 -3.115  1.00 21.11  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.753   -21.485 -2.442  1.00 23.60  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.456   -22.376 -2.957  1.00 22.93  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.508   -22.120 -3.330  1.00 22.59  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 4.132   -21.610 -3.742  1.00 20.63  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.820   -21.422 -5.077  1.00 26.36  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 3.132   -21.379 -2.797  1.00 24.32  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.573   -20.940 -5.462  1.00 28.59  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.885   -20.896 -3.194  1.00 25.33  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.620   -20.669 -4.519  1.00 26.28  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 8.045   -20.937 -1.263  1.00 20.58  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 9.224   -21.396 -0.524  1.00 21.95  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.999   -22.845 -0.071  1.00 24.02  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.861   -23.304 0.065   1.00 24.76  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.403   -20.443 0.668   1.00 22.61  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.899   -19.065 0.272   1.00 21.38  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 11.175  -18.897 -0.286  1.00 20.40  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 9.159   -17.917 0.566   1.00 20.34  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.608  -17.636 -0.657  1.00 18.79  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.632   -16.648 0.239   1.00 18.60  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.856  -16.519 -0.360  1.00 20.76  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 10.106  -23.573 0.105   1.00 23.55  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 10.021  -24.943 0.626   1.00 23.12  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.786   -25.917 -0.536  1.00 27.62  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.666  -26.722 -0.840  1.00 30.06  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.636   -25.825 -1.235  1.00 28.90  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.389   -26.680 -2.396  1.00 28.73  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 9.186   -26.204 -3.608  1.00 28.67  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.475   -26.977 -4.543  1.00 29.20  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.906   -26.738 -2.770  1.00 30.30  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.524   -25.433 -3.197  1.00 27.73  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.981   -27.254 -1.697  1.00 28.62  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.462   -24.887 -3.658  1.00 25.21  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 10.162  -24.271 -4.774  1.00 25.55  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.352   -24.389 -6.064  1.00 26.45  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.910   -24.385 -7.159  1.00 29.11  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.603  -24.793 -4.952  1.00 25.03  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.320  -24.816 -3.635  1.00 29.04  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 13.136  -25.863 -3.262  1.00 29.92  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.377  -23.909 -2.619  1.00 25.44  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.607  -25.628 -2.044  1.00 32.72  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 13.203  -24.419 -1.650  1.00 29.27  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 8.033   -24.428 -5.930  1.00 25.34  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 7.219   -24.469 -7.134  1.00 27.36  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.729   -23.067 -7.508  1.00 28.47  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.837   -22.122 -6.712  1.00 26.71  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 6.036   -25.401 -6.902  1.00 30.51  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.475   -26.842 -6.648  1.00 41.58  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.360   -27.756 -6.180  1.00 49.57  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 4.182   -27.348 -6.135  1.00 48.08  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.719   -28.901 -5.832  1.00 53.17  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.288   -22.898 -8.766  1.00 25.17  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.764   -21.623 -9.228  1.00 25.02  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.328   -21.843 -9.668  1.00 26.75  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 4.029   -22.830 -10.361 1.00 29.14  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.579   -21.078 -10.405 1.00 29.21  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.892   -20.732 -9.973  1.00 28.76  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.998   -19.797 -10.996 1.00 30.75  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.435   -20.935 -9.259  1.00 24.40  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 2.093   -20.850 -9.819  1.00 24.59  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.782   -19.395 -10.134 1.00 24.08  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.499   -18.471 -9.702  1.00 24.79  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 1.083   -21.402 -8.845  1.00 26.92  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.722   -19.162 -10.942 1.00 24.65  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.362   -17.801 -11.296 1.00 24.99  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -0.903  -17.399 -10.547 1.00 29.49  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -1.921  -18.090 -10.604 1.00 30.23  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? 0.070   -17.764 -12.797 1.00 26.28  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.272   -18.106 -13.645 1.00 28.79  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.424   -17.328 -13.589 1.00 33.55  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 1.193   -19.136 -14.581 1.00 34.44  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.528   -17.609 -14.399 1.00 43.69  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.300   -19.423 -15.369 1.00 37.41  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.444   -18.649 -15.308 1.00 35.69  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -0.821  -16.316 -9.763  1.00 22.59  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -1.938  -15.987 -8.880  1.00 22.56  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.221  -14.496 -8.994  1.00 22.29  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.353  -13.674 -9.321  1.00 22.52  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.595  -16.272 -7.414  1.00 24.39  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.529  -17.750 -7.051  1.00 24.36  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.208  -17.863 -5.558  1.00 24.29  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -2.911  -18.402 -7.329  1.00 29.14  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.476  -14.136 -8.688  1.00 20.96  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -3.812  -12.722 -8.621  1.00 21.09  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -3.823  -12.239 -7.163  1.00 19.64  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -3.777  -13.056 -6.230  1.00 19.75  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -3.909  -10.914 -6.961  1.00 20.89  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -3.864  -10.282 -5.626  1.00 21.53  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -4.850  -10.794 -4.588  1.00 21.35  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.550  -10.773 -3.396  1.00 20.64  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.160  -8.811  -5.928  1.00 21.91  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.585  -8.604  -7.327  1.00 25.06  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -3.881  -9.914  -8.037  1.00 21.71  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -5.985  -11.351 -5.061  1.00 23.21  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -6.950  -11.858 -4.092  1.00 21.91  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.410  -13.025 -3.273  1.00 21.92  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -6.858  -13.256 -2.144  1.00 23.14  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.233  -12.337 -4.780  1.00 27.06  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.072  -13.597 -5.565  1.00 31.24  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.454  -13.952 -6.096  1.00 35.29  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.407  -14.942 -7.189  1.00 38.64  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.175  -16.205 -6.496  1.00 39.22  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.340  -13.701 -3.789  1.00 20.73  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -4.780  -14.836 -3.100  1.00 22.61  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.420  -14.480 -2.466  1.00 21.19  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.734  -15.390 -2.000  1.00 21.73  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.685  -16.016 -4.070  1.00 22.90  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.078  -16.572 -4.390  1.00 27.23  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -6.901  -16.648 -3.439  1.00 28.66  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.309  -16.921 -5.551  1.00 28.01  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.063  -13.186 -2.441  1.00 19.54  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.748  -12.752 -1.923  1.00 18.44  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -1.891  -11.879 -0.671  1.00 17.05  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.502  -10.802 -0.698  1.00 20.34  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -0.996  -12.021 -3.045  1.00 19.38  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -0.897  -12.828 -4.337  1.00 19.47  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.163  -11.931 -5.358  1.00 21.70  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.135  -14.110 -4.191  1.00 21.95  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.304  -12.403 0.417   1.00 18.84  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.386  -11.715 1.723   1.00 19.52  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.012  -11.213 2.109   1.00 22.15  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.875   -12.032 2.308   1.00 23.37  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -1.854  -12.764 2.732   1.00 19.73  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.303  -13.179 2.473   1.00 21.35  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.632  -14.092 1.475   1.00 22.75  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.318  -12.644 3.272   1.00 22.37  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -4.968  -14.434 1.217   1.00 24.53  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.638  -13.016 3.000   1.00 21.94  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -5.944  -13.920 2.016   1.00 24.74  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? 0.214   -9.892  2.232   1.00 24.75  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.562   -9.393  2.546   1.00 21.81  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 2.127   -10.043 3.803   1.00 22.01  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.441   -10.273 4.810   1.00 23.11  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.260   -7.896  2.752   1.00 25.70  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.242   -7.620  1.639   1.00 25.92  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.725  -8.797  1.911   1.00 25.58  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.428   -10.420 3.756   1.00 23.46  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.957   -11.291 4.800   1.00 21.60  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.985   -10.634 6.198   1.00 21.01  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.607   -11.320 7.146   1.00 25.60  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.381   -11.677 4.343   1.00 23.91  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 6.146   -12.492 5.376   1.00 23.25  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.864   -13.842 5.609   1.00 23.06  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 7.173   -11.902 6.093   1.00 27.43  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.535   -14.612 6.568   1.00 24.01  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.871   -12.682 7.010   1.00 25.82  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.551   -13.998 7.269   1.00 27.89  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.290   -14.718 8.207   1.00 30.01  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.399   -9.373  6.252   0.50 17.21  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.589   -8.725  7.545   0.50 22.00  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 3.276   -8.692  8.315   0.50 20.61  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 3.259   -9.140  9.451   0.50 24.39  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.204   -7.351  7.429   0.50 23.54  ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 5.617   -6.781  8.775   0.50 36.37  ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 5.175   -5.652  9.096   0.50 41.98  ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 6.356   -7.495  9.502   0.50 41.42  ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 2.203   -8.264  7.634   1.00 28.64  ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? 0.858   -8.193  8.223   1.00 28.57  ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? 0.329   -9.566  8.657   1.00 29.61  ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -0.388  -9.648  9.660   1.00 28.40  ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? -0.087  -7.599  7.170   1.00 29.57  ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -1.525  -7.405  7.643   1.00 34.16  ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -2.283  -6.664  6.547   1.00 34.13  ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -3.440  -5.914  7.121   1.00 37.43  ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -4.436  -6.856  7.610   1.00 47.56  ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? 0.656   -10.651 7.922   1.00 26.81  ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? -0.024  -11.939 7.982   1.00 26.28  ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? 0.728   -13.015 8.773   1.00 28.34  ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? 0.206   -14.126 8.950   1.00 28.90  ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -0.300  -12.489 6.572   1.00 28.00  ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -1.129  -11.534 5.924   1.00 35.63  ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 2.000   -12.761 9.121   1.00 27.21  ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 2.828   -13.854 9.610   1.00 29.52  ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 2.373   -14.385 10.973  1.00 28.54  ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 2.508   -15.576 11.241  1.00 32.12  ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 4.309   -13.469 9.591   1.00 27.62  ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 4.696   -12.302 10.452  1.00 29.45  ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 6.181   -12.107 10.143  1.00 39.44  ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 6.763   -11.151 11.142  1.00 46.56  ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 6.186   -9.819  10.938  1.00 54.25  ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 1.798   -13.509 11.807  0.50 32.93  ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 1.831   -13.495 11.814  0.50 32.61  ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? 1.313   -13.932 13.117  0.50 34.08  ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 1.284   -13.909 13.100  0.50 33.90  ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? 0.177   -14.951 12.979  0.50 34.23  ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? 0.266   -15.029 12.893  0.50 34.26  ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? 0.031   -15.863 13.791  0.50 34.83  ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? 0.301   -16.072 13.557  0.50 34.66  ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? 0.936   -12.734 13.975  0.50 37.53  ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? 0.603   -12.736 13.784  0.50 36.47  ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 2.088   -11.948 14.589  0.50 39.61  ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? 0.057   -12.997 15.182  0.50 39.08  ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 3.230   -12.465 14.596  0.50 39.90  ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 0.875   -13.176 16.107  0.50 43.20  ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? 1.851   -10.806 15.041  0.50 37.78  ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -1.184  -13.008 15.332  0.50 43.04  ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -0.632  -14.811 11.926  1.00 29.00  ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -1.707  -15.737 11.661  1.00 28.72  ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -1.235  -16.970 10.902  1.00 31.38  ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -1.658  -18.079 11.213  1.00 34.44  ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -2.773  -14.949 10.900  1.00 29.37  ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -4.030  -15.743 10.729  1.00 30.76  ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -5.122  -14.833 10.146  1.00 36.73  ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -6.409  -15.549 9.866   1.00 43.82  ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -7.357  -14.634 9.210   1.00 46.40  ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -0.405  -16.791 9.857   1.00 29.23  ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? -0.163  -17.893 8.933   1.00 25.67  ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 1.218   -18.541 9.090   1.00 24.51  ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 1.459   -19.603 8.537   1.00 29.14  ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -0.288  -17.380 7.491   1.00 24.50  ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -1.701  -16.962 7.113   1.00 26.95  ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -2.823  -17.712 7.489   1.00 28.41  ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -1.914  -15.760 6.441   1.00 26.35  ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -4.108  -17.302 7.159   1.00 31.80  ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -3.191  -15.345 6.105   1.00 28.97  ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -4.285  -16.110 6.472   1.00 29.35  ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -5.512  -15.668 6.071   1.00 30.99  ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 2.115   -17.904 9.850   1.00 25.72  ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 3.498   -18.378 9.906   1.00 26.45  ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 3.721   -19.343 11.078  1.00 29.96  ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 4.507   -19.061 11.948  1.00 37.33  ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 2.938   -20.409 11.122  1.00 32.44  ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 3.070   -21.430 12.146  1.00 38.05  ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 3.389   -22.736 11.428  1.00 33.03  ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 2.971   -22.964 10.296  1.00 36.34  ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 1.817   -21.511 13.031  1.00 41.86  ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 1.567   -20.240 13.838  1.00 41.72  ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? 0.939   -20.428 15.211  1.00 46.33  ? 70  LYS A CD  1 
ATOM   570  N N   . PRO A 1 72 ? 4.139   -23.679 12.051  1.00 35.87  ? 71  PRO A N   1 
ATOM   571  C CA  . PRO A 1 72 ? 4.415   -24.952 11.381  1.00 34.01  ? 71  PRO A CA  1 
ATOM   572  C C   . PRO A 1 72 ? 3.200   -25.735 10.905  1.00 33.88  ? 71  PRO A C   1 
ATOM   573  O O   . PRO A 1 72 ? 2.137   -25.676 11.518  1.00 42.55  ? 71  PRO A O   1 
ATOM   574  C CB  . PRO A 1 72 ? 5.237   -25.739 12.438  1.00 39.75  ? 71  PRO A CB  1 
ATOM   575  C CG  . PRO A 1 72 ? 5.844   -24.666 13.322  1.00 44.97  ? 71  PRO A CG  1 
ATOM   576  C CD  . PRO A 1 72 ? 4.809   -23.524 13.356  1.00 41.90  ? 71  PRO A CD  1 
ATOM   577  N N   . ASN A 1 73 ? 3.362   -26.470 9.809   1.00 37.13  ? 72  ASN A N   1 
ATOM   578  C CA  . ASN A 1 73 ? 2.265   -27.189 9.190   1.00 41.44  ? 72  ASN A CA  1 
ATOM   579  C C   . ASN A 1 73 ? 2.824   -28.526 8.736   1.00 46.23  ? 72  ASN A C   1 
ATOM   580  O O   . ASN A 1 73 ? 3.998   -28.646 8.390   1.00 47.89  ? 72  ASN A O   1 
ATOM   581  C CB  . ASN A 1 73 ? 1.686   -26.367 8.035   1.00 41.59  ? 72  ASN A CB  1 
ATOM   582  C CG  . ASN A 1 73 ? 0.399   -26.893 7.438   1.00 51.33  ? 72  ASN A CG  1 
ATOM   583  O OD1 . ASN A 1 73 ? 0.421   -27.794 6.594   1.00 49.22  ? 72  ASN A OD1 1 
ATOM   584  N ND2 . ASN A 1 73 ? -0.734  -26.286 7.775   1.00 49.93  ? 72  ASN A ND2 1 
ATOM   585  N N   . LYS A 1 74 ? 1.962   -29.537 8.743   1.00 50.94  ? 73  LYS A N   1 
ATOM   586  C CA  . LYS A 1 74 ? 2.382   -30.891 8.447   1.00 44.95  ? 73  LYS A CA  1 
ATOM   587  C C   . LYS A 1 74 ? 2.727   -31.054 6.967   1.00 44.82  ? 73  LYS A C   1 
ATOM   588  O O   . LYS A 1 74 ? 3.398   -32.013 6.595   1.00 48.41  ? 73  LYS A O   1 
ATOM   589  C CB  . LYS A 1 74 ? 1.232   -31.796 8.928   1.00 50.79  ? 73  LYS A CB  1 
ATOM   590  C CG  . LYS A 1 74 ? 0.002   -31.907 8.011   1.00 52.50  ? 73  LYS A CG  1 
ATOM   591  N N   . ARG A 1 75 ? 2.288   -30.123 6.107   1.00 40.26  ? 74  ARG A N   1 
ATOM   592  C CA  . ARG A 1 75 ? 2.347   -30.365 4.677   1.00 39.30  ? 74  ARG A CA  1 
ATOM   593  C C   . ARG A 1 75 ? 3.791   -30.335 4.159   1.00 36.38  ? 74  ARG A C   1 
ATOM   594  O O   . ARG A 1 75 ? 4.611   -29.538 4.623   1.00 34.60  ? 74  ARG A O   1 
ATOM   595  C CB  . ARG A 1 75 ? 1.470   -29.335 3.950   1.00 43.90  ? 74  ARG A CB  1 
ATOM   596  C CG  . ARG A 1 75 ? -0.018  -29.428 4.264   1.00 51.19  ? 74  ARG A CG  1 
ATOM   597  C CD  . ARG A 1 75 ? -0.699  -30.631 3.632   1.00 42.41  ? 74  ARG A CD  1 
ATOM   598  N NE  . ARG A 1 75 ? -1.253  -30.333 2.309   1.00 54.78  ? 74  ARG A NE  1 
ATOM   599  C CZ  . ARG A 1 75 ? -2.386  -29.654 2.083   1.00 54.85  ? 74  ARG A CZ  1 
ATOM   600  N NH1 . ARG A 1 75 ? -2.792  -29.472 0.837   1.00 59.62  ? 74  ARG A NH1 1 
ATOM   601  N NH2 . ARG A 1 75 ? -3.113  -29.184 3.089   1.00 51.31  ? 74  ARG A NH2 1 
ATOM   602  N N   . LYS A 1 76 ? 4.064   -31.169 3.147   1.00 34.57  ? 75  LYS A N   1 
ATOM   603  C CA  . LYS A 1 76 ? 5.409   -31.327 2.609   1.00 36.68  ? 75  LYS A CA  1 
ATOM   604  C C   . LYS A 1 76 ? 5.971   -29.966 2.190   1.00 35.71  ? 75  LYS A C   1 
ATOM   605  O O   . LYS A 1 76 ? 5.372   -29.286 1.354   1.00 30.59  ? 75  LYS A O   1 
ATOM   606  C CB  . LYS A 1 76 ? 5.365   -32.279 1.410   1.00 38.17  ? 75  LYS A CB  1 
ATOM   607  C CG  . LYS A 1 76 ? 6.657   -32.525 0.640   1.00 41.36  ? 75  LYS A CG  1 
ATOM   608  C CD  . LYS A 1 76 ? 6.548   -33.610 -0.431  1.00 45.51  ? 75  LYS A CD  1 
ATOM   609  C CE  . LYS A 1 76 ? 7.785   -33.745 -1.272  1.00 51.82  ? 75  LYS A CE  1 
