data_7HHR
# 
_entry.id   7HHR 
# 
_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   7HHR         pdb_00007hhr 10.2210/pdb7hhr/pdb 
WWPDB D_1001407489 ?            ?                   
# 
_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                        7HHR 
_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,N-dimethylmorpholine-4-sulfonamide               194.252   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,N-dimethylmorpholine-4-sulfonamide YEB 
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 
YEB non-polymer         . N,N-dimethylmorpholine-4-sulfonamide ?                 'C6 H14 N2 O3 S' 194.252 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  ?  ?   ?   C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 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        YEB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   YEB 
_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 YEB 1   103 101 YEB LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 340 HOH HOH A . 
M 5 HOH 2   202 278 HOH HOH A . 
M 5 HOH 3   203 292 HOH HOH A . 
M 5 HOH 4   204 202 HOH HOH A . 
M 5 HOH 5   205 333 HOH HOH A . 
M 5 HOH 6   206 27  HOH HOH A . 
M 5 HOH 7   207 91  HOH HOH A . 
M 5 HOH 8   208 307 HOH HOH A . 
M 5 HOH 9   209 339 HOH HOH A . 
M 5 HOH 10  210 304 HOH HOH A . 
M 5 HOH 11  211 208 HOH HOH A . 
M 5 HOH 12  212 84  HOH HOH A . 
M 5 HOH 13  213 23  HOH HOH A . 
M 5 HOH 14  214 85  HOH HOH A . 
M 5 HOH 15  215 42  HOH HOH A . 
M 5 HOH 16  216 35  HOH HOH A . 
M 5 HOH 17  217 28  HOH HOH A . 
M 5 HOH 18  218 32  HOH HOH A . 
M 5 HOH 19  219 337 HOH HOH A . 
M 5 HOH 20  220 351 HOH HOH A . 
M 5 HOH 21  221 297 HOH HOH A . 
M 5 HOH 22  222 97  HOH HOH A . 
M 5 HOH 23  223 55  HOH HOH A . 
M 5 HOH 24  224 260 HOH HOH A . 
M 5 HOH 25  225 2   HOH HOH A . 
M 5 HOH 26  226 12  HOH HOH A . 
M 5 HOH 27  227 20  HOH HOH A . 
M 5 HOH 28  228 37  HOH HOH A . 
M 5 HOH 29  229 86  HOH HOH A . 
M 5 HOH 30  230 87  HOH HOH A . 
M 5 HOH 31  231 139 HOH HOH A . 
M 5 HOH 32  232 60  HOH HOH A . 
M 5 HOH 33  233 190 HOH HOH A . 
M 5 HOH 34  234 93  HOH HOH A . 
M 5 HOH 35  235 1   HOH HOH A . 
M 5 HOH 36  236 327 HOH HOH A . 
M 5 HOH 37  237 41  HOH HOH A . 
M 5 HOH 38  238 165 HOH HOH A . 
M 5 HOH 39  239 78  HOH HOH A . 
M 5 HOH 40  240 8   HOH HOH A . 
M 5 HOH 41  241 188 HOH HOH A . 
M 5 HOH 42  242 34  HOH HOH A . 
M 5 HOH 43  243 58  HOH HOH A . 
M 5 HOH 44  244 274 HOH HOH A . 
M 5 HOH 45  245 301 HOH HOH A . 
M 5 HOH 46  246 66  HOH HOH A . 
M 5 HOH 47  247 289 HOH HOH A . 
M 5 HOH 48  248 300 HOH HOH A . 
M 5 HOH 49  249 218 HOH HOH A . 
M 5 HOH 50  250 38  HOH HOH A . 
M 5 HOH 51  251 26  HOH HOH A . 
M 5 HOH 52  252 203 HOH HOH A . 
M 5 HOH 53  253 164 HOH HOH A . 
M 5 HOH 54  254 267 HOH HOH A . 
M 5 HOH 55  255 18  HOH HOH A . 
M 5 HOH 56  256 199 HOH HOH A . 
M 5 HOH 57  257 288 HOH HOH A . 
M 5 HOH 58  258 167 HOH HOH A . 
M 5 HOH 59  259 364 HOH HOH A . 
M 5 HOH 60  260 7   HOH HOH A . 
M 5 HOH 61  261 290 HOH HOH A . 
M 5 HOH 62  262 222 HOH HOH A . 
M 5 HOH 63  263 99  HOH HOH A . 
M 5 HOH 64  264 75  HOH HOH A . 
M 5 HOH 65  265 111 HOH HOH A . 
M 5 HOH 66  266 109 HOH HOH A . 
M 5 HOH 67  267 341 HOH HOH A . 
M 5 HOH 68  268 293 HOH HOH A . 
M 5 HOH 69  269 145 HOH HOH A . 
M 5 HOH 70  270 152 HOH HOH A . 
M 5 HOH 71  271 115 HOH HOH A . 
M 5 HOH 72  272 95  HOH HOH A . 
M 5 HOH 73  273 47  HOH HOH A . 
M 5 HOH 74  274 22  HOH HOH A . 
M 5 HOH 75  275 77  HOH HOH A . 
M 5 HOH 76  276 299 HOH HOH A . 
M 5 HOH 77  277 9   HOH HOH A . 
M 5 HOH 78  278 281 HOH HOH A . 
M 5 HOH 79  279 94  HOH HOH A . 
M 5 HOH 80  280 156 HOH HOH A . 
M 5 HOH 81  281 19  HOH HOH A . 
M 5 HOH 82  282 71  HOH HOH A . 
M 5 HOH 83  283 116 HOH HOH A . 
M 5 HOH 84  284 113 HOH HOH A . 
M 5 HOH 85  285 143 HOH HOH A . 
M 5 HOH 86  286 349 HOH HOH A . 
M 5 HOH 87  287 179 HOH HOH A . 
M 5 HOH 88  288 64  HOH HOH A . 
M 5 HOH 89  289 73  HOH HOH A . 
M 5 HOH 90  290 348 HOH HOH A . 
M 5 HOH 91  291 318 HOH HOH A . 
M 5 HOH 92  292 16  HOH HOH A . 
M 5 HOH 93  293 31  HOH HOH A . 
M 5 HOH 94  294 63  HOH HOH A . 
M 5 HOH 95  295 210 HOH HOH A . 
M 5 HOH 96  296 361 HOH HOH A . 
M 5 HOH 97  297 83  HOH HOH A . 
M 5 HOH 98  298 358 HOH HOH A . 
M 5 HOH 99  299 132 HOH HOH A . 
M 5 HOH 100 300 211 HOH HOH A . 
M 5 HOH 101 301 108 HOH HOH A . 
M 5 HOH 102 302 205 HOH HOH A . 
M 5 HOH 103 303 185 HOH HOH A . 
M 5 HOH 104 304 21  HOH HOH A . 
M 5 HOH 105 305 259 HOH HOH A . 
M 5 HOH 106 306 283 HOH HOH A . 
M 5 HOH 107 307 219 HOH HOH A . 
M 5 HOH 108 308 57  HOH HOH A . 
M 5 HOH 109 309 356 HOH HOH A . 
M 5 HOH 110 310 206 HOH HOH A . 
M 5 HOH 111 311 332 HOH HOH A . 
M 5 HOH 112 312 125 HOH HOH A . 
M 5 HOH 113 313 362 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 316 HOH HOH B . 
N 5 HOH 3   203 331 HOH HOH B . 
N 5 HOH 4   204 338 HOH HOH B . 
N 5 HOH 5   205 68  HOH HOH B . 
N 5 HOH 6   206 172 HOH HOH B . 
N 5 HOH 7   207 69  HOH HOH B . 
N 5 HOH 8   208 123 HOH HOH B . 
N 5 HOH 9   209 215 HOH HOH B . 
N 5 HOH 10  210 17  HOH HOH B . 
N 5 HOH 11  211 163 HOH HOH B . 
N 5 HOH 12  212 279 HOH HOH B . 
N 5 HOH 13  213 98  HOH HOH B . 
N 5 HOH 14  214 120 HOH HOH B . 
N 5 HOH 15  215 89  HOH HOH B . 
N 5 HOH 16  216 258 HOH HOH B . 
N 5 HOH 17  217 46  HOH HOH B . 
N 5 HOH 18  218 10  HOH HOH B . 
N 5 HOH 19  219 346 HOH HOH B . 
N 5 HOH 20  220 272 HOH HOH B . 
N 5 HOH 21  221 184 HOH HOH B . 
N 5 HOH 22  222 329 HOH HOH B . 
N 5 HOH 23  223 334 HOH HOH B . 
N 5 HOH 24  224 224 HOH HOH B . 
N 5 HOH 25  225 242 HOH HOH B . 
N 5 HOH 26  226 25  HOH HOH B . 
N 5 HOH 27  227 315 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  230 137 HOH HOH B . 
N 5 HOH 31  231 101 HOH HOH B . 
N 5 HOH 32  232 117 HOH HOH B . 
N 5 HOH 33  233 261 HOH HOH B . 
N 5 HOH 34  234 197 HOH HOH B . 
N 5 HOH 35  235 119 HOH HOH B . 
N 5 HOH 36  236 249 HOH HOH B . 
N 5 HOH 37  237 13  HOH HOH B . 
N 5 HOH 38  238 214 HOH HOH B . 
N 5 HOH 39  239 150 HOH HOH B . 
N 5 HOH 40  240 182 HOH HOH B . 
N 5 HOH 41  241 280 HOH HOH B . 
N 5 HOH 42  242 320 HOH HOH B . 
N 5 HOH 43  243 96  HOH HOH B . 
N 5 HOH 44  244 355 HOH HOH B . 
N 5 HOH 45  245 36  HOH HOH B . 
N 5 HOH 46  246 24  HOH HOH B . 
N 5 HOH 47  247 153 HOH HOH B . 
N 5 HOH 48  248 61  HOH HOH B . 
N 5 HOH 49  249 56  HOH HOH B . 
N 5 HOH 50  250 169 HOH HOH B . 
N 5 HOH 51  251 303 HOH HOH B . 
N 5 HOH 52  252 74  HOH HOH B . 
N 5 HOH 53  253 76  HOH HOH B . 
N 5 HOH 54  254 54  HOH HOH B . 
N 5 HOH 55  255 223 HOH HOH B . 
N 5 HOH 56  256 72  HOH HOH B . 
N 5 HOH 57  257 175 HOH HOH B . 
N 5 HOH 58  258 359 HOH HOH B . 
N 5 HOH 59  259 157 HOH HOH B . 
N 5 HOH 60  260 44  HOH HOH B . 
N 5 HOH 61  261 79  HOH HOH B . 
N 5 HOH 62  262 104 HOH HOH B . 
N 5 HOH 63  263 217 HOH HOH B . 
N 5 HOH 64  264 201 HOH HOH B . 
N 5 HOH 65  265 59  HOH HOH B . 
N 5 HOH 66  266 177 HOH HOH B . 
N 5 HOH 67  267 160 HOH HOH B . 
N 5 HOH 68  268 170 HOH HOH B . 
N 5 HOH 69  269 291 HOH HOH B . 
N 5 HOH 70  270 309 HOH HOH B . 
N 5 HOH 71  271 312 HOH HOH B . 
N 5 HOH 72  272 322 HOH HOH B . 
N 5 HOH 73  273 354 HOH HOH B . 
N 5 HOH 74  274 357 HOH HOH B . 
N 5 HOH 75  275 314 HOH HOH B . 
N 5 HOH 76  276 342 HOH HOH B . 
N 5 HOH 77  277 107 HOH HOH B . 
N 5 HOH 78  278 353 HOH HOH B . 
O 5 HOH 1   201 173 HOH HOH C . 
O 5 HOH 2   202 345 HOH HOH C . 
O 5 HOH 3   203 323 HOH HOH C . 
O 5 HOH 4   204 254 HOH HOH C . 
O 5 HOH 5   205 118 HOH HOH C . 
O 5 HOH 6   206 330 HOH HOH C . 
O 5 HOH 7   207 90  HOH HOH C . 
O 5 HOH 8   208 347 HOH HOH C . 
O 5 HOH 9   209 321 HOH HOH C . 
O 5 HOH 10  210 15  HOH HOH C . 
