data_7HGU
# 
_entry.id   7HGU 
# 
_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   7HGU         pdb_00007hgu 10.2210/pdb7hgu/pdb 
WWPDB D_1001407456 ?            ?                   
# 
_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                        7HGU 
_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-cycloheptyl-N-methylmethanesulfonamide           205.318   1   ? ?    ? ? 
5 water       nat water                                              18.015    264 ? ?    ? ? 
# 
_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-cycloheptyl-N-methylmethanesulfonamide VVJ 
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 
VVJ non-polymer         . N-cycloheptyl-N-methylmethanesulfonamide ?                 'C9 H19 N O2 S'  205.318 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 ?  ?   ?   B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        VVJ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   VVJ 
_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 VVJ 1   103 101 VVJ 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   202 362 HOH HOH A . 
M 5 HOH 3   203 341 HOH HOH A . 
M 5 HOH 4   204 208 HOH HOH A . 
M 5 HOH 5   205 66  HOH HOH A . 
M 5 HOH 6   206 259 HOH HOH A . 
M 5 HOH 7   207 335 HOH HOH A . 
M 5 HOH 8   208 304 HOH HOH A . 
M 5 HOH 9   209 202 HOH HOH A . 
M 5 HOH 10  210 293 HOH HOH A . 
M 5 HOH 11  211 55  HOH HOH A . 
M 5 HOH 12  212 355 HOH HOH A . 
M 5 HOH 13  213 354 HOH HOH A . 
M 5 HOH 14  214 91  HOH HOH A . 
M 5 HOH 15  215 85  HOH HOH A . 
M 5 HOH 16  216 86  HOH HOH A . 
M 5 HOH 17  217 7   HOH HOH A . 
M 5 HOH 18  218 87  HOH HOH A . 
M 5 HOH 19  219 71  HOH HOH A . 
M 5 HOH 20  220 97  HOH HOH A . 
M 5 HOH 21  221 28  HOH HOH A . 
M 5 HOH 22  222 32  HOH HOH A . 
M 5 HOH 23  223 142 HOH HOH A . 
M 5 HOH 24  224 139 HOH HOH A . 
M 5 HOH 25  225 77  HOH HOH A . 
M 5 HOH 26  226 290 HOH HOH A . 
M 5 HOH 27  227 167 HOH HOH A . 
M 5 HOH 28  228 8   HOH HOH A . 
M 5 HOH 29  229 27  HOH HOH A . 
M 5 HOH 30  230 111 HOH HOH A . 
M 5 HOH 31  231 1   HOH HOH A . 
M 5 HOH 32  232 34  HOH HOH A . 
M 5 HOH 33  233 38  HOH HOH A . 
M 5 HOH 34  234 292 HOH HOH A . 
M 5 HOH 35  235 188 HOH HOH A . 
M 5 HOH 36  236 41  HOH HOH A . 
M 5 HOH 37  237 12  HOH HOH A . 
M 5 HOH 38  238 23  HOH HOH A . 
M 5 HOH 39  239 37  HOH HOH A . 
M 5 HOH 40  240 289 HOH HOH A . 
M 5 HOH 41  241 301 HOH HOH A . 
M 5 HOH 42  242 344 HOH HOH A . 
M 5 HOH 43  243 260 HOH HOH A . 
M 5 HOH 44  244 42  HOH HOH A . 
M 5 HOH 45  245 26  HOH HOH A . 
M 5 HOH 46  246 274 HOH HOH A . 
M 5 HOH 47  247 199 HOH HOH A . 
M 5 HOH 48  248 99  HOH HOH A . 
M 5 HOH 49  249 190 HOH HOH A . 
M 5 HOH 50  250 58  HOH HOH A . 
M 5 HOH 51  251 2   HOH HOH A . 
M 5 HOH 52  252 60  HOH HOH A . 
M 5 HOH 53  253 267 HOH HOH A . 
M 5 HOH 54  254 203 HOH HOH A . 
M 5 HOH 55  255 115 HOH HOH A . 
M 5 HOH 56  256 218 HOH HOH A . 
M 5 HOH 57  257 93  HOH HOH A . 
M 5 HOH 58  258 94  HOH HOH A . 
M 5 HOH 59  259 18  HOH HOH A . 
M 5 HOH 60  260 288 HOH HOH A . 
M 5 HOH 61  261 300 HOH HOH A . 
M 5 HOH 62  262 78  HOH HOH A . 
M 5 HOH 63  263 84  HOH HOH A . 
M 5 HOH 64  264 109 HOH HOH A . 
M 5 HOH 65  265 95  HOH HOH A . 
M 5 HOH 66  266 145 HOH HOH A . 
M 5 HOH 67  267 278 HOH HOH A . 
M 5 HOH 68  268 14  HOH HOH A . 
M 5 HOH 69  269 222 HOH HOH A . 
M 5 HOH 70  270 297 HOH HOH A . 
M 5 HOH 71  271 35  HOH HOH A . 
M 5 HOH 72  272 20  HOH HOH A . 
M 5 HOH 73  273 351 HOH HOH A . 
M 5 HOH 74  274 116 HOH HOH A . 
M 5 HOH 75  275 151 HOH HOH A . 
M 5 HOH 76  276 164 HOH HOH A . 
M 5 HOH 77  277 327 HOH HOH A . 
M 5 HOH 78  278 19  HOH HOH A . 
M 5 HOH 79  279 143 HOH HOH A . 
M 5 HOH 80  280 131 HOH HOH A . 
M 5 HOH 81  281 9   HOH HOH A . 
M 5 HOH 82  282 21  HOH HOH A . 
M 5 HOH 83  283 16  HOH HOH A . 
M 5 HOH 84  284 64  HOH HOH A . 
M 5 HOH 85  285 179 HOH HOH A . 
M 5 HOH 86  286 165 HOH HOH A . 
M 5 HOH 87  287 353 HOH HOH A . 
M 5 HOH 88  288 156 HOH HOH A . 
M 5 HOH 89  289 318 HOH HOH A . 
M 5 HOH 90  290 211 HOH HOH A . 
M 5 HOH 91  291 281 HOH HOH A . 
M 5 HOH 92  292 296 HOH HOH A . 
M 5 HOH 93  293 73  HOH HOH A . 
M 5 HOH 94  294 113 HOH HOH A . 
M 5 HOH 95  295 22  HOH HOH A . 
M 5 HOH 96  296 31  HOH HOH A . 
M 5 HOH 97  297 47  HOH HOH A . 
M 5 HOH 98  298 359 HOH HOH A . 
M 5 HOH 99  299 210 HOH HOH A . 
M 5 HOH 100 300 83  HOH HOH A . 
M 5 HOH 101 301 75  HOH HOH A . 
M 5 HOH 102 302 108 HOH HOH A . 
M 5 HOH 103 303 283 HOH HOH A . 
M 5 HOH 104 304 219 HOH HOH A . 
M 5 HOH 105 305 63  HOH HOH A . 
M 5 HOH 106 306 185 HOH HOH A . 
M 5 HOH 107 307 57  HOH HOH A . 
M 5 HOH 108 308 205 HOH HOH A . 
M 5 HOH 109 309 152 HOH HOH A . 
M 5 HOH 110 310 358 HOH HOH A . 
M 5 HOH 111 311 313 HOH HOH A . 
M 5 HOH 112 312 332 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 215 HOH HOH B . 
N 5 HOH 3   203 242 HOH HOH B . 
N 5 HOH 4   204 249 HOH HOH B . 
N 5 HOH 5   205 258 HOH HOH B . 
N 5 HOH 6   206 272 HOH HOH B . 
N 5 HOH 7   207 89  HOH HOH B . 
N 5 HOH 8   208 356 HOH HOH B . 
N 5 HOH 9   209 98  HOH HOH B . 
N 5 HOH 10  210 360 HOH HOH B . 
N 5 HOH 11  211 348 HOH HOH B . 
N 5 HOH 12  212 123 HOH HOH B . 
N 5 HOH 13  213 69  HOH HOH B . 
N 5 HOH 14  214 59  HOH HOH B . 
N 5 HOH 15  215 329 HOH HOH B . 
N 5 HOH 16  216 320 HOH HOH B . 
N 5 HOH 17  217 117 HOH HOH B . 
N 5 HOH 18  218 96  HOH HOH B . 
N 5 HOH 19  219 261 HOH HOH B . 
N 5 HOH 20  220 172 HOH HOH B . 
N 5 HOH 21  221 54  HOH HOH B . 
N 5 HOH 22  222 137 HOH HOH B . 
N 5 HOH 23  223 119 HOH HOH B . 
N 5 HOH 24  224 10  HOH HOH B . 
N 5 HOH 25  225 17  HOH HOH B . 
N 5 HOH 26  226 68  HOH HOH B . 
N 5 HOH 27  227 352 HOH HOH B . 
N 5 HOH 28  228 5   HOH HOH B . 
N 5 HOH 29  229 6   HOH HOH B . 
N 5 HOH 30  230 169 HOH HOH B . 
N 5 HOH 31  231 280 HOH HOH B . 
N 5 HOH 32  232 72  HOH HOH B . 
N 5 HOH 33  233 279 HOH HOH B . 
N 5 HOH 34  234 76  HOH HOH B . 
N 5 HOH 35  235 25  HOH HOH B . 
N 5 HOH 36  236 101 HOH HOH B . 
N 5 HOH 37  237 363 HOH HOH B . 
N 5 HOH 38  238 303 HOH HOH B . 
N 5 HOH 39  239 315 HOH HOH B . 
N 5 HOH 40  240 24  HOH HOH B . 
N 5 HOH 41  241 224 HOH HOH B . 
N 5 HOH 42  242 79  HOH HOH B . 
N 5 HOH 43  243 74  HOH HOH B . 
N 5 HOH 44  244 13  HOH HOH B . 
N 5 HOH 45  245 61  HOH HOH B . 
N 5 HOH 46  246 217 HOH HOH B . 
N 5 HOH 47  247 197 HOH HOH B . 
N 5 HOH 48  248 214 HOH HOH B . 
N 5 HOH 49  249 150 HOH HOH B . 
N 5 HOH 50  250 120 HOH HOH B . 
N 5 HOH 51  251 175 HOH HOH B . 
N 5 HOH 52  252 36  HOH HOH B . 
N 5 HOH 53  253 177 HOH HOH B . 
N 5 HOH 54  254 46  HOH HOH B . 
N 5 HOH 55  255 153 HOH HOH B . 
N 5 HOH 56  256 357 HOH HOH B . 
N 5 HOH 57  257 168 HOH HOH B . 
N 5 HOH 58  258 44  HOH HOH B . 
N 5 HOH 59  259 182 HOH HOH B . 
N 5 HOH 60  260 331 HOH HOH B . 
N 5 HOH 61  261 319 HOH HOH B . 
N 5 HOH 62  262 334 HOH HOH B . 
N 5 HOH 63  263 201 HOH HOH B . 
N 5 HOH 64  264 104 HOH HOH B . 
N 5 HOH 65  265 157 HOH HOH B . 
N 5 HOH 66  266 223 HOH HOH B . 
N 5 HOH 67  267 291 HOH HOH B . 
N 5 HOH 68  268 160 HOH HOH B . 
N 5 HOH 69  269 163 HOH HOH B . 
N 5 HOH 70  270 316 HOH HOH B . 
N 5 HOH 71  271 336 HOH HOH B . 
N 5 HOH 72  272 333 HOH HOH B . 
N 5 HOH 73  273 322 HOH HOH B . 
N 5 HOH 74  274 170 HOH HOH B . 
N 5 HOH 75  275 314 HOH HOH B . 
N 5 HOH 76  276 92  HOH HOH B . 
N 5 HOH 77  277 107 HOH HOH B . 
N 5 HOH 78  278 312 HOH HOH B . 
O 5 HOH 1   201 361 HOH HOH C . 
O 5 HOH 2   202 321 HOH HOH C . 
O 5 HOH 3   203 338 HOH HOH C . 
O 5 HOH 4   204 161 HOH HOH C . 
O 5 HOH 5   205 323 HOH HOH C . 
O 5 HOH 6   206 317 HOH HOH C . 
O 5 HOH 7   207 45  HOH HOH C . 
O 5 HOH 8   208 342 HOH HOH C . 
O 5 HOH 9   209 226 HOH HOH C . 
O 5 HOH 10  210 346 HOH HOH C . 
O 5 HOH 11  211 15  HOH HOH C . 
O 5 HOH 12  212 173 HOH HOH C . 
O 5 HOH 13  213 134 HOH HOH C . 
O 5 HOH 14  214 295 HOH HOH C . 
O 5 HOH 15  215 254 HOH HOH C . 
O 5 HOH 16  216 118 HOH HOH C . 
O 5 HOH 17  217 49  HOH HOH C . 
O 5 HOH 18  218 340 HOH HOH C . 
O 5 HOH 19  219 189 HOH HOH C . 
O 5 HOH 20  220 284 HOH HOH C . 
O 5 HOH 21  221 4   HOH HOH C . 
O 5 HOH 22  222 269 HOH HOH C . 
O 5 HOH 23  223 347 HOH HOH C . 
O 5 HOH 24  224 90  HOH HOH C . 
O 5 HOH 25  225 326 HOH HOH C . 
O 5 HOH 26  226 184 HOH HOH C . 
O 5 HOH 27  227 126 HOH HOH C . 
O 5 HOH 28  228 102 HOH HOH C . 
O 5 HOH 29  229 149 HOH HOH C . 
O 5 HOH 30  230 171 HOH HOH C . 
O 5 HOH 31  231 271 HOH HOH C . 
O 5 HOH 32  232 56  HOH HOH C . 
O 5 HOH 33  233 337 HOH HOH C . 
O 5 HOH 34  234 82  HOH HOH C . 
O 5 HOH 35  235 122 HOH HOH C . 
O 5 HOH 36  236 132 HOH HOH C . 
O 5 HOH 37  237 40  HOH HOH C . 
O 5 HOH 38  238 343 HOH HOH C . 
O 5 HOH 39  239 275 HOH HOH C . 
O 5 HOH 40  240 48  HOH HOH C . 
O 5 HOH 41  241 299 HOH HOH C . 
O 5 HOH 42  242 302 HOH HOH C . 
O 5 HOH 43  243 43  HOH HOH C . 
O 5 HOH 44  244 148 HOH HOH C . 
O 5 HOH 45  245 62  HOH HOH C . 
O 5 HOH 46  246 287 HOH HOH C . 
O 5 HOH 47  247 130 HOH HOH C . 
O 5 HOH 48  248 135 HOH HOH C . 
O 5 HOH 49  249 294 HOH HOH C . 
O 5 HOH 50  250 328 HOH HOH C . 
O 5 HOH 51  251 67  HOH HOH C . 
O 5 HOH 52  252 309 HOH HOH C . 
O 5 HOH 53  253 298 HOH HOH C . 
O 5 HOH 54  254 53  HOH HOH C . 
O 5 HOH 55  255 209 HOH HOH C . 
O 5 HOH 56  256 325 HOH HOH C . 
O 5 HOH 57  257 241 HOH HOH C . 
O 5 HOH 58  258 146 HOH HOH C . 
O 5 HOH 59  259 246 HOH HOH C . 
O 5 HOH 60  260 65  HOH HOH C . 
O 5 HOH 61  261 198 HOH HOH C . 
O 5 HOH 62  262 305 HOH HOH C . 
O 5 HOH 63  263 330 HOH HOH C . 
O 5 HOH 64  264 324 HOH HOH C . 
O 5 HOH 65  265 70  HOH HOH C . 
O 5 HOH 66  266 270 HOH HOH C . 
O 5 HOH 67  267 345 HOH HOH C . 
O 5 HOH 68  268 103 HOH HOH C . 
O 5 HOH 69  269 349 HOH HOH C . 
O 5 HOH 70  270 339 HOH HOH C . 
O 5 HOH 71  271 206 HOH HOH C . 
O 5 HOH 72  272 310 HOH HOH C . 
O 5 HOH 73  273 125 HOH HOH C . 
O 5 HOH 74  274 350 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 34 ? CG  ? B LYS 35 CG  
10 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
11 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
12 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
13 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
14 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
15 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
16 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
17 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
18 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
19 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
20 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
21 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
22 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
23 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
24 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
25 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
26 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
27 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
28 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
29 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
30 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
31 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
32 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
33 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
34 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
35 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
36 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
37 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
38 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
39 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
40 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
41 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
42 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
43 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 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' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGU 
_cell.length_a           41.339 
_cell.length_b           41.771 
_cell.length_c           157.956 
_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                         7HGU 
_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          7HGU 
_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                     7HGU 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             78.98 
_reflns.d_resolution_high            1.67 
_reflns.number_obs                   31334 
_reflns.percent_possible_obs         95.1 
_reflns.pdbx_Rmerge_I_obs            0.075 
_reflns.pdbx_netI_over_sigmaI        8.9 
_reflns.pdbx_redundancy              5.1 
_reflns.pdbx_Rrim_I_all              0.083 
_reflns.pdbx_Rpim_I_all              0.034 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     160070 
_reflns.pdbx_chi_squared             0.81 
_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                  1.67 
_reflns_shell.d_res_low                   1.76 
_reflns_shell.number_measured_all         17998 
_reflns_shell.number_unique_obs           4176 
_reflns_shell.Rmerge_I_obs                1.249 
_reflns_shell.pdbx_chi_squared            0.50 
_reflns_shell.pdbx_redundancy             4.3 
_reflns_shell.percent_possible_obs        88.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.416 
_reflns_shell.pdbx_Rpim_I_all             0.651 
_reflns_shell.pdbx_CC_half                0.444 
_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                                 7HGU 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     29574 
_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                             78.98 
_refine.ls_d_res_high                            1.67 
_refine.ls_percent_reflns_obs                    94.67 
_refine.ls_R_factor_obs                          0.20600 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20298 
_refine.ls_R_factor_R_free                       0.25955 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  1621 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_refine.B_iso_mean                               40.489 
_refine.aniso_B[1][1]                            1.17 
_refine.aniso_B[2][2]                            -0.02 
_refine.aniso_B[3][3]                            -1.15 
_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                       0.124 
_refine.pdbx_overall_ESU_R_Free                  0.130 
_refine.overall_SU_ML                            0.125 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.041 
_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        2144 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             264 
_refine_hist.number_atoms_total               2459 
_refine_hist.d_res_high                       1.67 
_refine_hist.d_res_low                        78.98 
# 
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             0.006  0.012  ? 2297 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.565  1.839  ? 3122 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.275  5.000  ? 264  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.906  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.596 10.000 ? 312  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.126  0.200  ? 288  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1872 '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                  3.364  3.783  ? 1069 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.851  6.751  ? 1329 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.096  4.114  ? 1228 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.577  56.05  ? 3646 '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                       1.666 
_refine_ls_shell.d_res_low                        1.709 
_refine_ls_shell.number_reflns_R_work             1910 
_refine_ls_shell.R_factor_R_work                  0.364 
_refine_ls_shell.percent_reflns_obs               85.14 
_refine_ls_shell.R_factor_R_free                  0.419 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             95 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGU 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z216450634' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGU 
_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 7HGU A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGU B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGU 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 7HGU GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGU SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGU GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGU SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGU GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGU SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O ALA C 52 ? O ALA C 51 N ILE C 43 ? N ILE C 42 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGU 
_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 NE2 C HIS 89  ? ? O C HOH 201 ? ? 1.96 
2  1 O   C HOH 258 ? ? O C HOH 264 ? ? 1.99 
3  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.04 
4  1 O   B HOH 238 ? ? O B HOH 273 ? ? 2.04 
5  1 O2  C SO4 102 ? ? O C HOH 202 ? ? 2.05 
6  1 O   B ASP 27  ? B O B HOH 201 ? ? 2.05 
7  1 OD1 A ASP 62  ? ? O A HOH 202 ? ? 2.06 
8  1 O   B HOH 231 ? ? O B HOH 273 ? ? 2.09 
9  1 OH  C TYR 40  ? ? O C HOH 203 ? ? 2.11 
10 1 O   B HOH 237 ? ? O B HOH 259 ? ? 2.15 
11 1 O   A HOH 207 ? ? O A HOH 295 ? ? 2.18 
12 1 O   B PRO 37  ? ? O B HOH 202 ? ? 2.19 
13 1 O   C THR 47  ? ? O C HOH 204 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     265 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     283 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_545 
_pdbx_validate_symm_contact.dist              1.81 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                110.32 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            10.12 
_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 ? ? -153.98 62.39  
2 1 ASN B 38 ? ? 81.58   -13.67 
3 1 ASN B 87 ? ? -161.58 60.10  
4 1 ASN C 87 ? ? -150.20 57.19  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.73 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ILE 28 ? B ILE 29 
4  1 Y 1 B ALA 29 ? B ALA 30 
5  1 Y 1 B ASP 30 ? B ASP 31 
6  1 Y 1 B GLY 31 ? B GLY 32 
7  1 Y 1 B ALA 32 ? B ALA 33 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C 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 
VVJ N1   N N N 406 
VVJ C4   C N N 407 
VVJ C5   C N N 408 
VVJ C6   C N N 409 
VVJ C7   C N N 410 
VVJ C8   C N N 411 
VVJ C1   C N N 412 
VVJ C2   C N N 413 
VVJ C3   C N N 414 
VVJ S1   S N N 415 
VVJ O1   O N N 416 
VVJ O2   O N N 417 
VVJ C9   C N N 418 
VVJ H1   H N N 419 
VVJ H2   H N N 420 
VVJ H3   H N N 421 
VVJ H4   H N N 422 
VVJ H5   H N N 423 
VVJ H6   H N N 424 
VVJ H7   H N N 425 
VVJ H8   H N N 426 
VVJ H9   H N N 427 
VVJ H10  H N N 428 
VVJ H11  H N N 429 
VVJ H12  H N N 430 
VVJ H13  H N N 431 
VVJ H14  H N N 432 
VVJ H15  H N N 433 
VVJ H16  H N N 434 
VVJ H17  H N N 435 
VVJ H18  H N N 436 
VVJ H19  H N N 437 
# 
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 
VVJ C8  C7   sing N N 389 
VVJ C8  C2   sing N N 390 
VVJ C7  C6   sing N N 391 
VVJ O1  S1   doub N N 392 
VVJ C1  N1   sing N N 393 
VVJ C6  C5   sing N N 394 
VVJ C9  S1   sing N N 395 
VVJ N1  S1   sing N N 396 
VVJ N1  C2   sing N N 397 
VVJ S1  O2   doub N N 398 
VVJ C2  C3   sing N N 399 
VVJ C5  C4   sing N N 400 
VVJ C4  C3   sing N N 401 
VVJ C4  H1   sing N N 402 
VVJ C4  H2   sing N N 403 
VVJ C5  H3   sing N N 404 
VVJ C5  H4   sing N N 405 
VVJ C6  H5   sing N N 406 
VVJ C6  H6   sing N N 407 
VVJ C7  H7   sing N N 408 
VVJ C7  H8   sing N N 409 
VVJ C8  H9   sing N N 410 
VVJ C8  H10  sing N N 411 
VVJ C1  H11  sing N N 412 
VVJ C1  H12  sing N N 413 
VVJ C1  H13  sing N N 414 
VVJ C2  H14  sing N N 415 
VVJ C3  H15  sing N N 416 
VVJ C3  H16  sing N N 417 
VVJ C9  H17  sing N N 418 
VVJ C9  H18  sing N N 419 
VVJ C9  H19  sing N N 420 
# 
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                    7HGU 
_atom_sites.fract_transf_matrix[1][1]   0.024190 
_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]   0.023940 
_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]   0.006331 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 2  ? 0.454   4.259   2.589   1.00 47.71  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.621  3.606   1.795   1.00 54.83  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? -0.030  2.530   0.879   1.00 53.03  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.108   2.643   0.425   1.00 51.05  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.457  4.619   0.999   1.00 56.20  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.578  5.300   1.778   1.00 66.04  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.704  4.358   2.839   1.00 65.84  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -2.716  4.403   4.343   1.00 74.17  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.771  1.420   0.645   1.00 49.05  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.329  0.332   -0.236  1.00 47.67  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? -0.090  0.741   -1.690  1.00 43.86  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.805  1.569   -2.242  1.00 43.07  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.516  -0.673  -0.109  1.00 43.47  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -2.048  -0.407  1.282   1.00 42.93  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -2.045  1.110   1.323   1.00 45.64  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 0.934   0.147   -2.298  1.00 40.49  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.098   0.249   -3.730  1.00 39.10  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.565   -1.050  -4.318  1.00 35.21  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.097   -1.930  -3.587  1.00 33.19  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.588   0.391   -4.081  1.00 47.22  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.280   1.609   -3.552  1.00 61.44  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 2.940   2.274   -2.390  1.00 68.17  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.331   2.274   -4.065  1.00 66.17  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 3.759   3.302   -2.215  1.00 67.37  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.614   3.317   -3.221  1.00 70.51  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.651   -1.168  -5.645  1.00 29.84  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.412   -2.440  -6.289  1.00 31.73  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.542   -3.398  -5.921  1.00 30.84  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.609   -2.978  -5.459  1.00 28.36  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.315   -2.249  -7.786  1.00 35.36  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.274   -4.694  -6.092  1.00 31.07  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.299   -5.702  -5.865  1.00 29.98  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.444   -5.551  -6.872  1.00 32.35  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.221   -5.251  -8.058  1.00 30.17  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.639   -7.077  -6.008  1.00 28.84  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 0.870   -7.528  -4.769  1.00 29.01  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.545   -7.703  -3.556  1.00 28.80  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.506  -7.790  -4.813  1.00 26.45  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 0.881   -8.105  -2.397  1.00 27.73  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -1.165  -8.241  -3.654  1.00 26.23  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.485  -8.374  -2.458  1.00 28.19  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.674   -5.846  -6.404  1.00 28.84  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.839   -5.786  -7.276  1.00 30.39  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.741   -6.997  -7.003  1.00 25.39  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.751   -7.526  -5.891  1.00 26.74  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.561   -4.445  -7.044  1.00 32.79  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.234   -4.356  -5.675  1.00 34.48  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.607   -2.940  -5.231  1.00 39.34  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.340   -3.006  -3.923  1.00 39.35  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.480   -3.366  -2.798  1.00 38.36  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.546   -7.463  -7.985  1.00 27.26  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.499   -8.555  -7.760  1.00 25.94  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.257   -8.259  -6.465  1.00 25.16  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.606   -7.102  -6.213  1.00 26.67  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.415   -8.451  -9.025  1.00 27.29  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.474   -7.933  -10.082 1.00 31.83  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.598   -6.923  -9.363  1.00 29.55  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.445   -9.305  -5.640  1.00 24.45  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.178  -9.245  -4.381  1.00 22.41  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.236   -9.135  -3.178  1.00 22.57  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.604   -9.407  -2.028  1.00 25.04  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 7.976   -8.754  -3.408  1.00 22.20  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.071   -8.662  -2.275  1.00 20.85  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 6.816   -10.039 -1.674  1.00 22.05  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.631   -10.992 -2.407  1.00 21.76  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.728   -8.073  -2.706  1.00 24.45  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.705   -6.560  -2.908  1.00 28.85  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.669   -5.887  -2.484  1.00 30.86  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.722   -6.053  -3.478  1.00 28.56  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.715   -10.113 -0.331  1.00 21.00  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.498   -11.362 0.390   1.00 21.86  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.033   -11.447 0.816   1.00 22.77  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.468   -10.442 1.263   1.00 24.55  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.442   -11.437 1.592   1.00 21.81  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 8.929   -11.254 1.246   1.00 21.67  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.764   -11.398 2.509   1.00 25.79  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.353   -12.229 0.167   1.00 24.35  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.451   -12.659 0.711   1.00 20.49  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.019   -12.854 0.928   1.00 21.35  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.786   -14.238 1.521   1.00 23.61  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.673   -15.091 1.540   1.00 21.26  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.259   -12.728 -0.412  1.00 18.27  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.379   -11.318 -1.010  1.00 21.89  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.683   -13.772 -1.426  1.00 20.03  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.556   -14.452 1.995   1.00 21.36  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 0.983   -15.777 2.017   1.00 24.11  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.008   -15.807 0.849   1.00 25.53  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.746  -14.865 0.660   1.00 26.98  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.214   -15.953 3.338   1.00 24.37  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.169   -16.097 4.516   1.00 23.22  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.561   -14.993 5.261   1.00 26.02  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.640   -17.353 4.872   1.00 25.00  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.449   -15.141 6.315   1.00 31.32  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.520   -17.495 5.935   1.00 31.35  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 2.913   -16.400 6.658   1.00 31.69  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.123   -16.842 0.011   1.00 26.00  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.666  -16.962 -1.200  1.00 25.43  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.671  -18.085 -0.947  1.00 27.91  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.319  -19.120 -0.377  1.00 27.88  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.260   -17.262 -2.371  1.00 23.59  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.935  -17.843 -1.310  1.00 27.93  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.967  -18.828 -1.053  1.00 27.68  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.365  -19.509 -2.358  1.00 29.48  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.708  -18.842 -3.343  1.00 32.37  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -5.163  -18.181 -0.342  1.00 31.35  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -6.179  -19.230 0.108   1.00 34.88  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.697  -20.186 1.208   1.00 35.52  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.841  -20.976 1.806   1.00 43.22  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.470  -21.867 0.822   1.00 37.57  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.309  -20.845 -2.324  1.00 32.18  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.874  -21.681 -3.370  1.00 36.08  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.911  -22.621 -2.769  1.00 35.73  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.781  -23.015 -1.614  1.00 31.41  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.797  -22.563 -3.986  1.00 35.08  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -2.594  -21.743 -4.373  1.00 43.04  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -2.150  -21.998 -6.093  1.00 44.27  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -3.610  -22.396 -7.062  1.00 54.09  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.905  -22.956 -3.600  1.00 41.85  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.964  -23.908 -3.292  1.00 45.10  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.376  -25.152 -2.648  1.00 41.10  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.476  -25.782 -3.205  1.00 42.73  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.689  -24.370 -4.564  1.00 47.04  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -10.157 -24.726 -4.336  1.00 50.24  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.873 -23.822 -3.333  1.00 54.52  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.866  -25.448 -1.437  1.00 40.29  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.561  -26.700 -0.777  1.00 37.94  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -6.160  -26.740 -0.184  1.00 44.96  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.718  -27.816 0.202   1.00 47.69  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.470  -25.587 -0.109  1.00 40.30  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -4.208  -25.524 0.610   1.00 37.75  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -4.300  -24.410 1.636   1.00 36.81  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.995  -23.444 1.386   1.00 35.36  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -3.027  -25.090 -0.264  1.00 44.19  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.721  -26.082 -1.368  1.00 43.98  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.869  -27.158 -1.144  1.00 54.15  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -3.306  -25.950 -2.618  1.00 46.63  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -1.611  -28.077 -2.147  1.00 63.80  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -3.048  -26.858 -3.630  1.00 56.55  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -2.201  -27.924 -3.391  1.00 65.33  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -1.966  -28.810 -4.404  1.00 76.53  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.544  -24.469 2.761   1.00 36.05  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.496  -23.358 3.725   1.00 36.19  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.771  -22.175 3.064   1.00 31.89  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -2.062  -22.366 2.060   1.00 27.97  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.697  -23.956 4.915   1.00 35.87  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.785  -24.974 4.270   1.00 35.69  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.585  -25.539 3.090   1.00 37.94  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.995  -20.965 3.597   1.00 28.05  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -2.242  -19.777 3.207   1.00 27.39  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.753  -20.097 3.299   1.00 27.05  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -0.296  -20.548 4.354   1.00 28.30  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.644  -18.551 4.043   1.00 27.47  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -4.113  -18.226 3.888   1.00 31.80  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -5.133  -18.947 4.486   1.00 32.46  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.710  -17.248 3.190   1.00 31.10  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.308  -18.413 4.149   1.00 30.94  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -6.075  -17.370 3.362   1.00 31.05  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? -0.028  -19.846 2.192   1.00 26.42  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.279   -20.459 2.010   1.00 25.92  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.345   -19.385 1.836   1.00 26.70  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.148   -18.491 1.029   1.00 27.04  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.272   -21.355 0.763   1.00 26.21  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.375   -22.377 0.798   1.00 27.95  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 3.709   -22.158 0.598   1.00 27.74  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.238   -23.789 1.086   1.00 30.76  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.414   -23.331 0.728   1.00 28.85  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.544   -24.349 1.030   1.00 33.11  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.157   -24.636 1.368   1.00 38.18  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 3.789   -25.707 1.269   1.00 33.70  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.403   -25.981 1.581   1.00 38.25  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.699   -26.505 1.566   1.00 35.98  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.498   -19.475 2.551   1.00 23.66  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.570   -18.482 2.402   1.00 23.83  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.060   -18.465 0.956   1.00 23.00  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.291   -19.524 0.385   1.00 26.08  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.649   -18.945 3.402   1.00 24.06  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.363   -20.417 3.634   1.00 22.56  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 3.803   -20.506 3.548   1.00 22.45  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.191   -17.257 0.386   1.00 19.93  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.466   -17.122 -1.047  1.00 19.90  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.038   -15.733 -1.362  1.00 21.04  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.051   -14.848 -0.511  1.00 21.91  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.138   -17.400 -1.782  1.00 19.32  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.546   -15.527 -2.595  1.00 21.08  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 6.952   -14.195 -2.987  1.00 19.98  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.446   -13.941 -4.403  1.00 20.18  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.169   -14.897 -5.150  1.00 21.26  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.488   -14.095 -2.897  1.00 20.18  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.192   -15.005 -3.894  1.00 22.45  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 10.716  -14.858 -3.768  1.00 21.47  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.379  -15.637 -4.830  1.00 25.06  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.652  -16.044 -4.786  1.00 26.51  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.357  -15.928 -3.672  1.00 25.26  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.178  -16.635 -5.838  1.00 26.26  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.269   -12.669 -4.739  1.00 19.81  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.094   -12.298 -6.147  1.00 20.74  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.449   -12.408 -6.848  1.00 25.13  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.405   -11.748 -6.435  1.00 26.63  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.558   -10.854 -6.284  1.00 25.95  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.371   -10.564 -5.347  1.00 31.29  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.240   -10.572 -7.771  1.00 24.90  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.006   -10.825 -5.921  1.00 35.52  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.515   -13.237 -7.901  1.00 26.03  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.749   -13.425 -8.649  1.00 31.27  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 8.882   -12.370 -9.739  1.00 32.69  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 7.901   -11.763 -10.168 1.00 27.17  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 8.836   -14.791 -9.313  1.00 31.22  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 9.719   -15.803 -8.604  1.00 32.03  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.302  -15.456 -7.557  1.00 36.04  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 9.818   -16.931 -9.099  1.00 34.01  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.136  -12.185 -10.170 1.00 34.05  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.430  -11.555 -11.440 1.00 39.46  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.144  -12.559 -12.554 1.00 32.96  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.029  -13.757 -12.311 1.00 35.31  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 11.908  -11.213 -11.531 1.00 43.58  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.356  -10.012 -10.710 1.00 53.05  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.019  -8.869  -11.114 1.00 57.83  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.043  -10.234 -9.686  1.00 56.63  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.021  -12.049 -13.771 1.00 38.83  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 9.960   -12.909 -14.937 1.00 35.65  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.304  -12.731 -15.630 1.00 36.93  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.636  -11.605 -15.970 1.00 34.68  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.823   -12.415 -15.839 1.00 36.51  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.489   -12.371 -15.076 1.00 38.11  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.747   -13.261 -17.114 1.00 36.03  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.521   -11.314 -15.583 1.00 36.12  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.071  -13.816 -15.780 1.00 33.19  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.372  -13.695 -16.421 1.00 35.46  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.173  -13.401 -17.910 1.00 35.68  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.131  -13.708 -18.501 1.00 32.32  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.172  -14.954 -16.207 1.00 34.30  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.156  -12.720 -18.493 1.00 33.13  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.200  -12.635 -19.948 1.00 33.81  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 13.980  -14.013 -20.550 1.00 28.54  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.653  -14.962 -20.174 1.00 30.02  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.561  -12.119 -20.373 1.00 35.06  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.674  -10.613 -20.272 1.00 35.40  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.619  -9.965  -20.249 1.00 38.14  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.812  -10.119 -20.252 1.00 39.64  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.017  -14.097 -21.478 1.00 32.65  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 12.825  -15.300 -22.270 1.00 34.28  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 11.902  -16.322 -21.606 1.00 36.94  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.597  -17.348 -22.214 1.00 34.38  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.499  -16.039 -20.350 1.00 34.43  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.638  -16.918 -19.572 1.00 33.13  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.177   -16.649 -19.919 1.00 32.17  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.818   -15.552 -20.348 1.00 31.62  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 10.899  -16.731 -18.074 1.00 30.52  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.333   -17.666 -19.680 1.00 39.11  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 6.886   -17.596 -19.854 1.00 34.62  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.297   -16.533 -18.929 1.00 34.88  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.522   -16.569 -17.715 1.00 37.43  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.297   -18.993 -19.552 1.00 38.13  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 4.772   -18.970 -19.524 1.00 38.48  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 6.790   -20.048 -20.551 1.00 36.83  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.528   -15.609 -19.522 1.00 37.54  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 4.825   -14.539 -18.825 1.00 39.12  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.522   -15.080 -18.221 1.00 39.69  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 2.940   -16.032 -18.742 1.00 35.42  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.519   -13.351 -19.751 1.00 39.90  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.746   -12.583 -20.286 1.00 35.80  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.403   -11.416 -21.210 1.00 40.16  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.256   -11.804 -22.652 1.00 40.36  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 4.812   -10.631 -23.395 1.00 43.37  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.033   -14.485 -17.103 1.00 37.63  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.728   -14.831 -16.532 1.00 34.91  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.613   -14.335 -17.433 1.00 35.77  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.815   -13.442 -18.254 1.00 38.81  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.693   -14.079 -15.178 1.00 34.88  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.152   -13.748 -14.894 1.00 36.30  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.724   -13.467 -16.297 1.00 36.84  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.618  -14.866 -17.278 1.00 38.36  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.780  -14.229 -17.895 1.00 36.36  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.977  -12.801 -17.413 1.00 40.72  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.493  -12.422 -16.340 1.00 35.79  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.949  -15.119 -17.450 1.00 36.87  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.314  -16.452 -17.138 1.00 35.31  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.936  -16.123 -16.579 1.00 39.18  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.721  -11.986 -18.191 1.00 41.94  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -3.179  -10.669 -17.748 1.00 41.63  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.794  -10.712 -16.354 1.00 39.02  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.519  -11.639 -16.021 1.00 43.42  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -4.225  -10.267 -18.812 1.00 43.18  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.428  -11.494 -19.659 1.00 42.47  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.145  -12.296 -19.572 1.00 47.14  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.444  -9.710  -15.556 1.00 38.82  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.949  -9.473  -14.218 1.00 42.29  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.427  -10.479 -13.193 1.00 41.01  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.844  -10.391 -12.036 1.00 40.03  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.459  -9.250  -14.218 1.00 52.36  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.801  -7.993  -14.978 1.00 54.05  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.603  -6.885  -14.468 1.00 52.48  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.273  -8.146  -16.205 1.00 59.31  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.488  -11.369 -13.582 1.00 36.47  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.946  -12.366 -12.666 1.00 30.36  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.443  -12.131 -12.430 1.00 27.27  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.216   -11.522 -13.253 1.00 31.35  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -2.138  -13.796 -13.180 1.00 32.18  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.574  -14.176 -13.583 1.00 38.05  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.576  -13.854 -12.484 1.00 37.69  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -6.010  -14.283 -12.717 1.00 43.26  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -6.109  -15.747 -12.694 1.00 42.89  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.066   -12.623 -11.298 1.00 23.14  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.461   -12.435 -10.882 1.00 22.85  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.086   -13.820 -10.831 1.00 23.26  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.427   -14.790 -10.494 1.00 23.91  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.568   -11.828 -9.461  1.00 23.03  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.097   -10.384 -9.426  1.00 26.70  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.267  -10.098 -9.331  1.00 30.25  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 1.972   -9.321  -9.596  1.00 29.28  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.732  -8.791  -9.372  1.00 31.40  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.522   -8.008  -9.628  1.00 30.75  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.160   -7.753  -9.526  1.00 32.26  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.331  -6.483  -9.587  1.00 34.17  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.413   -13.967 -11.074 1.00 22.02  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.067   -15.251 -10.894 1.00 22.59  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.362   -15.411 -9.407  1.00 25.09  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.050   -14.567 -8.818  1.00 28.71  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.368   -15.110 -11.710 1.00 25.11  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.597   -13.630 -11.851 1.00 25.24  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.325   -12.881 -11.476 1.00 27.23  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 3.770   -16.437 -8.806  1.00 23.14  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 3.948   -16.638 -7.367  1.00 22.68  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 4.915   -17.783 -7.137  1.00 26.01  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.654   -18.926 -7.537  1.00 27.50  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.599   -16.881 -6.662  1.00 24.16  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.650   -15.735 -6.949  1.00 22.58  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 2.833   -17.037 -5.149  1.00 23.15  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.194   -14.359 -6.593  1.00 21.46  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.028   -17.486 -6.450  1.00 24.61  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 6.930   -18.550 -6.058  1.00 24.18  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.608   -18.968 -4.625  1.00 24.50  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.680   -18.149 -3.709  1.00 24.72  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.385   -18.062 -6.160  1.00 23.43  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.428   -19.094 -5.733  1.00 28.85  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 9.840   -20.099 -6.608  1.00 30.51  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 9.986   -19.061 -4.450  1.00 29.92  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 10.777  -21.047 -6.206  1.00 32.93  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 10.924  -20.005 -4.057  1.00 32.70  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.319  -20.994 -4.936  1.00 32.23  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.258   -20.251 -4.449  1.00 24.01  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 5.894   -20.784 -3.143  1.00 23.31  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.172   -21.293 -2.490  1.00 25.11  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 7.834   -22.192 -3.041  1.00 26.88  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 4.902   -21.952 -3.266  1.00 26.33  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.525   -21.484 -3.726  1.00 26.09  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.253   -21.247 -5.080  1.00 27.81  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.529   -21.225 -2.794  1.00 29.96  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.002   -20.763 -5.485  1.00 27.42  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.297   -20.717 -3.196  1.00 29.01  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.033   -20.505 -4.541  1.00 29.36  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.463   -20.764 -1.297  1.00 25.04  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.585   -21.264 -0.502  1.00 28.60  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.332   -22.709 -0.049  1.00 27.81  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.190   -23.168 0.136   1.00 28.43  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 8.902   -20.313 0.660   1.00 25.20  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.362   -18.911 0.294   1.00 23.58  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.640  -18.693 -0.254  1.00 22.46  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.581   -17.797 0.584   1.00 23.79  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.033  -17.411 -0.612  1.00 23.66  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.008   -16.500 0.279   1.00 23.93  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.250  -16.306 -0.323  1.00 26.51  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.428   -23.447 0.113   1.00 25.14  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.325   -24.815 0.581   1.00 29.19  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.146   -25.776 -0.589  1.00 34.23  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.017  -26.608 -0.844  1.00 35.65  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.035   -25.637 -1.324  1.00 33.95  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 7.768   -26.521 -2.452  1.00 35.21  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.584   -26.069 -3.659  1.00 34.91  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 8.954   -26.882 -4.528  1.00 34.13  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.270   -26.576 -2.749  1.00 33.19  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 5.916   -25.263 -3.162  1.00 36.37  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.455   -26.940 -1.529  1.00 37.48  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 8.856   -24.756 -3.702  1.00 30.78  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.572   -24.117 -4.796  1.00 29.81  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 8.796   -24.218 -6.111  1.00 29.95  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.392   -24.192 -7.185  1.00 33.44  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.020  -24.632 -4.921  1.00 32.05  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 11.715  -24.670 -3.604  1.00 36.88  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.541  -25.698 -3.223  1.00 37.58  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 11.691  -23.803 -2.568  1.00 33.61  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.002  -25.455 -1.998  1.00 42.23  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.515  -24.303 -1.590  1.00 35.91  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.463   -24.329 -6.027  1.00 33.12  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.587   -24.337 -7.188  1.00 33.78  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.125   -22.919 -7.507  1.00 31.17  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.167   -22.061 -6.629  1.00 30.65  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.369   -25.167 -6.795  1.00 38.84  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 5.666   -26.661 -6.739  1.00 47.04  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 4.520   -27.439 -6.121  1.00 55.23  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.401   -26.888 -5.919  1.00 57.87  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 4.788   -28.614 -5.803  1.00 61.80  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.742   -22.682 -8.775  1.00 28.58  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.209   -21.411 -9.248  1.00 29.20  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 3.749   -21.615 -9.649  1.00 29.44  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.418   -22.604 -10.303 1.00 33.83  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.039   -20.846 -10.405 1.00 33.86  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.339   -20.544 -9.897  1.00 28.81  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.442   -19.593 -11.033 1.00 31.67  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 2.887   -20.668 -9.270  1.00 28.91  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.563   -20.574 -9.874  1.00 28.74  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.281   -19.113 -10.215 1.00 31.86  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 1.976   -18.215 -9.745  1.00 28.09  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.494   -21.152 -8.965  1.00 29.48  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.224   -18.889 -11.003 1.00 27.21  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? -0.152  -17.548 -11.396 1.00 27.74  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.411  -17.198 -10.624 1.00 32.67  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.437  -17.849 -10.821 1.00 32.31  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.409  -17.549 -12.910 1.00 27.23  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 0.819   -17.819 -13.773 1.00 34.29  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.000   -17.111 -13.587 1.00 32.79  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.779   -18.779 -14.789 1.00 39.84  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.116   -17.363 -14.380 1.00 44.03  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 1.897   -19.030 -15.578 1.00 40.42  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.064   -18.333 -15.370 1.00 41.96  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.324  -16.173 -9.765  1.00 28.58  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.463  -15.789 -8.946  1.00 25.79  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.721  -14.295 -9.063  1.00 26.44  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.810  -13.538 -9.329  1.00 25.36  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -2.165  -16.094 -7.476  1.00 27.36  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -2.044  -17.570 -7.125  1.00 28.38  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.653  -17.567 -5.650  1.00 27.94  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.482  -18.046 -7.316  1.00 33.40  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.974  -13.891 -8.809  1.00 23.95  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.329  -12.476 -8.714  1.00 24.39  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.346  -11.985 -7.257  1.00 20.38  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.256  -12.767 -6.313  1.00 22.35  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.383  -10.654 -7.038  1.00 24.25  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.309  -10.079 -5.696  1.00 24.75  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.308  -10.600 -4.673  1.00 23.48  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -5.031  -10.569 -3.483  1.00 23.15  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.504  -8.585  -5.933  1.00 24.19  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -4.051  -8.370  -7.370  1.00 27.35  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.471  -9.627  -8.086  1.00 25.06  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.488  -11.047 -5.127  1.00 24.68  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.450  -11.548 -4.150  1.00 25.35  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.906  -12.739 -3.347  1.00 28.35  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.406  -13.004 -2.250  1.00 23.33  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.743  -12.027 -4.826  1.00 29.48  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.580  -13.307 -5.662  1.00 31.26  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.842  -13.555 -6.501  1.00 42.36  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.770  -14.778 -7.355  1.00 45.73  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.541  -15.963 -6.522  1.00 46.56  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.839  -13.414 -3.851  1.00 27.33  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.256  -14.578 -3.201  1.00 24.06  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.897  -14.286 -2.533  1.00 24.18  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.246  -15.235 -2.072  1.00 25.74  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -5.233  -15.750 -4.169  1.00 25.04  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.635  -16.285 -4.461  1.00 31.84  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.410  -16.396 -3.500  1.00 31.10  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.934  -16.563 -5.637  1.00 30.14  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.515  -12.991 -2.466  1.00 21.64  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.199  -12.539 -1.995  1.00 21.09  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.358  -11.672 -0.743  1.00 19.80  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.976  -10.598 -0.772  1.00 24.33  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.465  -11.804 -3.115  1.00 20.33  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.341  -12.580 -4.434  1.00 22.31  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.590  -11.770 -5.462  1.00 21.55  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.626  -13.911 -4.199  1.00 20.81  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.813  -12.174 0.361   1.00 21.13  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.912  -11.544 1.675   1.00 21.32  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.520  -11.092 2.094   1.00 22.54  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.341   -11.920 2.336   1.00 25.11  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.379  -12.601 2.666   1.00 23.76  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.816  -13.021 2.387   1.00 24.89  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -4.095  -13.977 1.409   1.00 25.34  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.872  -12.478 3.115   1.00 28.88  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.411  -14.382 1.158   1.00 32.60  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -6.180  -12.876 2.851   1.00 28.00  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.448  -13.832 1.903   1.00 27.75  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.256  -9.780  2.136   1.00 26.04  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.079   -9.284  2.500   1.00 26.00  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.616   -9.844  3.818   1.00 25.95  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 0.914   -9.907  4.816   1.00 25.57  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 0.860   -7.755  2.497   1.00 27.71  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.255  -7.535  1.484   1.00 28.65  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -1.200  -8.708  1.777   1.00 30.30  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 2.898   -10.272 3.791   1.00 26.68  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.503   -11.111 4.810   1.00 24.92  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.486   -10.424 6.180   1.00 24.36  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.070   -11.042 7.152   1.00 29.63  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 4.937   -11.438 4.353   1.00 27.07  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.697   -12.255 5.392   1.00 28.34  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.375   -13.583 5.620   1.00 28.09  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.744   -11.694 6.133   1.00 31.78  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.045   -14.341 6.568   1.00 32.28  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.440   -12.451 7.070   1.00 29.23  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.086   -13.770 7.281   1.00 31.61  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 7.737   -14.534 8.208   1.00 35.07  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 3.931   -9.166  6.249   1.00 29.23  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.047   -8.463  7.527   1.00 33.76  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.703   -8.460  8.258   1.00 35.53  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.633   -8.877  9.409   1.00 37.44  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 4.697   -7.097  7.355   1.00 35.43  ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 6.198   -7.092  7.058   1.00 51.78  ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 6.858   -8.142  7.265   1.00 55.42  ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 6.715   -6.030  6.617   1.00 66.07  ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 1.629   -8.037  7.569   1.00 33.97  ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? 