ATOM   610  N N   . GLY A 1 77 ? 7.126   -29.593 2.762   1.00 30.73  ? 76  GLY A N   1 
ATOM   611  C CA  . GLY A 1 77 ? 7.844   -28.418 2.272   1.00 30.26  ? 76  GLY A CA  1 
ATOM   612  C C   . GLY A 1 77 ? 7.529   -27.177 3.095   1.00 29.93  ? 76  GLY A C   1 
ATOM   613  O O   . GLY A 1 77 ? 8.270   -26.188 3.045   1.00 29.82  ? 76  GLY A O   1 
ATOM   614  N N   . PHE A 1 78 ? 6.439   -27.230 3.849   1.00 29.25  ? 77  PHE A N   1 
ATOM   615  C CA  . PHE A 1 78 ? 5.972   -26.020 4.498   1.00 27.53  ? 77  PHE A CA  1 
ATOM   616  C C   . PHE A 1 78 ? 6.981   -25.438 5.504   1.00 30.85  ? 77  PHE A C   1 
ATOM   617  O O   . PHE A 1 78 ? 7.214   -24.223 5.560   1.00 28.65  ? 77  PHE A O   1 
ATOM   618  C CB  . PHE A 1 78 ? 4.602   -26.297 5.117   1.00 30.27  ? 77  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 78 ? 3.892   -25.017 5.536   1.00 30.66  ? 77  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 78 ? 4.180   -24.357 6.726   1.00 30.33  ? 77  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 78 ? 2.926   -24.462 4.691   1.00 31.30  ? 77  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 78 ? 3.524   -23.179 7.064   1.00 30.02  ? 77  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 78 ? 2.264   -23.293 5.039   1.00 27.48  ? 77  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 78 ? 2.556   -22.640 6.215   1.00 26.68  ? 77  PHE A CZ  1 
ATOM   625  N N   . ASN A 1 79 ? 7.514   -26.276 6.411   1.00 28.70  ? 78  ASN A N   1 
ATOM   626  C CA  . ASN A 1 79 ? 8.402   -25.768 7.453   1.00 29.63  ? 78  ASN A CA  1 
ATOM   627  C C   . ASN A 1 79 ? 9.749   -25.303 6.864   1.00 25.33  ? 78  ASN A C   1 
ATOM   628  O O   . ASN A 1 79 ? 10.339  -24.328 7.360   1.00 29.01  ? 78  ASN A O   1 
ATOM   629  C CB  . ASN A 1 79 ? 8.555   -26.812 8.569   1.00 29.98  ? 78  ASN A CB  1 
ATOM   630  C CG  . ASN A 1 79 ? 7.206   -27.090 9.197   1.00 36.41  ? 78  ASN A CG  1 
ATOM   631  O OD1 . ASN A 1 79 ? 6.307   -26.229 9.179   1.00 32.21  ? 78  ASN A OD1 1 
ATOM   632  N ND2 . ASN A 1 79 ? 7.065   -28.269 9.802   1.00 31.86  ? 78  ASN A ND2 1 
ATOM   633  N N   . GLU A 1 80 ? 10.242  -25.976 5.829   1.00 25.72  ? 79  GLU A N   1 
ATOM   634  C CA  . GLU A 1 80 ? 11.395  -25.481 5.098   1.00 24.01  ? 79  GLU A CA  1 
ATOM   635  C C   . GLU A 1 80 ? 11.031  -24.101 4.554   1.00 25.31  ? 79  GLU A C   1 
ATOM   636  O O   . GLU A 1 80 ? 11.859  -23.188 4.559   1.00 22.94  ? 79  GLU A O   1 
ATOM   637  C CB  . GLU A 1 80 ? 11.840  -26.418 3.967   1.00 26.93  ? 79  GLU A CB  1 
ATOM   638  C CG  . GLU A 1 80 ? 13.125  -25.975 3.273   1.00 28.62  ? 79  GLU A CG  1 
ATOM   639  C CD  . GLU A 1 80 ? 13.604  -27.010 2.250   1.00 39.80  ? 79  GLU A CD  1 
ATOM   640  O OE1 . GLU A 1 80 ? 12.874  -27.969 1.898   1.00 41.95  ? 79  GLU A OE1 1 
ATOM   641  O OE2 . GLU A 1 80 ? 14.742  -26.851 1.789   1.00 35.98  ? 79  GLU A OE2 1 
ATOM   642  N N   . GLY A 1 81 ? 9.801   -23.985 4.011   1.00 25.64  ? 80  GLY A N   1 
ATOM   643  C CA  . GLY A 1 81 ? 9.401   -22.693 3.450   1.00 25.47  ? 80  GLY A CA  1 
ATOM   644  C C   . GLY A 1 81 ? 9.408   -21.586 4.506   1.00 22.45  ? 80  GLY A C   1 
ATOM   645  O O   . GLY A 1 81 ? 9.757   -20.442 4.182   1.00 23.35  ? 80  GLY A O   1 
ATOM   646  N N   . LEU A 1 82 ? 8.960   -21.880 5.751   1.00 22.24  ? 81  LEU A N   1 
ATOM   647  C CA  . LEU A 1 82 ? 8.989   -20.885 6.802   1.00 23.10  ? 81  LEU A CA  1 
ATOM   648  C C   . LEU A 1 82 ? 10.419  -20.408 7.061   1.00 22.98  ? 81  LEU A C   1 
ATOM   649  O O   . LEU A 1 82 ? 10.641  -19.203 7.308   1.00 22.61  ? 81  LEU A O   1 
ATOM   650  C CB  . LEU A 1 82 ? 8.313   -21.356 8.092   1.00 24.80  ? 81  LEU A CB  1 
ATOM   651  C CG  . LEU A 1 82 ? 6.807   -21.649 7.982   1.00 25.79  ? 81  LEU A CG  1 
ATOM   652  C CD1 . LEU A 1 82 ? 6.361   -22.312 9.293   1.00 28.00  ? 81  LEU A CD1 1 
ATOM   653  C CD2 . LEU A 1 82 ? 5.965   -20.389 7.760   1.00 27.31  ? 81  LEU A CD2 1 
ATOM   654  N N   . TRP A 1 83 ? 11.390  -21.347 6.955   1.00 22.90  ? 82  TRP A N   1 
ATOM   655  C CA  . TRP A 1 83 ? 12.759  -20.979 7.252   1.00 24.11  ? 82  TRP A CA  1 
ATOM   656  C C   . TRP A 1 83 ? 13.238  -20.025 6.163   1.00 21.79  ? 82  TRP A C   1 
ATOM   657  O O   . TRP A 1 83 ? 13.945  -19.067 6.432   1.00 23.40  ? 82  TRP A O   1 
ATOM   658  C CB  . TRP A 1 83 ? 13.651  -22.245 7.386   1.00 25.05  ? 82  TRP A CB  1 
ATOM   659  C CG  . TRP A 1 83 ? 15.101  -21.905 7.661   1.00 24.48  ? 82  TRP A CG  1 
ATOM   660  C CD1 . TRP A 1 83 ? 15.722  -21.804 8.874   1.00 25.73  ? 82  TRP A CD1 1 
ATOM   661  C CD2 . TRP A 1 83 ? 16.082  -21.551 6.669   1.00 24.10  ? 82  TRP A CD2 1 
ATOM   662  N NE1 . TRP A 1 83 ? 17.036  -21.437 8.701   1.00 27.08  ? 82  TRP A NE1 1 
ATOM   663  C CE2 . TRP A 1 83 ? 17.279  -21.277 7.361   1.00 25.00  ? 82  TRP A CE2 1 
ATOM   664  C CE3 . TRP A 1 83 ? 16.061  -21.474 5.265   1.00 25.24  ? 82  TRP A CE3 1 
ATOM   665  C CZ2 . TRP A 1 83 ? 18.446  -20.916 6.696   1.00 25.27  ? 82  TRP A CZ2 1 
ATOM   666  C CZ3 . TRP A 1 83 ? 17.215  -21.101 4.603   1.00 26.53  ? 82  TRP A CZ3 1 
ATOM   667  C CH2 . TRP A 1 83 ? 18.384  -20.817 5.320   1.00 28.05  ? 82  TRP A CH2 1 
ATOM   668  N N   . GLU A 1 84 ? 12.905  -20.343 4.907   1.00 20.18  ? 83  GLU A N   1 
ATOM   669  C CA  . GLU A 1 84 ? 13.430  -19.608 3.774   1.00 20.55  ? 83  GLU A CA  1 
ATOM   670  C C   . GLU A 1 84 ? 12.895  -18.182 3.810   1.00 21.63  ? 83  GLU A C   1 
ATOM   671  O O   . GLU A 1 84 ? 13.640  -17.235 3.614   1.00 20.93  ? 83  GLU A O   1 
ATOM   672  C CB  . GLU A 1 84 ? 13.017  -20.311 2.483   1.00 21.08  ? 83  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 84 ? 13.727  -21.653 2.340   1.00 21.84  ? 83  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 84 ? 13.340  -22.375 1.047   1.00 26.98  ? 83  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 84 ? 12.401  -21.949 0.358   1.00 24.72  ? 83  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 84 ? 13.927  -23.467 0.733   1.00 26.11  ? 83  GLU A OE2 1 
ATOM   677  N N   . ILE A 1 85 ? 11.581  -18.048 4.032   1.00 19.46  ? 84  ILE A N   1 
ATOM   678  C CA  . ILE A 1 85 ? 11.020  -16.706 3.961   1.00 19.66  ? 84  ILE A CA  1 
ATOM   679  C C   . ILE A 1 85 ? 11.598  -15.803 5.078   1.00 20.16  ? 84  ILE A C   1 
ATOM   680  O O   . ILE A 1 85 ? 11.749  -14.599 4.903   1.00 21.38  ? 84  ILE A O   1 
ATOM   681  C CB  . ILE A 1 85 ? 9.475   -16.727 3.944   1.00 18.74  ? 84  ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 85 ? 8.912   -15.354 3.560   1.00 19.64  ? 84  ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 85 ? 8.912   -17.106 5.318   1.00 21.33  ? 84  ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 85 ? 7.460   -15.434 3.033   1.00 18.54  ? 84  ILE A CD1 1 
ATOM   685  N N   . GLN A 1 86 ? 11.917  -16.394 6.246   1.00 20.19  ? 85  GLN A N   1 
ATOM   686  C CA  . GLN A 1 86 ? 12.438  -15.625 7.384   1.00 23.25  ? 85  GLN A CA  1 
ATOM   687  C C   . GLN A 1 86 ? 13.940  -15.360 7.252   1.00 23.39  ? 85  GLN A C   1 
ATOM   688  O O   . GLN A 1 86 ? 14.403  -14.263 7.658   1.00 26.38  ? 85  GLN A O   1 
ATOM   689  C CB  . GLN A 1 86 ? 12.138  -16.412 8.672   1.00 24.62  ? 85  GLN A CB  1 
ATOM   690  C CG  . GLN A 1 86 ? 12.545  -15.708 9.958   1.00 29.62  ? 85  GLN A CG  1 
ATOM   691  C CD  . GLN A 1 86 ? 11.902  -16.353 11.181  1.00 36.73  ? 85  GLN A CD  1 
ATOM   692  O OE1 . GLN A 1 86 ? 11.720  -17.582 11.256  1.00 36.82  ? 85  GLN A OE1 1 
ATOM   693  N NE2 . GLN A 1 86 ? 11.504  -15.522 12.140  1.00 42.82  ? 85  GLN A NE2 1 
ATOM   694  N N   . ASN A 1 87 ? 14.682  -16.314 6.682   1.00 22.12  ? 86  ASN A N   1 
ATOM   695  C CA  . ASN A 1 87 ? 16.135  -16.295 6.771   1.00 21.01  ? 86  ASN A CA  1 
ATOM   696  C C   . ASN A 1 87 ? 16.856  -15.946 5.475   1.00 22.80  ? 86  ASN A C   1 
ATOM   697  O O   . ASN A 1 87 ? 17.962  -15.389 5.543   1.00 25.19  ? 86  ASN A O   1 
ATOM   698  C CB  . ASN A 1 87 ? 16.663  -17.613 7.364   1.00 21.42  ? 86  ASN A CB  1 
ATOM   699  C CG  . ASN A 1 87 ? 16.210  -17.713 8.814   1.00 27.00  ? 86  ASN A CG  1 
ATOM   700  O OD1 . ASN A 1 87 ? 16.566  -16.860 9.641   1.00 29.85  ? 86  ASN A OD1 1 
ATOM   701  N ND2 . ASN A 1 87 ? 15.254  -18.573 9.119   1.00 26.05  ? 86  ASN A ND2 1 
ATOM   702  N N   . ASN A 1 88 ? 16.291  -16.308 4.317   1.00 22.02  ? 87  ASN A N   1 
ATOM   703  C CA  . ASN A 1 88 ? 16.941  -15.947 3.073   1.00 20.31  ? 87  ASN A CA  1 
ATOM   704  C C   . ASN A 1 88 ? 15.901  -15.856 1.962   1.00 23.01  ? 87  ASN A C   1 
ATOM   705  O O   . ASN A 1 88 ? 15.916  -16.588 0.975   1.00 21.28  ? 87  ASN A O   1 
ATOM   706  C CB  . ASN A 1 88 ? 18.103  -16.893 2.730   1.00 22.20  ? 87  ASN A CB  1 
ATOM   707  C CG  . ASN A 1 88 ? 19.142  -16.259 1.837   1.00 24.75  ? 87  ASN A CG  1 
ATOM   708  O OD1 . ASN A 1 88 ? 18.907  -15.247 1.174   1.00 23.18  ? 87  ASN A OD1 1 
ATOM   709  N ND2 . ASN A 1 88 ? 20.348  -16.818 1.841   1.00 27.18  ? 87  ASN A ND2 1 
ATOM   710  N N   . PRO A 1 89 ? 14.956  -14.901 2.072   1.00 20.95  ? 88  PRO A N   1 
ATOM   711  C CA  . PRO A 1 89 ? 13.838  -14.873 1.128   1.00 20.09  ? 88  PRO A CA  1 
ATOM   712  C C   . PRO A 1 89 ? 14.182  -14.445 -0.290  1.00 21.87  ? 88  PRO A C   1 
ATOM   713  O O   . PRO A 1 89 ? 13.379  -14.712 -1.172  1.00 20.38  ? 88  PRO A O   1 
ATOM   714  C CB  . PRO A 1 89 ? 12.910  -13.874 1.770   1.00 19.51  ? 88  PRO A CB  1 
ATOM   715  C CG  . PRO A 1 89 ? 13.820  -12.952 2.543   1.00 20.28  ? 88  PRO A CG  1 
ATOM   716  C CD  . PRO A 1 89 ? 14.838  -13.906 3.155   1.00 20.56  ? 88  PRO A CD  1 
ATOM   717  N N   . HIS A 1 90 ? 15.384  -13.886 -0.495  1.00 18.87  ? 89  HIS A N   1 
ATOM   718  C CA  . HIS A 1 90 ? 15.746  -13.340 -1.797  1.00 18.03  ? 89  HIS A CA  1 
ATOM   719  C C   . HIS A 1 90 ? 16.851  -14.155 -2.485  1.00 21.00  ? 89  HIS A C   1 
ATOM   720  O O   . HIS A 1 90 ? 17.320  -13.747 -3.554  1.00 22.31  ? 89  HIS A O   1 
ATOM   721  C CB  . HIS A 1 90 ? 16.124  -11.839 -1.682  1.00 20.42  ? 89  HIS A CB  1 
ATOM   722  C CG  . HIS A 1 90 ? 15.029  -11.026 -1.111  1.00 21.15  ? 89  HIS A CG  1 
ATOM   723  N ND1 . HIS A 1 90 ? 13.786  -10.926 -1.704  1.00 20.22  ? 89  HIS A ND1 1 
ATOM   724  C CD2 . HIS A 1 90 ? 14.977  -10.304 0.014   1.00 20.06  ? 89  HIS A CD2 1 
ATOM   725  C CE1 . HIS A 1 90 ? 13.035  -10.087 -0.986  1.00 19.56  ? 89  HIS A CE1 1 
ATOM   726  N NE2 . HIS A 1 90 ? 13.737  -9.717  0.091   1.00 21.98  ? 89  HIS A NE2 1 
ATOM   727  N N   . ALA A 1 91 ? 17.119  -15.345 -1.961  1.00 20.48  ? 90  ALA A N   1 
ATOM   728  C CA  . ALA A 1 91 ? 18.168  -16.185 -2.536  1.00 21.57  ? 90  ALA A CA  1 
ATOM   729  C C   . ALA A 1 91 ? 17.710  -16.876 -3.816  1.00 26.10  ? 90  ALA A C   1 
ATOM   730  O O   . ALA A 1 91 ? 16.526  -17.025 -4.082  1.00 23.83  ? 90  ALA A O   1 
ATOM   731  C CB  . ALA A 1 91 ? 18.619  -17.199 -1.514  1.00 24.11  ? 90  ALA A CB  1 
ATOM   732  N N   . SER A 1 92 ? 18.698  -17.415 -4.544  1.00 25.73  ? 91  SER A N   1 
ATOM   733  C CA  . SER A 1 92 ? 18.433  -18.324 -5.643  1.00 29.06  ? 91  SER A CA  1 
ATOM   734  C C   . SER A 1 92 ? 18.146  -19.715 -5.085  1.00 31.19  ? 91  SER A C   1 
ATOM   735  O O   . SER A 1 92 ? 18.960  -20.247 -4.322  1.00 30.71  ? 91  SER A O   1 
ATOM   736  C CB  . SER A 1 92 ? 19.642  -18.329 -6.513  1.00 32.31  ? 91  SER A CB  1 
ATOM   737  O OG  . SER A 1 92 ? 19.536  -19.448 -7.363  1.00 35.44  ? 91  SER A OG  1 
ATOM   738  N N   . TYR A 1 93 ? 16.982  -20.282 -5.448  1.00 27.31  ? 92  TYR A N   1 
ATOM   739  C CA  . TYR A 1 93 ? 16.595  -21.609 -5.005  1.00 29.20  ? 92  TYR A CA  1 
ATOM   740  C C   . TYR A 1 93 ? 16.452  -22.559 -6.190  1.00 35.19  ? 92  TYR A C   1 
ATOM   741  O O   . TYR A 1 93 ? 15.986  -23.671 -6.012  1.00 44.57  ? 92  TYR A O   1 
ATOM   742  C CB  . TYR A 1 93 ? 15.275  -21.567 -4.211  1.00 27.32  ? 92  TYR A CB  1 
ATOM   743  C CG  . TYR A 1 93 ? 15.444  -20.977 -2.822  1.00 26.46  ? 92  TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 93 ? 15.895  -21.757 -1.748  1.00 27.38  ? 92  TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 93 ? 15.128  -19.634 -2.567  1.00 23.82  ? 92  TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 93 ? 16.053  -21.213 -0.480  1.00 31.22  ? 92  TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 93 ? 15.273  -19.105 -1.303  1.00 25.68  ? 92  TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 93 ? 15.720  -19.887 -0.259  1.00 27.41  ? 92  TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 93 ? 15.977  -19.382 0.983   1.00 26.48  ? 92  TYR A OH  1 
ATOM   750  N N   . SER A 1 94 ? 16.891  -22.126 -7.365  1.00 44.44  ? 93  SER A N   1 
ATOM   751  C CA  . SER A 1 94 ? 16.884  -22.962 -8.556  1.00 56.03  ? 93  SER A CA  1 
ATOM   752  C C   . SER A 1 94 ? 18.083  -23.928 -8.530  1.00 69.16  ? 93  SER A C   1 
ATOM   753  O O   . SER A 1 94 ? 19.069  -23.634 -7.799  1.00 68.46  ? 93  SER A O   1 
ATOM   754  C CB  . SER A 1 94 ? 16.905  -22.101 -9.790  1.00 55.25  ? 93  SER A CB  1 
ATOM   755  O OG  . SER A 1 94 ? 18.129  -21.377 -9.845  1.00 58.57  ? 93  SER A OG  1 
ATOM   756  O OXT . SER A 1 94 ? 17.998  -24.945 -9.255  1.00 83.85  ? 93  SER A OXT 1 
ATOM   757  N N   . MET B 1 2  ? 38.804  -11.015 -42.166 1.00 60.14  ? 1   MET B N   1 
ATOM   758  C CA  . MET B 1 2  ? 38.489  -11.974 -43.255 1.00 54.96  ? 1   MET B CA  1 
ATOM   759  C C   . MET B 1 2  ? 36.974  -12.178 -43.280 1.00 51.10  ? 1   MET B C   1 
ATOM   760  O O   . MET B 1 2  ? 36.385  -12.458 -42.232 1.00 56.77  ? 1   MET B O   1 
ATOM   761  C CB  . MET B 1 2  ? 39.249  -13.293 -43.038 1.00 57.45  ? 1   MET B CB  1 
ATOM   762  C CG  . MET B 1 2  ? 39.201  -14.287 -44.195 1.00 74.29  ? 1   MET B CG  1 
ATOM   763  S SD  . MET B 1 2  ? 39.952  -13.764 -45.754 1.00 82.56  ? 1   MET B SD  1 
ATOM   764  C CE  . MET B 1 2  ? 41.308  -12.753 -45.141 1.00 57.69  ? 1   MET B CE  1 
ATOM   765  N N   . PRO B 1 3  ? 36.290  -11.993 -44.442 1.00 44.03  ? 2   PRO B N   1 
ATOM   766  C CA  . PRO B 1 3  ? 34.850  -12.254 -44.530 1.00 40.16  ? 2   PRO B CA  1 
ATOM   767  C C   . PRO B 1 3  ? 34.528  -13.690 -44.116 1.00 44.12  ? 2   PRO B C   1 
ATOM   768  O O   . PRO B 1 3  ? 35.345  -14.582 -44.317 1.00 46.03  ? 2   PRO B O   1 
ATOM   769  C CB  . PRO B 1 3  ? 34.489  -11.985 -45.988 1.00 40.36  ? 2   PRO B CB  1 
ATOM   770  C CG  . PRO B 1 3  ? 35.583  -11.024 -46.444 1.00 36.23  ? 2   PRO B CG  1 
ATOM   771  C CD  . PRO B 1 3  ? 36.846  -11.472 -45.699 1.00 36.77  ? 2   PRO B CD  1 
ATOM   772  N N   . HIS B 1 4  ? 33.359  -13.878 -43.482 1.00 42.35  ? 3   HIS B N   1 
ATOM   773  C CA  . HIS B 1 4  ? 32.907  -15.201 -43.063 1.00 39.32  ? 3   HIS B CA  1 
ATOM   774  C C   . HIS B 1 4  ? 31.523  -15.466 -43.648 1.00 36.52  ? 3   HIS B C   1 
ATOM   775  O O   . HIS B 1 4  ? 30.937  -14.603 -44.305 1.00 35.79  ? 3   HIS B O   1 
ATOM   776  C CB  . HIS B 1 4  ? 32.987  -15.338 -41.541 1.00 44.42  ? 3   HIS B CB  1 
ATOM   777  C CG  . HIS B 1 4  ? 34.392  -15.415 -41.034 1.00 58.52  ? 3   HIS B CG  1 
ATOM   778  N ND1 . HIS B 1 4  ? 35.333  -16.265 -41.583 1.00 58.70  ? 3   HIS B ND1 1 
ATOM   779  C CD2 . HIS B 1 4  ? 35.008  -14.783 -40.015 1.00 56.48  ? 3   HIS B CD2 1 
ATOM   780  C CE1 . HIS B 1 4  ? 36.477  -16.136 -40.923 1.00 54.12  ? 3   HIS B CE1 1 
ATOM   781  N NE2 . HIS B 1 4  ? 36.302  -15.244 -39.969 1.00 59.23  ? 3   HIS B NE2 1 
ATOM   782  N N   . ALA B 1 5  ? 30.986  -16.671 -43.419 1.00 32.50  ? 4   ALA B N   1 
ATOM   783  C CA  . ALA B 1 5  ? 29.684  -16.981 -43.983 1.00 34.92  ? 4   ALA B CA  1 
ATOM   784  C C   . ALA B 1 5  ? 28.660  -15.948 -43.523 1.00 33.33  ? 4   ALA B C   1 
ATOM   785  O O   . ALA B 1 5  ? 27.759  -15.568 -44.277 1.00 34.82  ? 4   ALA B O   1 
ATOM   786  C CB  . ALA B 1 5  ? 29.289  -18.365 -43.521 1.00 34.87  ? 4   ALA B CB  1 
ATOM   787  N N   . PHE B 1 6  ? 28.762  -15.590 -42.242 1.00 39.25  ? 5   PHE B N   1 
ATOM   788  C CA  . PHE B 1 6  ? 27.929  -14.557 -41.649 1.00 40.08  ? 5   PHE B CA  1 
ATOM   789  C C   . PHE B 1 6  ? 28.783  -13.323 -41.347 1.00 35.43  ? 5   PHE B C   1 
ATOM   790  O O   . PHE B 1 6  ? 29.883  -13.440 -40.822 1.00 38.94  ? 5   PHE B O   1 
ATOM   791  C CB  . PHE B 1 6  ? 27.382  -15.048 -40.306 1.00 38.41  ? 5   PHE B CB  1 
ATOM   792  C CG  . PHE B 1 6  ? 26.318  -16.134 -40.382 1.00 34.83  ? 5   PHE B CG  1 
ATOM   793  C CD1 . PHE B 1 6  ? 24.979  -15.793 -40.545 1.00 31.15  ? 5   PHE B CD1 1 
ATOM   794  C CD2 . PHE B 1 6  ? 26.643  -17.491 -40.322 1.00 33.73  ? 5   PHE B CD2 1 
ATOM   795  C CE1 . PHE B 1 6  ? 23.991  -16.758 -40.631 1.00 32.77  ? 5   PHE B CE1 1 
ATOM   796  C CE2 . PHE B 1 6  ? 25.634  -18.450 -40.388 1.00 29.78  ? 5   PHE B CE2 1 
ATOM   797  C CZ  . PHE B 1 6  ? 24.318  -18.100 -40.510 1.00 30.62  ? 5   PHE B CZ  1 
ATOM   798  N N   . LYS B 1 7  ? 28.247  -12.154 -41.697 1.00 39.91  ? 6   LYS B N   1 
ATOM   799  C CA  . LYS B 1 7  ? 28.973  -10.909 -41.482 1.00 37.29  ? 6   LYS B CA  1 
ATOM   800  C C   . LYS B 1 7  ? 28.200  -10.069 -40.467 1.00 38.32  ? 6   LYS B C   1 
ATOM   801  O O   . LYS B 1 7  ? 26.972  -10.198 -40.356 1.00 33.98  ? 6   LYS B O   1 
ATOM   802  C CB  . LYS B 1 7  ? 29.057  -10.165 -42.813 1.00 43.99  ? 6   LYS B CB  1 
ATOM   803  C CG  . LYS B 1 7  ? 27.742  -9.828  -43.474 1.00 43.45  ? 6   LYS B CG  1 
ATOM   804  C CD  . LYS B 1 7  ? 27.948  -9.335  -44.907 1.00 49.99  ? 6   LYS B CD  1 
ATOM   805  C CE  . LYS B 1 7  ? 26.701  -8.956  -45.649 1.00 48.69  ? 6   LYS B CE  1 
ATOM   806  N NZ  . LYS B 1 7  ? 25.802  -10.087 -45.923 1.00 51.02  ? 6   LYS B NZ  1 
ATOM   807  N N   . PRO B 1 8  ? 28.879  -9.127  -39.769 1.00 40.63  ? 7   PRO B N   1 
ATOM   808  C CA  . PRO B 1 8  ? 28.217  -8.187  -38.858 1.00 32.16  ? 7   PRO B CA  1 
ATOM   809  C C   . PRO B 1 8  ? 27.048  -7.516  -39.541 1.00 29.90  ? 7   PRO B C   1 
ATOM   810  O O   . PRO B 1 8  ? 27.155  -7.063  -40.700 1.00 34.99  ? 7   PRO B O   1 
ATOM   811  C CB  . PRO B 1 8  ? 29.384  -7.230  -38.632 1.00 37.11  ? 7   PRO B CB  1 
ATOM   812  C CG  . PRO B 1 8  ? 30.569  -8.183  -38.546 1.00 41.34  ? 7   PRO B CG  1 
ATOM   813  C CD  . PRO B 1 8  ? 30.331  -8.869  -39.863 1.00 42.55  ? 7   PRO B CD  1 
ATOM   814  N N   . GLY B 1 9  ? 25.911  -7.474  -38.832 1.00 27.73  ? 8   GLY B N   1 
ATOM   815  C CA  . GLY B 1 9  ? 24.675  -6.865  -39.284 1.00 26.28  ? 8   GLY B CA  1 
ATOM   816  C C   . GLY B 1 9  ? 23.713  -7.843  -39.959 1.00 24.39  ? 8   GLY B C   1 
ATOM   817  O O   . GLY B 1 9  ? 22.570  -7.494  -40.253 1.00 27.45  ? 8   GLY B O   1 
ATOM   818  N N   . ASP B 1 10 ? 24.183  -9.072  -40.275 1.00 26.38  ? 9   ASP B N   1 
ATOM   819  C CA  . ASP B 1 10 ? 23.244  -10.055 -40.795 1.00 27.25  ? 9   ASP B CA  1 
ATOM   820  C C   . ASP B 1 10 ? 22.179  -10.407 -39.738 1.00 22.64  ? 9   ASP B C   1 
ATOM   821  O O   . ASP B 1 10 ? 22.483  -10.475 -38.540 1.00 26.52  ? 9   ASP B O   1 
ATOM   822  C CB  . ASP B 1 10 ? 23.938  -11.363 -41.149 1.00 28.13  ? 9   ASP B CB  1 
ATOM   823  C CG  . ASP B 1 10 ? 24.717  -11.414 -42.459 1.00 38.98  ? 9   ASP B CG  1 
ATOM   824  O OD1 . ASP B 1 10 ? 24.403  -10.597 -43.340 1.00 35.88  ? 9   ASP B OD1 1 
ATOM   825  O OD2 . ASP B 1 10 ? 25.611  -12.304 -42.569 1.00 38.82  ? 9   ASP B OD2 1 
ATOM   826  N N   . LEU B 1 11 ? 20.964  -10.569 -40.218 1.00 24.83  ? 10  LEU B N   1 
ATOM   827  C CA  . LEU B 1 11 ? 19.828  -10.805 -39.327 1.00 25.68  ? 10  LEU B CA  1 
ATOM   828  C C   . LEU B 1 11 ? 19.576  -12.308 -39.329 1.00 25.18  ? 10  LEU B C   1 
ATOM   829  O O   . LEU B 1 11 ? 19.642  -12.900 -40.414 1.00 26.60  ? 10  LEU B O   1 
ATOM   830  C CB  . LEU B 1 11 ? 18.613  -9.991  -39.764 1.00 26.88  ? 10  LEU B CB  1 
ATOM   831  C CG  . LEU B 1 11 ? 18.860  -8.476  -39.875 1.00 25.37  ? 10  LEU B CG  1 
ATOM   832  C CD1 . LEU B 1 11 ? 17.520  -7.816  -40.239 1.00 26.62  ? 10  LEU B CD1 1 
ATOM   833  C CD2 . LEU B 1 11 ? 19.468  -8.006  -38.544 1.00 27.78  ? 10  LEU B CD2 1 
ATOM   834  N N   . VAL B 1 12 ? 19.223  -12.877 -38.149 1.00 23.35  ? 11  VAL B N   1 
ATOM   835  C CA  . VAL B 1 12 ? 19.011  -14.331 -38.036 1.00 21.91  ? 11  VAL B CA  1 
ATOM   836  C C   . VAL B 1 12 ? 17.908  -14.596 -37.019 1.00 24.93  ? 11  VAL B C   1 
ATOM   837  O O   . VAL B 1 12 ? 17.538  -13.711 -36.254 1.00 24.10  ? 11  VAL B O   1 
ATOM   838  C CB  . VAL B 1 12 ? 20.310  -15.003 -37.539 1.00 23.52  ? 11  VAL B CB  1 
ATOM   839  C CG1 . VAL B 1 12 ? 21.458  -14.847 -38.568 1.00 25.53  ? 11  VAL B CG1 1 
ATOM   840  C CG2 . VAL B 1 12 ? 20.756  -14.549 -36.136 1.00 23.70  ? 11  VAL B CG2 1 
ATOM   841  N N   . PHE B 1 13 ? 17.458  -15.861 -36.949 1.00 22.97  ? 12  PHE B N   1 
ATOM   842  C CA  . PHE B 1 13 ? 16.952  -16.387 -35.688 1.00 24.13  ? 12  PHE B CA  1 
ATOM   843  C C   . PHE B 1 13 ? 18.061  -17.246 -35.095 1.00 20.97  ? 12  PHE B C   1 
ATOM   844  O O   . PHE B 1 13 ? 18.682  -18.029 -35.839 1.00 24.95  ? 12  PHE B O   1 
ATOM   845  C CB  . PHE B 1 13 ? 15.727  -17.257 -35.918 1.00 23.99  ? 12  PHE B CB  1 
ATOM   846  C CG  . PHE B 1 13 ? 14.522  -16.429 -36.333 1.00 22.90  ? 12  PHE B CG  1 
ATOM   847  C CD1 . PHE B 1 13 ? 14.308  -16.119 -37.680 1.00 26.60  ? 12  PHE B CD1 1 
ATOM   848  C CD2 . PHE B 1 13 ? 13.625  -15.954 -35.375 1.00 24.81  ? 12  PHE B CD2 1 
ATOM   849  C CE1 . PHE B 1 13 ? 13.221  -15.361 -38.060 1.00 29.05  ? 12  PHE B CE1 1 
ATOM   850  C CE2 . PHE B 1 13 ? 12.529  -15.198 -35.766 1.00 26.87  ? 12  PHE B CE2 1 
ATOM   851  C CZ  . PHE B 1 13 ? 12.331  -14.903 -37.112 1.00 31.86  ? 12  PHE B CZ  1 
ATOM   852  N N   . ALA B 1 14 ? 18.301  -17.102 -33.780 1.00 20.73  ? 13  ALA B N   1 
ATOM   853  C CA  . ALA B 1 14 ? 19.340  -17.833 -33.098 1.00 23.23  ? 13  ALA B CA  1 
ATOM   854  C C   . ALA B 1 14 ? 18.709  -18.774 -32.074 1.00 22.72  ? 13  ALA B C   1 
ATOM   855  O O   . ALA B 1 14 ? 17.764  -18.397 -31.353 1.00 24.75  ? 13  ALA B O   1 
ATOM   856  C CB  . ALA B 1 14 ? 20.331  -16.884 -32.430 1.00 23.72  ? 13  ALA B CB  1 
ATOM   857  N N   . LYS B 1 15 ? 19.243  -20.007 -32.030 1.00 21.64  ? 14  LYS B N   1 
ATOM   858  C CA  . LYS B 1 15 ? 18.616  -21.038 -31.189 1.00 25.30  ? 14  LYS B CA  1 
ATOM   859  C C   . LYS B 1 15 ? 19.503  -21.313 -29.987 1.00 24.98  ? 14  LYS B C   1 
ATOM   860  O O   . LYS B 1 15 ? 20.699  -21.599 -30.108 1.00 26.69  ? 14  LYS B O   1 
ATOM   861  C CB  . LYS B 1 15 ? 18.411  -22.306 -32.026 1.00 26.36  ? 14  LYS B CB  1 
ATOM   862  C CG  . LYS B 1 15 ? 17.700  -23.446 -31.182 1.00 25.11  ? 14  LYS B CG  1 
ATOM   863  C CD  . LYS B 1 15 ? 16.231  -23.060 -31.024 1.00 28.46  ? 14  LYS B CD  1 
ATOM   864  C CE  . LYS B 1 15 ? 15.356  -24.203 -30.368 1.00 29.42  ? 14  LYS B CE  1 
ATOM   865  N NZ  . LYS B 1 15 ? 15.847  -24.362 -29.007 1.00 27.32  ? 14  LYS B NZ  1 
ATOM   866  N N   . MET B 1 16 ? 18.897  -21.162 -28.808 1.00 24.53  ? 15  MET B N   1 
ATOM   867  C CA  . MET B 1 16 ? 19.511  -21.527 -27.536 1.00 28.64  ? 15  MET B CA  1 
ATOM   868  C C   . MET B 1 16 ? 18.670  -22.638 -26.902 1.00 29.26  ? 15  MET B C   1 
ATOM   869  O O   . MET B 1 16 ? 17.437  -22.623 -26.972 1.00 28.22  ? 15  MET B O   1 
ATOM   870  C CB  . MET B 1 16 ? 19.549  -20.341 -26.562 1.00 31.35  ? 15  MET B CB  1 
ATOM   871  C CG  . MET B 1 16 ? 20.068  -19.061 -27.141 1.00 39.88  ? 15  MET B CG  1 
ATOM   872  S SD  . MET B 1 16 ? 21.314  -18.319 -26.066 1.00 60.95  ? 15  MET B SD  1 
ATOM   873  C CE  . MET B 1 16 ? 22.482  -19.386 -26.904 1.00 36.84  ? 15  MET B CE  1 
ATOM   874  N N   . LYS B 1 17 ? 19.352  -23.546 -26.186 1.00 31.61  ? 16  LYS B N   1 
ATOM   875  C CA  . LYS B 1 17 ? 18.647  -24.612 -25.486 1.00 32.92  ? 16  LYS B CA  1 