O 5 HOH 11  211 161 HOH HOH C . 
O 5 HOH 12  212 103 HOH HOH C . 
O 5 HOH 13  213 275 HOH HOH C . 
O 5 HOH 14  214 134 HOH HOH C . 
O 5 HOH 15  215 317 HOH HOH C . 
O 5 HOH 16  216 102 HOH HOH C . 
O 5 HOH 17  217 142 HOH HOH C . 
O 5 HOH 18  218 269 HOH HOH C . 
O 5 HOH 19  219 336 HOH HOH C . 
O 5 HOH 20  220 326 HOH HOH C . 
O 5 HOH 21  221 294 HOH HOH C . 
O 5 HOH 22  222 295 HOH HOH C . 
O 5 HOH 23  223 49  HOH HOH C . 
O 5 HOH 24  224 4   HOH HOH C . 
O 5 HOH 25  225 45  HOH HOH C . 
O 5 HOH 26  226 126 HOH HOH C . 
O 5 HOH 27  227 363 HOH HOH C . 
O 5 HOH 28  228 209 HOH HOH C . 
O 5 HOH 29  229 122 HOH HOH C . 
O 5 HOH 30  230 148 HOH HOH C . 
O 5 HOH 31  231 352 HOH HOH C . 
O 5 HOH 32  232 67  HOH HOH C . 
O 5 HOH 33  233 40  HOH HOH C . 
O 5 HOH 34  234 271 HOH HOH C . 
O 5 HOH 35  235 168 HOH HOH C . 
O 5 HOH 36  236 298 HOH HOH C . 
O 5 HOH 37  237 130 HOH HOH C . 
O 5 HOH 38  238 302 HOH HOH C . 
O 5 HOH 39  239 284 HOH HOH C . 
O 5 HOH 40  240 135 HOH HOH C . 
O 5 HOH 41  241 189 HOH HOH C . 
O 5 HOH 42  242 305 HOH HOH C . 
O 5 HOH 43  243 62  HOH HOH C . 
O 5 HOH 44  244 328 HOH HOH C . 
O 5 HOH 45  245 287 HOH HOH C . 
O 5 HOH 46  246 146 HOH HOH C . 
O 5 HOH 47  247 65  HOH HOH C . 
O 5 HOH 48  248 131 HOH HOH C . 
O 5 HOH 49  249 82  HOH HOH C . 
O 5 HOH 50  250 48  HOH HOH C . 
O 5 HOH 51  251 171 HOH HOH C . 
O 5 HOH 52  252 343 HOH HOH C . 
O 5 HOH 53  253 53  HOH HOH C . 
O 5 HOH 54  254 319 HOH HOH C . 
O 5 HOH 55  255 198 HOH HOH C . 
O 5 HOH 56  256 226 HOH HOH C . 
O 5 HOH 57  257 149 HOH HOH C . 
O 5 HOH 58  258 43  HOH HOH C . 
O 5 HOH 59  259 324 HOH HOH C . 
O 5 HOH 60  260 344 HOH HOH C . 
O 5 HOH 61  261 70  HOH HOH C . 
O 5 HOH 62  262 350 HOH HOH C . 
O 5 HOH 63  263 335 HOH HOH C . 
O 5 HOH 64  264 270 HOH HOH C . 
O 5 HOH 65  265 246 HOH HOH C . 
O 5 HOH 66  266 296 HOH HOH C . 
O 5 HOH 67  267 151 HOH HOH C . 
O 5 HOH 68  268 325 HOH HOH C . 
O 5 HOH 69  269 241 HOH HOH C . 
O 5 HOH 70  270 360 HOH HOH C . 
O 5 HOH 71  271 92  HOH HOH C . 
O 5 HOH 72  272 310 HOH HOH C . 
O 5 HOH 73  273 313 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 73 ? CD  ? A LYS 74 CD  
4  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
5  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
6  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
7  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
8  1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
9  1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
10 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
11 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
12 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
13 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
14 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
15 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
16 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
17 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
18 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
19 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
20 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
21 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
22 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
23 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
24 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
25 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
26 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
27 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
28 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
29 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
30 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
31 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
32 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
33 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
34 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
35 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
36 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
37 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
38 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
39 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
40 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
41 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
42 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
43 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
44 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
45 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
46 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
47 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHR 
_cell.length_a           41.410 
_cell.length_b           41.730 
_cell.length_c           156.780 
_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                         7HHR 
_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          7HHR 
_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                     7HHR 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             40.33 
_reflns.d_resolution_high            2.03 
_reflns.number_obs                   18369 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.171 
_reflns.pdbx_netI_over_sigmaI        6.7 
_reflns.pdbx_redundancy              6.4 
_reflns.pdbx_Rrim_I_all              0.186 
_reflns.pdbx_Rpim_I_all              0.073 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     117388 
_reflns.pdbx_chi_squared             0.99 
_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                  2.03 
_reflns_shell.d_res_low                   2.08 
_reflns_shell.number_measured_all         8243 
_reflns_shell.number_unique_obs           1346 
_reflns_shell.Rmerge_I_obs                2.466 
_reflns_shell.pdbx_chi_squared            0.90 
_reflns_shell.pdbx_redundancy             6.1 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             2.696 
_reflns_shell.pdbx_Rpim_I_all             1.078 
_reflns_shell.pdbx_CC_half                0.293 
_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                                 7HHR 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17345 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.36 
_refine.ls_d_res_high                            2.03 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_R_factor_obs                          0.19537 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19067 
_refine.ls_R_factor_R_free                       0.27825 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  970 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.929 
_refine.B_iso_mean                               48.567 
_refine.aniso_B[1][1]                            1.37 
_refine.aniso_B[2][2]                            -0.48 
_refine.aniso_B[3][3]                            -0.89 
_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                       0.224 
_refine.pdbx_overall_ESU_R_Free                  0.216 
_refine.overall_SU_ML                            0.206 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             8.115 
_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        2122 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             264 
_refine_hist.number_atoms_total               2436 
_refine_hist.d_res_high                       2.03 
_refine_hist.d_res_low                        40.36 
# 
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             0.007  0.012  ? 2265 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.757  1.837  ? 3080 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.415  5.000  ? 261  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       7.536  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.251 10.000 ? 308  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.123  0.200  ? 285  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1842 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  4.537  4.606  ? 1057 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.077  8.224  ? 1314 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.494  4.916  ? 1208 '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       11.585 69.77  ? 3604 '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                       2.030 
_refine_ls_shell.d_res_low                        2.083 
_refine_ls_shell.number_reflns_R_work             1270 
_refine_ls_shell.R_factor_R_work                  0.344 
_refine_ls_shell.percent_reflns_obs               99.78 
_refine_ls_shell.R_factor_R_free                  0.420 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             72 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHR 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z57744712' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHR 
_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 7HHR A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHR B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHR 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 7HHR GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHR SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHR GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHR SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHR GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHR SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O 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                   7HHR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 219 ? ? O  A HOH 245 ? ? 1.68 
2  1 OD1 A ASP 27  ? ? O  A HOH 201 ? ? 1.94 
3  1 O   A HOH 227 ? ? O  A HOH 306 ? ? 2.03 
4  1 O   B HOH 231 ? ? O  B HOH 258 ? ? 2.12 
5  1 OE1 A GLU 49  ? ? O  A HOH 202 ? ? 2.13 
6  1 N   B GLY 17  ? ? O1 B SO4 102 ? ? 2.13 
7  1 O   A HOH 256 ? ? O  A HOH 304 ? ? 2.14 
8  1 O   A HOH 201 ? ? O  A HOH 274 ? ? 2.15 
9  1 O   A HOH 228 ? ? O  A HOH 285 ? ? 2.17 
10 1 O   B ASP 27  ? ? O  B HOH 201 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 203 ? ? 1_555 O A HOH 262 ? ? 4_545 1.93 
2 1 O A HOH 272 ? ? 1_555 O A HOH 292 ? ? 4_545 2.07 
# 
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 PRO A 71 ? ? -49.63  153.84 
2 1 ASN A 87 ? ? -151.62 67.96  
3 1 ASN B 38 ? ? 81.66   -5.41  
4 1 ASN B 87 ? ? -157.89 60.37  
5 1 ASN C 87 ? ? -147.32 55.96  
# 
_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            147.79 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     24 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.076 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C HIS 3  ? C HIS 4  
11 1 Y 1 C ASP 27 ? C ASP 28 
12 1 Y 1 C ILE 28 ? C ILE 29 
13 1 Y 1 C ALA 29 ? C ALA 30 
14 1 Y 1 C ASP 30 ? C ASP 31 
15 1 Y 1 C GLY 31 ? C GLY 32 
16 1 Y 1 C ALA 32 ? C ALA 33 
17 1 Y 1 C VAL 33 ? C VAL 34 
18 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
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 
YEB C01  C N N 406 
YEB C03  C N N 407 
YEB C08  C N N 408 
YEB C09  C N N 409 
YEB C11  C N N 410 
YEB C12  C N N 411 
YEB N02  N N N 412 
YEB N07  N N N 413 
YEB O05  O N N 414 
YEB O06  O N N 415 
YEB O10  O N N 416 
YEB S04  S N N 417 
YEB H011 H N N 418 
YEB H012 H N N 419 
YEB H013 H N N 420 
YEB H032 H N N 421 
YEB H033 H N N 422 
YEB H031 H N N 423 
YEB H081 H N N 424 
YEB H082 H N N 425 
YEB H092 H N N 426 
YEB H091 H N N 427 
YEB H111 H N N 428 
YEB H112 H N N 429 
YEB H122 H N N 430 
YEB H121 H N N 431 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
YEB N02 C01  sing N N 389 
YEB C03 N02  sing N N 390 
YEB S04 N02  sing N N 391 
YEB O05 S04  doub N N 392 
YEB O06 S04  doub N N 393 
YEB N07 S04  sing N N 394 
YEB C08 N07  sing N N 395 
YEB C09 C08  sing N N 396 
YEB O10 C09  sing N N 397 
YEB C11 O10  sing N N 398 
YEB C12 C11  sing N N 399 
YEB N07 C12  sing N N 400 
YEB C01 H011 sing N N 401 
YEB C01 H012 sing N N 402 
YEB C01 H013 sing N N 403 
YEB C03 H032 sing N N 404 
YEB C03 H033 sing N N 405 
YEB C03 H031 sing N N 406 
YEB C08 H081 sing N N 407 
YEB C08 H082 sing N N 408 
YEB C09 H092 sing N N 409 
YEB C09 H091 sing N N 410 
YEB C11 H111 sing N N 411 
YEB C11 H112 sing N N 412 
YEB C12 H122 sing N N 413 
YEB C12 H121 sing N N 414 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HHR 
_atom_sites.fract_transf_matrix[1][1]   0.024149 
_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]   0.023964 
_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]   0.006378 