0.290   -7.998  8.158   1.00 35.26  ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? -0.232  -9.373  8.600   1.00 34.45  ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -0.943  -9.460  9.606   1.00 37.43  ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? -0.658  -7.306  7.171   1.00 31.37  ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -2.118  -7.215  7.620   1.00 35.48  ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -2.871  -6.481  6.517   1.00 38.96  ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -4.110  -5.799  7.019   1.00 45.00  ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -4.984  -6.711  7.748   1.00 45.30  ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? 0.115   -10.450 7.886   1.00 28.78  ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? -0.571  -11.743 7.963   1.00 29.48  ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? 0.198   -12.804 8.739   1.00 31.30  ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? -0.326  -13.897 8.949   1.00 30.37  ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -0.816  -12.296 6.568   1.00 29.34  ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -1.830  -11.512 5.974   1.00 37.11  ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 1.459   -12.514 9.091   1.00 31.18  ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 2.324   -13.563 9.609   1.00 35.72  ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 1.860   -14.075 10.980  1.00 33.36  ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 2.008   -15.259 11.273  1.00 32.99  ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 3.805   -13.166 9.570   1.00 36.93  ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 4.224   -12.051 10.511  1.00 42.06  ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 5.748   -12.095 10.564  1.00 47.84  ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 6.304   -11.077 11.509  1.00 58.99  ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 6.087   -9.693  11.072  1.00 62.15  ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 1.281   -13.187 11.794  0.50 33.98  ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 1.308   -13.190 11.814  0.50 34.35  ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? 0.791   -13.580 13.111  0.50 38.12  ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 0.796   -13.646 13.101  0.50 38.52  ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? -0.352  -14.598 12.976  0.50 37.17  ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? -0.228  -14.758 12.863  0.50 36.43  ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? -0.559  -15.435 13.852  0.50 38.19  ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? -0.218  -15.794 13.528  0.50 32.98  ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? 0.527   -12.366 13.995  0.50 37.20  ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? 0.255   -12.496 13.939  0.50 40.27  ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 1.751   -11.656 14.569  0.50 39.61  ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? -0.004  -12.828 15.403  0.50 44.43  ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 2.894   -12.088 14.288  0.50 38.35  ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 0.983   -13.033 16.146  0.50 45.86  ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? 1.558   -10.669 15.311  0.50 42.05  ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -1.187  -12.901 15.787  0.50 47.11  ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -1.080  -14.557 11.854  1.00 34.27  ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -2.197  -15.454 11.633  1.00 34.17  ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -1.757  -16.741 10.942  1.00 34.87  ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -2.212  -17.833 11.288  1.00 30.61  ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -3.224  -14.736 10.750  1.00 37.88  ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -4.541  -15.459 10.571  1.00 43.99  ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -5.585  -14.529 9.954   1.00 51.77  ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -6.906  -15.172 9.655   1.00 56.36  ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -7.898  -14.190 9.209   1.00 50.58  ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -0.913  -16.601 9.913   1.00 32.00  ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? -0.705  -17.685 8.976   1.00 30.56  ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 0.677   -18.312 9.142   1.00 30.57  ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 0.904   -19.379 8.585   1.00 31.77  ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -0.845  -17.256 7.510   1.00 27.80  ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -2.246  -16.809 7.130   1.00 31.18  ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -3.377  -17.528 7.519   1.00 34.70  ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -2.436  -15.659 6.370   1.00 34.86  ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -4.656  -17.109 7.184   1.00 33.77  ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -3.710  -15.238 6.012   1.00 35.32  ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -4.817  -15.960 6.426   1.00 34.39  ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -6.046  -15.516 6.053   1.00 35.79  ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 1.559   -17.686 9.914   1.00 30.44  ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 2.954   -18.116 9.966   1.00 35.19  ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 3.179   -19.054 11.152  1.00 35.19  ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 3.762   -18.658 12.143  1.00 41.76  ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 2.583   -20.241 11.056  1.00 38.43  ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 2.547   -21.244 12.109  1.00 40.13  ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 2.781   -22.591 11.431  1.00 37.62  ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 2.361   -22.797 10.292  1.00 33.91  ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 1.206   -21.230 12.858  1.00 42.79  ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 0.903   -19.956 13.643  1.00 48.70  ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? -0.267  -20.041 14.623  1.00 53.12  ? 70  LYS A CD  1 
ATOM   570  N N   . PRO A 1 72 ? 3.454   -23.555 12.098  1.00 39.77  ? 71  PRO A N   1 
ATOM   571  C CA  . PRO A 1 72 ? 3.743   -24.844 11.466  1.00 36.66  ? 71  PRO A CA  1 
ATOM   572  C C   . PRO A 1 72 ? 2.496   -25.529 10.939  1.00 40.81  ? 71  PRO A C   1 
ATOM   573  O O   . PRO A 1 72 ? 1.400   -25.334 11.473  1.00 38.42  ? 71  PRO A O   1 
ATOM   574  C CB  . PRO A 1 72 ? 4.407   -25.635 12.598  1.00 41.54  ? 71  PRO A CB  1 
ATOM   575  C CG  . PRO A 1 72 ? 5.026   -24.557 13.457  1.00 43.23  ? 71  PRO A CG  1 
ATOM   576  C CD  . PRO A 1 72 ? 3.979   -23.449 13.471  1.00 39.31  ? 71  PRO A CD  1 
ATOM   577  N N   . ASN A 1 73 ? 2.698   -26.314 9.878   1.00 40.45  ? 72  ASN A N   1 
ATOM   578  C CA  . ASN A 1 73 ? 1.619   -27.000 9.193   1.00 48.72  ? 72  ASN A CA  1 
ATOM   579  C C   . ASN A 1 73 ? 2.158   -28.336 8.700   1.00 54.15  ? 72  ASN A C   1 
ATOM   580  O O   . ASN A 1 73 ? 3.332   -28.443 8.339   1.00 51.22  ? 72  ASN A O   1 
ATOM   581  C CB  . ASN A 1 73 ? 1.057   -26.110 8.088   1.00 50.45  ? 72  ASN A CB  1 
ATOM   582  C CG  . ASN A 1 73 ? -0.278  -26.570 7.567   1.00 48.46  ? 72  ASN A CG  1 
ATOM   583  O OD1 . ASN A 1 73 ? -0.328  -27.485 6.744   1.00 48.48  ? 72  ASN A OD1 1 
ATOM   584  N ND2 . ASN A 1 73 ? -1.353  -25.901 7.962   1.00 48.50  ? 72  ASN A ND2 1 
ATOM   585  N N   . LYS A 1 74 ? 1.274   -29.341 8.692   1.00 54.53  ? 73  LYS A N   1 
ATOM   586  C CA  . LYS A 1 74 ? 1.614   -30.712 8.359   1.00 52.40  ? 73  LYS A CA  1 
ATOM   587  C C   . LYS A 1 74 ? 2.080   -30.823 6.906   1.00 55.19  ? 73  LYS A C   1 
ATOM   588  O O   . LYS A 1 74 ? 2.922   -31.664 6.592   1.00 56.04  ? 73  LYS A O   1 
ATOM   589  C CB  . LYS A 1 74 ? 0.417   -31.619 8.676   1.00 58.99  ? 73  LYS A CB  1 
ATOM   590  C CG  . LYS A 1 74 ? -0.796  -31.514 7.745   1.00 57.69  ? 73  LYS A CG  1 
ATOM   591  N N   . ARG A 1 75 ? 1.556   -29.960 6.027   1.00 51.21  ? 74  ARG A N   1 
ATOM   592  C CA  . ARG A 1 75 ? 1.707   -30.129 4.585   1.00 47.52  ? 74  ARG A CA  1 
ATOM   593  C C   . ARG A 1 75 ? 3.180   -30.082 4.173   1.00 42.83  ? 74  ARG A C   1 
ATOM   594  O O   . ARG A 1 75 ? 3.976   -29.355 4.777   1.00 40.28  ? 74  ARG A O   1 
ATOM   595  C CB  . ARG A 1 75 ? 0.816   -29.126 3.841   1.00 47.94  ? 74  ARG A CB  1 
ATOM   596  C CG  . ARG A 1 75 ? -0.644  -29.302 4.227   1.00 50.74  ? 74  ARG A CG  1 
ATOM   597  C CD  . ARG A 1 75 ? -1.310  -30.426 3.442   1.00 51.12  ? 74  ARG A CD  1 
ATOM   598  N NE  . ARG A 1 75 ? -2.283  -29.920 2.463   1.00 66.74  ? 74  ARG A NE  1 
ATOM   599  C CZ  . ARG A 1 75 ? -3.441  -29.304 2.764   1.00 65.05  ? 74  ARG A CZ  1 
ATOM   600  N NH1 . ARG A 1 75 ? -4.186  -28.814 1.789   1.00 56.90  ? 74  ARG A NH1 1 
ATOM   601  N NH2 . ARG A 1 75 ? -3.844  -29.165 4.027   1.00 56.80  ? 74  ARG A NH2 1 
ATOM   602  N N   . LYS A 1 76 ? 3.503   -30.860 3.127   1.00 42.07  ? 75  LYS A N   1 
ATOM   603  C CA  . LYS A 1 76 ? 4.850   -31.039 2.596   1.00 46.20  ? 75  LYS A CA  1 
ATOM   604  C C   . LYS A 1 76 ? 5.437   -29.701 2.149   1.00 40.15  ? 75  LYS A C   1 
ATOM   605  O O   . LYS A 1 76 ? 4.820   -28.995 1.344   1.00 40.54  ? 75  LYS A O   1 
ATOM   606  C CB  . LYS A 1 76 ? 4.828   -31.996 1.394   1.00 49.51  ? 75  LYS A CB  1 
ATOM   607  C CG  . LYS A 1 76 ? 6.154   -32.238 0.684   1.00 50.95  ? 75  LYS A CG  1 
ATOM   608  C CD  . LYS A 1 76 ? 6.261   -33.592 -0.015  1.00 56.63  ? 75  LYS A CD  1 
ATOM   609  C CE  . LYS A 1 76 ? 7.649   -33.857 -0.534  1.00 55.74  ? 75  LYS A CE  1 
ATOM   610  N N   . GLY A 1 77 ? 6.631   -29.370 2.675   1.00 36.34  ? 76  GLY A N   1 
ATOM   611  C CA  . GLY A 1 77 ? 7.341   -28.170 2.259   1.00 35.46  ? 76  GLY A CA  1 
ATOM   612  C C   . GLY A 1 77 ? 6.955   -26.932 3.071   1.00 35.68  ? 76  GLY A C   1 
ATOM   613  O O   . GLY A 1 77 ? 7.636   -25.910 2.985   1.00 33.69  ? 76  GLY A O   1 
ATOM   614  N N   . PHE A 1 78 ? 5.868   -27.014 3.843   1.00 33.92  ? 77  PHE A N   1 
ATOM   615  C CA  . PHE A 1 78 ? 5.351   -25.820 4.489   1.00 36.39  ? 77  PHE A CA  1 
ATOM   616  C C   . PHE A 1 78 ? 6.361   -25.214 5.477   1.00 34.95  ? 77  PHE A C   1 
ATOM   617  O O   . PHE A 1 78 ? 6.560   -24.001 5.522   1.00 30.70  ? 77  PHE A O   1 
ATOM   618  C CB  . PHE A 1 78 ? 4.004   -26.112 5.150   1.00 32.66  ? 77  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 78 ? 3.252   -24.841 5.515   1.00 32.76  ? 77  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 78 ? 3.488   -24.194 6.725   1.00 30.45  ? 77  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 78 ? 2.306   -24.302 4.639   1.00 28.42  ? 77  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 78 ? 2.828   -23.009 7.039   1.00 33.21  ? 77  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 78 ? 1.643   -23.120 4.956   1.00 25.58  ? 77  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 78 ? 1.887   -22.481 6.167   1.00 26.50  ? 77  PHE A CZ  1 
ATOM   625  N N   . ASN A 1 79 ? 6.929   -26.047 6.347   1.00 31.19  ? 78  ASN A N   1 
ATOM   626  C CA  . ASN A 1 79 ? 7.734   -25.538 7.447   1.00 32.04  ? 78  ASN A CA  1 
ATOM   627  C C   . ASN A 1 79 ? 9.091   -25.090 6.893   1.00 31.62  ? 78  ASN A C   1 
ATOM   628  O O   . ASN A 1 79 ? 9.680   -24.105 7.371   1.00 30.12  ? 78  ASN A O   1 
ATOM   629  C CB  . ASN A 1 79 ? 7.889   -26.599 8.530   1.00 33.52  ? 78  ASN A CB  1 
ATOM   630  C CG  . ASN A 1 79 ? 6.571   -26.929 9.194   1.00 39.71  ? 78  ASN A CG  1 
ATOM   631  O OD1 . ASN A 1 79 ? 5.649   -26.107 9.187   1.00 36.84  ? 78  ASN A OD1 1 
ATOM   632  N ND2 . ASN A 1 79 ? 6.476   -28.106 9.808   1.00 38.22  ? 78  ASN A ND2 1 
ATOM   633  N N   . GLU A 1 80 ? 9.578   -25.851 5.897   1.00 28.85  ? 79  GLU A N   1 
ATOM   634  C CA  . GLU A 1 80 ? 10.712  -25.416 5.096   1.00 30.94  ? 79  GLU A CA  1 
ATOM   635  C C   . GLU A 1 80 ? 10.409  -24.019 4.547   1.00 30.39  ? 79  GLU A C   1 
ATOM   636  O O   . GLU A 1 80 ? 11.248  -23.126 4.633   1.00 27.56  ? 79  GLU A O   1 
ATOM   637  C CB  . GLU A 1 80 ? 11.116  -26.365 3.969   1.00 31.42  ? 79  GLU A CB  1 
ATOM   638  C CG  . GLU A 1 80 ? 12.402  -25.931 3.258   1.00 34.86  ? 79  GLU A CG  1 
ATOM   639  C CD  . GLU A 1 80 ? 12.941  -26.785 2.129   1.00 40.58  ? 79  GLU A CD  1 
ATOM   640  O OE1 . GLU A 1 80 ? 12.270  -27.751 1.715   1.00 46.00  ? 79  GLU A OE1 1 
ATOM   641  O OE2 . GLU A 1 80 ? 14.045  -26.467 1.651   1.00 46.35  ? 79  GLU A OE2 1 
ATOM   642  N N   . GLY A 1 81 ? 9.182   -23.827 4.035   1.00 30.18  ? 80  GLY A N   1 
ATOM   643  C CA  . GLY A 1 81 ? 8.786   -22.543 3.453   1.00 28.66  ? 80  GLY A CA  1 
ATOM   644  C C   . GLY A 1 81 ? 8.758   -21.407 4.476   1.00 25.57  ? 80  GLY A C   1 
ATOM   645  O O   . GLY A 1 81 ? 9.110   -20.260 4.170   1.00 25.75  ? 80  GLY A O   1 
ATOM   646  N N   . LEU A 1 82 ? 8.347   -21.727 5.708   1.00 23.67  ? 81  LEU A N   1 
ATOM   647  C CA  . LEU A 1 82 ? 8.357   -20.744 6.780   1.00 26.82  ? 81  LEU A CA  1 
ATOM   648  C C   . LEU A 1 82 ? 9.794   -20.298 7.061   1.00 27.66  ? 81  LEU A C   1 
ATOM   649  O O   . LEU A 1 82 ? 10.026  -19.114 7.275   1.00 26.46  ? 81  LEU A O   1 
ATOM   650  C CB  . LEU A 1 82 ? 7.680   -21.242 8.059   1.00 27.73  ? 81  LEU A CB  1 
ATOM   651  C CG  . LEU A 1 82 ? 6.176   -21.521 7.972   1.00 30.06  ? 81  LEU A CG  1 
ATOM   652  C CD1 . LEU A 1 82 ? 5.795   -22.175 9.288   1.00 29.99  ? 81  LEU A CD1 1 
ATOM   653  C CD2 . LEU A 1 82 ? 5.339   -20.263 7.782   1.00 28.78  ? 81  LEU A CD2 1 
ATOM   654  N N   . TRP A 1 83 ? 10.755  -21.240 7.058   1.00 26.30  ? 82  TRP A N   1 
ATOM   655  C CA  . TRP A 1 83 ? 12.150  -20.869 7.295   1.00 27.91  ? 82  TRP A CA  1 
ATOM   656  C C   . TRP A 1 83 ? 12.627  -19.912 6.206   1.00 27.43  ? 82  TRP A C   1 
ATOM   657  O O   . TRP A 1 83 ? 13.277  -18.900 6.485   1.00 27.50  ? 82  TRP A O   1 
ATOM   658  C CB  . TRP A 1 83 ? 13.076  -22.096 7.428   1.00 27.25  ? 82  TRP A CB  1 
ATOM   659  C CG  . TRP A 1 83 ? 14.526  -21.722 7.658   1.00 27.33  ? 82  TRP A CG  1 
ATOM   660  C CD1 . TRP A 1 83 ? 15.146  -21.575 8.862   1.00 28.17  ? 82  TRP A CD1 1 
ATOM   661  C CD2 . TRP A 1 83 ? 15.507  -21.384 6.658   1.00 26.47  ? 82  TRP A CD2 1 
ATOM   662  N NE1 . TRP A 1 83 ? 16.455  -21.216 8.684   1.00 28.39  ? 82  TRP A NE1 1 
ATOM   663  C CE2 . TRP A 1 83 ? 16.695  -21.058 7.339   1.00 30.62  ? 82  TRP A CE2 1 
ATOM   664  C CE3 . TRP A 1 83 ? 15.487  -21.315 5.262   1.00 26.96  ? 82  TRP A CE3 1 
ATOM   665  C CZ2 . TRP A 1 83 ? 17.867  -20.686 6.674   1.00 30.80  ? 82  TRP A CZ2 1 
ATOM   666  C CZ3 . TRP A 1 83 ? 16.635  -20.953 4.604   1.00 30.10  ? 82  TRP A CZ3 1 
ATOM   667  C CH2 . TRP A 1 83 ? 17.804  -20.620 5.298   1.00 34.69  ? 82  TRP A CH2 1 
ATOM   668  N N   . GLU A 1 84 ? 12.281  -20.226 4.951   1.00 26.50  ? 83  GLU A N   1 
ATOM   669  C CA  . GLU A 1 84 ? 12.837  -19.481 3.835   1.00 23.96  ? 83  GLU A CA  1 
ATOM   670  C C   . GLU A 1 84 ? 12.302  -18.052 3.829   1.00 24.69  ? 83  GLU A C   1 
ATOM   671  O O   . GLU A 1 84 ? 13.051  -17.109 3.628   1.00 25.25  ? 83  GLU A O   1 
ATOM   672  C CB  . GLU A 1 84 ? 12.452  -20.150 2.526   1.00 23.38  ? 83  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 84 ? 13.153  -21.489 2.335   1.00 26.21  ? 83  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 84 ? 12.742  -22.187 1.040   1.00 30.98  ? 83  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 84 ? 11.819  -21.712 0.333   1.00 31.53  ? 83  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 84 ? 13.325  -23.274 0.766   1.00 29.70  ? 83  GLU A OE2 1 
ATOM   677  N N   . ILE A 1 85 ? 10.992  -17.889 4.047   1.00 23.43  ? 84  ILE A N   1 
ATOM   678  C CA  . ILE A 1 85 ? 10.424  -16.556 3.966   1.00 24.21  ? 84  ILE A CA  1 
ATOM   679  C C   . ILE A 1 85 ? 10.985  -15.644 5.065   1.00 25.04  ? 84  ILE A C   1 
ATOM   680  O O   . ILE A 1 85 ? 11.127  -14.435 4.859   1.00 25.04  ? 84  ILE A O   1 
ATOM   681  C CB  . ILE A 1 85 ? 8.879   -16.603 3.957   1.00 23.00  ? 84  ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 85 ? 8.301   -15.214 3.520   1.00 22.49  ? 84  ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 85 ? 8.336   -17.044 5.328   1.00 22.68  ? 84  ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 85 ? 6.840   -15.266 3.112   1.00 22.89  ? 84  ILE A CD1 1 
ATOM   685  N N   . GLN A 1 86 ? 11.294  -16.222 6.239   1.00 23.33  ? 85  GLN A N   1 
ATOM   686  C CA  . GLN A 1 86 ? 11.775  -15.464 7.385   1.00 24.69  ? 85  GLN A CA  1 
ATOM   687  C C   . GLN A 1 86 ? 13.286  -15.221 7.251   1.00 25.91  ? 85  GLN A C   1 
ATOM   688  O O   . GLN A 1 86 ? 13.765  -14.158 7.642   1.00 31.07  ? 85  GLN A O   1 
ATOM   689  C CB  . GLN A 1 86 ? 11.392  -16.180 8.691   1.00 29.19  ? 85  GLN A CB  1 
ATOM   690  C CG  . GLN A 1 86 ? 11.735  -15.402 9.963   1.00 37.10  ? 85  GLN A CG  1 
ATOM   691  C CD  . GLN A 1 86 ? 11.049  -15.922 11.219  1.00 42.60  ? 85  GLN A CD  1 
ATOM   692  O OE1 . GLN A 1 86 ? 10.624  -17.089 11.300  1.00 41.94  ? 85  GLN A OE1 1 
ATOM   693  N NE2 . GLN A 1 86 ? 10.932  -15.055 12.221  1.00 38.78  ? 85  GLN A NE2 1 
ATOM   694  N N   . ASN A 1 87 ? 14.020  -16.192 6.691   1.00 24.84  ? 86  ASN A N   1 
ATOM   695  C CA  . ASN A 1 87 ? 15.476  -16.180 6.806   1.00 23.22  ? 86  ASN A CA  1 
ATOM   696  C C   . ASN A 1 87 ? 16.224  -15.900 5.501   1.00 26.10  ? 86  ASN A C   1 
ATOM   697  O O   . ASN A 1 87 ? 17.371  -15.429 5.566   1.00 26.35  ? 86  ASN A O   1 
ATOM   698  C CB  . ASN A 1 87 ? 16.019  -17.407 7.510   1.00 25.83  ? 86  ASN A CB  1 
ATOM   699  C CG  . ASN A 1 87 ? 15.448  -17.503 8.905   1.00 30.79  ? 86  ASN A CG  1 
ATOM   700  O OD1 . ASN A 1 87 ? 15.696  -16.624 9.731   1.00 35.14  ? 86  ASN A OD1 1 
ATOM   701  N ND2 . ASN A 1 87 ? 14.634  -18.513 9.153   1.00 31.14  ? 86  ASN A ND2 1 
ATOM   702  N N   . ASN A 1 88 ? 15.665  -16.258 4.333   1.00 26.36  ? 87  ASN A N   1 
ATOM   703  C CA  . ASN A 1 88 ? 16.336  -15.900 3.084   1.00 26.12  ? 87  ASN A CA  1 
ATOM   704  C C   . ASN A 1 88 ? 15.319  -15.793 1.934   1.00 23.51  ? 87  ASN A C   1 
ATOM   705  O O   . ASN A 1 88 ? 15.364  -16.546 0.969   1.00 26.97  ? 87  ASN A O   1 
ATOM   706  C CB  . ASN A 1 88 ? 17.483  -16.855 2.751   1.00 27.46  ? 87  ASN A CB  1 
ATOM   707  C CG  . ASN A 1 88 ? 18.532  -16.214 1.867   1.00 27.94  ? 87  ASN A CG  1 
ATOM   708  O OD1 . ASN A 1 88 ? 18.301  -15.155 1.250   1.00 27.33  ? 87  ASN A OD1 1 
ATOM   709  N ND2 . ASN A 1 88 ? 19.726  -16.813 1.840   1.00 27.24  ? 87  ASN A ND2 1 
ATOM   710  N N   . PRO A 1 89 ? 14.349  -14.856 2.022   1.00 23.57  ? 88  PRO A N   1 
ATOM   711  C CA  . PRO A 1 89 ? 13.198  -14.853 1.120   1.00 22.81  ? 88  PRO A CA  1 
ATOM   712  C C   . PRO A 1 89 ? 13.550  -14.390 -0.295  1.00 23.31  ? 88  PRO A C   1 
ATOM   713  O O   . PRO A 1 89 ? 12.755  -14.556 -1.189  1.00 23.93  ? 88  PRO A O   1 
ATOM   714  C CB  . PRO A 1 89 ? 12.242  -13.903 1.856   1.00 22.05  ? 88  PRO A CB  1 
ATOM   715  C CG  . PRO A 1 89 ? 13.183  -12.890 2.478   1.00 22.71  ? 88  PRO A CG  1 
ATOM   716  C CD  . PRO A 1 89 ? 14.258  -13.811 3.063   1.00 21.67  ? 88  PRO A CD  1 
ATOM   717  N N   . HIS A 1 90 ? 14.766  -13.843 -0.504  1.00 21.50  ? 89  HIS A N   1 
ATOM   718  C CA  . HIS A 1 90 ? 15.116  -13.304 -1.818  1.00 24.45  ? 89  HIS A CA  1 
ATOM   719  C C   . HIS A 1 90 ? 16.269  -14.065 -2.482  1.00 22.96  ? 89  HIS A C   1 
ATOM   720  O O   . HIS A 1 90 ? 16.754  -13.660 -3.559  1.00 24.81  ? 89  HIS A O   1 
ATOM   721  C CB  . HIS A 1 90 ? 15.497  -11.824 -1.668  1.00 22.73  ? 89  HIS A CB  1 
ATOM   722  C CG  . HIS A 1 90 ? 14.435  -10.964 -1.092  1.00 26.39  ? 89  HIS A CG  1 
ATOM   723  N ND1 . HIS A 1 90 ? 13.182  -10.813 -1.684  1.00 24.53  ? 89  HIS A ND1 1 
ATOM   724  C CD2 . HIS A 1 90 ? 14.403  -10.284 0.057   1.00 23.82  ? 89  HIS A CD2 1 
ATOM   725  C CE1 . HIS A 1 90 ? 12.467  -9.969  -0.957  1.00 22.92  ? 89  HIS A CE1 1 
ATOM   726  N NE2 . HIS A 1 90 ? 13.176  -9.659  0.121   1.00 25.96  ? 89  HIS A NE2 1 
ATOM   727  N N   . ALA A 1 91 ? 16.611  -15.229 -1.908  1.00 24.94  ? 90  ALA A N   1 
ATOM   728  C CA  . ALA A 1 91 ? 17.649  -16.094 -2.456  1.00 26.39  ? 90  ALA A CA  1 
ATOM   729  C C   . ALA A 1 91 ? 17.193  -16.770 -3.745  1.00 29.00  ? 90  ALA A C   1 
ATOM   730  O O   . ALA A 1 91 ? 16.008  -16.930 -4.009  1.00 27.68  ? 90  ALA A O   1 
ATOM   731  C CB  . ALA A 1 91 ? 18.090  -17.135 -1.446  1.00 25.84  ? 90  ALA A CB  1 
ATOM   732  N N   . SER A 1 92 ? 18.178  -17.257 -4.507  1.00 28.89  ? 91  SER A N   1 
ATOM   733  C CA  . SER A 1 92 ? 17.883  -18.152 -5.616  1.00 31.33  ? 91  SER A CA  1 
ATOM   734  C C   . SER A 1 92 ? 17.579  -19.552 -5.078  1.00 32.37  ? 91  SER A C   1 
ATOM   735  O O   . SER A 1 92 ? 18.393  -20.149 -4.381  1.00 34.81  ? 91  SER A O   1 
ATOM   736  C CB  . SER A 1 92 ? 19.039  -18.178 -6.571  1.00 34.25  ? 91  SER A CB  1 
ATOM   737  O OG  . SER A 1 92 ? 18.833  -19.248 -7.471  1.00 39.89  ? 91  SER A OG  1 
ATOM   738  N N   . TYR A 1 93 ? 16.393  -20.084 -5.376  1.00 31.02  ? 92  TYR A N   1 
ATOM   739  C CA  . TYR A 1 93 ? 16.037  -21.439 -4.979  1.00 34.05  ? 92  TYR A CA  1 
ATOM   740  C C   . TYR A 1 93 ? 15.998  -22.346 -6.214  1.00 43.02  ? 92  TYR A C   1 
ATOM   741  O O   . TYR A 1 93 ? 15.390  -23.416 -6.183  1.00 44.99  ? 92  TYR A O   1 
ATOM   742  C CB  . TYR A 1 93 ? 14.692  -21.462 -4.230  1.00 31.27  ? 92  TYR A CB  1 
ATOM   743  C CG  . TYR A 1 93 ? 14.812  -20.878 -2.831  1.00 30.22  ? 92  TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 93 ? 15.190  -21.661 -1.749  1.00 32.82  ? 92  TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 93 ? 14.570  -19.526 -2.608  1.00 29.94  ? 92  TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 93 ? 15.326  -21.098 -0.485  1.00 35.37  ? 92  TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 93 ? 14.692  -18.959 -1.353  1.00 27.03  ? 92  TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 93 ? 15.068  -19.747 -0.284  1.00 29.33  ? 92  TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 93 ? 15.242  -19.188 0.947   1.00 31.71  ? 92  TYR A OH  1 
ATOM   750  N N   . SER A 1 94 ? 16.670  -21.902 -7.281  1.00 52.21  ? 93  SER A N   1 
ATOM   751  C CA  . SER A 1 94 ? 16.712  -22.529 -8.595  1.00 66.23  ? 93  SER A CA  1 
ATOM   752  C C   . SER A 1 94 ? 17.106  -24.010 -8.490  1.00 75.08  ? 93  SER A C   1 
ATOM   753  O O   . SER A 1 94 ? 17.860  -24.347 -7.542  1.00 80.04  ? 93  SER A O   1 
ATOM   754  C CB  . SER A 1 94 ? 17.674  -21.795 -9.507  1.00 63.44  ? 93  SER A CB  1 
ATOM   755  O OG  . SER A 1 94 ? 17.372  -20.407 -9.561  1.00 73.02  ? 93  SER A OG  1 
ATOM   756  O OXT . SER A 1 94 ? 16.673  -24.771 -9.388  1.00 80.25  ? 93  SER A OXT 1 
ATOM   757  N N   . MET B 1 2  ? 39.007  -10.982 -42.034 1.00 100.49 ? 1   MET B N   1 
ATOM   758  C CA  . MET B 1 2  ? 38.611  -12.078 -42.959 1.00 99.66  ? 1   MET B CA  1 
ATOM   759  C C   . MET B 1 2  ? 37.088  -12.220 -42.943 1.00 88.31  ? 1   MET B C   1 
ATOM   760  O O   . MET B 1 2  ? 36.507  -12.562 -41.911 1.00 80.16  ? 1   MET B O   1 
ATOM   761  C CB  . MET B 1 2  ? 39.279  -13.400 -42.557 1.00 109.42 ? 1   MET B CB  1 
ATOM   762  C CG  . MET B 1 2  ? 39.442  -14.409 -43.690 1.00 114.03 ? 1   MET B CG  1 
ATOM   763  S SD  . MET B 1 2  ? 40.653  -13.940 -44.945 1.00 108.70 ? 1   MET B SD  1 
ATOM   764  C CE  . MET B 1 2  ? 42.113  -13.665 -43.932 1.00 113.18 ? 1   MET B CE  1 
ATOM   765  N N   . PRO B 1 3  ? 36.390  -11.947 -44.075 1.00 76.90  ? 2   PRO B N   1 
ATOM   766  C CA  . PRO B 1 3  ? 34.940  -12.146 -44.150 1.00 70.85  ? 2   PRO B CA  1 
ATOM   767  C C   . PRO B 1 3  ? 34.554  -13.568 -43.756 1.00 65.99  ? 2   PRO B C   1 
ATOM   768  O O   . PRO B 1 3  ? 35.299  -14.516 -44.006 1.00 63.38  ? 2   PRO B O   1 
ATOM   769  C CB  . PRO B 1 3  ? 34.595  -11.819 -45.614 1.00 71.84  ? 2   PRO B CB  1 
ATOM   770  C CG  . PRO B 1 3  ? 35.710  -10.889 -46.044 1.00 67.42  ? 2   PRO B CG  1 
ATOM   771  C CD  . PRO B 1 3  ? 36.950  -11.404 -45.325 1.00 64.87  ? 2   PRO B CD  1 
ATOM   772  N N   . HIS B 1 4  ? 33.396  -13.692 -43.096 1.00 65.36  ? 3   HIS B N   1 
ATOM   773  C CA  . HIS B 1 4  ? 32.902  -14.989 -42.656 1.00 68.38  ? 3   HIS B CA  1 
ATOM   774  C C   . HIS B 1 4  ? 31.502  -15.234 -43.218 1.00 63.83  ? 3   HIS B C   1 
ATOM   775  O O   . HIS B 1 4  ? 30.873  -14.317 -43.757 1.00 62.79  ? 3   HIS B O   1 
ATOM   776  C CB  . HIS B 1 4  ? 33.030  -15.137 -41.134 1.00 73.06  ? 3   HIS B CB  1 
ATOM   777  C CG  . HIS B 1 4  ? 34.409  -15.500 -40.669 1.00 78.56  ? 3   HIS B CG  1 
ATOM   778  N ND1 . HIS B 1 4  ? 35.233  -16.366 -41.359 1.00 74.56  ? 3   HIS B ND1 1 
ATOM   779  C CD2 . HIS B 1 4  ? 35.090  -15.130 -39.568 1.00 71.80  ? 3   HIS B CD2 1 
ATOM   780  C CE1 . HIS B 1 4  ? 36.374  -16.500 -40.695 1.00 70.48  ? 3   HIS B CE1 1 
ATOM   781  N NE2 . HIS B 1 4  ? 36.305  -15.759 -39.606 1.00 70.76  ? 3   HIS B NE2 1 
ATOM   782  N N   . ALA B 1 5  ? 31.035  -16.489 -43.110 1.00 52.32  ? 4   ALA B N   1 
ATOM   783  C CA  . ALA B 1 5  ? 29.740  -16.858 -43.654 1.00 48.91  ? 4   ALA B CA  1 
ATOM   784  C C   . ALA B 1 5  ? 28.692  -15.890 -43.124 1.00 48.31  ? 4   ALA B C   1 
ATOM   785  O O   . ALA B 1 5  ? 27.933  -15.309 -43.895 1.00 50.14  ? 4   ALA B O   1 
ATOM   786  C CB  . ALA B 1 5  ? 29.398  -18.277 -43.283 1.00 56.53  ? 4   ALA B CB  1 
ATOM   787  N N   . PHE B 1 6  ? 28.652  -15.768 -41.796 1.00 44.12  ? 5   PHE B N   1 
ATOM   788  C CA  . PHE B 1 6  ? 27.888  -14.723 -41.142 1.00 49.36  ? 5   PHE B CA  1 
ATOM   789  C C   . PHE B 1 6  ? 28.807  -13.538 -40.855 1.00 49.91  ? 5   PHE B C   1 
ATOM   790  O O   . PHE B 1 6  ? 29.927  -13.722 -40.375 1.00 51.71  ? 5   PHE B O   1 