ATOM   876  C C   . LYS B 1 17 ? 17.662  -23.993 -24.484 1.00 28.33  ? 16  LYS B C   1 
ATOM   877  O O   . LYS B 1 17 ? 18.012  -23.083 -23.737 1.00 33.14  ? 16  LYS B O   1 
ATOM   878  C CB  . LYS B 1 17 ? 19.713  -25.533 -24.871 1.00 38.07  ? 16  LYS B CB  1 
ATOM   879  C CG  . LYS B 1 17 ? 19.139  -26.807 -24.212 1.00 43.41  ? 16  LYS B CG  1 
ATOM   880  C CD  . LYS B 1 17 ? 20.163  -27.606 -23.412 1.00 47.70  ? 16  LYS B CD  1 
ATOM   881  N N   . GLY B 1 18 ? 16.418  -24.472 -24.534 1.00 31.52  ? 17  GLY B N   1 
ATOM   882  C CA  . GLY B 1 18 ? 15.362  -24.014 -23.638 1.00 34.04  ? 17  GLY B CA  1 
ATOM   883  C C   . GLY B 1 18 ? 14.531  -22.862 -24.203 1.00 34.77  ? 17  GLY B C   1 
ATOM   884  O O   . GLY B 1 18 ? 13.585  -22.405 -23.552 1.00 31.89  ? 17  GLY B O   1 
ATOM   885  N N   . TYR B 1 19 ? 14.887  -22.354 -25.401 1.00 30.44  ? 18  TYR B N   1 
ATOM   886  C CA  . TYR B 1 19 ? 14.172  -21.167 -25.874 1.00 26.47  ? 18  TYR B CA  1 
ATOM   887  C C   . TYR B 1 19 ? 13.762  -21.367 -27.330 1.00 27.09  ? 18  TYR B C   1 
ATOM   888  O O   . TYR B 1 19 ? 14.449  -22.104 -28.033 1.00 28.35  ? 18  TYR B O   1 
ATOM   889  C CB  . TYR B 1 19 ? 15.053  -19.901 -25.876 1.00 25.77  ? 18  TYR B CB  1 
ATOM   890  C CG  . TYR B 1 19 ? 15.538  -19.575 -24.466 1.00 28.52  ? 18  TYR B CG  1 
ATOM   891  C CD1 . TYR B 1 19 ? 14.770  -18.805 -23.600 1.00 32.62  ? 18  TYR B CD1 1 
ATOM   892  C CD2 . TYR B 1 19 ? 16.720  -20.140 -23.999 1.00 30.25  ? 18  TYR B CD2 1 
ATOM   893  C CE1 . TYR B 1 19 ? 15.217  -18.557 -22.300 1.00 31.55  ? 18  TYR B CE1 1 
ATOM   894  C CE2 . TYR B 1 19 ? 17.168  -19.901 -22.704 1.00 32.80  ? 18  TYR B CE2 1 
ATOM   895  C CZ  . TYR B 1 19 ? 16.395  -19.134 -21.855 1.00 32.07  ? 18  TYR B CZ  1 
ATOM   896  O OH  . TYR B 1 19 ? 16.877  -18.922 -20.580 1.00 39.79  ? 18  TYR B OH  1 
ATOM   897  N N   . PRO B 1 20 ? 12.711  -20.691 -27.842 1.00 26.14  ? 19  PRO B N   1 
ATOM   898  C CA  . PRO B 1 20 ? 12.332  -20.779 -29.257 1.00 23.82  ? 19  PRO B CA  1 
ATOM   899  C C   . PRO B 1 20 ? 13.395  -20.045 -30.075 1.00 24.30  ? 19  PRO B C   1 
ATOM   900  O O   . PRO B 1 20 ? 14.065  -19.185 -29.548 1.00 24.54  ? 19  PRO B O   1 
ATOM   901  C CB  . PRO B 1 20 ? 11.011  -20.052 -29.373 1.00 24.95  ? 19  PRO B CB  1 
ATOM   902  C CG  . PRO B 1 20 ? 10.993  -19.115 -28.186 1.00 25.74  ? 19  PRO B CG  1 
ATOM   903  C CD  . PRO B 1 20 ? 11.841  -19.778 -27.094 1.00 26.05  ? 19  PRO B CD  1 
ATOM   904  N N   . HIS B 1 21 ? 13.535  -20.426 -31.351 1.00 24.34  ? 20  HIS B N   1 
ATOM   905  C CA  . HIS B 1 21 ? 14.382  -19.643 -32.266 1.00 23.52  ? 20  HIS B CA  1 
ATOM   906  C C   . HIS B 1 21 ? 14.096  -18.141 -32.121 1.00 23.04  ? 20  HIS B C   1 
ATOM   907  O O   . HIS B 1 21 ? 12.945  -17.730 -32.234 1.00 24.68  ? 20  HIS B O   1 
ATOM   908  C CB  . HIS B 1 21 ? 14.152  -20.112 -33.699 1.00 24.50  ? 20  HIS B CB  1 
ATOM   909  C CG  . HIS B 1 21 ? 14.359  -21.596 -33.905 1.00 24.64  ? 20  HIS B CG  1 
ATOM   910  N ND1 . HIS B 1 21 ? 13.478  -22.586 -33.456 1.00 26.88  ? 20  HIS B ND1 1 
ATOM   911  C CD2 . HIS B 1 21 ? 15.380  -22.241 -34.478 1.00 27.25  ? 20  HIS B CD2 1 
ATOM   912  C CE1 . HIS B 1 21 ? 13.964  -23.783 -33.780 1.00 28.41  ? 20  HIS B CE1 1 
ATOM   913  N NE2 . HIS B 1 21 ? 15.113  -23.612 -34.416 1.00 25.93  ? 20  HIS B NE2 1 
ATOM   914  N N   . TRP B 1 22 ? 15.179  -17.357 -31.943 1.00 22.61  ? 21  TRP B N   1 
ATOM   915  C CA  . TRP B 1 22 ? 14.975  -16.032 -31.361 1.00 21.49  ? 21  TRP B CA  1 
ATOM   916  C C   . TRP B 1 22 ? 15.464  -14.953 -32.326 1.00 23.53  ? 21  TRP B C   1 
ATOM   917  O O   . TRP B 1 22 ? 16.582  -15.084 -32.797 1.00 22.32  ? 21  TRP B O   1 
ATOM   918  C CB  . TRP B 1 22 ? 15.721  -15.932 -30.026 1.00 23.99  ? 21  TRP B CB  1 
ATOM   919  C CG  . TRP B 1 22 ? 15.197  -14.796 -29.173 1.00 23.45  ? 21  TRP B CG  1 
ATOM   920  C CD1 . TRP B 1 22 ? 15.446  -13.452 -29.299 1.00 24.00  ? 21  TRP B CD1 1 
ATOM   921  C CD2 . TRP B 1 22 ? 14.258  -14.920 -28.071 1.00 24.97  ? 21  TRP B CD2 1 
ATOM   922  N NE1 . TRP B 1 22 ? 14.719  -12.745 -28.354 1.00 23.97  ? 21  TRP B NE1 1 
ATOM   923  C CE2 . TRP B 1 22 ? 14.003  -13.616 -27.576 1.00 24.17  ? 21  TRP B CE2 1 
ATOM   924  C CE3 . TRP B 1 22 ? 13.641  -16.026 -27.462 1.00 27.25  ? 21  TRP B CE3 1 
ATOM   925  C CZ2 . TRP B 1 22 ? 13.141  -13.362 -26.503 1.00 25.14  ? 21  TRP B CZ2 1 
ATOM   926  C CZ3 . TRP B 1 22 ? 12.816  -15.784 -26.382 1.00 26.38  ? 21  TRP B CZ3 1 
ATOM   927  C CH2 . TRP B 1 22 ? 12.552  -14.475 -25.942 1.00 25.72  ? 21  TRP B CH2 1 
ATOM   928  N N   . PRO B 1 23 ? 14.703  -13.853 -32.601 1.00 22.75  ? 22  PRO B N   1 
ATOM   929  C CA  . PRO B 1 23 ? 15.211  -12.825 -33.533 1.00 21.37  ? 22  PRO B CA  1 
ATOM   930  C C   . PRO B 1 23 ? 16.509  -12.209 -33.014 1.00 23.84  ? 22  PRO B C   1 
ATOM   931  O O   . PRO B 1 23 ? 16.619  -11.848 -31.832 1.00 22.97  ? 22  PRO B O   1 
ATOM   932  C CB  . PRO B 1 23 ? 14.027  -11.767 -33.598 1.00 20.22  ? 22  PRO B CB  1 
ATOM   933  C CG  . PRO B 1 23 ? 13.361  -11.967 -32.236 1.00 21.24  ? 22  PRO B CG  1 
ATOM   934  C CD  . PRO B 1 23 ? 13.384  -13.521 -32.059 1.00 21.76  ? 22  PRO B CD  1 
ATOM   935  N N   . ALA B 1 24 ? 17.520  -12.100 -33.890 1.00 21.22  ? 23  ALA B N   1 
ATOM   936  C CA  . ALA B 1 24 ? 18.858  -11.752 -33.426 1.00 20.81  ? 23  ALA B CA  1 
ATOM   937  C C   . ALA B 1 24 ? 19.673  -11.188 -34.596 1.00 21.05  ? 23  ALA B C   1 
ATOM   938  O O   . ALA B 1 24 ? 19.229  -11.244 -35.743 1.00 24.61  ? 23  ALA B O   1 
ATOM   939  C CB  . ALA B 1 24 ? 19.574  -12.916 -32.719 1.00 23.33  ? 23  ALA B CB  1 
ATOM   940  N N   . ARG B 1 25 ? 20.834  -10.639 -34.239 1.00 23.99  ? 24  ARG B N   1 
ATOM   941  C CA  . ARG B 1 25 ? 21.761  -10.172 -35.273 1.00 23.32  ? 24  ARG B CA  1 
ATOM   942  C C   . ARG B 1 25 ? 23.159  -10.658 -34.954 1.00 23.30  ? 24  ARG B C   1 
ATOM   943  O O   . ARG B 1 25 ? 23.525  -10.911 -33.809 1.00 23.91  ? 24  ARG B O   1 
ATOM   944  C CB  . ARG B 1 25 ? 21.754  -8.644  -35.394 1.00 25.30  ? 24  ARG B CB  1 
ATOM   945  C CG  . ARG B 1 25 ? 22.345  -7.895  -34.205 1.00 25.48  ? 24  ARG B CG  1 
ATOM   946  C CD  . ARG B 1 25 ? 22.087  -6.382  -34.397 1.00 24.54  ? 24  ARG B CD  1 
ATOM   947  N NE  . ARG B 1 25 ? 22.757  -5.700  -33.290 1.00 27.05  ? 24  ARG B NE  1 
ATOM   948  C CZ  . ARG B 1 25 ? 22.477  -4.453  -32.870 1.00 28.71  ? 24  ARG B CZ  1 
ATOM   949  N NH1 . ARG B 1 25 ? 21.503  -3.780  -33.470 1.00 28.62  ? 24  ARG B NH1 1 
ATOM   950  N NH2 . ARG B 1 25 ? 23.139  -3.950  -31.832 1.00 26.04  ? 24  ARG B NH2 1 
ATOM   951  N N   . ILE B 1 26 ? 23.995  -10.732 -36.013 1.00 24.58  ? 25  ILE B N   1 
ATOM   952  C CA  . ILE B 1 26 ? 25.413  -10.924 -35.786 1.00 25.32  ? 25  ILE B CA  1 
ATOM   953  C C   . ILE B 1 26 ? 25.983  -9.546  -35.465 1.00 28.11  ? 25  ILE B C   1 
ATOM   954  O O   . ILE B 1 26 ? 25.724  -8.611  -36.225 1.00 32.51  ? 25  ILE B O   1 
ATOM   955  C CB  . ILE B 1 26 ? 26.051  -11.387 -37.111 1.00 31.32  ? 25  ILE B CB  1 
ATOM   956  C CG1 . ILE B 1 26 ? 25.339  -12.609 -37.715 1.00 31.28  ? 25  ILE B CG1 1 
ATOM   957  C CG2 . ILE B 1 26 ? 27.566  -11.574 -36.981 1.00 36.17  ? 25  ILE B CG2 1 
ATOM   958  C CD1 . ILE B 1 26 ? 25.333  -13.825 -36.806 1.00 29.94  ? 25  ILE B CD1 1 
ATOM   959  N N   . ASP B 1 27 ? 26.755  -9.494  -34.377 1.00 29.52  ? 26  ASP B N   1 
ATOM   960  C CA  . ASP B 1 27 ? 27.440  -8.259  -33.989 1.00 34.43  ? 26  ASP B CA  1 
ATOM   961  C C   . ASP B 1 27 ? 28.898  -8.236  -34.473 1.00 38.20  ? 26  ASP B C   1 
ATOM   962  O O   . ASP B 1 27 ? 29.443  -9.266  -34.873 1.00 40.71  ? 26  ASP B O   1 
ATOM   963  C CB  . ASP B 1 27 ? 27.375  -8.079  -32.485 1.00 31.04  ? 26  ASP B CB  1 
ATOM   964  C CG  . ASP B 1 27 ? 26.183  -7.337  -31.894 1.00 33.14  ? 26  ASP B CG  1 
ATOM   965  O OD1 . ASP B 1 27 ? 25.360  -6.793  -32.686 1.00 38.54  ? 26  ASP B OD1 1 
ATOM   966  O OD2 . ASP B 1 27 ? 26.116  -7.279  -30.614 1.00 33.80  ? 26  ASP B OD2 1 
ATOM   967  N N   . ASP B 1 28 ? 29.523  -7.039  -34.419 1.00 48.13  ? 27  ASP B N   1 
ATOM   968  C CA  . ASP B 1 28 ? 30.960  -6.812  -34.564 1.00 57.19  ? 27  ASP B CA  1 
ATOM   969  C C   . ASP B 1 28 ? 31.703  -7.212  -33.287 1.00 61.55  ? 27  ASP B C   1 
ATOM   970  O O   . ASP B 1 28 ? 31.080  -7.498  -32.266 1.00 63.22  ? 27  ASP B O   1 
ATOM   971  C CB  . ASP B 1 28 ? 31.270  -5.335  -34.746 1.00 58.58  ? 27  ASP B CB  1 
ATOM   972  C CG  . ASP B 1 28 ? 30.729  -4.685  -36.009 1.00 68.94  ? 27  ASP B CG  1 
ATOM   973  O OD1 . ASP B 1 28 ? 31.353  -4.882  -37.088 1.00 68.77  ? 27  ASP B OD1 1 
ATOM   974  O OD2 . ASP B 1 28 ? 29.696  -3.984  -35.899 1.00 63.76  ? 27  ASP B OD2 1 
ATOM   975  N N   . ILE B 1 29 ? 33.044  -7.180  -33.327 1.00 65.83  ? 28  ILE B N   1 
ATOM   976  C CA  . ILE B 1 29 ? 33.842  -7.586  -32.179 1.00 72.90  ? 28  ILE B CA  1 
ATOM   977  C C   . ILE B 1 29 ? 34.118  -6.365  -31.280 1.00 81.09  ? 28  ILE B C   1 
ATOM   978  O O   . ILE B 1 29 ? 34.633  -5.351  -31.813 1.00 80.51  ? 28  ILE B O   1 
ATOM   979  C CB  . ILE B 1 29 ? 35.132  -8.313  -32.608 1.00 67.69  ? 28  ILE B CB  1 
ATOM   980  N N   . VAL B 1 34 ? 36.979  -9.623  -25.325 1.00 66.14  ? 33  VAL B N   1 
ATOM   981  C CA  . VAL B 1 34 ? 36.827  -11.089 -25.577 1.00 74.45  ? 33  VAL B CA  1 
ATOM   982  C C   . VAL B 1 34 ? 36.573  -11.272 -27.071 1.00 81.17  ? 33  VAL B C   1 
ATOM   983  O O   . VAL B 1 34 ? 35.860  -10.470 -27.677 1.00 92.99  ? 33  VAL B O   1 
ATOM   984  C CB  . VAL B 1 34 ? 35.691  -11.667 -24.701 1.00 71.92  ? 33  VAL B CB  1 
ATOM   985  C CG1 . VAL B 1 34 ? 34.355  -10.957 -24.912 1.00 69.64  ? 33  VAL B CG1 1 
ATOM   986  C CG2 . VAL B 1 34 ? 35.527  -13.180 -24.843 1.00 65.01  ? 33  VAL B CG2 1 
ATOM   987  N N   . LYS B 1 35 ? 37.207  -12.289 -27.670 1.00 75.86  ? 34  LYS B N   1 
ATOM   988  C CA  . LYS B 1 35 ? 36.849  -12.715 -29.017 1.00 65.10  ? 34  LYS B CA  1 
ATOM   989  C C   . LYS B 1 35 ? 36.027  -14.006 -28.922 1.00 60.53  ? 34  LYS B C   1 
ATOM   990  O O   . LYS B 1 35 ? 36.143  -14.745 -27.938 1.00 58.86  ? 34  LYS B O   1 
ATOM   991  C CB  . LYS B 1 35 ? 38.096  -12.758 -29.908 1.00 68.98  ? 34  LYS B CB  1 
ATOM   992  N N   . PRO B 1 36 ? 35.129  -14.315 -29.896 1.00 53.81  ? 35  PRO B N   1 
ATOM   993  C CA  . PRO B 1 36 ? 34.339  -15.552 -29.833 1.00 51.87  ? 35  PRO B CA  1 
ATOM   994  C C   . PRO B 1 36 ? 35.232  -16.786 -29.758 1.00 45.98  ? 35  PRO B C   1 
ATOM   995  O O   . PRO B 1 36 ? 36.357  -16.747 -30.244 1.00 53.90  ? 35  PRO B O   1 
ATOM   996  C CB  . PRO B 1 36 ? 33.486  -15.539 -31.118 1.00 49.68  ? 35  PRO B CB  1 
ATOM   997  C CG  . PRO B 1 36 ? 34.080  -14.443 -31.986 1.00 54.04  ? 35  PRO B CG  1 
ATOM   998  C CD  . PRO B 1 36 ? 34.807  -13.481 -31.065 1.00 48.83  ? 35  PRO B CD  1 
ATOM   999  N N   . PRO B 1 37 ? 34.793  -17.908 -29.142 1.00 44.97  ? 36  PRO B N   1 
ATOM   1000 C CA  . PRO B 1 37 ? 35.539  -19.156 -29.251 1.00 45.07  ? 36  PRO B CA  1 
ATOM   1001 C C   . PRO B 1 37 ? 35.618  -19.474 -30.740 1.00 51.06  ? 36  PRO B C   1 
ATOM   1002 O O   . PRO B 1 37 ? 34.882  -18.892 -31.546 1.00 51.10  ? 36  PRO B O   1 
ATOM   1003 C CB  . PRO B 1 37 ? 34.683  -20.182 -28.472 1.00 46.39  ? 36  PRO B CB  1 
ATOM   1004 C CG  . PRO B 1 37 ? 33.797  -19.341 -27.566 1.00 47.00  ? 36  PRO B CG  1 
ATOM   1005 C CD  . PRO B 1 37 ? 33.574  -18.044 -28.327 1.00 48.19  ? 36  PRO B CD  1 
ATOM   1006 N N   . PRO B 1 38 ? 36.495  -20.417 -31.157 1.00 51.22  ? 37  PRO B N   1 
ATOM   1007 C CA  . PRO B 1 38 ? 36.600  -20.797 -32.572 1.00 52.19  ? 37  PRO B CA  1 
ATOM   1008 C C   . PRO B 1 38 ? 35.257  -21.232 -33.165 1.00 45.79  ? 37  PRO B C   1 
ATOM   1009 O O   . PRO B 1 38 ? 34.490  -21.922 -32.498 1.00 48.27  ? 37  PRO B O   1 
ATOM   1010 C CB  . PRO B 1 38 ? 37.633  -21.954 -32.546 1.00 50.93  ? 37  PRO B CB  1 
ATOM   1011 C CG  . PRO B 1 38 ? 38.444  -21.713 -31.279 1.00 49.26  ? 37  PRO B CG  1 
ATOM   1012 C CD  . PRO B 1 38 ? 37.424  -21.166 -30.285 1.00 56.42  ? 37  PRO B CD  1 
ATOM   1013 N N   . ASN B 1 39 ? 34.986  -20.812 -34.408 1.00 44.84  ? 38  ASN B N   1 
ATOM   1014 C CA  . ASN B 1 39 ? 33.810  -21.250 -35.166 1.00 51.82  ? 38  ASN B CA  1 
ATOM   1015 C C   . ASN B 1 39 ? 32.512  -20.524 -34.769 1.00 43.26  ? 38  ASN B C   1 
ATOM   1016 O O   . ASN B 1 39 ? 31.474  -20.761 -35.366 1.00 37.99  ? 38  ASN B O   1 
ATOM   1017 C CB  . ASN B 1 39 ? 33.584  -22.759 -35.061 1.00 50.20  ? 38  ASN B CB  1 
ATOM   1018 C CG  . ASN B 1 39 ? 34.810  -23.577 -35.421 1.00 63.82  ? 38  ASN B CG  1 
ATOM   1019 O OD1 . ASN B 1 39 ? 35.196  -24.474 -34.663 1.00 63.99  ? 38  ASN B OD1 1 
ATOM   1020 N ND2 . ASN B 1 39 ? 35.429  -23.297 -36.563 1.00 59.60  ? 38  ASN B ND2 1 
ATOM   1021 N N   . LYS B 1 40 ? 32.544  -19.643 -33.758 1.00 45.67  ? 39  LYS B N   1 
ATOM   1022 C CA  . LYS B 1 40 ? 31.323  -19.015 -33.274 1.00 38.08  ? 39  LYS B CA  1 
ATOM   1023 C C   . LYS B 1 40 ? 31.319  -17.525 -33.583 1.00 37.41  ? 39  LYS B C   1 
ATOM   1024 O O   . LYS B 1 40 ? 32.344  -16.971 -33.964 1.00 39.88  ? 39  LYS B O   1 
ATOM   1025 C CB  . LYS B 1 40 ? 31.252  -19.221 -31.763 1.00 39.48  ? 39  LYS B CB  1 
ATOM   1026 C CG  . LYS B 1 40 ? 31.054  -20.675 -31.392 1.00 40.41  ? 39  LYS B CG  1 
ATOM   1027 C CD  . LYS B 1 40 ? 30.791  -20.767 -29.892 1.00 51.36  ? 39  LYS B CD  1 
ATOM   1028 C CE  . LYS B 1 40 ? 29.900  -21.872 -29.430 1.00 61.44  ? 39  LYS B CE  1 
ATOM   1029 N NZ  . LYS B 1 40 ? 30.397  -23.186 -29.839 1.00 63.79  ? 39  LYS B NZ  1 
ATOM   1030 N N   . TYR B 1 41 ? 30.149  -16.898 -33.405 1.00 32.15  ? 40  TYR B N   1 
ATOM   1031 C CA  . TYR B 1 41 ? 29.883  -15.506 -33.760 1.00 29.60  ? 40  TYR B CA  1 
ATOM   1032 C C   . TYR B 1 41 ? 29.284  -14.797 -32.548 1.00 33.46  ? 40  TYR B C   1 
ATOM   1033 O O   . TYR B 1 41 ? 28.552  -15.401 -31.764 1.00 29.80  ? 40  TYR B O   1 
ATOM   1034 C CB  . TYR B 1 41 ? 28.859  -15.378 -34.890 1.00 30.54  ? 40  TYR B CB  1 
ATOM   1035 C CG  . TYR B 1 41 ? 29.327  -15.874 -36.251 1.00 31.35  ? 40  TYR B CG  1 
ATOM   1036 C CD1 . TYR B 1 41 ? 30.000  -15.040 -37.127 1.00 33.33  ? 40  TYR B CD1 1 
ATOM   1037 C CD2 . TYR B 1 41 ? 29.062  -17.178 -36.658 1.00 31.27  ? 40  TYR B CD2 1 
ATOM   1038 C CE1 . TYR B 1 41 ? 30.426  -15.494 -38.369 1.00 39.41  ? 40  TYR B CE1 1 
ATOM   1039 C CE2 . TYR B 1 41 ? 29.463  -17.641 -37.899 1.00 35.75  ? 40  TYR B CE2 1 
ATOM   1040 C CZ  . TYR B 1 41 ? 30.158  -16.796 -38.758 1.00 37.94  ? 40  TYR B CZ  1 
ATOM   1041 O OH  . TYR B 1 41 ? 30.542  -17.219 -40.015 1.00 34.59  ? 40  TYR B OH  1 
ATOM   1042 N N   . PRO B 1 42 ? 29.502  -13.470 -32.379 1.00 33.65  ? 41  PRO B N   1 
ATOM   1043 C CA  . PRO B 1 42 ? 28.808  -12.734 -31.322 1.00 30.52  ? 41  PRO B CA  1 
ATOM   1044 C C   . PRO B 1 42 ? 27.398  -12.441 -31.808 1.00 28.86  ? 41  PRO B C   1 
ATOM   1045 O O   . PRO B 1 42 ? 27.199  -11.808 -32.854 1.00 28.64  ? 41  PRO B O   1 
ATOM   1046 C CB  . PRO B 1 42 ? 29.627  -11.426 -31.136 1.00 32.96  ? 41  PRO B CB  1 
ATOM   1047 C CG  . PRO B 1 42 ? 30.555  -11.347 -32.335 1.00 36.51  ? 41  PRO B CG  1 
ATOM   1048 C CD  . PRO B 1 42 ? 30.382  -12.609 -33.195 1.00 34.76  ? 41  PRO B CD  1 
ATOM   1049 N N   . ILE B 1 43 ? 26.426  -12.930 -31.007 1.00 27.88  ? 42  ILE B N   1 
ATOM   1050 C CA  . ILE B 1 43 ? 25.001  -12.738 -31.257 1.00 24.84  ? 42  ILE B CA  1 
ATOM   1051 C C   . ILE B 1 43 ? 24.405  -11.713 -30.292 1.00 25.85  ? 42  ILE B C   1 
ATOM   1052 O O   . ILE B 1 43 ? 24.690  -11.773 -29.120 1.00 27.99  ? 42  ILE B O   1 
ATOM   1053 C CB  . ILE B 1 43 ? 24.309  -14.101 -31.097 1.00 24.44  ? 42  ILE B CB  1 
ATOM   1054 C CG1 . ILE B 1 43 ? 25.042  -15.151 -32.004 1.00 27.44  ? 42  ILE B CG1 1 
ATOM   1055 C CG2 . ILE B 1 43 ? 22.820  -13.958 -31.476 1.00 25.58  ? 42  ILE B CG2 1 
ATOM   1056 C CD1 . ILE B 1 43 ? 25.089  -14.807 -33.479 1.00 27.19  ? 42  ILE B CD1 1 
ATOM   1057 N N   . PHE B 1 44 ? 23.582  -10.826 -30.827 1.00 25.98  ? 43  PHE B N   1 
ATOM   1058 C CA  . PHE B 1 44 ? 22.738  -9.935  -30.036 1.00 27.04  ? 43  PHE B CA  1 
ATOM   1059 C C   . PHE B 1 44 ? 21.293  -10.367 -30.255 1.00 24.43  ? 43  PHE B C   1 
ATOM   1060 O O   . PHE B 1 44 ? 20.797  -10.393 -31.377 1.00 24.82  ? 43  PHE B O   1 
ATOM   1061 C CB  . PHE B 1 44 ? 22.947  -8.487  -30.496 1.00 26.16  ? 43  PHE B CB  1 
ATOM   1062 C CG  . PHE B 1 44 ? 22.018  -7.475  -29.830 1.00 26.70  ? 43  PHE B CG  1 
ATOM   1063 C CD1 . PHE B 1 44 ? 20.855  -7.060  -30.469 1.00 24.57  ? 43  PHE B CD1 1 
ATOM   1064 C CD2 . PHE B 1 44 ? 22.316  -6.956  -28.578 1.00 32.31  ? 43  PHE B CD2 1 
ATOM   1065 C CE1 . PHE B 1 44 ? 19.995  -6.142  -29.858 1.00 28.28  ? 43  PHE B CE1 1 
ATOM   1066 C CE2 . PHE B 1 44 ? 21.470  -6.013  -27.979 1.00 27.11  ? 43  PHE B CE2 1 
ATOM   1067 C CZ  . PHE B 1 44 ? 20.331  -5.624  -28.623 1.00 28.92  ? 43  PHE B CZ  1 
ATOM   1068 N N   . PHE B 1 45 ? 20.592  -10.673 -29.147 1.00 23.41  ? 44  PHE B N   1 
ATOM   1069 C CA  . PHE B 1 45 ? 19.204  -11.080 -29.147 1.00 24.10  ? 44  PHE B CA  1 
ATOM   1070 C C   . PHE B 1 45 ? 18.323  -9.860  -28.979 1.00 23.86  ? 44  PHE B C   1 
ATOM   1071 O O   . PHE B 1 45 ? 18.442  -9.094  -27.995 1.00 24.93  ? 44  PHE B O   1 
ATOM   1072 C CB  . PHE B 1 45 ? 19.024  -12.055 -27.971 1.00 22.65  ? 44  PHE B CB  1 
ATOM   1073 C CG  . PHE B 1 45 ? 19.721  -13.401 -28.129 1.00 23.76  ? 44  PHE B CG  1 
ATOM   1074 C CD1 . PHE B 1 45 ? 21.052  -13.589 -27.815 1.00 26.42  ? 44  PHE B CD1 1 
ATOM   1075 C CD2 . PHE B 1 45 ? 19.031  -14.476 -28.688 1.00 23.75  ? 44  PHE B CD2 1 
ATOM   1076 C CE1 . PHE B 1 45 ? 21.691  -14.801 -28.040 1.00 27.56  ? 44  PHE B CE1 1 
ATOM   1077 C CE2 . PHE B 1 45 ? 19.653  -15.697 -28.859 1.00 24.68  ? 44  PHE B CE2 1 
ATOM   1078 C CZ  . PHE B 1 45 ? 20.995  -15.853 -28.579 1.00 25.51  ? 44  PHE B CZ  1 
ATOM   1079 N N   . PHE B 1 46 ? 17.489  -9.650  -30.000 1.00 23.64  ? 45  PHE B N   1 
ATOM   1080 C CA  . PHE B 1 46 ? 16.559  -8.541  -30.002 1.00 22.40  ? 45  PHE B CA  1 
ATOM   1081 C C   . PHE B 1 46 ? 15.554  -8.709  -28.853 1.00 25.70  ? 45  PHE B C   1 
ATOM   1082 O O   . PHE B 1 46 ? 15.220  -9.822  -28.449 1.00 24.64  ? 45  PHE B O   1 
ATOM   1083 C CB  . PHE B 1 46 ? 15.800  -8.351  -31.312 1.00 22.48  ? 45  PHE B CB  1 
ATOM   1084 C CG  . PHE B 1 46 ? 16.750  -7.873  -32.403 1.00 24.94  ? 45  PHE B CG  1 
ATOM   1085 C CD1 . PHE B 1 46 ? 17.235  -6.557  -32.382 1.00 27.17  ? 45  PHE B CD1 1 
ATOM   1086 C CD2 . PHE B 1 46 ? 17.061  -8.711  -33.482 1.00 23.61  ? 45  PHE B CD2 1 
ATOM   1087 C CE1 . PHE B 1 46 ? 18.111  -6.142  -33.384 1.00 26.36  ? 45  PHE B CE1 1 
ATOM   1088 C CE2 . PHE B 1 46 ? 17.903  -8.264  -34.521 1.00 24.70  ? 45  PHE B CE2 1 
ATOM   1089 C CZ  . PHE B 1 46 ? 18.387  -6.966  -34.465 1.00 24.98  ? 45  PHE B CZ  1 
ATOM   1090 N N   . GLY B 1 47 ? 15.045  -7.586  -28.352 1.00 25.29  ? 46  GLY B N   1 
ATOM   1091 C CA  . GLY B 1 47 ? 14.002  -7.649  -27.319 1.00 25.09  ? 46  GLY B CA  1 
ATOM   1092 C C   . GLY B 1 47 ? 14.587  -7.742  -25.909 1.00 28.24  ? 46  GLY B C   1 
ATOM   1093 O O   . GLY B 1 47 ? 14.404  -6.844  -25.081 1.00 30.78  ? 46  GLY B O   1 
ATOM   1094 N N   . THR B 1 48 ? 15.323  -8.816  -25.641 1.00 26.25  ? 47  THR B N   1 
ATOM   1095 C CA  . THR B 1 48 ? 16.004  -9.069  -24.380 1.00 27.30  ? 47  THR B CA  1 
ATOM   1096 C C   . THR B 1 48 ? 17.295  -8.264  -24.305 1.00 28.73  ? 47  THR B C   1 
ATOM   1097 O O   . THR B 1 48 ? 17.756  -7.912  -23.211 1.00 30.94  ? 47  THR B O   1 
ATOM   1098 C CB  . THR B 1 48 ? 16.289  -10.565 -24.210 1.00 30.17  ? 47  THR B CB  1 
ATOM   1099 O OG1 . THR B 1 48 ? 17.256  -11.000 -25.193 1.00 29.58  ? 47  THR B OG1 1 
ATOM   1100 C CG2 . THR B 1 48 ? 15.010  -11.396 -24.203 1.00 26.42  ? 47  THR B CG2 1 
ATOM   1101 N N   . HIS B 1 49 ? 17.889  -8.014  -25.471 1.00 27.56  ? 48  HIS B N   1 
ATOM   1102 C CA  . HIS B 1 49 ? 19.182  -7.353  -25.585 1.00 28.09  ? 48  HIS B CA  1 
ATOM   1103 C C   . HIS B 1 49 ? 20.280  -8.149  -24.902 1.00 28.61  ? 48  HIS B C   1 
ATOM   1104 O O   . HIS B 1 49 ? 21.289  -7.559  -24.505 1.00 35.32  ? 48  HIS B O   1 
ATOM   1105 C CB  . HIS B 1 49 ? 19.137  -5.870  -25.151 1.00 28.07  ? 48  HIS B CB  1 
ATOM   1106 C CG  . HIS B 1 49 ? 17.979  -5.159  -25.726 1.00 31.19  ? 48  HIS B CG  1 
ATOM   1107 N ND1 . HIS B 1 49 ? 17.273  -4.233  -24.988 1.00 33.24  ? 48  HIS B ND1 1 
ATOM   1108 C CD2 . HIS B 1 49 ? 17.362  -5.215  -26.926 1.00 28.49  ? 48  HIS B CD2 1 
ATOM   1109 C CE1 . HIS B 1 49 ? 16.261  -3.778  -25.716 1.00 41.48  ? 48  HIS B CE1 1 
ATOM   1110 N NE2 . HIS B 1 49 ? 16.311  -4.353  -26.909 1.00 33.94  ? 48  HIS B NE2 1 
ATOM   1111 N N   . GLU B 1 50 ? 20.136  -9.473  -24.801 1.00 28.07  ? 49  GLU B N   1 
ATOM   1112 C CA  . GLU B 1 50 ? 21.195  -10.313 -24.270 1.00 28.17  ? 49  GLU B CA  1 
ATOM   1113 C C   . GLU B 1 50 ? 22.213  -10.628 -25.383 1.00 28.07  ? 49  GLU B C   1 
ATOM   1114 O O   . GLU B 1 50 ? 21.939  -10.437 -26.587 1.00 26.62  ? 49  GLU B O   1 
ATOM   1115 C CB  . GLU B 1 50 ? 20.598  -11.656 -23.837 1.00 32.14  ? 49  GLU B CB  1 
ATOM   1116 C CG  . GLU B 1 50 ? 19.554  -11.530 -22.726 1.00 33.72  ? 49  GLU B CG  1 
ATOM   1117 C CD  . GLU B 1 50 ? 20.087  -11.788 -21.333 1.00 40.98  ? 49  GLU B CD  1 
ATOM   1118 O OE1 . GLU B 1 50 ? 21.278  -12.102 -21.156 1.00 44.00  ? 49  GLU B OE1 1 
ATOM   1119 O OE2 . GLU B 1 50 ? 19.276  -11.661 -20.385 1.00 36.92  ? 49  GLU B OE2 1 
ATOM   1120 N N   . THR B 1 51 ? 23.351  -11.190 -24.966 1.00 28.04  ? 50  THR B N   1 
ATOM   1121 C CA  . THR B 1 51 ? 24.410  -11.557 -25.914 1.00 31.44  ? 50  THR B CA  1 
ATOM   1122 C C   . THR B 1 51 ? 24.911  -12.953 -25.585 1.00 33.91  ? 50  THR B C   1 
ATOM   1123 O O   . THR B 1 51 ? 24.828  -13.400 -24.443 1.00 37.11  ? 50  THR B O   1 
ATOM   1124 C CB  . THR B 1 51 ? 25.547  -10.530 -26.018 1.00 34.13  ? 50  THR B CB  1 
ATOM   1125 O OG1 . THR B 1 51 ? 26.101  -10.393 -24.720 1.00 36.06  ? 50  THR B OG1 1 
ATOM   1126 C CG2 . THR B 1 51 ? 25.076  -9.145  -26.408 1.00 31.23  ? 50  THR B CG2 1 
ATOM   1127 N N   . ALA B 1 52 ? 25.360  -13.679 -26.621 1.00 33.02  ? 51  ALA B N   1 
ATOM   1128 C CA  . ALA B 1 52 ? 26.047  -14.949 -26.476 1.00 33.41  ? 51  ALA B CA  1 
ATOM   1129 C C   . ALA B 1 52 ? 26.857  -15.239 -27.732 1.00 29.92  ? 51  ALA B C   1 
ATOM   1130 O O   . ALA B 1 52 ? 26.718  -14.545 -28.740 1.00 29.31  ? 51  ALA B O   1 
ATOM   1131 C CB  . ALA B 1 52 ? 25.098  -16.096 -26.173 1.00 31.75  ? 51  ALA B CB  1 
ATOM   1132 N N   . PHE B 1 53 ? 27.737  -16.237 -27.623 1.00 30.96  ? 52  PHE B N   1 
ATOM   1133 C CA  . PHE B 1 53 ? 28.445  -16.778 -28.773 1.00 32.08  ? 52  PHE B CA  1 
ATOM   1134 C C   . PHE B 1 53 ? 27.754  -18.056 -29.247 1.00 30.48  ? 52  PHE B C   1 
ATOM   1135 O O   . PHE B 1 53 ? 27.554  -19.003 -28.475 1.00 34.06  ? 52  PHE B O   1 
ATOM   1136 C CB  . PHE B 1 53 ? 29.895  -17.081 -28.382 1.00 32.60  ? 52  PHE B CB  1 
ATOM   1137 C CG  . PHE B 1 53 ? 30.683  -15.869 -27.921 1.00 35.39  ? 52  PHE B CG  1 
ATOM   1138 C CD1 . PHE B 1 53 ? 30.974  -14.839 -28.810 1.00 37.91  ? 52  PHE B CD1 1 
ATOM   1139 C CD2 . PHE B 1 53 ? 31.157  -15.781 -26.617 1.00 42.79  ? 52  PHE B CD2 1 
ATOM   1140 C CE1 . PHE B 1 53 ? 31.709  -13.730 -28.409 1.00 40.76  ? 52  PHE B CE1 1 
ATOM   1141 C CE2 . PHE B 1 53 ? 31.886  -14.667 -26.211 1.00 44.39  ? 52  PHE B CE2 1 
ATOM   1142 C CZ  . PHE B 1 53 ? 32.160  -13.652 -27.101 1.00 42.09  ? 52  PHE B CZ  1 
ATOM   1143 N N   . LEU B 1 54 ? 27.414  -18.093 -30.544 1.00 29.62  ? 53  LEU B N   1 
ATOM   1144 C CA  . LEU B 1 54 ? 26.810  -19.271 -31.139 1.00 27.47  ? 53  LEU B CA  1 