_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  ? -0.313  4.321   2.608   1.00 65.03  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -1.408  3.687   1.826   1.00 69.29  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? -0.824  2.709   0.804   1.00 61.84  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 0.210   2.979   0.200   1.00 66.77  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -2.322  4.737   1.182   1.00 75.03  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -3.222  5.451   2.190   1.00 85.52  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -4.304  4.401   3.188   1.00 78.92  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.676  5.491   4.572   1.00 80.18  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -1.415  1.497   0.663   1.00 70.54  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.953  0.487   -0.298  1.00 57.63  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? -0.611  0.965   -1.713  1.00 58.14  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -1.228  1.897   -2.242  1.00 52.85  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -2.140  -0.511  -0.294  1.00 52.03  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -2.605  -0.465  1.120   1.00 66.12  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -2.516  1.002   1.506   1.00 64.69  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 0.424   0.327   -2.274  1.00 46.00  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 0.732   0.331   -3.693  1.00 51.80  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.196   -0.978  -4.277  1.00 48.48  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? -0.324  -1.821  -3.538  1.00 40.55  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.253   0.425   -3.880  1.00 58.67  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 2.872   1.649   -3.278  1.00 71.78  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.126   1.789   -1.927  1.00 86.34  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 3.261   2.804   -3.846  1.00 75.90  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 3.661   2.983   -1.695  1.00 82.16  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 3.748   3.615   -2.849  1.00 86.77  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.316   -1.135  -5.602  1.00 43.76  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.060   -2.395  -6.274  1.00 40.41  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.168   -3.361  -5.861  1.00 38.42  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.213   -2.928  -5.349  1.00 40.23  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.043   -2.173  -7.765  1.00 41.70  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 0.921   -4.662  -6.019  1.00 31.17  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 1.968   -5.629  -5.714  1.00 34.16  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.112   -5.470  -6.714  1.00 41.37  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 2.868   -5.090  -7.856  1.00 42.25  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.395   -7.044  -5.831  1.00 34.46  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 0.588   -7.448  -4.597  1.00 33.35  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.231   -7.671  -3.367  1.00 34.07  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.796  -7.656  -4.680  1.00 31.35  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 0.495   -8.028  -2.239  1.00 40.97  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -1.519  -8.045  -3.555  1.00 32.58  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.882  -8.225  -2.339  1.00 36.24  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.350   -5.784  -6.296  1.00 37.84  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.489   -5.753  -7.202  1.00 38.88  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.377   -6.969  -6.934  1.00 36.37  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.293   -7.560  -5.864  1.00 37.06  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.241   -4.430  -7.004  1.00 42.19  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 6.860   -4.338  -5.625  1.00 43.49  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.222   -2.929  -5.153  1.00 48.65  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 7.834   -2.964  -3.768  1.00 45.26  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 6.886   -3.301  -2.684  1.00 50.28  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.237   -7.399  -7.887  1.00 36.27  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.168   -8.510  -7.651  1.00 33.77  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 8.946   -8.245  -6.359  1.00 32.53  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.341   -7.104  -6.123  1.00 31.36  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.072   -8.330  -8.908  1.00 32.63  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.106   -7.906  -9.993  1.00 36.71  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.376   -6.813  -9.237  1.00 35.13  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.139   -9.283  -5.520  1.00 32.80  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 9.826   -9.168  -4.226  1.00 25.64  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 8.857   -9.105  -3.029  1.00 35.28  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.241   -9.412  -1.891  1.00 39.16  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 7.616   -8.636  -3.253  1.00 28.61  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 6.632   -8.546  -2.190  1.00 31.14  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 6.397   -9.925  -1.580  1.00 30.17  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.224   -10.911 -2.303  1.00 30.97  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.319   -7.903  -2.633  1.00 31.15  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.368   -6.389  -2.804  1.00 32.91  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.339   -5.795  -2.356  1.00 35.03  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.469   -5.817  -3.439  1.00 32.83  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.329   -9.962  -0.245  1.00 28.29  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.153   -11.245 0.443   1.00 33.42  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 4.696   -11.342 0.870   1.00 31.16  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.105   -10.330 1.259   1.00 32.91  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.122   -11.435 1.614   1.00 27.45  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 8.613   -11.227 1.301   1.00 29.55  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.370   -11.450 2.593   1.00 28.84  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.118   -12.236 0.288   1.00 30.48  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.123   -12.548 0.746   1.00 27.42  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 2.687   -12.719 0.935   1.00 33.14  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.407   -14.089 1.543   1.00 30.39  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.288   -14.944 1.595   1.00 33.65  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 1.920   -12.571 -0.394  1.00 33.54  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.193   -11.214 -1.050  1.00 33.11  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.192   -13.742 -1.360  1.00 29.58  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.169   -14.269 1.987   1.00 29.38  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 0.571   -15.593 2.080   1.00 30.48  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? -0.426  -15.673 0.937   1.00 34.37  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -1.181  -14.737 0.723   1.00 31.45  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? -0.152  -15.907 3.396   1.00 30.38  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 0.823   -16.051 4.551   1.00 28.79  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.242   -14.931 5.257   1.00 33.39  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.279   -17.303 4.951   1.00 32.47  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.188   -15.057 6.260   1.00 32.31  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.201   -17.432 5.984   1.00 33.93  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 2.650   -16.312 6.634   1.00 32.61  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? -0.371  -16.774 0.181   1.00 32.56  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -1.109  -16.873 -1.067  1.00 37.90  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -2.130  -17.989 -0.870  1.00 40.54  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.794  -19.036 -0.309  1.00 39.32  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? -0.153  -17.142 -2.243  1.00 28.56  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -3.381  -17.735 -1.262  1.00 38.09  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -4.417  -18.706 -0.942  1.00 40.52  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.850  -19.435 -2.205  1.00 40.20  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -5.324  -18.801 -3.147  1.00 41.04  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -5.665  -18.102 -0.288  1.00 37.78  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -6.677  -19.168 0.155   1.00 45.53  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -6.140  -20.192 1.152   1.00 44.03  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -7.272  -20.954 1.788   1.00 44.49  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.886  -21.881 0.839   1.00 39.12  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.733  -20.764 -2.183  1.00 40.10  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -5.391  -21.556 -3.210  1.00 49.28  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -6.381  -22.557 -2.637  1.00 49.35  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -6.223  -22.994 -1.509  1.00 49.10  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -4.359  -22.267 -4.067  1.00 42.67  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -3.610  -21.197 -4.814  1.00 53.87  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -2.454  -21.999 -5.914  1.00 53.88  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -3.574  -22.585 -7.194  1.00 67.71  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -7.386  -22.880 -3.462  1.00 61.88  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -8.475  -23.798 -3.169  1.00 61.90  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.903  -25.090 -2.610  1.00 54.97  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -7.083  -25.739 -3.245  1.00 50.24  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -9.321  -24.031 -4.428  1.00 73.73  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -10.832 -23.978 -4.206  1.00 70.64  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -11.547 -22.893 -5.003  1.00 73.53  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -8.294  -25.411 -1.377  1.00 50.22  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.920  -26.694 -0.820  1.00 45.30  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -6.555  -26.660 -0.146  1.00 52.37  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -6.114  -27.681 0.367   1.00 52.32  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.877  -25.504 -0.139  1.00 41.27  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -4.658  -25.420 0.651   1.00 44.30  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -4.812  -24.346 1.712   1.00 38.25  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -5.554  -23.390 1.508   1.00 44.18  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -3.407  -25.083 -0.167  1.00 51.07  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -3.139  -26.116 -1.243  1.00 53.02  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -2.280  -27.185 -1.025  1.00 57.15  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -3.757  -25.997 -2.484  1.00 61.85  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -2.066  -28.129 -2.018  1.00 64.78  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -3.540  -26.921 -3.487  1.00 69.54  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -2.697  -27.993 -3.250  1.00 79.09  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -2.528  -28.883 -4.274  1.00 88.60  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -4.062  -24.419 2.836   1.00 38.42  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.997  -23.284 3.767   1.00 40.31  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -3.222  -22.122 3.121   1.00 38.94  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -2.477  -22.324 2.159   1.00 35.20  