ATOM   791  C CB  . PHE B 1 6  ? 27.306  -15.215 -39.816 1.00 47.23  ? 5   PHE B CB  1 
ATOM   792  C CG  . PHE B 1 6  ? 26.190  -16.244 -39.934 1.00 39.42  ? 5   PHE B CG  1 
ATOM   793  C CD1 . PHE B 1 6  ? 24.879  -15.847 -40.161 1.00 37.40  ? 5   PHE B CD1 1 
ATOM   794  C CD2 . PHE B 1 6  ? 26.461  -17.599 -39.796 1.00 39.39  ? 5   PHE B CD2 1 
ATOM   795  C CE1 . PHE B 1 6  ? 23.865  -16.784 -40.250 1.00 37.49  ? 5   PHE B CE1 1 
ATOM   796  C CE2 . PHE B 1 6  ? 25.440  -18.536 -39.881 1.00 33.33  ? 5   PHE B CE2 1 
ATOM   797  C CZ  . PHE B 1 6  ? 24.150  -18.125 -40.096 1.00 32.93  ? 5   PHE B CZ  1 
ATOM   798  N N   . LYS B 1 7  ? 28.302  -12.327 -41.123 1.00 48.76  ? 6   LYS B N   1 
ATOM   799  C CA  . LYS B 1 7  ? 29.039  -11.098 -40.861 1.00 50.12  ? 6   LYS B CA  1 
ATOM   800  C C   . LYS B 1 7  ? 28.247  -10.221 -39.895 1.00 46.76  ? 6   LYS B C   1 
ATOM   801  O O   . LYS B 1 7  ? 27.013  -10.270 -39.880 1.00 43.29  ? 6   LYS B O   1 
ATOM   802  C CB  . LYS B 1 7  ? 29.296  -10.335 -42.161 1.00 48.34  ? 6   LYS B CB  1 
ATOM   803  C CG  . LYS B 1 7  ? 28.053  -9.976  -42.946 1.00 49.37  ? 6   LYS B CG  1 
ATOM   804  C CD  . LYS B 1 7  ? 28.416  -9.259  -44.240 1.00 57.49  ? 6   LYS B CD  1 
ATOM   805  C CE  . LYS B 1 7  ? 27.194  -8.827  -44.978 1.00 58.13  ? 6   LYS B CE  1 
ATOM   806  N NZ  . LYS B 1 7  ? 26.322  -9.966  -45.290 1.00 60.24  ? 6   LYS B NZ  1 
ATOM   807  N N   . PRO B 1 8  ? 28.916  -9.376  -39.075 1.00 51.90  ? 7   PRO B N   1 
ATOM   808  C CA  . PRO B 1 8  ? 28.206  -8.499  -38.141 1.00 47.66  ? 7   PRO B CA  1 
ATOM   809  C C   . PRO B 1 8  ? 27.137  -7.676  -38.850 1.00 45.05  ? 7   PRO B C   1 
ATOM   810  O O   . PRO B 1 8  ? 27.348  -7.200  -39.967 1.00 48.68  ? 7   PRO B O   1 
ATOM   811  C CB  . PRO B 1 8  ? 29.349  -7.661  -37.569 1.00 49.39  ? 7   PRO B CB  1 
ATOM   812  C CG  . PRO B 1 8  ? 30.524  -8.612  -37.600 1.00 49.89  ? 7   PRO B CG  1 
ATOM   813  C CD  . PRO B 1 8  ? 30.382  -9.218  -38.989 1.00 55.24  ? 7   PRO B CD  1 
ATOM   814  N N   . GLY B 1 9  ? 25.965  -7.577  -38.206 1.00 42.81  ? 8   GLY B N   1 
ATOM   815  C CA  . GLY B 1 9  ? 24.798  -6.942  -38.790 1.00 37.77  ? 8   GLY B CA  1 
ATOM   816  C C   . GLY B 1 9  ? 23.840  -7.942  -39.433 1.00 34.29  ? 8   GLY B C   1 
ATOM   817  O O   . GLY B 1 9  ? 22.705  -7.596  -39.757 1.00 34.72  ? 8   GLY B O   1 
ATOM   818  N N   . ASP B 1 10 ? 24.298  -9.183  -39.648 1.00 36.44  ? 9   ASP B N   1 
ATOM   819  C CA  . ASP B 1 10 ? 23.449  -10.224 -40.217 1.00 32.83  ? 9   ASP B CA  1 
ATOM   820  C C   . ASP B 1 10 ? 22.309  -10.529 -39.239 1.00 28.59  ? 9   ASP B C   1 
ATOM   821  O O   . ASP B 1 10 ? 22.536  -10.618 -38.040 1.00 31.40  ? 9   ASP B O   1 
ATOM   822  C CB  . ASP B 1 10 ? 24.245  -11.493 -40.502 1.00 36.14  ? 9   ASP B CB  1 
ATOM   823  C CG  . ASP B 1 10 ? 24.947  -11.557 -41.855 1.00 41.94  ? 9   ASP B CG  1 
ATOM   824  O OD1 . ASP B 1 10 ? 24.598  -10.742 -42.736 1.00 41.88  ? 9   ASP B OD1 1 
ATOM   825  O OD2 . ASP B 1 10 ? 25.837  -12.431 -42.013 1.00 43.03  ? 9   ASP B OD2 1 
ATOM   826  N N   . LEU B 1 11 ? 21.098  -10.649 -39.762 1.00 29.33  ? 10  LEU B N   1 
ATOM   827  C CA  . LEU B 1 11 ? 19.952  -10.884 -38.897 1.00 31.96  ? 10  LEU B CA  1 
ATOM   828  C C   . LEU B 1 11 ? 19.591  -12.366 -38.945 1.00 30.68  ? 10  LEU B C   1 
ATOM   829  O O   . LEU B 1 11 ? 19.701  -12.975 -39.997 1.00 31.18  ? 10  LEU B O   1 
ATOM   830  C CB  . LEU B 1 11 ? 18.845  -9.996  -39.447 1.00 31.50  ? 10  LEU B CB  1 
ATOM   831  C CG  . LEU B 1 11 ? 19.150  -8.490  -39.466 1.00 29.97  ? 10  LEU B CG  1 
ATOM   832  C CD1 . LEU B 1 11 ? 17.844  -7.830  -39.844 1.00 30.05  ? 10  LEU B CD1 1 
ATOM   833  C CD2 . LEU B 1 11 ? 19.678  -8.008  -38.109 1.00 29.70  ? 10  LEU B CD2 1 
ATOM   834  N N   . VAL B 1 12 ? 19.215  -12.946 -37.792 1.00 27.20  ? 11  VAL B N   1 
ATOM   835  C CA  . VAL B 1 12 ? 18.977  -14.378 -37.704 1.00 26.70  ? 11  VAL B CA  1 
ATOM   836  C C   . VAL B 1 12 ? 17.852  -14.622 -36.698 1.00 29.96  ? 11  VAL B C   1 
ATOM   837  O O   . VAL B 1 12 ? 17.455  -13.708 -35.962 1.00 27.04  ? 11  VAL B O   1 
ATOM   838  C CB  . VAL B 1 12 ? 20.250  -15.118 -37.238 1.00 29.19  ? 11  VAL B CB  1 
ATOM   839  C CG1 . VAL B 1 12 ? 21.409  -14.952 -38.222 1.00 29.86  ? 11  VAL B CG1 1 
ATOM   840  C CG2 . VAL B 1 12 ? 20.664  -14.729 -35.813 1.00 27.54  ? 11  VAL B CG2 1 
ATOM   841  N N   . PHE B 1 13 ? 17.333  -15.853 -36.698 1.00 26.68  ? 12  PHE B N   1 
ATOM   842  C CA  . PHE B 1 13 ? 16.814  -16.413 -35.455 1.00 28.53  ? 12  PHE B CA  1 
ATOM   843  C C   . PHE B 1 13 ? 17.912  -17.270 -34.839 1.00 32.60  ? 12  PHE B C   1 
ATOM   844  O O   . PHE B 1 13 ? 18.548  -18.052 -35.563 1.00 33.95  ? 12  PHE B O   1 
ATOM   845  C CB  . PHE B 1 13 ? 15.521  -17.193 -35.656 1.00 27.30  ? 12  PHE B CB  1 
ATOM   846  C CG  . PHE B 1 13 ? 14.346  -16.359 -36.118 1.00 29.47  ? 12  PHE B CG  1 
ATOM   847  C CD1 . PHE B 1 13 ? 14.125  -16.122 -37.473 1.00 31.22  ? 12  PHE B CD1 1 
ATOM   848  C CD2 . PHE B 1 13 ? 13.478  -15.791 -35.196 1.00 30.64  ? 12  PHE B CD2 1 
ATOM   849  C CE1 . PHE B 1 13 ? 13.043  -15.360 -37.884 1.00 36.60  ? 12  PHE B CE1 1 
ATOM   850  C CE2 . PHE B 1 13 ? 12.387  -15.043 -35.611 1.00 31.02  ? 12  PHE B CE2 1 
ATOM   851  C CZ  . PHE B 1 13 ? 12.172  -14.827 -36.960 1.00 36.97  ? 12  PHE B CZ  1 
ATOM   852  N N   . ALA B 1 14 ? 18.100  -17.126 -33.506 1.00 28.63  ? 13  ALA B N   1 
ATOM   853  C CA  . ALA B 1 14 ? 19.135  -17.824 -32.763 1.00 28.52  ? 13  ALA B CA  1 
ATOM   854  C C   . ALA B 1 14 ? 18.486  -18.782 -31.756 1.00 29.92  ? 13  ALA B C   1 
ATOM   855  O O   . ALA B 1 14 ? 17.521  -18.412 -31.104 1.00 29.40  ? 13  ALA B O   1 
ATOM   856  C CB  . ALA B 1 14 ? 20.029  -16.824 -32.080 1.00 29.11  ? 13  ALA B CB  1 
ATOM   857  N N   . LYS B 1 15 ? 18.996  -20.013 -31.680 1.00 29.89  ? 14  LYS B N   1 
ATOM   858  C CA  . LYS B 1 15 ? 18.358  -21.086 -30.922 1.00 30.81  ? 14  LYS B CA  1 
ATOM   859  C C   . LYS B 1 15 ? 19.191  -21.394 -29.688 1.00 30.50  ? 14  LYS B C   1 
ATOM   860  O O   . LYS B 1 15 ? 20.365  -21.741 -29.806 1.00 33.55  ? 14  LYS B O   1 
ATOM   861  C CB  . LYS B 1 15 ? 18.107  -22.344 -31.773 1.00 31.12  ? 14  LYS B CB  1 
ATOM   862  C CG  . LYS B 1 15 ? 17.336  -23.464 -31.054 1.00 30.01  ? 14  LYS B CG  1 
ATOM   863  C CD  . LYS B 1 15 ? 15.902  -23.007 -30.748 1.00 32.27  ? 14  LYS B CD  1 
ATOM   864  C CE  . LYS B 1 15 ? 14.989  -24.108 -30.187 1.00 31.69  ? 14  LYS B CE  1 
ATOM   865  N NZ  . LYS B 1 15 ? 15.374  -24.395 -28.807 1.00 30.38  ? 14  LYS B NZ  1 
ATOM   866  N N   . MET B 1 16 ? 18.558  -21.256 -28.513 1.00 33.32  ? 15  MET B N   1 
ATOM   867  C CA  . MET B 1 16 ? 19.141  -21.618 -27.228 1.00 36.72  ? 15  MET B CA  1 
ATOM   868  C C   . MET B 1 16 ? 18.279  -22.725 -26.622 1.00 34.82  ? 15  MET B C   1 
ATOM   869  O O   . MET B 1 16 ? 17.050  -22.674 -26.728 1.00 29.36  ? 15  MET B O   1 
ATOM   870  C CB  . MET B 1 16 ? 19.108  -20.431 -26.254 1.00 39.86  ? 15  MET B CB  1 
ATOM   871  C CG  . MET B 1 16 ? 19.823  -19.186 -26.736 1.00 42.28  ? 15  MET B CG  1 
ATOM   872  S SD  . MET B 1 16 ? 21.601  -19.182 -26.436 1.00 49.09  ? 15  MET B SD  1 
ATOM   873  C CE  . MET B 1 16 ? 21.717  -18.859 -24.673 1.00 40.20  ? 15  MET B CE  1 
ATOM   874  N N   . LYS B 1 17 ? 18.920  -23.694 -25.959 1.00 34.63  ? 16  LYS B N   1 
ATOM   875  C CA  . LYS B 1 17 ? 18.177  -24.742 -25.265 1.00 42.27  ? 16  LYS B CA  1 
ATOM   876  C C   . LYS B 1 17 ? 17.209  -24.096 -24.267 1.00 36.40  ? 16  LYS B C   1 
ATOM   877  O O   . LYS B 1 17 ? 17.602  -23.224 -23.505 1.00 41.02  ? 16  LYS B O   1 
ATOM   878  C CB  . LYS B 1 17 ? 19.158  -25.698 -24.577 1.00 50.07  ? 16  LYS B CB  1 
ATOM   879  C CG  . LYS B 1 17 ? 18.554  -27.007 -24.059 1.00 54.87  ? 16  LYS B CG  1 
ATOM   880  C CD  . LYS B 1 17 ? 19.588  -27.898 -23.374 1.00 60.03  ? 16  LYS B CD  1 
ATOM   881  C CE  . LYS B 1 17 ? 19.068  -29.268 -23.060 1.00 60.33  ? 16  LYS B CE  1 
ATOM   882  N NZ  . LYS B 1 17 ? 18.039  -29.239 -22.018 1.00 55.60  ? 16  LYS B NZ  1 
ATOM   883  N N   . GLY B 1 18 ? 15.931  -24.481 -24.319 1.00 38.93  ? 17  GLY B N   1 
ATOM   884  C CA  . GLY B 1 18 ? 14.950  -23.940 -23.395 1.00 38.96  ? 17  GLY B CA  1 
ATOM   885  C C   . GLY B 1 18 ? 14.087  -22.826 -23.992 1.00 40.74  ? 17  GLY B C   1 
ATOM   886  O O   . GLY B 1 18 ? 13.125  -22.402 -23.358 1.00 36.38  ? 17  GLY B O   1 
ATOM   887  N N   . TYR B 1 19 ? 14.427  -22.340 -25.201 1.00 35.74  ? 18  TYR B N   1 
ATOM   888  C CA  . TYR B 1 19 ? 13.783  -21.133 -25.696 1.00 32.07  ? 18  TYR B CA  1 
ATOM   889  C C   . TYR B 1 19 ? 13.427  -21.320 -27.164 1.00 30.06  ? 18  TYR B C   1 
ATOM   890  O O   . TYR B 1 19 ? 14.114  -22.046 -27.870 1.00 34.01  ? 18  TYR B O   1 
ATOM   891  C CB  . TYR B 1 19 ? 14.756  -19.953 -25.589 1.00 28.36  ? 18  TYR B CB  1 
ATOM   892  C CG  . TYR B 1 19 ? 15.180  -19.732 -24.146 1.00 31.10  ? 18  TYR B CG  1 
ATOM   893  C CD1 . TYR B 1 19 ? 14.410  -18.957 -23.282 1.00 34.88  ? 18  TYR B CD1 1 
ATOM   894  C CD2 . TYR B 1 19 ? 16.325  -20.340 -23.649 1.00 35.86  ? 18  TYR B CD2 1 
ATOM   895  C CE1 . TYR B 1 19 ? 14.779  -18.803 -21.952 1.00 36.65  ? 18  TYR B CE1 1 
ATOM   896  C CE2 . TYR B 1 19 ? 16.713  -20.175 -22.329 1.00 41.86  ? 18  TYR B CE2 1 
ATOM   897  C CZ  . TYR B 1 19 ? 15.939  -19.400 -21.486 1.00 41.40  ? 18  TYR B CZ  1 
ATOM   898  O OH  . TYR B 1 19 ? 16.355  -19.272 -20.195 1.00 46.33  ? 18  TYR B OH  1 
ATOM   899  N N   . PRO B 1 20 ? 12.351  -20.678 -27.659 1.00 31.57  ? 19  PRO B N   1 
ATOM   900  C CA  . PRO B 1 20 ? 12.062  -20.684 -29.097 1.00 27.15  ? 19  PRO B CA  1 
ATOM   901  C C   . PRO B 1 20 ? 13.165  -19.976 -29.890 1.00 27.79  ? 19  PRO B C   1 
ATOM   902  O O   . PRO B 1 20 ? 13.910  -19.162 -29.350 1.00 27.95  ? 19  PRO B O   1 
ATOM   903  C CB  . PRO B 1 20 ? 10.740  -19.956 -29.162 1.00 26.56  ? 19  PRO B CB  1 
ATOM   904  C CG  . PRO B 1 20 ? 10.786  -18.979 -27.989 1.00 32.06  ? 19  PRO B CG  1 
ATOM   905  C CD  . PRO B 1 20 ? 11.447  -19.806 -26.899 1.00 31.38  ? 19  PRO B CD  1 
ATOM   906  N N   . HIS B 1 21 ? 13.289  -20.338 -31.178 1.00 25.81  ? 20  HIS B N   1 
ATOM   907  C CA  . HIS B 1 21 ? 14.180  -19.615 -32.079 1.00 27.60  ? 20  HIS B CA  1 
ATOM   908  C C   . HIS B 1 21 ? 13.929  -18.120 -31.929 1.00 25.59  ? 20  HIS B C   1 
ATOM   909  O O   . HIS B 1 21 ? 12.788  -17.662 -32.028 1.00 28.22  ? 20  HIS B O   1 
ATOM   910  C CB  . HIS B 1 21 ? 13.871  -20.046 -33.521 1.00 26.67  ? 20  HIS B CB  1 
ATOM   911  C CG  . HIS B 1 21 ? 14.088  -21.512 -33.717 1.00 27.46  ? 20  HIS B CG  1 
ATOM   912  N ND1 . HIS B 1 21 ? 13.135  -22.448 -33.370 1.00 30.32  ? 20  HIS B ND1 1 
ATOM   913  C CD2 . HIS B 1 21 ? 15.144  -22.207 -34.184 1.00 30.41  ? 20  HIS B CD2 1 
ATOM   914  C CE1 . HIS B 1 21 ? 13.594  -23.665 -33.650 1.00 31.14  ? 20  HIS B CE1 1 
ATOM   915  N NE2 . HIS B 1 21 ? 14.818  -23.549 -34.132 1.00 31.42  ? 20  HIS B NE2 1 
ATOM   916  N N   . TRP B 1 22 ? 14.999  -17.364 -31.702 1.00 25.06  ? 21  TRP B N   1 
ATOM   917  C CA  . TRP B 1 22 ? 14.799  -16.041 -31.129 1.00 25.99  ? 21  TRP B CA  1 
ATOM   918  C C   . TRP B 1 22 ? 15.351  -14.974 -32.073 1.00 29.46  ? 21  TRP B C   1 
ATOM   919  O O   . TRP B 1 22 ? 16.494  -15.115 -32.510 1.00 27.69  ? 21  TRP B O   1 
ATOM   920  C CB  . TRP B 1 22 ? 15.467  -15.972 -29.751 1.00 25.89  ? 21  TRP B CB  1 
ATOM   921  C CG  . TRP B 1 22 ? 14.986  -14.815 -28.915 1.00 28.23  ? 21  TRP B CG  1 
ATOM   922  C CD1 . TRP B 1 22 ? 15.287  -13.492 -29.063 1.00 26.96  ? 21  TRP B CD1 1 
ATOM   923  C CD2 . TRP B 1 22 ? 14.039  -14.897 -27.819 1.00 29.38  ? 21  TRP B CD2 1 
ATOM   924  N NE1 . TRP B 1 22 ? 14.622  -12.747 -28.116 1.00 29.79  ? 21  TRP B NE1 1 
ATOM   925  C CE2 . TRP B 1 22 ? 13.835  -13.578 -27.349 1.00 29.73  ? 21  TRP B CE2 1 
ATOM   926  C CE3 . TRP B 1 22 ? 13.359  -15.954 -27.196 1.00 28.17  ? 21  TRP B CE3 1 
ATOM   927  C CZ2 . TRP B 1 22 ? 12.975  -13.293 -26.279 1.00 30.11  ? 21  TRP B CZ2 1 
ATOM   928  C CZ3 . TRP B 1 22 ? 12.493  -15.669 -26.153 1.00 29.88  ? 21  TRP B CZ3 1 
ATOM   929  C CH2 . TRP B 1 22 ? 12.287  -14.352 -25.712 1.00 27.21  ? 21  TRP B CH2 1 
ATOM   930  N N   . PRO B 1 23 ? 14.577  -13.906 -32.409 1.00 27.95  ? 22  PRO B N   1 
ATOM   931  C CA  . PRO B 1 23 ? 15.060  -12.826 -33.291 1.00 29.69  ? 22  PRO B CA  1 
ATOM   932  C C   . PRO B 1 23 ? 16.352  -12.227 -32.747 1.00 29.14  ? 22  PRO B C   1 
ATOM   933  O O   . PRO B 1 23 ? 16.476  -11.956 -31.552 1.00 30.39  ? 22  PRO B O   1 
ATOM   934  C CB  . PRO B 1 23 ? 13.881  -11.817 -33.322 1.00 31.57  ? 22  PRO B CB  1 
ATOM   935  C CG  . PRO B 1 23 ? 13.084  -12.145 -32.048 1.00 27.70  ? 22  PRO B CG  1 
ATOM   936  C CD  . PRO B 1 23 ? 13.194  -13.670 -31.957 1.00 28.16  ? 22  PRO B CD  1 
ATOM   937  N N   . ALA B 1 24 ? 17.368  -12.073 -33.601 1.00 25.70  ? 23  ALA B N   1 
ATOM   938  C CA  . ALA B 1 24 ? 18.698  -11.783 -33.081 1.00 26.41  ? 23  ALA B CA  1 
ATOM   939  C C   . ALA B 1 24 ? 19.582  -11.274 -34.214 1.00 28.93  ? 23  ALA B C   1 
ATOM   940  O O   . ALA B 1 24 ? 19.166  -11.293 -35.376 1.00 30.86  ? 23  ALA B O   1 
ATOM   941  C CB  . ALA B 1 24 ? 19.304  -13.034 -32.480 1.00 28.52  ? 23  ALA B CB  1 
ATOM   942  N N   . ARG B 1 25 ? 20.803  -10.867 -33.843 1.00 30.18  ? 24  ARG B N   1 
ATOM   943  C CA  . ARG B 1 25 ? 21.750  -10.364 -34.825 1.00 34.33  ? 24  ARG B CA  1 
ATOM   944  C C   . ARG B 1 25 ? 23.146  -10.835 -34.454 1.00 28.29  ? 24  ARG B C   1 
ATOM   945  O O   . ARG B 1 25 ? 23.426  -11.161 -33.302 1.00 30.12  ? 24  ARG B O   1 
ATOM   946  C CB  . ARG B 1 25 ? 21.715  -8.837  -34.975 1.00 31.00  ? 24  ARG B CB  1 
ATOM   947  C CG  . ARG B 1 25 ? 22.378  -8.096  -33.825 1.00 33.96  ? 24  ARG B CG  1 
ATOM   948  C CD  . ARG B 1 25 ? 22.127  -6.591  -33.977 1.00 32.84  ? 24  ARG B CD  1 
ATOM   949  N NE  . ARG B 1 25 ? 22.667  -5.838  -32.846 1.00 29.70  ? 24  ARG B NE  1 
ATOM   950  C CZ  . ARG B 1 25 ? 22.351  -4.566  -32.550 1.00 29.99  ? 24  ARG B CZ  1 
ATOM   951  N NH1 . ARG B 1 25 ? 21.418  -3.919  -33.233 1.00 28.73  ? 24  ARG B NH1 1 
ATOM   952  N NH2 . ARG B 1 25 ? 22.947  -3.985  -31.528 1.00 31.06  ? 24  ARG B NH2 1 
ATOM   953  N N   . ILE B 1 26 ? 24.000  -10.909 -35.477 1.00 30.53  ? 25  ILE B N   1 
ATOM   954  C CA  . ILE B 1 26 ? 25.438  -11.030 -35.295 1.00 32.65  ? 25  ILE B CA  1 
ATOM   955  C C   . ILE B 1 26 ? 25.963  -9.637  -34.953 1.00 32.00  ? 25  ILE B C   1 
ATOM   956  O O   . ILE B 1 26 ? 25.799  -8.713  -35.743 1.00 35.80  ? 25  ILE B O   1 
ATOM   957  C CB  . ILE B 1 26 ? 26.107  -11.523 -36.597 1.00 33.18  ? 25  ILE B CB  1 
ATOM   958  C CG1 . ILE B 1 26 ? 25.372  -12.717 -37.231 1.00 33.56  ? 25  ILE B CG1 1 
ATOM   959  C CG2 . ILE B 1 26 ? 27.615  -11.767 -36.406 1.00 32.27  ? 25  ILE B CG2 1 
ATOM   960  C CD1 . ILE B 1 26 ? 25.426  -14.004 -36.424 1.00 32.88  ? 25  ILE B CD1 1 
ATOM   961  N N   . ASP B 1 27 ? 26.637  -9.526  -33.812 1.00 35.67  ? 26  ASP B N   1 
ATOM   962  C CA  . ASP B 1 27 ? 27.357  -8.331  -33.402 1.00 41.70  ? 26  ASP B CA  1 
ATOM   963  C C   . ASP B 1 27 ? 28.845  -8.449  -33.766 1.00 47.06  ? 26  ASP B C   1 
ATOM   964  O O   . ASP B 1 27 ? 29.312  -9.524  -34.129 1.00 43.39  ? 26  ASP B O   1 
ATOM   965  C CB  . ASP B 1 27 ? 27.231  -8.190  -31.899 1.00 39.40  ? 26  ASP B CB  1 
ATOM   966  C CG  . ASP B 1 27 ? 26.002  -7.458  -31.384 1.00 42.40  ? 26  ASP B CG  1 
ATOM   967  O OD1 . ASP B 1 27 ? 25.200  -6.980  -32.217 1.00 41.14  ? 26  ASP B OD1 1 
ATOM   968  O OD2 . ASP B 1 27 ? 25.880  -7.357  -30.141 1.00 42.66  ? 26  ASP B OD2 1 
ATOM   969  N N   A ASP B 1 28 ? 29.598  -7.372  -33.505 0.51 52.79  ? 27  ASP B N   1 
ATOM   970  N N   B ASP B 1 28 ? 29.556  -7.311  -33.752 0.49 47.30  ? 27  ASP B N   1 
ATOM   971  C CA  A ASP B 1 28 ? 31.001  -7.250  -33.872 0.51 57.96  ? 27  ASP B CA  1 
ATOM   972  C CA  B ASP B 1 28 ? 30.991  -7.266  -33.999 0.49 47.56  ? 27  ASP B CA  1 
ATOM   973  C C   A ASP B 1 28 ? 31.862  -8.142  -32.966 0.51 60.70  ? 27  ASP B C   1 
ATOM   974  C C   B ASP B 1 28 ? 31.738  -7.626  -32.712 0.49 46.97  ? 27  ASP B C   1 
ATOM   975  O O   A ASP B 1 28 ? 32.625  -7.577  -32.132 0.51 64.83  ? 27  ASP B O   1 
ATOM   976  O O   B ASP B 1 28 ? 31.231  -7.231  -31.643 0.49 46.04  ? 27  ASP B O   1 
ATOM   977  C CB  A ASP B 1 28 ? 31.418  -5.786  -33.885 0.51 57.25  ? 27  ASP B CB  1 
ATOM   978  C CB  B ASP B 1 28 ? 31.445  -5.914  -34.537 0.49 45.13  ? 27  ASP B CB  1 
ATOM   979  C CG  A ASP B 1 28 ? 30.289  -4.811  -34.188 0.51 56.42  ? 27  ASP B CG  1 
ATOM   980  C CG  B ASP B 1 28 ? 31.911  -5.891  -35.987 0.49 43.67  ? 27  ASP B CG  1 
ATOM   981  O OD1 A ASP B 1 28 ? 30.227  -4.325  -35.335 0.51 54.52  ? 27  ASP B OD1 1 
ATOM   982  O OD1 B ASP B 1 28 ? 32.892  -6.596  -36.300 0.49 46.24  ? 27  ASP B OD1 1 
ATOM   983  O OD2 A ASP B 1 28 ? 29.474  -4.559  -33.270 0.51 54.34  ? 27  ASP B OD2 1 
ATOM   984  O OD2 B ASP B 1 28 ? 31.312  -5.152  -36.790 0.49 41.93  ? 27  ASP B OD2 1 
ATOM   985  N N   . VAL B 1 34 ? 35.645  -10.127 -24.009 1.00 73.50  ? 33  VAL B N   1 
ATOM   986  C CA  . VAL B 1 34 ? 36.159  -11.469 -24.423 1.00 78.92  ? 33  VAL B CA  1 
ATOM   987  C C   . VAL B 1 34 ? 35.838  -11.671 -25.902 1.00 81.73  ? 33  VAL B C   1 
ATOM   988  O O   . VAL B 1 34 ? 34.756  -11.301 -26.348 1.00 85.27  ? 33  VAL B O   1 
ATOM   989  C CB  . VAL B 1 34 ? 35.570  -12.599 -23.551 1.00 79.93  ? 33  VAL B CB  1 
ATOM   990  C CG1 . VAL B 1 34 ? 34.045  -12.596 -23.526 1.00 82.39  ? 33  VAL B CG1 1 
ATOM   991  C CG2 . VAL B 1 34 ? 36.083  -13.977 -23.958 1.00 79.91  ? 33  VAL B CG2 1 
ATOM   992  N N   . LYS B 1 35 ? 36.788  -12.257 -26.646 1.00 84.38  ? 34  LYS B N   1 
ATOM   993  C CA  . LYS B 1 35 ? 36.571  -12.656 -28.032 1.00 85.25  ? 34  LYS B CA  1 
ATOM   994  C C   . LYS B 1 35 ? 35.711  -13.925 -28.078 1.00 82.63  ? 34  LYS B C   1 
ATOM   995  O O   . LYS B 1 35 ? 35.693  -14.694 -27.113 1.00 86.40  ? 34  LYS B O   1 
ATOM   996  C CB  . LYS B 1 35 ? 37.912  -12.858 -28.749 1.00 78.21  ? 34  LYS B CB  1 
ATOM   997  N N   . PRO B 1 36 ? 34.961  -14.190 -29.180 1.00 75.81  ? 35  PRO B N   1 
ATOM   998  C CA  . PRO B 1 36 ? 34.188  -15.434 -29.300 1.00 67.35  ? 35  PRO B CA  1 
ATOM   999  C C   . PRO B 1 36 ? 35.104  -16.655 -29.332 1.00 59.83  ? 35  PRO B C   1 
ATOM   1000 O O   . PRO B 1 36 ? 36.220  -16.573 -29.837 1.00 68.81  ? 35  PRO B O   1 
ATOM   1001 C CB  . PRO B 1 36 ? 33.393  -15.275 -30.615 1.00 65.36  ? 35  PRO B CB  1 
ATOM   1002 C CG  . PRO B 1 36 ? 34.169  -14.228 -31.397 1.00 66.94  ? 35  PRO B CG  1 
ATOM   1003 C CD  . PRO B 1 36 ? 34.801  -13.312 -30.355 1.00 70.29  ? 35  PRO B CD  1 
ATOM   1004 N N   . PRO B 1 37 ? 34.686  -17.820 -28.783 1.00 58.22  ? 36  PRO B N   1 
ATOM   1005 C CA  . PRO B 1 37 ? 35.416  -19.066 -29.016 1.00 52.51  ? 36  PRO B CA  1 
ATOM   1006 C C   . PRO B 1 37 ? 35.469  -19.332 -30.523 1.00 61.68  ? 36  PRO B C   1 
ATOM   1007 O O   . PRO B 1 37 ? 34.711  -18.739 -31.297 1.00 55.54  ? 36  PRO B O   1 
ATOM   1008 C CB  . PRO B 1 37 ? 34.586  -20.133 -28.269 1.00 50.20  ? 36  PRO B CB  1 
ATOM   1009 C CG  . PRO B 1 37 ? 33.759  -19.352 -27.272 1.00 51.53  ? 36  PRO B CG  1 
ATOM   1010 C CD  . PRO B 1 37 ? 33.510  -17.996 -27.916 1.00 53.00  ? 36  PRO B CD  1 
ATOM   1011 N N   . PRO B 1 38 ? 36.364  -20.226 -31.004 1.00 63.31  ? 37  PRO B N   1 
ATOM   1012 C CA  . PRO B 1 38 ? 36.383  -20.584 -32.427 1.00 65.54  ? 37  PRO B CA  1 
ATOM   1013 C C   . PRO B 1 38 ? 35.058  -21.194 -32.901 1.00 61.66  ? 37  PRO B C   1 
ATOM   1014 O O   . PRO B 1 38 ? 34.395  -21.924 -32.162 1.00 58.49  ? 37  PRO B O   1 
ATOM   1015 C CB  . PRO B 1 38 ? 37.575  -21.557 -32.571 1.00 64.85  ? 37  PRO B CB  1 
ATOM   1016 C CG  . PRO B 1 38 ? 38.376  -21.400 -31.283 1.00 59.95  ? 37  PRO B CG  1 
ATOM   1017 C CD  . PRO B 1 38 ? 37.400  -20.922 -30.217 1.00 65.84  ? 37  PRO B CD  1 
ATOM   1018 N N   . ASN B 1 39 ? 34.668  -20.853 -34.135 1.00 57.81  ? 38  ASN B N   1 
ATOM   1019 C CA  . ASN B 1 39 ? 33.478  -21.395 -34.778 1.00 55.86  ? 38  ASN B CA  1 
ATOM   1020 C C   . ASN B 1 39 ? 32.203  -20.676 -34.333 1.00 52.42  ? 38  ASN B C   1 
ATOM   1021 O O   . ASN B 1 39 ? 31.168  -20.849 -34.968 1.00 43.42  ? 38  ASN B O   1 
ATOM   1022 C CB  . ASN B 1 39 ? 33.306  -22.892 -34.538 1.00 51.08  ? 38  ASN B CB  1 
ATOM   1023 C CG  . ASN B 1 39 ? 34.492  -23.732 -34.961 1.00 67.18  ? 38  ASN B CG  1 
ATOM   1024 O OD1 . ASN B 1 39 ? 34.529  -24.930 -34.649 1.00 76.36  ? 38  ASN B OD1 1 
ATOM   1025 N ND2 . ASN B 1 39 ? 35.469  -23.149 -35.646 1.00 61.74  ? 38  ASN B ND2 1 
ATOM   1026 N N   . LYS B 1 40 ? 32.271  -19.879 -33.254 1.00 54.04  ? 39  LYS B N   1 
ATOM   1027 C CA  . LYS B 1 40 ? 31.086  -19.267 -32.664 1.00 47.79  ? 39  LYS B CA  1 
ATOM   1028 C C   . LYS B 1 40 ? 31.037  -17.762 -32.954 1.00 48.86  ? 39  LYS B C   1 
ATOM   1029 O O   . LYS B 1 40 ? 32.046  -17.138 -33.283 1.00 47.93  ? 39  LYS B O   1 
ATOM   1030 C CB  . LYS B 1 40 ? 31.030  -19.683 -31.190 1.00 45.99  ? 39  LYS B CB  1 
ATOM   1031 C CG  . LYS B 1 40 ? 30.920  -21.198 -31.012 1.00 53.15  ? 39  LYS B CG  1 
ATOM   1032 C CD  . LYS B 1 40 ? 30.887  -21.692 -29.572 1.00 62.94  ? 39  LYS B CD  1 
ATOM   1033 C CE  . LYS B 1 40 ? 29.536  -21.774 -28.933 1.00 68.47  ? 39  LYS B CE  1 
ATOM   1034 N NZ  . LYS B 1 40 ? 28.780  -22.932 -29.419 1.00 80.29  ? 39  LYS B NZ  1 
ATOM   1035 N N   . TYR B 1 41 ? 29.840  -17.174 -32.860 1.00 40.37  ? 40  TYR B N   1 
ATOM   1036 C CA  . TYR B 1 41 ? 29.722  -15.746 -33.106 1.00 42.26  ? 40  TYR B CA  1 
ATOM   1037 C C   . TYR B 1 41 ? 29.108  -15.044 -31.899 1.00 44.03  ? 40  TYR B C   1 
ATOM   1038 O O   . TYR B 1 41 ? 28.354  -15.661 -31.151 1.00 43.95  ? 40  TYR B O   1 
ATOM   1039 C CB  . TYR B 1 41 ? 28.776  -15.494 -34.279 1.00 42.89  ? 40  TYR B CB  1 
ATOM   1040 C CG  . TYR B 1 41 ? 29.246  -15.961 -35.648 1.00 45.48  ? 40  TYR B CG  1 
ATOM   1041 C CD1 . TYR B 1 41 ? 29.741  -15.052 -36.579 1.00 43.32  ? 40  TYR B CD1 1 
ATOM   1042 C CD2 . TYR B 1 41 ? 29.156  -17.295 -36.019 1.00 43.96  ? 40  TYR B CD2 1 
ATOM   1043 C CE1 . TYR B 1 41 ? 30.163  -15.470 -37.832 1.00 45.00  ? 40  TYR B CE1 1 
ATOM   1044 C CE2 . TYR B 1 41 ? 29.562  -17.722 -37.275 1.00 44.31  ? 40  TYR B CE2 1 
ATOM   1045 C CZ  . TYR B 1 41 ? 30.078  -16.808 -38.177 1.00 43.82  ? 40  TYR B CZ  1 
ATOM   1046 O OH  . TYR B 1 41 ? 30.470  -17.223 -39.421 1.00 46.71  ? 40  TYR B OH  1 
ATOM   1047 N N   . PRO B 1 42 ? 29.377  -13.727 -31.712 1.00 44.20  ? 41  PRO B N   1 
ATOM   1048 C CA  . PRO B 1 42 ? 28.653  -12.918 -30.732 1.00 38.13  ? 41  PRO B CA  1 
ATOM   1049 C C   . PRO B 1 42 ? 27.232  -12.679 -31.221 1.00 35.84  ? 41  PRO B C   1 
ATOM   1050 O O   . PRO B 1 42 ? 27.017  -12.071 -32.277 1.00 40.57  ? 41  PRO B O   1 
ATOM   1051 C CB  . PRO B 1 42 ? 29.448  -11.602 -30.663 1.00 41.35  ? 41  PRO B CB  1 
ATOM   1052 C CG  . PRO B 1 42 ? 30.148  -11.509 -32.007 1.00 43.99  ? 41  PRO B CG  1 
ATOM   1053 C CD  . PRO B 1 42 ? 30.379  -12.944 -32.451 1.00 45.34  ? 41  PRO B CD  1 
ATOM   1054 N N   . ILE B 1 43 ? 26.268  -13.140 -30.419 1.00 34.36  ? 42  ILE B N   1 
ATOM   1055 C CA  . ILE B 1 43 ? 24.861  -12.952 -30.732 1.00 31.21  ? 42  ILE B CA  1 
ATOM   1056 C C   . ILE B 1 43 ? 24.233  -11.953 -29.763 1.00 32.37  ? 42  ILE B C   1 
ATOM   1057 O O   . ILE B 1 43 ? 24.437  -12.062 -28.558 1.00 34.50  ? 42  ILE B O   1 
ATOM   1058 C CB  . ILE B 1 43 ? 24.115  -14.290 -30.654 1.00 31.93  ? 42  ILE B CB  1 
ATOM   1059 C CG1 . ILE B 1 43 ? 24.832  -15.423 -31.443 1.00 32.88  ? 42  ILE B CG1 1 
ATOM   1060 C CG2 . ILE B 1 43 ? 22.670  -14.097 -31.114 1.00 31.20  ? 42  ILE B CG2 1 
ATOM   1061 C CD1 . ILE B 1 43 ? 25.116  -15.083 -32.903 1.00 31.91  ? 42  ILE B CD1 1 
ATOM   1062 N N   . PHE B 1 44 ? 23.448  -11.021 -30.317 1.00 31.35  ? 43  PHE B N   1 
ATOM   1063 C CA  . PHE B 1 44 ? 22.606  -10.125 -29.543 1.00 33.96  ? 43  PHE B CA  1 
ATOM   1064 C C   . PHE B 1 44 ? 21.145  -10.517 -29.756 1.00 29.14  ? 43  PHE B C   1 
ATOM   1065 O O   . PHE B 1 44 ? 20.679  -10.559 -30.897 1.00 28.70  ? 43  PHE B O   1 
ATOM   1066 C CB  . PHE B 1 44 ? 22.869  -8.668  -29.957 1.00 32.99  ? 43  PHE B CB  1 
ATOM   1067 C CG  . PHE B 1 44 ? 21.901  -7.678  -29.325 1.00 33.75  ? 43  PHE B CG  1 
ATOM   1068 C CD1 . PHE B 1 44 ? 20.731  -7.305  -29.981 1.00 33.68  ? 43  PHE B CD1 1 
ATOM   1069 C CD2 . PHE B 1 44 ? 22.145  -7.161  -28.056 1.00 40.67  ? 43  PHE B CD2 1 
ATOM   1070 C CE1 . PHE B 1 44 ? 19.858  -6.396  -29.405 1.00 36.78  ? 43  PHE B CE1 1 
ATOM   1071 C CE2 . PHE B 1 44 ? 21.274  -6.244  -27.485 1.00 43.63  ? 43  PHE B CE2 1 
ATOM   1072 C CZ  . PHE B 1 44 ? 20.131  -5.870  -28.165 1.00 42.02  ? 43  PHE B CZ  1 
ATOM   1073 N N   . PHE B 1 45 ? 20.433  -10.829 -28.655 1.00 28.98  ? 44  PHE B N   1 
ATOM   1074 C CA  . PHE B 1 45 ? 19.017  -11.164 -28.766 1.00 27.74  ? 44  PHE B CA  1 
ATOM   1075 C C   . PHE B 1 45 ? 18.126  -9.923  -28.649 1.00 28.68  ? 44  PHE B C   1 
ATOM   1076 O O   . PHE B 1 45 ? 18.076  -9.265  -27.612 1.00 30.88  ? 44  PHE B O   1 
ATOM   1077 C CB  . PHE B 1 45 ? 18.675  -12.196 -27.689 1.00 28.00  ? 44  PHE B CB  1 
ATOM   1078 C CG  . PHE B 1 45 ? 19.427  -13.511 -27.835 1.00 26.17  ? 44  PHE B CG  1 
ATOM   1079 C CD1 . PHE B 1 45 ? 20.748  -13.635 -27.410 1.00 29.52  ? 44  PHE B CD1 1 
ATOM   1080 C CD2 . PHE B 1 45 ? 18.803  -14.634 -28.358 1.00 26.50  ? 44  PHE B CD2 1 
ATOM   1081 C CE1 . PHE B 1 45 ? 21.426  -14.836 -27.564 1.00 33.26  ? 44  PHE B CE1 1 
ATOM   1082 C CE2 . PHE B 1 45 ? 19.467  -15.843 -28.464 1.00 31.22  ? 44  PHE B CE2 1 
ATOM   1083 C CZ  . PHE B 1 45 ? 20.795  -15.932 -28.120 1.00 30.74  ? 44  PHE B CZ  1 
ATOM   1084 N N   . PHE B 1 46 ? 17.348  -9.644  -29.700 1.00 27.24  ? 45  PHE B N   1 
ATOM   1085 C CA  . PHE B 1 46 ? 16.411  -8.540  -29.637 1.00 29.31  ? 45  PHE B CA  1 
ATOM   1086 C C   . PHE B 1 46 ? 15.397  -8.781  -28.507 1.00 31.05  ? 45  PHE B C   1 
ATOM   1087 O O   . PHE B 1 46 ? 15.136  -9.925  -28.132 1.00 30.34  ? 45  PHE B O   1 
ATOM   1088 C CB  . PHE B 1 46 ? 15.670  -8.321  -30.949 1.00 28.03  ? 45  PHE B CB  1 
ATOM   1089 C CG  . PHE B 1 46 ? 16.601  -7.880  -32.068 1.00 32.39  ? 45  PHE B CG  1 
ATOM   1090 C CD1 . PHE B 1 46 ? 17.076  -6.564  -32.125 1.00 33.01  ? 45  PHE B CD1 1 
ATOM   1091 C CD2 . PHE B 1 46 ? 16.998  -8.774  -33.061 1.00 31.15  ? 45  PHE B CD2 1 
ATOM   1092 C CE1 . PHE B 1 46 ? 17.918  -6.144  -33.168 1.00 33.37  ? 45  PHE B CE1 1 
ATOM   1093 C CE2 . PHE B 1 46 ? 17.856  -8.353  -34.083 1.00 32.77  ? 45  PHE B CE2 1 
ATOM   1094 C CZ  . PHE B 1 46 ? 18.301  -7.039  -34.145 1.00 31.37  ? 45  PHE B CZ  1 
ATOM   1095 N N   . GLY B 1 47 ? 14.821  -7.682  -28.002 1.00 30.18  ? 46  GLY B N   1 
ATOM   1096 C CA  . GLY B 1 47 ? 13.785  -7.727  -26.970 1.00 33.19  ? 46  GLY B CA  1 
ATOM   1097 C C   . GLY B 1 47 ? 14.371  -7.847  -25.562 1.00 37.43  ? 46  GLY B C   1 
ATOM   1098 O O   . GLY B 1 47 ? 13.942  -7.154  -24.650 1.00 43.59  ? 46  GLY B O   1 
ATOM   1099 N N   . THR B 1 48 ? 15.313  -8.769  -25.365 1.00 37.38  ? 47  THR B N   1 
ATOM   1100 C CA  . THR B 1 48 ? 15.852  -9.043  -24.048 1.00 33.07  ? 47  THR B CA  1 
ATOM   1101 C C   . THR B 1 48 ? 17.158  -8.281  -23.898 1.00 36.35  ? 47  THR B C   1 
ATOM   1102 O O   . THR B 1 48 ? 17.613  -8.006  -22.785 1.00 35.41  ? 47  THR B O   1 
ATOM   1103 C CB  . THR B 1 48 ? 16.103  -10.543 -23.869 1.00 34.96  ? 47  THR B CB  1 
ATOM   1104 O OG1 . THR B 1 48 ? 17.065  -10.917 -24.852 1.00 33.57  ? 47  THR B OG1 1 
ATOM   1105 C CG2 . THR B 1 48 ? 14.828  -11.362 -23.923 1.00 34.75  ? 47  THR B CG2 1 
ATOM   1106 N N   . HIS B 1 49 ? 17.772  -8.006  -25.051 1.00 35.96  ? 48  HIS B N   1 
ATOM   1107 C CA  . HIS B 1 49 ? 19.090  -7.395  -25.137 1.00 39.22  ? 48  HIS B CA  1 
ATOM   1108 C C   . HIS B 1 49 ? 20.163  -8.234  -24.436 1.00 42.27  ? 48  HIS B C   1 
ATOM   1109 O O   . HIS B 1 49 ? 21.192  -7.691  -24.051 1.00 52.19  ? 48  HIS B O   1 
ATOM   1110 C CB  . HIS B 1 49 ? 19.020  -5.896  -24.791 1.00 40.57  ? 48  HIS B CB  1 
ATOM   1111 C CG  . HIS B 1 49 ? 17.832  -5.211  -25.397 1.00 38.72  ? 48  HIS B CG  1 
ATOM   1112 N ND1 . HIS B 1 49 ? 17.140  -4.215  -24.747 1.00 44.34  ? 48  HIS B ND1 1 
ATOM   1113 C CD2 . HIS B 1 49 ? 17.183  -5.402  -26.567 1.00 45.70  ? 48  HIS B CD2 1 
ATOM   1114 C CE1 . HIS B 1 49 ? 16.112  -3.832  -25.491 1.00 48.41  ? 48  HIS B CE1 1 
ATOM   1115 N NE2 . HIS B 1 49 ? 16.123  -4.528  -26.607 1.00 49.32  ? 48  HIS B NE2 1 
ATOM   1116 N N   . GLU B 1 50 ? 19.940  -9.548  -24.290 1.00 38.13  ? 49  GLU B N   1 
ATOM   1117 C CA  . GLU B 1 50 ? 20.964  -10.461 -23.791 1.00 42.45  ? 49  GLU B CA  1 
ATOM   1118 C C   . GLU B 1 50 ? 21.939  -10.796 -24.920 1.00 37.34  ? 49  GLU B C   1 
ATOM   1119 O O   . GLU B 1 50 ? 21.620  -10.573 -26.081 1.00 37.69  ? 49  GLU B O   1 
ATOM   1120 C CB  . GLU B 1 50 ? 20.338  -11.816 -23.461 1.00 48.04  ? 49  GLU B CB  1 
ATOM   1121 C CG  . GLU B 1 50 ? 19.385  -11.787 -22.271 1.00 44.71  ? 49  GLU B CG  1 
ATOM   1122 C CD  . GLU B 1 50 ? 20.090  -11.943 -20.938 1.00 51.50  ? 49  GLU B CD  1 
ATOM   1123 O OE1 . GLU B 1 50 ? 21.310  -12.198 -20.911 1.00 53.89  ? 49  GLU B OE1 1 
ATOM   1124 O OE2 . GLU B 1 50 ? 19.402  -11.814 -19.911 1.00 53.43  ? 49  GLU B OE2 1 
ATOM   1125 N N   . THR B 1 51 ? 23.129  -11.312 -24.576 1.00 37.83  ? 50  THR B N   1 
ATOM   1126 C CA  . THR B 1 51 ? 24.109  -11.772 -25.559 1.00 35.72  ? 50  THR B CA  1 
ATOM   1127 C C   . THR B 1 51 ? 24.542  -13.198 -25.211 1.00 37.15  ? 50  THR B C   1 
ATOM   1128 O O   . THR B 1 51 ? 24.482  -13.614 -24.057 1.00 35.77  ? 50  THR B O   1 
ATOM   1129 C CB  . THR B 1 51 ? 25.309  -10.820 -25.638 1.00 37.83  ? 50  THR B CB  1 
ATOM   1130 O OG1 . THR B 1 51 ? 25.844  -10.890 -24.324 1.00 42.92  ? 50  THR B OG1 1 
ATOM   1131 C CG2 . THR B 1 51 ? 24.932  -9.382  -25.957 1.00 36.75  ? 50  THR B CG2 1 