ATOM   1145 C C   . LEU B 1 54 ? 27.547  -19.627 -32.431 1.00 29.68  ? 53  LEU B C   1 
ATOM   1146 O O   . LEU B 1 54 ? 28.072  -18.747 -33.129 1.00 31.83  ? 53  LEU B O   1 
ATOM   1147 C CB  . LEU B 1 54 ? 25.321  -19.075 -31.475 1.00 27.43  ? 53  LEU B CB  1 
ATOM   1148 C CG  . LEU B 1 54 ? 24.361  -19.009 -30.282 1.00 28.43  ? 53  LEU B CG  1 
ATOM   1149 C CD1 . LEU B 1 54 ? 22.962  -18.711 -30.754 1.00 28.09  ? 53  LEU B CD1 1 
ATOM   1150 C CD2 . LEU B 1 54 ? 24.427  -20.362 -29.596 1.00 36.68  ? 53  LEU B CD2 1 
ATOM   1151 N N   . GLY B 1 55 ? 27.506  -20.930 -32.744 1.00 30.51  ? 54  GLY B N   1 
ATOM   1152 C CA  . GLY B 1 55 ? 28.021  -21.475 -33.992 1.00 30.31  ? 54  GLY B CA  1 
ATOM   1153 C C   . GLY B 1 55 ? 26.941  -21.491 -35.077 1.00 28.50  ? 54  GLY B C   1 
ATOM   1154 O O   . GLY B 1 55 ? 25.742  -21.368 -34.795 1.00 28.12  ? 54  GLY B O   1 
ATOM   1155 N N   . PRO B 1 56 ? 27.309  -21.668 -36.368 1.00 26.65  ? 55  PRO B N   1 
ATOM   1156 C CA  . PRO B 1 56 ? 26.305  -21.762 -37.428 1.00 26.18  ? 55  PRO B CA  1 
ATOM   1157 C C   . PRO B 1 56 ? 25.139  -22.738 -37.325 1.00 24.54  ? 55  PRO B C   1 
ATOM   1158 O O   . PRO B 1 56 ? 24.089  -22.470 -37.903 1.00 25.88  ? 55  PRO B O   1 
ATOM   1159 C CB  . PRO B 1 56 ? 27.119  -22.015 -38.723 1.00 30.12  ? 55  PRO B CB  1 
ATOM   1160 C CG  . PRO B 1 56 ? 28.570  -21.954 -38.340 1.00 33.42  ? 55  PRO B CG  1 
ATOM   1161 C CD  . PRO B 1 56 ? 28.703  -21.745 -36.852 1.00 30.68  ? 55  PRO B CD  1 
ATOM   1162 N N   . LYS B 1 57 ? 25.336  -23.857 -36.612 1.00 26.95  ? 56  LYS B N   1 
ATOM   1163 C CA  . LYS B 1 57 ? 24.267  -24.843 -36.534 1.00 26.52  ? 56  LYS B CA  1 
ATOM   1164 C C   . LYS B 1 57 ? 23.030  -24.251 -35.858 1.00 27.27  ? 56  LYS B C   1 
ATOM   1165 O O   . LYS B 1 57 ? 21.932  -24.757 -36.070 1.00 27.26  ? 56  LYS B O   1 
ATOM   1166 C CB  . LYS B 1 57 ? 24.679  -26.149 -35.829 1.00 33.29  ? 56  LYS B CB  1 
ATOM   1167 C CG  . LYS B 1 57 ? 24.883  -26.072 -34.324 1.00 38.71  ? 56  LYS B CG  1 
ATOM   1168 C CD  . LYS B 1 57 ? 24.835  -27.459 -33.676 1.00 42.15  ? 56  LYS B CD  1 
ATOM   1169 C CE  . LYS B 1 57 ? 25.130  -27.470 -32.198 1.00 44.71  ? 56  LYS B CE  1 
ATOM   1170 N NZ  . LYS B 1 57 ? 24.117  -26.793 -31.391 1.00 50.31  ? 56  LYS B NZ  1 
ATOM   1171 N N   . ASP B 1 58 ? 23.225  -23.150 -35.080 1.00 25.09  ? 57  ASP B N   1 
ATOM   1172 C CA  . ASP B 1 58 ? 22.153  -22.527 -34.315 1.00 26.31  ? 57  ASP B CA  1 
ATOM   1173 C C   . ASP B 1 58 ? 21.703  -21.193 -34.924 1.00 24.78  ? 57  ASP B C   1 
ATOM   1174 O O   . ASP B 1 58 ? 20.976  -20.428 -34.266 1.00 24.94  ? 57  ASP B O   1 
ATOM   1175 C CB  . ASP B 1 58 ? 22.612  -22.397 -32.879 1.00 25.49  ? 57  ASP B CB  1 
ATOM   1176 C CG  . ASP B 1 58 ? 22.775  -23.728 -32.152 1.00 30.72  ? 57  ASP B CG  1 
ATOM   1177 O OD1 . ASP B 1 58 ? 21.844  -24.586 -32.297 1.00 31.15  ? 57  ASP B OD1 1 
ATOM   1178 O OD2 . ASP B 1 58 ? 23.774  -23.850 -31.403 1.00 35.40  ? 57  ASP B OD2 1 
ATOM   1179 N N   . LEU B 1 59 ? 22.199  -20.880 -36.136 1.00 24.10  ? 58  LEU B N   1 
ATOM   1180 C CA  . LEU B 1 59 ? 21.930  -19.575 -36.739 1.00 23.79  ? 58  LEU B CA  1 
ATOM   1181 C C   . LEU B 1 59 ? 21.178  -19.769 -38.047 1.00 23.30  ? 58  LEU B C   1 
ATOM   1182 O O   . LEU B 1 59 ? 21.649  -20.457 -38.970 1.00 25.38  ? 58  LEU B O   1 
ATOM   1183 C CB  . LEU B 1 59 ? 23.247  -18.829 -36.940 1.00 23.49  ? 58  LEU B CB  1 
ATOM   1184 C CG  . LEU B 1 59 ? 24.083  -18.589 -35.689 1.00 24.33  ? 58  LEU B CG  1 
ATOM   1185 C CD1 . LEU B 1 59 ? 25.359  -17.833 -36.047 1.00 25.97  ? 58  LEU B CD1 1 
ATOM   1186 C CD2 . LEU B 1 59 ? 23.227  -17.682 -34.769 1.00 28.37  ? 58  LEU B CD2 1 
ATOM   1187 N N   . PHE B 1 60 ? 19.993  -19.179 -38.128 1.00 22.02  ? 59  PHE B N   1 
ATOM   1188 C CA  . PHE B 1 60 ? 19.073  -19.374 -39.242 1.00 24.79  ? 59  PHE B CA  1 
ATOM   1189 C C   . PHE B 1 60 ? 18.876  -18.030 -39.931 1.00 24.95  ? 59  PHE B C   1 
ATOM   1190 O O   . PHE B 1 60 ? 18.335  -17.119 -39.335 1.00 25.41  ? 59  PHE B O   1 
ATOM   1191 C CB  . PHE B 1 60 ? 17.744  -19.931 -38.692 1.00 23.30  ? 59  PHE B CB  1 
ATOM   1192 C CG  . PHE B 1 60 ? 17.866  -21.336 -38.091 1.00 24.32  ? 59  PHE B CG  1 
ATOM   1193 C CD1 . PHE B 1 60 ? 18.396  -21.499 -36.805 1.00 26.49  ? 59  PHE B CD1 1 
ATOM   1194 C CD2 . PHE B 1 60 ? 17.457  -22.452 -38.824 1.00 27.45  ? 59  PHE B CD2 1 
ATOM   1195 C CE1 . PHE B 1 60 ? 18.557  -22.768 -36.266 1.00 29.40  ? 59  PHE B CE1 1 
ATOM   1196 C CE2 . PHE B 1 60 ? 17.583  -23.730 -38.266 1.00 27.38  ? 59  PHE B CE2 1 
ATOM   1197 C CZ  . PHE B 1 60 ? 18.163  -23.873 -37.012 1.00 28.42  ? 59  PHE B CZ  1 
ATOM   1198 N N   . PRO B 1 61 ? 19.350  -17.818 -41.183 1.00 27.58  ? 60  PRO B N   1 
ATOM   1199 C CA  . PRO B 1 61 ? 19.125  -16.511 -41.846 1.00 27.07  ? 60  PRO B CA  1 
ATOM   1200 C C   . PRO B 1 61 ? 17.666  -16.043 -41.780 1.00 25.50  ? 60  PRO B C   1 
ATOM   1201 O O   . PRO B 1 61 ? 16.712  -16.796 -42.020 1.00 27.25  ? 60  PRO B O   1 
ATOM   1202 C CB  . PRO B 1 61 ? 19.617  -16.823 -43.289 1.00 29.04  ? 60  PRO B CB  1 
ATOM   1203 C CG  . PRO B 1 61 ? 20.734  -17.815 -43.080 1.00 35.84  ? 60  PRO B CG  1 
ATOM   1204 C CD  . PRO B 1 61 ? 20.192  -18.751 -41.962 1.00 32.93  ? 60  PRO B CD  1 
ATOM   1205 N N   . TYR B 1 62 ? 17.473  -14.739 -41.418 1.00 26.82  ? 61  TYR B N   1 
ATOM   1206 C CA  . TYR B 1 62 ? 16.158  -14.227 -41.099 1.00 29.07  ? 61  TYR B CA  1 
ATOM   1207 C C   . TYR B 1 62 ? 15.177  -14.273 -42.257 1.00 30.10  ? 61  TYR B C   1 
ATOM   1208 O O   . TYR B 1 62 ? 14.068  -14.745 -42.062 1.00 30.31  ? 61  TYR B O   1 
ATOM   1209 C CB  . TYR B 1 62 ? 16.346  -12.790 -40.605 1.00 29.94  ? 61  TYR B CB  1 
ATOM   1210 C CG  . TYR B 1 62 ? 15.022  -12.090 -40.377 1.00 32.67  ? 61  TYR B CG  1 
ATOM   1211 C CD1 . TYR B 1 62 ? 14.268  -12.354 -39.251 1.00 33.19  ? 61  TYR B CD1 1 
ATOM   1212 C CD2 . TYR B 1 62 ? 14.609  -11.068 -41.232 1.00 40.26  ? 61  TYR B CD2 1 
ATOM   1213 C CE1 . TYR B 1 62 ? 13.083  -11.676 -39.017 1.00 32.80  ? 61  TYR B CE1 1 
ATOM   1214 C CE2 . TYR B 1 62 ? 13.434  -10.371 -41.001 1.00 39.82  ? 61  TYR B CE2 1 
ATOM   1215 C CZ  . TYR B 1 62 ? 12.670  -10.689 -39.894 1.00 39.11  ? 61  TYR B CZ  1 
ATOM   1216 O OH  . TYR B 1 62 ? 11.511  -10.025 -39.690 1.00 39.41  ? 61  TYR B OH  1 
ATOM   1217 N N   . ASP B 1 63 ? 15.573  -13.773 -43.443 1.00 33.08  ? 62  ASP B N   1 
ATOM   1218 C CA  . ASP B 1 63 ? 14.711  -13.772 -44.626 1.00 40.23  ? 62  ASP B CA  1 
ATOM   1219 C C   . ASP B 1 63 ? 14.151  -15.161 -44.920 1.00 33.68  ? 62  ASP B C   1 
ATOM   1220 O O   . ASP B 1 63 ? 12.935  -15.341 -44.969 1.00 42.77  ? 62  ASP B O   1 
ATOM   1221 C CB  . ASP B 1 63 ? 15.405  -13.162 -45.833 1.00 48.90  ? 62  ASP B CB  1 
ATOM   1222 C CG  . ASP B 1 63 ? 15.229  -11.659 -45.989 1.00 66.82  ? 62  ASP B CG  1 
ATOM   1223 O OD1 . ASP B 1 63 ? 14.595  -11.035 -45.102 1.00 67.11  ? 62  ASP B OD1 1 
ATOM   1224 O OD2 . ASP B 1 63 ? 15.717  -11.124 -47.010 1.00 76.14  ? 62  ASP B OD2 1 
ATOM   1225 N N   . LYS B 1 64 ? 15.041  -16.136 -45.057 1.00 38.28  ? 63  LYS B N   1 
ATOM   1226 C CA  . LYS B 1 64 ? 14.664  -17.523 -45.284 1.00 37.62  ? 63  LYS B CA  1 
ATOM   1227 C C   . LYS B 1 64 ? 13.697  -18.027 -44.214 1.00 34.77  ? 63  LYS B C   1 
ATOM   1228 O O   . LYS B 1 64 ? 12.749  -18.749 -44.530 1.00 40.37  ? 63  LYS B O   1 
ATOM   1229 C CB  . LYS B 1 64 ? 15.898  -18.426 -45.309 1.00 40.27  ? 63  LYS B CB  1 
ATOM   1230 C CG  . LYS B 1 64 ? 15.593  -19.854 -45.722 1.00 42.35  ? 63  LYS B CG  1 
ATOM   1231 C CD  . LYS B 1 64 ? 16.844  -20.706 -45.642 1.00 46.48  ? 63  LYS B CD  1 
ATOM   1232 C CE  . LYS B 1 64 ? 16.782  -21.979 -46.448 1.00 50.52  ? 63  LYS B CE  1 
ATOM   1233 N NZ  . LYS B 1 64 ? 15.597  -22.820 -46.282 1.00 46.39  ? 63  LYS B NZ  1 
ATOM   1234 N N   . SER B 1 65 ? 13.892  -17.622 -42.953 1.00 32.91  ? 64  SER B N   1 
ATOM   1235 C CA  . SER B 1 65 ? 13.246  -18.403 -41.887 1.00 36.90  ? 64  SER B CA  1 
ATOM   1236 C C   . SER B 1 65 ? 12.133  -17.653 -41.141 1.00 34.97  ? 64  SER B C   1 
ATOM   1237 O O   . SER B 1 65 ? 11.463  -18.212 -40.274 1.00 34.86  ? 64  SER B O   1 
ATOM   1238 C CB  . SER B 1 65 ? 14.280  -19.013 -40.972 1.00 38.47  ? 64  SER B CB  1 
ATOM   1239 O OG  . SER B 1 65 ? 15.012  -17.983 -40.323 1.00 50.90  ? 64  SER B OG  1 
ATOM   1240 N N   . LYS B 1 66 ? 11.849  -16.404 -41.528 1.00 34.41  ? 65  LYS B N   1 
ATOM   1241 C CA  . LYS B 1 66 ? 10.918  -15.598 -40.744 1.00 34.59  ? 65  LYS B CA  1 
ATOM   1242 C C   . LYS B 1 66 ? 9.477   -16.130 -40.748 1.00 37.47  ? 65  LYS B C   1 
ATOM   1243 O O   . LYS B 1 66 ? 8.759   -15.978 -39.757 1.00 36.72  ? 65  LYS B O   1 
ATOM   1244 C CB  . LYS B 1 66 ? 10.979  -14.109 -41.101 1.00 33.33  ? 65  LYS B CB  1 
ATOM   1245 C CG  . LYS B 1 66 ? 10.526  -13.777 -42.522 1.00 37.36  ? 65  LYS B CG  1 
ATOM   1246 C CD  . LYS B 1 66 ? 10.916  -12.357 -42.939 1.00 47.28  ? 65  LYS B CD  1 
ATOM   1247 N N   . ASP B 1 67 ? 8.997   -16.721 -41.845 1.00 37.06  ? 66  ASP B N   1 
ATOM   1248 C CA  . ASP B 1 67 ? 7.596   -17.113 -41.806 1.00 44.61  ? 66  ASP B CA  1 
ATOM   1249 C C   . ASP B 1 67 ? 7.400   -18.303 -40.855 1.00 44.12  ? 66  ASP B C   1 
ATOM   1250 O O   . ASP B 1 67 ? 6.330   -18.476 -40.254 1.00 44.25  ? 66  ASP B O   1 
ATOM   1251 C CB  . ASP B 1 67 ? 6.963   -17.160 -43.189 1.00 57.78  ? 66  ASP B CB  1 
ATOM   1252 C CG  . ASP B 1 67 ? 7.589   -18.129 -44.176 1.00 67.40  ? 66  ASP B CG  1 
ATOM   1253 O OD1 . ASP B 1 67 ? 7.839   -17.716 -45.335 1.00 75.53  ? 66  ASP B OD1 1 
ATOM   1254 O OD2 . ASP B 1 67 ? 7.813   -19.289 -43.779 1.00 82.57  ? 66  ASP B OD2 1 
ATOM   1255 N N   . LYS B 1 68 ? 8.460   -19.100 -40.706 1.00 40.40  ? 67  LYS B N   1 
ATOM   1256 C CA  . LYS B 1 68 ? 8.457   -20.257 -39.827 1.00 35.39  ? 67  LYS B CA  1 
ATOM   1257 C C   . LYS B 1 68 ? 8.670   -19.858 -38.367 1.00 33.07  ? 67  LYS B C   1 
ATOM   1258 O O   . LYS B 1 68 ? 7.940   -20.346 -37.505 1.00 33.69  ? 67  LYS B O   1 
ATOM   1259 C CB  . LYS B 1 68 ? 9.553   -21.229 -40.267 1.00 37.02  ? 67  LYS B CB  1 
ATOM   1260 C CG  . LYS B 1 68 ? 9.734   -22.482 -39.427 1.00 41.19  ? 67  LYS B CG  1 
ATOM   1261 C CD  . LYS B 1 68 ? 10.588  -23.466 -40.222 1.00 52.20  ? 67  LYS B CD  1 
ATOM   1262 C CE  . LYS B 1 68 ? 10.992  -24.691 -39.464 1.00 54.03  ? 67  LYS B CE  1 
ATOM   1263 N NZ  . LYS B 1 68 ? 9.839   -25.500 -39.066 1.00 55.52  ? 67  LYS B NZ  1 
ATOM   1264 N N   . TYR B 1 69 ? 9.649   -18.981 -38.089 1.00 29.46  ? 68  TYR B N   1 
ATOM   1265 C CA  . TYR B 1 69 ? 10.090  -18.730 -36.710 1.00 26.03  ? 68  TYR B CA  1 
ATOM   1266 C C   . TYR B 1 69 ? 9.582   -17.382 -36.199 1.00 27.89  ? 68  TYR B C   1 
ATOM   1267 O O   . TYR B 1 69 ? 9.691   -17.107 -35.006 1.00 30.61  ? 68  TYR B O   1 
ATOM   1268 C CB  . TYR B 1 69 ? 11.611  -18.832 -36.519 1.00 26.92  ? 68  TYR B CB  1 
ATOM   1269 C CG  . TYR B 1 69 ? 12.233  -20.195 -36.804 1.00 29.33  ? 68  TYR B CG  1 
ATOM   1270 C CD1 . TYR B 1 69 ? 11.702  -21.359 -36.252 1.00 27.69  ? 68  TYR B CD1 1 
ATOM   1271 C CD2 . TYR B 1 69 ? 13.337  -20.317 -37.646 1.00 32.66  ? 68  TYR B CD2 1 
ATOM   1272 C CE1 . TYR B 1 69 ? 12.263  -22.607 -36.516 1.00 29.93  ? 68  TYR B CE1 1 
ATOM   1273 C CE2 . TYR B 1 69 ? 13.884  -21.555 -37.950 1.00 31.50  ? 68  TYR B CE2 1 
ATOM   1274 C CZ  . TYR B 1 69 ? 13.359  -22.697 -37.355 1.00 32.74  ? 68  TYR B CZ  1 
ATOM   1275 O OH  . TYR B 1 69 ? 13.894  -23.918 -37.656 1.00 32.36  ? 68  TYR B OH  1 
ATOM   1276 N N   . GLY B 1 70 ? 9.085   -16.516 -37.091 1.00 31.96  ? 69  GLY B N   1 
ATOM   1277 C CA  . GLY B 1 70 ? 8.794   -15.150 -36.682 1.00 36.65  ? 69  GLY B CA  1 
ATOM   1278 C C   . GLY B 1 70 ? 7.364   -14.945 -36.162 1.00 39.40  ? 69  GLY B C   1 
ATOM   1279 O O   . GLY B 1 70 ? 6.771   -13.887 -36.389 1.00 39.37  ? 69  GLY B O   1 
ATOM   1280 N N   . LYS B 1 71 ? 6.814   -15.925 -35.432 1.00 37.24  ? 70  LYS B N   1 
ATOM   1281 C CA  . LYS B 1 71 ? 5.453   -15.774 -34.940 1.00 39.51  ? 70  LYS B CA  1 
ATOM   1282 C C   . LYS B 1 71 ? 5.524   -15.321 -33.497 1.00 41.01  ? 70  LYS B C   1 
ATOM   1283 O O   . LYS B 1 71 ? 6.383   -15.792 -32.753 1.00 37.28  ? 70  LYS B O   1 
ATOM   1284 C CB  . LYS B 1 71 ? 4.680   -17.095 -34.806 1.00 41.29  ? 70  LYS B CB  1 
ATOM   1285 C CG  . LYS B 1 71 ? 3.784   -17.478 -35.976 1.00 57.35  ? 70  LYS B CG  1 
ATOM   1286 C CD  . LYS B 1 71 ? 4.543   -17.832 -37.248 1.00 56.75  ? 70  LYS B CD  1 
ATOM   1287 C CE  . LYS B 1 71 ? 3.623   -18.065 -38.411 1.00 67.70  ? 70  LYS B CE  1 
ATOM   1288 N NZ  . LYS B 1 71 ? 4.280   -17.722 -39.678 1.00 70.13  ? 70  LYS B NZ  1 
ATOM   1289 N N   . PRO B 1 72 ? 4.593   -14.453 -33.044 1.00 38.75  ? 71  PRO B N   1 
ATOM   1290 C CA  . PRO B 1 72 ? 4.565   -14.076 -31.632 1.00 37.09  ? 71  PRO B CA  1 
ATOM   1291 C C   . PRO B 1 72 ? 4.411   -15.255 -30.676 1.00 34.89  ? 71  PRO B C   1 
ATOM   1292 O O   . PRO B 1 72 ? 3.854   -16.299 -31.029 1.00 36.92  ? 71  PRO B O   1 
ATOM   1293 C CB  . PRO B 1 72 ? 3.404   -13.090 -31.548 1.00 38.98  ? 71  PRO B CB  1 
ATOM   1294 C CG  . PRO B 1 72 ? 3.314   -12.544 -32.948 1.00 43.71  ? 71  PRO B CG  1 
ATOM   1295 C CD  . PRO B 1 72 ? 3.609   -13.730 -33.866 1.00 37.27  ? 71  PRO B CD  1 
ATOM   1296 N N   . ASN B 1 73 ? 4.935   -15.075 -29.455 1.00 37.10  ? 72  ASN B N   1 
ATOM   1297 C CA  . ASN B 1 73 ? 4.747   -16.063 -28.403 1.00 32.92  ? 72  ASN B CA  1 
ATOM   1298 C C   . ASN B 1 73 ? 4.684   -15.356 -27.043 1.00 37.15  ? 72  ASN B C   1 
ATOM   1299 O O   . ASN B 1 73 ? 4.730   -14.123 -26.966 1.00 42.38  ? 72  ASN B O   1 
ATOM   1300 C CB  . ASN B 1 73 ? 5.761   -17.202 -28.468 1.00 34.92  ? 72  ASN B CB  1 
ATOM   1301 C CG  . ASN B 1 73 ? 7.190   -16.772 -28.207 1.00 32.18  ? 72  ASN B CG  1 
ATOM   1302 O OD1 . ASN B 1 73 ? 7.467   -16.058 -27.227 1.00 31.52  ? 72  ASN B OD1 1 
ATOM   1303 N ND2 . ASN B 1 73 ? 8.101   -17.187 -29.097 1.00 28.51  ? 72  ASN B ND2 1 
ATOM   1304 N N   . LYS B 1 74 ? 4.647   -16.151 -25.973 1.00 38.52  ? 73  LYS B N   1 
ATOM   1305 C CA  . LYS B 1 74 ? 4.483   -15.595 -24.631 1.00 41.11  ? 73  LYS B CA  1 
ATOM   1306 C C   . LYS B 1 74 ? 5.814   -15.513 -23.856 1.00 41.19  ? 73  LYS B C   1 
ATOM   1307 O O   . LYS B 1 74 ? 5.813   -15.315 -22.633 1.00 39.58  ? 73  LYS B O   1 
ATOM   1308 C CB  . LYS B 1 74 ? 3.399   -16.412 -23.901 1.00 38.79  ? 73  LYS B CB  1 
ATOM   1309 N N   . ARG B 1 75 ? 6.961   -15.682 -24.535 1.00 31.69  ? 74  ARG B N   1 
ATOM   1310 C CA  . ARG B 1 75 ? 8.255   -15.560 -23.872 1.00 29.57  ? 74  ARG B CA  1 
ATOM   1311 C C   . ARG B 1 75 ? 8.617   -14.076 -23.704 1.00 31.32  ? 74  ARG B C   1 
ATOM   1312 O O   . ARG B 1 75 ? 8.444   -13.244 -24.590 1.00 30.79  ? 74  ARG B O   1 
ATOM   1313 C CB  . ARG B 1 75 ? 9.377   -16.348 -24.571 1.00 31.24  ? 74  ARG B CB  1 
ATOM   1314 C CG  . ARG B 1 75 ? 9.277   -17.863 -24.734 1.00 28.44  ? 74  ARG B CG  1 
ATOM   1315 C CD  . ARG B 1 75 ? 9.112   -18.664 -23.448 1.00 34.72  ? 74  ARG B CD  1 
ATOM   1316 N NE  . ARG B 1 75 ? 9.365   -20.088 -23.731 1.00 28.90  ? 74  ARG B NE  1 
ATOM   1317 C CZ  . ARG B 1 75 ? 10.490  -20.718 -23.493 1.00 32.09  ? 74  ARG B CZ  1 
ATOM   1318 N NH1 . ARG B 1 75 ? 11.497  -20.076 -22.924 1.00 36.75  ? 74  ARG B NH1 1 
ATOM   1319 N NH2 . ARG B 1 75 ? 10.626  -21.984 -23.869 1.00 36.05  ? 74  ARG B NH2 1 
ATOM   1320 N N   . LYS B 1 76 ? 9.105   -13.713 -22.513 1.00 29.26  ? 75  LYS B N   1 
ATOM   1321 C CA  . LYS B 1 76 ? 9.486   -12.337 -22.239 1.00 26.41  ? 75  LYS B CA  1 
ATOM   1322 C C   . LYS B 1 76 ? 10.567  -11.833 -23.208 1.00 25.42  ? 75  LYS B C   1 
ATOM   1323 O O   . LYS B 1 76 ? 11.639  -12.460 -23.299 1.00 26.50  ? 75  LYS B O   1 
ATOM   1324 C CB  . LYS B 1 76 ? 10.021  -12.280 -20.797 1.00 29.81  ? 75  LYS B CB  1 
ATOM   1325 C CG  . LYS B 1 76 ? 10.386  -10.852 -20.416 1.00 29.49  ? 75  LYS B CG  1 
ATOM   1326 C CD  . LYS B 1 76 ? 10.848  -10.735 -18.972 1.00 33.22  ? 75  LYS B CD  1 
ATOM   1327 C CE  . LYS B 1 76 ? 11.120  -9.297  -18.631 1.00 39.61  ? 75  LYS B CE  1 
ATOM   1328 N NZ  . LYS B 1 76 ? 11.607  -9.110  -17.255 1.00 44.99  ? 75  LYS B NZ  1 
ATOM   1329 N N   . GLY B 1 77 ? 10.251  -10.699 -23.853 1.00 25.50  ? 76  GLY B N   1 
ATOM   1330 C CA  . GLY B 1 77 ? 11.158  -10.010 -24.791 1.00 24.25  ? 76  GLY B CA  1 
ATOM   1331 C C   . GLY B 1 77 ? 10.963  -10.454 -26.242 1.00 28.93  ? 76  GLY B C   1 
ATOM   1332 O O   . GLY B 1 77 ? 11.478  -9.815  -27.154 1.00 27.34  ? 76  GLY B O   1 
ATOM   1333 N N   . PHE B 1 78 ? 10.255  -11.562 -26.479 1.00 25.41  ? 77  PHE B N   1 
ATOM   1334 C CA  . PHE B 1 78 ? 10.130  -12.081 -27.849 1.00 25.21  ? 77  PHE B CA  1 
ATOM   1335 C C   . PHE B 1 78 ? 9.403   -11.108 -28.785 1.00 28.37  ? 77  PHE B C   1 
ATOM   1336 O O   . PHE B 1 78 ? 9.861   -10.819 -29.896 1.00 26.52  ? 77  PHE B O   1 
ATOM   1337 C CB  . PHE B 1 78 ? 9.418   -13.440 -27.865 1.00 25.54  ? 77  PHE B CB  1 
ATOM   1338 C CG  . PHE B 1 78 ? 9.659   -14.152 -29.180 1.00 25.22  ? 77  PHE B CG  1 
ATOM   1339 C CD1 . PHE B 1 78 ? 10.738  -15.018 -29.301 1.00 24.43  ? 77  PHE B CD1 1 
ATOM   1340 C CD2 . PHE B 1 78 ? 8.748   -14.023 -30.229 1.00 27.40  ? 77  PHE B CD2 1 
ATOM   1341 C CE1 . PHE B 1 78 ? 10.969  -15.675 -30.516 1.00 22.60  ? 77  PHE B CE1 1 
ATOM   1342 C CE2 . PHE B 1 78 ? 8.984   -14.687 -31.434 1.00 27.58  ? 77  PHE B CE2 1 
ATOM   1343 C CZ  . PHE B 1 78 ? 10.084  -15.529 -31.541 1.00 25.24  ? 77  PHE B CZ  1 
ATOM   1344 N N   . ASN B 1 79 ? 8.228   -10.625 -28.419 1.00 27.30  ? 78  ASN B N   1 
ATOM   1345 C CA  . ASN B 1 79 ? 7.463   -9.783  -29.333 1.00 28.79  ? 78  ASN B CA  1 
ATOM   1346 C C   . ASN B 1 79 ? 8.164   -8.427  -29.508 1.00 28.84  ? 78  ASN B C   1 
ATOM   1347 O O   . ASN B 1 79 ? 8.163   -7.882  -30.616 1.00 29.02  ? 78  ASN B O   1 
ATOM   1348 C CB  . ASN B 1 79 ? 5.980   -9.703  -28.964 1.00 33.45  ? 78  ASN B CB  1 
ATOM   1349 C CG  . ASN B 1 79 ? 5.262   -11.039 -28.949 1.00 36.55  ? 78  ASN B CG  1 
ATOM   1350 O OD1 . ASN B 1 79 ? 5.751   -12.034 -29.490 1.00 34.25  ? 78  ASN B OD1 1 
ATOM   1351 N ND2 . ASN B 1 79 ? 4.098   -11.112 -28.312 1.00 39.12  ? 78  ASN B ND2 1 
ATOM   1352 N N   . GLU B 1 80 ? 8.858   -7.956  -28.471 1.00 28.91  ? 79  GLU B N   1 
ATOM   1353 C CA  . GLU B 1 80 ? 9.611   -6.720  -28.625 1.00 29.88  ? 79  GLU B CA  1 
ATOM   1354 C C   . GLU B 1 80 ? 10.730  -6.973  -29.639 1.00 28.67  ? 79  GLU B C   1 
ATOM   1355 O O   . GLU B 1 80 ? 11.038  -6.080  -30.453 1.00 27.49  ? 79  GLU B O   1 
ATOM   1356 C CB  . GLU B 1 80 ? 10.263  -6.256  -27.332 1.00 28.91  ? 79  GLU B CB  1 
ATOM   1357 C CG  . GLU B 1 80 ? 9.247   -5.614  -26.392 1.00 39.70  ? 79  GLU B CG  1 
ATOM   1358 N N   . GLY B 1 81 ? 11.309  -8.188  -29.559 1.00 26.60  ? 80  GLY B N   1 
ATOM   1359 C CA  . GLY B 1 81 ? 12.400  -8.613  -30.440 1.00 30.39  ? 80  GLY B CA  1 
ATOM   1360 C C   . GLY B 1 81 ? 11.948  -8.674  -31.900 1.00 27.13  ? 80  GLY B C   1 
ATOM   1361 O O   . GLY B 1 81 ? 12.710  -8.290  -32.812 1.00 24.95  ? 80  GLY B O   1 
ATOM   1362 N N   . LEU B 1 82 ? 10.726  -9.147  -32.118 1.00 25.64  ? 81  LEU B N   1 
ATOM   1363 C CA  . LEU B 1 82 ? 10.138  -9.173  -33.449 1.00 27.34  ? 81  LEU B CA  1 
ATOM   1364 C C   . LEU B 1 82 ? 10.029  -7.737  -33.949 1.00 27.24  ? 81  LEU B C   1 
ATOM   1365 O O   . LEU B 1 82 ? 10.322  -7.477  -35.115 1.00 27.97  ? 81  LEU B O   1 
ATOM   1366 C CB  . LEU B 1 82 ? 8.790   -9.901  -33.504 1.00 29.11  ? 81  LEU B CB  1 
ATOM   1367 C CG  . LEU B 1 82 ? 8.853   -11.424 -33.318 1.00 27.95  ? 81  LEU B CG  1 
ATOM   1368 C CD1 . LEU B 1 82 ? 7.427   -12.012 -33.296 1.00 28.42  ? 81  LEU B CD1 1 
ATOM   1369 C CD2 . LEU B 1 82 ? 9.796   -12.174 -34.302 1.00 26.51  ? 81  LEU B CD2 1 
ATOM   1370 N N   . TRP B 1 83 ? 9.610   -6.829  -33.065 1.00 27.65  ? 82  TRP B N   1 
ATOM   1371 C CA  . TRP B 1 83 ? 9.477   -5.425  -33.421 1.00 29.92  ? 82  TRP B CA  1 
ATOM   1372 C C   . TRP B 1 83 ? 10.821  -4.846  -33.860 1.00 29.58  ? 82  TRP B C   1 
ATOM   1373 O O   . TRP B 1 83 ? 10.880  -4.198  -34.909 1.00 28.97  ? 82  TRP B O   1 
ATOM   1374 C CB  . TRP B 1 83 ? 8.859   -4.579  -32.293 1.00 30.15  ? 82  TRP B CB  1 
ATOM   1375 C CG  . TRP B 1 83 ? 8.566   -3.177  -32.787 1.00 30.32  ? 82  TRP B CG  1 
ATOM   1376 C CD1 . TRP B 1 83 ? 7.416   -2.748  -33.383 1.00 38.07  ? 82  TRP B CD1 1 
ATOM   1377 C CD2 . TRP B 1 83 ? 9.484   -2.066  -32.832 1.00 34.76  ? 82  TRP B CD2 1 
ATOM   1378 N NE1 . TRP B 1 83 ? 7.545   -1.438  -33.776 1.00 37.78  ? 82  TRP B NE1 1 
ATOM   1379 C CE2 . TRP B 1 83 ? 8.800   -0.994  -33.448 1.00 34.78  ? 82  TRP B CE2 1 
ATOM   1380 C CE3 . TRP B 1 83 ? 10.805  -1.864  -32.393 1.00 30.98  ? 82  TRP B CE3 1 
ATOM   1381 C CZ2 . TRP B 1 83 ? 9.401   0.259   -33.630 1.00 32.66  ? 82  TRP B CZ2 1 
ATOM   1382 C CZ3 . TRP B 1 83 ? 11.386  -0.621  -32.551 1.00 35.83  ? 82  TRP B CZ3 1 
ATOM   1383 C CH2 . TRP B 1 83 ? 10.692  0.415   -33.180 1.00 31.75  ? 82  TRP B CH2 1 
ATOM   1384 N N   . GLU B 1 84 ? 11.882  -5.128  -33.085 1.00 25.12  ? 83  GLU B N   1 
ATOM   1385 C CA  . GLU B 1 84 ? 13.188  -4.547  -33.320 1.00 26.48  ? 83  GLU B CA  1 
ATOM   1386 C C   . GLU B 1 84 ? 13.802  -5.068  -34.628 1.00 26.19  ? 83  GLU B C   1 
ATOM   1387 O O   . GLU B 1 84 ? 14.398  -4.302  -35.391 1.00 26.97  ? 83  GLU B O   1 
ATOM   1388 C CB  . GLU B 1 84 ? 14.126  -4.777  -32.144 1.00 25.30  ? 83  GLU B CB  1 
ATOM   1389 C CG  . GLU B 1 84 ? 13.642  -4.113  -30.848 1.00 27.28  ? 83  GLU B CG  1 
ATOM   1390 C CD  . GLU B 1 84 ? 14.551  -4.428  -29.689 1.00 30.16  ? 83  GLU B CD  1 
ATOM   1391 O OE1 . GLU B 1 84 ? 15.469  -5.294  -29.808 1.00 28.19  ? 83  GLU B OE1 1 
ATOM   1392 O OE2 . GLU B 1 84 ? 14.368  -3.794  -28.596 1.00 31.28  ? 83  GLU B OE2 1 
ATOM   1393 N N   . ILE B 1 85 ? 13.657  -6.365  -34.901 1.00 24.96  ? 84  ILE B N   1 
ATOM   1394 C CA  . ILE B 1 85 ? 14.385  -6.920  -36.060 1.00 24.06  ? 84  ILE B CA  1 
ATOM   1395 C C   . ILE B 1 85 ? 13.741  -6.383  -37.350 1.00 25.47  ? 84  ILE B C   1 
ATOM   1396 O O   . ILE B 1 85 ? 14.421  -6.160  -38.368 1.00 25.54  ? 84  ILE B O   1 
ATOM   1397 C CB  . ILE B 1 85 ? 14.443  -8.462  -36.025 1.00 23.56  ? 84  ILE B CB  1 
ATOM   1398 C CG1 . ILE B 1 85 ? 15.473  -8.996  -37.074 1.00 24.00  ? 84  ILE B CG1 1 
ATOM   1399 C CG2 . ILE B 1 85 ? 13.071  -9.079  -36.252 1.00 24.04  ? 84  ILE B CG2 1 
ATOM   1400 C CD1 . ILE B 1 85 ? 15.996  -10.403 -36.707 1.00 24.09  ? 84  ILE B CD1 1 
ATOM   1401 N N   . GLN B 1 86 ? 12.449  -6.086  -37.255 1.00 25.37  ? 85  GLN B N   1 
ATOM   1402 C CA  . GLN B 1 86 ? 11.614  -5.554  -38.325 1.00 28.43  ? 85  GLN B CA  1 
ATOM   1403 C C   . GLN B 1 86 ? 11.897  -4.068  -38.540 1.00 32.82  ? 85  GLN B C   1 
ATOM   1404 O O   . GLN B 1 86 ? 11.987  -3.604  -39.680 1.00 32.13  ? 85  GLN B O   1 
ATOM   1405 C CB  . GLN B 1 86 ? 10.137  -5.840  -38.004 1.00 35.49  ? 85  GLN B CB  1 
ATOM   1406 C CG  . GLN B 1 86 ? 9.634   -7.222  -38.444 1.00 47.96  ? 85  GLN B CG  1 
ATOM   1407 C CD  . GLN B 1 86 ? 8.520   -7.864  -37.620 1.00 52.96  ? 85  GLN B CD  1 
ATOM   1408 O OE1 . GLN B 1 86 ? 7.399   -7.345  -37.455 1.00 54.78  ? 85  GLN B OE1 1 
ATOM   1409 N NE2 . GLN B 1 86 ? 8.818   -9.059  -37.120 1.00 44.50  ? 85  GLN B NE2 1 
ATOM   1410 N N   . ASN B 1 87 ? 11.981  -3.312  -37.444 1.00 26.54  ? 86  ASN B N   1 
ATOM   1411 C CA  . ASN B 1 87 ? 11.828  -1.863  -37.603 1.00 27.12  ? 86  ASN B CA  1 
ATOM   1412 C C   . ASN B 1 87 ? 13.113  -1.096  -37.390 1.00 29.37  ? 86  ASN B C   1 
ATOM   1413 O O   . ASN B 1 87 ? 13.217  0.049   -37.866 1.00 29.92  ? 86  ASN B O   1 
ATOM   1414 C CB  . ASN B 1 87 ? 10.850  -1.292  -36.575 1.00 33.13  ? 86  ASN B CB  1 