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -3.278  -23.886 4.964   1.00 37.51  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -2.404  -24.970 4.361   1.00 42.87  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -3.191  -25.546 3.219   1.00 38.23  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -3.433  -20.910 3.637   1.00 32.48  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -2.696  -19.740 3.207   1.00 37.89  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -1.200  -20.036 3.291   1.00 40.48  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -0.685  -20.433 4.341   1.00 36.66  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -3.110  -18.519 4.026   1.00 40.00  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -4.560  -18.176 3.895   1.00 43.64  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -5.547  -18.905 4.534   1.00 41.59  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -5.180  -17.183 3.237   1.00 39.96  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.734  -18.380 4.243   1.00 39.19  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -6.535  -17.328 3.450   1.00 46.78  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? -0.491  -19.787 2.183   1.00 34.74  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 0.805   -20.417 2.025   1.00 35.88  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 1.886   -19.351 1.877   1.00 31.19  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 1.697   -18.441 1.090   1.00 32.91  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 0.778   -21.377 0.819   1.00 36.61  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 1.864   -22.410 0.923   1.00 36.89  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 3.203   -22.188 0.764   1.00 38.31  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 1.726   -23.812 1.241   1.00 40.43  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 3.908   -23.352 0.951   1.00 45.60  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.034   -24.364 1.248   1.00 42.51  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 0.640   -24.652 1.510   1.00 37.91  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 3.281   -25.709 1.523   1.00 41.54  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 0.889   -25.984 1.773   1.00 43.19  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.190   -26.504 1.797   1.00 38.86  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.048   -19.448 2.578   1.00 34.48  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.128   -18.478 2.417   1.00 35.10  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 4.646   -18.515 0.983   1.00 30.38  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 4.814   -19.590 0.387   1.00 28.53  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.185   -18.889 3.479   1.00 35.83  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 4.890   -20.330 3.733   1.00 31.00  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 3.385   -20.474 3.583   1.00 32.78  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 4.858   -17.313 0.440   1.00 30.80  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.021   -17.113 -0.995  1.00 30.36  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 5.554   -15.699 -1.287  1.00 30.43  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 5.564   -14.849 -0.408  1.00 31.60  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 3.685   -17.398 -1.682  1.00 30.43  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.093   -15.479 -2.495  1.00 30.54  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 6.540   -14.156 -2.936  1.00 32.37  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.036   -13.924 -4.373  1.00 29.26  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 5.734   -14.882 -5.092  1.00 32.35  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.075   -14.046 -2.870  1.00 30.01  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 8.767   -15.092 -3.739  1.00 31.81  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 10.273  -14.831 -3.884  1.00 34.17  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 10.989  -15.779 -4.754  1.00 32.72  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.308  -16.094 -4.763  1.00 36.16  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.096  -15.797 -3.737  1.00 32.69  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 12.816  -16.831 -5.744  1.00 29.03  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 5.875   -12.655 -4.754  1.00 31.91  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 5.696   -12.252 -6.142  1.00 29.59  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.066   -12.400 -6.814  1.00 35.63  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.027   -11.723 -6.427  1.00 35.50  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.184   -10.805 -6.258  1.00 31.81  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.057   -10.437 -5.262  1.00 36.85  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 4.774   -10.484 -7.693  1.00 34.87  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 2.718   -11.112 -5.507  1.00 33.50  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.155   -13.327 -7.773  1.00 32.91  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.370   -13.539 -8.549  1.00 40.62  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 8.574   -12.457 -9.606  1.00 41.18  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 7.631   -11.817 -10.072 1.00 38.99  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 8.455   -14.933 -9.163  1.00 36.39  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 9.434   -15.867 -8.464  1.00 37.40  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.098  -15.420 -7.489  1.00 36.86  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 9.529   -17.043 -8.880  1.00 40.20  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 9.845   -12.229 -9.955  1.00 47.71  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.151  -11.544 -11.200 1.00 51.22  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 9.867   -12.493 -12.351 1.00 43.84  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.031  -13.695 -12.220 1.00 49.50  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 11.616  -11.161 -11.278 1.00 55.75  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 11.990  -9.958  -10.431 1.00 64.36  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 11.661  -8.822  -10.853 1.00 65.90  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 12.583  -10.176 -9.350  1.00 65.72  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 9.464   -11.941 -13.485 1.00 48.35  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 9.465   -12.731 -14.700 1.00 47.56  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 10.843  -12.609 -15.353 1.00 48.27  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.260  -11.509 -15.731 1.00 43.49  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.337   -12.250 -15.625 1.00 42.89  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 6.983   -12.323 -14.885 1.00 47.36  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.345   -13.042 -16.945 1.00 36.13  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 5.972   -11.254 -15.281 1.00 42.58  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 11.523  -13.755 -15.496 1.00 46.58  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 12.812  -13.839 -16.173 1.00 46.17  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 12.674  -13.687 -17.695 1.00 50.28  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 11.663  -14.049 -18.314 1.00 44.24  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 13.551  -15.121 -15.808 1.00 45.43  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 13.740  -13.139 -18.288 1.00 48.81  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 13.940  -13.076 -19.729 1.00 41.35  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 13.674  -14.450 -20.320 1.00 36.42  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.228  -15.422 -19.829 1.00 41.43  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.323  -12.516 -20.014 1.00 37.97  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.317  -10.995 -19.999 1.00 44.12  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.212  -10.403 -19.973 1.00 48.68  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.396  -10.403 -20.011 1.00 42.53  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 12.748  -14.535 -21.289 1.00 36.99  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 12.443  -15.818 -21.906 1.00 39.38  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 11.351  -16.630 -21.201 1.00 42.85  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 10.918  -17.637 -21.736 1.00 45.19  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 10.900  -16.211 -20.011 1.00 47.06  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 9.947   -16.990 -19.219 1.00 43.78  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 8.533   -16.680 -19.679 1.00 46.64  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.284   -15.595 -20.207 1.00 42.14  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 10.078  -16.637 -17.746 1.00 40.03  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 7.614   -17.614 -19.396 1.00 38.89  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 6.196   -17.462 -19.668 1.00 38.30  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 5.642   -16.366 -18.767 1.00 44.18  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 5.883   -16.403 -17.566 1.00 46.71  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 5.477   -18.801 -19.392 1.00 39.78  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 3.958   -18.675 -19.453 1.00 43.42  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 5.973   -19.885 -20.346 1.00 42.37  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 4.942   -15.393 -19.379 1.00 40.21  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 4.299   -14.274 -18.704 1.00 41.21  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 2.976   -14.764 -18.127 1.00 47.98  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 2.338   -15.640 -18.699 1.00 46.41  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.025   -13.084 -19.639 1.00 35.57  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.352   -12.444 -20.072 1.00 42.06  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.297   -11.338 -21.122 1.00 46.68  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 4.750   -11.746 -22.459 1.00 46.65  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 4.819   -10.565 -23.314 1.00 49.68  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 2.531   -14.231 -16.971 1.00 45.26  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.200   -14.553 -16.462 1.00 46.14  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.099   -14.081 -17.402 1.00 50.49  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.328   -13.235 -18.266 1.00 47.93  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.125   -13.808 -15.106 1.00 48.94  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 2.288   -12.840 -15.105 1.00 47.96  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.316   -13.371 -16.075 1.00 43.54  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -1.153  -14.557 -17.228 1.00 46.23  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -2.294  -13.875 -17.829 1.00 45.80  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -2.412  -12.456 -17.279 1.00 46.95  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.935  -12.185 -16.182 1.00 45.66  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -3.495  -14.776 -17.443 1.00 46.35  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.883  -16.127 -17.103 1.00 40.46  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -1.527  -15.789 -16.516 1.00 44.81  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -3.107  -11.538 -17.995 1.00 55.84  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -3.423  -10.203 -17.479 1.00 57.53  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -4.035  -10.232 -16.078 1.00 53.97  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.845  -11.105 -15.751 1.00 45.26  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -4.451  -9.688  -18.522 1.00 62.05  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.978  -10.948 -19.178 1.00 59.90  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.718  -11.785 -19.316 1.00 64.11  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.631  -9.265  -15.251 1.00 49.76  