ATOM   1132 N N   . ALA B 1 52 ? 24.953  -13.966 -26.225 1.00 35.73  ? 51  ALA B N   1 
ATOM   1133 C CA  . ALA B 1 52 ? 25.595  -15.253 -26.000 1.00 34.87  ? 51  ALA B CA  1 
ATOM   1134 C C   . ALA B 1 52 ? 26.482  -15.562 -27.198 1.00 40.08  ? 51  ALA B C   1 
ATOM   1135 O O   . ALA B 1 52 ? 26.471  -14.818 -28.173 1.00 44.06  ? 51  ALA B O   1 
ATOM   1136 C CB  . ALA B 1 52 ? 24.574  -16.336 -25.771 1.00 34.72  ? 51  ALA B CB  1 
ATOM   1137 N N   . PHE B 1 53 ? 27.245  -16.649 -27.098 1.00 37.72  ? 52  PHE B N   1 
ATOM   1138 C CA  . PHE B 1 53 ? 28.012  -17.162 -28.219 1.00 45.82  ? 52  PHE B CA  1 
ATOM   1139 C C   . PHE B 1 53 ? 27.324  -18.417 -28.755 1.00 41.10  ? 52  PHE B C   1 
ATOM   1140 O O   . PHE B 1 53 ? 27.112  -19.371 -28.010 1.00 39.70  ? 52  PHE B O   1 
ATOM   1141 C CB  . PHE B 1 53 ? 29.427  -17.490 -27.725 1.00 47.40  ? 52  PHE B CB  1 
ATOM   1142 C CG  . PHE B 1 53 ? 30.243  -16.286 -27.280 1.00 45.28  ? 52  PHE B CG  1 
ATOM   1143 C CD1 . PHE B 1 53 ? 30.408  -15.194 -28.118 1.00 46.62  ? 52  PHE B CD1 1 
ATOM   1144 C CD2 . PHE B 1 53 ? 30.808  -16.238 -26.010 1.00 49.70  ? 52  PHE B CD2 1 
ATOM   1145 C CE1 . PHE B 1 53 ? 31.137  -14.088 -27.708 1.00 54.25  ? 52  PHE B CE1 1 
ATOM   1146 C CE2 . PHE B 1 53 ? 31.545  -15.133 -25.604 1.00 52.95  ? 52  PHE B CE2 1 
ATOM   1147 C CZ  . PHE B 1 53 ? 31.708  -14.060 -26.452 1.00 51.00  ? 52  PHE B CZ  1 
ATOM   1148 N N   . LEU B 1 54 ? 27.026  -18.419 -30.064 1.00 38.69  ? 53  LEU B N   1 
ATOM   1149 C CA  . LEU B 1 54 ? 26.414  -19.564 -30.715 1.00 33.90  ? 53  LEU B CA  1 
ATOM   1150 C C   . LEU B 1 54 ? 27.158  -19.903 -32.004 1.00 34.71  ? 53  LEU B C   1 
ATOM   1151 O O   . LEU B 1 54 ? 27.696  -19.016 -32.677 1.00 33.44  ? 53  LEU B O   1 
ATOM   1152 C CB  . LEU B 1 54 ? 24.957  -19.273 -31.053 1.00 32.28  ? 53  LEU B CB  1 
ATOM   1153 C CG  . LEU B 1 54 ? 23.989  -19.151 -29.876 1.00 35.20  ? 53  LEU B CG  1 
ATOM   1154 C CD1 . LEU B 1 54 ? 22.686  -18.633 -30.470 1.00 32.32  ? 53  LEU B CD1 1 
ATOM   1155 C CD2 . LEU B 1 54 ? 23.814  -20.530 -29.237 1.00 33.13  ? 53  LEU B CD2 1 
ATOM   1156 N N   . GLY B 1 55 ? 27.116  -21.192 -32.356 1.00 35.81  ? 54  GLY B N   1 
ATOM   1157 C CA  . GLY B 1 55 ? 27.668  -21.676 -33.609 1.00 34.67  ? 54  GLY B CA  1 
ATOM   1158 C C   . GLY B 1 55 ? 26.596  -21.688 -34.687 1.00 33.70  ? 54  GLY B C   1 
ATOM   1159 O O   . GLY B 1 55 ? 25.399  -21.610 -34.391 1.00 36.28  ? 54  GLY B O   1 
ATOM   1160 N N   . PRO B 1 56 ? 26.992  -21.740 -35.979 1.00 30.31  ? 55  PRO B N   1 
ATOM   1161 C CA  . PRO B 1 56 ? 26.031  -21.737 -37.076 1.00 31.20  ? 55  PRO B CA  1 
ATOM   1162 C C   . PRO B 1 56 ? 24.876  -22.729 -37.000 1.00 29.39  ? 55  PRO B C   1 
ATOM   1163 O O   . PRO B 1 56 ? 23.837  -22.427 -37.544 1.00 29.40  ? 55  PRO B O   1 
ATOM   1164 C CB  . PRO B 1 56 ? 26.851  -21.899 -38.360 1.00 30.60  ? 55  PRO B CB  1 
ATOM   1165 C CG  . PRO B 1 56 ? 28.299  -21.735 -37.938 1.00 29.51  ? 55  PRO B CG  1 
ATOM   1166 C CD  . PRO B 1 56 ? 28.392  -21.724 -36.424 1.00 33.01  ? 55  PRO B CD  1 
ATOM   1167 N N   . LYS B 1 57 ? 25.036  -23.869 -36.297 1.00 32.97  ? 56  LYS B N   1 
ATOM   1168 C CA  . LYS B 1 57 ? 23.974  -24.870 -36.221 1.00 35.12  ? 56  LYS B CA  1 
ATOM   1169 C C   . LYS B 1 57 ? 22.726  -24.248 -35.598 1.00 33.12  ? 56  LYS B C   1 
ATOM   1170 O O   . LYS B 1 57 ? 21.597  -24.661 -35.893 1.00 30.79  ? 56  LYS B O   1 
ATOM   1171 C CB  . LYS B 1 57 ? 24.390  -26.163 -35.499 1.00 35.75  ? 56  LYS B CB  1 
ATOM   1172 C CG  . LYS B 1 57 ? 24.590  -26.066 -33.994 1.00 35.72  ? 56  LYS B CG  1 
ATOM   1173 C CD  . LYS B 1 57 ? 24.624  -27.427 -33.298 1.00 38.73  ? 56  LYS B CD  1 
ATOM   1174 C CE  . LYS B 1 57 ? 24.711  -27.309 -31.791 1.00 43.44  ? 56  LYS B CE  1 
ATOM   1175 N NZ  . LYS B 1 57 ? 23.416  -26.977 -31.182 1.00 50.35  ? 56  LYS B NZ  1 
ATOM   1176 N N   . ASP B 1 58 ? 22.949  -23.215 -34.774 1.00 33.88  ? 57  ASP B N   1 
ATOM   1177 C CA  . ASP B 1 58 ? 21.857  -22.612 -34.018 1.00 33.05  ? 57  ASP B CA  1 
ATOM   1178 C C   . ASP B 1 58 ? 21.452  -21.255 -34.587 1.00 32.09  ? 57  ASP B C   1 
ATOM   1179 O O   . ASP B 1 58 ? 20.686  -20.527 -33.935 1.00 28.97  ? 57  ASP B O   1 
ATOM   1180 C CB  . ASP B 1 58 ? 22.189  -22.537 -32.536 1.00 31.67  ? 57  ASP B CB  1 
ATOM   1181 C CG  . ASP B 1 58 ? 22.246  -23.886 -31.832 1.00 39.52  ? 57  ASP B CG  1 
ATOM   1182 O OD1 . ASP B 1 58 ? 21.330  -24.698 -32.058 1.00 37.41  ? 57  ASP B OD1 1 
ATOM   1183 O OD2 . ASP B 1 58 ? 23.199  -24.092 -31.067 1.00 41.75  ? 57  ASP B OD2 1 
ATOM   1184 N N   . LEU B 1 59 ? 21.907  -20.951 -35.819 1.00 29.75  ? 58  LEU B N   1 
ATOM   1185 C CA  . LEU B 1 59 ? 21.721  -19.620 -36.393 1.00 29.82  ? 58  LEU B CA  1 
ATOM   1186 C C   . LEU B 1 59 ? 21.017  -19.760 -37.734 1.00 31.68  ? 58  LEU B C   1 
ATOM   1187 O O   . LEU B 1 59 ? 21.541  -20.400 -38.641 1.00 31.01  ? 58  LEU B O   1 
ATOM   1188 C CB  . LEU B 1 59 ? 23.047  -18.871 -36.545 1.00 32.92  ? 58  LEU B CB  1 
ATOM   1189 C CG  . LEU B 1 59 ? 23.839  -18.627 -35.258 1.00 33.27  ? 58  LEU B CG  1 
ATOM   1190 C CD1 . LEU B 1 59 ? 25.183  -17.962 -35.528 1.00 35.58  ? 58  LEU B CD1 1 
ATOM   1191 C CD2 . LEU B 1 59 ? 23.015  -17.783 -34.281 1.00 28.93  ? 58  LEU B CD2 1 
ATOM   1192 N N   . PHE B 1 60 ? 19.799  -19.232 -37.807 1.00 27.81  ? 59  PHE B N   1 
ATOM   1193 C CA  . PHE B 1 60 ? 18.943  -19.404 -38.960 1.00 28.21  ? 59  PHE B CA  1 
ATOM   1194 C C   . PHE B 1 60 ? 18.782  -18.040 -39.627 1.00 32.73  ? 59  PHE B C   1 
ATOM   1195 O O   . PHE B 1 60 ? 18.167  -17.148 -39.062 1.00 29.09  ? 59  PHE B O   1 
ATOM   1196 C CB  . PHE B 1 60 ? 17.595  -19.937 -38.471 1.00 25.28  ? 59  PHE B CB  1 
ATOM   1197 C CG  . PHE B 1 60 ? 17.672  -21.339 -37.876 1.00 26.33  ? 59  PHE B CG  1 
ATOM   1198 C CD1 . PHE B 1 60 ? 18.089  -21.529 -36.557 1.00 28.03  ? 59  PHE B CD1 1 
ATOM   1199 C CD2 . PHE B 1 60 ? 17.315  -22.459 -38.628 1.00 28.90  ? 59  PHE B CD2 1 
ATOM   1200 C CE1 . PHE B 1 60 ? 18.164  -22.811 -36.007 1.00 29.18  ? 59  PHE B CE1 1 
ATOM   1201 C CE2 . PHE B 1 60 ? 17.391  -23.742 -38.074 1.00 28.71  ? 59  PHE B CE2 1 
ATOM   1202 C CZ  . PHE B 1 60 ? 17.825  -23.911 -36.771 1.00 29.23  ? 59  PHE B CZ  1 
ATOM   1203 N N   . PRO B 1 61 ? 19.331  -17.821 -40.845 1.00 35.62  ? 60  PRO B N   1 
ATOM   1204 C CA  . PRO B 1 61 ? 19.166  -16.530 -41.520 1.00 34.82  ? 60  PRO B CA  1 
ATOM   1205 C C   . PRO B 1 61 ? 17.711  -16.048 -41.528 1.00 30.93  ? 60  PRO B C   1 
ATOM   1206 O O   . PRO B 1 61 ? 16.788  -16.800 -41.819 1.00 33.85  ? 60  PRO B O   1 
ATOM   1207 C CB  . PRO B 1 61 ? 19.793  -16.766 -42.929 1.00 31.91  ? 60  PRO B CB  1 
ATOM   1208 C CG  . PRO B 1 61 ? 20.764  -17.909 -42.724 1.00 39.64  ? 60  PRO B CG  1 
ATOM   1209 C CD  . PRO B 1 61 ? 20.169  -18.772 -41.604 1.00 36.12  ? 60  PRO B CD  1 
ATOM   1210 N N   . TYR B 1 62 ? 17.495  -14.765 -41.193 1.00 29.93  ? 61  TYR B N   1 
ATOM   1211 C CA  . TYR B 1 62 ? 16.176  -14.263 -40.838 1.00 33.75  ? 61  TYR B CA  1 
ATOM   1212 C C   . TYR B 1 62 ? 15.203  -14.254 -42.010 1.00 34.31  ? 61  TYR B C   1 
ATOM   1213 O O   . TYR B 1 62 ? 14.042  -14.639 -41.865 1.00 37.08  ? 61  TYR B O   1 
ATOM   1214 C CB  . TYR B 1 62 ? 16.327  -12.842 -40.297 1.00 37.09  ? 61  TYR B CB  1 
ATOM   1215 C CG  . TYR B 1 62 ? 15.016  -12.097 -40.100 1.00 35.28  ? 61  TYR B CG  1 
ATOM   1216 C CD1 . TYR B 1 62 ? 14.249  -12.300 -38.963 1.00 35.60  ? 61  TYR B CD1 1 
ATOM   1217 C CD2 . TYR B 1 62 ? 14.599  -11.135 -41.010 1.00 38.45  ? 61  TYR B CD2 1 
ATOM   1218 C CE1 . TYR B 1 62 ? 13.082  -11.591 -38.749 1.00 39.05  ? 61  TYR B CE1 1 
ATOM   1219 C CE2 . TYR B 1 62 ? 13.425  -10.425 -40.818 1.00 43.47  ? 61  TYR B CE2 1 
ATOM   1220 C CZ  . TYR B 1 62 ? 12.675  -10.650 -39.678 1.00 40.05  ? 61  TYR B CZ  1 
ATOM   1221 O OH  . TYR B 1 62 ? 11.529  -9.949  -39.490 1.00 43.30  ? 61  TYR B OH  1 
ATOM   1222 N N   . ASP B 1 63 ? 15.688  -13.826 -43.186 1.00 41.49  ? 62  ASP B N   1 
ATOM   1223 C CA  . ASP B 1 63 ? 14.844  -13.777 -44.374 1.00 45.18  ? 62  ASP B CA  1 
ATOM   1224 C C   . ASP B 1 63 ? 14.279  -15.158 -44.700 1.00 39.93  ? 62  ASP B C   1 
ATOM   1225 O O   . ASP B 1 63 ? 13.072  -15.302 -44.871 1.00 42.78  ? 62  ASP B O   1 
ATOM   1226 C CB  . ASP B 1 63 ? 15.508  -13.025 -45.513 1.00 49.63  ? 62  ASP B CB  1 
ATOM   1227 C CG  . ASP B 1 63 ? 14.952  -11.627 -45.737 1.00 61.75  ? 62  ASP B CG  1 
ATOM   1228 O OD1 . ASP B 1 63 ? 14.705  -10.911 -44.735 1.00 61.93  ? 62  ASP B OD1 1 
ATOM   1229 O OD2 . ASP B 1 63 ? 14.759  -11.268 -46.917 1.00 74.11  ? 62  ASP B OD2 1 
ATOM   1230 N N   . LYS B 1 64 ? 15.152  -16.169 -44.735 1.00 43.23  ? 63  LYS B N   1 
ATOM   1231 C CA  . LYS B 1 64 ? 14.728  -17.523 -45.058 1.00 41.45  ? 63  LYS B CA  1 
ATOM   1232 C C   . LYS B 1 64 ? 13.647  -18.035 -44.094 1.00 40.10  ? 63  LYS B C   1 
ATOM   1233 O O   . LYS B 1 64 ? 12.715  -18.709 -44.521 1.00 45.69  ? 63  LYS B O   1 
ATOM   1234 C CB  . LYS B 1 64 ? 15.946  -18.450 -45.044 1.00 44.70  ? 63  LYS B CB  1 
ATOM   1235 C CG  . LYS B 1 64 ? 15.608  -19.860 -45.481 1.00 41.97  ? 63  LYS B CG  1 
ATOM   1236 C CD  . LYS B 1 64 ? 16.850  -20.690 -45.744 1.00 44.28  ? 63  LYS B CD  1 
ATOM   1237 C CE  . LYS B 1 64 ? 16.519  -21.969 -46.469 1.00 50.32  ? 63  LYS B CE  1 
ATOM   1238 N NZ  . LYS B 1 64 ? 15.413  -22.716 -45.867 1.00 49.78  ? 63  LYS B NZ  1 
ATOM   1239 N N   . SER B 1 65 ? 13.757  -17.699 -42.800 1.00 40.04  ? 64  SER B N   1 
ATOM   1240 C CA  . SER B 1 65 ? 13.088  -18.457 -41.748 1.00 37.05  ? 64  SER B CA  1 
ATOM   1241 C C   . SER B 1 65 ? 12.001  -17.670 -40.999 1.00 36.35  ? 64  SER B C   1 
ATOM   1242 O O   . SER B 1 65 ? 11.326  -18.226 -40.130 1.00 36.71  ? 64  SER B O   1 
ATOM   1243 C CB  . SER B 1 65 ? 14.107  -19.039 -40.808 1.00 39.32  ? 64  SER B CB  1 
ATOM   1244 O OG  . SER B 1 65 ? 14.905  -17.998 -40.274 1.00 51.38  ? 64  SER B OG  1 
ATOM   1245 N N   . LYS B 1 66 ? 11.787  -16.397 -41.355 1.00 37.46  ? 65  LYS B N   1 
ATOM   1246 C CA  . LYS B 1 66 ? 10.886  -15.534 -40.600 1.00 39.66  ? 65  LYS B CA  1 
ATOM   1247 C C   . LYS B 1 66 ? 9.444   -16.034 -40.637 1.00 44.01  ? 65  LYS B C   1 
ATOM   1248 O O   . LYS B 1 66 ? 8.697   -15.825 -39.681 1.00 46.88  ? 65  LYS B O   1 
ATOM   1249 C CB  . LYS B 1 66 ? 10.945  -14.049 -40.989 1.00 41.90  ? 65  LYS B CB  1 
ATOM   1250 C CG  . LYS B 1 66 ? 10.731  -13.792 -42.474 1.00 41.07  ? 65  LYS B CG  1 
ATOM   1251 C CD  . LYS B 1 66 ? 10.791  -12.351 -42.966 1.00 54.94  ? 65  LYS B CD  1 
ATOM   1252 C CE  . LYS B 1 66 ? 10.513  -12.282 -44.442 1.00 55.04  ? 65  LYS B CE  1 
ATOM   1253 N NZ  . LYS B 1 66 ? 9.233   -12.914 -44.792 1.00 65.49  ? 65  LYS B NZ  1 
ATOM   1254 N N   . ASP B 1 67 ? 9.017   -16.689 -41.718 1.00 44.00  ? 66  ASP B N   1 
ATOM   1255 C CA  . ASP B 1 67 ? 7.614   -17.084 -41.687 1.00 49.61  ? 66  ASP B CA  1 
ATOM   1256 C C   . ASP B 1 67 ? 7.424   -18.299 -40.776 1.00 46.93  ? 66  ASP B C   1 
ATOM   1257 O O   . ASP B 1 67 ? 6.336   -18.512 -40.238 1.00 51.04  ? 66  ASP B O   1 
ATOM   1258 C CB  . ASP B 1 67 ? 6.934   -17.066 -43.051 1.00 65.35  ? 66  ASP B CB  1 
ATOM   1259 C CG  . ASP B 1 67 ? 7.450   -18.025 -44.116 1.00 76.59  ? 66  ASP B CG  1 
ATOM   1260 O OD1 . ASP B 1 67 ? 7.672   -17.557 -45.263 1.00 79.04  ? 66  ASP B OD1 1 
ATOM   1261 O OD2 . ASP B 1 67 ? 7.595   -19.230 -43.805 1.00 74.62  ? 66  ASP B OD2 1 
ATOM   1262 N N   . LYS B 1 68 ? 8.504   -19.063 -40.568 1.00 41.17  ? 67  LYS B N   1 
ATOM   1263 C CA  . LYS B 1 68 ? 8.468   -20.238 -39.707 1.00 40.20  ? 67  LYS B CA  1 
ATOM   1264 C C   . LYS B 1 68 ? 8.658   -19.832 -38.246 1.00 38.85  ? 67  LYS B C   1 
ATOM   1265 O O   . LYS B 1 68 ? 7.926   -20.307 -37.378 1.00 39.34  ? 67  LYS B O   1 
ATOM   1266 C CB  . LYS B 1 68 ? 9.509   -21.234 -40.228 1.00 42.99  ? 67  LYS B CB  1 
ATOM   1267 C CG  . LYS B 1 68 ? 9.644   -22.570 -39.513 1.00 53.09  ? 67  LYS B CG  1 
ATOM   1268 C CD  . LYS B 1 68 ? 10.422  -23.520 -40.420 1.00 58.38  ? 67  LYS B CD  1 
ATOM   1269 C CE  . LYS B 1 68 ? 11.112  -24.634 -39.691 1.00 69.15  ? 67  LYS B CE  1 
ATOM   1270 N NZ  . LYS B 1 68 ? 10.194  -25.604 -39.082 1.00 74.02  ? 67  LYS B NZ  1 
ATOM   1271 N N   . TYR B 1 69 ? 9.605   -18.919 -37.965 1.00 36.84  ? 68  TYR B N   1 
ATOM   1272 C CA  . TYR B 1 69 ? 9.962   -18.671 -36.567 1.00 33.22  ? 68  TYR B CA  1 
ATOM   1273 C C   . TYR B 1 69 ? 9.446   -17.326 -36.044 1.00 36.51  ? 68  TYR B C   1 
ATOM   1274 O O   . TYR B 1 69 ? 9.513   -17.063 -34.834 1.00 33.24  ? 68  TYR B O   1 
ATOM   1275 C CB  . TYR B 1 69 ? 11.480  -18.715 -36.373 1.00 32.29  ? 68  TYR B CB  1 
ATOM   1276 C CG  . TYR B 1 69 ? 12.070  -20.086 -36.673 1.00 32.85  ? 68  TYR B CG  1 
ATOM   1277 C CD1 . TYR B 1 69 ? 11.514  -21.250 -36.148 1.00 35.67  ? 68  TYR B CD1 1 
ATOM   1278 C CD2 . TYR B 1 69 ? 13.171  -20.210 -37.515 1.00 36.07  ? 68  TYR B CD2 1 
ATOM   1279 C CE1 . TYR B 1 69 ? 12.052  -22.501 -36.430 1.00 35.82  ? 68  TYR B CE1 1 
ATOM   1280 C CE2 . TYR B 1 69 ? 13.722  -21.448 -37.797 1.00 37.23  ? 68  TYR B CE2 1 
ATOM   1281 C CZ  . TYR B 1 69 ? 13.153  -22.594 -37.263 1.00 38.75  ? 68  TYR B CZ  1 
ATOM   1282 O OH  . TYR B 1 69 ? 13.703  -23.805 -37.547 1.00 37.54  ? 68  TYR B OH  1 
ATOM   1283 N N   . GLY B 1 70 ? 8.959   -16.463 -36.942 1.00 35.85  ? 69  GLY B N   1 
ATOM   1284 C CA  . GLY B 1 70 ? 8.614   -15.125 -36.485 1.00 44.93  ? 69  GLY B CA  1 
ATOM   1285 C C   . GLY B 1 70 ? 7.170   -14.977 -35.998 1.00 47.88  ? 69  GLY B C   1 
ATOM   1286 O O   . GLY B 1 70 ? 6.545   -13.968 -36.295 1.00 50.97  ? 69  GLY B O   1 
ATOM   1287 N N   . LYS B 1 71 ? 6.644   -15.952 -35.241 1.00 47.29  ? 70  LYS B N   1 
ATOM   1288 C CA  . LYS B 1 71 ? 5.296   -15.818 -34.710 1.00 47.30  ? 70  LYS B CA  1 
ATOM   1289 C C   . LYS B 1 71 ? 5.367   -15.374 -33.254 1.00 46.86  ? 70  LYS B C   1 
ATOM   1290 O O   . LYS B 1 71 ? 6.165   -15.930 -32.503 1.00 44.75  ? 70  LYS B O   1 
ATOM   1291 C CB  . LYS B 1 71 ? 4.427   -17.084 -34.687 1.00 46.07  ? 70  LYS B CB  1 
ATOM   1292 C CG  . LYS B 1 71 ? 3.709   -17.409 -35.993 1.00 56.65  ? 70  LYS B CG  1 
ATOM   1293 C CD  . LYS B 1 71 ? 4.391   -18.483 -36.830 1.00 54.26  ? 70  LYS B CD  1 
ATOM   1294 C CE  . LYS B 1 71 ? 3.630   -18.837 -38.073 1.00 58.71  ? 70  LYS B CE  1 
ATOM   1295 N NZ  . LYS B 1 71 ? 3.719   -17.804 -39.110 1.00 62.69  ? 70  LYS B NZ  1 
ATOM   1296 N N   . PRO B 1 72 ? 4.501   -14.426 -32.810 1.00 46.07  ? 71  PRO B N   1 
ATOM   1297 C CA  . PRO B 1 72 ? 4.494   -13.974 -31.412 1.00 44.98  ? 71  PRO B CA  1 
ATOM   1298 C C   . PRO B 1 72 ? 4.259   -15.144 -30.455 1.00 44.30  ? 71  PRO B C   1 
ATOM   1299 O O   . PRO B 1 72 ? 3.664   -16.152 -30.836 1.00 39.49  ? 71  PRO B O   1 
ATOM   1300 C CB  . PRO B 1 72 ? 3.381   -12.897 -31.299 1.00 44.55  ? 71  PRO B CB  1 
ATOM   1301 C CG  . PRO B 1 72 ? 2.938   -12.639 -32.730 1.00 49.56  ? 71  PRO B CG  1 
ATOM   1302 C CD  . PRO B 1 72 ? 3.471   -13.761 -33.628 1.00 47.62  ? 71  PRO B CD  1 
ATOM   1303 N N   . ASN B 1 73 ? 4.745   -15.004 -29.212 1.00 41.29  ? 72  ASN B N   1 
ATOM   1304 C CA  . ASN B 1 73 ? 4.475   -15.989 -28.176 1.00 40.28  ? 72  ASN B CA  1 
ATOM   1305 C C   . ASN B 1 73 ? 4.492   -15.296 -26.808 1.00 38.83  ? 72  ASN B C   1 
ATOM   1306 O O   . ASN B 1 73 ? 4.630   -14.072 -26.718 1.00 42.82  ? 72  ASN B O   1 
ATOM   1307 C CB  . ASN B 1 73 ? 5.421   -17.182 -28.260 1.00 40.21  ? 72  ASN B CB  1 
ATOM   1308 C CG  . ASN B 1 73 ? 6.868   -16.786 -28.069 1.00 41.38  ? 72  ASN B CG  1 
ATOM   1309 O OD1 . ASN B 1 73 ? 7.189   -16.076 -27.113 1.00 39.61  ? 72  ASN B OD1 1 
ATOM   1310 N ND2 . ASN B 1 73 ? 7.758   -17.217 -28.956 1.00 40.21  ? 72  ASN B ND2 1 
ATOM   1311 N N   . LYS B 1 74 ? 4.431   -16.092 -25.743 1.00 40.32  ? 73  LYS B N   1 
ATOM   1312 C CA  . LYS B 1 74 ? 4.283   -15.534 -24.399 1.00 43.86  ? 73  LYS B CA  1 
ATOM   1313 C C   . LYS B 1 74 ? 5.607   -15.476 -23.623 1.00 41.86  ? 73  LYS B C   1 
ATOM   1314 O O   . LYS B 1 74 ? 5.611   -15.254 -22.404 1.00 38.84  ? 73  LYS B O   1 
ATOM   1315 C CB  . LYS B 1 74 ? 3.144   -16.259 -23.665 1.00 45.90  ? 73  LYS B CB  1 
ATOM   1316 C CG  . LYS B 1 74 ? 3.439   -17.690 -23.212 1.00 51.09  ? 73  LYS B CG  1 
ATOM   1317 C CD  . LYS B 1 74 ? 2.300   -18.685 -23.423 1.00 53.51  ? 73  LYS B CD  1 
ATOM   1318 N N   . ARG B 1 75 ? 6.737   -15.662 -24.318 1.00 32.81  ? 74  ARG B N   1 
ATOM   1319 C CA  . ARG B 1 75 ? 8.035   -15.475 -23.686 1.00 33.63  ? 74  ARG B CA  1 
ATOM   1320 C C   . ARG B 1 75 ? 8.328   -13.971 -23.590 1.00 33.93  ? 74  ARG B C   1 
ATOM   1321 O O   . ARG B 1 75 ? 8.102   -13.232 -24.551 1.00 36.96  ? 74  ARG B O   1 
ATOM   1322 C CB  . ARG B 1 75 ? 9.172   -16.270 -24.345 1.00 35.76  ? 74  ARG B CB  1 
ATOM   1323 C CG  . ARG B 1 75 ? 8.990   -17.760 -24.599 1.00 34.65  ? 74  ARG B CG  1 
ATOM   1324 C CD  . ARG B 1 75 ? 8.859   -18.570 -23.302 1.00 35.77  ? 74  ARG B CD  1 
ATOM   1325 N NE  . ARG B 1 75 ? 9.063   -20.002 -23.551 1.00 35.89  ? 74  ARG B NE  1 
ATOM   1326 C CZ  . ARG B 1 75 ? 10.219  -20.624 -23.386 1.00 32.78  ? 74  ARG B CZ  1 
ATOM   1327 N NH1 . ARG B 1 75 ? 11.287  -19.962 -22.977 1.00 36.02  ? 74  ARG B NH1 1 
ATOM   1328 N NH2 . ARG B 1 75 ? 10.330  -21.905 -23.677 1.00 33.95  ? 74  ARG B NH2 1 
ATOM   1329 N N   . LYS B 1 76 ? 8.819   -13.535 -22.411 1.00 30.93  ? 75  LYS B N   1 
ATOM   1330 C CA  . LYS B 1 76 ? 9.153   -12.151 -22.119 1.00 29.89  ? 75  LYS B CA  1 
ATOM   1331 C C   . LYS B 1 76 ? 10.254  -11.691 -23.079 1.00 29.08  ? 75  LYS B C   1 
ATOM   1332 O O   . LYS B 1 76 ? 11.312  -12.320 -23.159 1.00 30.92  ? 75  LYS B O   1 
ATOM   1333 C CB  . LYS B 1 76 ? 9.709   -12.084 -20.689 1.00 34.64  ? 75  LYS B CB  1 
ATOM   1334 C CG  . LYS B 1 76 ? 10.091  -10.680 -20.193 1.00 34.41  ? 75  LYS B CG  1 
ATOM   1335 C CD  . LYS B 1 76 ? 10.692  -10.671 -18.792 1.00 39.21  ? 75  LYS B CD  1 
ATOM   1336 C CE  . LYS B 1 76 ? 11.118  -9.284  -18.359 1.00 42.54  ? 75  LYS B CE  1 
ATOM   1337 N NZ  . LYS B 1 76 ? 11.273  -9.174  -16.902 1.00 50.86  ? 75  LYS B NZ  1 
ATOM   1338 N N   . GLY B 1 77 ? 9.996   -10.571 -23.748 1.00 30.50  ? 76  GLY B N   1 
ATOM   1339 C CA  . GLY B 1 77 ? 10.975  -9.930  -24.619 1.00 30.50  ? 76  GLY B CA  1 
ATOM   1340 C C   . GLY B 1 77 ? 10.762  -10.336 -26.076 1.00 31.11  ? 76  GLY B C   1 
ATOM   1341 O O   . GLY B 1 77 ? 11.282  -9.687  -26.983 1.00 31.94  ? 76  GLY B O   1 
ATOM   1342 N N   . PHE B 1 78 ? 9.967   -11.396 -26.316 1.00 30.48  ? 77  PHE B N   1 
ATOM   1343 C CA  . PHE B 1 78 ? 9.885   -11.996 -27.647 1.00 30.88  ? 77  PHE B CA  1 
ATOM   1344 C C   . PHE B 1 78 ? 9.202   -11.060 -28.627 1.00 33.50  ? 77  PHE B C   1 
ATOM   1345 O O   . PHE B 1 78 ? 9.718   -10.822 -29.722 1.00 30.34  ? 77  PHE B O   1 
ATOM   1346 C CB  . PHE B 1 78 ? 9.159   -13.347 -27.700 1.00 30.09  ? 77  PHE B CB  1 
ATOM   1347 C CG  . PHE B 1 78 ? 9.426   -14.090 -29.006 1.00 30.95  ? 77  PHE B CG  1 
ATOM   1348 C CD1 . PHE B 1 78 ? 10.552  -14.910 -29.132 1.00 31.25  ? 77  PHE B CD1 1 
ATOM   1349 C CD2 . PHE B 1 78 ? 8.542   -13.990 -30.070 1.00 35.39  ? 77  PHE B CD2 1 
ATOM   1350 C CE1 . PHE B 1 78 ? 10.813  -15.587 -30.313 1.00 30.32  ? 77  PHE B CE1 1 
ATOM   1351 C CE2 . PHE B 1 78 ? 8.800   -14.676 -31.249 1.00 35.19  ? 77  PHE B CE2 1 
ATOM   1352 C CZ  . PHE B 1 78 ? 9.939   -15.461 -31.358 1.00 31.63  ? 77  PHE B CZ  1 
ATOM   1353 N N   . ASN B 1 79 ? 8.019   -10.556 -28.260 1.00 33.36  ? 78  ASN B N   1 
ATOM   1354 C CA  . ASN B 1 79 ? 7.283   -9.724  -29.196 1.00 34.36  ? 78  ASN B CA  1 
ATOM   1355 C C   . ASN B 1 79 ? 7.992   -8.390  -29.419 1.00 33.82  ? 78  ASN B C   1 
ATOM   1356 O O   . ASN B 1 79 ? 7.902   -7.814  -30.504 1.00 34.03  ? 78  ASN B O   1 
ATOM   1357 C CB  . ASN B 1 79 ? 5.832   -9.540  -28.782 1.00 34.59  ? 78  ASN B CB  1 
ATOM   1358 C CG  . ASN B 1 79 ? 5.085   -10.850 -28.839 1.00 42.89  ? 78  ASN B CG  1 
ATOM   1359 O OD1 . ASN B 1 79 ? 5.620   -11.867 -29.305 1.00 42.36  ? 78  ASN B OD1 1 
ATOM   1360 N ND2 . ASN B 1 79 ? 3.863   -10.856 -28.330 1.00 42.70  ? 78  ASN B ND2 1 
ATOM   1361 N N   . GLU B 1 80 ? 8.682   -7.911  -28.389 1.00 33.75  ? 79  GLU B N   1 
ATOM   1362 C CA  . GLU B 1 80 ? 9.461   -6.691  -28.532 1.00 36.14  ? 79  GLU B CA  1 
ATOM   1363 C C   . GLU B 1 80 ? 10.624  -6.948  -29.493 1.00 29.44  ? 79  GLU B C   1 
ATOM   1364 O O   . GLU B 1 80 ? 10.941  -6.087  -30.310 1.00 34.34  ? 79  GLU B O   1 
ATOM   1365 C CB  . GLU B 1 80 ? 10.004  -6.208  -27.192 1.00 32.85  ? 79  GLU B CB  1 
ATOM   1366 C CG  . GLU B 1 80 ? 8.993   -5.352  -26.437 1.00 43.00  ? 79  GLU B CG  1 
ATOM   1367 N N   . GLY B 1 81 ? 11.247  -8.127  -29.363 1.00 28.61  ? 80  GLY B N   1 
ATOM   1368 C CA  . GLY B 1 81 ? 12.356  -8.555  -30.202 1.00 25.59  ? 80  GLY B CA  1 
ATOM   1369 C C   . GLY B 1 81 ? 11.920  -8.635  -31.662 1.00 30.69  ? 80  GLY B C   1 
ATOM   1370 O O   . GLY B 1 81 ? 12.659  -8.192  -32.546 1.00 29.63  ? 80  GLY B O   1 
ATOM   1371 N N   . LEU B 1 82 ? 10.696  -9.135  -31.879 1.00 26.67  ? 81  LEU B N   1 
ATOM   1372 C CA  . LEU B 1 82 ? 10.082  -9.132  -33.201 1.00 31.43  ? 81  LEU B CA  1 
ATOM   1373 C C   . LEU B 1 82 ? 9.970   -7.709  -33.741 1.00 33.80  ? 81  LEU B C   1 
ATOM   1374 O O   . LEU B 1 82 ? 10.240  -7.469  -34.917 1.00 32.17  ? 81  LEU B O   1 
ATOM   1375 C CB  . LEU B 1 82 ? 8.733   -9.855  -33.228 1.00 29.91  ? 81  LEU B CB  1 
ATOM   1376 C CG  . LEU B 1 82 ? 8.812   -11.374 -33.026 1.00 29.68  ? 81  LEU B CG  1 
ATOM   1377 C CD1 . LEU B 1 82 ? 7.433   -12.026 -33.084 1.00 30.77  ? 81  LEU B CD1 1 
ATOM   1378 C CD2 . LEU B 1 82 ? 9.747   -12.010 -34.054 1.00 30.20  ? 81  LEU B CD2 1 
ATOM   1379 N N   . TRP B 1 83 ? 9.538   -6.770  -32.899 1.00 32.22  ? 82  TRP B N   1 
ATOM   1380 C CA  . TRP B 1 83 ? 9.423   -5.386  -33.335 1.00 34.61  ? 82  TRP B CA  1 
ATOM   1381 C C   . TRP B 1 83 ? 10.793  -4.828  -33.721 1.00 32.16  ? 82  TRP B C   1 
ATOM   1382 O O   . TRP B 1 83 ? 10.923  -4.135  -34.730 1.00 33.35  ? 82  TRP B O   1 
ATOM   1383 C CB  . TRP B 1 83 ? 8.786   -4.506  -32.250 1.00 33.67  ? 82  TRP B CB  1 
ATOM   1384 C CG  . TRP B 1 83 ? 8.459   -3.131  -32.771 1.00 35.46  ? 82  TRP B CG  1 
ATOM   1385 C CD1 . TRP B 1 83 ? 7.296   -2.735  -33.358 1.00 37.01  ? 82  TRP B CD1 1 
ATOM   1386 C CD2 . TRP B 1 83 ? 9.351   -1.999  -32.829 1.00 37.96  ? 82  TRP B CD2 1 
ATOM   1387 N NE1 . TRP B 1 83 ? 7.384   -1.425  -33.742 1.00 39.78  ? 82  TRP B NE1 1 
ATOM   1388 C CE2 . TRP B 1 83 ? 8.631   -0.947  -33.431 1.00 39.06  ? 82  TRP B CE2 1 
ATOM   1389 C CE3 . TRP B 1 83 ? 10.673  -1.776  -32.416 1.00 40.52  ? 82  TRP B CE3 1 
ATOM   1390 C CZ2 . TRP B 1 83 ? 9.197   0.312   -33.638 1.00 42.86  ? 82  TRP B CZ2 1 
ATOM   1391 C CZ3 . TRP B 1 83 ? 11.226  -0.527  -32.602 1.00 45.42  ? 82  TRP B CZ3 1 
ATOM   1392 C CH2 . TRP B 1 83 ? 10.498  0.494   -33.215 1.00 44.95  ? 82  TRP B CH2 1 
ATOM   1393 N N   . GLU B 1 84 ? 11.801  -5.145  -32.912 1.00 28.91  ? 83  GLU B N   1 
ATOM   1394 C CA  . GLU B 1 84 ? 13.136  -4.601  -33.100 1.00 29.25  ? 83  GLU B CA  1 
ATOM   1395 C C   . GLU B 1 84 ? 13.773  -5.091  -34.401 1.00 31.81  ? 83  GLU B C   1 
ATOM   1396 O O   . GLU B 1 84 ? 14.398  -4.311  -35.137 1.00 31.52  ? 83  GLU B O   1 
ATOM   1397 C CB  . GLU B 1 84 ? 14.060  -4.910  -31.929 1.00 29.47  ? 83  GLU B CB  1 
ATOM   1398 C CG  . GLU B 1 84 ? 13.573  -4.290  -30.622 1.00 33.70  ? 83  GLU B CG  1 
ATOM   1399 C CD  . GLU B 1 84 ? 14.504  -4.532  -29.464 1.00 32.59  ? 83  GLU B CD  1 
ATOM   1400 O OE1 . GLU B 1 84 ? 15.513  -5.259  -29.588 1.00 31.72  ? 83  GLU B OE1 1 
ATOM   1401 O OE2 . GLU B 1 84 ? 14.209  -3.948  -28.399 1.00 36.25  ? 83  GLU B OE2 1 
ATOM   1402 N N   . ILE B 1 85 ? 13.604  -6.381  -34.695 1.00 29.27  ? 84  ILE B N   1 
ATOM   1403 C CA  . ILE B 1 85 ? 14.320  -6.963  -35.827 1.00 30.80  ? 84  ILE B CA  1 
ATOM   1404 C C   . ILE B 1 85 ? 13.732  -6.430  -37.135 1.00 33.25  ? 84  ILE B C   1 
ATOM   1405 O O   . ILE B 1 85 ? 14.452  -6.305  -38.133 1.00 30.80  ? 84  ILE B O   1 
ATOM   1406 C CB  . ILE B 1 85 ? 14.377  -8.505  -35.764 1.00 30.92  ? 84  ILE B CB  1 
ATOM   1407 C CG1 . ILE B 1 85 ? 15.390  -9.086  -36.786 1.00 31.23  ? 84  ILE B CG1 1 
ATOM   1408 C CG2 . ILE B 1 85 ? 12.994  -9.138  -35.933 1.00 30.20  ? 84  ILE B CG2 1 
ATOM   1409 C CD1 . ILE B 1 85 ? 15.843  -10.507 -36.463 1.00 33.07  ? 84  ILE B CD1 1 
ATOM   1410 N N   . GLN B 1 86 ? 12.428  -6.107  -37.093 1.00 32.96  ? 85  GLN B N   1 
ATOM   1411 C CA  . GLN B 1 86 ? 11.625  -5.610  -38.200 1.00 36.28  ? 85  GLN B CA  1 
ATOM   1412 C C   . GLN B 1 86 ? 11.806  -4.094  -38.374 1.00 33.98  ? 85  GLN B C   1 
ATOM   1413 O O   . GLN B 1 86 ? 11.872  -3.631  -39.501 1.00 35.33  ? 85  GLN B O   1 
ATOM   1414 C CB  . GLN B 1 86 ? 10.149  -5.975  -37.969 1.00 38.92  ? 85  GLN B CB  1 
ATOM   1415 C CG  . GLN B 1 86 ? 9.807   -7.454  -38.172 1.00 46.93  ? 85  GLN B CG  1 
ATOM   1416 C CD  . GLN B 1 86 ? 8.618   -7.979  -37.382 1.00 55.23  ? 85  GLN B CD  1 
ATOM   1417 O OE1 . GLN B 1 86 ? 7.487   -7.472  -37.442 1.00 52.81  ? 85  GLN B OE1 1 
ATOM   1418 N NE2 . GLN B 1 86 ? 8.865   -9.045  -36.636 1.00 48.18  ? 85  GLN B NE2 1 
ATOM   1419 N N   . ASN B 1 87 ? 11.931  -3.319  -37.281 1.00 31.73  ? 86  ASN B N   1 
ATOM   1420 C CA  . ASN B 1 87 ? 11.815  -1.864  -37.384 1.00 32.30  ? 86  ASN B CA  1 
ATOM   1421 C C   . ASN B 1 87 ? 13.135  -1.117  -37.204 1.00 32.15  ? 86  ASN B C   1 
ATOM   1422 O O   . ASN B 1 87 ? 13.251  0.024   -37.655 1.00 35.61  ? 86  ASN B O   1 
ATOM   1423 C CB  . ASN B 1 87 ? 10.725  -1.301  -36.469 1.00 36.54  ? 86  ASN B CB  1 
ATOM   1424 C CG  . ASN B 1 87 ? 9.368   -1.836  -36.865 1.00 38.78  ? 86  ASN B CG  1 
ATOM   1425 O OD1 . ASN B 1 87 ? 8.892   -1.541  -37.962 1.00 40.63  ? 86  ASN B OD1 1 
ATOM   1426 N ND2 . ASN B 1 87 ? 8.786   -2.711  -36.057 1.00 40.22  ? 86  ASN B ND2 1 
ATOM   1427 N N   . ASN B 1 88 ? 14.092  -1.702  -36.486 1.00 30.46  ? 87  ASN B N   1 
ATOM   1428 C CA  . ASN B 1 88 ? 15.349  -1.027  -36.237 1.00 33.92  ? 87  ASN B CA  1 
ATOM   1429 C C   . ASN B 1 88 ? 16.400  -2.039  -35.813 1.00 31.37  ? 87  ASN B C   1 
ATOM   1430 O O   . ASN B 1 88 ? 16.918  -1.966  -34.692 1.00 30.56  ? 87  ASN B O   1 
ATOM   1431 C CB  . ASN B 1 88 ? 15.227  0.083   -35.191 1.00 36.83  ? 87  ASN B CB  1 
ATOM   1432 C CG  . ASN B 1 88 ? 16.267  1.156   -35.408 1.00 38.05  ? 87  ASN B CG  1 
ATOM   1433 O OD1 . ASN B 1 88 ? 17.283  0.924   -36.071 1.00 33.79  ? 87  ASN B OD1 1 
ATOM   1434 N ND2 . ASN B 1 88 ? 16.038  2.342   -34.857 1.00 36.35  ? 87  ASN B ND2 1 
ATOM   1435 N N   . PRO B 1 89 ? 16.705  -3.034  -36.678 1.00 30.34  ? 88  PRO B N   1 
ATOM   1436 C CA  . PRO B 1 89 ? 17.611  -4.119  -36.302 1.00 28.09  ? 88  PRO B CA  1 
ATOM   1437 C C   . PRO B 1 89 ? 19.051  -3.699  -36.024 1.00 28.60  ? 88  PRO B C   1 
ATOM   1438 O O   . PRO B 1 89 ? 19.775  -4.418  -35.346 1.00 32.12  ? 88  PRO B O   1 
ATOM   1439 C CB  . PRO B 1 89 ? 17.517  -5.053  -37.513 1.00 25.75  ? 88  PRO B CB  1 
ATOM   1440 C CG  . PRO B 1 89 ? 17.199  -4.116  -38.654 1.00 27.54  ? 88  PRO B CG  1 
ATOM   1441 C CD  . PRO B 1 89 ? 16.171  -3.162  -38.057 1.00 27.13  ? 88  PRO B CD  1 
ATOM   1442 N N   . HIS B 1 90 ? 19.456  -2.521  -36.531 1.00 28.27  ? 89  HIS B N   1 
ATOM   1443 C CA  . HIS B 1 90 ? 20.850  -2.096  -36.441 1.00 28.80  ? 89  HIS B CA  1 
ATOM   1444 C C   . HIS B 1 90 ? 21.057  -1.000  -35.393 1.00 32.78  ? 89  HIS B C   1 
ATOM   1445 O O   . HIS B 1 90 ? 22.145  -0.438  -35.299 1.00 32.26  ? 89  HIS B O   1 
ATOM   1446 C CB  . HIS B 1 90 ? 21.367  -1.676  -37.831 1.00 28.98  ? 89  HIS B CB  1 
ATOM   1447 C CG  . HIS B 1 90 ? 21.196  -2.777  -38.832 1.00 30.21  ? 89  HIS B CG  1 
ATOM   1448 N ND1 . HIS B 1 90 ? 21.763  -4.019  -38.643 1.00 30.51  ? 89  HIS B ND1 1 
ATOM   1449 C CD2 . HIS B 1 90 ? 20.560  -2.837  -40.024 1.00 30.58  ? 89  HIS B CD2 1 
ATOM   1450 C CE1 . HIS B 1 90 ? 21.458  -4.802  -39.670 1.00 30.77  ? 89  HIS B CE1 1 
ATOM   1451 N NE2 . HIS B 1 90 ? 20.747  -4.098  -40.524 1.00 30.17  ? 89  HIS B NE2 1 
ATOM   1452 N N   . ALA B 1 91 ? 20.073  -0.794  -34.511 1.00 32.04  ? 90  ALA B N   1 
ATOM   1453 C CA  . ALA B 1 91 ? 20.186  0.302   -33.554 1.00 32.78  ? 90  ALA B CA  1 
ATOM   1454 C C   . ALA B 1 91 ? 21.074  -0.094  -32.380 1.00 36.17  ? 90  ALA B C   1 
ATOM   1455 O O   . ALA B 1 91 ? 21.410  -1.267  -32.187 1.00 33.55  ? 90  ALA B O   1 
ATOM   1456 C CB  . ALA B 1 91 ? 18.801  0.743   -33.087 1.00 30.22  ? 90  ALA B CB  1 
ATOM   1457 N N   . SER B 1 92 ? 21.455  0.909   -31.586 1.00 37.02  ? 91  SER B N   1 
ATOM   1458 C CA  . SER B 1 92 ? 22.096  0.663   -30.307 1.00 39.84  ? 91  SER B CA  1 
ATOM   1459 C C   . SER B 1 92 ? 21.009  0.375   -29.266 1.00 41.68  ? 91  SER B C   1 
ATOM   1460 O O   . SER B 1 92 ? 20.016  1.098   -29.196 1.00 42.89  ? 91  SER B O   1 
ATOM   1461 C CB  . SER B 1 92 ? 22.963  1.843   -29.919 1.00 43.30  ? 91  SER B CB  1 
ATOM   1462 O OG  . SER B 1 92 ? 23.670  1.550   -28.721 1.00 53.36  ? 91  SER B OG  1 
ATOM   1463 N N   . TYR B 1 93 ? 21.171  -0.738  -28.533 1.00 38.89  ? 92  TYR B N   1 
ATOM   1464 C CA  . TYR B 1 93 ? 20.242  -1.189  -27.504 1.00 41.04  ? 92  TYR B CA  1 
ATOM   1465 C C   . TYR B 1 93 ? 20.976  -1.234  -26.162 1.00 47.49  ? 92  TYR B C   1 
ATOM   1466 O O   . TYR B 1 93 ? 20.361  -1.451  -25.119 1.00 52.49  ? 92  TYR B O   1 
ATOM   1467 C CB  . TYR B 1 93 ? 19.556  -2.507  -27.885 1.00 34.69  ? 92  TYR B CB  1 
ATOM   1468 C CG  . TYR B 1 93 ? 18.575  -2.361  -29.038 1.00 32.97  ? 92  TYR B CG  1 
ATOM   1469 C CD1 . TYR B 1 93 ? 17.298  -1.849  -28.837 1.00 32.06  ? 92  TYR B CD1 1 
ATOM   1470 C CD2 . TYR B 1 93 ? 18.923  -2.728  -30.337 1.00 31.35  ? 92  TYR B CD2 1 
ATOM   1471 C CE1 . TYR B 1 93 ? 16.405  -1.690  -29.883 1.00 34.06  ? 92  TYR B CE1 1 
ATOM   1472 C CE2 . TYR B 1 93 ? 18.028  -2.585  -31.389 1.00 30.01  ? 92  TYR B CE2 1 