ATOM   1415 C CG  . ASN B 1 87 ? 9.461   -1.724  -36.962 1.00 37.26  ? 86  ASN B CG  1 
ATOM   1416 O OD1 . ASN B 1 87 ? 8.892   -1.181  -37.913 1.00 46.57  ? 86  ASN B OD1 1 
ATOM   1417 N ND2 . ASN B 1 87 ? 8.958   -2.780  -36.352 1.00 38.79  ? 86  ASN B ND2 1 
ATOM   1418 N N   . ASN B 1 88 ? 14.065  -1.644  -36.638 1.00 27.57  ? 87  ASN B N   1 
ATOM   1419 C CA  . ASN B 1 88 ? 15.341  -0.962  -36.407 1.00 28.19  ? 87  ASN B CA  1 
ATOM   1420 C C   . ASN B 1 88 ? 16.409  -1.965  -35.981 1.00 27.29  ? 87  ASN B C   1 
ATOM   1421 O O   . ASN B 1 88 ? 17.008  -1.902  -34.895 1.00 25.59  ? 87  ASN B O   1 
ATOM   1422 C CB  . ASN B 1 88 ? 15.206  0.205   -35.428 1.00 34.04  ? 87  ASN B CB  1 
ATOM   1423 C CG  . ASN B 1 88 ? 16.286  1.252   -35.597 1.00 33.18  ? 87  ASN B CG  1 
ATOM   1424 O OD1 . ASN B 1 88 ? 17.298  1.060   -36.288 1.00 29.93  ? 87  ASN B OD1 1 
ATOM   1425 N ND2 . ASN B 1 88 ? 16.084  2.384   -34.944 1.00 34.99  ? 87  ASN B ND2 1 
ATOM   1426 N N   . PRO B 1 89 ? 16.709  -2.929  -36.892 1.00 26.65  ? 88  PRO B N   1 
ATOM   1427 C CA  . PRO B 1 89 ? 17.645  -4.014  -36.562 1.00 24.36  ? 88  PRO B CA  1 
ATOM   1428 C C   . PRO B 1 89 ? 19.076  -3.587  -36.295 1.00 23.31  ? 88  PRO B C   1 
ATOM   1429 O O   . PRO B 1 89 ? 19.861  -4.325  -35.703 1.00 24.45  ? 88  PRO B O   1 
ATOM   1430 C CB  . PRO B 1 89 ? 17.581  -4.935  -37.810 1.00 23.91  ? 88  PRO B CB  1 
ATOM   1431 C CG  . PRO B 1 89 ? 17.094  -4.019  -38.956 1.00 21.59  ? 88  PRO B CG  1 
ATOM   1432 C CD  . PRO B 1 89 ? 16.156  -3.025  -38.261 1.00 25.53  ? 88  PRO B CD  1 
ATOM   1433 N N   . HIS B 1 90 ? 19.454  -2.384  -36.826 1.00 23.75  ? 89  HIS B N   1 
ATOM   1434 C CA  . HIS B 1 90 ? 20.847  -1.958  -36.750 1.00 24.37  ? 89  HIS B CA  1 
ATOM   1435 C C   . HIS B 1 90 ? 21.107  -0.867  -35.699 1.00 26.81  ? 89  HIS B C   1 
ATOM   1436 O O   . HIS B 1 90 ? 22.255  -0.424  -35.575 1.00 27.09  ? 89  HIS B O   1 
ATOM   1437 C CB  . HIS B 1 90 ? 21.367  -1.525  -38.130 1.00 23.67  ? 89  HIS B CB  1 
ATOM   1438 C CG  . HIS B 1 90 ? 21.213  -2.614  -39.143 1.00 26.96  ? 89  HIS B CG  1 
ATOM   1439 N ND1 . HIS B 1 90 ? 21.797  -3.847  -38.987 1.00 25.86  ? 89  HIS B ND1 1 
ATOM   1440 C CD2 . HIS B 1 90 ? 20.584  -2.652  -40.318 1.00 25.55  ? 89  HIS B CD2 1 
ATOM   1441 C CE1 . HIS B 1 90 ? 21.507  -4.593  -40.032 1.00 24.76  ? 89  HIS B CE1 1 
ATOM   1442 N NE2 . HIS B 1 90 ? 20.746  -3.902  -40.828 1.00 25.27  ? 89  HIS B NE2 1 
ATOM   1443 N N   . ALA B 1 91 ? 20.101  -0.613  -34.849 1.00 26.08  ? 90  ALA B N   1 
ATOM   1444 C CA  . ALA B 1 91 ? 20.269  0.401   -33.811 1.00 28.02  ? 90  ALA B CA  1 
ATOM   1445 C C   . ALA B 1 91 ? 21.254  -0.004  -32.708 1.00 32.09  ? 90  ALA B C   1 
ATOM   1446 O O   . ALA B 1 91 ? 21.555  -1.169  -32.457 1.00 28.67  ? 90  ALA B O   1 
ATOM   1447 C CB  . ALA B 1 91 ? 18.917  0.791   -33.258 1.00 28.55  ? 90  ALA B CB  1 
ATOM   1448 N N   . SER B 1 92 ? 21.754  1.016   -31.983 1.00 31.69  ? 91  SER B N   1 
ATOM   1449 C CA  . SER B 1 92 ? 22.393  0.825   -30.706 1.00 35.90  ? 91  SER B CA  1 
ATOM   1450 C C   . SER B 1 92 ? 21.304  0.607   -29.660 1.00 38.80  ? 91  SER B C   1 
ATOM   1451 O O   . SER B 1 92 ? 20.403  1.445   -29.509 1.00 39.16  ? 91  SER B O   1 
ATOM   1452 C CB  . SER B 1 92 ? 23.187  2.099   -30.361 1.00 38.55  ? 91  SER B CB  1 
ATOM   1453 O OG  . SER B 1 92 ? 23.570  2.051   -29.001 1.00 46.14  ? 91  SER B OG  1 
ATOM   1454 N N   . TYR B 1 93 ? 21.435  -0.511  -28.940 1.00 35.97  ? 92  TYR B N   1 
ATOM   1455 C CA  . TYR B 1 93 ? 20.571  -0.917  -27.850 1.00 39.34  ? 92  TYR B CA  1 
ATOM   1456 C C   . TYR B 1 93 ? 21.376  -0.845  -26.555 1.00 50.55  ? 92  TYR B C   1 
ATOM   1457 O O   . TYR B 1 93 ? 21.028  -1.486  -25.567 1.00 51.16  ? 92  TYR B O   1 
ATOM   1458 C CB  . TYR B 1 93 ? 19.972  -2.302  -28.142 1.00 34.34  ? 92  TYR B CB  1 
ATOM   1459 C CG  . TYR B 1 93 ? 18.960  -2.233  -29.279 1.00 28.28  ? 92  TYR B CG  1 
ATOM   1460 C CD1 . TYR B 1 93 ? 17.664  -1.799  -29.032 1.00 32.15  ? 92  TYR B CD1 1 
ATOM   1461 C CD2 . TYR B 1 93 ? 19.262  -2.613  -30.600 1.00 29.95  ? 92  TYR B CD2 1 
ATOM   1462 C CE1 . TYR B 1 93 ? 16.717  -1.670  -30.032 1.00 31.00  ? 92  TYR B CE1 1 
ATOM   1463 C CE2 . TYR B 1 93 ? 18.323  -2.452  -31.615 1.00 26.84  ? 92  TYR B CE2 1 
ATOM   1464 C CZ  . TYR B 1 93 ? 17.037  -2.023  -31.331 1.00 30.58  ? 92  TYR B CZ  1 
ATOM   1465 O OH  . TYR B 1 93 ? 16.047  -1.900  -32.280 1.00 30.35  ? 92  TYR B OH  1 
ATOM   1466 N N   . SER B 1 94 ? 22.429  -0.014  -26.588 1.00 63.99  ? 93  SER B N   1 
ATOM   1467 C CA  . SER B 1 94 ? 23.355  0.211   -25.486 1.00 71.20  ? 93  SER B CA  1 
ATOM   1468 C C   . SER B 1 94 ? 22.621  0.824   -24.283 1.00 77.13  ? 93  SER B C   1 
ATOM   1469 O O   . SER B 1 94 ? 21.559  1.453   -24.511 1.00 75.49  ? 93  SER B O   1 
ATOM   1470 C CB  . SER B 1 94 ? 24.500  1.103   -25.920 1.00 68.60  ? 93  SER B CB  1 
ATOM   1471 O OG  . SER B 1 94 ? 25.423  0.399   -26.738 1.00 71.00  ? 93  SER B OG  1 
ATOM   1472 O OXT . SER B 1 94 ? 23.146  0.665   -23.152 1.00 82.95  ? 93  SER B OXT 1 
ATOM   1473 N N   . HIS C 1 4  ? 32.752  -24.354 26.924  1.00 68.67  ? 3   HIS C N   1 
ATOM   1474 C CA  . HIS C 1 4  ? 31.808  -23.238 27.209  1.00 76.24  ? 3   HIS C CA  1 
ATOM   1475 C C   . HIS C 1 4  ? 31.109  -23.488 28.551  1.00 86.50  ? 3   HIS C C   1 
ATOM   1476 O O   . HIS C 1 4  ? 31.731  -23.973 29.499  1.00 84.34  ? 3   HIS C O   1 
ATOM   1477 C CB  . HIS C 1 4  ? 30.896  -22.992 25.997  1.00 76.52  ? 3   HIS C CB  1 
ATOM   1478 N N   . ALA C 1 5  ? 29.811  -23.158 28.610  1.00 84.63  ? 4   ALA C N   1 
ATOM   1479 C CA  . ALA C 1 5  ? 29.026  -23.131 29.835  1.00 77.65  ? 4   ALA C CA  1 
ATOM   1480 C C   . ALA C 1 5  ? 27.542  -23.093 29.479  1.00 77.29  ? 4   ALA C C   1 
ATOM   1481 O O   . ALA C 1 5  ? 27.110  -22.226 28.719  1.00 76.65  ? 4   ALA C O   1 
ATOM   1482 C CB  . ALA C 1 5  ? 29.384  -21.890 30.608  1.00 80.44  ? 4   ALA C CB  1 
ATOM   1483 N N   . PHE C 1 6  ? 26.768  -24.016 30.060  1.00 60.47  ? 5   PHE C N   1 
ATOM   1484 C CA  . PHE C 1 6  ? 25.375  -24.171 29.696  1.00 52.31  ? 5   PHE C CA  1 
ATOM   1485 C C   . PHE C 1 6  ? 24.536  -24.271 30.966  1.00 54.87  ? 5   PHE C C   1 
ATOM   1486 O O   . PHE C 1 6  ? 24.885  -25.017 31.873  1.00 67.93  ? 5   PHE C O   1 
ATOM   1487 C CB  . PHE C 1 6  ? 25.279  -25.407 28.779  1.00 46.87  ? 5   PHE C CB  1 
ATOM   1488 C CG  . PHE C 1 6  ? 26.098  -25.366 27.490  1.00 43.14  ? 5   PHE C CG  1 
ATOM   1489 C CD1 . PHE C 1 6  ? 27.245  -26.136 27.332  1.00 42.74  ? 5   PHE C CD1 1 
ATOM   1490 C CD2 . PHE C 1 6  ? 25.729  -24.547 26.422  1.00 48.42  ? 5   PHE C CD2 1 
ATOM   1491 C CE1 . PHE C 1 6  ? 27.989  -26.101 26.157  1.00 47.13  ? 5   PHE C CE1 1 
ATOM   1492 C CE2 . PHE C 1 6  ? 26.465  -24.535 25.243  1.00 41.89  ? 5   PHE C CE2 1 
ATOM   1493 C CZ  . PHE C 1 6  ? 27.599  -25.294 25.108  1.00 39.31  ? 5   PHE C CZ  1 
ATOM   1494 N N   . LYS C 1 7  ? 23.431  -23.523 31.029  1.00 52.84  ? 6   LYS C N   1 
ATOM   1495 C CA  . LYS C 1 7  ? 22.475  -23.641 32.122  1.00 52.43  ? 6   LYS C CA  1 
ATOM   1496 C C   . LYS C 1 7  ? 21.127  -23.962 31.495  1.00 47.69  ? 6   LYS C C   1 
ATOM   1497 O O   . LYS C 1 7  ? 20.988  -23.822 30.280  1.00 53.57  ? 6   LYS C O   1 
ATOM   1498 C CB  . LYS C 1 7  ? 22.463  -22.392 33.020  1.00 51.80  ? 6   LYS C CB  1 
ATOM   1499 N N   . PRO C 1 8  ? 20.119  -24.442 32.264  1.00 50.25  ? 7   PRO C N   1 
ATOM   1500 C CA  . PRO C 1 8  ? 18.788  -24.697 31.710  1.00 54.20  ? 7   PRO C CA  1 
ATOM   1501 C C   . PRO C 1 8  ? 18.284  -23.512 30.886  1.00 61.11  ? 7   PRO C C   1 
ATOM   1502 O O   . PRO C 1 8  ? 18.391  -22.360 31.307  1.00 68.36  ? 7   PRO C O   1 
ATOM   1503 C CB  . PRO C 1 8  ? 17.961  -24.954 32.981  1.00 58.89  ? 7   PRO C CB  1 
ATOM   1504 C CG  . PRO C 1 8  ? 18.958  -25.631 33.898  1.00 51.66  ? 7   PRO C CG  1 
ATOM   1505 C CD  . PRO C 1 8  ? 20.225  -24.808 33.691  1.00 46.98  ? 7   PRO C CD  1 
ATOM   1506 N N   . GLY C 1 9  ? 17.779  -23.805 29.683  1.00 58.28  ? 8   GLY C N   1 
ATOM   1507 C CA  . GLY C 1 9  ? 17.166  -22.788 28.845  1.00 51.40  ? 8   GLY C CA  1 
ATOM   1508 C C   . GLY C 1 9  ? 18.057  -22.329 27.690  1.00 52.44  ? 8   GLY C C   1 
ATOM   1509 O O   . GLY C 1 9  ? 17.519  -21.843 26.697  1.00 54.15  ? 8   GLY C O   1 
ATOM   1510 N N   . ASP C 1 10 ? 19.389  -22.478 27.827  1.00 43.80  ? 9   ASP C N   1 
ATOM   1511 C CA  . ASP C 1 10 ? 20.374  -22.113 26.822  1.00 39.73  ? 9   ASP C CA  1 
ATOM   1512 C C   . ASP C 1 10 ? 20.125  -22.854 25.503  1.00 41.69  ? 9   ASP C C   1 
ATOM   1513 O O   . ASP C 1 10 ? 20.000  -24.076 25.483  1.00 37.54  ? 9   ASP C O   1 
ATOM   1514 C CB  . ASP C 1 10 ? 21.796  -22.388 27.285  1.00 45.87  ? 9   ASP C CB  1 
ATOM   1515 C CG  . ASP C 1 10 ? 22.372  -21.449 28.343  1.00 58.36  ? 9   ASP C CG  1 
ATOM   1516 O OD1 . ASP C 1 10 ? 21.691  -20.468 28.687  1.00 60.31  ? 9   ASP C OD1 1 
ATOM   1517 O OD2 . ASP C 1 10 ? 23.496  -21.717 28.828  1.00 60.25  ? 9   ASP C OD2 1 
ATOM   1518 N N   . LEU C 1 11 ? 20.103  -22.099 24.398  1.00 41.45  ? 10  LEU C N   1 
ATOM   1519 C CA  . LEU C 1 11 ? 19.808  -22.640 23.080  1.00 39.06  ? 10  LEU C CA  1 
ATOM   1520 C C   . LEU C 1 11 ? 21.084  -23.115 22.388  1.00 32.97  ? 10  LEU C C   1 
ATOM   1521 O O   . LEU C 1 11 ? 22.111  -22.437 22.344  1.00 37.28  ? 10  LEU C O   1 
ATOM   1522 C CB  . LEU C 1 11 ? 19.069  -21.551 22.293  1.00 34.95  ? 10  LEU C CB  1 
ATOM   1523 C CG  . LEU C 1 11 ? 17.788  -21.025 22.941  1.00 35.92  ? 10  LEU C CG  1 
ATOM   1524 C CD1 . LEU C 1 11 ? 17.189  -20.061 21.922  1.00 38.27  ? 10  LEU C CD1 1 
ATOM   1525 C CD2 . LEU C 1 11 ? 16.812  -22.153 23.286  1.00 34.30  ? 10  LEU C CD2 1 
ATOM   1526 N N   . VAL C 1 12 ? 21.006  -24.298 21.739  1.00 32.66  ? 11  VAL C N   1 
ATOM   1527 C CA  . VAL C 1 12 ? 22.198  -24.968 21.250  1.00 31.15  ? 11  VAL C CA  1 
ATOM   1528 C C   . VAL C 1 12 ? 21.850  -25.679 19.930  1.00 29.70  ? 11  VAL C C   1 
ATOM   1529 O O   . VAL C 1 12 ? 20.660  -25.837 19.660  1.00 29.47  ? 11  VAL C O   1 
ATOM   1530 C CB  . VAL C 1 12 ? 22.780  -26.009 22.236  1.00 33.33  ? 11  VAL C CB  1 
ATOM   1531 C CG1 . VAL C 1 12 ? 23.236  -25.358 23.549  1.00 36.30  ? 11  VAL C CG1 1 
ATOM   1532 C CG2 . VAL C 1 12 ? 21.806  -27.159 22.502  1.00 34.80  ? 11  VAL C CG2 1 
ATOM   1533 N N   . PHE C 1 13 ? 22.892  -26.058 19.185  1.00 29.71  ? 12  PHE C N   1 
ATOM   1534 C CA  . PHE C 1 13 ? 22.863  -27.224 18.294  1.00 28.46  ? 12  PHE C CA  1 
ATOM   1535 C C   . PHE C 1 13 ? 23.539  -28.414 18.982  1.00 29.47  ? 12  PHE C C   1 
ATOM   1536 O O   . PHE C 1 13 ? 24.663  -28.317 19.506  1.00 29.66  ? 12  PHE C O   1 
ATOM   1537 C CB  . PHE C 1 13 ? 23.535  -27.005 16.933  1.00 31.95  ? 12  PHE C CB  1 
ATOM   1538 C CG  . PHE C 1 13 ? 22.748  -26.023 16.092  1.00 34.31  ? 12  PHE C CG  1 
ATOM   1539 C CD1 . PHE C 1 13 ? 21.700  -26.460 15.275  1.00 31.92  ? 12  PHE C CD1 1 
ATOM   1540 C CD2 . PHE C 1 13 ? 23.060  -24.663 16.110  1.00 34.83  ? 12  PHE C CD2 1 
ATOM   1541 C CE1 . PHE C 1 13 ? 20.986  -25.561 14.501  1.00 33.75  ? 12  PHE C CE1 1 
ATOM   1542 C CE2 . PHE C 1 13 ? 22.317  -23.776 15.356  1.00 37.15  ? 12  PHE C CE2 1 
ATOM   1543 C CZ  . PHE C 1 13 ? 21.304  -24.231 14.535  1.00 36.15  ? 12  PHE C CZ  1 
ATOM   1544 N N   . ALA C 1 14 ? 22.880  -29.590 18.948  1.00 26.97  ? 13  ALA C N   1 
ATOM   1545 C CA  . ALA C 1 14 ? 23.342  -30.744 19.711  1.00 25.27  ? 13  ALA C CA  1 
ATOM   1546 C C   . ALA C 1 14 ? 23.604  -31.871 18.722  1.00 29.44  ? 13  ALA C C   1 
ATOM   1547 O O   . ALA C 1 14 ? 22.726  -32.128 17.885  1.00 27.19  ? 13  ALA C O   1 
ATOM   1548 C CB  . ALA C 1 14 ? 22.274  -31.153 20.705  1.00 24.08  ? 13  ALA C CB  1 
ATOM   1549 N N   . LYS C 1 15 ? 24.808  -32.464 18.805  1.00 26.70  ? 14  LYS C N   1 
ATOM   1550 C CA  . LYS C 1 15 ? 25.213  -33.490 17.851  1.00 28.81  ? 14  LYS C CA  1 
ATOM   1551 C C   . LYS C 1 15 ? 25.162  -34.865 18.507  1.00 26.83  ? 14  LYS C C   1 
ATOM   1552 O O   . LYS C 1 15 ? 25.880  -35.147 19.468  1.00 31.91  ? 14  LYS C O   1 
ATOM   1553 C CB  . LYS C 1 15 ? 26.625  -33.185 17.316  1.00 29.82  ? 14  LYS C CB  1 
ATOM   1554 C CG  . LYS C 1 15 ? 27.099  -34.187 16.239  1.00 29.53  ? 14  LYS C CG  1 
ATOM   1555 C CD  . LYS C 1 15 ? 26.248  -34.044 14.971  1.00 30.51  ? 14  LYS C CD  1 
ATOM   1556 C CE  . LYS C 1 15 ? 26.654  -34.857 13.745  1.00 31.38  ? 14  LYS C CE  1 
ATOM   1557 N NZ  . LYS C 1 15 ? 26.646  -36.293 14.019  1.00 31.23  ? 14  LYS C NZ  1 
ATOM   1558 N N   . MET C 1 16 ? 24.335  -35.768 17.958  1.00 24.61  ? 15  MET C N   1 
ATOM   1559 C CA  . MET C 1 16 ? 24.350  -37.187 18.315  1.00 26.47  ? 15  MET C CA  1 
ATOM   1560 C C   . MET C 1 16 ? 24.863  -37.973 17.115  1.00 31.62  ? 15  MET C C   1 
ATOM   1561 O O   . MET C 1 16 ? 24.650  -37.569 15.966  1.00 26.15  ? 15  MET C O   1 
ATOM   1562 C CB  . MET C 1 16 ? 22.919  -37.665 18.588  1.00 29.05  ? 15  MET C CB  1 
ATOM   1563 C CG  . MET C 1 16 ? 22.278  -36.954 19.762  1.00 33.45  ? 15  MET C CG  1 
ATOM   1564 S SD  . MET C 1 16 ? 20.691  -37.693 20.193  1.00 38.13  ? 15  MET C SD  1 
ATOM   1565 C CE  . MET C 1 16 ? 19.783  -37.116 18.745  1.00 38.01  ? 15  MET C CE  1 
ATOM   1566 N N   . LYS C 1 17 ? 25.494  -39.129 17.386  1.00 29.93  ? 16  LYS C N   1 
ATOM   1567 C CA  . LYS C 1 17 ? 25.869  -40.009 16.286  1.00 31.64  ? 16  LYS C CA  1 
ATOM   1568 C C   . LYS C 1 17 ? 24.604  -40.449 15.534  1.00 26.17  ? 16  LYS C C   1 
ATOM   1569 O O   . LYS C 1 17 ? 23.616  -40.896 16.126  1.00 30.67  ? 16  LYS C O   1 
ATOM   1570 C CB  . LYS C 1 17 ? 26.635  -41.194 16.893  1.00 31.03  ? 16  LYS C CB  1 
ATOM   1571 C CG  . LYS C 1 17 ? 27.151  -42.239 15.908  1.00 35.05  ? 16  LYS C CG  1 
ATOM   1572 C CD  . LYS C 1 17 ? 28.309  -41.506 15.244  1.00 36.13  ? 16  LYS C CD  1 
ATOM   1573 C CE  . LYS C 1 17 ? 29.192  -42.459 14.497  1.00 49.58  ? 16  LYS C CE  1 
ATOM   1574 N NZ  . LYS C 1 17 ? 30.361  -41.701 14.049  1.00 41.83  ? 16  LYS C NZ  1 
ATOM   1575 N N   . GLY C 1 18 ? 24.682  -40.327 14.214  1.00 32.06  ? 17  GLY C N   1 
ATOM   1576 C CA  . GLY C 1 18 ? 23.598  -40.808 13.369  1.00 32.69  ? 17  GLY C CA  1 
ATOM   1577 C C   . GLY C 1 18 ? 22.682  -39.673 12.912  1.00 30.05  ? 17  GLY C C   1 
ATOM   1578 O O   . GLY C 1 18 ? 21.697  -39.962 12.236  1.00 29.06  ? 17  GLY C O   1 
ATOM   1579 N N   . TYR C 1 19 ? 22.938  -38.432 13.374  1.00 28.28  ? 18  TYR C N   1 
ATOM   1580 C CA  . TYR C 1 19 ? 22.026  -37.297 13.137  1.00 28.23  ? 18  TYR C CA  1 
ATOM   1581 C C   . TYR C 1 19 ? 22.815  -36.025 12.890  1.00 28.11  ? 18  TYR C C   1 
ATOM   1582 O O   . TYR C 1 19 ? 23.910  -35.844 13.406  1.00 26.85  ? 18  TYR C O   1 
ATOM   1583 C CB  . TYR C 1 19 ? 21.168  -36.962 14.368  1.00 24.09  ? 18  TYR C CB  1 
ATOM   1584 C CG  . TYR C 1 19 ? 20.336  -38.160 14.757  1.00 27.35  ? 18  TYR C CG  1 
ATOM   1585 C CD1 . TYR C 1 19 ? 20.852  -39.167 15.563  1.00 27.71  ? 18  TYR C CD1 1 
ATOM   1586 C CD2 . TYR C 1 19 ? 19.027  -38.248 14.316  1.00 27.59  ? 18  TYR C CD2 1 
ATOM   1587 C CE1 . TYR C 1 19 ? 20.072  -40.249 15.930  1.00 29.34  ? 18  TYR C CE1 1 
ATOM   1588 C CE2 . TYR C 1 19 ? 18.239  -39.331 14.666  1.00 31.40  ? 18  TYR C CE2 1 
ATOM   1589 C CZ  . TYR C 1 19 ? 18.764  -40.318 15.480  1.00 31.07  ? 18  TYR C CZ  1 
ATOM   1590 O OH  . TYR C 1 19 ? 17.960  -41.385 15.786  1.00 42.11  ? 18  TYR C OH  1 
ATOM   1591 N N   . PRO C 1 20 ? 22.271  -35.090 12.090  1.00 28.30  ? 19  PRO C N   1 
ATOM   1592 C CA  . PRO C 1 20 ? 22.919  -33.800 11.844  1.00 26.89  ? 19  PRO C CA  1 
ATOM   1593 C C   . PRO C 1 20 ? 22.851  -32.979 13.132  1.00 27.84  ? 19  PRO C C   1 
ATOM   1594 O O   . PRO C 1 20 ? 22.064  -33.264 14.033  1.00 25.04  ? 19  PRO C O   1 
ATOM   1595 C CB  . PRO C 1 20 ? 22.044  -33.171 10.720  1.00 31.08  ? 19  PRO C CB  1 
ATOM   1596 C CG  . PRO C 1 20 ? 20.709  -33.800 10.934  1.00 26.11  ? 19  PRO C CG  1 
ATOM   1597 C CD  . PRO C 1 20 ? 20.959  -35.213 11.420  1.00 25.14  ? 19  PRO C CD  1 
ATOM   1598 N N   . HIS C 1 21 ? 23.685  -31.950 13.186  1.00 27.04  ? 20  HIS C N   1 
ATOM   1599 C CA  . HIS C 1 21 ? 23.628  -31.028 14.327  1.00 25.89  ? 20  HIS C CA  1 
ATOM   1600 C C   . HIS C 1 21 ? 22.214  -30.463 14.454  1.00 28.78  ? 20  HIS C C   1 
ATOM   1601 O O   . HIS C 1 21 ? 21.670  -29.929 13.497  1.00 27.13  ? 20  HIS C O   1 
ATOM   1602 C CB  . HIS C 1 21 ? 24.610  -29.876 14.118  1.00 30.84  ? 20  HIS C CB  1 
ATOM   1603 C CG  . HIS C 1 21 ? 26.046  -30.296 14.155  1.00 31.15  ? 20  HIS C CG  1 
ATOM   1604 N ND1 . HIS C 1 21 ? 26.720  -30.952 13.146  1.00 33.90  ? 20  HIS C ND1 1 
ATOM   1605 C CD2 . HIS C 1 21 ? 26.942  -30.117 15.151  1.00 35.64  ? 20  HIS C CD2 1 
ATOM   1606 C CE1 . HIS C 1 21 ? 27.968  -31.186 13.535  1.00 40.59  ? 20  HIS C CE1 1 
ATOM   1607 N NE2 . HIS C 1 21 ? 28.132  -30.668 14.746  1.00 35.60  ? 20  HIS C NE2 1 
ATOM   1608 N N   . TRP C 1 22 ? 21.614  -30.563 15.655  1.00 24.85  ? 21  TRP C N   1 
ATOM   1609 C CA  . TRP C 1 22 ? 20.163  -30.476 15.763  1.00 24.23  ? 21  TRP C CA  1 
ATOM   1610 C C   . TRP C 1 22 ? 19.773  -29.312 16.673  1.00 25.52  ? 21  TRP C C   1 
ATOM   1611 O O   . TRP C 1 22 ? 20.357  -29.155 17.758  1.00 25.57  ? 21  TRP C O   1 
ATOM   1612 C CB  . TRP C 1 22 ? 19.613  -31.797 16.347  1.00 25.39  ? 21  TRP C CB  1 
ATOM   1613 C CG  . TRP C 1 22 ? 18.159  -32.002 15.995  1.00 23.98  ? 21  TRP C CG  1 
ATOM   1614 C CD1 . TRP C 1 22 ? 17.058  -31.429 16.552  1.00 25.18  ? 21  TRP C CD1 1 
ATOM   1615 C CD2 . TRP C 1 22 ? 17.682  -32.868 14.933  1.00 24.90  ? 21  TRP C CD2 1 
ATOM   1616 N NE1 . TRP C 1 22 ? 15.921  -31.877 15.907  1.00 25.98  ? 21  TRP C NE1 1 
ATOM   1617 C CE2 . TRP C 1 22 ? 16.269  -32.750 14.914  1.00 27.55  ? 21  TRP C CE2 1 
ATOM   1618 C CE3 . TRP C 1 22 ? 18.322  -33.734 14.031  1.00 25.56  ? 21  TRP C CE3 1 
ATOM   1619 C CZ2 . TRP C 1 22 ? 15.493  -33.495 14.008  1.00 27.40  ? 21  TRP C CZ2 1 
ATOM   1620 C CZ3 . TRP C 1 22 ? 17.564  -34.409 13.085  1.00 25.79  ? 21  TRP C CZ3 1 
ATOM   1621 C CH2 . TRP C 1 22 ? 16.168  -34.306 13.118  1.00 26.80  ? 21  TRP C CH2 1 
ATOM   1622 N N   . PRO C 1 23 ? 18.772  -28.475 16.308  1.00 28.92  ? 22  PRO C N   1 
ATOM   1623 C CA  . PRO C 1 23 ? 18.353  -27.380 17.198  1.00 26.01  ? 22  PRO C CA  1 
ATOM   1624 C C   . PRO C 1 23 ? 17.798  -27.934 18.508  1.00 24.76  ? 22  PRO C C   1 
ATOM   1625 O O   . PRO C 1 23 ? 16.953  -28.820 18.523  1.00 25.47  ? 22  PRO C O   1 
ATOM   1626 C CB  . PRO C 1 23 ? 17.310  -26.658 16.306  1.00 28.75  ? 22  PRO C CB  1 
ATOM   1627 C CG  . PRO C 1 23 ? 16.765  -27.731 15.394  1.00 25.47  ? 22  PRO C CG  1 
ATOM   1628 C CD  . PRO C 1 23 ? 18.031  -28.485 15.022  1.00 26.58  ? 22  PRO C CD  1 
ATOM   1629 N N   . ALA C 1 24 ? 18.311  -27.405 19.623  1.00 27.41  ? 23  ALA C N   1 
ATOM   1630 C CA  . ALA C 1 24 ? 18.016  -28.007 20.915  1.00 31.20  ? 23  ALA C CA  1 
ATOM   1631 C C   . ALA C 1 24 ? 18.135  -26.950 22.005  1.00 32.48  ? 23  ALA C C   1 
ATOM   1632 O O   . ALA C 1 24 ? 18.623  -25.852 21.752  1.00 32.23  ? 23  ALA C O   1 
ATOM   1633 C CB  . ALA C 1 24 ? 19.039  -29.112 21.163  1.00 29.80  ? 23  ALA C CB  1 
ATOM   1634 N N   . ARG C 1 25 ? 17.708  -27.302 23.227  1.00 31.98  ? 24  ARG C N   1 
ATOM   1635 C CA  . ARG C 1 25 ? 18.080  -26.504 24.389  1.00 33.74  ? 24  ARG C CA  1 
ATOM   1636 C C   . ARG C 1 25 ? 18.526  -27.400 25.552  1.00 31.88  ? 24  ARG C C   1 
ATOM   1637 O O   . ARG C 1 25 ? 18.191  -28.583 25.585  1.00 32.83  ? 24  ARG C O   1 
ATOM   1638 C CB  . ARG C 1 25 ? 16.875  -25.697 24.875  1.00 34.08  ? 24  ARG C CB  1 
ATOM   1639 C CG  . ARG C 1 25 ? 15.615  -26.454 25.251  1.00 37.90  ? 24  ARG C CG  1 
ATOM   1640 C CD  . ARG C 1 25 ? 14.612  -25.546 25.988  1.00 42.28  ? 24  ARG C CD  1 
ATOM   1641 N NE  . ARG C 1 25 ? 13.408  -26.350 26.254  1.00 51.98  ? 24  ARG C NE  1 
ATOM   1642 C CZ  . ARG C 1 25 ? 12.147  -26.119 25.910  1.00 54.22  ? 24  ARG C CZ  1 
ATOM   1643 N NH1 . ARG C 1 25 ? 11.802  -24.983 25.333  1.00 50.54  ? 24  ARG C NH1 1 
ATOM   1644 N NH2 . ARG C 1 25 ? 11.219  -27.030 26.169  1.00 57.59  ? 24  ARG C NH2 1 
ATOM   1645 N N   . ILE C 1 26 ? 19.295  -26.801 26.464  1.00 34.71  ? 25  ILE C N   1 
ATOM   1646 C CA  . ILE C 1 26 ? 19.662  -27.383 27.752  1.00 36.67  ? 25  ILE C CA  1 
ATOM   1647 C C   . ILE C 1 26 ? 18.458  -27.307 28.673  1.00 41.62  ? 25  ILE C C   1 
ATOM   1648 O O   . ILE C 1 26 ? 17.931  -26.219 28.888  1.00 43.65  ? 25  ILE C O   1 
ATOM   1649 C CB  . ILE C 1 26 ? 20.848  -26.629 28.389  1.00 37.85  ? 25  ILE C CB  1 
ATOM   1650 C CG1 . ILE C 1 26 ? 22.021  -26.382 27.456  1.00 40.04  ? 25  ILE C CG1 1 
ATOM   1651 C CG2 . ILE C 1 26 ? 21.292  -27.317 29.689  1.00 42.50  ? 25  ILE C CG2 1 
ATOM   1652 C CD1 . ILE C 1 26 ? 22.787  -27.612 27.007  1.00 42.54  ? 25  ILE C CD1 1 
ATOM   1653 N N   . ASP C 1 27 ? 18.058  -28.454 29.221  1.00 42.56  ? 26  ASP C N   1 
ATOM   1654 C CA  . ASP C 1 27 ? 16.987  -28.537 30.202  1.00 51.37  ? 26  ASP C CA  1 
ATOM   1655 C C   . ASP C 1 27 ? 17.559  -28.529 31.619  1.00 56.70  ? 26  ASP C C   1 
ATOM   1656 O O   . ASP C 1 27 ? 18.771  -28.667 31.799  1.00 54.18  ? 26  ASP C O   1 
ATOM   1657 C CB  . ASP C 1 27 ? 16.235  -29.847 30.057  1.00 50.16  ? 26  ASP C CB  1 
ATOM   1658 C CG  . ASP C 1 27 ? 14.958  -29.805 29.238  1.00 57.49  ? 26  ASP C CG  1 
ATOM   1659 O OD1 . ASP C 1 27 ? 14.718  -28.765 28.585  1.00 56.10  ? 26  ASP C OD1 1 
ATOM   1660 O OD2 . ASP C 1 27 ? 14.200  -30.806 29.315  1.00 60.20  ? 26  ASP C OD2 1 
ATOM   1661 N N   . ASP C 1 28 ? 16.666  -28.375 32.612  1.00 66.71  ? 27  ASP C N   1 
ATOM   1662 C CA  . ASP C 1 28 ? 17.000  -28.455 34.029  1.00 66.57  ? 27  ASP C CA  1 
ATOM   1663 C C   . ASP C 1 28 ? 16.921  -29.917 34.475  1.00 64.10  ? 27  ASP C C   1 
ATOM   1664 O O   . ASP C 1 28 ? 16.302  -30.677 33.711  1.00 55.86  ? 27  ASP C O   1 
ATOM   1665 C CB  . ASP C 1 28 ? 16.078  -27.603 34.887  1.00 66.22  ? 27  ASP C CB  1 
ATOM   1666 N N   . LYS C 1 35 ? 19.697  -38.940 37.768  1.00 51.79  ? 34  LYS C N   1 
ATOM   1667 C CA  . LYS C 1 35 ? 20.720  -37.898 37.496  1.00 56.49  ? 34  LYS C CA  1 
ATOM   1668 C C   . LYS C 1 35 ? 21.443  -38.241 36.191  1.00 53.32  ? 34  LYS C C   1 
ATOM   1669 O O   . LYS C 1 35 ? 21.458  -39.389 35.747  1.00 51.42  ? 34  LYS C O   1 
ATOM   1670 C CB  . LYS C 1 35 ? 21.658  -37.730 38.698  1.00 56.78  ? 34  LYS C CB  1 
ATOM   1671 N N   . PRO C 1 36 ? 22.025  -37.241 35.499  1.00 52.34  ? 35  PRO C N   1 
ATOM   1672 C CA  . PRO C 1 36 ? 22.757  -37.509 34.265  1.00 47.05  ? 35  PRO C CA  1 
ATOM   1673 C C   . PRO C 1 36 ? 23.906  -38.494 34.499  1.00 48.56  ? 35  PRO C C   1 
ATOM   1674 O O   . PRO C 1 36 ? 24.349  -38.735 35.638  1.00 41.43  ? 35  PRO C O   1 
ATOM   1675 C CB  . PRO C 1 36 ? 23.254  -36.110 33.823  1.00 52.66  ? 35  PRO C CB  1 
ATOM   1676 C CG  . PRO C 1 36 ? 22.339  -35.138 34.534  1.00 51.53  ? 35  PRO C CG  1 
ATOM   1677 C CD  . PRO C 1 36 ? 21.972  -35.809 35.853  1.00 52.61  ? 35  PRO C CD  1 
ATOM   1678 N N   . PRO C 1 37 ? 24.427  -39.121 33.429  1.00 45.38  ? 36  PRO C N   1 
ATOM   1679 C CA  . PRO C 1 37 ? 25.722  -39.777 33.531  1.00 43.74  ? 36  PRO C CA  1 
ATOM   1680 C C   . PRO C 1 37 ? 26.672  -38.627 33.855  1.00 41.02  ? 36  PRO C C   1 
ATOM   1681 O O   . PRO C 1 37 ? 26.364  -37.448 33.626  1.00 35.85  ? 36  PRO C O   1 
ATOM   1682 C CB  . PRO C 1 37 ? 25.931  -40.345 32.124  1.00 43.09  ? 36  PRO C CB  1 
ATOM   1683 C CG  . PRO C 1 37 ? 24.521  -40.488 31.613  1.00 42.42  ? 36  PRO C CG  1 