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -4.195  -9.105  -13.919 1.00 53.56  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.786  -10.225 -12.958 1.00 46.28  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -4.297  -10.245 -11.849 1.00 48.41  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.702  -8.858  -13.965 1.00 57.72  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -6.013  -7.562  -14.679 1.00 61.55  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.493  -6.501  -14.317 1.00 67.15  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.827  -7.626  -15.717 1.00 63.28  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.883  -11.130 -13.383 1.00 41.88  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -2.343  -12.221 -12.569 1.00 42.73  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.835  -12.019 -12.347 1.00 45.33  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? -0.166  -11.360 -13.152 1.00 48.07  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -2.512  -13.616 -13.194 1.00 45.51  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.911  -14.169 -13.494 1.00 41.46  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.848  -13.978 -12.306 1.00 50.63  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -6.299  -14.247 -12.563 1.00 53.32  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -6.457  -15.693 -12.747 1.00 61.35  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? -0.309  -12.598 -11.250 1.00 38.59  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.080   -12.463 -10.847 1.00 35.31  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 1.682   -13.853 -10.742 1.00 33.08  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.022   -14.776 -10.298 1.00 36.50  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.227   -11.823 -9.457  1.00 35.66  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 0.812   -10.360 -9.432  1.00 36.73  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.497  -9.988  -9.128  1.00 43.79  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 1.694   -9.365  -9.814  1.00 37.19  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.891  -8.659  -9.161  1.00 43.70  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.320   -8.026  -9.842  1.00 40.27  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.019   -7.680  -9.517  1.00 44.78  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.368  -6.374  -9.507  1.00 50.39  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 2.978   -14.016 -11.087 1.00 33.30  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 3.688   -15.266 -10.831 1.00 31.93  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 3.989   -15.380 -9.336  1.00 31.15  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 4.664   -14.538 -8.735  1.00 34.03  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 4.970   -15.144 -11.677 1.00 32.74  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.155   -13.662 -11.891 1.00 34.17  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 3.832   -12.963 -11.649 1.00 34.34  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 3.457   -16.432 -8.725  1.00 30.97  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 3.599   -16.610 -7.296  1.00 30.27  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 4.456   -17.841 -7.069  1.00 33.72  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.095   -18.940 -7.503  1.00 33.43  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.238   -16.716 -6.576  1.00 32.98  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.270   -15.545 -6.865  1.00 28.63  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 2.477   -16.952 -5.092  1.00 32.05  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 1.817   -14.172 -6.493  1.00 26.82  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 5.593   -17.617 -6.401  1.00 33.02  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 6.491   -18.665 -5.943  1.00 32.50  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.161   -18.996 -4.483  1.00 33.00  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.287   -18.149 -3.599  1.00 26.95  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 7.957   -18.210 -6.086  1.00 31.90  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 8.983   -19.266 -5.676  1.00 32.68  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 9.317   -20.322 -6.530  1.00 37.44  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 9.667   -19.171 -4.459  1.00 39.76  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 10.271  -21.262 -6.162  1.00 37.40  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 10.625  -20.114 -4.094  1.00 38.98  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 10.932  -21.159 -4.957  1.00 37.04  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 5.736   -20.250 -4.260  1.00 31.47  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 5.418   -20.824 -2.965  1.00 30.11  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 6.715   -21.290 -2.315  1.00 36.70  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 7.443   -22.113 -2.911  1.00 34.84  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 4.434   -21.996 -3.187  1.00 33.56  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.087   -21.487 -3.689  1.00 35.44  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 2.866   -21.242 -5.055  1.00 34.91  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.069   -21.192 -2.791  1.00 38.60  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 1.659   -20.713 -5.500  1.00 35.92  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 0.854   -20.663 -3.251  1.00 40.26  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 0.651   -20.426 -4.601  1.00 30.39  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 6.986   -20.762 -1.101  1.00 35.54  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.099   -21.252 -0.300  1.00 35.36  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 7.867   -22.722 0.051   1.00 35.51  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 6.720   -23.191 0.138   1.00 30.46  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 8.450   -20.384 0.913   1.00 35.02  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 8.925   -19.009 0.471   1.00 35.55  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.132  -18.850 -0.215  1.00 30.26  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.136   -17.886 0.708   1.00 31.77  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 10.559  -17.589 -0.606  1.00 33.97  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 8.541   -16.626 0.274   1.00 32.65  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 9.770   -16.459 -0.365  1.00 28.28  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 8.975   -23.455 0.214   1.00 34.41  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 8.865   -24.824 0.682   1.00 36.78  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 8.696   -25.826 -0.463  1.00 43.83  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 9.558   -26.684 -0.612  1.00 42.16  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 7.599   -25.716 -1.246  1.00 40.57  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 7.329   -26.596 -2.385  1.00 39.39  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.043   -26.081 -3.636  1.00 44.70  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 8.179   -26.792 -4.644  1.00 47.22  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 5.819   -26.647 -2.647  1.00 39.08  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 5.434   -25.314 -2.952  1.00 40.13  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.006   -27.015 -1.428  1.00 38.13  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 8.410   -24.794 -3.607  1.00 36.05  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.079   -24.161 -4.725  1.00 35.69  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 8.211   -24.279 -5.977  1.00 39.66  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 8.734   -24.250 -7.094  1.00 43.40  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 10.517  -24.679 -4.892  1.00 35.76  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 11.269  -24.705 -3.596  1.00 40.65  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 11.906  -25.824 -3.110  1.00 40.11  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 11.431  -23.760 -2.659  1.00 40.96  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 12.433  -25.560 -1.922  1.00 43.25  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.163  -24.307 -1.634  1.00 42.36  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 6.881   -24.372 -5.811  1.00 41.07  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.028   -24.372 -6.992  1.00 41.29  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 5.694   -22.931 -7.373  1.00 39.76  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 5.902   -22.028 -6.565  1.00 37.04  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 4.759   -25.163 -6.720  1.00 45.70  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 5.002   -26.664 -6.730  1.00 50.58  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 3.809   -27.311 -6.057  1.00 61.67  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 2.751   -26.639 -5.925  1.00 63.07  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 3.981   -28.462 -5.603  1.00 68.83  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.260   -22.733 -8.628  1.00 37.87  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 4.718   -21.473 -9.126  1.00 40.13  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 3.265   -21.641 -9.559  1.00 39.57  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 2.933   -22.578 -10.268 1.00 44.15  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 5.514   -20.946 -10.321 1.00 39.76  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 6.824   -20.676 -9.837  1.00 37.00  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 4.911   -19.665 -10.894 1.00 35.52  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 2.420   -20.670 -9.200  1.00 38.08  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.105   -20.562 -9.815  1.00 35.72  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 0.838   -19.104 -10.137 1.00 35.51  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 1.570   -18.212 -9.692  1.00 34.73  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.010   -21.168 -8.956  1.00 35.00  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? -0.177  -18.875 -10.971 1.00 33.22  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? -0.548  -17.514 -11.314 1.00 34.54  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.805  -17.176 -10.514 1.00 42.18  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.727  -17.986 -10.507 1.00 45.11  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.731  -17.442 -12.830 1.00 36.20  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 0.528   -17.651 -13.667 1.00 37.47  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 1.605   -16.770 -13.564 1.00 37.14  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.569   -18.643 -14.643 1.00 41.95  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 2.739   -16.944 -14.356 1.00 46.56  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 1.696   -18.814 -15.440 1.00 42.01  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 2.778   -17.958 -15.300 1.00 43.45  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.811  -16.020 -9.827  1.00 37.12  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.910  -15.648 -8.942  1.00 36.55  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -3.183  -14.156 -9.065  1.00 36.88  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -2.252  -13.372 -9.271  1.00 37.81  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -2.658  -15.985 -7.471  1.00 37.00  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -2.364  -17.444 -7.102  1.00 35.03  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -2.058  -17.431 -5.603  1.00 34.44  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.600  -18.253 -7.393  1.00 39.66  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -4.462  -13.784 -8.890  1.00 36.53  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.862  -12.383 -8.755  1.00 31.34  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.762  -11.866 -7.317  1.00 28.51  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.726  -12.627 -6.355  1.00 29.51  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.725  -10.540 -7.095  