ATOM   1473 C CZ  . TYR B 1 93 ? 16.768  -2.066  -31.165 1.00 31.98  ? 92  TYR B CZ  1 
ATOM   1474 O OH  . TYR B 1 93 ? 15.863  -1.905  -32.179 1.00 29.25  ? 92  TYR B OH  1 
ATOM   1475 N N   . SER B 1 94 ? 22.297  -1.030  -26.234 1.00 55.38  ? 93  SER B N   1 
ATOM   1476 C CA  . SER B 1 94 ? 23.190  -0.678  -25.138 1.00 66.44  ? 93  SER B CA  1 
ATOM   1477 C C   . SER B 1 94 ? 22.448  -0.631  -23.795 1.00 80.42  ? 93  SER B C   1 
ATOM   1478 O O   . SER B 1 94 ? 21.739  0.380   -23.561 1.00 84.35  ? 93  SER B O   1 
ATOM   1479 C CB  . SER B 1 94 ? 23.857  0.641   -25.422 1.00 65.96  ? 93  SER B CB  1 
ATOM   1480 O OG  . SER B 1 94 ? 24.636  0.561   -26.606 1.00 69.40  ? 93  SER B OG  1 
ATOM   1481 O OXT . SER B 1 94 ? 22.610  -1.603  -23.028 1.00 93.30  ? 93  SER B OXT 1 
ATOM   1482 N N   . HIS C 1 4  ? 32.386  -23.452 27.024  1.00 86.71  ? 3   HIS C N   1 
ATOM   1483 C CA  . HIS C 1 4  ? 31.209  -22.558 27.223  1.00 95.33  ? 3   HIS C CA  1 
ATOM   1484 C C   . HIS C 1 4  ? 30.538  -22.919 28.554  1.00 95.72  ? 3   HIS C C   1 
ATOM   1485 O O   . HIS C 1 4  ? 31.195  -23.457 29.447  1.00 95.42  ? 3   HIS C O   1 
ATOM   1486 C CB  . HIS C 1 4  ? 30.335  -22.570 25.959  1.00 95.14  ? 3   HIS C CB  1 
ATOM   1487 C CG  . HIS C 1 4  ? 29.591  -21.298 25.701  1.00 96.82  ? 3   HIS C CG  1 
ATOM   1488 N ND1 . HIS C 1 4  ? 28.286  -21.084 26.092  1.00 99.95  ? 3   HIS C ND1 1 
ATOM   1489 C CD2 . HIS C 1 4  ? 29.977  -20.175 25.080  1.00 95.70  ? 3   HIS C CD2 1 
ATOM   1490 C CE1 . HIS C 1 4  ? 27.908  -19.868 25.722  1.00 98.24  ? 3   HIS C CE1 1 
ATOM   1491 N NE2 . HIS C 1 4  ? 28.922  -19.298 25.108  1.00 97.10  ? 3   HIS C NE2 1 
ATOM   1492 N N   . ALA C 1 5  ? 29.240  -22.599 28.684  1.00 89.61  ? 4   ALA C N   1 
ATOM   1493 C CA  . ALA C 1 5  ? 28.417  -22.939 29.839  1.00 79.83  ? 4   ALA C CA  1 
ATOM   1494 C C   . ALA C 1 5  ? 26.939  -22.752 29.500  1.00 75.21  ? 4   ALA C C   1 
ATOM   1495 O O   . ALA C 1 5  ? 26.606  -21.940 28.640  1.00 77.43  ? 4   ALA C O   1 
ATOM   1496 C CB  . ALA C 1 5  ? 28.801  -22.070 31.002  1.00 83.68  ? 4   ALA C CB  1 
ATOM   1497 N N   . PHE C 1 6  ? 26.056  -23.480 30.203  1.00 61.79  ? 5   PHE C N   1 
ATOM   1498 C CA  . PHE C 1 6  ? 24.666  -23.590 29.780  1.00 55.86  ? 5   PHE C CA  1 
ATOM   1499 C C   . PHE C 1 6  ? 23.765  -23.738 31.003  1.00 60.95  ? 5   PHE C C   1 
ATOM   1500 O O   . PHE C 1 6  ? 24.072  -24.518 31.901  1.00 68.82  ? 5   PHE C O   1 
ATOM   1501 C CB  . PHE C 1 6  ? 24.488  -24.812 28.863  1.00 53.55  ? 5   PHE C CB  1 
ATOM   1502 C CG  . PHE C 1 6  ? 25.390  -24.875 27.632  1.00 49.01  ? 5   PHE C CG  1 
ATOM   1503 C CD1 . PHE C 1 6  ? 26.571  -25.609 27.645  1.00 52.04  ? 5   PHE C CD1 1 
ATOM   1504 C CD2 . PHE C 1 6  ? 25.072  -24.175 26.471  1.00 51.24  ? 5   PHE C CD2 1 
ATOM   1505 C CE1 . PHE C 1 6  ? 27.405  -25.632 26.535  1.00 51.78  ? 5   PHE C CE1 1 
ATOM   1506 C CE2 . PHE C 1 6  ? 25.905  -24.212 25.358  1.00 49.25  ? 5   PHE C CE2 1 
ATOM   1507 C CZ  . PHE C 1 6  ? 27.064  -24.945 25.390  1.00 52.77  ? 5   PHE C CZ  1 
ATOM   1508 N N   . LYS C 1 7  ? 22.638  -23.014 31.007  1.00 54.77  ? 6   LYS C N   1 
ATOM   1509 C CA  . LYS C 1 7  ? 21.631  -23.135 32.053  1.00 56.71  ? 6   LYS C CA  1 
ATOM   1510 C C   . LYS C 1 7  ? 20.289  -23.465 31.402  1.00 52.77  ? 6   LYS C C   1 
ATOM   1511 O O   . LYS C 1 7  ? 20.113  -23.243 30.201  1.00 50.97  ? 6   LYS C O   1 
ATOM   1512 C CB  . LYS C 1 7  ? 21.595  -21.887 32.950  1.00 56.11  ? 6   LYS C CB  1 
ATOM   1513 N N   . PRO C 1 8  ? 19.299  -24.014 32.148  1.00 57.40  ? 7   PRO C N   1 
ATOM   1514 C CA  . PRO C 1 8  ? 18.012  -24.391 31.551  1.00 54.22  ? 7   PRO C CA  1 
ATOM   1515 C C   . PRO C 1 8  ? 17.321  -23.259 30.784  1.00 60.44  ? 7   PRO C C   1 
ATOM   1516 O O   . PRO C 1 8  ? 17.267  -22.117 31.250  1.00 59.99  ? 7   PRO C O   1 
ATOM   1517 C CB  . PRO C 1 8  ? 17.175  -24.908 32.738  1.00 59.00  ? 7   PRO C CB  1 
ATOM   1518 C CG  . PRO C 1 8  ? 18.210  -25.290 33.788  1.00 57.80  ? 7   PRO C CG  1 
ATOM   1519 C CD  . PRO C 1 8  ? 19.372  -24.325 33.589  1.00 58.58  ? 7   PRO C CD  1 
ATOM   1520 N N   . GLY C 1 9  ? 16.812  -23.587 29.587  1.00 58.27  ? 8   GLY C N   1 
ATOM   1521 C CA  . GLY C 1 9  ? 16.174  -22.608 28.720  1.00 52.54  ? 8   GLY C CA  1 
ATOM   1522 C C   . GLY C 1 9  ? 17.115  -22.052 27.647  1.00 51.95  ? 8   GLY C C   1 
ATOM   1523 O O   . GLY C 1 9  ? 16.636  -21.437 26.697  1.00 52.81  ? 8   GLY C O   1 
ATOM   1524 N N   . ASP C 1 10 ? 18.435  -22.278 27.794  1.00 47.58  ? 9   ASP C N   1 
ATOM   1525 C CA  . ASP C 1 10 ? 19.454  -21.827 26.851  1.00 41.38  ? 9   ASP C CA  1 
ATOM   1526 C C   . ASP C 1 10 ? 19.354  -22.562 25.512  1.00 41.43  ? 9   ASP C C   1 
ATOM   1527 O O   . ASP C 1 10 ? 19.263  -23.779 25.480  1.00 44.71  ? 9   ASP C O   1 
ATOM   1528 C CB  . ASP C 1 10 ? 20.863  -22.037 27.378  1.00 45.46  ? 9   ASP C CB  1 
ATOM   1529 C CG  . ASP C 1 10 ? 21.394  -20.951 28.305  1.00 56.54  ? 9   ASP C CG  1 
ATOM   1530 O OD1 . ASP C 1 10 ? 20.568  -20.169 28.833  1.00 58.72  ? 9   ASP C OD1 1 
ATOM   1531 O OD2 . ASP C 1 10 ? 22.635  -20.870 28.463  1.00 56.54  ? 9   ASP C OD2 1 
ATOM   1532 N N   . LEU C 1 11 ? 19.445  -21.809 24.404  1.00 44.16  ? 10  LEU C N   1 
ATOM   1533 C CA  . LEU C 1 11 ? 19.128  -22.315 23.075  1.00 43.15  ? 10  LEU C CA  1 
ATOM   1534 C C   . LEU C 1 11 ? 20.411  -22.746 22.364  1.00 39.26  ? 10  LEU C C   1 
ATOM   1535 O O   . LEU C 1 11 ? 21.383  -22.001 22.318  1.00 37.97  ? 10  LEU C O   1 
ATOM   1536 C CB  . LEU C 1 11 ? 18.367  -21.264 22.259  1.00 40.54  ? 10  LEU C CB  1 
ATOM   1537 C CG  . LEU C 1 11 ? 17.080  -20.693 22.864  1.00 38.93  ? 10  LEU C CG  1 
ATOM   1538 C CD1 . LEU C 1 11 ? 16.465  -19.659 21.913  1.00 39.07  ? 10  LEU C CD1 1 
ATOM   1539 C CD2 . LEU C 1 11 ? 16.049  -21.770 23.184  1.00 36.77  ? 10  LEU C CD2 1 
ATOM   1540 N N   . VAL C 1 12 ? 20.389  -23.951 21.770  1.00 36.30  ? 11  VAL C N   1 
ATOM   1541 C CA  . VAL C 1 12 ? 21.592  -24.545 21.208  1.00 33.42  ? 11  VAL C CA  1 
ATOM   1542 C C   . VAL C 1 12 ? 21.212  -25.273 19.916  1.00 30.73  ? 11  VAL C C   1 
ATOM   1543 O O   . VAL C 1 12 ? 20.031  -25.432 19.624  1.00 30.84  ? 11  VAL C O   1 
ATOM   1544 C CB  . VAL C 1 12 ? 22.228  -25.527 22.214  1.00 32.40  ? 11  VAL C CB  1 
ATOM   1545 C CG1 . VAL C 1 12 ? 22.648  -24.841 23.519  1.00 31.85  ? 11  VAL C CG1 1 
ATOM   1546 C CG2 . VAL C 1 12 ? 21.296  -26.698 22.515  1.00 33.31  ? 11  VAL C CG2 1 
ATOM   1547 N N   . PHE C 1 13 ? 22.231  -25.655 19.140  1.00 30.87  ? 12  PHE C N   1 
ATOM   1548 C CA  . PHE C 1 13 ? 22.160  -26.813 18.263  1.00 28.90  ? 12  PHE C CA  1 
ATOM   1549 C C   . PHE C 1 13 ? 22.856  -27.968 18.974  1.00 30.10  ? 12  PHE C C   1 
ATOM   1550 O O   . PHE C 1 13 ? 23.928  -27.794 19.561  1.00 36.14  ? 12  PHE C O   1 
ATOM   1551 C CB  . PHE C 1 13 ? 22.774  -26.586 16.877  1.00 31.16  ? 12  PHE C CB  1 
ATOM   1552 C CG  . PHE C 1 13 ? 21.988  -25.574 16.058  1.00 36.21  ? 12  PHE C CG  1 
ATOM   1553 C CD1 . PHE C 1 13 ? 20.920  -25.980 15.248  1.00 35.70  ? 12  PHE C CD1 1 
ATOM   1554 C CD2 . PHE C 1 13 ? 22.275  -24.210 16.143  1.00 35.82  ? 12  PHE C CD2 1 
ATOM   1555 C CE1 . PHE C 1 13 ? 20.192  -25.052 14.520  1.00 34.20  ? 12  PHE C CE1 1 
ATOM   1556 C CE2 . PHE C 1 13 ? 21.530  -23.281 15.419  1.00 37.72  ? 12  PHE C CE2 1 
ATOM   1557 C CZ  . PHE C 1 13 ? 20.500  -23.701 14.603  1.00 37.34  ? 12  PHE C CZ  1 
ATOM   1558 N N   . ALA C 1 14 ? 22.203  -29.131 18.949  1.00 30.15  ? 13  ALA C N   1 
ATOM   1559 C CA  . ALA C 1 14 ? 22.654  -30.291 19.702  1.00 29.34  ? 13  ALA C CA  1 
ATOM   1560 C C   . ALA C 1 14 ? 22.953  -31.414 18.716  1.00 31.91  ? 13  ALA C C   1 
ATOM   1561 O O   . ALA C 1 14 ? 22.116  -31.728 17.878  1.00 27.12  ? 13  ALA C O   1 
ATOM   1562 C CB  . ALA C 1 14 ? 21.567  -30.696 20.686  1.00 34.28  ? 13  ALA C CB  1 
ATOM   1563 N N   . LYS C 1 15 ? 24.158  -31.997 18.800  1.00 29.39  ? 14  LYS C N   1 
ATOM   1564 C CA  . LYS C 1 15 ? 24.537  -33.035 17.856  1.00 32.05  ? 14  LYS C CA  1 
ATOM   1565 C C   . LYS C 1 15 ? 24.519  -34.387 18.549  1.00 34.54  ? 14  LYS C C   1 
ATOM   1566 O O   . LYS C 1 15 ? 25.194  -34.579 19.558  1.00 34.88  ? 14  LYS C O   1 
ATOM   1567 C CB  . LYS C 1 15 ? 25.964  -32.828 17.324  1.00 33.98  ? 14  LYS C CB  1 
ATOM   1568 C CG  . LYS C 1 15 ? 26.398  -33.841 16.273  1.00 31.40  ? 14  LYS C CG  1 
ATOM   1569 C CD  . LYS C 1 15 ? 25.586  -33.765 14.985  1.00 29.61  ? 14  LYS C CD  1 
ATOM   1570 C CE  . LYS C 1 15 ? 26.131  -34.615 13.841  1.00 28.46  ? 14  LYS C CE  1 
ATOM   1571 N NZ  . LYS C 1 15 ? 25.914  -36.039 14.119  1.00 29.07  ? 14  LYS C NZ  1 
ATOM   1572 N N   . MET C 1 16 ? 23.785  -35.317 17.933  1.00 32.29  ? 15  MET C N   1 
ATOM   1573 C CA  . MET C 1 16 ? 23.708  -36.711 18.314  1.00 33.92  ? 15  MET C CA  1 
ATOM   1574 C C   . MET C 1 16 ? 24.220  -37.524 17.133  1.00 37.24  ? 15  MET C C   1 
ATOM   1575 O O   . MET C 1 16 ? 24.064  -37.105 15.977  1.00 31.40  ? 15  MET C O   1 
ATOM   1576 C CB  . MET C 1 16 ? 22.258  -37.128 18.576  1.00 32.27  ? 15  MET C CB  1 
ATOM   1577 C CG  . MET C 1 16 ? 21.737  -36.693 19.938  1.00 33.89  ? 15  MET C CG  1 
ATOM   1578 S SD  . MET C 1 16 ? 20.100  -37.364 20.278  1.00 43.61  ? 15  MET C SD  1 
ATOM   1579 C CE  . MET C 1 16 ? 19.212  -36.795 18.817  1.00 38.05  ? 15  MET C CE  1 
ATOM   1580 N N   . LYS C 1 17 ? 24.806  -38.693 17.434  1.00 38.68  ? 16  LYS C N   1 
ATOM   1581 C CA  . LYS C 1 17 ? 25.270  -39.572 16.365  1.00 40.47  ? 16  LYS C CA  1 
ATOM   1582 C C   . LYS C 1 17 ? 24.055  -40.010 15.546  1.00 32.10  ? 16  LYS C C   1 
ATOM   1583 O O   . LYS C 1 17 ? 23.087  -40.518 16.102  1.00 30.36  ? 16  LYS C O   1 
ATOM   1584 C CB  . LYS C 1 17 ? 25.998  -40.813 16.908  1.00 42.16  ? 16  LYS C CB  1 
ATOM   1585 C CG  . LYS C 1 17 ? 26.646  -41.708 15.850  1.00 42.09  ? 16  LYS C CG  1 
ATOM   1586 C CD  . LYS C 1 17 ? 27.973  -41.142 15.358  1.00 44.84  ? 16  LYS C CD  1 
ATOM   1587 C CE  . LYS C 1 17 ? 28.476  -41.779 14.102  1.00 51.96  ? 16  LYS C CE  1 
ATOM   1588 N NZ  . LYS C 1 17 ? 29.863  -41.355 13.887  1.00 47.47  ? 16  LYS C NZ  1 
ATOM   1589 N N   . GLY C 1 18 ? 24.140  -39.805 14.228  1.00 35.38  ? 17  GLY C N   1 
ATOM   1590 C CA  . GLY C 1 18 ? 23.122  -40.274 13.310  1.00 38.43  ? 17  GLY C CA  1 
ATOM   1591 C C   . GLY C 1 18 ? 22.105  -39.181 12.960  1.00 38.36  ? 17  GLY C C   1 
ATOM   1592 O O   . GLY C 1 18 ? 21.095  -39.476 12.331  1.00 36.40  ? 17  GLY C O   1 
ATOM   1593 N N   . TYR C 1 19 ? 22.360  -37.940 13.403  1.00 35.54  ? 18  TYR C N   1 
ATOM   1594 C CA  . TYR C 1 19 ? 21.420  -36.832 13.250  1.00 35.64  ? 18  TYR C CA  1 
ATOM   1595 C C   . TYR C 1 19 ? 22.215  -35.569 12.942  1.00 31.95  ? 18  TYR C C   1 
ATOM   1596 O O   . TYR C 1 19 ? 23.338  -35.395 13.403  1.00 32.19  ? 18  TYR C O   1 
ATOM   1597 C CB  . TYR C 1 19 ? 20.597  -36.601 14.527  1.00 31.80  ? 18  TYR C CB  1 
ATOM   1598 C CG  . TYR C 1 19 ? 19.749  -37.797 14.916  1.00 36.22  ? 18  TYR C CG  1 
ATOM   1599 C CD1 . TYR C 1 19 ? 20.275  -38.874 15.636  1.00 33.14  ? 18  TYR C CD1 1 
ATOM   1600 C CD2 . TYR C 1 19 ? 18.415  -37.853 14.532  1.00 35.79  ? 18  TYR C CD2 1 
ATOM   1601 C CE1 . TYR C 1 19 ? 19.484  -39.964 15.962  1.00 37.41  ? 18  TYR C CE1 1 
ATOM   1602 C CE2 . TYR C 1 19 ? 17.617  -38.930 14.863  1.00 44.30  ? 18  TYR C CE2 1 
ATOM   1603 C CZ  . TYR C 1 19 ? 18.154  -39.988 15.570  1.00 42.94  ? 18  TYR C CZ  1 
ATOM   1604 O OH  . TYR C 1 19 ? 17.308  -41.015 15.860  1.00 49.87  ? 18  TYR C OH  1 
ATOM   1605 N N   . PRO C 1 20 ? 21.652  -34.655 12.127  1.00 34.16  ? 19  PRO C N   1 
ATOM   1606 C CA  . PRO C 1 20 ? 22.263  -33.342 11.918  1.00 30.06  ? 19  PRO C CA  1 
ATOM   1607 C C   . PRO C 1 20 ? 22.226  -32.551 13.233  1.00 27.28  ? 19  PRO C C   1 
ATOM   1608 O O   . PRO C 1 20 ? 21.431  -32.843 14.136  1.00 29.92  ? 19  PRO C O   1 
ATOM   1609 C CB  . PRO C 1 20 ? 21.327  -32.742 10.854  1.00 32.98  ? 19  PRO C CB  1 
ATOM   1610 C CG  . PRO C 1 20 ? 19.982  -33.378 11.139  1.00 32.62  ? 19  PRO C CG  1 
ATOM   1611 C CD  . PRO C 1 20 ? 20.347  -34.817 11.453  1.00 34.24  ? 19  PRO C CD  1 
ATOM   1612 N N   . HIS C 1 21 ? 23.074  -31.526 13.311  1.00 29.77  ? 20  HIS C N   1 
ATOM   1613 C CA  . HIS C 1 21 ? 22.995  -30.540 14.380  1.00 29.18  ? 20  HIS C CA  1 
ATOM   1614 C C   . HIS C 1 21 ? 21.550  -30.047 14.478  1.00 29.63  ? 20  HIS C C   1 
ATOM   1615 O O   . HIS C 1 21 ? 20.983  -29.568 13.489  1.00 28.41  ? 20  HIS C O   1 
ATOM   1616 C CB  . HIS C 1 21 ? 23.997  -29.418 14.133  1.00 30.72  ? 20  HIS C CB  1 
ATOM   1617 C CG  . HIS C 1 21 ? 25.416  -29.895 14.203  1.00 29.58  ? 20  HIS C CG  1 
ATOM   1618 N ND1 . HIS C 1 21 ? 26.023  -30.617 13.193  1.00 36.88  ? 20  HIS C ND1 1 
ATOM   1619 C CD2 . HIS C 1 21 ? 26.325  -29.775 15.181  1.00 36.14  ? 20  HIS C CD2 1 
ATOM   1620 C CE1 . HIS C 1 21 ? 27.283  -30.900 13.549  1.00 34.92  ? 20  HIS C CE1 1 
ATOM   1621 N NE2 . HIS C 1 21 ? 27.501  -30.370 14.748  1.00 33.39  ? 20  HIS C NE2 1 
ATOM   1622 N N   . TRP C 1 22 ? 20.950  -30.254 15.656  1.00 29.10  ? 21  TRP C N   1 
ATOM   1623 C CA  . TRP C 1 22 ? 19.504  -30.146 15.800  1.00 26.05  ? 21  TRP C CA  1 
ATOM   1624 C C   . TRP C 1 22 ? 19.135  -28.958 16.687  1.00 26.94  ? 21  TRP C C   1 
ATOM   1625 O O   . TRP C 1 22 ? 19.702  -28.798 17.780  1.00 29.99  ? 21  TRP C O   1 
ATOM   1626 C CB  . TRP C 1 22 ? 18.940  -31.448 16.394  1.00 30.66  ? 21  TRP C CB  1 
ATOM   1627 C CG  . TRP C 1 22 ? 17.483  -31.686 16.064  1.00 32.59  ? 21  TRP C CG  1 
ATOM   1628 C CD1 . TRP C 1 22 ? 16.377  -31.116 16.634  1.00 31.81  ? 21  TRP C CD1 1 
ATOM   1629 C CD2 . TRP C 1 22 ? 16.992  -32.583 15.035  1.00 32.65  ? 21  TRP C CD2 1 
ATOM   1630 N NE1 . TRP C 1 22 ? 15.237  -31.594 16.033  1.00 30.90  ? 21  TRP C NE1 1 
ATOM   1631 C CE2 . TRP C 1 22 ? 15.583  -32.484 15.047  1.00 31.05  ? 21  TRP C CE2 1 
ATOM   1632 C CE3 . TRP C 1 22 ? 17.605  -33.429 14.096  1.00 30.40  ? 21  TRP C CE3 1 
ATOM   1633 C CZ2 . TRP C 1 22 ? 14.796  -33.216 14.155  1.00 31.42  ? 21  TRP C CZ2 1 
ATOM   1634 C CZ3 . TRP C 1 22 ? 16.824  -34.140 13.208  1.00 31.47  ? 21  TRP C CZ3 1 
ATOM   1635 C CH2 . TRP C 1 22 ? 15.431  -34.045 13.258  1.00 29.33  ? 21  TRP C CH2 1 
ATOM   1636 N N   . PRO C 1 23 ? 18.118  -28.136 16.321  1.00 29.54  ? 22  PRO C N   1 
ATOM   1637 C CA  . PRO C 1 23 ? 17.677  -27.049 17.202  1.00 30.80  ? 22  PRO C CA  1 
ATOM   1638 C C   . PRO C 1 23 ? 17.126  -27.568 18.534  1.00 30.47  ? 22  PRO C C   1 
ATOM   1639 O O   . PRO C 1 23 ? 16.321  -28.503 18.574  1.00 29.74  ? 22  PRO C O   1 
ATOM   1640 C CB  . PRO C 1 23 ? 16.635  -26.292 16.353  1.00 32.68  ? 22  PRO C CB  1 
ATOM   1641 C CG  . PRO C 1 23 ? 16.142  -27.344 15.375  1.00 28.41  ? 22  PRO C CG  1 
ATOM   1642 C CD  . PRO C 1 23 ? 17.410  -28.143 15.027  1.00 27.64  ? 22  PRO C CD  1 
ATOM   1643 N N   . ALA C 1 24 ? 17.608  -26.988 19.634  1.00 30.83  ? 23  ALA C N   1 
ATOM   1644 C CA  . ALA C 1 24 ? 17.278  -27.550 20.940  1.00 31.76  ? 23  ALA C CA  1 
ATOM   1645 C C   . ALA C 1 24 ? 17.452  -26.508 22.043  1.00 34.38  ? 23  ALA C C   1 
ATOM   1646 O O   . ALA C 1 24 ? 17.976  -25.409 21.804  1.00 33.29  ? 23  ALA C O   1 
ATOM   1647 C CB  . ALA C 1 24 ? 18.130  -28.794 21.202  1.00 29.03  ? 23  ALA C CB  1 
ATOM   1648 N N   . ARG C 1 25 ? 17.053  -26.885 23.272  1.00 34.64  ? 24  ARG C N   1 
ATOM   1649 C CA  . ARG C 1 25 ? 17.354  -26.067 24.440  1.00 38.39  ? 24  ARG C CA  1 
ATOM   1650 C C   . ARG C 1 25 ? 17.810  -26.964 25.594  1.00 39.01  ? 24  ARG C C   1 
ATOM   1651 O O   . ARG C 1 25 ? 17.496  -28.158 25.616  1.00 38.75  ? 24  ARG C O   1 
ATOM   1652 C CB  . ARG C 1 25 ? 16.128  -25.283 24.923  1.00 38.78  ? 24  ARG C CB  1 
ATOM   1653 C CG  . ARG C 1 25 ? 14.945  -26.079 25.454  1.00 42.20  ? 24  ARG C CG  1 
ATOM   1654 C CD  . ARG C 1 25 ? 13.819  -25.178 25.950  1.00 43.24  ? 24  ARG C CD  1 
ATOM   1655 N NE  . ARG C 1 25 ? 12.638  -25.990 26.267  1.00 45.92  ? 24  ARG C NE  1 
ATOM   1656 C CZ  . ARG C 1 25 ? 11.373  -25.760 25.921  1.00 55.88  ? 24  ARG C CZ  1 
ATOM   1657 N NH1 . ARG C 1 25 ? 11.054  -24.710 25.177  1.00 49.33  ? 24  ARG C NH1 1 
ATOM   1658 N NH2 . ARG C 1 25 ? 10.420  -26.587 26.332  1.00 56.24  ? 24  ARG C NH2 1 
ATOM   1659 N N   . ILE C 1 26 ? 18.515  -26.352 26.547  1.00 36.89  ? 25  ILE C N   1 
ATOM   1660 C CA  . ILE C 1 26 ? 18.864  -26.980 27.819  1.00 45.49  ? 25  ILE C CA  1 
ATOM   1661 C C   . ILE C 1 26 ? 17.597  -27.128 28.666  1.00 49.96  ? 25  ILE C C   1 
ATOM   1662 O O   . ILE C 1 26 ? 16.843  -26.176 28.852  1.00 49.86  ? 25  ILE C O   1 
ATOM   1663 C CB  . ILE C 1 26 ? 19.956  -26.190 28.567  1.00 48.07  ? 25  ILE C CB  1 
ATOM   1664 C CG1 . ILE C 1 26 ? 21.117  -25.775 27.684  1.00 43.48  ? 25  ILE C CG1 1 
ATOM   1665 C CG2 . ILE C 1 26 ? 20.449  -26.930 29.813  1.00 50.36  ? 25  ILE C CG2 1 
ATOM   1666 C CD1 . ILE C 1 26 ? 21.932  -26.925 27.121  1.00 44.37  ? 25  ILE C CD1 1 
ATOM   1667 N N   . ASP C 1 27 ? 17.369  -28.337 29.177  1.00 51.99  ? 26  ASP C N   1 
ATOM   1668 C CA  . ASP C 1 27 ? 16.269  -28.587 30.098  1.00 65.40  ? 26  ASP C CA  1 
ATOM   1669 C C   . ASP C 1 27 ? 16.688  -28.308 31.540  1.00 68.88  ? 26  ASP C C   1 
ATOM   1670 O O   . ASP C 1 27 ? 17.845  -27.985 31.801  1.00 66.74  ? 26  ASP C O   1 
ATOM   1671 C CB  . ASP C 1 27 ? 15.657  -29.962 29.888  1.00 67.79  ? 26  ASP C CB  1 
ATOM   1672 C CG  . ASP C 1 27 ? 14.213  -29.926 29.421  1.00 71.57  ? 26  ASP C CG  1 
ATOM   1673 O OD1 . ASP C 1 27 ? 13.884  -28.984 28.670  1.00 72.96  ? 26  ASP C OD1 1 
ATOM   1674 O OD2 . ASP C 1 27 ? 13.437  -30.826 29.826  1.00 60.91  ? 26  ASP C OD2 1 
ATOM   1675 N N   . ASP C 1 28 ? 15.718  -28.427 32.458  1.00 81.97  ? 27  ASP C N   1 
ATOM   1676 C CA  . ASP C 1 28 ? 15.934  -28.261 33.887  1.00 81.64  ? 27  ASP C CA  1 
ATOM   1677 C C   . ASP C 1 28 ? 15.949  -29.637 34.543  1.00 83.51  ? 27  ASP C C   1 
ATOM   1678 O O   . ASP C 1 28 ? 15.004  -30.403 34.375  1.00 98.68  ? 27  ASP C O   1 
ATOM   1679 C CB  . ASP C 1 28 ? 14.853  -27.385 34.501  1.00 82.78  ? 27  ASP C CB  1 
ATOM   1680 N N   . ILE C 1 29 ? 17.016  -29.937 35.295  1.00 79.63  ? 28  ILE C N   1 
ATOM   1681 C CA  . ILE C 1 29 ? 17.140  -31.225 35.959  1.00 83.45  ? 28  ILE C CA  1 
ATOM   1682 C C   . ILE C 1 29 ? 16.683  -31.079 37.420  1.00 85.34  ? 28  ILE C C   1 
ATOM   1683 O O   . ILE C 1 29 ? 15.512  -31.437 37.692  1.00 84.34  ? 28  ILE C O   1 
ATOM   1684 C CB  . ILE C 1 29 ? 18.577  -31.771 35.854  1.00 85.57  ? 28  ILE C CB  1 
ATOM   1685 N N   . LYS C 1 35 ? 19.490  -38.528 37.939  1.00 72.07  ? 34  LYS C N   1 
ATOM   1686 C CA  . LYS C 1 35 ? 20.399  -37.391 37.631  1.00 71.25  ? 34  LYS C CA  1 
ATOM   1687 C C   . LYS C 1 35 ? 21.129  -37.682 36.318  1.00 67.40  ? 34  LYS C C   1 
ATOM   1688 O O   . LYS C 1 35 ? 21.211  -38.839 35.898  1.00 67.86  ? 34  LYS C O   1 
ATOM   1689 C CB  . LYS C 1 35 ? 21.324  -37.102 38.824  1.00 69.04  ? 34  LYS C CB  1 
ATOM   1690 N N   . PRO C 1 36 ? 21.652  -36.642 35.620  1.00 64.88  ? 35  PRO C N   1 
ATOM   1691 C CA  . PRO C 1 36 ? 22.406  -36.837 34.377  1.00 63.88  ? 35  PRO C CA  1 
ATOM   1692 C C   . PRO C 1 36 ? 23.634  -37.730 34.572  1.00 67.96  ? 35  PRO C C   1 
ATOM   1693 O O   . PRO C 1 36 ? 24.239  -37.730 35.646  1.00 58.60  ? 35  PRO C O   1 
ATOM   1694 C CB  . PRO C 1 36 ? 22.818  -35.398 33.986  1.00 64.47  ? 35  PRO C CB  1 
ATOM   1695 C CG  . PRO C 1 36 ? 21.851  -34.490 34.713  1.00 64.85  ? 35  PRO C CG  1 
ATOM   1696 C CD  . PRO C 1 36 ? 21.554  -35.222 36.009  1.00 65.43  ? 35  PRO C CD  1 
ATOM   1697 N N   . PRO C 1 37 ? 24.063  -38.511 33.551  1.00 64.49  ? 36  PRO C N   1 
ATOM   1698 C CA  . PRO C 1 37 ? 25.393  -39.127 33.586  1.00 59.35  ? 36  PRO C CA  1 
ATOM   1699 C C   . PRO C 1 37 ? 26.412  -38.008 33.811  1.00 58.81  ? 36  PRO C C   1 
ATOM   1700 O O   . PRO C 1 37 ? 26.149  -36.855 33.459  1.00 52.35  ? 36  PRO C O   1 
ATOM   1701 C CB  . PRO C 1 37 ? 25.528  -39.803 32.202  1.00 55.18  ? 36  PRO C CB  1 
ATOM   1702 C CG  . PRO C 1 37 ? 24.092  -40.035 31.775  1.00 57.63  ? 36  PRO C CG  1 
ATOM   1703 C CD  . PRO C 1 37 ? 23.305  -38.853 32.336  1.00 57.95  ? 36  PRO C CD  1 
ATOM   1704 N N   . PRO C 1 38 ? 27.585  -38.299 34.428  1.00 50.48  ? 37  PRO C N   1 
ATOM   1705 C CA  . PRO C 1 38 ? 28.569  -37.261 34.742  1.00 50.53  ? 37  PRO C CA  1 
ATOM   1706 C C   . PRO C 1 38 ? 28.806  -36.332 33.556  1.00 44.18  ? 37  PRO C C   1 
ATOM   1707 O O   . PRO C 1 38 ? 28.986  -36.809 32.442  1.00 37.74  ? 37  PRO C O   1 
ATOM   1708 C CB  . PRO C 1 38 ? 29.830  -38.101 35.078  1.00 53.43  ? 37  PRO C CB  1 
ATOM   1709 C CG  . PRO C 1 38 ? 29.264  -39.385 35.655  1.00 52.56  ? 37  PRO C CG  1 
ATOM   1710 C CD  . PRO C 1 38 ? 28.025  -39.648 34.825  1.00 53.52  ? 37  PRO C CD  1 
ATOM   1711 N N   . ASN C 1 39 ? 28.768  -35.019 33.821  1.00 43.11  ? 38  ASN C N   1 
ATOM   1712 C CA  . ASN C 1 39 ? 29.085  -33.961 32.871  1.00 44.77  ? 38  ASN C CA  1 
ATOM   1713 C C   . ASN C 1 39 ? 28.133  -33.960 31.671  1.00 44.28  ? 38  ASN C C   1 
ATOM   1714 O O   . ASN C 1 39 ? 28.549  -33.561 30.583  1.00 45.09  ? 38  ASN C O   1 
ATOM   1715 C CB  . ASN C 1 39 ? 30.533  -34.036 32.389  1.00 52.29  ? 38  ASN C CB  1 
ATOM   1716 C CG  . ASN C 1 39 ? 31.007  -32.739 31.773  1.00 60.59  ? 38  ASN C CG  1 
ATOM   1717 O OD1 . ASN C 1 39 ? 30.449  -31.669 32.046  1.00 72.06  ? 38  ASN C OD1 1 
ATOM   1718 N ND2 . ASN C 1 39 ? 32.044  -32.808 30.953  1.00 64.44  ? 38  ASN C ND2 1 
ATOM   1719 N N   . LYS C 1 40 ? 26.873  -34.392 31.858  1.00 40.16  ? 39  LYS C N   1 
ATOM   1720 C CA  . LYS C 1 40 ? 25.916  -34.352 30.752  1.00 41.38  ? 39  LYS C CA  1 
ATOM   1721 C C   . LYS C 1 40 ? 24.778  -33.381 31.054  1.00 39.92  ? 39  LYS C C   1 
ATOM   1722 O O   . LYS C 1 40 ? 24.350  -33.235 32.197  1.00 40.69  ? 39  LYS C O   1 
ATOM   1723 C CB  . LYS C 1 40 ? 25.273  -35.693 30.382  1.00 38.96  ? 39  LYS C CB  1 
ATOM   1724 C CG  . LYS C 1 40 ? 26.231  -36.807 29.990  1.00 45.36  ? 39  LYS C CG  1 
ATOM   1725 C CD  . LYS C 1 40 ? 27.094  -36.527 28.770  1.00 49.50  ? 39  LYS C CD  1 
ATOM   1726 C CE  . LYS C 1 40 ? 27.751  -37.796 28.316  1.00 54.10  ? 39  LYS C CE  1 
ATOM   1727 N NZ  . LYS C 1 40 ? 28.809  -37.510 27.340  1.00 57.81  ? 39  LYS C NZ  1 
ATOM   1728 N N   . TYR C 1 41 ? 24.270  -32.733 29.999  1.00 37.31  ? 40  TYR C N   1 
ATOM   1729 C CA  . TYR C 1 41 ? 23.137  -31.825 30.129  1.00 37.00  ? 40  TYR C CA  1 
ATOM   1730 C C   . TYR C 1 41 ? 21.877  -32.516 29.619  1.00 43.73  ? 40  TYR C C   1 
ATOM   1731 O O   . TYR C 1 41 ? 21.950  -33.310 28.668  1.00 41.35  ? 40  TYR C O   1 
ATOM   1732 C CB  . TYR C 1 41 ? 23.313  -30.586 29.240  1.00 36.95  ? 40  TYR C CB  1 
ATOM   1733 C CG  . TYR C 1 41 ? 24.401  -29.620 29.677  1.00 40.75  ? 40  TYR C CG  1 
ATOM   1734 C CD1 . TYR C 1 41 ? 25.716  -29.737 29.228  1.00 43.39  ? 40  TYR C CD1 1 
ATOM   1735 C CD2 . TYR C 1 41 ? 24.095  -28.577 30.539  1.00 42.16  ? 40  TYR C CD2 1 
ATOM   1736 C CE1 . TYR C 1 41 ? 26.691  -28.837 29.637  1.00 50.12  ? 40  TYR C CE1 1 
ATOM   1737 C CE2 . TYR C 1 41 ? 25.052  -27.667 30.943  1.00 47.98  ? 40  TYR C CE2 1 
ATOM   1738 C CZ  . TYR C 1 41 ? 26.352  -27.801 30.496  1.00 51.06  ? 40  TYR C CZ  1 
ATOM   1739 O OH  . TYR C 1 41 ? 27.233  -26.857 30.928  1.00 61.91  ? 40  TYR C OH  1 
ATOM   1740 N N   . PRO C 1 42 ? 20.700  -32.217 30.231  1.00 40.96  ? 41  PRO C N   1 
ATOM   1741 C CA  . PRO C 1 42 ? 19.409  -32.668 29.715  1.00 37.11  ? 41  PRO C CA  1 
ATOM   1742 C C   . PRO C 1 42 ? 19.006  -31.712 28.596  1.00 35.63  ? 41  PRO C C   1 
ATOM   1743 O O   . PRO C 1 42 ? 18.991  -30.499 28.798  1.00 37.19  ? 41  PRO C O   1 
ATOM   1744 C CB  . PRO C 1 42 ? 18.497  -32.546 30.943  1.00 35.50  ? 41  PRO C CB  1 
ATOM   1745 C CG  . PRO C 1 42 ? 19.058  -31.379 31.705  1.00 39.56  ? 41  PRO C CG  1 
ATOM   1746 C CD  . PRO C 1 42 ? 20.563  -31.421 31.469  1.00 39.54  ? 41  PRO C CD  1 
ATOM   1747 N N   . ILE C 1 43 ? 18.731  -32.290 27.424  1.00 34.88  ? 42  ILE C N   1 
ATOM   1748 C CA  . ILE C 1 43 ? 18.424  -31.559 26.200  1.00 34.10  ? 42  ILE C CA  1 
ATOM   1749 C C   . ILE C 1 43 ? 16.987  -31.859 25.801  1.00 36.38  ? 42  ILE C C   1 
ATOM   1750 O O   . ILE C 1 43 ? 16.566  -33.019 25.817  1.00 39.50  ? 42  ILE C O   1 
ATOM   1751 C CB  . ILE C 1 43 ? 19.418  -31.956 25.091  1.00 32.22  ? 42  ILE C CB  1 
ATOM   1752 C CG1 . ILE C 1 43 ? 20.884  -31.719 25.538  1.00 32.83  ? 42  ILE C CG1 1 
ATOM   1753 C CG2 . ILE C 1 43 ? 19.078  -31.281 23.746  1.00 29.98  ? 42  ILE C CG2 1 
ATOM   1754 C CD1 . ILE C 1 43 ? 21.238  -30.278 25.867  1.00 32.21  ? 42  ILE C CD1 1 
ATOM   1755 N N   . PHE C 1 44 ? 16.255  -30.800 25.411  1.00 35.68  ? 43  PHE C N   1 
ATOM   1756 C CA  . PHE C 1 44 ? 14.975  -30.912 24.740  1.00 34.32  ? 43  PHE C CA  1 
ATOM   1757 C C   . PHE C 1 44 ? 15.169  -30.501 23.281  1.00 33.95  ? 43  PHE C C   1 
ATOM   1758 O O   . PHE C 1 44 ? 15.675  -29.415 23.017  1.00 33.19  ? 43  PHE C O   1 
ATOM   1759 C CB  . PHE C 1 44 ? 14.026  -29.872 25.336  1.00 38.02  ? 43  PHE C CB  1 
ATOM   1760 C CG  . PHE C 1 44 ? 12.625  -29.854 24.734  1.00 41.31  ? 43  PHE C CG  1 
ATOM   1761 C CD1 . PHE C 1 44 ? 11.674  -30.814 25.091  1.00 42.76  ? 43  PHE C CD1 1 
ATOM   1762 C CD2 . PHE C 1 44 ? 12.247  -28.853 23.834  1.00 43.23  ? 43  PHE C CD2 1 
ATOM   1763 C CE1 . PHE C 1 44 ? 10.387  -30.784 24.554  1.00 46.82  ? 43  PHE C CE1 1 
ATOM   1764 C CE2 . PHE C 1 44 ? 10.966  -28.834 23.290  1.00 41.69  ? 43  PHE C CE2 1 
ATOM   1765 C CZ  . PHE C 1 44 ? 10.036  -29.795 23.655  1.00 45.04  ? 43  PHE C CZ  1 
ATOM   1766 N N   . PHE C 1 45 ? 14.763  -31.366 22.354  1.00 31.79  ? 44  PHE C N   1 
ATOM   1767 C CA  . PHE C 1 45 ? 14.929  -31.114 20.929  1.00 33.44  ? 44  PHE C CA  1 
ATOM   1768 C C   . PHE C 1 45 ? 13.663  -30.456 20.394  1.00 34.29  ? 44  PHE C C   1 
ATOM   1769 O O   . PHE C 1 45 ? 12.568  -30.982 20.597  1.00 33.07  ? 44  PHE C O   1 
ATOM   1770 C CB  . PHE C 1 45 ? 15.188  -32.417 20.169  1.00 33.50  ? 44  PHE C CB  1 
ATOM   1771 C CG  . PHE C 1 45 ? 16.569  -32.992 20.463  1.00 34.41  ? 44  PHE C CG  1 
ATOM   1772 C CD1 . PHE C 1 45 ? 17.680  -32.589 19.727  1.00 33.71  ? 44  PHE C CD1 1 
ATOM   1773 C CD2 . PHE C 1 45 ? 16.761  -33.877 21.523  1.00 35.21  ? 44  PHE C CD2 1 
ATOM   1774 C CE1 . PHE C 1 45 ? 18.950  -33.099 20.021  1.00 35.93  ? 44  PHE C CE1 1 
ATOM   1775 C CE2 . PHE C 1 45 ? 18.025  -34.378 21.818  1.00 38.26  ? 44  PHE C CE2 1 
ATOM   1776 C CZ  . PHE C 1 45 ? 19.115  -33.988 21.075  1.00 36.24  ? 44  PHE C CZ  1 
ATOM   1777 N N   . PHE C 1 46 ? 13.819  -29.326 19.685  1.00 31.05  ? 45  PHE C N   1 
ATOM   1778 C CA  . PHE C 1 46 ? 12.657  -28.710 19.042  1.00 31.54  ? 45  PHE C CA  1 
ATOM   1779 C C   . PHE C 1 46 ? 12.115  -29.618 17.930  1.00 34.23  ? 45  PHE C C   1 
ATOM   1780 O O   . PHE C 1 46 ? 12.864  -30.372 17.307  1.00 32.23  ? 45  PHE C O   1 
ATOM   1781 C CB  . PHE C 1 46 ? 12.911  -27.242 18.638  1.00 30.02  ? 45  PHE C CB  1 
ATOM   1782 C CG  . PHE C 1 46 ? 13.173  -26.275 19.783  1.00 31.52  ? 45  PHE C CG  1 
ATOM   1783 C CD1 . PHE C 1 46 ? 12.130  -25.841 20.597  1.00 34.55  ? 45  PHE C CD1 1 
ATOM   1784 C CD2 . PHE C 1 46 ? 14.460  -25.791 20.042  1.00 31.01  ? 45  PHE C CD2 1 
ATOM   1785 C CE1 . PHE C 1 46 ? 12.384  -24.937 21.614  1.00 33.41  ? 45  PHE C CE1 1 
ATOM   1786 C CE2 . PHE C 1 46 ? 14.710  -24.888 21.069  1.00 33.82  ? 45  PHE C CE2 1 
ATOM   1787 C CZ  . PHE C 1 46 ? 13.668  -24.459 21.850  1.00 33.06  ? 45  PHE C CZ  1 
ATOM   1788 N N   . GLY C 1 47 ? 10.803  -29.520 17.661  1.00 31.19  ? 46  GLY C N   1 
ATOM   1789 C CA  . GLY C 1 47 ? 10.209  -30.196 16.516  1.00 35.11  ? 46  GLY C CA  1 
ATOM   1790 C C   . GLY C 1 47 ? 9.726   -31.590 16.904  1.00 42.66  ? 46  GLY C C   1 
ATOM   1791 O O   . GLY C 1 47 ? 8.519   -31.828 16.994  1.00 41.76  ? 46  GLY C O   1 
ATOM   1792 N N   . THR C 1 48 ? 10.687  -32.486 17.181  1.00 42.42  ? 47  THR C N   1 
ATOM   1793 C CA  . THR C 1 48 ? 10.383  -33.840 17.629  1.00 39.21  ? 47  THR C CA  1 
ATOM   1794 C C   . THR C 1 48 ? 9.884   -33.816 19.075  1.00 39.83  ? 47  THR C C   1 
ATOM   1795 O O   . THR C 1 48 ? 9.118   -34.696 19.460  1.00 44.38  ? 47  THR C O   1 
ATOM   1796 C CB  . THR C 1 48 ? 11.610  -34.743 17.520  1.00 36.54  ? 47  THR C CB  1 
ATOM   1797 O OG1 . THR C 1 48 ? 12.436  -34.192 18.538  1.00 34.65  ? 47  THR C OG1 1 
ATOM   1798 C CG2 . THR C 1 48 ? 12.263  -34.753 16.151  1.00 36.15  ? 47  THR C CG2 1 
ATOM   1799 N N   . HIS C 1 49 ? 10.354  -32.847 19.876  1.00 35.93  ? 48  HIS C N   1 
ATOM   1800 C CA  . HIS C 1 49 ? 10.029  -32.700 21.299  1.00 43.11  ? 48  HIS C CA  1 
ATOM   1801 C C   . HIS C 1 49 ? 10.557  -33.858 22.150  1.00 43.85  ? 48  HIS C C   1 
ATOM   1802 O O   . HIS C 1 49 ? 9.962   -34.197 23.174  1.00 43.75  ? 48  HIS C O   1 
ATOM   1803 C CB  . HIS C 1 49 ? 8.531   -32.447 21.522  1.00 45.21  ? 48  HIS C CB  1 
ATOM   1804 C CG  . HIS C 1 49 ? 8.001   -31.378 20.626  1.00 47.23  ? 48  HIS C CG  1 
ATOM   1805 N ND1 . HIS C 1 49 ? 6.883   -31.558 19.842  1.00 54.96  ? 48  HIS C ND1 1 
ATOM   1806 C CD2 . HIS C 1 49 ? 8.473   -30.155 20.337  1.00 45.57  ? 48  HIS C CD2 1 
ATOM   1807 C CE1 . HIS C 1 49 ? 6.673   -30.457 19.126  1.00 57.18  ? 48  HIS C CE1 1 
ATOM   1808 N NE2 . HIS C 1 49 ? 7.622   -29.590 19.420  1.00 55.15  ? 48  HIS C NE2 1 
ATOM   1809 N N   . GLU C 1 50 ? 11.687  -34.444 21.739  1.00 43.61  ? 49  GLU C N   1 
ATOM   1810 C CA  . GLU C 1 50 ? 12.289  -35.543 22.484  1.00 43.43  ? 49  GLU C CA  1 
ATOM   1811 C C   . GLU C 1 50 ? 13.352  -34.995 23.430  1.00 46.06  ? 49  GLU C C   1 
ATOM   1812 O O   . GLU C 1 50 ? 13.679  -33.807 23.370  1.00 40.73  ? 49  GLU C O   1 
ATOM   1813 C CB  . GLU C 1 50 ? 12.752  -36.587 21.476  1.00 40.57  ? 49  GLU C CB  1 
ATOM   1814 C CG  . GLU C 1 50 ? 11.565  -37.232 20.763  1.00 46.87  ? 49  GLU C CG  1 