ATOM   1684 C CD  . PRO C 1 37 ? 23.837  -39.231 32.087  1.00 40.24  ? 36  PRO C CD  1 
ATOM   1685 N N   . PRO C 1 38 ? 27.863  -38.947 34.404  1.00 38.90  ? 37  PRO C N   1 
ATOM   1686 C CA  . PRO C 1 38 ? 28.855  -37.924 34.719  1.00 37.28  ? 37  PRO C CA  1 
ATOM   1687 C C   . PRO C 1 38 ? 29.131  -37.004 33.543  1.00 35.21  ? 37  PRO C C   1 
ATOM   1688 O O   . PRO C 1 38 ? 29.356  -37.477 32.427  1.00 38.61  ? 37  PRO C O   1 
ATOM   1689 C CB  . PRO C 1 38 ? 30.070  -38.804 35.071  1.00 38.17  ? 37  PRO C CB  1 
ATOM   1690 C CG  . PRO C 1 38 ? 29.416  -40.003 35.726  1.00 38.50  ? 37  PRO C CG  1 
ATOM   1691 C CD  . PRO C 1 38 ? 28.290  -40.314 34.758  1.00 41.30  ? 37  PRO C CD  1 
ATOM   1692 N N   . ASN C 1 39 ? 29.042  -35.693 33.822  1.00 34.61  ? 38  ASN C N   1 
ATOM   1693 C CA  . ASN C 1 39 ? 29.471  -34.634 32.934  1.00 33.60  ? 38  ASN C CA  1 
ATOM   1694 C C   . ASN C 1 39 ? 28.579  -34.578 31.699  1.00 35.47  ? 38  ASN C C   1 
ATOM   1695 O O   . ASN C 1 39 ? 29.030  -34.108 30.650  1.00 41.95  ? 38  ASN C O   1 
ATOM   1696 C CB  . ASN C 1 39 ? 30.929  -34.780 32.525  1.00 35.70  ? 38  ASN C CB  1 
ATOM   1697 C CG  . ASN C 1 39 ? 31.574  -33.539 31.945  1.00 41.34  ? 38  ASN C CG  1 
ATOM   1698 O OD1 . ASN C 1 39 ? 31.348  -32.423 32.423  1.00 54.33  ? 38  ASN C OD1 1 
ATOM   1699 N ND2 . ASN C 1 39 ? 32.420  -33.710 30.937  1.00 43.60  ? 38  ASN C ND2 1 
ATOM   1700 N N   . LYS C 1 40 ? 27.323  -35.026 31.846  1.00 32.13  ? 39  LYS C N   1 
ATOM   1701 C CA  . LYS C 1 40 ? 26.414  -34.901 30.723  1.00 30.01  ? 39  LYS C CA  1 
ATOM   1702 C C   . LYS C 1 40 ? 25.275  -33.950 31.058  1.00 29.56  ? 39  LYS C C   1 
ATOM   1703 O O   . LYS C 1 40 ? 24.811  -33.856 32.186  1.00 32.16  ? 39  LYS C O   1 
ATOM   1704 C CB  . LYS C 1 40 ? 25.743  -36.221 30.328  1.00 31.35  ? 39  LYS C CB  1 
ATOM   1705 C CG  . LYS C 1 40 ? 26.668  -37.342 29.988  1.00 37.18  ? 39  LYS C CG  1 
ATOM   1706 C CD  . LYS C 1 40 ? 27.558  -37.156 28.779  1.00 41.56  ? 39  LYS C CD  1 
ATOM   1707 C CE  . LYS C 1 40 ? 28.474  -38.341 28.529  1.00 38.64  ? 39  LYS C CE  1 
ATOM   1708 N NZ  . LYS C 1 40 ? 29.202  -38.158 27.269  1.00 47.10  ? 39  LYS C NZ  1 
ATOM   1709 N N   . TYR C 1 41 ? 24.792  -33.264 30.012  1.00 29.03  ? 40  TYR C N   1 
ATOM   1710 C CA  . TYR C 1 41 ? 23.692  -32.314 30.124  1.00 30.78  ? 40  TYR C CA  1 
ATOM   1711 C C   . TYR C 1 41 ? 22.413  -32.952 29.607  1.00 31.19  ? 40  TYR C C   1 
ATOM   1712 O O   . TYR C 1 41 ? 22.457  -33.701 28.633  1.00 29.61  ? 40  TYR C O   1 
ATOM   1713 C CB  . TYR C 1 41 ? 23.848  -31.072 29.234  1.00 27.54  ? 40  TYR C CB  1 
ATOM   1714 C CG  . TYR C 1 41 ? 24.993  -30.170 29.672  1.00 30.36  ? 40  TYR C CG  1 
ATOM   1715 C CD1 . TYR C 1 41 ? 26.286  -30.378 29.210  1.00 29.97  ? 40  TYR C CD1 1 
ATOM   1716 C CD2 . TYR C 1 41 ? 24.781  -29.123 30.567  1.00 36.33  ? 40  TYR C CD2 1 
ATOM   1717 C CE1 . TYR C 1 41 ? 27.351  -29.602 29.628  1.00 40.38  ? 40  TYR C CE1 1 
ATOM   1718 C CE2 . TYR C 1 41 ? 25.833  -28.315 30.963  1.00 35.58  ? 40  TYR C CE2 1 
ATOM   1719 C CZ  . TYR C 1 41 ? 27.114  -28.561 30.512  1.00 39.16  ? 40  TYR C CZ  1 
ATOM   1720 O OH  . TYR C 1 41 ? 28.164  -27.804 30.925  1.00 45.94  ? 40  TYR C OH  1 
ATOM   1721 N N   . PRO C 1 42 ? 21.250  -32.624 30.214  1.00 32.53  ? 41  PRO C N   1 
ATOM   1722 C CA  . PRO C 1 42 ? 19.945  -33.062 29.712  1.00 31.31  ? 41  PRO C CA  1 
ATOM   1723 C C   . PRO C 1 42 ? 19.603  -32.160 28.533  1.00 33.13  ? 41  PRO C C   1 
ATOM   1724 O O   . PRO C 1 42 ? 19.619  -30.935 28.680  1.00 33.60  ? 41  PRO C O   1 
ATOM   1725 C CB  . PRO C 1 42 ? 18.967  -32.844 30.885  1.00 33.60  ? 41  PRO C CB  1 
ATOM   1726 C CG  . PRO C 1 42 ? 19.680  -31.847 31.762  1.00 35.30  ? 41  PRO C CG  1 
ATOM   1727 C CD  . PRO C 1 42 ? 21.160  -31.749 31.402  1.00 38.18  ? 41  PRO C CD  1 
ATOM   1728 N N   . ILE C 1 43 ? 19.304  -32.799 27.389  1.00 28.88  ? 42  ILE C N   1 
ATOM   1729 C CA  . ILE C 1 43 ? 19.011  -32.008 26.198  1.00 28.89  ? 42  ILE C CA  1 
ATOM   1730 C C   . ILE C 1 43 ? 17.568  -32.243 25.785  1.00 28.69  ? 42  ILE C C   1 
ATOM   1731 O O   . ILE C 1 43 ? 17.055  -33.369 25.796  1.00 30.95  ? 42  ILE C O   1 
ATOM   1732 C CB  . ILE C 1 43 ? 19.999  -32.384 25.079  1.00 26.25  ? 42  ILE C CB  1 
ATOM   1733 C CG1 . ILE C 1 43 ? 21.478  -32.229 25.512  1.00 28.68  ? 42  ILE C CG1 1 
ATOM   1734 C CG2 . ILE C 1 43 ? 19.653  -31.630 23.776  1.00 28.84  ? 42  ILE C CG2 1 
ATOM   1735 C CD1 . ILE C 1 43 ? 21.938  -30.805 25.810  1.00 29.19  ? 42  ILE C CD1 1 
ATOM   1736 N N   . PHE C 1 44 ? 16.904  -31.170 25.312  1.00 31.60  ? 43  PHE C N   1 
ATOM   1737 C CA  . PHE C 1 44 ? 15.629  -31.352 24.636  1.00 28.32  ? 43  PHE C CA  1 
ATOM   1738 C C   . PHE C 1 44 ? 15.774  -30.876 23.187  1.00 26.18  ? 43  PHE C C   1 
ATOM   1739 O O   . PHE C 1 44 ? 16.368  -29.808 22.976  1.00 29.94  ? 43  PHE C O   1 
ATOM   1740 C CB  . PHE C 1 44 ? 14.625  -30.384 25.286  1.00 34.34  ? 43  PHE C CB  1 
ATOM   1741 C CG  . PHE C 1 44 ? 13.240  -30.327 24.644  1.00 34.11  ? 43  PHE C CG  1 
ATOM   1742 C CD1 . PHE C 1 44 ? 12.288  -31.310 24.903  1.00 36.02  ? 43  PHE C CD1 1 
ATOM   1743 C CD2 . PHE C 1 44 ? 12.913  -29.287 23.763  1.00 36.48  ? 43  PHE C CD2 1 
ATOM   1744 C CE1 . PHE C 1 44 ? 11.031  -31.271 24.304  1.00 42.25  ? 43  PHE C CE1 1 
ATOM   1745 C CE2 . PHE C 1 44 ? 11.650  -29.242 23.168  1.00 36.02  ? 43  PHE C CE2 1 
ATOM   1746 C CZ  . PHE C 1 44 ? 10.719  -30.227 23.447  1.00 41.72  ? 43  PHE C CZ  1 
ATOM   1747 N N   . PHE C 1 45 ? 15.312  -31.721 22.263  1.00 28.32  ? 44  PHE C N   1 
ATOM   1748 C CA  . PHE C 1 45 ? 15.510  -31.497 20.838  1.00 29.48  ? 44  PHE C CA  1 
ATOM   1749 C C   . PHE C 1 45 ? 14.247  -30.849 20.293  1.00 28.97  ? 44  PHE C C   1 
ATOM   1750 O O   . PHE C 1 45 ? 13.162  -31.410 20.398  1.00 31.73  ? 44  PHE C O   1 
ATOM   1751 C CB  . PHE C 1 45 ? 15.806  -32.803 20.108  1.00 27.63  ? 44  PHE C CB  1 
ATOM   1752 C CG  . PHE C 1 45 ? 17.178  -33.387 20.420  1.00 26.22  ? 44  PHE C CG  1 
ATOM   1753 C CD1 . PHE C 1 45 ? 18.311  -33.009 19.700  1.00 26.88  ? 44  PHE C CD1 1 
ATOM   1754 C CD2 . PHE C 1 45 ? 17.329  -34.308 21.470  1.00 28.87  ? 44  PHE C CD2 1 
ATOM   1755 C CE1 . PHE C 1 45 ? 19.566  -33.560 19.989  1.00 29.52  ? 44  PHE C CE1 1 
ATOM   1756 C CE2 . PHE C 1 45 ? 18.579  -34.837 21.765  1.00 29.97  ? 44  PHE C CE2 1 
ATOM   1757 C CZ  . PHE C 1 45 ? 19.694  -34.467 21.018  1.00 28.06  ? 44  PHE C CZ  1 
ATOM   1758 N N   . PHE C 1 46 ? 14.399  -29.675 19.654  1.00 31.01  ? 45  PHE C N   1 
ATOM   1759 C CA  . PHE C 1 46 ? 13.190  -29.123 19.054  1.00 26.01  ? 45  PHE C CA  1 
ATOM   1760 C C   . PHE C 1 46 ? 12.756  -29.935 17.837  1.00 28.55  ? 45  PHE C C   1 
ATOM   1761 O O   . PHE C 1 46 ? 13.539  -30.692 17.228  1.00 27.77  ? 45  PHE C O   1 
ATOM   1762 C CB  . PHE C 1 46 ? 13.450  -27.663 18.650  1.00 27.95  ? 45  PHE C CB  1 
ATOM   1763 C CG  . PHE C 1 46 ? 13.765  -26.657 19.740  1.00 27.82  ? 45  PHE C CG  1 
ATOM   1764 C CD1 . PHE C 1 46 ? 12.765  -26.141 20.562  1.00 32.44  ? 45  PHE C CD1 1 
ATOM   1765 C CD2 . PHE C 1 46 ? 15.080  -26.211 19.914  1.00 28.01  ? 45  PHE C CD2 1 
ATOM   1766 C CE1 . PHE C 1 46 ? 13.100  -25.211 21.552  1.00 32.43  ? 45  PHE C CE1 1 
ATOM   1767 C CE2 . PHE C 1 46 ? 15.401  -25.313 20.922  1.00 34.76  ? 45  PHE C CE2 1 
ATOM   1768 C CZ  . PHE C 1 46 ? 14.411  -24.811 21.729  1.00 32.13  ? 45  PHE C CZ  1 
ATOM   1769 N N   . GLY C 1 47 ? 11.489  -29.763 17.440  1.00 27.75  ? 46  GLY C N   1 
ATOM   1770 C CA  . GLY C 1 47 ? 10.992  -30.509 16.300  1.00 33.19  ? 46  GLY C CA  1 
ATOM   1771 C C   . GLY C 1 47 ? 10.544  -31.915 16.699  1.00 35.90  ? 46  GLY C C   1 
ATOM   1772 O O   . GLY C 1 47 ? 9.351   -32.212 16.638  1.00 39.67  ? 46  GLY C O   1 
ATOM   1773 N N   . THR C 1 48 ? 11.494  -32.790 17.098  1.00 30.58  ? 47  THR C N   1 
ATOM   1774 C CA  . THR C 1 48 ? 11.127  -34.137 17.527  1.00 32.78  ? 47  THR C CA  1 
ATOM   1775 C C   . THR C 1 48 ? 10.585  -34.122 18.958  1.00 32.53  ? 47  THR C C   1 
ATOM   1776 O O   . THR C 1 48 ? 9.841   -35.034 19.327  1.00 38.24  ? 47  THR C O   1 
ATOM   1777 C CB  . THR C 1 48 ? 12.357  -35.034 17.447  1.00 31.15  ? 47  THR C CB  1 
ATOM   1778 O OG1 . THR C 1 48 ? 13.210  -34.484 18.455  1.00 33.46  ? 47  THR C OG1 1 
ATOM   1779 C CG2 . THR C 1 48 ? 12.930  -35.128 16.047  1.00 32.21  ? 47  THR C CG2 1 
ATOM   1780 N N   . HIS C 1 49 ? 10.955  -33.116 19.759  1.00 31.65  ? 48  HIS C N   1 
ATOM   1781 C CA  . HIS C 1 49 ? 10.598  -33.008 21.170  1.00 36.99  ? 48  HIS C CA  1 
ATOM   1782 C C   . HIS C 1 49 ? 11.092  -34.209 21.986  1.00 36.95  ? 48  HIS C C   1 
ATOM   1783 O O   . HIS C 1 49 ? 10.487  -34.566 22.998  1.00 39.03  ? 48  HIS C O   1 
ATOM   1784 C CB  . HIS C 1 49 ? 9.088   -32.782 21.346  1.00 34.64  ? 48  HIS C CB  1 
ATOM   1785 C CG  . HIS C 1 49 ? 8.541   -31.691 20.466  1.00 41.85  ? 48  HIS C CG  1 
ATOM   1786 N ND1 . HIS C 1 49 ? 7.373   -31.850 19.746  1.00 46.22  ? 48  HIS C ND1 1 
ATOM   1787 C CD2 . HIS C 1 49 ? 8.992   -30.464 20.169  1.00 43.16  ? 48  HIS C CD2 1 
ATOM   1788 C CE1 . HIS C 1 49 ? 7.139   -30.753 19.035  1.00 49.87  ? 48  HIS C CE1 1 
ATOM   1789 N NE2 . HIS C 1 49 ? 8.106   -29.893 19.276  1.00 44.52  ? 48  HIS C NE2 1 
ATOM   1790 N N   . GLU C 1 50 ? 12.201  -34.814 21.563  1.00 34.01  ? 49  GLU C N   1 
ATOM   1791 C CA  . GLU C 1 50 ? 12.811  -35.903 22.311  1.00 34.03  ? 49  GLU C CA  1 
ATOM   1792 C C   . GLU C 1 50 ? 13.920  -35.374 23.230  1.00 32.50  ? 49  GLU C C   1 
ATOM   1793 O O   . GLU C 1 50 ? 14.308  -34.208 23.192  1.00 32.95  ? 49  GLU C O   1 
ATOM   1794 C CB  . GLU C 1 50 ? 13.266  -36.989 21.346  1.00 38.73  ? 49  GLU C CB  1 
ATOM   1795 C CG  . GLU C 1 50 ? 12.117  -37.592 20.543  1.00 45.52  ? 49  GLU C CG  1 
ATOM   1796 C CD  . GLU C 1 50 ? 12.678  -38.546 19.512  1.00 56.75  ? 49  GLU C CD  1 
ATOM   1797 O OE1 . GLU C 1 50 ? 13.877  -38.904 19.627  1.00 64.05  ? 49  GLU C OE1 1 
ATOM   1798 O OE2 . GLU C 1 50 ? 11.932  -38.900 18.573  1.00 62.64  ? 49  GLU C OE2 1 
ATOM   1799 N N   . THR C 1 51 ? 14.395  -36.250 24.133  1.00 37.59  ? 50  THR C N   1 
ATOM   1800 C CA  . THR C 1 51 ? 15.416  -35.904 25.122  1.00 35.29  ? 50  THR C CA  1 
ATOM   1801 C C   . THR C 1 51 ? 16.526  -36.955 25.063  1.00 30.41  ? 50  THR C C   1 
ATOM   1802 O O   . THR C 1 51 ? 16.323  -38.090 24.632  1.00 35.07  ? 50  THR C O   1 
ATOM   1803 C CB  . THR C 1 51 ? 14.848  -35.812 26.547  1.00 36.85  ? 50  THR C CB  1 
ATOM   1804 O OG1 . THR C 1 51 ? 14.348  -37.132 26.788  1.00 37.97  ? 50  THR C OG1 1 
ATOM   1805 C CG2 . THR C 1 51 ? 13.821  -34.705 26.747  1.00 40.12  ? 50  THR C CG2 1 
ATOM   1806 N N   . ALA C 1 52 ? 17.731  -36.516 25.425  1.00 32.04  ? 51  ALA C N   1 
ATOM   1807 C CA  . ALA C 1 52 ? 18.908  -37.353 25.569  1.00 33.10  ? 51  ALA C CA  1 
ATOM   1808 C C   . ALA C 1 52 ? 19.873  -36.632 26.501  1.00 34.50  ? 51  ALA C C   1 
ATOM   1809 O O   . ALA C 1 52 ? 19.642  -35.493 26.864  1.00 33.23  ? 51  ALA C O   1 
ATOM   1810 C CB  . ALA C 1 52 ? 19.549  -37.637 24.240  1.00 33.27  ? 51  ALA C CB  1 
ATOM   1811 N N   . PHE C 1 53 ? 20.947  -37.321 26.905  1.00 34.95  ? 52  PHE C N   1 
ATOM   1812 C CA  . PHE C 1 53 ? 22.022  -36.732 27.685  1.00 33.03  ? 52  PHE C CA  1 
ATOM   1813 C C   . PHE C 1 53 ? 23.219  -36.603 26.764  1.00 32.38  ? 52  PHE C C   1 
ATOM   1814 O O   . PHE C 1 53 ? 23.606  -37.574 26.122  1.00 34.04  ? 52  PHE C O   1 
ATOM   1815 C CB  . PHE C 1 53 ? 22.423  -37.720 28.791  1.00 34.35  ? 52  PHE C CB  1 
ATOM   1816 C CG  . PHE C 1 53 ? 21.450  -37.634 29.952  1.00 35.44  ? 52  PHE C CG  1 
ATOM   1817 C CD1 . PHE C 1 53 ? 21.230  -36.427 30.599  1.00 36.29  ? 52  PHE C CD1 1 
ATOM   1818 C CD2 . PHE C 1 53 ? 20.707  -38.747 30.350  1.00 48.82  ? 52  PHE C CD2 1 
ATOM   1819 C CE1 . PHE C 1 53 ? 20.322  -36.335 31.649  1.00 43.22  ? 52  PHE C CE1 1 
ATOM   1820 C CE2 . PHE C 1 53 ? 19.796  -38.648 31.403  1.00 44.07  ? 52  PHE C CE2 1 
ATOM   1821 C CZ  . PHE C 1 53 ? 19.606  -37.440 32.047  1.00 41.53  ? 52  PHE C CZ  1 
ATOM   1822 N N   . LEU C 1 54 ? 23.841  -35.425 26.734  1.00 29.94  ? 53  LEU C N   1 
ATOM   1823 C CA  . LEU C 1 54 ? 25.013  -35.249 25.887  1.00 26.18  ? 53  LEU C CA  1 
ATOM   1824 C C   . LEU C 1 54 ? 26.094  -34.476 26.641  1.00 30.02  ? 53  LEU C C   1 
ATOM   1825 O O   . LEU C 1 54 ? 25.779  -33.707 27.547  1.00 30.69  ? 53  LEU C O   1 
ATOM   1826 C CB  . LEU C 1 54 ? 24.640  -34.500 24.605  1.00 29.32  ? 53  LEU C CB  1 
ATOM   1827 C CG  . LEU C 1 54 ? 23.792  -35.279 23.590  1.00 33.42  ? 53  LEU C CG  1 
ATOM   1828 C CD1 . LEU C 1 54 ? 23.503  -34.344 22.453  1.00 33.01  ? 53  LEU C CD1 1 
ATOM   1829 C CD2 . LEU C 1 54 ? 24.523  -36.537 23.036  1.00 38.73  ? 53  LEU C CD2 1 
ATOM   1830 N N   . GLY C 1 55 ? 27.354  -34.697 26.255  1.00 32.37  ? 54  GLY C N   1 
ATOM   1831 C CA  . GLY C 1 55 ? 28.470  -33.986 26.853  1.00 34.71  ? 54  GLY C CA  1 
ATOM   1832 C C   . GLY C 1 55 ? 28.790  -32.696 26.102  1.00 39.89  ? 54  GLY C C   1 
ATOM   1833 O O   . GLY C 1 55 ? 28.323  -32.453 24.977  1.00 35.20  ? 54  GLY C O   1 
ATOM   1834 N N   . PRO C 1 56 ? 29.590  -31.796 26.712  1.00 38.53  ? 55  PRO C N   1 
ATOM   1835 C CA  . PRO C 1 56 ? 29.809  -30.461 26.162  1.00 39.86  ? 55  PRO C CA  1 
ATOM   1836 C C   . PRO C 1 56 ? 30.441  -30.430 24.776  1.00 38.39  ? 55  PRO C C   1 
ATOM   1837 O O   . PRO C 1 56 ? 30.183  -29.498 24.015  1.00 50.14  ? 55  PRO C O   1 
ATOM   1838 C CB  . PRO C 1 56 ? 30.687  -29.741 27.240  1.00 41.84  ? 55  PRO C CB  1 
ATOM   1839 C CG  . PRO C 1 56 ? 31.298  -30.869 28.041  1.00 37.18  ? 55  PRO C CG  1 
ATOM   1840 C CD  . PRO C 1 56 ? 30.270  -31.993 28.009  1.00 40.01  ? 55  PRO C CD  1 
ATOM   1841 N N   . LYS C 1 57 ? 31.206  -31.474 24.444  1.00 40.08  ? 56  LYS C N   1 
ATOM   1842 C CA  . LYS C 1 57 ? 31.859  -31.567 23.151  1.00 44.29  ? 56  LYS C CA  1 
ATOM   1843 C C   . LYS C 1 57 ? 30.803  -31.646 22.049  1.00 46.08  ? 56  LYS C C   1 
ATOM   1844 O O   . LYS C 1 57 ? 31.098  -31.356 20.888  1.00 41.79  ? 56  LYS C O   1 
ATOM   1845 C CB  . LYS C 1 57 ? 32.636  -32.882 23.040  1.00 43.72  ? 56  LYS C CB  1 
ATOM   1846 N N   . ASP C 1 58 ? 29.589  -32.075 22.428  1.00 40.83  ? 57  ASP C N   1 
ATOM   1847 C CA  . ASP C 1 58 ? 28.538  -32.333 21.447  1.00 40.30  ? 57  ASP C CA  1 
ATOM   1848 C C   . ASP C 1 58 ? 27.588  -31.146 21.295  1.00 37.14  ? 57  ASP C C   1 
ATOM   1849 O O   . ASP C 1 58 ? 26.607  -31.243 20.555  1.00 34.73  ? 57  ASP C O   1 
ATOM   1850 C CB  . ASP C 1 58 ? 27.768  -33.602 21.771  1.00 37.25  ? 57  ASP C CB  1 
ATOM   1851 C CG  . ASP C 1 58 ? 28.616  -34.853 21.920  1.00 43.40  ? 57  ASP C CG  1 
ATOM   1852 O OD1 . ASP C 1 58 ? 29.583  -34.974 21.168  1.00 43.52  ? 57  ASP C OD1 1 
ATOM   1853 O OD2 . ASP C 1 58 ? 28.269  -35.704 22.756  1.00 49.43  ? 57  ASP C OD2 1 
ATOM   1854 N N   . LEU C 1 59 ? 27.859  -30.027 21.976  1.00 32.59  ? 58  LEU C N   1 
ATOM   1855 C CA  . LEU C 1 59 ? 26.927  -28.911 22.050  1.00 34.62  ? 58  LEU C CA  1 
ATOM   1856 C C   . LEU C 1 59 ? 27.581  -27.642 21.506  1.00 37.41  ? 58  LEU C C   1 
ATOM   1857 O O   . LEU C 1 59 ? 28.766  -27.437 21.769  1.00 43.15  ? 58  LEU C O   1 
ATOM   1858 C CB  . LEU C 1 59 ? 26.525  -28.703 23.513  1.00 33.08  ? 58  LEU C CB  1 
ATOM   1859 C CG  . LEU C 1 59 ? 26.024  -29.963 24.220  1.00 30.85  ? 58  LEU C CG  1 
ATOM   1860 C CD1 . LEU C 1 59 ? 25.753  -29.738 25.690  1.00 29.82  ? 58  LEU C CD1 1 
ATOM   1861 C CD2 . LEU C 1 59 ? 24.736  -30.400 23.505  1.00 29.23  ? 58  LEU C CD2 1 
ATOM   1862 N N   . PHE C 1 60 ? 26.785  -26.803 20.818  1.00 39.13  ? 59  PHE C N   1 
ATOM   1863 C CA  . PHE C 1 60 ? 27.265  -25.591 20.146  1.00 37.48  ? 59  PHE C CA  1 
ATOM   1864 C C   . PHE C 1 60 ? 26.281  -24.461 20.428  1.00 39.48  ? 59  PHE C C   1 
ATOM   1865 O O   . PHE C 1 60 ? 25.101  -24.578 20.120  1.00 36.71  ? 59  PHE C O   1 
ATOM   1866 C CB  . PHE C 1 60 ? 27.451  -25.823 18.635  1.00 36.20  ? 59  PHE C CB  1 
ATOM   1867 C CG  . PHE C 1 60 ? 28.402  -26.973 18.338  1.00 35.50  ? 59  PHE C CG  1 
ATOM   1868 C CD1 . PHE C 1 60 ? 27.951  -28.290 18.327  1.00 35.11  ? 59  PHE C CD1 1 
ATOM   1869 C CD2 . PHE C 1 60 ? 29.768  -26.758 18.121  1.00 41.46  ? 59  PHE C CD2 1 
ATOM   1870 C CE1 . PHE C 1 60 ? 28.813  -29.354 18.127  1.00 36.04  ? 59  PHE C CE1 1 
ATOM   1871 C CE2 . PHE C 1 60 ? 30.632  -27.828 17.888  1.00 38.78  ? 59  PHE C CE2 1 
ATOM   1872 C CZ  . PHE C 1 60 ? 30.162  -29.128 17.888  1.00 41.47  ? 59  PHE C CZ  1 
ATOM   1873 N N   . PRO C 1 61 ? 26.691  -23.306 21.015  1.00 40.60  ? 60  PRO C N   1 
ATOM   1874 C CA  . PRO C 1 61 ? 25.721  -22.255 21.330  1.00 40.74  ? 60  PRO C CA  1 
ATOM   1875 C C   . PRO C 1 61 ? 25.040  -21.761 20.058  1.00 34.56  ? 60  PRO C C   1 
ATOM   1876 O O   . PRO C 1 61 ? 25.667  -21.655 19.011  1.00 40.47  ? 60  PRO C O   1 
ATOM   1877 C CB  . PRO C 1 61 ? 26.502  -21.136 22.073  1.00 42.65  ? 60  PRO C CB  1 
ATOM   1878 C CG  . PRO C 1 61 ? 27.903  -21.696 22.209  1.00 44.42  ? 60  PRO C CG  1 
ATOM   1879 C CD  . PRO C 1 61 ? 28.077  -22.947 21.362  1.00 46.57  ? 60  PRO C CD  1 
ATOM   1880 N N   . TYR C 1 62 ? 23.721  -21.545 20.178  1.00 42.33  ? 61  TYR C N   1 
ATOM   1881 C CA  . TYR C 1 62 ? 22.828  -21.333 19.055  1.00 41.41  ? 61  TYR C CA  1 
ATOM   1882 C C   . TYR C 1 62 ? 23.234  -20.084 18.282  1.00 51.43  ? 61  TYR C C   1 
ATOM   1883 O O   . TYR C 1 62 ? 23.461  -20.159 17.073  1.00 57.44  ? 61  TYR C O   1 
ATOM   1884 C CB  . TYR C 1 62 ? 21.382  -21.169 19.512  1.00 44.16  ? 61  TYR C CB  1 
ATOM   1885 C CG  . TYR C 1 62 ? 20.441  -20.814 18.372  1.00 44.17  ? 61  TYR C CG  1 
ATOM   1886 C CD1 . TYR C 1 62 ? 20.231  -21.695 17.306  1.00 45.30  ? 61  TYR C CD1 1 
ATOM   1887 C CD2 . TYR C 1 62 ? 19.729  -19.619 18.386  1.00 45.87  ? 61  TYR C CD2 1 
ATOM   1888 C CE1 . TYR C 1 62 ? 19.350  -21.381 16.275  1.00 41.97  ? 61  TYR C CE1 1 
ATOM   1889 C CE2 . TYR C 1 62 ? 18.850  -19.300 17.363  1.00 47.30  ? 61  TYR C CE2 1 
ATOM   1890 C CZ  . TYR C 1 62 ? 18.659  -20.177 16.306  1.00 40.80  ? 61  TYR C CZ  1 
ATOM   1891 O OH  . TYR C 1 62 ? 17.793  -19.784 15.314  1.00 42.96  ? 61  TYR C OH  1 
ATOM   1892 N N   . ASP C 1 63 ? 23.350  -18.955 18.999  1.00 52.16  ? 62  ASP C N   1 
ATOM   1893 C CA  . ASP C 1 63 ? 23.634  -17.692 18.332  1.00 52.27  ? 62  ASP C CA  1 
ATOM   1894 C C   . ASP C 1 63 ? 24.962  -17.768 17.598  1.00 46.00  ? 62  ASP C C   1 
ATOM   1895 O O   . ASP C 1 63 ? 25.072  -17.262 16.481  1.00 49.94  ? 62  ASP C O   1 
ATOM   1896 C CB  . ASP C 1 63 ? 23.356  -16.479 19.204  1.00 54.29  ? 62  ASP C CB  1 
ATOM   1897 C CG  . ASP C 1 63 ? 21.877  -16.123 19.230  1.00 70.78  ? 62  ASP C CG  1 
ATOM   1898 O OD1 . ASP C 1 63 ? 21.308  -16.055 20.340  1.00 73.57  ? 62  ASP C OD1 1 
ATOM   1899 O OD2 . ASP C 1 63 ? 21.291  -15.971 18.128  1.00 74.88  ? 62  ASP C OD2 1 
ATOM   1900 N N   . LYS C 1 64 ? 25.925  -18.469 18.191  1.00 41.61  ? 63  LYS C N   1 
ATOM   1901 C CA  . LYS C 1 64 ? 27.273  -18.512 17.664  1.00 46.31  ? 63  LYS C CA  1 
ATOM   1902 C C   . LYS C 1 64 ? 27.336  -19.421 16.440  1.00 45.03  ? 63  LYS C C   1 
ATOM   1903 O O   . LYS C 1 64 ? 28.129  -19.162 15.546  1.00 40.17  ? 63  LYS C O   1 
ATOM   1904 C CB  . LYS C 1 64 ? 28.299  -18.898 18.739  1.00 50.55  ? 63  LYS C CB  1 
ATOM   1905 N N   . SER C 1 65 ? 26.462  -20.451 16.357  1.00 39.00  ? 64  SER C N   1 
ATOM   1906 C CA  . SER C 1 65 ? 26.707  -21.470 15.347  1.00 35.49  ? 64  SER C CA  1 
ATOM   1907 C C   . SER C 1 65 ? 25.557  -21.565 14.341  1.00 33.07  ? 64  SER C C   1 
ATOM   1908 O O   . SER C 1 65 ? 25.655  -22.354 13.408  1.00 35.54  ? 64  SER C O   1 
ATOM   1909 C CB  . SER C 1 65 ? 27.022  -22.831 15.956  1.00 39.65  ? 64  SER C CB  1 
ATOM   1910 O OG  . SER C 1 65 ? 25.893  -23.274 16.697  1.00 43.37  ? 64  SER C OG  1 
ATOM   1911 N N   . LYS C 1 66 ? 24.503  -20.758 14.510  1.00 34.23  ? 65  LYS C N   1 
ATOM   1912 C CA  . LYS C 1 66 ? 23.349  -20.884 13.624  1.00 35.51  ? 65  LYS C CA  1 
ATOM   1913 C C   . LYS C 1 66 ? 23.713  -20.593 12.167  1.00 40.43  ? 65  LYS C C   1 
ATOM   1914 O O   . LYS C 1 66 ? 23.188  -21.234 11.261  1.00 36.21  ? 65  LYS C O   1 
ATOM   1915 C CB  . LYS C 1 66 ? 22.145  -20.053 14.066  1.00 39.90  ? 65  LYS C CB  1 
ATOM   1916 C CG  . LYS C 1 66 ? 22.418  -18.565 14.212  1.00 33.60  ? 65  LYS C CG  1 
ATOM   1917 C CD  . LYS C 1 66 ? 21.075  -17.922 14.528  1.00 40.24  ? 65  LYS C CD  1 
ATOM   1918 C CE  . LYS C 1 66 ? 21.219  -16.450 14.730  1.00 41.69  ? 65  LYS C CE  1 
ATOM   1919 N NZ  . LYS C 1 66 ? 19.893  -15.977 15.094  1.00 47.62  ? 65  LYS C NZ  1 
ATOM   1920 N N   . ASP C 1 67 ? 24.668  -19.686 11.922  1.00 39.02  ? 66  ASP C N   1 
ATOM   1921 C CA  . ASP C 1 67 ? 25.046  -19.400 10.537  1.00 39.59  ? 66  ASP C CA  1 
ATOM   1922 C C   . ASP C 1 67 ? 25.460  -20.686 9.802   1.00 38.99  ? 66  ASP C C   1 
ATOM   1923 O O   . ASP C 1 67 ? 25.123  -20.872 8.639   1.00 37.55  ? 66  ASP C O   1 
ATOM   1924 C CB  . ASP C 1 67 ? 25.895  -18.129 10.425  1.00 38.81  ? 66  ASP C CB  1 
ATOM   1925 C CG  . ASP C 1 67 ? 27.411  -18.214 10.596  1.00 53.05  ? 66  ASP C CG  1 
ATOM   1926 O OD1 . ASP C 1 67 ? 27.995  -19.320 10.421  1.00 53.74  ? 66  ASP C OD1 1 
ATOM   1927 O OD2 . ASP C 1 67 ? 28.016  -17.156 10.918  1.00 56.46  ? 66  ASP C OD2 1 
ATOM   1928 N N   . LYS C 1 68 ? 26.086  -21.629 10.523  1.00 36.27  ? 67  LYS C N   1 
ATOM   1929 C CA  . LYS C 1 68 ? 26.568  -22.893 9.978   1.00 36.13  ? 67  LYS C CA  1 
ATOM   1930 C C   . LYS C 1 68 ? 25.559  -24.061 10.076  1.00 32.55  ? 67  LYS C C   1 
ATOM   1931 O O   . LYS C 1 68 ? 25.433  -24.860 9.146   1.00 38.42  ? 67  LYS C O   1 
ATOM   1932 C CB  . LYS C 1 68 ? 27.780  -23.253 10.836  1.00 33.48  ? 67  LYS C CB  1 
ATOM   1933 C CG  . LYS C 1 68 ? 28.627  -24.405 10.360  1.00 38.12  ? 67  LYS C CG  1 
ATOM   1934 C CD  . LYS C 1 68 ? 29.870  -24.433 11.255  1.00 49.81  ? 67  LYS C CD  1 
ATOM   1935 C CE  . LYS C 1 68 ? 30.710  -25.679 11.223  1.00 64.01  ? 67  LYS C CE  1 
ATOM   1936 N NZ  . LYS C 1 68 ? 31.072  -26.173 9.888   1.00 69.57  ? 67  LYS C NZ  1 
ATOM   1937 N N   . TYR C 1 69 ? 24.860  -24.204 11.214  1.00 30.38  ? 68  TYR C N   1 
ATOM   1938 C CA  . TYR C 1 69 ? 24.002  -25.383 11.360  1.00 30.53  ? 68  TYR C CA  1 
ATOM   1939 C C   . TYR C 1 69 ? 22.523  -25.055 11.151  1.00 32.78  ? 68  TYR C C   1 
ATOM   1940 O O   . TYR C 1 69 ? 21.733  -25.973 10.973  1.00 30.89  ? 68  TYR C O   1 
ATOM   1941 C CB  . TYR C 1 69 ? 24.174  -25.991 12.770  1.00 28.75  ? 68  TYR C CB  1 
ATOM   1942 C CG  . TYR C 1 69 ? 25.596  -26.454 13.060  1.00 27.26  ? 68  TYR C CG  1 
ATOM   1943 C CD1 . TYR C 1 69 ? 26.298  -27.262 12.171  1.00 31.66  ? 68  TYR C CD1 1 
ATOM   1944 C CD2 . TYR C 1 69 ? 26.207  -26.085 14.256  1.00 36.13  ? 68  TYR C CD2 1 
ATOM   1945 C CE1 . TYR C 1 69 ? 27.583  -27.716 12.457  1.00 34.06  ? 68  TYR C CE1 1 
ATOM   1946 C CE2 . TYR C 1 69 ? 27.488  -26.531 14.549  1.00 33.25  ? 68  TYR C CE2 1 
ATOM   1947 C CZ  . TYR C 1 69 ? 28.175  -27.317 13.645  1.00 36.56  ? 68  TYR C CZ  1 
ATOM   1948 O OH  . TYR C 1 69 ? 29.443  -27.697 13.992  1.00 41.45  ? 68  TYR C OH  1 
ATOM   1949 N N   . GLY C 1 70 ? 22.133  -23.763 11.192  1.00 30.78  ? 69  GLY C N   1 
ATOM   1950 C CA  . GLY C 1 70 ? 20.721  -23.406 11.127  1.00 30.77  ? 69  GLY C CA  1 
ATOM   1951 C C   . GLY C 1 70 ? 20.319  -23.283 9.667   1.00 33.03  ? 69  GLY C C   1 
ATOM   1952 O O   . GLY C 1 70 ? 20.283  -22.187 9.115   1.00 34.48  ? 69  GLY C O   1 