1.00 34.55  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.758  -9.969  -5.732  1.00 35.40  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.744  -10.459 -4.661  1.00 38.72  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -5.468  -10.370 -3.459  1.00 36.32  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.971  -8.498  -6.058  1.00 39.11  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -4.209  -8.302  -7.332  1.00 36.67  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.591  -9.532  -8.149  1.00 32.40  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.904  -10.988 -5.077  1.00 38.86  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.863  -11.539 -4.115  1.00 37.33  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -7.294  -12.730 -3.342  1.00 37.68  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.766  -13.018 -2.241  1.00 34.23  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -9.179  -12.026 -4.727  1.00 39.31  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -9.089  -13.161 -5.745  1.00 45.02  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -10.438 -13.342 -6.453  1.00 59.70  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -10.583 -14.411 -7.497  1.00 56.78  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -10.156 -15.711 -6.966  1.00 58.86  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -6.273  -13.408 -3.891  1.00 35.28  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.676  -14.556 -3.227  1.00 34.01  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -4.366  -14.241 -2.506  1.00 37.15  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.682  -15.162 -2.013  1.00 36.97  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -5.552  -15.695 -4.224  1.00 44.03  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.924  -16.234 -4.598  1.00 42.40  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.728  -16.411 -3.662  1.00 40.19  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -7.200  -16.380 -5.798  1.00 43.23  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -4.045  -12.944 -2.417  1.00 32.59  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.723  -12.528 -1.962  1.00 30.13  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.824  -11.687 -0.691  1.00 27.45  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -3.423  -10.612 -0.718  1.00 27.55  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -2.043  -11.751 -3.087  1.00 24.42  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.832  -12.490 -4.408  1.00 27.85  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -1.050  -11.656 -5.422  1.00 24.55  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -1.161  -13.835 -4.162  1.00 30.52  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -2.175  -12.163 0.384   1.00 31.19  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -2.242  -11.546 1.702   1.00 38.46  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.863  -11.082 2.154   1.00 34.79  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? -0.017  -11.900 2.515   1.00 31.96  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.772  -12.596 2.679   1.00 33.92  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -4.223  -12.984 2.416   1.00 33.48  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -4.545  -13.955 1.466   1.00 35.70  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -5.258  -12.400 3.143   1.00 32.72  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.877  -14.287 1.241   1.00 38.04  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -6.588  -12.792 2.968   1.00 35.15  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.896  -13.723 1.997   1.00 30.05  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.586  -9.755  2.161   1.00 34.95  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 0.726   -9.237  2.574   1.00 33.20  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.260   -9.832  3.878   1.00 33.65  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 0.552   -9.894  4.892   1.00 36.69  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 0.445   -7.698  2.693   1.00 37.79  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.594  -7.469  1.587   1.00 38.87  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -1.513  -8.688  1.746   1.00 38.40  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 2.514   -10.280 3.809   1.00 33.15  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.189   -11.091 4.818   1.00 33.11  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.106   -10.451 6.212   1.00 33.23  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 2.600   -11.073 7.159   1.00 33.05  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 4.651   -11.314 4.395   1.00 36.12  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.405   -12.090 5.453   1.00 36.77  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.081   -13.429 5.691   1.00 34.52  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.427   -11.509 6.207   1.00 32.12  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 5.735   -14.167 6.661   1.00 30.72  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.097   -12.256 7.178   1.00 34.39  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 6.732   -13.571 7.419   1.00 35.99  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 7.343   -14.340 8.368   1.00 45.50  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 3.571   -9.207  6.313   1.00 30.98  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 3.669   -8.516  7.595   1.00 45.73  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.327   -8.441  8.337   1.00 45.94  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.260   -8.795  9.517   1.00 40.76  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 4.414   -7.201  7.477   1.00 51.05  ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 5.924   -7.351  7.580   1.00 68.75  ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 6.406   -7.885  8.613   1.00 64.57  ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 6.606   -6.931  6.630   1.00 79.17  ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 1.262   -8.016  7.632   1.00 47.21  ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? -0.078  -7.899  8.210   1.00 43.61  ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? -0.670  -9.247  8.627   1.00 44.60  ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -1.434  -9.273  9.587   1.00 46.94  ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? -1.062  -7.138  7.317   1.00 42.48  ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -2.534  -7.520  7.501   1.00 47.19  ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -3.483  -6.671  6.672   1.00 44.29  ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -4.077  -5.618  7.516   1.00 49.19  ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -5.342  -6.120  8.047   1.00 50.43  ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? -0.321  -10.347 7.933   1.00 38.68  ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? -1.054  -11.611 8.017   1.00 40.47  ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? -0.281  -12.709 8.747   1.00 38.16  ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? -0.818  -13.814 8.942   1.00 34.61  ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -1.377  -12.129 6.626   1.00 38.42  ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -2.223  -11.226 5.937   1.00 58.83  ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 0.999   -12.448 9.052   1.00 41.23  ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 1.883   -13.485 9.593   1.00 44.28  ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 1.417   -14.006 10.951  1.00 43.01  ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 1.576   -15.196 11.232  1.00 42.73  ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 3.361   -13.102 9.703   1.00 45.80  ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 3.609   -11.760 10.320  1.00 49.85  ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 5.100   -11.500 10.273  1.00 64.39  ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 5.346   -10.271 11.082  1.00 69.96  ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 6.390   -9.515  10.392  1.00 72.62  ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 0.835   -13.125 11.776  0.50 46.03  ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 0.850   -13.128 11.793  0.50 45.01  ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? 0.341   -13.533 13.086  0.50 46.40  ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 0.345   -13.602 13.076  0.50 44.39  ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? -0.793  -14.551 12.927  0.50 43.35  ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? -0.717  -14.669 12.836  0.50 42.59  ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? -0.918  -15.466 13.730  0.50 38.71  ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? -0.722  -15.701 13.496  0.50 38.77  ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? 0.038   -12.331 13.970  0.50 53.01  ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? -0.266  -12.513 13.939  0.50 48.00  ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 1.242   -11.553 14.495  0.50 55.63  ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? -0.654  -12.990 15.332  0.50 49.85  ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 2.359   -12.123 14.552  0.50 55.72  ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 0.268   -13.282 16.127  0.50 50.59  ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? 1.060   -10.369 14.836  0.50 57.16  ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -1.871  -13.102 15.601  0.50 49.27  ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -1.600  -14.410 11.870  1.00 43.69  ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -2.710  -15.313 11.621  1.00 47.40  ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -2.207  -16.598 10.956  1.00 48.96  ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -2.606  -17.693 11.337  1.00 47.57  ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -3.770  -14.545 10.819  1.00 44.91  ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -5.074  -15.310 10.607  1.00 52.45  ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -6.243  -14.448 10.132  1.00 59.20  ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -7.481  -15.254 9.835   1.00 72.53  ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -8.474  -14.511 9.046   1.00 62.15  ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -1.313  -16.463 9.967   1.00 42.75  ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? -1.030  -17.565 9.064   1.00 38.49  ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 0.335   -18.195 9.324   1.00 39.12  ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 0.563   -19.304 8.844   1.00 40.14  ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -1.169  -17.134 7.593   1.00 40.72  ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -2.569  -16.688 7.198   1.00 39.87  ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -3.693  -17.433 7.565   1.00 37.73  ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -2.769  -15.517 6.463   1.00 43.68  ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -4.968  -17.017 7.217   1.00 37.64  ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -4.043  -15.103 6.092   1.00 42.02  ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -5.143  -15.854 6.479   1.00 44.20  ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -6.400  -15.464 6.107   1.00 41.52  ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 1.228   -17.494 10.057  1.00 36.89  ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 2.622   -17.906 10.153  1.00 36.83  ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 2.834   -18.946 11.258  1.00 38.81  ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 3.525   -18.691 12.222  1.00 39.08  ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 2.223   -20.123 11.131  1.00 44.86  ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 2.189   -21.087 12.227  1.00 49.02  ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 2.347   -22.468 11.623  1.00 42.86  ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 1.836   -22.705 10.543  1.00 37.70  ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 0.856   -21.072 12.992  1.00 46.58  ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 0.829   -20.000 14.069  1.00 57.18  ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? -0.538  -19.819 14.712  1.00 66.42  ? 70  LYS A CD  1 