ATOM   1815 C CD  . GLU C 1 50 ? 12.001  -38.200 19.689  1.00 47.49  ? 49  GLU C CD  1 
ATOM   1816 O OE1 . GLU C 1 50 ? 13.181  -38.611 19.693  1.00 51.78  ? 49  GLU C OE1 1 
ATOM   1817 O OE2 . GLU C 1 50 ? 11.165  -38.495 18.817  1.00 53.23  ? 49  GLU C OE2 1 
ATOM   1818 N N   . THR C 1 51 ? 13.840  -35.849 24.348  1.00 43.19  ? 50  THR C N   1 
ATOM   1819 C CA  . THR C 1 51 ? 14.878  -35.420 25.278  1.00 48.09  ? 50  THR C CA  1 
ATOM   1820 C C   . THR C 1 51 ? 16.086  -36.361 25.196  1.00 39.59  ? 50  THR C C   1 
ATOM   1821 O O   . THR C 1 51 ? 15.989  -37.481 24.706  1.00 40.47  ? 50  THR C O   1 
ATOM   1822 C CB  . THR C 1 51 ? 14.354  -35.221 26.708  1.00 48.70  ? 50  THR C CB  1 
ATOM   1823 O OG1 . THR C 1 51 ? 13.668  -36.407 27.091  1.00 53.11  ? 50  THR C OG1 1 
ATOM   1824 C CG2 . THR C 1 51 ? 13.460  -34.003 26.887  1.00 41.79  ? 50  THR C CG2 1 
ATOM   1825 N N   . ALA C 1 52 ? 17.245  -35.867 25.621  1.00 41.02  ? 51  ALA C N   1 
ATOM   1826 C CA  . ALA C 1 52 ? 18.437  -36.695 25.719  1.00 40.87  ? 51  ALA C CA  1 
ATOM   1827 C C   . ALA C 1 52 ? 19.422  -36.036 26.670  1.00 40.36  ? 51  ALA C C   1 
ATOM   1828 O O   . ALA C 1 52 ? 19.212  -34.898 27.090  1.00 42.85  ? 51  ALA C O   1 
ATOM   1829 C CB  . ALA C 1 52 ? 19.048  -36.938 24.354  1.00 36.92  ? 51  ALA C CB  1 
ATOM   1830 N N   . PHE C 1 53 ? 20.469  -36.792 27.040  1.00 41.60  ? 52  PHE C N   1 
ATOM   1831 C CA  . PHE C 1 53 ? 21.614  -36.246 27.750  1.00 40.05  ? 52  PHE C CA  1 
ATOM   1832 C C   . PHE C 1 53 ? 22.760  -36.090 26.761  1.00 39.06  ? 52  PHE C C   1 
ATOM   1833 O O   . PHE C 1 53 ? 23.107  -37.042 26.060  1.00 36.58  ? 52  PHE C O   1 
ATOM   1834 C CB  . PHE C 1 53 ? 22.022  -37.221 28.859  1.00 40.01  ? 52  PHE C CB  1 
ATOM   1835 C CG  . PHE C 1 53 ? 21.111  -37.132 30.068  1.00 44.24  ? 52  PHE C CG  1 
ATOM   1836 C CD1 . PHE C 1 53 ? 20.894  -35.912 30.709  1.00 46.25  ? 52  PHE C CD1 1 
ATOM   1837 C CD2 . PHE C 1 53 ? 20.417  -38.251 30.518  1.00 53.34  ? 52  PHE C CD2 1 
ATOM   1838 C CE1 . PHE C 1 53 ? 20.046  -35.826 31.805  1.00 46.72  ? 52  PHE C CE1 1 
ATOM   1839 C CE2 . PHE C 1 53 ? 19.574  -38.160 31.619  1.00 51.91  ? 52  PHE C CE2 1 
ATOM   1840 C CZ  . PHE C 1 53 ? 19.387  -36.951 32.254  1.00 47.45  ? 52  PHE C CZ  1 
ATOM   1841 N N   . LEU C 1 54 ? 23.362  -34.897 26.737  1.00 36.17  ? 53  LEU C N   1 
ATOM   1842 C CA  . LEU C 1 54 ? 24.496  -34.663 25.859  1.00 37.86  ? 53  LEU C CA  1 
ATOM   1843 C C   . LEU C 1 54 ? 25.591  -33.918 26.619  1.00 34.62  ? 53  LEU C C   1 
ATOM   1844 O O   . LEU C 1 54 ? 25.305  -33.132 27.508  1.00 35.30  ? 53  LEU C O   1 
ATOM   1845 C CB  . LEU C 1 54 ? 24.087  -33.933 24.571  1.00 36.46  ? 53  LEU C CB  1 
ATOM   1846 C CG  . LEU C 1 54 ? 23.416  -34.779 23.481  1.00 40.53  ? 53  LEU C CG  1 
ATOM   1847 C CD1 . LEU C 1 54 ? 22.915  -33.900 22.355  1.00 35.56  ? 53  LEU C CD1 1 
ATOM   1848 C CD2 . LEU C 1 54 ? 24.339  -35.841 22.895  1.00 45.31  ? 53  LEU C CD2 1 
ATOM   1849 N N   . GLY C 1 55 ? 26.840  -34.194 26.247  1.00 39.41  ? 54  GLY C N   1 
ATOM   1850 C CA  . GLY C 1 55 ? 28.005  -33.483 26.744  1.00 35.68  ? 54  GLY C CA  1 
ATOM   1851 C C   . GLY C 1 55 ? 28.181  -32.150 26.027  1.00 41.39  ? 54  GLY C C   1 
ATOM   1852 O O   . GLY C 1 55 ? 27.746  -31.968 24.872  1.00 36.89  ? 54  GLY C O   1 
ATOM   1853 N N   . PRO C 1 56 ? 28.872  -31.189 26.678  1.00 39.70  ? 55  PRO C N   1 
ATOM   1854 C CA  . PRO C 1 56 ? 28.957  -29.825 26.152  1.00 42.57  ? 55  PRO C CA  1 
ATOM   1855 C C   . PRO C 1 56 ? 29.701  -29.773 24.816  1.00 39.65  ? 55  PRO C C   1 
ATOM   1856 O O   . PRO C 1 56 ? 29.537  -28.824 24.057  1.00 44.77  ? 55  PRO C O   1 
ATOM   1857 C CB  . PRO C 1 56 ? 29.646  -29.042 27.294  1.00 41.50  ? 55  PRO C CB  1 
ATOM   1858 C CG  . PRO C 1 56 ? 30.462  -30.105 28.014  1.00 44.12  ? 55  PRO C CG  1 
ATOM   1859 C CD  . PRO C 1 56 ? 29.632  -31.378 27.932  1.00 45.08  ? 55  PRO C CD  1 
ATOM   1860 N N   . LYS C 1 57 ? 30.479  -30.819 24.521  1.00 36.19  ? 56  LYS C N   1 
ATOM   1861 C CA  . LYS C 1 57 ? 31.145  -30.993 23.239  1.00 41.76  ? 56  LYS C CA  1 
ATOM   1862 C C   . LYS C 1 57 ? 30.111  -31.002 22.118  1.00 40.96  ? 56  LYS C C   1 
ATOM   1863 O O   . LYS C 1 57 ? 30.390  -30.608 20.991  1.00 39.23  ? 56  LYS C O   1 
ATOM   1864 C CB  . LYS C 1 57 ? 31.769  -32.390 23.106  1.00 43.71  ? 56  LYS C CB  1 
ATOM   1865 N N   . ASP C 1 58 ? 28.914  -31.492 22.443  1.00 41.18  ? 57  ASP C N   1 
ATOM   1866 C CA  . ASP C 1 58 ? 27.923  -31.761 21.420  1.00 40.63  ? 57  ASP C CA  1 
ATOM   1867 C C   . ASP C 1 58 ? 26.946  -30.600 21.301  1.00 39.37  ? 57  ASP C C   1 
ATOM   1868 O O   . ASP C 1 58 ? 25.931  -30.746 20.629  1.00 35.99  ? 57  ASP C O   1 
ATOM   1869 C CB  . ASP C 1 58 ? 27.233  -33.081 21.699  1.00 44.68  ? 57  ASP C CB  1 
ATOM   1870 C CG  . ASP C 1 58 ? 28.201  -34.251 21.683  1.00 45.97  ? 57  ASP C CG  1 
ATOM   1871 O OD1 . ASP C 1 58 ? 29.284  -34.086 21.090  1.00 54.90  ? 57  ASP C OD1 1 
ATOM   1872 O OD2 . ASP C 1 58 ? 27.869  -35.295 22.274  1.00 50.18  ? 57  ASP C OD2 1 
ATOM   1873 N N   . LEU C 1 59 ? 27.289  -29.462 21.921  1.00 36.24  ? 58  LEU C N   1 
ATOM   1874 C CA  . LEU C 1 59 ? 26.362  -28.347 22.085  1.00 39.48  ? 58  LEU C CA  1 
ATOM   1875 C C   . LEU C 1 59 ? 26.997  -27.062 21.576  1.00 42.20  ? 58  LEU C C   1 
ATOM   1876 O O   . LEU C 1 59 ? 28.180  -26.823 21.841  1.00 40.10  ? 58  LEU C O   1 
ATOM   1877 C CB  . LEU C 1 59 ? 25.995  -28.187 23.556  1.00 37.42  ? 58  LEU C CB  1 
ATOM   1878 C CG  . LEU C 1 59 ? 25.345  -29.388 24.242  1.00 39.11  ? 58  LEU C CG  1 
ATOM   1879 C CD1 . LEU C 1 59 ? 25.039  -28.931 25.659  1.00 39.07  ? 58  LEU C CD1 1 
ATOM   1880 C CD2 . LEU C 1 59 ? 24.075  -29.874 23.528  1.00 31.19  ? 58  LEU C CD2 1 
ATOM   1881 N N   . PHE C 1 60 ? 26.175  -26.254 20.881  1.00 41.68  ? 59  PHE C N   1 
ATOM   1882 C CA  . PHE C 1 60 ? 26.578  -25.017 20.223  1.00 38.49  ? 59  PHE C CA  1 
ATOM   1883 C C   . PHE C 1 60 ? 25.534  -23.931 20.485  1.00 43.43  ? 59  PHE C C   1 
ATOM   1884 O O   . PHE C 1 60 ? 24.351  -24.140 20.203  1.00 40.55  ? 59  PHE C O   1 
ATOM   1885 C CB  . PHE C 1 60 ? 26.768  -25.259 18.720  1.00 37.73  ? 59  PHE C CB  1 
ATOM   1886 C CG  . PHE C 1 60 ? 27.697  -26.419 18.384  1.00 38.93  ? 59  PHE C CG  1 
ATOM   1887 C CD1 . PHE C 1 60 ? 27.236  -27.736 18.372  1.00 36.09  ? 59  PHE C CD1 1 
ATOM   1888 C CD2 . PHE C 1 60 ? 29.038  -26.188 18.059  1.00 41.91  ? 59  PHE C CD2 1 
ATOM   1889 C CE1 . PHE C 1 60 ? 28.096  -28.790 18.078  1.00 34.64  ? 59  PHE C CE1 1 
ATOM   1890 C CE2 . PHE C 1 60 ? 29.889  -27.246 17.743  1.00 38.95  ? 59  PHE C CE2 1 
ATOM   1891 C CZ  . PHE C 1 60 ? 29.419  -28.543 17.770  1.00 38.02  ? 59  PHE C CZ  1 
ATOM   1892 N N   . PRO C 1 61 ? 25.907  -22.754 21.064  1.00 40.83  ? 60  PRO C N   1 
ATOM   1893 C CA  . PRO C 1 61 ? 24.930  -21.687 21.310  1.00 41.10  ? 60  PRO C CA  1 
ATOM   1894 C C   . PRO C 1 61 ? 24.230  -21.282 20.014  1.00 36.92  ? 60  PRO C C   1 
ATOM   1895 O O   . PRO C 1 61 ? 24.867  -21.167 18.964  1.00 42.06  ? 60  PRO C O   1 
ATOM   1896 C CB  . PRO C 1 61 ? 25.702  -20.513 21.950  1.00 42.49  ? 60  PRO C CB  1 
ATOM   1897 C CG  . PRO C 1 61 ? 27.095  -21.052 22.216  1.00 41.89  ? 60  PRO C CG  1 
ATOM   1898 C CD  . PRO C 1 61 ? 27.265  -22.399 21.518  1.00 44.99  ? 60  PRO C CD  1 
ATOM   1899 N N   . TYR C 1 62 ? 22.904  -21.108 20.114  1.00 40.66  ? 61  TYR C N   1 
ATOM   1900 C CA  . TYR C 1 62 ? 22.024  -20.853 18.985  1.00 40.92  ? 61  TYR C CA  1 
ATOM   1901 C C   . TYR C 1 62 ? 22.501  -19.638 18.198  1.00 49.19  ? 61  TYR C C   1 
ATOM   1902 O O   . TYR C 1 62 ? 22.664  -19.719 16.981  1.00 45.50  ? 61  TYR C O   1 
ATOM   1903 C CB  . TYR C 1 62 ? 20.561  -20.712 19.414  1.00 44.61  ? 61  TYR C CB  1 
ATOM   1904 C CG  . TYR C 1 62 ? 19.597  -20.373 18.285  1.00 46.83  ? 61  TYR C CG  1 
ATOM   1905 C CD1 . TYR C 1 62 ? 19.406  -21.254 17.219  1.00 46.36  ? 61  TYR C CD1 1 
ATOM   1906 C CD2 . TYR C 1 62 ? 18.859  -19.191 18.300  1.00 45.76  ? 61  TYR C CD2 1 
ATOM   1907 C CE1 . TYR C 1 62 ? 18.536  -20.951 16.181  1.00 42.19  ? 61  TYR C CE1 1 
ATOM   1908 C CE2 . TYR C 1 62 ? 17.983  -18.881 17.271  1.00 45.76  ? 61  TYR C CE2 1 
ATOM   1909 C CZ  . TYR C 1 62 ? 17.832  -19.758 16.208  1.00 42.37  ? 61  TYR C CZ  1 
ATOM   1910 O OH  . TYR C 1 62 ? 16.951  -19.456 15.214  1.00 41.46  ? 61  TYR C OH  1 
ATOM   1911 N N   . ASP C 1 63 ? 22.732  -18.527 18.911  1.00 55.87  ? 62  ASP C N   1 
ATOM   1912 C CA  . ASP C 1 63 ? 23.114  -17.273 18.281  1.00 62.79  ? 62  ASP C CA  1 
ATOM   1913 C C   . ASP C 1 63 ? 24.455  -17.387 17.566  1.00 55.27  ? 62  ASP C C   1 
ATOM   1914 O O   . ASP C 1 63 ? 24.605  -16.866 16.468  1.00 61.22  ? 62  ASP C O   1 
ATOM   1915 C CB  . ASP C 1 63 ? 23.041  -16.107 19.250  1.00 70.47  ? 62  ASP C CB  1 
ATOM   1916 C CG  . ASP C 1 63 ? 21.717  -15.365 19.193  1.00 76.81  ? 62  ASP C CG  1 
ATOM   1917 O OD1 . ASP C 1 63 ? 20.915  -15.536 20.133  1.00 76.60  ? 62  ASP C OD1 1 
ATOM   1918 O OD2 . ASP C 1 63 ? 21.499  -14.643 18.190  1.00 84.75  ? 62  ASP C OD2 1 
ATOM   1919 N N   . LYS C 1 64 ? 25.414  -18.081 18.178  1.00 52.22  ? 63  LYS C N   1 
ATOM   1920 C CA  . LYS C 1 64 ? 26.748  -18.162 17.601  1.00 48.57  ? 63  LYS C CA  1 
ATOM   1921 C C   . LYS C 1 64 ? 26.752  -19.006 16.328  1.00 43.94  ? 63  LYS C C   1 
ATOM   1922 O O   . LYS C 1 64 ? 27.568  -18.758 15.448  1.00 42.93  ? 63  LYS C O   1 
ATOM   1923 C CB  . LYS C 1 64 ? 27.823  -18.692 18.560  1.00 45.16  ? 63  LYS C CB  1 
ATOM   1924 N N   . SER C 1 65 ? 25.858  -20.003 16.219  1.00 40.34  ? 64  SER C N   1 
ATOM   1925 C CA  . SER C 1 65 ? 26.111  -21.060 15.242  1.00 39.65  ? 64  SER C CA  1 
ATOM   1926 C C   . SER C 1 65 ? 24.954  -21.240 14.248  1.00 38.19  ? 64  SER C C   1 
ATOM   1927 O O   . SER C 1 65 ? 24.997  -22.133 13.394  1.00 35.01  ? 64  SER C O   1 
ATOM   1928 C CB  . SER C 1 65 ? 26.449  -22.358 15.943  1.00 41.32  ? 64  SER C CB  1 
ATOM   1929 O OG  . SER C 1 65 ? 25.291  -22.830 16.622  1.00 42.14  ? 64  SER C OG  1 
ATOM   1930 N N   . LYS C 1 66 ? 23.909  -20.411 14.376  1.00 35.47  ? 65  LYS C N   1 
ATOM   1931 C CA  . LYS C 1 66 ? 22.718  -20.588 13.551  1.00 37.15  ? 65  LYS C CA  1 
ATOM   1932 C C   . LYS C 1 66 ? 23.048  -20.375 12.076  1.00 38.89  ? 65  LYS C C   1 
ATOM   1933 O O   . LYS C 1 66 ? 22.506  -21.074 11.226  1.00 38.54  ? 65  LYS C O   1 
ATOM   1934 C CB  . LYS C 1 66 ? 21.496  -19.782 14.010  1.00 40.18  ? 65  LYS C CB  1 
ATOM   1935 C CG  . LYS C 1 66 ? 21.667  -18.271 14.071  1.00 42.41  ? 65  LYS C CG  1 
ATOM   1936 C CD  . LYS C 1 66 ? 20.452  -17.514 14.594  1.00 44.53  ? 65  LYS C CD  1 
ATOM   1937 C CE  . LYS C 1 66 ? 20.719  -16.042 14.556  1.00 52.22  ? 65  LYS C CE  1 
ATOM   1938 N NZ  . LYS C 1 66 ? 19.814  -15.283 15.420  1.00 64.43  ? 65  LYS C NZ  1 
ATOM   1939 N N   . ASP C 1 67 ? 23.967  -19.443 11.781  1.00 41.69  ? 66  ASP C N   1 
ATOM   1940 C CA  . ASP C 1 67 ? 24.390  -19.214 10.400  1.00 43.41  ? 66  ASP C CA  1 
ATOM   1941 C C   . ASP C 1 67 ? 24.833  -20.527 9.748   1.00 42.76  ? 66  ASP C C   1 
ATOM   1942 O O   . ASP C 1 67 ? 24.632  -20.728 8.552   1.00 43.47  ? 66  ASP C O   1 
ATOM   1943 C CB  . ASP C 1 67 ? 25.356  -18.038 10.259  1.00 45.77  ? 66  ASP C CB  1 
ATOM   1944 C CG  . ASP C 1 67 ? 26.740  -18.175 10.891  1.00 57.52  ? 66  ASP C CG  1 
ATOM   1945 O OD1 . ASP C 1 67 ? 27.002  -19.193 11.571  1.00 60.40  ? 66  ASP C OD1 1 
ATOM   1946 O OD2 . ASP C 1 67 ? 27.555  -17.237 10.722  1.00 61.36  ? 66  ASP C OD2 1 
ATOM   1947 N N   . LYS C 1 68 ? 25.404  -21.439 10.547  1.00 37.35  ? 67  LYS C N   1 
ATOM   1948 C CA  . LYS C 1 68 ? 25.961  -22.685 10.047  1.00 36.18  ? 67  LYS C CA  1 
ATOM   1949 C C   . LYS C 1 68 ? 24.945  -23.831 10.065  1.00 39.47  ? 67  LYS C C   1 
ATOM   1950 O O   . LYS C 1 68 ? 24.847  -24.587 9.092   1.00 39.07  ? 67  LYS C O   1 
ATOM   1951 C CB  . LYS C 1 68 ? 27.195  -23.020 10.890  1.00 36.89  ? 67  LYS C CB  1 
ATOM   1952 C CG  . LYS C 1 68 ? 27.955  -24.287 10.553  1.00 44.80  ? 67  LYS C CG  1 
ATOM   1953 C CD  . LYS C 1 68 ? 29.234  -24.355 11.386  1.00 53.87  ? 67  LYS C CD  1 
ATOM   1954 C CE  . LYS C 1 68 ? 29.968  -25.659 11.340  1.00 57.71  ? 67  LYS C CE  1 
ATOM   1955 N NZ  . LYS C 1 68 ? 30.320  -26.083 9.982   1.00 67.55  ? 67  LYS C NZ  1 
ATOM   1956 N N   . TYR C 1 69 ? 24.215  -23.998 11.180  1.00 32.29  ? 68  TYR C N   1 
ATOM   1957 C CA  . TYR C 1 69 ? 23.389  -25.190 11.329  1.00 31.74  ? 68  TYR C CA  1 
ATOM   1958 C C   . TYR C 1 69 ? 21.901  -24.877 11.148  1.00 31.82  ? 68  TYR C C   1 
ATOM   1959 O O   . TYR C 1 69 ? 21.109  -25.798 11.038  1.00 32.82  ? 68  TYR C O   1 
ATOM   1960 C CB  . TYR C 1 69 ? 23.593  -25.762 12.739  1.00 33.20  ? 68  TYR C CB  1 
ATOM   1961 C CG  . TYR C 1 69 ? 25.018  -26.173 13.077  1.00 36.26  ? 68  TYR C CG  1 
ATOM   1962 C CD1 . TYR C 1 69 ? 25.779  -26.953 12.207  1.00 38.27  ? 68  TYR C CD1 1 
ATOM   1963 C CD2 . TYR C 1 69 ? 25.603  -25.757 14.266  1.00 38.96  ? 68  TYR C CD2 1 
ATOM   1964 C CE1 . TYR C 1 69 ? 27.076  -27.329 12.529  1.00 38.45  ? 68  TYR C CE1 1 
ATOM   1965 C CE2 . TYR C 1 69 ? 26.903  -26.112 14.589  1.00 40.45  ? 68  TYR C CE2 1 
ATOM   1966 C CZ  . TYR C 1 69 ? 27.636  -26.906 13.725  1.00 43.49  ? 68  TYR C CZ  1 
ATOM   1967 O OH  . TYR C 1 69 ? 28.923  -27.225 14.080  1.00 43.04  ? 68  TYR C OH  1 
ATOM   1968 N N   . GLY C 1 70 ? 21.519  -23.592 11.184  1.00 31.20  ? 69  GLY C N   1 
ATOM   1969 C CA  . GLY C 1 70 ? 20.117  -23.194 11.097  1.00 35.11  ? 69  GLY C CA  1 
ATOM   1970 C C   . GLY C 1 70 ? 19.699  -23.054 9.632   1.00 35.04  ? 69  GLY C C   1 
ATOM   1971 O O   . GLY C 1 70 ? 19.665  -21.962 9.066   1.00 37.53  ? 69  GLY C O   1 
ATOM   1972 N N   . LYS C 1 71 ? 19.469  -24.194 9.005   1.00 37.27  ? 70  LYS C N   1 
ATOM   1973 C CA  . LYS C 1 71 ? 19.163  -24.254 7.586   1.00 38.85  ? 70  LYS C CA  1 
ATOM   1974 C C   . LYS C 1 71 ? 18.317  -25.499 7.414   1.00 38.13  ? 70  LYS C C   1 
ATOM   1975 O O   . LYS C 1 71 ? 18.536  -26.487 8.112   1.00 38.81  ? 70  LYS C O   1 
ATOM   1976 C CB  . LYS C 1 71 ? 20.419  -24.352 6.709   1.00 38.91  ? 70  LYS C CB  1 
ATOM   1977 C CG  . LYS C 1 71 ? 21.418  -25.406 7.188   1.00 44.69  ? 70  LYS C CG  1 
ATOM   1978 C CD  . LYS C 1 71 ? 22.551  -25.858 6.277   1.00 51.54  ? 70  LYS C CD  1 
ATOM   1979 C CE  . LYS C 1 71 ? 23.407  -26.857 7.009   1.00 49.69  ? 70  LYS C CE  1 
ATOM   1980 N N   . PRO C 1 72 ? 17.297  -25.481 6.529   1.00 32.91  ? 71  PRO C N   1 
ATOM   1981 C CA  . PRO C 1 72 ? 16.353  -26.590 6.475   1.00 33.40  ? 71  PRO C CA  1 
ATOM   1982 C C   . PRO C 1 72 ? 17.009  -27.915 6.106   1.00 37.70  ? 71  PRO C C   1 
ATOM   1983 O O   . PRO C 1 72 ? 18.073  -27.964 5.478   1.00 40.81  ? 71  PRO C O   1 
ATOM   1984 C CB  . PRO C 1 72 ? 15.373  -26.099 5.410   1.00 34.51  ? 71  PRO C CB  1 
ATOM   1985 C CG  . PRO C 1 72 ? 15.448  -24.584 5.548   1.00 32.80  ? 71  PRO C CG  1 
ATOM   1986 C CD  . PRO C 1 72 ? 16.962  -24.378 5.610   1.00 33.07  ? 71  PRO C CD  1 
ATOM   1987 N N   . ASN C 1 73 ? 16.380  -28.990 6.552   1.00 34.68  ? 72  ASN C N   1 
ATOM   1988 C CA  . ASN C 1 73 ? 16.648  -30.286 5.958   1.00 41.10  ? 72  ASN C CA  1 
ATOM   1989 C C   . ASN C 1 73 ? 15.423  -31.153 6.186   1.00 38.71  ? 72  ASN C C   1 
ATOM   1990 O O   . ASN C 1 73 ? 14.510  -30.761 6.912   1.00 35.92  ? 72  ASN C O   1 
ATOM   1991 C CB  . ASN C 1 73 ? 17.983  -30.901 6.373   1.00 46.09  ? 72  ASN C CB  1 
ATOM   1992 C CG  . ASN C 1 73 ? 17.921  -31.425 7.787   1.00 43.26  ? 72  ASN C CG  1 
ATOM   1993 O OD1 . ASN C 1 73 ? 17.031  -32.217 8.130   1.00 37.89  ? 72  ASN C OD1 1 
ATOM   1994 N ND2 . ASN C 1 73 ? 18.828  -30.946 8.616   1.00 45.90  ? 72  ASN C ND2 1 
ATOM   1995 N N   . LYS C 1 74 ? 15.414  -32.315 5.534   1.00 41.57  ? 73  LYS C N   1 
ATOM   1996 C CA  . LYS C 1 74 ? 14.167  -33.036 5.367   1.00 39.48  ? 73  LYS C CA  1 
ATOM   1997 C C   . LYS C 1 74 ? 13.988  -34.041 6.498   1.00 40.42  ? 73  LYS C C   1 
ATOM   1998 O O   . LYS C 1 74 ? 13.014  -34.794 6.499   1.00 45.39  ? 73  LYS C O   1 
ATOM   1999 C CB  . LYS C 1 74 ? 14.094  -33.581 3.933   1.00 40.19  ? 73  LYS C CB  1 
ATOM   2000 C CG  . LYS C 1 74 ? 13.442  -32.604 2.939   1.00 43.66  ? 73  LYS C CG  1 
ATOM   2001 N N   . ARG C 1 75 ? 14.899  -34.035 7.485   1.00 37.33  ? 74  ARG C N   1 
ATOM   2002 C CA  . ARG C 1 75 ? 14.777  -34.993 8.581   1.00 35.86  ? 74  ARG C CA  1 
ATOM   2003 C C   . ARG C 1 75 ? 13.510  -34.687 9.372   1.00 36.06  ? 74  ARG C C   1 
ATOM   2004 O O   . ARG C 1 75 ? 13.180  -33.515 9.600   1.00 34.19  ? 74  ARG C O   1 
ATOM   2005 C CB  . ARG C 1 75 ? 15.966  -35.051 9.561   1.00 36.57  ? 74  ARG C CB  1 
ATOM   2006 C CG  . ARG C 1 75 ? 17.308  -35.435 8.945   1.00 43.17  ? 74  ARG C CG  1 
ATOM   2007 C CD  . ARG C 1 75 ? 17.472  -36.882 8.455   1.00 44.09  ? 74  ARG C CD  1 
ATOM   2008 N NE  . ARG C 1 75 ? 17.351  -37.846 9.559   1.00 41.77  ? 74  ARG C NE  1 
ATOM   2009 C CZ  . ARG C 1 75 ? 18.405  -38.324 10.233  1.00 42.08  ? 74  ARG C CZ  1 
ATOM   2010 N NH1 . ARG C 1 75 ? 18.224  -38.961 11.374  1.00 46.37  ? 74  ARG C NH1 1 
ATOM   2011 N NH2 . ARG C 1 75 ? 19.631  -38.079 9.816   1.00 37.41  ? 74  ARG C NH2 1 
ATOM   2012 N N   . LYS C 1 76 ? 12.846  -35.757 9.832   1.00 36.24  ? 75  LYS C N   1 
ATOM   2013 C CA  . LYS C 1 76 ? 11.529  -35.636 10.438  1.00 39.51  ? 75  LYS C CA  1 
ATOM   2014 C C   . LYS C 1 76 ? 11.578  -34.641 11.591  1.00 40.64  ? 75  LYS C C   1 
ATOM   2015 O O   . LYS C 1 76 ? 12.360  -34.787 12.535  1.00 38.37  ? 75  LYS C O   1 
ATOM   2016 C CB  . LYS C 1 76 ? 10.893  -36.981 10.812  1.00 44.45  ? 75  LYS C CB  1 
ATOM   2017 C CG  . LYS C 1 76 ? 9.473   -36.857 11.368  1.00 50.92  ? 75  LYS C CG  1 
ATOM   2018 C CD  . LYS C 1 76 ? 8.727   -38.170 11.580  1.00 56.15  ? 75  LYS C CD  1 
ATOM   2019 C CE  . LYS C 1 76 ? 7.580   -38.013 12.531  1.00 52.78  ? 75  LYS C CE  1 
ATOM   2020 N NZ  . LYS C 1 76 ? 7.009   -39.329 12.829  1.00 65.13  ? 75  LYS C NZ  1 
ATOM   2021 N N   . GLY C 1 77 ? 10.732  -33.611 11.498  1.00 40.70  ? 76  GLY C N   1 
ATOM   2022 C CA  . GLY C 1 77 ? 10.541  -32.735 12.639  1.00 34.96  ? 76  GLY C CA  1 
ATOM   2023 C C   . GLY C 1 77 ? 11.516  -31.559 12.628  1.00 31.25  ? 76  GLY C C   1 
ATOM   2024 O O   . GLY C 1 77 ? 11.342  -30.622 13.400  1.00 34.20  ? 76  GLY C O   1 
ATOM   2025 N N   . PHE C 1 78 ? 12.541  -31.617 11.764  1.00 32.91  ? 77  PHE C N   1 
ATOM   2026 C CA  . PHE C 1 78 ? 13.630  -30.653 11.822  1.00 30.22  ? 77  PHE C CA  1 
ATOM   2027 C C   . PHE C 1 78 ? 13.110  -29.246 11.526  1.00 32.76  ? 77  PHE C C   1 
ATOM   2028 O O   . PHE C 1 78 ? 13.455  -28.291 12.227  1.00 31.22  ? 77  PHE C O   1 
ATOM   2029 C CB  . PHE C 1 78 ? 14.771  -31.015 10.870  1.00 31.21  ? 77  PHE C CB  1 
ATOM   2030 C CG  . PHE C 1 78 ? 16.044  -30.216 11.090  1.00 31.42  ? 77  PHE C CG  1 
ATOM   2031 C CD1 . PHE C 1 78 ? 16.238  -28.983 10.482  1.00 31.96  ? 77  PHE C CD1 1 
ATOM   2032 C CD2 . PHE C 1 78 ? 17.053  -30.711 11.907  1.00 32.63  ? 77  PHE C CD2 1 
ATOM   2033 C CE1 . PHE C 1 78 ? 17.412  -28.263 10.694  1.00 31.72  ? 77  PHE C CE1 1 
ATOM   2034 C CE2 . PHE C 1 78 ? 18.233  -29.995 12.107  1.00 31.37  ? 77  PHE C CE2 1 
ATOM   2035 C CZ  . PHE C 1 78 ? 18.402  -28.768 11.513  1.00 31.12  ? 77  PHE C CZ  1 
ATOM   2036 N N   . ASN C 1 79 ? 12.336  -29.108 10.438  1.00 32.36  ? 78  ASN C N   1 
ATOM   2037 C CA  . ASN C 1 79 ? 11.985  -27.773 9.966   1.00 34.80  ? 78  ASN C CA  1 
ATOM   2038 C C   . ASN C 1 79 ? 11.018  -27.136 10.962  1.00 32.61  ? 78  ASN C C   1 
ATOM   2039 O O   . ASN C 1 79 ? 11.095  -25.935 11.272  1.00 28.77  ? 78  ASN C O   1 
ATOM   2040 C CB  . ASN C 1 79 ? 11.493  -27.807 8.523   1.00 32.82  ? 78  ASN C CB  1 
ATOM   2041 C CG  . ASN C 1 79 ? 12.605  -28.165 7.565   1.00 34.06  ? 78  ASN C CG  1 
ATOM   2042 O OD1 . ASN C 1 79 ? 13.780  -27.945 7.867   1.00 31.83  ? 78  ASN C OD1 1 
ATOM   2043 N ND2 . ASN C 1 79 ? 12.265  -28.632 6.372   1.00 36.43  ? 78  ASN C ND2 1 
ATOM   2044 N N   . GLU C 1 80 ? 10.157  -27.985 11.530  1.00 34.25  ? 79  GLU C N   1 
ATOM   2045 C CA  . GLU C 1 80 ? 9.283   -27.552 12.604  1.00 33.47  ? 79  GLU C CA  1 
ATOM   2046 C C   . GLU C 1 80 ? 10.099  -27.101 13.811  1.00 36.56  ? 79  GLU C C   1 
ATOM   2047 O O   . GLU C 1 80 ? 9.752   -26.092 14.426  1.00 34.23  ? 79  GLU C O   1 
ATOM   2048 C CB  . GLU C 1 80 ? 8.220   -28.601 12.932  1.00 37.58  ? 79  GLU C CB  1 
ATOM   2049 C CG  . GLU C 1 80 ? 7.224   -28.109 13.979  1.00 38.28  ? 79  GLU C CG  1 
ATOM   2050 C CD  . GLU C 1 80 ? 5.962   -28.951 14.142  1.00 48.37  ? 79  GLU C CD  1 
ATOM   2051 O OE1 . GLU C 1 80 ? 5.841   -30.027 13.520  1.00 49.40  ? 79  GLU C OE1 1 
ATOM   2052 O OE2 . GLU C 1 80 ? 5.067   -28.514 14.890  1.00 46.10  ? 79  GLU C OE2 1 
ATOM   2053 N N   . GLY C 1 81 ? 11.204  -27.815 14.110  1.00 31.72  ? 80  GLY C N   1 
ATOM   2054 C CA  . GLY C 1 81 ? 12.094  -27.426 15.199  1.00 29.73  ? 80  GLY C CA  1 
ATOM   2055 C C   . GLY C 1 81 ? 12.704  -26.049 14.948  1.00 29.29  ? 80  GLY C C   1 
ATOM   2056 O O   . GLY C 1 81 ? 12.915  -25.247 15.861  1.00 28.18  ? 80  GLY C O   1 
ATOM   2057 N N   . LEU C 1 82 ? 13.039  -25.799 13.687  1.00 28.15  ? 81  LEU C N   1 
ATOM   2058 C CA  . LEU C 1 82 ? 13.675  -24.548 13.313  1.00 30.59  ? 81  LEU C CA  1 
ATOM   2059 C C   . LEU C 1 82 ? 12.692  -23.392 13.544  1.00 28.14  ? 81  LEU C C   1 
ATOM   2060 O O   . LEU C 1 82 ? 13.089  -22.315 13.994  1.00 29.08  ? 81  LEU C O   1 
ATOM   2061 C CB  . LEU C 1 82 ? 14.090  -24.662 11.844  1.00 31.37  ? 81  LEU C CB  1 
ATOM   2062 C CG  . LEU C 1 82 ? 15.408  -25.373 11.524  1.00 29.54  ? 81  LEU C CG  1 
ATOM   2063 C CD1 . LEU C 1 82 ? 15.584  -25.302 10.010  1.00 31.57  ? 81  LEU C CD1 1 
ATOM   2064 C CD2 . LEU C 1 82 ? 16.629  -24.710 12.152  1.00 28.29  ? 81  LEU C CD2 1 
ATOM   2065 N N   . TRP C 1 83 ? 11.407  -23.626 13.263  1.00 29.80  ? 82  TRP C N   1 
ATOM   2066 C CA  . TRP C 1 83 ? 10.411  -22.590 13.497  1.00 34.62  ? 82  TRP C CA  1 
ATOM   2067 C C   . TRP C 1 83 ? 10.248  -22.321 14.996  1.00 32.79  ? 82  TRP C C   1 
ATOM   2068 O O   . TRP C 1 83 ? 10.167  -21.162 15.416  1.00 33.48  ? 82  TRP C O   1 
ATOM   2069 C CB  . TRP C 1 83 ? 9.069   -22.946 12.849  1.00 38.03  ? 82  TRP C CB  1 
ATOM   2070 C CG  . TRP C 1 83 ? 8.042   -21.856 13.013  1.00 45.27  ? 82  TRP C CG  1 
ATOM   2071 C CD1 . TRP C 1 83 ? 7.775   -20.830 12.151  1.00 40.79  ? 82  TRP C CD1 1 
ATOM   2072 C CD2 . TRP C 1 83 ? 7.152   -21.682 14.138  1.00 43.83  ? 82  TRP C CD2 1 
ATOM   2073 N NE1 . TRP C 1 83 ? 6.783   -20.035 12.658  1.00 43.25  ? 82  TRP C NE1 1 
ATOM   2074 C CE2 . TRP C 1 83 ? 6.378   -20.529 13.869  1.00 42.17  ? 82  TRP C CE2 1 
ATOM   2075 C CE3 . TRP C 1 83 ? 6.941   -22.383 15.336  1.00 44.27  ? 82  TRP C CE3 1 
ATOM   2076 C CZ2 . TRP C 1 83 ? 5.408   -20.065 14.753  1.00 45.87  ? 82  TRP C CZ2 1 
ATOM   2077 C CZ3 . TRP C 1 83 ? 5.980   -21.923 16.209  1.00 46.58  ? 82  TRP C CZ3 1 
ATOM   2078 C CH2 . TRP C 1 83 ? 5.222   -20.784 15.915  1.00 50.08  ? 82  TRP C CH2 1 
ATOM   2079 N N   . GLU C 1 84 ? 10.263  -23.390 15.796  1.00 35.64  ? 83  GLU C N   1 
ATOM   2080 C CA  . GLU C 1 84 ? 10.044  -23.259 17.230  1.00 36.91  ? 83  GLU C CA  1 
ATOM   2081 C C   . GLU C 1 84 ? 11.171  -22.465 17.879  1.00 33.86  ? 83  GLU C C   1 
ATOM   2082 O O   . GLU C 1 84 ? 10.929  -21.637 18.762  1.00 33.89  ? 83  GLU C O   1 
ATOM   2083 C CB  . GLU C 1 84 ? 9.907   -24.617 17.924  1.00 32.87  ? 83  GLU C CB  1 
ATOM   2084 C CG  . GLU C 1 84 ? 8.612   -25.315 17.525  1.00 38.91  ? 83  GLU C CG  1 
ATOM   2085 C CD  . GLU C 1 84 ? 8.500   -26.738 18.027  1.00 41.85  ? 83  GLU C CD  1 
ATOM   2086 O OE1 . GLU C 1 84 ? 9.466   -27.115 18.716  1.00 37.49  ? 83  GLU C OE1 1 
ATOM   2087 O OE2 . GLU C 1 84 ? 7.486   -27.449 17.755  1.00 42.03  ? 83  GLU C OE2 1 
ATOM   2088 N N   . ILE C 1 85 ? 12.409  -22.734 17.440  1.00 32.69  ? 84  ILE C N   1 
ATOM   2089 C CA  . ILE C 1 85 ? 13.564  -22.175 18.113  1.00 32.04  ? 84  ILE C CA  1 
ATOM   2090 C C   . ILE C 1 85 ? 13.656  -20.674 17.870  1.00 34.11  ? 84  ILE C C   1 
ATOM   2091 O O   . ILE C 1 85 ? 14.149  -19.947 18.730  1.00 35.76  ? 84  ILE C O   1 
ATOM   2092 C CB  . ILE C 1 85 ? 14.872  -22.937 17.830  1.00 30.32  ? 84  ILE C CB  1 
ATOM   2093 C CG1 . ILE C 1 85 ? 15.982  -22.432 18.757  1.00 31.29  ? 84  ILE C CG1 1 
ATOM   2094 C CG2 . ILE C 1 85 ? 15.284  -22.922 16.353  1.00 32.90  ? 84  ILE C CG2 1 
ATOM   2095 C CD1 . ILE C 1 85 ? 17.229  -23.290 18.800  1.00 31.24  ? 84  ILE C CD1 1 
ATOM   2096 N N   . GLN C 1 86 ? 13.202  -20.246 16.688  1.00 33.53  ? 85  GLN C N   1 
ATOM   2097 C CA  . GLN C 1 86 ? 13.211  -18.847 16.294  1.00 34.54  ? 85  GLN C CA  1 
ATOM   2098 C C   . GLN C 1 86 ? 11.988  -18.114 16.835  1.00 32.77  ? 85  GLN C C   1 
ATOM   2099 O O   . GLN C 1 86 ? 12.115  -16.955 17.209  1.00 39.27  ? 85  GLN C O   1 
ATOM   2100 C CB  . GLN C 1 86 ? 13.169  -18.746 14.766  1.00 33.56  ? 85  GLN C CB  1 
ATOM   2101 C CG  . GLN C 1 86 ? 13.507  -17.356 14.231  1.00 39.39  ? 85  GLN C CG  1 
ATOM   2102 C CD  . GLN C 1 86 ? 14.035  -17.376 12.804  1.00 39.40  ? 85  GLN C CD  1 
ATOM   2103 O OE1 . GLN C 1 86 ? 13.893  -18.363 12.078  1.00 40.18  ? 85  GLN C OE1 1 
ATOM   2104 N NE2 . GLN C 1 86 ? 14.659  -16.283 12.392  1.00 41.04  ? 85  GLN C NE2 1 
ATOM   2105 N N   . ASN C 1 87 ? 10.837  -18.802 16.891  1.00 36.01  ? 86  ASN C N   1 
ATOM   2106 C CA  . ASN C 1 87 ? 9.522   -18.175 17.007  1.00 41.82  ? 86  ASN C CA  1 
ATOM   2107 C C   . ASN C 1 87 ? 8.801   -18.502 18.324  1.00 44.65  ? 86  ASN C C   1 
ATOM   2108 O O   . ASN C 1 87 ? 7.985   -17.703 18.766  1.00 44.39  ? 86  ASN C O   1 
ATOM   2109 C CB  . ASN C 1 87 ? 8.632   -18.460 15.801  1.00 40.34  ? 86  ASN C CB  1 
ATOM   2110 C CG  . ASN C 1 87 ? 9.217   -17.818 14.564  1.00 42.87  ? 86  ASN C CG  1 
ATOM   2111 O OD1 . ASN C 1 87 ? 9.231   -16.582 14.456  1.00 42.47  ? 86  ASN C OD1 1 
ATOM   2112 N ND2 . ASN C 1 87 ? 9.783   -18.626 13.679  1.00 40.45  ? 86  ASN C ND2 1 
ATOM   2113 N N   . ASN C 1 88 ? 9.060   -19.660 18.947  1.00 43.74  ? 87  ASN C N   1 
ATOM   2114 C CA  . ASN C 1 88 ? 8.328   -20.022 20.167  1.00 41.22  ? 87  ASN C CA  1 
ATOM   2115 C C   . ASN C 1 88 ? 9.204   -20.894 21.066  1.00 42.53  ? 87  ASN C C   1 
ATOM   2116 O O   . ASN C 1 88 ? 8.821   -22.029 21.382  1.00 46.89  ? 87  ASN C O   1 
ATOM   2117 C CB  . ASN C 1 88 ? 7.045   -20.783 19.823  1.00 40.46  ? 87  ASN C CB  1 
ATOM   2118 C CG  . ASN C 1 88 ? 5.995   -20.778 20.915  1.00 51.41  ? 87  ASN C CG  1 
ATOM   2119 O OD1 . ASN C 1 88 ? 6.079   -19.997 21.868  1.00 46.87  ? 87  ASN C OD1 1 
ATOM   2120 N ND2 . ASN C 1 88 ? 4.994   -21.644 20.793  1.00 50.64  ? 87  ASN C ND2 1 
ATOM   2121 N N   . PRO C 1 89 ? 10.407  -20.416 21.474  1.00 38.50  ? 88  PRO C N   1 
ATOM   2122 C CA  . PRO C 1 89 ? 11.423  -21.279 22.089  1.00 40.95  ? 88  PRO C CA  1 
ATOM   2123 C C   . PRO C 1 89 ? 11.228  -21.768 23.523  1.00 47.70  ? 88  PRO C C   1 
ATOM   2124 O O   . PRO C 1 89 ? 12.043  -22.564 24.002  1.00 45.78  ? 88  PRO C O   1 
ATOM   2125 C CB  . PRO C 1 89 ? 12.745  -20.488 21.969  1.00 33.98  ? 88  PRO C CB  1 
ATOM   2126 C CG  . PRO C 1 89 ? 12.328  -19.049 21.768  1.00 38.95  ? 88  PRO C CG  1 
ATOM   2127 C CD  . PRO C 1 89 ? 10.881  -19.038 21.291  1.00 37.57  ? 88  PRO C CD  1 
ATOM   2128 N N   . HIS C 1 90 ? 10.168  -21.277 24.184  1.00 52.05  ? 89  HIS C N   1 
ATOM   2129 C CA  . HIS C 1 90 ? 9.954   -21.523 25.602  1.00 46.36  ? 89  HIS C CA  1 
ATOM   2130 C C   . HIS C 1 90 ? 8.522   -21.973 25.888  1.00 54.20  ? 89  HIS C C   1 
ATOM   2131 O O   . HIS C 1 90 ? 8.109   -21.978 27.042  1.00 58.81  ? 89  HIS C O   1 
ATOM   2132 C CB  . HIS C 1 90 ? 10.337  -20.294 26.434  1.00 46.22  ? 89  HIS C CB  1 
ATOM   2133 C CG  . HIS C 1 90 ? 11.762  -19.873 26.289  1.00 46.38  ? 89  HIS C CG  1 
ATOM   2134 N ND1 . HIS C 1 90 ? 12.837  -20.715 26.477  1.00 47.07  ? 89  HIS C ND1 1 
ATOM   2135 C CD2 . HIS C 1 90 ? 12.285  -18.671 25.997  1.00 47.37  ? 89  HIS C CD2 1 
ATOM   2136 C CE1 . HIS C 1 90 ? 13.966  -20.037 26.294  1.00 44.26  ? 89  HIS C CE1 1 
ATOM   2137 N NE2 . HIS C 1 90 ? 13.652  -18.795 25.991  1.00 44.74  ? 89  HIS C NE2 1 
ATOM   2138 N N   . ALA C 1 91 ? 7.773   -22.366 24.848  1.00 55.53  ? 90  ALA C N   1 
ATOM   2139 C CA  . ALA C 1 91 ? 6.485   -23.019 25.052  1.00 57.64  ? 90  ALA C CA  1 
ATOM   2140 C C   . ALA C 1 91 ? 6.702   -24.430 25.605  1.00 61.09  ? 90  ALA C C   1 
ATOM   2141 O O   . ALA C 1 91 ? 7.830   -24.915 25.629  1.00 62.96  ? 90  ALA C O   1 
ATOM   2142 C CB  . ALA C 1 91 ? 5.665   -23.007 23.777  1.00 56.42  ? 90  ALA C CB  1 
ATOM   2143 N N   . SER C 1 92 ? 5.614   -25.087 26.036  1.00 69.52  ? 91  SER C N   1 
ATOM   2144 C CA  . SER C 1 92 ? 5.673   -26.300 26.843  1.00 71.10  ? 91  SER C CA  1 
ATOM   2145 C C   . SER C 1 92 ? 5.937   -27.554 26.006  1.00 75.05  ? 91  SER C C   1 
ATOM   2146 O O   . SER C 1 92 ? 6.783   -28.370 26.372  1.00 69.78  ? 91  SER C O   1 
ATOM   2147 C CB  . SER C 1 92 ? 4.429   -26.449 27.681  1.00 73.55  ? 91  SER C CB  1 
ATOM   2148 O OG  . SER C 1 92 ? 4.365   -25.423 28.662  1.00 75.97  ? 91  SER C OG  1 
ATOM   2149 N N   . TYR C 1 93 ? 5.183   -27.713 24.908  1.00 76.25  ? 92  TYR C N   1 
ATOM   2150 C CA  . TYR C 1 93 ? 5.288   -28.854 24.008  1.00 78.08  ? 92  TYR C CA  1 
ATOM   2151 C C   . TYR C 1 93 ? 5.139   -30.160 24.808  1.00 87.66  ? 92  TYR C C   1 
ATOM   2152 O O   . TYR C 1 93 ? 4.744   -31.195 24.217  1.00 90.65  ? 92  TYR C O   1 
ATOM   2153 C CB  . TYR C 1 93 ? 6.580   -28.811 23.180  1.00 78.39  ? 92  TYR C CB  1 
ATOM   2154 C CG  . TYR C 1 93 ? 6.785   -27.542 22.356  1.00 72.17  ? 92  TYR C CG  1 
ATOM   2155 C CD1 . TYR C 1 93 ? 6.160   -27.381 21.122  1.00 63.67  ? 92  TYR C CD1 1 