ATOM   1953 N N   . LYS C 1 71 ? 20.204  -24.437 9.026   1.00 31.03  ? 70  LYS C N   1 
ATOM   1954 C CA  . LYS C 1 71 ? 19.819  -24.486 7.622   1.00 33.31  ? 70  LYS C CA  1 
ATOM   1955 C C   . LYS C 1 71 ? 18.986  -25.743 7.462   1.00 33.25  ? 70  LYS C C   1 
ATOM   1956 O O   . LYS C 1 71 ? 19.157  -26.717 8.201   1.00 34.07  ? 70  LYS C O   1 
ATOM   1957 C CB  . LYS C 1 71 ? 21.005  -24.563 6.659   1.00 34.71  ? 70  LYS C CB  1 
ATOM   1958 C CG  . LYS C 1 71 ? 22.038  -25.572 7.094   1.00 36.62  ? 70  LYS C CG  1 
ATOM   1959 C CD  . LYS C 1 71 ? 23.128  -26.006 6.125   1.00 46.54  ? 70  LYS C CD  1 
ATOM   1960 C CE  . LYS C 1 71 ? 23.964  -27.072 6.781   1.00 54.71  ? 70  LYS C CE  1 
ATOM   1961 N N   . PRO C 1 72 ? 18.000  -25.746 6.551   1.00 29.20  ? 71  PRO C N   1 
ATOM   1962 C CA  . PRO C 1 72 ? 17.078  -26.870 6.472   1.00 25.68  ? 71  PRO C CA  1 
ATOM   1963 C C   . PRO C 1 72 ? 17.745  -28.185 6.106   1.00 29.67  ? 71  PRO C C   1 
ATOM   1964 O O   . PRO C 1 72 ? 18.751  -28.232 5.393   1.00 32.77  ? 71  PRO C O   1 
ATOM   1965 C CB  . PRO C 1 72 ? 16.104  -26.407 5.369   1.00 27.09  ? 71  PRO C CB  1 
ATOM   1966 C CG  . PRO C 1 72 ? 16.161  -24.902 5.489   1.00 28.29  ? 71  PRO C CG  1 
ATOM   1967 C CD  . PRO C 1 72 ? 17.624  -24.606 5.690   1.00 28.01  ? 71  PRO C CD  1 
ATOM   1968 N N   . ASN C 1 73 ? 17.075  -29.233 6.547   1.00 30.21  ? 72  ASN C N   1 
ATOM   1969 C CA  . ASN C 1 73 ? 17.337  -30.521 5.935   1.00 36.19  ? 72  ASN C CA  1 
ATOM   1970 C C   . ASN C 1 73 ? 16.100  -31.395 6.087   1.00 30.85  ? 72  ASN C C   1 
ATOM   1971 O O   . ASN C 1 73 ? 15.142  -31.061 6.774   1.00 32.04  ? 72  ASN C O   1 
ATOM   1972 C CB  . ASN C 1 73 ? 18.695  -31.120 6.301   1.00 37.49  ? 72  ASN C CB  1 
ATOM   1973 C CG  . ASN C 1 73 ? 18.711  -31.713 7.689   1.00 38.62  ? 72  ASN C CG  1 
ATOM   1974 O OD1 . ASN C 1 73 ? 17.845  -32.518 8.043   1.00 37.96  ? 72  ASN C OD1 1 
ATOM   1975 N ND2 . ASN C 1 73 ? 19.743  -31.395 8.447   1.00 39.81  ? 72  ASN C ND2 1 
ATOM   1976 N N   . LYS C 1 74 ? 16.163  -32.558 5.448   1.00 33.06  ? 73  LYS C N   1 
ATOM   1977 C CA  . LYS C 1 74 ? 14.951  -33.333 5.264   1.00 29.56  ? 73  LYS C CA  1 
ATOM   1978 C C   . LYS C 1 74 ? 14.761  -34.324 6.396   1.00 30.76  ? 73  LYS C C   1 
ATOM   1979 O O   . LYS C 1 74 ? 13.714  -34.984 6.441   1.00 33.91  ? 73  LYS C O   1 
ATOM   1980 C CB  . LYS C 1 74 ? 14.935  -34.052 3.913   1.00 35.51  ? 73  LYS C CB  1 
ATOM   1981 C CG  . LYS C 1 74 ? 14.681  -33.082 2.740   1.00 44.22  ? 73  LYS C CG  1 
ATOM   1982 C CD  . LYS C 1 74 ? 16.000  -32.824 2.025   1.00 50.68  ? 73  LYS C CD  1 
ATOM   1983 N N   . ARG C 1 75 ? 15.699  -34.364 7.360   1.00 26.68  ? 74  ARG C N   1 
ATOM   1984 C CA  . ARG C 1 75 ? 15.493  -35.297 8.466   1.00 28.86  ? 74  ARG C CA  1 
ATOM   1985 C C   . ARG C 1 75 ? 14.200  -34.984 9.233   1.00 30.19  ? 74  ARG C C   1 
ATOM   1986 O O   . ARG C 1 75 ? 13.810  -33.821 9.454   1.00 31.06  ? 74  ARG C O   1 
ATOM   1987 C CB  . ARG C 1 75 ? 16.739  -35.411 9.381   1.00 29.54  ? 74  ARG C CB  1 
ATOM   1988 C CG  . ARG C 1 75 ? 18.068  -35.661 8.661   1.00 31.19  ? 74  ARG C CG  1 
ATOM   1989 C CD  . ARG C 1 75 ? 18.398  -37.071 8.129   1.00 38.01  ? 74  ARG C CD  1 
ATOM   1990 N NE  . ARG C 1 75 ? 18.320  -38.000 9.252   1.00 36.20  ? 74  ARG C NE  1 
ATOM   1991 C CZ  . ARG C 1 75 ? 19.444  -38.449 9.834   1.00 29.91  ? 74  ARG C CZ  1 
ATOM   1992 N NH1 . ARG C 1 75 ? 19.341  -39.043 10.990  1.00 36.07  ? 74  ARG C NH1 1 
ATOM   1993 N NH2 . ARG C 1 75 ? 20.604  -38.149 9.282   1.00 32.97  ? 74  ARG C NH2 1 
ATOM   1994 N N   . LYS C 1 76 ? 13.540  -36.058 9.680   1.00 33.75  ? 75  LYS C N   1 
ATOM   1995 C CA  . LYS C 1 76 ? 12.244  -35.971 10.328  1.00 34.49  ? 75  LYS C CA  1 
ATOM   1996 C C   . LYS C 1 76 ? 12.288  -35.009 11.509  1.00 32.09  ? 75  LYS C C   1 
ATOM   1997 O O   . LYS C 1 76 ? 13.077  -35.170 12.454  1.00 32.65  ? 75  LYS C O   1 
ATOM   1998 C CB  . LYS C 1 76 ? 11.687  -37.340 10.748  1.00 33.80  ? 75  LYS C CB  1 
ATOM   1999 C CG  . LYS C 1 76 ? 10.241  -37.273 11.192  1.00 41.02  ? 75  LYS C CG  1 
ATOM   2000 C CD  . LYS C 1 76 ? 9.618   -38.637 11.481  1.00 48.83  ? 75  LYS C CD  1 
ATOM   2001 N N   . GLY C 1 77 ? 11.464  -33.956 11.399  1.00 33.79  ? 76  GLY C N   1 
ATOM   2002 C CA  . GLY C 1 77 ? 11.204  -33.048 12.509  1.00 30.57  ? 76  GLY C CA  1 
ATOM   2003 C C   . GLY C 1 77 ? 12.172  -31.858 12.508  1.00 28.06  ? 76  GLY C C   1 
ATOM   2004 O O   . GLY C 1 77 ? 12.027  -30.947 13.316  1.00 33.03  ? 76  GLY C O   1 
ATOM   2005 N N   . PHE C 1 78 ? 13.162  -31.881 11.608  1.00 28.98  ? 77  PHE C N   1 
ATOM   2006 C CA  . PHE C 1 78 ? 14.269  -30.942 11.679  1.00 26.48  ? 77  PHE C CA  1 
ATOM   2007 C C   . PHE C 1 78 ? 13.750  -29.520 11.432  1.00 29.60  ? 77  PHE C C   1 
ATOM   2008 O O   . PHE C 1 78 ? 14.118  -28.572 12.126  1.00 26.43  ? 77  PHE C O   1 
ATOM   2009 C CB  . PHE C 1 78 ? 15.362  -31.333 10.681  1.00 30.39  ? 77  PHE C CB  1 
ATOM   2010 C CG  . PHE C 1 78 ? 16.634  -30.553 10.968  1.00 27.29  ? 77  PHE C CG  1 
ATOM   2011 C CD1 . PHE C 1 78 ? 16.810  -29.259 10.472  1.00 29.60  ? 77  PHE C CD1 1 
ATOM   2012 C CD2 . PHE C 1 78 ? 17.643  -31.086 11.764  1.00 25.82  ? 77  PHE C CD2 1 
ATOM   2013 C CE1 . PHE C 1 78 ? 17.962  -28.534 10.745  1.00 30.18  ? 77  PHE C CE1 1 
ATOM   2014 C CE2 . PHE C 1 78 ? 18.835  -30.373 11.987  1.00 26.63  ? 77  PHE C CE2 1 
ATOM   2015 C CZ  . PHE C 1 78 ? 19.001  -29.100 11.484  1.00 27.79  ? 77  PHE C CZ  1 
ATOM   2016 N N   . ASN C 1 79 ? 12.957  -29.363 10.364  1.00 30.87  ? 78  ASN C N   1 
ATOM   2017 C CA  . ASN C 1 79 ? 12.615  -28.003 9.956   1.00 32.02  ? 78  ASN C CA  1 
ATOM   2018 C C   . ASN C 1 79 ? 11.631  -27.362 10.925  1.00 31.19  ? 78  ASN C C   1 
ATOM   2019 O O   . ASN C 1 79 ? 11.692  -26.154 11.240  1.00 30.53  ? 78  ASN C O   1 
ATOM   2020 C CB  . ASN C 1 79 ? 12.150  -27.955 8.508   1.00 30.72  ? 78  ASN C CB  1 
ATOM   2021 C CG  . ASN C 1 79 ? 13.272  -28.321 7.569   1.00 29.98  ? 78  ASN C CG  1 
ATOM   2022 O OD1 . ASN C 1 79 ? 14.430  -28.020 7.864   1.00 27.14  ? 78  ASN C OD1 1 
ATOM   2023 N ND2 . ASN C 1 79 ? 12.958  -28.987 6.461   1.00 29.65  ? 78  ASN C ND2 1 
ATOM   2024 N N   . GLU C 1 80 ? 10.734  -28.176 11.453  1.00 31.58  ? 79  GLU C N   1 
ATOM   2025 C CA  . GLU C 1 80 ? 9.911   -27.664 12.532  1.00 30.35  ? 79  GLU C CA  1 
ATOM   2026 C C   . GLU C 1 80 ? 10.785  -27.255 13.722  1.00 38.20  ? 79  GLU C C   1 
ATOM   2027 O O   . GLU C 1 80 ? 10.543  -26.229 14.359  1.00 32.98  ? 79  GLU C O   1 
ATOM   2028 C CB  . GLU C 1 80 ? 8.826   -28.689 12.841  1.00 36.94  ? 79  GLU C CB  1 
ATOM   2029 C CG  . GLU C 1 80 ? 7.981   -28.278 14.035  1.00 35.94  ? 79  GLU C CG  1 
ATOM   2030 C CD  . GLU C 1 80 ? 6.740   -29.114 14.230  1.00 46.73  ? 79  GLU C CD  1 
ATOM   2031 O OE1 . GLU C 1 80 ? 6.663   -30.254 13.732  1.00 54.28  ? 79  GLU C OE1 1 
ATOM   2032 O OE2 . GLU C 1 80 ? 5.828   -28.584 14.881  1.00 49.28  ? 79  GLU C OE2 1 
ATOM   2033 N N   . GLY C 1 81 ? 11.821  -28.057 14.026  1.00 29.90  ? 80  GLY C N   1 
ATOM   2034 C CA  . GLY C 1 81 ? 12.752  -27.677 15.079  1.00 29.10  ? 80  GLY C CA  1 
ATOM   2035 C C   . GLY C 1 81 ? 13.397  -26.311 14.841  1.00 31.19  ? 80  GLY C C   1 
ATOM   2036 O O   . GLY C 1 81 ? 13.570  -25.542 15.781  1.00 30.88  ? 80  GLY C O   1 
ATOM   2037 N N   . LEU C 1 82 ? 13.827  -26.059 13.589  1.00 30.59  ? 81  LEU C N   1 
ATOM   2038 C CA  . LEU C 1 82 ? 14.413  -24.761 13.238  1.00 32.27  ? 81  LEU C CA  1 
ATOM   2039 C C   . LEU C 1 82 ? 13.408  -23.648 13.518  1.00 28.70  ? 81  LEU C C   1 
ATOM   2040 O O   . LEU C 1 82 ? 13.788  -22.555 13.951  1.00 30.51  ? 81  LEU C O   1 
ATOM   2041 C CB  . LEU C 1 82 ? 14.830  -24.714 11.769  1.00 30.42  ? 81  LEU C CB  1 
ATOM   2042 C CG  . LEU C 1 82 ? 16.091  -25.489 11.372  1.00 28.19  ? 81  LEU C CG  1 
ATOM   2043 C CD1 . LEU C 1 82 ? 16.430  -25.344 9.891   1.00 27.11  ? 81  LEU C CD1 1 
ATOM   2044 C CD2 . LEU C 1 82 ? 17.314  -25.138 12.177  1.00 23.98  ? 81  LEU C CD2 1 
ATOM   2045 N N   . TRP C 1 83 ? 12.139  -23.912 13.244  1.00 28.93  ? 82  TRP C N   1 
ATOM   2046 C CA  . TRP C 1 83 ? 11.162  -22.854 13.459  1.00 34.95  ? 82  TRP C CA  1 
ATOM   2047 C C   . TRP C 1 83 ? 11.061  -22.591 14.964  1.00 38.36  ? 82  TRP C C   1 
ATOM   2048 O O   . TRP C 1 83 ? 11.098  -21.439 15.398  1.00 34.84  ? 82  TRP C O   1 
ATOM   2049 C CB  . TRP C 1 83 ? 9.795   -23.214 12.855  1.00 34.21  ? 82  TRP C CB  1 
ATOM   2050 C CG  . TRP C 1 83 ? 8.819   -22.072 12.967  1.00 39.02  ? 82  TRP C CG  1 
ATOM   2051 C CD1 . TRP C 1 83 ? 8.633   -21.065 12.058  1.00 40.33  ? 82  TRP C CD1 1 
ATOM   2052 C CD2 . TRP C 1 83 ? 7.929   -21.780 14.069  1.00 43.26  ? 82  TRP C CD2 1 
ATOM   2053 N NE1 . TRP C 1 83 ? 7.676   -20.188 12.496  1.00 36.86  ? 82  TRP C NE1 1 
ATOM   2054 C CE2 . TRP C 1 83 ? 7.225   -20.596 13.725  1.00 41.08  ? 82  TRP C CE2 1 
ATOM   2055 C CE3 . TRP C 1 83 ? 7.653   -22.402 15.297  1.00 40.92  ? 82  TRP C CE3 1 
ATOM   2056 C CZ2 . TRP C 1 83 ? 6.274   -20.031 14.573  1.00 45.93  ? 82  TRP C CZ2 1 
ATOM   2057 C CZ3 . TRP C 1 83 ? 6.710   -21.840 16.134  1.00 48.63  ? 82  TRP C CZ3 1 
ATOM   2058 C CH2 . TRP C 1 83 ? 6.051   -20.659 15.782  1.00 46.67  ? 82  TRP C CH2 1 
ATOM   2059 N N   . GLU C 1 84 ? 11.027  -23.671 15.761  1.00 33.02  ? 83  GLU C N   1 
ATOM   2060 C CA  . GLU C 1 84 ? 10.870  -23.529 17.205  1.00 35.49  ? 83  GLU C CA  1 
ATOM   2061 C C   . GLU C 1 84 ? 12.044  -22.791 17.852  1.00 37.65  ? 83  GLU C C   1 
ATOM   2062 O O   . GLU C 1 84 ? 11.845  -21.912 18.702  1.00 39.22  ? 83  GLU C O   1 
ATOM   2063 C CB  . GLU C 1 84 ? 10.685  -24.901 17.848  1.00 31.76  ? 83  GLU C CB  1 
ATOM   2064 C CG  . GLU C 1 84 ? 9.368   -25.575 17.475  1.00 35.80  ? 83  GLU C CG  1 
ATOM   2065 C CD  . GLU C 1 84 ? 9.273   -26.990 17.981  1.00 41.32  ? 83  GLU C CD  1 
ATOM   2066 O OE1 . GLU C 1 84 ? 10.290  -27.483 18.552  1.00 37.34  ? 83  GLU C OE1 1 
ATOM   2067 O OE2 . GLU C 1 84 ? 8.197   -27.595 17.784  1.00 42.34  ? 83  GLU C OE2 1 
ATOM   2068 N N   . ILE C 1 85 ? 13.280  -23.120 17.458  1.00 33.59  ? 84  ILE C N   1 
ATOM   2069 C CA  . ILE C 1 85 ? 14.448  -22.507 18.075  1.00 33.77  ? 84  ILE C CA  1 
ATOM   2070 C C   . ILE C 1 85 ? 14.507  -20.998 17.811  1.00 34.45  ? 84  ILE C C   1 
ATOM   2071 O O   . ILE C 1 85 ? 14.983  -20.245 18.648  1.00 36.33  ? 84  ILE C O   1 
ATOM   2072 C CB  . ILE C 1 85 ? 15.747  -23.243 17.727  1.00 34.05  ? 84  ILE C CB  1 
ATOM   2073 C CG1 . ILE C 1 85 ? 16.847  -22.898 18.744  1.00 34.28  ? 84  ILE C CG1 1 
ATOM   2074 C CG2 . ILE C 1 85 ? 16.157  -23.019 16.257  1.00 30.95  ? 84  ILE C CG2 1 
ATOM   2075 C CD1 . ILE C 1 85 ? 18.028  -23.856 18.797  1.00 32.49  ? 84  ILE C CD1 1 
ATOM   2076 N N   . GLN C 1 86 ? 14.008  -20.567 16.646  1.00 30.50  ? 85  GLN C N   1 
ATOM   2077 C CA  . GLN C 1 86 ? 14.087  -19.155 16.280  1.00 33.96  ? 85  GLN C CA  1 
ATOM   2078 C C   . GLN C 1 86 ? 12.902  -18.340 16.805  1.00 38.01  ? 85  GLN C C   1 
ATOM   2079 O O   . GLN C 1 86 ? 13.068  -17.157 17.087  1.00 42.14  ? 85  GLN C O   1 
ATOM   2080 C CB  . GLN C 1 86 ? 14.123  -19.026 14.753  1.00 32.93  ? 85  GLN C CB  1 
ATOM   2081 C CG  . GLN C 1 86 ? 14.348  -17.593 14.262  1.00 32.80  ? 85  GLN C CG  1 
ATOM   2082 C CD  . GLN C 1 86 ? 14.736  -17.541 12.794  1.00 35.44  ? 85  GLN C CD  1 
ATOM   2083 O OE1 . GLN C 1 86 ? 14.616  -18.529 12.049  1.00 37.13  ? 85  GLN C OE1 1 
ATOM   2084 N NE2 . GLN C 1 86 ? 15.291  -16.407 12.385  1.00 38.64  ? 85  GLN C NE2 1 
ATOM   2085 N N   . ASN C 1 87 ? 11.732  -18.955 16.918  1.00 35.26  ? 86  ASN C N   1 
ATOM   2086 C CA  . ASN C 1 87 ? 10.476  -18.240 17.079  1.00 41.44  ? 86  ASN C CA  1 
ATOM   2087 C C   . ASN C 1 87 ? 9.793   -18.571 18.404  1.00 43.89  ? 86  ASN C C   1 
ATOM   2088 O O   . ASN C 1 87 ? 8.925   -17.816 18.828  1.00 45.41  ? 86  ASN C O   1 
ATOM   2089 C CB  . ASN C 1 87 ? 9.461   -18.546 15.983  1.00 40.30  ? 86  ASN C CB  1 
ATOM   2090 C CG  . ASN C 1 87 ? 9.944   -18.028 14.655  1.00 41.57  ? 86  ASN C CG  1 
ATOM   2091 O OD1 . ASN C 1 87 ? 10.004  -16.808 14.474  1.00 41.18  ? 86  ASN C OD1 1 
ATOM   2092 N ND2 . ASN C 1 87 ? 10.345  -18.920 13.756  1.00 34.93  ? 86  ASN C ND2 1 
ATOM   2093 N N   . ASN C 1 88 ? 10.113  -19.717 19.015  1.00 43.11  ? 87  ASN C N   1 
ATOM   2094 C CA  . ASN C 1 88 ? 9.370   -20.117 20.206  1.00 43.17  ? 87  ASN C CA  1 
ATOM   2095 C C   . ASN C 1 88 ? 10.235  -20.980 21.125  1.00 39.92  ? 87  ASN C C   1 
ATOM   2096 O O   . ASN C 1 88 ? 9.798   -22.055 21.547  1.00 47.13  ? 87  ASN C O   1 
ATOM   2097 C CB  . ASN C 1 88 ? 8.055   -20.802 19.847  1.00 46.45  ? 87  ASN C CB  1 
ATOM   2098 C CG  . ASN C 1 88 ? 7.100   -20.818 21.022  1.00 52.10  ? 87  ASN C CG  1 
ATOM   2099 O OD1 . ASN C 1 88 ? 7.339   -20.132 22.029  1.00 54.94  ? 87  ASN C OD1 1 
ATOM   2100 N ND2 . ASN C 1 88 ? 6.024   -21.582 20.907  1.00 48.04  ? 87  ASN C ND2 1 
ATOM   2101 N N   . PRO C 1 89 ? 11.472  -20.550 21.445  1.00 40.04  ? 88  PRO C N   1 
ATOM   2102 C CA  . PRO C 1 89 ? 12.457  -21.448 22.058  1.00 39.06  ? 88  PRO C CA  1 
ATOM   2103 C C   . PRO C 1 89 ? 12.182  -21.887 23.495  1.00 44.37  ? 88  PRO C C   1 
ATOM   2104 O O   . PRO C 1 89 ? 12.776  -22.862 23.961  1.00 39.05  ? 88  PRO C O   1 
ATOM   2105 C CB  . PRO C 1 89 ? 13.772  -20.693 21.927  1.00 38.58  ? 88  PRO C CB  1 
ATOM   2106 C CG  . PRO C 1 89 ? 13.332  -19.234 21.935  1.00 44.88  ? 88  PRO C CG  1 
ATOM   2107 C CD  . PRO C 1 89 ? 12.023  -19.218 21.163  1.00 40.48  ? 88  PRO C CD  1 
ATOM   2108 N N   . HIS C 1 90 ? 11.243  -21.208 24.165  1.00 46.69  ? 89  HIS C N   1 
ATOM   2109 C CA  . HIS C 1 90 ? 11.010  -21.506 25.573  1.00 48.74  ? 89  HIS C CA  1 
ATOM   2110 C C   . HIS C 1 90 ? 9.563   -21.918 25.863  1.00 53.89  ? 89  HIS C C   1 
ATOM   2111 O O   . HIS C 1 90 ? 9.151   -21.913 27.019  1.00 64.04  ? 89  HIS C O   1 
ATOM   2112 C CB  . HIS C 1 90 ? 11.573  -20.396 26.463  1.00 41.16  ? 89  HIS C CB  1 
ATOM   2113 C CG  . HIS C 1 90 ? 12.999  -20.026 26.206  1.00 38.16  ? 89  HIS C CG  1 
ATOM   2114 N ND1 . HIS C 1 90 ? 13.387  -18.803 25.699  1.00 42.86  ? 89  HIS C ND1 1 
ATOM   2115 C CD2 . HIS C 1 90 ? 14.141  -20.695 26.452  1.00 41.28  ? 89  HIS C CD2 1 
ATOM   2116 C CE1 . HIS C 1 90 ? 14.713  -18.755 25.595  1.00 41.60  ? 89  HIS C CE1 1 
ATOM   2117 N NE2 . HIS C 1 90 ? 15.197  -19.897 26.066  1.00 44.99  ? 89  HIS C NE2 1 
ATOM   2118 N N   . ALA C 1 91 ? 8.798   -22.322 24.842  1.00 56.05  ? 90  ALA C N   1 
ATOM   2119 C CA  . ALA C 1 91 ? 7.463   -22.871 25.059  1.00 54.63  ? 90  ALA C CA  1 
ATOM   2120 C C   . ALA C 1 91 ? 7.558   -24.282 25.647  1.00 62.55  ? 90  ALA C C   1 
ATOM   2121 O O   . ALA C 1 91 ? 8.641   -24.866 25.695  1.00 67.92  ? 90  ALA C O   1 
ATOM   2122 C CB  . ALA C 1 91 ? 6.654   -22.853 23.783  1.00 53.34  ? 90  ALA C CB  1 
ATOM   2123 N N   . SER C 1 92 ? 6.404   -24.829 26.065  1.00 70.93  ? 91  SER C N   1 
ATOM   2124 C CA  . SER C 1 92 ? 6.302   -26.102 26.772  1.00 71.76  ? 91  SER C CA  1 
ATOM   2125 C C   . SER C 1 92 ? 6.745   -27.278 25.906  1.00 68.98  ? 91  SER C C   1 
ATOM   2126 O O   . SER C 1 92 ? 7.798   -27.855 26.147  1.00 78.54  ? 91  SER C O   1 
ATOM   2127 C CB  . SER C 1 92 ? 4.901   -26.334 27.293  1.00 68.85  ? 91  SER C CB  1 
ATOM   2128 O OG  . SER C 1 92 ? 4.641   -25.487 28.397  1.00 75.33  ? 91  SER C OG  1 
ATOM   2129 N N   . TYR C 1 93 ? 5.905   -27.642 24.928  1.00 71.36  ? 92  TYR C N   1 
ATOM   2130 C CA  . TYR C 1 93 ? 6.067   -28.835 24.107  1.00 75.47  ? 92  TYR C CA  1 
ATOM   2131 C C   . TYR C 1 93 ? 5.944   -30.082 24.993  1.00 82.35  ? 92  TYR C C   1 
ATOM   2132 O O   . TYR C 1 93 ? 4.855   -30.277 25.581  1.00 92.88  ? 92  TYR C O   1 
ATOM   2133 C CB  . TYR C 1 93 ? 7.377   -28.838 23.309  1.00 68.60  ? 92  TYR C CB  1 
ATOM   2134 C CG  . TYR C 1 93 ? 7.676   -27.556 22.540  1.00 61.81  ? 92  TYR C CG  1 
ATOM   2135 C CD1 . TYR C 1 93 ? 7.022   -27.260 21.345  1.00 56.53  ? 92  TYR C CD1 1 
ATOM   2136 C CD2 . TYR C 1 93 ? 8.628   -26.651 23.001  1.00 60.88  ? 92  TYR C CD2 1 
ATOM   2137 C CE1 . TYR C 1 93 ? 7.288   -26.094 20.645  1.00 58.88  ? 92  TYR C CE1 1 
ATOM   2138 C CE2 . TYR C 1 93 ? 8.908   -25.484 22.304  1.00 61.26  ? 92  TYR C CE2 1 
ATOM   2139 C CZ  . TYR C 1 93 ? 8.240   -25.206 21.124  1.00 61.13  ? 92  TYR C CZ  1 
ATOM   2140 O OH  . TYR C 1 93 ? 8.516   -24.051 20.438  1.00 65.36  ? 92  TYR C OH  1 
HETATM 2141 S S   . SO4 D 2 .  ? 1.487   -33.869 1.863   1.00 103.72 ? 101 SO4 A S   1 
HETATM 2142 O O1  . SO4 D 2 .  ? 2.327   -34.458 0.852   1.00 81.22  ? 101 SO4 A O1  1 
HETATM 2143 O O2  . SO4 D 2 .  ? 1.425   -32.441 1.679   1.00 94.33  ? 101 SO4 A O2  1 
HETATM 2144 O O3  . SO4 D 2 .  ? 0.161   -34.430 1.763   1.00 111.17 ? 101 SO4 A O3  1 
HETATM 2145 O O4  . SO4 D 2 .  ? 2.032   -34.156 3.162   1.00 101.04 ? 101 SO4 A O4  1 
HETATM 2146 S S   . SO4 E 2 .  ? -9.016  -24.678 1.401   1.00 92.10  ? 102 SO4 A S   1 
HETATM 2147 O O1  . SO4 E 2 .  ? -9.824  -24.242 0.287   1.00 82.44  ? 102 SO4 A O1  1 
HETATM 2148 O O2  . SO4 E 2 .  ? -9.159  -23.754 2.498   1.00 84.65  ? 102 SO4 A O2  1 
HETATM 2149 O O3  . SO4 E 2 .  ? -9.423  -25.996 1.821   1.00 90.07  ? 102 SO4 A O3  1 
HETATM 2150 O O4  . SO4 E 2 .  ? -7.638  -24.722 1.004   1.00 102.87 ? 102 SO4 A O4  1 
HETATM 2151 C C1  . EDO F 3 .  ? 14.166  -19.614 -7.494  1.00 38.94  ? 103 EDO A C1  1 
HETATM 2152 O O1  . EDO F 3 .  ? 15.328  -18.833 -7.242  1.00 30.33  ? 103 EDO A O1  1 
HETATM 2153 C C2  . EDO F 3 .  ? 13.280  -19.069 -8.573  1.00 34.65  ? 103 EDO A C2  1 
HETATM 2154 O O2  . EDO F 3 .  ? 12.810  -17.771 -8.292  1.00 32.57  ? 103 EDO A O2  1 
HETATM 2155 S S   . SO4 G 2 .  ? 9.209   -29.531 5.760   1.00 54.15  ? 104 SO4 A S   1 
HETATM 2156 O O1  . SO4 G 2 .  ? 10.077  -28.766 4.935   1.00 48.95  ? 104 SO4 A O1  1 
HETATM 2157 O O2  . SO4 G 2 .  ? 8.683   -30.645 4.986   1.00 56.91  ? 104 SO4 A O2  1 
HETATM 2158 O O3  . SO4 G 2 .  ? 9.942   -30.031 6.910   1.00 56.97  ? 104 SO4 A O3  1 
HETATM 2159 O O4  . SO4 G 2 .  ? 8.103   -28.715 6.182   1.00 64.26  ? 104 SO4 A O4  1 
HETATM 2160 S S   . SO4 H 2 .  ? 7.467   -8.493  -24.840 1.00 71.60  ? 101 SO4 B S   1 
HETATM 2161 O O1  . SO4 H 2 .  ? 8.599   -8.519  -25.746 1.00 37.62  ? 101 SO4 B O1  1 
HETATM 2162 O O2  . SO4 H 2 .  ? 6.326   -9.124  -25.470 1.00 52.98  ? 101 SO4 B O2  1 
HETATM 2163 O O3  . SO4 H 2 .  ? 7.719   -9.203  -23.582 1.00 41.99  ? 101 SO4 B O3  1 
HETATM 2164 O O4  . SO4 H 2 .  ? 7.225   -7.087  -24.572 1.00 59.80  ? 101 SO4 B O4  1 
HETATM 2165 S S   . SO4 I 2 .  ? 14.625  -27.020 -26.491 1.00 48.86  ? 102 SO4 B S   1 
HETATM 2166 O O1  . SO4 I 2 .  ? 15.855  -26.407 -26.068 1.00 53.68  ? 102 SO4 B O1  1 
HETATM 2167 O O2  . SO4 I 2 .  ? 14.926  -28.300 -27.096 1.00 58.01  ? 102 SO4 B O2  1 
HETATM 2168 O O3  . SO4 I 2 .  ? 13.775  -27.215 -25.352 1.00 62.59  ? 102 SO4 B O3  1 
HETATM 2169 O O4  . SO4 I 2 .  ? 13.943  -26.178 -27.440 1.00 49.95  ? 102 SO4 B O4  1 
HETATM 2170 N N1  . VVG J 4 .  ? 18.512  -15.228 -23.150 0.69 31.68  ? 103 VVG B N1  1 
HETATM 2171 C C4  . VVG J 4 .  ? 20.634  -14.972 -24.379 0.69 32.61  ? 103 VVG B C4  1 
HETATM 2172 C C5  . VVG J 4 .  ? 22.017  -15.051 -24.392 0.69 34.91  ? 103 VVG B C5  1 
HETATM 2173 C C6  . VVG J 4 .  ? 22.716  -15.323 -23.227 0.69 38.77  ? 103 VVG B C6  1 
HETATM 2174 C C7  . VVG J 4 .  ? 22.036  -15.515 -22.036 0.69 39.75  ? 103 VVG B C7  1 
HETATM 2175 C C8  . VVG J 4 .  ? 20.667  -15.417 -22.043 0.69 41.43  ? 103 VVG B C8  1 
HETATM 2176 C C1  . VVG J 4 .  ? 17.056  -16.547 -26.250 0.69 26.51  ? 103 VVG B C1  1 
HETATM 2177 C C2  . VVG J 4 .  ? 16.633  -16.255 -24.849 0.69 30.91  ? 103 VVG B C2  1 
HETATM 2178 S S1  . VVG J 4 .  ? 17.334  -14.760 -24.177 0.69 27.06  ? 103 VVG B S1  1 
HETATM 2179 O O1  . VVG J 4 .  ? 16.251  -14.431 -23.313 0.69 26.09  ? 103 VVG B O1  1 
HETATM 2180 O O2  . VVG J 4 .  ? 17.787  -13.784 -25.116 0.69 28.80  ? 103 VVG B O2  1 
HETATM 2181 C C3  . VVG J 4 .  ? 19.930  -15.162 -23.188 0.69 35.52  ? 103 VVG B C3  1 
HETATM 2182 F F1  . VVG J 4 .  ? 19.986  -15.565 -20.877 0.69 42.89  ? 103 VVG B F1  1 
HETATM 2183 C C1  . EDO K 3 .  ? 16.831  -36.530 16.454  1.00 36.25  ? 101 EDO C C1  1 
HETATM 2184 O O1  . EDO K 3 .  ? 15.764  -37.143 15.726  1.00 35.74  ? 101 EDO C O1  1 
HETATM 2185 C C2  . EDO K 3 .  ? 16.395  -35.468 17.402  1.00 35.02  ? 101 EDO C C2  1 
HETATM 2186 O O2  . EDO K 3 .  ? 15.551  -36.024 18.336  1.00 33.73  ? 101 EDO C O2  1 
HETATM 2187 S S   . SO4 L 2 .  ? 29.347  -38.629 12.363  1.00 92.41  ? 102 SO4 C S   1 
HETATM 2188 O O1  . SO4 L 2 .  ? 30.301  -37.796 11.673  1.00 94.21  ? 102 SO4 C O1  1 
HETATM 2189 O O2  . SO4 L 2 .  ? 28.022  -38.148 12.098  1.00 81.87  ? 102 SO4 C O2  1 
HETATM 2190 O O3  . SO4 L 2 .  ? 29.462  -39.988 11.908  1.00 75.92  ? 102 SO4 C O3  1 
HETATM 2191 O O4  . SO4 L 2 .  ? 29.602  -38.576 13.781  1.00 94.90  ? 102 SO4 C O4  1 
HETATM 2192 O O   . HOH M 5 .  ? 8.901   -32.349 4.090   1.00 50.07  ? 201 HOH A O   1 
HETATM 2193 O O   . HOH M 5 .  ? -5.632  -13.299 -16.608 1.00 46.41  ? 202 HOH A O   1 
HETATM 2194 O O   . HOH M 5 .  ? -2.340  -11.725 13.761  1.00 47.63  ? 203 HOH A O   1 
HETATM 2195 O O   . HOH M 5 .  ? 5.856   -29.121 6.783   1.00 51.49  ? 204 HOH A O   1 
HETATM 2196 O O   . HOH M 5 .  ? 3.942   -34.866 4.458   1.00 58.44  ? 205 HOH A O   1 