ATOM   570  C CE  . LYS A 1 71 ? -0.559  -18.493 15.418  1.00 79.88  ? 70  LYS A CE  1 
ATOM   571  N NZ  . LYS A 1 71 ? -1.925  -18.060 15.730  1.00 89.05  ? 70  LYS A NZ  1 
ATOM   572  N N   . PRO A 1 72 ? 3.109   -23.387 12.248  1.00 45.25  ? 71  PRO A N   1 
ATOM   573  C CA  . PRO A 1 72 ? 3.389   -24.674 11.610  1.00 41.18  ? 71  PRO A CA  1 
ATOM   574  C C   . PRO A 1 72 ? 2.112   -25.329 11.099  1.00 42.55  ? 71  PRO A C   1 
ATOM   575  O O   . PRO A 1 72 ? 1.009   -25.048 11.574  1.00 45.59  ? 71  PRO A O   1 
ATOM   576  C CB  . PRO A 1 72 ? 4.089   -25.475 12.738  1.00 46.31  ? 71  PRO A CB  1 
ATOM   577  C CG  . PRO A 1 72 ? 4.786   -24.403 13.568  1.00 39.28  ? 71  PRO A CG  1 
ATOM   578  C CD  . PRO A 1 72 ? 3.805   -23.211 13.540  1.00 45.27  ? 71  PRO A CD  1 
ATOM   579  N N   . ASN A 1 73 ? 2.286   -26.161 10.082  1.00 41.89  ? 72  ASN A N   1 
ATOM   580  C CA  . ASN A 1 73 ? 1.183   -26.813 9.417   1.00 51.03  ? 72  ASN A CA  1 
ATOM   581  C C   . ASN A 1 73 ? 1.703   -28.173 8.983   1.00 52.22  ? 72  ASN A C   1 
ATOM   582  O O   . ASN A 1 73 ? 2.890   -28.295 8.691   1.00 47.50  ? 72  ASN A O   1 
ATOM   583  C CB  . ASN A 1 73 ? 0.686   -25.973 8.244   1.00 48.00  ? 72  ASN A CB  1 
ATOM   584  C CG  . ASN A 1 73 ? -0.570  -26.519 7.609   1.00 51.10  ? 72  ASN A CG  1 
ATOM   585  O OD1 . ASN A 1 73 ? -0.562  -27.606 7.027   1.00 56.70  ? 72  ASN A OD1 1 
ATOM   586  N ND2 . ASN A 1 73 ? -1.665  -25.775 7.680   1.00 61.16  ? 72  ASN A ND2 1 
ATOM   587  N N   . LYS A 1 74 ? 0.782   -29.144 8.907   1.00 53.73  ? 73  LYS A N   1 
ATOM   588  C CA  . LYS A 1 74 ? 1.082   -30.545 8.668   1.00 52.25  ? 73  LYS A CA  1 
ATOM   589  C C   . LYS A 1 74 ? 1.544   -30.744 7.222   1.00 59.30  ? 73  LYS A C   1 
ATOM   590  O O   . LYS A 1 74 ? 2.342   -31.649 6.955   1.00 56.21  ? 73  LYS A O   1 
ATOM   591  C CB  . LYS A 1 74 ? -0.104  -31.413 9.128   1.00 55.20  ? 73  LYS A CB  1 
ATOM   592  C CG  . LYS A 1 74 ? -1.414  -31.397 8.319   1.00 55.84  ? 73  LYS A CG  1 
ATOM   593  N N   . ARG A 1 75 ? 1.084   -29.872 6.305   1.00 51.99  ? 74  ARG A N   1 
ATOM   594  C CA  . ARG A 1 75 ? 1.270   -30.093 4.871   1.00 51.91  ? 74  ARG A CA  1 
ATOM   595  C C   . ARG A 1 75 ? 2.758   -30.136 4.488   1.00 56.13  ? 74  ARG A C   1 
ATOM   596  O O   . ARG A 1 75 ? 3.598   -29.437 5.077   1.00 44.47  ? 74  ARG A O   1 
ATOM   597  C CB  . ARG A 1 75 ? 0.511   -29.082 4.001   1.00 55.68  ? 74  ARG A CB  1 
ATOM   598  C CG  . ARG A 1 75 ? -0.937  -28.890 4.417   1.00 57.64  ? 74  ARG A CG  1 
ATOM   599  C CD  . ARG A 1 75 ? -1.759  -30.115 4.077   1.00 67.32  ? 74  ARG A CD  1 
ATOM   600  N NE  . ARG A 1 75 ? -2.618  -29.894 2.910   1.00 69.37  ? 74  ARG A NE  1 
ATOM   601  C CZ  . ARG A 1 75 ? -3.762  -29.204 2.957   1.00 71.60  ? 74  ARG A CZ  1 
ATOM   602  N NH1 . ARG A 1 75 ? -4.480  -29.072 1.851   1.00 58.16  ? 74  ARG A NH1 1 
ATOM   603  N NH2 . ARG A 1 75 ? -4.189  -28.672 4.105   1.00 69.28  ? 74  ARG A NH2 1 
ATOM   604  N N   . LYS A 1 76 ? 3.057   -30.960 3.471   1.00 46.34  ? 75  LYS A N   1 
ATOM   605  C CA  . LYS A 1 76 ? 4.403   -31.139 2.948   1.00 50.97  ? 75  LYS A CA  1 
ATOM   606  C C   . LYS A 1 76 ? 4.932   -29.800 2.429   1.00 46.55  ? 75  LYS A C   1 
ATOM   607  O O   . LYS A 1 76 ? 4.256   -29.104 1.665   1.00 44.43  ? 75  LYS A O   1 
ATOM   608  C CB  . LYS A 1 76 ? 4.394   -32.174 1.816   1.00 47.25  ? 75  LYS A CB  1 
ATOM   609  C CG  . LYS A 1 76 ? 5.742   -32.538 1.198   1.00 60.10  ? 75  LYS A CG  1 
ATOM   610  C CD  . LYS A 1 76 ? 5.651   -33.555 0.058   1.00 61.57  ? 75  LYS A CD  1 
ATOM   611  C CE  . LYS A 1 76 ? 7.018   -33.865 -0.487  1.00 60.79  ? 75  LYS A CE  1 
ATOM   612  N N   . GLY A 1 77 ? 6.154   -29.459 2.847   1.00 40.30  ? 76  GLY A N   1 
ATOM   613  C CA  . GLY A 1 77 ? 6.823   -28.260 2.379   1.00 40.36  ? 76  GLY A CA  1 
ATOM   614  C C   . GLY A 1 77 ? 6.480   -27.018 3.200   1.00 38.38  ? 76  GLY A C   1 
ATOM   615  O O   . GLY A 1 77 ? 7.218   -26.039 3.142   1.00 39.95  ? 76  GLY A O   1 
ATOM   616  N N   . PHE A 1 78 ? 5.382   -27.051 3.966   1.00 32.69  ? 77  PHE A N   1 
ATOM   617  C CA  . PHE A 1 78 ? 4.891   -25.835 4.609   1.00 41.79  ? 77  PHE A CA  1 
ATOM   618  C C   . PHE A 1 78 ? 5.919   -25.224 5.574   1.00 44.16  ? 77  PHE A C   1 
ATOM   619  O O   . PHE A 1 78 ? 6.151   -23.998 5.596   1.00 34.90  ? 77  PHE A O   1 
ATOM   620  C CB  . PHE A 1 78 ? 3.560   -26.106 5.326   1.00 35.49  ? 77  PHE A CB  1 
ATOM   621  C CG  . PHE A 1 78 ? 2.873   -24.822 5.738   1.00 38.12  ? 77  PHE A CG  1 
ATOM   622  C CD1 . PHE A 1 78 ? 3.192   -24.194 6.938   1.00 38.93  ? 77  PHE A CD1 1 
ATOM   623  C CD2 . PHE A 1 78 ? 1.904   -24.251 4.922   1.00 35.59  ? 77  PHE A CD2 1 
ATOM   624  C CE1 . PHE A 1 78 ? 2.585   -22.995 7.282   1.00 41.46  ? 77  PHE A CE1 1 
ATOM   625  C CE2 . PHE A 1 78 ? 1.298   -23.058 5.278   1.00 33.26  ? 77  PHE A CE2 1 
ATOM   626  C CZ  . PHE A 1 78 ? 1.642   -22.432 6.455   1.00 33.60  ? 77  PHE A CZ  1 
ATOM   627  N N   . ASN A 1 79 ? 6.514   -26.068 6.422   1.00 40.97  ? 78  ASN A N   1 
ATOM   628  C CA  . ASN A 1 79 ? 7.337   -25.506 7.492   1.00 41.90  ? 78  ASN A CA  1 
ATOM   629  C C   . ASN A 1 79 ? 8.677   -25.069 6.904   1.00 41.17  ? 78  ASN A C   1 
ATOM   630  O O   . ASN A 1 79 ? 9.328   -24.110 7.368   1.00 37.07  ? 78  ASN A O   1 
ATOM   631  C CB  . ASN A 1 79 ? 7.487   -26.483 8.656   1.00 42.18  ? 78  ASN A CB  1 
ATOM   632  C CG  . ASN A 1 79 ? 6.205   -26.711 9.427   1.00 46.64  ? 78  ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 79 ? 5.349   -25.821 9.499   1.00 45.40  ? 78  ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 79 ? 6.075   -27.882 10.050  1.00 42.56  ? 78  ASN A ND2 1 
ATOM   635  N N   . GLU A 1 80 ? 9.096   -25.790 5.855   1.00 35.53  ? 79  GLU A N   1 
ATOM   636  C CA  . GLU A 1 80 ? 10.275  -25.316 5.146   1.00 36.73  ? 79  GLU A CA  1 
ATOM   637  C C   . GLU A 1 80 ? 10.005  -23.903 4.610   1.00 37.13  ? 79  GLU A C   1 
ATOM   638  O O   . GLU A 1 80 ? 10.869  -23.023 4.674   1.00 38.03  ? 79  GLU A O   1 
ATOM   639  C CB  . GLU A 1 80 ? 10.699  -26.306 4.070   1.00 37.85  ? 79  GLU A CB  1 
ATOM   640  C CG  . GLU A 1 80 ? 11.921  -25.832 3.293   1.00 46.64  ? 79  GLU A CG  1 
ATOM   641  C CD  . GLU A 1 80 ? 12.583  -26.782 2.312   1.00 53.28  ? 79  GLU A CD  1 
ATOM   642  O OE1 . GLU A 1 80 ? 11.890  -27.580 1.655   1.00 53.99  ? 79  GLU A OE1 1 
ATOM   643  O OE2 . GLU A 1 80 ? 13.821  -26.672 2.168   1.00 55.48  ? 79  GLU A OE2 1 
ATOM   644  N N   . GLY A 1 81 ? 8.784   -23.700 4.100   1.00 33.53  ? 80  GLY A N   1 
ATOM   645  C CA  . GLY A 1 81 ? 8.386   -22.464 3.458   1.00 36.12  ? 80  GLY A CA  1 
ATOM   646  C C   . GLY A 1 81 ? 8.330   -21.329 4.468   1.00 31.79  ? 80  GLY A C   1 
ATOM   647  O O   . GLY A 1 81 ? 8.740   -20.224 4.143   1.00 33.87  ? 80  GLY A O   1 
ATOM   648  N N   . LEU A 1 82 ? 7.895   -21.640 5.702   1.00 33.78  ? 81  LEU A N   1 
ATOM   649  C CA  . LEU A 1 82 ? 7.954   -20.692 6.816   1.00 36.46  ? 81  LEU A CA  1 
ATOM   650  C C   . LEU A 1 82 ? 9.406   -20.322 7.126   1.00 38.64  ? 81  LEU A C   1 
ATOM   651  O O   . LEU A 1 82 ? 9.701   -19.177 7.438   1.00 33.19  ? 81  LEU A O   1 
ATOM   652  C CB  . LEU A 1 82 ? 7.230   -21.073 8.109   1.00 34.04  ? 81  LEU A CB  1 
ATOM   653  C CG  . LEU A 1 82 ? 5.704   -21.204 8.066   1.00 35.82  ? 81  LEU A CG  1 
ATOM   654  C CD1 . LEU A 1 82 ? 5.277   -21.718 9.440   1.00 38.88  ? 81  LEU A CD1 1 
ATOM   655  C CD2 . LEU A 1 82 ? 4.955   -19.905 7.767   1.00 35.20  ? 81  LEU A CD2 1 
ATOM   656  N N   . TRP A 1 83 ? 10.329  -21.284 7.061   1.00 38.17  ? 82  TRP A N   1 
ATOM   657  C CA  . TRP A 1 83 ? 11.722  -20.901 7.272   1.00 41.49  ? 82  TRP A CA  1 
ATOM   658  C C   . TRP A 1 83 ? 12.237  -19.953 6.163   1.00 38.48  ? 82  TRP A C   1 
ATOM   659  O O   . TRP A 1 83 ? 12.897  -18.948 6.439   1.00 35.81  ? 82  TRP A O   1 
ATOM   660  C CB  . TRP A 1 83 ? 12.622  -22.133 7.494   1.00 35.56  ? 82  TRP A CB  1 
ATOM   661  C CG  . TRP A 1 83 ? 14.072  -21.760 7.686   1.00 40.48  ? 82  TRP A CG  1 
ATOM   662  C CD1 . TRP A 1 83 ? 14.723  -21.594 8.872   1.00 38.11  ? 82  TRP A CD1 1 
ATOM   663  C CD2 . TRP A 1 83 ? 15.030  -21.440 6.655   1.00 37.73  ? 82  TRP A CD2 1 
ATOM   664  N NE1 . TRP A 1 83 ? 16.019  -21.225 8.655   1.00 42.83  ? 82  TRP A NE1 1 
ATOM   665  C CE2 . TRP A 1 83 ? 16.240  -21.114 7.309   1.00 39.39  ? 82  TRP A CE2 1 
ATOM   666  C CE3 . TRP A 1 83 ? 14.987  -21.405 5.252   1.00 37.20  ? 82  TRP A CE3 1 
ATOM   667  C CZ2 . TRP A 1 83 ? 17.396  -20.759 6.611   1.00 38.40  ? 82  TRP A CZ2 1 
ATOM   668  C CZ3 . TRP A 1 83 ? 16.123  -21.056 4.554   1.00 36.42  ? 82  TRP A CZ3 1 
ATOM   669  C CH2 . TRP A 1 83 ? 17.303  -20.712 5.237   1.00 43.57  ? 82  TRP A CH2 1 
ATOM   670  N N   . GLU A 1 84 ? 11.902  -20.237 4.902   1.00 34.79  ? 83  GLU A N   1 
ATOM   671  C CA  . GLU A 1 84 ? 12.416  -19.455 3.783   1.00 32.99  ? 83  GLU A CA  1 
ATOM   672  C C   . GLU A 1 84 ? 11.885  -18.016 3.818   1.00 34.87  ? 83  GLU A C   1 
ATOM   673  O O   . GLU A 1 84 ? 12.636  -17.064 3.623   1.00 37.05  ? 83  GLU A O   1 
ATOM   674  C CB  . GLU A 1 84 ? 12.094  -20.161 2.472   1.00 34.06  ? 83  GLU A CB  1 
ATOM   675  C CG  . GLU A 1 84 ? 12.734  -21.547 2.321   1.00 37.10  ? 83  GLU A CG  1 
ATOM   676  C CD  . GLU A 1 84 ? 12.261  -22.307 1.072   1.00 42.63  ? 83  GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 84 ? 11.312  -21.851 0.379   1.00 36.62  ? 83  GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 84 ? 12.845  -23.382 0.771   1.00 42.97  ? 83  GLU A OE2 1 
ATOM   679  N N   . ILE A 1 85 ? 10.579  -17.847 4.060   1.00 32.16  ? 84  ILE A N   1 
ATOM   680  C CA  . ILE A 1 85 ? 9.970   -16.535 3.952   1.00 31.25  ? 84  ILE A CA  1 
ATOM   681  C C   . ILE A 1 85 ? 10.523  -15.677 5.092   1.00 37.59  ? 84  ILE A C   1 
ATOM   682  O O   . ILE A 1 85 ? 10.546  -14.457 4.945   1.00 32.70  ? 84  ILE A O   1 
ATOM   683  C CB  . ILE A 1 85 ? 8.417   -16.560 3.958   1.00 33.18  ? 84  ILE A CB  1 
ATOM   684  C CG1 . ILE A 1 85 ? 7.826   -15.205 3.531   1.00 31.21  ? 84  ILE A CG1 1 
ATOM   685  C CG2 . ILE A 1 85 ? 7.853   -16.978 5.325   1.00 26.00  ? 84  ILE A CG2 1 
ATOM   686  C CD1 . ILE A 1 85 ? 6.392   -15.240 3.023   1.00 29.78  ? 84  ILE A CD1 1 
ATOM   687  N N   . GLN A 1 86 ? 10.938  -16.309 6.211   1.00 32.75  ? 85  GLN A N   1 
ATOM   688  C CA  . GLN A 1 86 ? 11.426  -15.543 7.356   1.00 38.14  ? 85  GLN A CA  1 
ATOM   689  C C   . GLN A 1 86 ? 12.941  -15.290 7.294   1.00 35.54  ? 85  GLN A C   1 
ATOM   690  O O   . GLN A 1 86 ? 13.373  -14.204 7.666   1.00 37.37  ? 85  GLN A O   1 
ATOM   691  C CB  . GLN A 1 86 ? 10.903  -16.056 8.703   1.00 40.20  ? 85  GLN A CB  1 
ATOM   692  C CG  . GLN A 1 86 ? 11.316  -15.195 9.896   1.00 52.94  ? 85  GLN A CG  1 
ATOM   693  C CD  . GLN A 1 86 ? 10.754  -15.649 11.231  1.00 61.50  ? 85  GLN A CD  1 
ATOM   694  O OE1 . GLN A 1 86 ? 10.148  -16.727 11.364  1.00 52.05  ? 85  GLN A OE1 1 
ATOM   695  N NE2 . GLN A 1 86 ? 10.959  -14.811 12.245  1.00 56.75  ? 85  GLN A NE2 1 
ATOM   696  N N   . ASN A 1 87 ? 13.727  -16.243 6.759   1.00 32.20  ? 86  ASN A N   1 
ATOM   697  C CA  . ASN A 1 87 ? 15.189  -16.229 6.844   1.00 33.75  ? 86  ASN A CA  1 
ATOM   698  C C   . ASN A 1 87 ? 15.903  -15.911 5.523   1.00 36.38  ? 86  ASN A C   1 
ATOM   699  O O   . ASN A 1 87 ? 16.988  -15.337 5.552   1.00 38.31  ? 86  ASN A O   1 
ATOM   700  C CB  . ASN A 1 87 ? 15.726  -17.492 7.507   1.00 37.52  ? 86  ASN A CB  1 
ATOM   701  C CG  . ASN A 1 87 ? 15.156  -17.562 8.906   1.00 43.08  ? 86  ASN A CG  1 
ATOM   702  O OD1 . ASN A 1 87 ? 15.479  -16.710 9.734   1.00 39.56  ? 86  ASN A OD1 1 
ATOM   703  N ND2 . ASN A 1 87 ? 14.195  -18.437 9.141   1.00 39.26  ? 86  ASN A ND2 1 
ATOM   704  N N   . ASN A 1 88 ? 15.367  -16.315 4.360   1.00 34.51  ? 87  ASN A N   1 
ATOM   705  C CA  . ASN A 1 88 ? 16.002  -15.842 3.138   1.00 37.12  ? 87  ASN A CA  1 
ATOM   706  C C   . ASN A 1 88 ? 14.975  -15.762 2.011   1.00 35.65  ? 87  ASN A C   1 
ATOM   707  O O   . ASN A 1 88 ? 15.050  -16.531 1.043   1.00 30.85  ? 87  ASN A O   1 
ATOM   708  C CB  . ASN A 1 88 ? 17.189  -16.713 2.739   1.00 38.29  ? 87  ASN A CB  1 
ATOM   709  C CG  . ASN A 1 88 ? 18.137  -16.040 1.764   1.00 39.81  ? 87  ASN A CG  1 
ATOM   710  O OD1 . ASN A 1 88 ? 17.792  -15.072 1.069   1.00 35.04  ? 87  ASN A OD1 1 
ATOM   711  N ND2 . ASN A 1 88 ? 19.352  -16.560 1.684   1.00 40.76  ? 87  ASN A ND2 1 
ATOM   712  N N   . PRO A 1 89 ? 13.996  -14.829 2.105   1.00 34.28  ? 88  PRO A N   1 