ATOM   2156 C CD2 . TYR C 1 93 ? 7.610   -26.510 22.802  1.00 65.85  ? 92  TYR C CD2 1 
ATOM   2157 C CE1 . TYR C 1 93 ? 6.333   -26.232 20.369  1.00 57.38  ? 92  TYR C CE1 1 
ATOM   2158 C CE2 . TYR C 1 93 ? 7.803   -25.361 22.047  1.00 55.82  ? 92  TYR C CE2 1 
ATOM   2159 C CZ  . TYR C 1 93 ? 7.160   -25.220 20.829  1.00 55.08  ? 92  TYR C CZ  1 
ATOM   2160 O OH  . TYR C 1 93 ? 7.319   -24.083 20.077  1.00 49.25  ? 92  TYR C OH  1 
HETATM 2161 S S   . SO4 D 2 .  ? 0.893   -33.352 1.758   1.00 83.02  ? 101 SO4 A S   1 
HETATM 2162 O O1  . SO4 D 2 .  ? 1.243   -34.095 0.571   1.00 70.32  ? 101 SO4 A O1  1 
HETATM 2163 O O2  . SO4 D 2 .  ? 1.101   -31.944 1.527   1.00 78.90  ? 101 SO4 A O2  1 
HETATM 2164 O O3  . SO4 D 2 .  ? -0.493  -33.591 2.083   1.00 86.51  ? 101 SO4 A O3  1 
HETATM 2165 O O4  . SO4 D 2 .  ? 1.712   -33.776 2.857   1.00 74.76  ? 101 SO4 A O4  1 
HETATM 2166 S S   . SO4 E 2 .  ? -10.160 -24.502 1.218   1.00 110.23 ? 102 SO4 A S   1 
HETATM 2167 O O1  . SO4 E 2 .  ? -10.090 -24.460 -0.219  1.00 108.90 ? 102 SO4 A O1  1 
HETATM 2168 O O2  . SO4 E 2 .  ? -10.111 -23.164 1.744   1.00 109.54 ? 102 SO4 A O2  1 
HETATM 2169 O O3  . SO4 E 2 .  ? -11.395 -25.129 1.611   1.00 117.10 ? 102 SO4 A O3  1 
HETATM 2170 O O4  . SO4 E 2 .  ? -9.049  -25.257 1.736   1.00 106.64 ? 102 SO4 A O4  1 
HETATM 2171 C C1  . EDO F 3 .  ? 13.687  -19.397 -7.410  1.00 43.44  ? 103 EDO A C1  1 
HETATM 2172 O O1  . EDO F 3 .  ? 14.903  -18.658 -7.319  1.00 33.43  ? 103 EDO A O1  1 
HETATM 2173 C C2  . EDO F 3 .  ? 12.795  -18.980 -8.540  1.00 40.24  ? 103 EDO A C2  1 
HETATM 2174 O O2  . EDO F 3 .  ? 12.190  -17.710 -8.364  1.00 35.94  ? 103 EDO A O2  1 
HETATM 2175 S S   . SO4 G 2 .  ? 8.657   -29.353 5.600   1.00 62.96  ? 104 SO4 A S   1 
HETATM 2176 O O1  . SO4 G 2 .  ? 9.538   -28.792 4.626   1.00 60.15  ? 104 SO4 A O1  1 
HETATM 2177 O O2  . SO4 G 2 .  ? 8.064   -30.560 5.074   1.00 73.93  ? 104 SO4 A O2  1 
HETATM 2178 O O3  . SO4 G 2 .  ? 9.409   -29.655 6.794   1.00 64.27  ? 104 SO4 A O3  1 
HETATM 2179 O O4  . SO4 G 2 .  ? 7.598   -28.424 5.900   1.00 74.92  ? 104 SO4 A O4  1 
HETATM 2180 S S   . SO4 H 2 .  ? 7.176   -8.293  -24.741 1.00 69.56  ? 101 SO4 B S   1 
HETATM 2181 O O1  . SO4 H 2 .  ? 8.254   -8.477  -25.679 1.00 44.82  ? 101 SO4 B O1  1 
HETATM 2182 O O2  . SO4 H 2 .  ? 5.917   -8.600  -25.368 1.00 53.59  ? 101 SO4 B O2  1 
HETATM 2183 O O3  . SO4 H 2 .  ? 7.338   -9.159  -23.576 1.00 49.43  ? 101 SO4 B O3  1 
HETATM 2184 O O4  . SO4 H 2 .  ? 7.198   -6.908  -24.336 1.00 59.52  ? 101 SO4 B O4  1 
HETATM 2185 S S   . SO4 I 2 .  ? 14.047  -26.923 -26.339 1.00 64.86  ? 102 SO4 B S   1 
HETATM 2186 O O1  . SO4 I 2 .  ? 15.467  -26.838 -26.148 1.00 59.58  ? 102 SO4 B O1  1 
HETATM 2187 O O2  . SO4 I 2 .  ? 13.698  -28.244 -26.807 1.00 69.01  ? 102 SO4 B O2  1 
HETATM 2188 O O3  . SO4 I 2 .  ? 13.392  -26.671 -25.078 1.00 66.63  ? 102 SO4 B O3  1 
HETATM 2189 O O4  . SO4 I 2 .  ? 13.621  -25.948 -27.308 1.00 59.23  ? 102 SO4 B O4  1 
HETATM 2190 N N1  . VVJ J 4 .  ? 18.299  -15.312 -23.617 0.75 45.41  ? 103 VVJ B N1  1 
HETATM 2191 C C4  . VVJ J 4 .  ? 20.391  -17.729 -21.628 0.75 51.27  ? 103 VVJ B C4  1 
HETATM 2192 C C5  . VVJ J 4 .  ? 21.070  -16.530 -20.981 0.75 51.74  ? 103 VVJ B C5  1 
HETATM 2193 C C6  . VVJ J 4 .  ? 20.358  -15.968 -19.766 0.75 51.41  ? 103 VVJ B C6  1 
HETATM 2194 C C7  . VVJ J 4 .  ? 18.838  -15.947 -19.826 0.75 50.19  ? 103 VVJ B C7  1 
HETATM 2195 C C8  . VVJ J 4 .  ? 18.253  -15.404 -21.126 0.75 53.29  ? 103 VVJ B C8  1 
HETATM 2196 C C1  . VVJ J 4 .  ? 19.564  -14.926 -24.257 0.75 45.16  ? 103 VVJ B C1  1 
HETATM 2197 C C2  . VVJ J 4 .  ? 18.304  -16.230 -22.436 0.75 51.78  ? 103 VVJ B C2  1 
HETATM 2198 C C3  . VVJ J 4 .  ? 19.331  -17.390 -22.668 0.75 51.38  ? 103 VVJ B C3  1 
HETATM 2199 S S1  . VVJ J 4 .  ? 16.904  -14.884 -24.319 0.75 47.14  ? 103 VVJ B S1  1 
HETATM 2200 O O1  . VVJ J 4 .  ? 15.915  -14.844 -23.290 0.75 48.90  ? 103 VVJ B O1  1 
HETATM 2201 O O2  . VVJ J 4 .  ? 17.153  -13.701 -25.085 0.75 40.78  ? 103 VVJ B O2  1 
HETATM 2202 C C9  . VVJ J 4 .  ? 16.509  -16.186 -25.424 0.75 44.15  ? 103 VVJ B C9  1 
HETATM 2203 C C1  . EDO K 3 .  ? 16.313  -36.060 16.604  1.00 47.78  ? 101 EDO C C1  1 
HETATM 2204 O O1  . EDO K 3 .  ? 15.349  -36.676 15.764  1.00 50.85  ? 101 EDO C O1  1 
HETATM 2205 C C2  . EDO K 3 .  ? 15.766  -35.111 17.594  1.00 40.16  ? 101 EDO C C2  1 
HETATM 2206 O O2  . EDO K 3 .  ? 14.870  -35.741 18.465  1.00 36.82  ? 101 EDO C O2  1 
HETATM 2207 S S   . SO4 L 2 .  ? 28.649  -38.061 12.263  1.00 92.36  ? 102 SO4 C S   1 
HETATM 2208 O O1  . SO4 L 2 .  ? 29.956  -37.487 12.060  1.00 95.56  ? 102 SO4 C O1  1 
HETATM 2209 O O2  . SO4 L 2 .  ? 27.685  -37.357 11.463  1.00 92.68  ? 102 SO4 C O2  1 
HETATM 2210 O O3  . SO4 L 2 .  ? 28.661  -39.446 11.882  1.00 91.12  ? 102 SO4 C O3  1 
HETATM 2211 O O4  . SO4 L 2 .  ? 28.290  -37.950 13.653  1.00 103.62 ? 102 SO4 C O4  1 
HETATM 2212 O O   . HOH M 5 .  ? 8.387   -31.883 3.553   1.00 61.16  ? 201 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 7.697   -9.167  8.839   1.00 50.21  ? 202 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 10.242  -19.008 10.295  1.00 77.83  ? 203 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 0.486   -24.660 13.394  1.00 58.78  ? 204 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 10.748  -29.532 2.895   1.00 49.16  ? 205 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 3.597   -34.052 4.105   1.00 56.35  ? 206 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 10.772  -9.255  -13.109 1.00 50.84  ? 207 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -3.180  -30.540 -3.287  1.00 68.00  ? 208 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 5.351   -28.821 6.664   1.00 50.39  ? 209 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? -4.105  -11.199 6.759   1.00 53.10  ? 210 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 8.683   -17.945 -11.025 1.00 33.36  ? 211 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? -2.006  -9.475  4.612   1.00 66.30  ? 212 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 15.074  -17.041 -18.919 1.00 46.67  ? 213 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? -2.633  3.231   -2.071  1.00 42.16  ? 214 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 8.948   -22.455 -9.533  1.00 37.56  ? 215 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 15.386  -24.116 1.991   1.00 46.75  ? 216 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? -1.243  -20.840 6.727   1.00 41.16  ? 217 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? 6.715   -10.373 -12.068 1.00 43.19  ? 218 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? -0.194  -33.637 4.709   1.00 55.86  ? 219 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 10.465  -5.125  -7.750  1.00 35.84  ? 220 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 4.167   -3.479  -3.202  1.00 39.58  ? 221 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? -8.223  -15.739 -1.065  1.00 34.60  ? 222 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 4.541   -1.305  -6.170  1.00 38.32  ? 223 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 0.583   -10.850 -15.822 1.00 57.01  ? 224 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 16.151  -11.778 -17.015 1.00 47.19  ? 225 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 2.275   -24.995 -10.116 1.00 51.10  ? 226 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? -1.082  -28.958 9.859   1.00 59.19  ? 227 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 19.392  -15.650 7.290   1.00 30.70  ? 228 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 1.506   -4.626  -10.153 1.00 37.67  ? 229 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 2.802   -29.474 -0.358  1.00 42.88  ? 230 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? -3.837  -8.122  -1.343  1.00 22.08  ? 231 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 9.277   -6.156  -1.880  1.00 43.50  ? 232 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -8.903  -20.813 -1.207  1.00 44.25  ? 233 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 12.543  -9.427  -7.149  1.00 45.25  ? 234 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? -4.697  -21.114 6.064   1.00 39.87  ? 235 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 1.521   0.647   -7.472  1.00 42.38  ? 236 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? -6.017  -15.563 -8.148  1.00 30.97  ? 237 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 11.027  -11.890 5.855   1.00 37.33  ? 238 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 4.176   -7.717  1.099   1.00 35.54  ? 239 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 13.563  -15.535 -9.354  1.00 40.28  ? 240 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 16.936  -17.690 -9.771  1.00 48.24  ? 241 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 11.516  -16.290 -14.681 1.00 46.52  ? 242 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? -8.086  -17.282 6.673   1.00 41.12  ? 243 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? -6.413  -11.112 -11.284 1.00 43.22  ? 244 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 10.662  -23.550 9.904   1.00 37.70  ? 245 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 11.108  -12.340 -6.192  1.00 32.76  ? 246 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 8.109   -17.702 -15.722 1.00 47.21  ? 247 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 1.651   -18.493 -18.411 1.00 46.62  ? 248 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 9.566   -13.051 9.720   1.00 43.74  ? 249 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 8.303   -18.007 9.190   1.00 50.13  ? 250 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -2.170  -21.806 -0.688  1.00 32.09  ? 251 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? -5.989  -19.466 -5.764  1.00 37.07  ? 252 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? 12.930  -11.951 -4.256  1.00 24.36  ? 253 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? -0.247  -23.135 9.247   1.00 45.67  ? 254 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 6.176   -16.034 -14.954 1.00 41.77  ? 255 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? -1.315  -20.469 10.667  1.00 69.83  ? 256 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? -4.928  -25.724 -5.601  1.00 56.25  ? 257 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -7.854  -21.306 -5.750  1.00 62.94  ? 258 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 1.407   -10.316 11.632  1.00 36.63  ? 259 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 15.367  -11.851 -5.320  1.00 38.82  ? 260 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? -1.629  -11.601 11.409  1.00 43.75  ? 261 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? -8.367  -16.614 1.784   1.00 50.21  ? 262 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? -6.156  -13.907 -16.744 1.00 52.91  ? 263 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 10.598  -5.954  -3.754  1.00 48.53  ? 264 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 13.088  -11.361 7.969   1.00 58.32  ? 265 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? -1.466  -7.255  11.419  1.00 50.78  ? 266 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 1.749   -24.615 -6.674  1.00 60.17  ? 267 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 4.856   -7.503  4.027   1.00 37.38  ? 268 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? -6.166  -12.649 6.670   1.00 45.19  ? 269 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? 2.111   -6.121  5.380   1.00 35.68  ? 270 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? 7.824   -8.068  4.443   1.00 45.35  ? 271 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? 7.477   -7.721  1.333   1.00 33.65  ? 272 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? -5.994  -16.992 -9.943  1.00 45.19  ? 273 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? 2.863   -10.054 -13.186 1.00 50.81  ? 274 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -9.982  -16.285 9.878   1.00 61.94  ? 275 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 12.444  -13.167 -8.465  1.00 39.37  ? 276 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? -4.037  -26.793 6.855   1.00 56.06  ? 277 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 20.934  -16.494 -3.450  1.00 29.95  ? 278 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 5.973   -5.865  0.501   1.00 55.43  ? 279 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? 13.965  -13.103 10.547  1.00 49.14  ? 280 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? 10.714  -7.795  0.377   1.00 25.71  ? 281 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? 8.423   -16.270 -13.165 1.00 39.59  ? 282 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? -7.625  -11.333 -8.030  1.00 30.09  ? 283 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? 8.651   -27.689 -7.538  1.00 55.06  ? 284 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 13.099  -28.194 -5.057  1.00 53.48  ? 285 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 12.944  -14.936 -12.006 1.00 51.42  ? 286 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? 8.781   -12.727 12.298  1.00 58.22  ? 287 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? -7.152  -19.520 6.866   1.00 56.64  ? 288 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? -3.930  -8.021  10.461  1.00 51.27  ? 289 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? 14.925  -27.924 -1.064  1.00 56.84  ? 290 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? 21.951  -16.594 -0.466  1.00 40.55  ? 291 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? 1.108   -28.726 -7.411  1.00 55.47  ? 292 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? -11.836 -15.956 -4.123  1.00 52.90  ? 293 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? -8.447  -19.556 -3.580  1.00 49.61  ? 294 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? 8.661   -8.992  -13.607 1.00 41.54  ? 295 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? -6.416  -26.130 3.645   1.00 51.20  ? 296 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? 9.700   -20.568 -18.530 1.00 37.75  ? 297 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? -0.917  -3.216  -10.686 1.00 51.03  ? 298 HOH A O   1 
HETATM 2310 O O   . HOH M 5 .  ? -4.028  -11.094 9.851   1.00 47.68  ? 299 HOH A O   1 
HETATM 2311 O O   . HOH M 5 .  ? -7.470  -14.081 -9.273  1.00 55.99  ? 300 HOH A O   1 
HETATM 2312 O O   . HOH M 5 .  ? 6.877   -29.995 -3.263  1.00 46.65  ? 301 HOH A O   1 
HETATM 2313 O O   . HOH M 5 .  ? 4.693   -6.532  -11.096 1.00 48.50  ? 302 HOH A O   1 
HETATM 2314 O O   . HOH M 5 .  ? -11.182 -12.892 -2.467  1.00 61.90  ? 303 HOH A O   1 
HETATM 2315 O O   . HOH M 5 .  ? 10.512  -2.272  -0.784  1.00 54.47  ? 304 HOH A O   1 
HETATM 2316 O O   . HOH M 5 .  ? -6.089  -23.335 -7.321  1.00 49.44  ? 305 HOH A O   1 
HETATM 2317 O O   . HOH M 5 .  ? -10.689 -28.064 -1.723  1.00 59.94  ? 306 HOH A O   1 
HETATM 2318 O O   . HOH M 5 .  ? 4.438   -9.824  -11.363 1.00 51.78  ? 307 HOH A O   1 
HETATM 2319 O O   . HOH M 5 .  ? -6.653  -22.766 5.418   1.00 52.80  ? 308 HOH A O   1 
HETATM 2320 O O   . HOH M 5 .  ? 9.464   -3.590  1.201   1.00 63.96  ? 309 HOH A O   1 
HETATM 2321 O O   . HOH M 5 .  ? 9.172   -31.334 -6.115  1.00 56.62  ? 310 HOH A O   1 
HETATM 2322 O O   . HOH M 5 .  ? 8.591   -22.505 -19.129 1.00 72.07  ? 311 HOH A O   1 
HETATM 2323 O O   . HOH M 5 .  ? 3.999   -3.428  2.508   1.00 63.64  ? 312 HOH A O   1 
HETATM 2324 O O   . HOH N 5 .  ? 30.979  -8.467  -30.021 1.00 58.24  ? 201 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 34.713  -22.899 -30.223 1.00 68.98  ? 202 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 6.105   -7.305  -32.018 1.00 54.66  ? 203 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 24.111  -1.752  -35.842 1.00 64.71  ? 204 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 27.695  -8.011  -28.649 1.00 50.86  ? 205 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 10.064  -11.383 -38.162 1.00 52.13  ? 206 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 6.359   -12.123 -25.865 1.00 41.21  ? 207 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 1.679   -16.123 -32.271 1.00 55.09  ? 208 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 24.552  -5.407  -29.466 1.00 41.78  ? 209 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 12.897  -26.076 -37.050 1.00 54.22  ? 210 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 28.021  -4.665  -36.393 1.00 58.75  ? 211 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 25.946  -4.810  -33.147 1.00 49.52  ? 212 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 30.145  -19.678 -39.960 1.00 42.78  ? 213 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 8.778   -8.894  -16.397 1.00 41.26  ? 214 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 10.098  -19.485 -43.199 1.00 57.51  ? 215 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 17.325  -19.360 -42.086 1.00 60.08  ? 216 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 27.531  -17.828 -24.758 1.00 48.94  ? 217 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 19.630  -25.508 -33.911 1.00 44.09  ? 218 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 22.381  -23.454 -28.635 1.00 44.75  ? 219 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 13.918  -4.185  -41.115 1.00 88.31  ? 220 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 25.443  -6.098  -35.362 1.00 50.14  ? 221 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 20.915  -13.354 -42.355 1.00 40.21  ? 222 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 32.639  -18.085 -41.619 1.00 70.34  ? 223 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 16.585  -19.196 -28.645 1.00 27.52  ? 224 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 25.858  -23.186 -30.948 1.00 38.54  ? 225 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 10.471  -16.700 -44.063 1.00 65.57  ? 226 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 15.486  -26.174 -34.700 1.00 46.50  ? 227 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 18.113  -0.614  -38.219 1.00 30.80  ? 228 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 10.290  -18.809 -32.824 1.00 30.31  ? 229 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 12.643  -22.385 -20.624 1.00 48.62  ? 230 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 21.258  3.546   -32.487 1.00 37.42  ? 231 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 23.933  -11.559 -21.653 1.00 49.69  ? 232 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 25.545  -0.599  -29.021 1.00 62.61  ? 233 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 7.420   -8.299  -20.829 1.00 52.49  ? 234 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 23.671  -4.282  -36.493 1.00 34.32  ? 235 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 7.631   -18.514 -31.552 1.00 43.58  ? 236 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 4.580   -19.044 -25.619 1.00 62.21  ? 237 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 17.833  4.649   -34.384 1.00 50.07  ? 238 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 6.989   -18.996 -34.892 1.00 54.17  ? 239 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 14.398  -6.623  -41.087 1.00 45.24  ? 240 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 19.896  -3.206  -22.758 1.00 56.24  ? 241 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 17.664  -3.125  -22.024 1.00 52.19  ? 242 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 14.461  -24.211 -40.402 1.00 49.56  ? 243 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 10.356  -21.601 -32.673 1.00 41.07  ? 244 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 20.651  -9.785  -42.589 1.00 38.29  ? 245 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 9.458   -0.507  -40.711 1.00 51.95  ? 246 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 1.453   -12.634 -28.248 1.00 53.49  ? 247 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 17.981  -15.529 -45.508 1.00 39.25  ? 248 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 23.587  -2.514  -28.796 1.00 41.55  ? 249 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 17.894  -26.077 -28.905 1.00 39.60  ? 250 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 26.891  -10.250 -28.746 1.00 60.70  ? 251 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 21.315  -6.647  -42.311 1.00 40.02  ? 252 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 17.427  -0.440  -25.274 1.00 55.37  ? 253 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 17.251  -9.654  -43.467 1.00 52.86  ? 254 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 20.572  -25.260 -29.045 1.00 71.07  ? 255 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 31.752  -23.293 -36.918 1.00 56.31  ? 256 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 7.564   -27.260 -38.287 1.00 58.55  ? 257 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 25.143  -6.248  -42.107 1.00 46.02  ? 258 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 6.171   -20.330 -24.951 1.00 42.61  ? 259 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 20.290  -21.561 -22.708 1.00 54.35  ? 260 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 7.229   -22.928 -24.000 1.00 57.74  ? 261 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 28.380  -12.984 -24.226 1.00 51.50  ? 262 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 14.457  -8.096  -42.978 1.00 61.33  ? 263 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 27.855  -24.829 -34.723 1.00 35.74  ? 264 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 7.148   -12.622 -39.386 1.00 70.60  ? 265 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 2.827   -7.737  -27.050 1.00 69.79  ? 266 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 9.651   -6.196  -40.749 1.00 48.80  ? 267 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 16.670  -25.460 -20.775 1.00 83.75  ? 268 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 12.445  -20.255 -19.508 1.00 58.09  ? 269 HOH B O   1 
HETATM 2393 O O   . HOH N 5 .  ? 38.484  -12.811 -38.736 1.00 70.28  ? 270 HOH B O   1 
HETATM 2394 O O   . HOH N 5 .  ? 24.146  -4.276  -27.586 1.00 61.91  ? 271 HOH B O   1 
HETATM 2395 O O   . HOH N 5 .  ? 28.084  -15.347 -22.937 1.00 55.72  ? 272 HOH B O   1 
HETATM 2396 O O   . HOH N 5 .  ? 19.366  4.147   -33.131 1.00 51.35  ? 273 HOH B O   1 
HETATM 2397 O O   . HOH N 5 .  ? 31.378  -12.003 -36.755 1.00 81.81  ? 274 HOH B O   1 
HETATM 2398 O O   . HOH N 5 .  ? 15.454  -21.992 -41.564 1.00 63.61  ? 275 HOH B O   1 
HETATM 2399 O O   . HOH N 5 .  ? 7.409   -21.379 -29.765 1.00 50.17  ? 276 HOH B O   1 
HETATM 2400 O O   . HOH N 5 .  ? 7.364   -9.762  -18.586 1.00 44.59  ? 277 HOH B O   1 
HETATM 2401 O O   . HOH N 5 .  ? 21.985  -29.213 -35.192 1.00 55.54  ? 278 HOH B O   1 
HETATM 2402 O O   . HOH O 5 .  ? 14.911  -17.462 25.290  1.00 70.85  ? 201 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 26.188  -37.328 10.059  1.00 45.19  ? 202 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 29.168  -27.302 30.225  1.00 56.66  ? 203 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 8.305   -36.454 18.429  1.00 50.69  ? 204 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 19.633  -20.641 30.794  1.00 62.89  ? 205 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 11.954  -28.004 27.981  1.00 50.10  ? 206 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 21.793  -28.101 11.077  1.00 30.71  ? 207 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 27.926  -35.728 24.684  1.00 59.32  ? 208 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 7.199   -31.446 12.064  1.00 54.62  ? 209 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 24.855  -20.278 29.308  1.00 66.36  ? 210 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 19.489  -41.325 12.244  1.00 33.99  ? 211 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 5.360   -26.551 16.417  1.00 49.96  ? 212 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 22.639  -41.121 18.502  1.00 45.43  ? 213 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 20.218  -40.817 38.732  1.00 62.37  ? 214 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 26.014  -38.918 12.720  1.00 39.29  ? 215 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 17.063  -16.946 14.700  1.00 49.63  ? 216 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 27.746  -36.932 15.977  1.00 46.11  ? 217 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 22.257  -20.160 23.980  1.00 49.77  ? 218 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 13.674  -36.847 13.529  1.00 42.68  ? 219 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 29.886  -31.031 15.672  1.00 49.76  ? 220 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 21.587  -33.994 16.623  1.00 30.12  ? 221 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 14.511  -20.936 12.121  1.00 37.91  ? 222 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 14.141  -32.201 32.627  1.00 56.93  ? 223 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 12.301  -31.249 8.317   1.00 39.41  ? 224 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 15.939  -37.648 20.009  1.00 53.22  ? 225 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 31.537  -29.368 32.930  1.00 73.01  ? 226 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 15.028  -17.422 19.228  1.00 40.25  ? 227 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 24.680  -30.987 10.829  1.00 37.27  ? 228 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 31.349  -42.787 12.076  1.00 56.43  ? 229 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 2.519   -29.050 13.925  1.00 54.74  ? 230 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 18.735  -19.793 10.538  1.00 40.46  ? 231 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 30.722  -39.539 27.267  1.00 42.51  ? 232 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 33.331  -21.698 29.016  1.00 51.54  ? 233 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 26.362  -34.257 35.041  1.00 86.16  ? 234 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 20.422  -28.545 8.407   1.00 39.21  ? 235 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 18.614  -26.714 3.010   1.00 47.37  ? 236 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 6.544   -17.923 10.806  1.00 40.35  ? 237 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 30.082  -28.976 12.166  1.00 56.13  ? 238 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 25.549  -17.806 13.690  1.00 55.07  ? 239 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 29.419  -39.431 31.377  1.00 43.52  ? 240 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 9.145   -30.204 10.028  1.00 43.08  ? 241 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 31.494  -33.141 25.861  1.00 50.78  ? 242 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 20.460  -39.555 26.268  1.00 46.59  ? 243 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 8.147   -19.019 23.607  1.00 52.32  ? 244 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 24.869  -39.390 20.224  1.00 38.35  ? 245 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 13.910  -29.316 4.081   1.00 46.61  ? 246 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 20.590  -29.055 4.488   1.00 55.85  ? 247 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 30.573  -43.358 15.928  1.00 66.70  ? 248 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 26.958  -37.682 25.052  1.00 46.14  ? 249 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 13.769  -38.550 9.249   1.00 52.00  ? 250 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 25.599  -17.425 21.129  1.00 58.42  ? 251 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 33.113  -24.498 31.552  1.00 49.19  ? 252 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 30.432  -35.176 28.400  1.00 52.61  ? 253 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 21.924  -18.594 21.848  1.00 61.71  ? 254 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 27.509  -15.148 13.000  1.00 55.58  ? 255 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 14.328  -39.481 16.936  1.00 55.84  ? 256 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 17.589  -36.563 29.167  1.00 76.52  ? 257 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 19.809  -12.994 13.279  1.00 43.79  ? 258 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 4.644   -24.116 18.428  1.00 76.39  ? 259 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 29.693  -32.128 18.208  1.00 49.45  ? 260 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 19.176  -18.560 25.038  1.00 47.09  ? 261 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 27.546  -24.334 33.234  1.00 62.57  ? 262 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 15.303  -19.253 29.115  1.00 56.81  ? 263 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 21.754  -13.389 13.170  1.00 47.50  ? 264 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 28.656  -41.063 27.150  1.00 46.10  ? 265 HOH C O   1 
HETATM 2467 O O   . HOH O 5 .  ? 11.542  -21.049 10.728  1.00 35.74  ? 266 HOH C O   1 
HETATM 2468 O O   . HOH O 5 .  ? 29.499  -33.350 14.035  1.00 58.58  ? 267 HOH C O   1 
HETATM 2469 O O   . HOH O 5 .  ? 31.706  -38.778 29.596  1.00 57.09  ? 268 HOH C O   1 
HETATM 2470 O O   . HOH O 5 .  ? 16.620  -16.242 24.293  1.00 57.51  ? 269 HOH C O   1 
HETATM 2471 O O   . HOH O 5 .  ? 10.604  -15.988 24.342  1.00 53.28  ? 270 HOH C O   1 
HETATM 2472 O O   . HOH O 5 .  ? 33.204  -44.125 15.046  1.00 46.80  ? 271 HOH C O   1 
HETATM 2473 O O   . HOH O 5 .  ? 37.011  -24.027 26.758  1.00 56.42  ? 272 HOH C O   1 
HETATM 2474 O O   . HOH O 5 .  ? 15.096  -41.989 8.093   1.00 63.64  ? 273 HOH C O   1 
HETATM 2475 O O   . HOH O 5 .  ? 22.242  -15.082 24.956  1.00 58.15  ? 274 HOH C O   1 
# 