HETATM 2197 O O   . HOH M 5 .  ? 0.762   -10.587 -15.415 1.00 45.18  ? 206 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? 10.795  -9.306  -13.404 1.00 64.15  ? 207 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? -2.206  -30.954 -3.654  1.00 53.93  ? 208 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? -7.460  -14.090 6.754   1.00 74.52  ? 209 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? 11.222  -29.742 2.916   1.00 45.14  ? 210 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 4.278   -10.471 13.464  1.00 57.69  ? 211 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? -6.494  -25.519 -5.622  1.00 54.58  ? 212 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? 16.032  -24.650 1.911   1.00 40.63  ? 213 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? 0.020   -33.631 4.657   1.00 59.15  ? 214 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 7.196   -10.626 -12.060 1.00 34.95  ? 215 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 13.119  -12.041 8.003   1.00 52.64  ? 216 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 4.828   -7.935  1.164   1.00 34.95  ? 217 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 9.287   -18.253 -10.990 1.00 35.57  ? 218 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 11.375  -23.813 9.686   1.00 37.06  ? 219 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 8.267   -17.981 -15.948 1.00 54.32  ? 220 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? 14.175  -15.692 -9.259  1.00 37.13  ? 221 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 14.751  -17.573 -19.216 1.00 42.92  ? 222 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 1.435   -24.768 13.930  1.00 50.59  ? 223 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 9.410   -18.532 9.582   1.00 47.89  ? 224 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 4.677   -3.548  -3.233  1.00 30.40  ? 225 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? -2.186  3.310   -2.125  1.00 39.78  ? 226 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 20.050  -15.585 7.233   1.00 29.91  ? 227 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -7.629  -17.227 6.714   1.00 41.07  ? 228 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? -3.613  -10.810 6.720   1.00 37.84  ? 229 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 13.370  -28.033 -4.871  1.00 47.02  ? 230 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? -0.427  -21.006 6.916   1.00 32.76  ? 231 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? -7.835  -15.776 -1.033  1.00 36.41  ? 232 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? -0.499  -29.539 9.915   1.00 53.05  ? 233 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 11.702  -12.033 5.868   1.00 33.32  ? 234 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 9.829   -6.025  -1.617  1.00 31.97  ? 235 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 11.029  -5.169  -7.809  1.00 34.55  ? 236 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? -4.026  -21.300 6.069   1.00 38.21  ? 237 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? 16.723  -12.158 -17.118 1.00 38.59  ? 238 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? -0.465  -20.584 11.210  1.00 58.76  ? 239 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 8.179   -17.479 8.524   1.00 39.46  ? 240 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 2.584   -25.190 -10.041 1.00 35.19  ? 241 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 3.351   -29.646 -0.530  1.00 36.51  ? 242 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 13.067  -9.569  -7.262  1.00 42.81  ? 243 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 11.846  -16.455 -14.796 1.00 41.07  ? 244 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 2.025   -4.615  -10.202 1.00 34.88  ? 245 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? -1.603  -22.032 -0.655  1.00 26.51  ? 246 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 1.903   0.577   -7.440  1.00 38.36  ? 247 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 9.659   -20.168 -18.530 1.00 40.80  ? 248 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 13.449  -12.077 -4.234  1.00 21.70  ? 249 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 2.410   -25.201 -6.512  1.00 52.13  ? 250 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? -5.571  -15.960 -8.086  1.00 28.20  ? 251 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 17.344  -12.904 1.371   1.00 21.30  ? 252 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 11.674  -12.414 -6.173  1.00 26.83  ? 253 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? -5.560  -19.735 -5.720  1.00 37.45  ? 254 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? -1.130  -7.549  11.415  1.00 44.50  ? 255 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 0.387   -23.441 9.205   1.00 46.39  ? 256 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 10.185  -13.190 9.680   1.00 39.96  ? 257 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 15.864  -12.046 -5.365  1.00 35.09  ? 258 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 1.405   -18.400 -18.716 1.00 47.22  ? 259 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? -1.302  -11.836 11.304  1.00 36.14  ? 260 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 11.441  -6.008  -3.857  1.00 45.62  ? 261 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 9.863   -30.527 9.760   1.00 33.61  ? 262 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 12.748  -13.330 -8.585  1.00 43.89  ? 263 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? -7.707  -16.668 1.663   1.00 43.01  ? 264 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? -6.107  -11.620 -11.360 1.00 41.45  ? 265 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 8.930   -16.301 -13.214 1.00 36.90  ? 266 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? -7.054  -21.652 -5.915  1.00 50.82  ? 267 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? -8.409  -21.121 -1.232  1.00 38.57  ? 268 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 8.137   -7.871  1.215   1.00 28.71  ? 269 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? -8.642  -16.083 -12.688 1.00 50.00  ? 270 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? 1.894   -10.564 11.668  1.00 35.82  ? 271 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? -5.917  -12.818 6.692   1.00 38.31  ? 272 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? 6.840   -6.035  0.509   1.00 46.89  ? 273 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 6.459   -16.181 -14.919 1.00 48.64  ? 274 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? -4.202  -25.871 -5.597  1.00 43.15  ? 275 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 5.217   -7.544  3.967   1.00 35.51  ? 276 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 3.121   -9.860  -13.144 1.00 46.89  ? 277 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? 11.208  -7.926  0.381   1.00 26.38  ? 278 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 14.671  -29.520 3.884   1.00 39.36  ? 279 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? -3.830  -26.469 7.663   1.00 58.33  ? 280 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 15.286  -13.401 10.523  1.00 50.69  ? 281 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? -8.049  -19.553 -3.379  1.00 51.18  ? 282 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 21.570  -16.778 -3.444  1.00 30.52  ? 283 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 22.432  -16.696 -0.512  1.00 40.18  ? 284 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? -7.079  -11.538 -8.020  1.00 29.20  ? 285 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 9.670   -2.704  -0.317  1.00 68.32  ? 286 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 10.702  -27.711 -7.408  1.00 53.13  ? 287 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 13.361  -15.169 -12.216 1.00 48.65  ? 288 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 17.242  -18.221 -9.801  1.00 48.29  ? 289 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -3.670  -7.873  10.618  1.00 46.10  ? 290 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? -10.991 -16.152 -3.746  1.00 53.91  ? 291 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? 17.492  -13.857 10.697  1.00 47.87  ? 292 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 15.563  -28.371 -1.089  1.00 52.27  ? 293 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -5.364  -17.333 -16.005 1.00 55.28  ? 294 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -5.529  -23.598 -6.868  1.00 43.76  ? 295 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? -5.738  -26.550 3.555   1.00 47.57  ? 296 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 1.335   -29.618 -7.074  1.00 57.19  ? 297 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 8.816   -9.064  -13.825 1.00 38.69  ? 298 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? -3.652  -11.036 9.536   1.00 48.01  ? 299 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? 4.996   -6.976  -10.935 1.00 47.55  ? 300 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? -0.215  -3.457  -11.142 1.00 57.82  ? 301 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? 11.939  -21.360 10.533  1.00 41.83  ? 302 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? -9.793  -28.443 -1.673  1.00 50.46  ? 303 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? -7.095  -14.062 -9.269  1.00 40.69  ? 304 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 11.642  -2.059  -2.049  1.00 45.23  ? 305 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? -6.010  -22.718 5.735   1.00 61.85  ? 306 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? 7.876   -30.635 -1.758  1.00 58.60  ? 307 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? -2.926  -21.532 7.742   1.00 49.91  ? 308 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 15.284  -13.738 -12.614 1.00 49.79  ? 309 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? 4.899   -9.625  -11.351 1.00 43.13  ? 310 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? 8.261   -8.317  4.460   1.00 36.42  ? 311 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? -11.179 -13.599 -2.962  1.00 45.37  ? 312 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? -9.571  -21.638 -6.197  1.00 49.77  ? 313 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? -6.872  -19.249 8.524   1.00 49.53  ? 314 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? 8.545   -22.507 -19.405 1.00 52.56  ? 315 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? -4.875  -21.063 -8.332  1.00 57.45  ? 316 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? 4.865   -3.193  1.528   1.00 79.50  ? 317 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? -12.951 -25.171 -4.473  1.00 64.09  ? 318 HOH A O   1 
HETATM 2310 O O   . HOH N 5 .  ? 30.503  -7.847  -30.174 1.00 45.68  ? 201 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 20.040  -22.054 -23.227 1.00 54.37  ? 202 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 22.090  -3.414  -24.520 1.00 65.83  ? 203 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 10.067  -11.234 -38.107 1.00 50.57  ? 204 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 25.161  -5.022  -29.884 1.00 38.48  ? 205 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 12.967  -4.506  -41.878 1.00 43.59  ? 206 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 21.096  -25.998 -30.256 1.00 58.42  ? 207 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 30.047  -12.704 -45.839 1.00 78.02  ? 208 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 30.407  -19.789 -40.416 1.00 35.78  ? 209 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 27.922  -8.110  -28.930 1.00 40.32  ? 210 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 11.337  -8.099  -41.452 1.00 46.56  ? 211 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 26.244  -22.964 -31.233 1.00 37.95  ? 212 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 6.645   -12.184 -26.196 1.00 38.14  ? 213 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 23.434  -2.218  -29.195 1.00 42.50  ? 214 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 10.327  -19.710 -43.085 1.00 49.81  ? 215 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 18.804  -0.021  -25.555 1.00 57.99  ? 216 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 24.441  -1.776  -36.291 1.00 45.27  ? 217 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 8.380   -27.677 -38.547 1.00 59.76  ? 218 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 17.751  -19.712 -42.189 1.00 49.96  ? 219 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 25.925  -4.394  -33.749 1.00 48.41  ? 220 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 20.682  -13.332 -42.852 1.00 37.35  ? 221 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 3.320   -8.771  -27.172 1.00 54.81  ? 222 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 21.786  2.974   -26.752 1.00 54.93  ? 223 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 26.284  -0.276  -29.227 1.00 51.52  ? 224 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 23.657  -11.050 -21.961 1.00 38.01  ? 225 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 10.571  -18.846 -33.015 1.00 27.67  ? 226 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 21.624  3.686   -32.616 1.00 42.70  ? 227 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 25.363  -5.898  -35.911 1.00 42.47  ? 228 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 32.252  -11.808 -42.000 1.00 44.23  ? 229 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 8.950   -8.722  -16.505 1.00 42.13  ? 230 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 16.778  -19.244 -28.885 1.00 24.04  ? 231 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 13.322  -22.224 -20.769 1.00 54.94  ? 232 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 19.923  -25.531 -34.130 1.00 38.58  ? 233 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 6.054   -7.344  -32.409 1.00 50.09  ? 234 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 17.628  -15.659 -20.489 1.00 47.23  ? 235 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 10.345  -16.806 -44.342 1.00 45.33  ? 236 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 18.116  -0.478  -38.532 1.00 27.70  ? 237 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 7.198   -19.218 -35.003 1.00 45.91  ? 238 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 4.601   -18.987 -25.739 1.00 55.61  ? 239 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 28.095  -17.451 -25.069 1.00 41.32  ? 240 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 34.810  -23.200 -29.949 1.00 63.38  ? 241 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 22.862  -22.975 -28.813 1.00 38.94  ? 242 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 31.783  -12.303 -38.990 1.00 55.73  ? 243 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 23.783  -4.127  -36.920 1.00 30.20  ? 244 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 32.615  -18.863 -42.473 1.00 44.27  ? 245 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 14.295  -6.407  -41.245 1.00 39.44  ? 246 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 20.449  -10.060 -43.023 1.00 36.67  ? 247 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 27.272  -10.453 -28.992 1.00 50.74  ? 248 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 14.734  -24.433 -40.399 1.00 40.55  ? 249 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 7.623   -8.058  -20.903 1.00 49.09  ? 250 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 10.695  -21.890 -32.840 1.00 34.56  ? 251 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 7.797   -18.411 -31.758 1.00 46.42  ? 252 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 31.882  -21.125 -38.277 1.00 40.31  ? 253 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 3.953   -19.299 -30.943 1.00 53.98  ? 254 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 21.100  -6.379  -42.635 1.00 37.37  ? 255 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 7.521   -12.434 -38.934 1.00 47.05  ? 256 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 12.336  -4.629  -24.850 1.00 47.46  ? 257 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 27.856  -24.725 -35.145 1.00 34.72  ? 258 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 17.877  -3.558  -22.066 1.00 51.88  ? 259 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 17.011  -9.499  -44.013 1.00 48.00  ? 260 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 18.504  -25.880 -28.851 1.00 40.46  ? 261 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 20.115  -7.909  -21.187 1.00 48.91  ? 262 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 24.848  -6.618  -42.745 1.00 49.04  ? 263 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 1.729   -13.148 -28.306 1.00 46.93  ? 264 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 6.529   -20.675 -25.048 1.00 40.22  ? 265 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 18.136  -15.962 -45.883 1.00 46.59  ? 266 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 18.433  4.601   -34.358 1.00 36.69  ? 267 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 18.663  -13.262 -44.658 1.00 45.90  ? 268 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 20.312  3.927   -33.111 1.00 38.60  ? 269 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 9.822   -6.062  -41.135 1.00 48.73  ? 270 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 39.156  -13.115 -39.168 1.00 62.95  ? 271 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 15.215  -8.012  -43.100 1.00 42.01  ? 272 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 16.720  -0.586  -25.601 1.00 56.65  ? 273 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 17.398  -25.338 -20.815 1.00 61.01  ? 274 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 31.586  -11.621 -36.888 1.00 51.86  ? 275 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 13.067  -19.899 -19.481 1.00 52.58  ? 276 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 24.522  -4.145  -28.253 1.00 56.78  ? 277 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 16.659  1.938   -30.465 1.00 64.66  ? 278 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 11.517  -24.052 -29.914 1.00 47.46  ? 279 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 13.819  -5.789  -18.082 1.00 58.48  ? 280 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 15.200  -21.872 -41.922 1.00 51.27  ? 281 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 7.445   -9.926  -18.645 1.00 43.18  ? 282 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 22.538  -29.331 -35.613 1.00 41.56  ? 283 HOH B O   1 
HETATM 2393 O O   . HOH O 5 .  ? 27.126  -38.002 10.266  1.00 37.94  ? 201 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 26.625  -39.511 12.721  1.00 39.23  ? 202 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 27.248  -25.525 31.526  1.00 94.84  ? 203 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 20.106  -20.408 30.306  1.00 77.51  ? 204 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 13.301  -20.010 10.925  1.00 57.84  ? 205 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 14.843  -39.157 16.804  1.00 55.34  ? 206 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 19.386  -20.337 10.510  1.00 39.24  ? 207 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 12.226  -28.523 28.117  1.00 54.97  ? 208 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 13.041  -31.653 8.088   1.00 30.80  ? 209 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 31.838  -33.535 25.819  1.00 46.79  ? 210 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 17.497  -17.254 15.009  1.00 43.71  ? 211 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 23.152  -41.757 18.517  1.00 39.44  ? 212 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 27.906  -37.722 25.066  1.00 51.45  ? 213 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 27.426  -19.199 12.952  1.00 59.91  ? 214 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 7.904   -31.747 11.996  1.00 53.52  ? 215 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 25.765  -19.683 6.392   1.00 36.81  ? 216 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 20.136  -42.079 12.175  1.00 27.70  ? 217 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 30.463  -40.650 9.547   1.00 38.55  ? 218 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 5.900   -26.663 16.844  1.00 50.63  ? 219 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 22.853  -18.629 21.601  1.00 54.08  ? 220 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 14.839  -37.333 13.201  1.00 39.90  ? 221 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 15.320  -21.165 12.199  1.00 38.95  ? 222 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 16.456  -38.013 19.951  1.00 47.36  ? 223 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 25.731  -33.952 34.744  1.00 49.06  ? 224 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 15.932  -17.788 19.348  1.00 44.50  ? 225 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 19.417  -26.816 3.146   1.00 53.02  ? 226 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 25.878  -17.631 13.888  1.00 45.07  ? 227 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 28.262  -37.430 15.959  1.00 41.98  ? 228 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 7.137   -18.088 10.772  1.00 41.69  ? 229 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 22.308  -28.708 11.091  1.00 33.65  ? 230 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 33.430  -24.503 31.625  1.00 50.94  ? 231 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 30.505  -31.610 15.832  1.00 52.81  ? 232 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 30.936  -29.207 12.201  1.00 50.41  ? 233 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 20.106  -41.320 39.144  1.00 67.39  ? 234 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 20.992  -28.910 8.414   1.00 34.71  ? 235 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 29.902  -39.986 31.356  1.00 38.61  ? 236 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 25.395  -31.488 10.759  1.00 37.99  ? 237 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 22.239  -34.537 16.513  1.00 25.37  ? 238 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 9.272   -18.977 23.683  1.00 46.62  ? 239 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 9.549   -37.565 17.901  1.00 53.69  ? 240 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 31.414  -39.926 27.219  1.00 43.74  ? 241 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 20.833  -40.129 26.480  1.00 38.99  ? 242 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 30.589  -17.487 9.752   1.00 46.97  ? 243 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 31.580  -43.605 15.828  1.00 50.78  ? 244 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 14.276  -38.840 9.286   1.00 56.32  ? 245 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 20.209  -19.207 24.795  1.00 50.67  ? 246 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 25.650  -39.778 20.232  1.00 36.13  ? 247 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 28.336  -15.031 12.971  1.00 62.60  ? 248 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 21.343  -29.675 4.723   1.00 60.32  ? 249 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 25.116  -18.224 21.393  1.00 58.55  ? 250 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 30.635  -35.700 28.576  1.00 52.23  ? 251 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 16.342  -38.493 11.584  1.00 43.72  ? 252 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 17.659  -21.327 12.605  1.00 50.05  ? 253 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 30.448  -32.856 18.183  1.00 45.81  ? 254 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 2.750   -28.585 14.046  1.00 59.94  ? 255 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 31.986  -43.717 12.149  1.00 57.76  ? 256 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 29.787  -25.520 32.595  1.00 58.21  ? 257 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 20.838  -13.114 13.250  1.00 47.78  ? 258 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 17.260  -36.831 29.193  1.00 60.22  ? 259 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 29.254  -41.790 27.260  1.00 40.31  ? 260 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 13.329  -22.937 27.956  1.00 77.14  ? 261 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 25.314  -36.448 10.035  1.00 55.83  ? 262 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 22.635  -14.102 13.433  1.00 49.54  ? 263 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 5.140   -24.341 18.571  1.00 61.72  ? 264 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 24.019  -15.919 11.929  1.00 42.84  ? 265 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 27.238  -39.758 24.177  1.00 56.74  ? 266 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 21.969  -43.375 36.686  1.00 58.21  ? 267 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 9.155   -35.951 14.215  1.00 51.58  ? 268 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 15.106  -34.513 35.534  1.00 63.09  ? 269 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 28.950  -18.232 29.120  1.00 57.40  ? 270 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 28.476  -41.785 29.808  1.00 42.49  ? 271 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 33.614  -44.706 15.270  1.00 38.37  ? 272 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 18.194  -16.513 27.472  1.00 53.23  ? 273 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 37.449  -25.556 26.431  1.00 75.24  ? 274 HOH C O   1 
# 