ATOM   713  C CA  . PRO A 1 89 ? 12.886  -14.828 1.155   1.00 33.13  ? 88  PRO A CA  1 
ATOM   714  C C   . PRO A 1 89 ? 13.193  -14.381 -0.271  1.00 32.11  ? 88  PRO A C   1 
ATOM   715  O O   . PRO A 1 89 ? 12.360  -14.643 -1.135  1.00 35.90  ? 88  PRO A O   1 
ATOM   716  C CB  . PRO A 1 89 ? 11.886  -13.913 1.838   1.00 29.47  ? 88  PRO A CB  1 
ATOM   717  C CG  . PRO A 1 89 ? 12.768  -12.911 2.546   1.00 28.88  ? 88  PRO A CG  1 
ATOM   718  C CD  . PRO A 1 89 ? 13.877  -13.766 3.126   1.00 31.12  ? 88  PRO A CD  1 
ATOM   719  N N   . HIS A 1 90 ? 14.367  -13.747 -0.498  1.00 34.57  ? 89  HIS A N   1 
ATOM   720  C CA  . HIS A 1 90 ? 14.798  -13.242 -1.803  1.00 34.98  ? 89  HIS A CA  1 
ATOM   721  C C   . HIS A 1 90 ? 15.857  -14.109 -2.494  1.00 34.03  ? 89  HIS A C   1 
ATOM   722  O O   . HIS A 1 90 ? 16.385  -13.720 -3.544  1.00 31.70  ? 89  HIS A O   1 
ATOM   723  C CB  . HIS A 1 90 ? 15.199  -11.761 -1.732  1.00 31.30  ? 89  HIS A CB  1 
ATOM   724  C CG  . HIS A 1 90 ? 14.108  -10.943 -1.102  1.00 34.34  ? 89  HIS A CG  1 
ATOM   725  N ND1 . HIS A 1 90 ? 12.825  -10.854 -1.630  1.00 31.58  ? 89  HIS A ND1 1 
ATOM   726  C CD2 . HIS A 1 90 ? 14.091  -10.249 0.041   1.00 29.98  ? 89  HIS A CD2 1 
ATOM   727  C CE1 . HIS A 1 90 ? 12.079  -10.091 -0.846  1.00 28.92  ? 89  HIS A CE1 1 
ATOM   728  N NE2 . HIS A 1 90 ? 12.824  -9.707  0.173   1.00 36.35  ? 89  HIS A NE2 1 
ATOM   729  N N   . ALA A 1 91 ? 16.130  -15.299 -1.948  1.00 32.20  ? 90  ALA A N   1 
ATOM   730  C CA  . ALA A 1 91 ? 17.170  -16.157 -2.529  1.00 36.21  ? 90  ALA A CA  1 
ATOM   731  C C   . ALA A 1 91 ? 16.718  -16.772 -3.843  1.00 34.07  ? 90  ALA A C   1 
ATOM   732  O O   . ALA A 1 91 ? 15.538  -16.776 -4.199  1.00 37.45  ? 90  ALA A O   1 
ATOM   733  C CB  . ALA A 1 91 ? 17.598  -17.273 -1.577  1.00 32.01  ? 90  ALA A CB  1 
ATOM   734  N N   . SER A 1 92 ? 17.694  -17.362 -4.518  1.00 35.89  ? 91  SER A N   1 
ATOM   735  C CA  . SER A 1 92 ? 17.418  -18.268 -5.610  1.00 36.29  ? 91  SER A CA  1 
ATOM   736  C C   . SER A 1 92 ? 17.127  -19.659 -5.056  1.00 35.82  ? 91  SER A C   1 
ATOM   737  O O   . SER A 1 92 ? 17.935  -20.240 -4.333  1.00 39.81  ? 91  SER A O   1 
ATOM   738  C CB  . SER A 1 92 ? 18.567  -18.286 -6.562  1.00 38.89  ? 91  SER A CB  1 
ATOM   739  O OG  . SER A 1 92 ? 18.477  -19.465 -7.349  1.00 52.95  ? 91  SER A OG  1 
ATOM   740  N N   . TYR A 1 93 ? 15.955  -20.193 -5.395  1.00 40.73  ? 92  TYR A N   1 
ATOM   741  C CA  . TYR A 1 93 ? 15.595  -21.557 -5.032  1.00 47.74  ? 92  TYR A CA  1 
ATOM   742  C C   . TYR A 1 93 ? 15.601  -22.433 -6.289  1.00 55.29  ? 92  TYR A C   1 
ATOM   743  O O   . TYR A 1 93 ? 15.043  -23.530 -6.281  1.00 55.59  ? 92  TYR A O   1 
ATOM   744  C CB  . TYR A 1 93 ? 14.265  -21.575 -4.264  1.00 41.02  ? 92  TYR A CB  1 
ATOM   745  C CG  . TYR A 1 93 ? 14.399  -20.946 -2.882  1.00 46.53  ? 92  TYR A CG  1 
ATOM   746  C CD1 . TYR A 1 93 ? 14.829  -21.700 -1.784  1.00 40.18  ? 92  TYR A CD1 1 
ATOM   747  C CD2 . TYR A 1 93 ? 14.118  -19.595 -2.671  1.00 38.73  ? 92  TYR A CD2 1 
ATOM   748  C CE1 . TYR A 1 93 ? 14.986  -21.120 -0.526  1.00 41.14  ? 92  TYR A CE1 1 
ATOM   749  C CE2 . TYR A 1 93 ? 14.259  -19.013 -1.416  1.00 41.82  ? 92  TYR A CE2 1 
ATOM   750  C CZ  . TYR A 1 93 ? 14.712  -19.771 -0.339  1.00 44.37  ? 92  TYR A CZ  1 
ATOM   751  O OH  . TYR A 1 93 ? 14.881  -19.204 0.901   1.00 40.19  ? 92  TYR A OH  1 
ATOM   752  N N   . SER A 1 94 ? 16.264  -21.935 -7.345  1.00 64.66  ? 93  SER A N   1 
ATOM   753  C CA  . SER A 1 94 ? 16.389  -22.577 -8.652  1.00 82.53  ? 93  SER A CA  1 
ATOM   754  C C   . SER A 1 94 ? 16.912  -24.027 -8.558  1.00 81.53  ? 93  SER A C   1 
ATOM   755  O O   . SER A 1 94 ? 17.445  -24.415 -7.490  1.00 79.23  ? 93  SER A O   1 
ATOM   756  C CB  . SER A 1 94 ? 17.258  -21.750 -9.595  1.00 82.90  ? 93  SER A CB  1 
ATOM   757  O OG  . SER A 1 94 ? 16.778  -20.419 -9.736  1.00 90.44  ? 93  SER A OG  1 
ATOM   758  O OXT . SER A 1 94 ? 16.783  -24.730 -9.582  1.00 99.03  ? 93  SER A OXT 1 
ATOM   759  N N   . MET B 1 2  ? 38.713  -11.356 -40.707 1.00 77.88  ? 1   MET B N   1 
ATOM   760  C CA  . MET B 1 2  ? 38.574  -12.248 -41.889 1.00 95.64  ? 1   MET B CA  1 
ATOM   761  C C   . MET B 1 2  ? 37.082  -12.490 -42.108 1.00 90.58  ? 1   MET B C   1 
ATOM   762  O O   . MET B 1 2  ? 36.363  -12.767 -41.146 1.00 96.04  ? 1   MET B O   1 
ATOM   763  C CB  . MET B 1 2  ? 39.348  -13.562 -41.677 1.00 106.94 ? 1   MET B CB  1 
ATOM   764  C CG  . MET B 1 2  ? 39.751  -14.321 -42.950 1.00 111.95 ? 1   MET B CG  1 
ATOM   765  S SD  . MET B 1 2  ? 41.082  -13.708 -44.015 1.00 115.37 ? 1   MET B SD  1 
ATOM   766  C CE  . MET B 1 2  ? 42.630  -13.984 -43.136 1.00 108.01 ? 1   MET B CE  1 
ATOM   767  N N   . PRO B 1 3  ? 36.548  -12.323 -43.346 1.00 79.99  ? 2   PRO B N   1 
ATOM   768  C CA  . PRO B 1 3  ? 35.151  -12.671 -43.611 1.00 77.85  ? 2   PRO B CA  1 
ATOM   769  C C   . PRO B 1 3  ? 34.852  -14.115 -43.199 1.00 72.29  ? 2   PRO B C   1 
ATOM   770  O O   . PRO B 1 3  ? 35.682  -15.007 -43.382 1.00 69.26  ? 2   PRO B O   1 
ATOM   771  C CB  . PRO B 1 3  ? 34.955  -12.397 -45.113 1.00 78.04  ? 2   PRO B CB  1 
ATOM   772  C CG  . PRO B 1 3  ? 36.061  -11.414 -45.451 1.00 72.48  ? 2   PRO B CG  1 
ATOM   773  C CD  . PRO B 1 3  ? 37.227  -11.751 -44.525 1.00 65.11  ? 2   PRO B CD  1 
ATOM   774  N N   . HIS B 1 4  ? 33.679  -14.281 -42.571 1.00 74.16  ? 3   HIS B N   1 
ATOM   775  C CA  . HIS B 1 4  ? 33.085  -15.538 -42.125 1.00 81.63  ? 3   HIS B CA  1 
ATOM   776  C C   . HIS B 1 4  ? 31.665  -15.613 -42.691 1.00 83.45  ? 3   HIS B C   1 
ATOM   777  O O   . HIS B 1 4  ? 31.143  -14.587 -43.144 1.00 83.94  ? 3   HIS B O   1 
ATOM   778  C CB  . HIS B 1 4  ? 33.076  -15.593 -40.593 1.00 81.21  ? 3   HIS B CB  1 
ATOM   779  C CG  . HIS B 1 4  ? 34.436  -15.774 -40.000 1.00 88.49  ? 3   HIS B CG  1 
ATOM   780  N ND1 . HIS B 1 4  ? 35.362  -16.652 -40.529 1.00 86.23  ? 3   HIS B ND1 1 
ATOM   781  C CD2 . HIS B 1 4  ? 35.015  -15.211 -38.927 1.00 77.25  ? 3   HIS B CD2 1 
ATOM   782  C CE1 . HIS B 1 4  ? 36.467  -16.605 -39.801 1.00 83.27  ? 3   HIS B CE1 1 
ATOM   783  N NE2 . HIS B 1 4  ? 36.275  -15.733 -38.825 1.00 86.76  ? 3   HIS B NE2 1 
ATOM   784  N N   . ALA B 1 5  ? 31.038  -16.806 -42.682 1.00 65.18  ? 4   ALA B N   1 
ATOM   785  C CA  . ALA B 1 5  ? 29.762  -16.922 -43.377 1.00 57.87  ? 4   ALA B CA  1 
ATOM   786  C C   . ALA B 1 5  ? 28.731  -15.999 -42.729 1.00 55.67  ? 4   ALA B C   1 
ATOM   787  O O   . ALA B 1 5  ? 27.915  -15.391 -43.421 1.00 61.49  ? 4   ALA B O   1 
ATOM   788  C CB  . ALA B 1 5  ? 29.285  -18.343 -43.432 1.00 64.10  ? 4   ALA B CB  1 
ATOM   789  N N   . PHE B 1 6  ? 28.790  -15.911 -41.395 1.00 53.09  ? 5   PHE B N   1 
ATOM   790  C CA  . PHE B 1 6  ? 28.074  -14.905 -40.620 1.00 61.67  ? 5   PHE B CA  1 
ATOM   791  C C   . PHE B 1 6  ? 28.993  -13.699 -40.357 1.00 56.56  ? 5   PHE B C   1 
ATOM   792  O O   . PHE B 1 6  ? 30.108  -13.846 -39.860 1.00 58.93  ? 5   PHE B O   1 
ATOM   793  C CB  . PHE B 1 6  ? 27.471  -15.527 -39.349 1.00 48.14  ? 5   PHE B CB  1 
ATOM   794  C CG  . PHE B 1 6  ? 26.285  -16.472 -39.551 1.00 45.21  ? 5   PHE B CG  1 
ATOM   795  C CD1 . PHE B 1 6  ? 25.003  -15.975 -39.815 1.00 43.09  ? 5   PHE B CD1 1 
ATOM   796  C CD2 . PHE B 1 6  ? 26.455  -17.854 -39.450 1.00 41.56  ? 5   PHE B CD2 1 
ATOM   797  C CE1 . PHE B 1 6  ? 23.931  -16.838 -39.986 1.00 46.06  ? 5   PHE B CE1 1 
ATOM   798  C CE2 . PHE B 1 6  ? 25.378  -18.714 -39.600 1.00 41.04  ? 5   PHE B CE2 1 
ATOM   799  C CZ  . PHE B 1 6  ? 24.121  -18.209 -39.891 1.00 45.51  ? 5   PHE B CZ  1 
ATOM   800  N N   . LYS B 1 7  ? 28.519  -12.498 -40.696 1.00 54.20  ? 6   LYS B N   1 
ATOM   801  C CA  . LYS B 1 7  ? 29.260  -11.271 -40.423 1.00 52.94  ? 6   LYS B CA  1 
ATOM   802  C C   . LYS B 1 7  ? 28.470  -10.390 -39.445 1.00 58.60  ? 6   LYS B C   1 
ATOM   803  O O   . LYS B 1 7  ? 27.235  -10.450 -39.381 1.00 42.97  ? 6   LYS B O   1 
ATOM   804  C CB  . LYS B 1 7  ? 29.552  -10.574 -41.754 1.00 52.00  ? 6   LYS B CB  1 
ATOM   805  C CG  . LYS B 1 7  ? 28.344  -10.288 -42.618 1.00 54.04  ? 6   LYS B CG  1 
ATOM   806  C CD  . LYS B 1 7  ? 28.670  -9.448  -43.849 1.00 67.09  ? 6   LYS B CD  1 
ATOM   807  C CE  . LYS B 1 7  ? 27.392  -9.002  -44.468 1.00 58.47  ? 6   LYS B CE  1 
ATOM   808  N NZ  . LYS B 1 7  ? 26.463  -10.114 -44.257 1.00 63.11  ? 6   LYS B NZ  1 
ATOM   809  N N   . PRO B 1 8  ? 29.151  -9.549  -38.630 1.00 62.70  ? 7   PRO B N   1 
ATOM   810  C CA  . PRO B 1 8  ? 28.460  -8.668  -37.691 1.00 56.50  ? 7   PRO B CA  1 
ATOM   811  C C   . PRO B 1 8  ? 27.355  -7.937  -38.431 1.00 49.56  ? 7   PRO B C   1 
ATOM   812  O O   . PRO B 1 8  ? 27.570  -7.411  -39.510 1.00 54.63  ? 7   PRO B O   1 
ATOM   813  C CB  . PRO B 1 8  ? 29.575  -7.745  -37.253 1.00 57.89  ? 7   PRO B CB  1 
ATOM   814  C CG  . PRO B 1 8  ? 30.762  -8.667  -37.233 1.00 62.31  ? 7   PRO B CG  1 
ATOM   815  C CD  . PRO B 1 8  ? 30.613  -9.417  -38.547 1.00 68.45  ? 7   PRO B CD  1 
ATOM   816  N N   . GLY B 1 9  ? 26.155  -7.969  -37.851 1.00 45.94  ? 8   GLY B N   1 
ATOM   817  C CA  . GLY B 1 9  ? 25.033  -7.282  -38.453 1.00 40.45  ? 8   GLY B CA  1 
ATOM   818  C C   . GLY B 1 9  ? 23.993  -8.246  -39.017 1.00 37.92  ? 8   GLY B C   1 
ATOM   819  O O   . GLY B 1 9  ? 22.872  -7.829  -39.279 1.00 43.42  ? 8   GLY B O   1 
ATOM   820  N N   . ASP B 1 10 ? 24.376  -9.508  -39.254 1.00 40.53  ? 9   ASP B N   1 
ATOM   821  C CA  . ASP B 1 10 ? 23.472  -10.486 -39.852 1.00 40.34  ? 9   ASP B CA  1 
ATOM   822  C C   . ASP B 1 10 ? 22.325  -10.782 -38.887 1.00 42.93  ? 9   ASP B C   1 
ATOM   823  O O   . ASP B 1 10 ? 22.525  -10.826 -37.668 1.00 37.26  ? 9   ASP B O   1 
ATOM   824  C CB  . ASP B 1 10 ? 24.195  -11.781 -40.181 1.00 44.55  ? 9   ASP B CB  1 
ATOM   825  C CG  . ASP B 1 10 ? 24.991  -11.763 -41.480 1.00 49.11  ? 9   ASP B CG  1 
ATOM   826  O OD1 . ASP B 1 10 ? 24.650  -10.938 -42.345 1.00 45.54  ? 9   ASP B OD1 1 
ATOM   827  O OD2 . ASP B 1 10 ? 25.974  -12.539 -41.586 1.00 50.16  ? 9   ASP B OD2 1 
ATOM   828  N N   . LEU B 1 11 ? 21.124  -10.960 -39.441 1.00 33.59  ? 10  LEU B N   1 
ATOM   829  C CA  . LEU B 1 11 ? 19.949  -11.163 -38.611 1.00 37.02  ? 10  LEU B CA  1 
ATOM   830  C C   . LEU B 1 11 ? 19.554  -12.642 -38.657 1.00 35.39  ? 10  LEU B C   1 
ATOM   831  O O   . LEU B 1 11 ? 19.542  -13.248 -39.741 1.00 34.99  ? 10  LEU B O   1 
ATOM   832  C CB  . LEU B 1 11 ? 18.819  -10.252 -39.113 1.00 36.25  ? 10  LEU B CB  1 
ATOM   833  C CG  . LEU B 1 11 ? 19.163  -8.755  -39.208 1.00 38.66  ? 10  LEU B CG  1 
ATOM   834  C CD1 . LEU B 1 11 ? 18.014  -7.913  -39.694 1.00 29.84  ? 10  LEU B CD1 1 
ATOM   835  C CD2 . LEU B 1 11 ? 19.650  -8.234  -37.855 1.00 34.38  ? 10  LEU B CD2 1 
ATOM   836  N N   . VAL B 1 12 ? 19.178  -13.188 -37.488 1.00 32.94  ? 11  VAL B N   1 
ATOM   837  C CA  . VAL B 1 12 ? 18.943  -14.614 -37.363 1.00 34.40  ? 11  VAL B CA  1 
ATOM   838  C C   . VAL B 1 12 ? 17.792  -14.844 -36.388 1.00 37.77  ? 11  VAL B C   1 
ATOM   839  O O   . VAL B 1 12 ? 17.355  -13.927 -35.675 1.00 36.07  ? 11  VAL B O   1 
ATOM   840  C CB  . VAL B 1 12 ? 20.237  -15.341 -36.919 1.00 35.84  ? 11  VAL B CB  1 
ATOM   841  C CG1 . VAL B 1 12 ? 21.418  -15.099 -37.876 1.00 32.02  ? 11  VAL B CG1 1 
ATOM   842  C CG2 . VAL B 1 12 ? 20.635  -14.971 -35.496 1.00 37.93  ? 11  VAL B CG2 1 
ATOM   843  N N   . PHE B 1 13 ? 17.289  -16.082 -36.388 1.00 35.34  ? 12  PHE B N   1 
ATOM   844  C CA  . PHE B 1 13 ? 16.761  -16.629 -35.154 1.00 36.02  ? 12  PHE B CA  1 
ATOM   845  C C   . PHE B 1 13 ? 17.849  -17.489 -34.533 1.00 40.64  ? 12  PHE B C   1 
ATOM   846  O O   . PHE B 1 13 ? 18.514  -18.244 -35.264 1.00 36.36  ? 12  PHE B O   1 
ATOM   847  C CB  . PHE B 1 13 ? 15.516  -17.447 -35.449 1.00 34.20  ? 12  PHE B CB  1 
ATOM   848  C CG  . PHE B 1 13 ? 14.353  -16.568 -35.876 1.00 38.53  ? 12  PHE B CG  1 
ATOM   849  C CD1 . PHE B 1 13 ? 14.089  -16.328 -37.226 1.00 40.25  ? 12  PHE B CD1 1 
ATOM   850  C CD2 . PHE B 1 13 ? 13.541  -15.965 -34.923 1.00 34.29  ? 12  PHE B CD2 1 
ATOM   851  C CE1 . PHE B 1 13 ? 13.001  -15.548 -37.605 1.00 39.60  ? 12  PHE B CE1 1 
ATOM   852  C CE2 . PHE B 1 13 ? 12.447  -15.198 -35.308 1.00 36.70  ? 12  PHE B CE2 1 
ATOM   853  C CZ  . PHE B 1 13 ? 12.196  -14.971 -36.646 1.00 40.79  ? 12  PHE B CZ  1 
ATOM   854  N N   . ALA B 1 14 ? 18.044  -17.325 -33.208 1.00 35.56  ? 13  ALA B N   1 
ATOM   855  C CA  . ALA B 1 14 ? 19.073  -18.047 -32.479 1.00 34.42  ? 13  ALA B CA  1 
ATOM   856  C C   . ALA B 1 14 ? 18.426  -19.006 -31.472 1.00 39.46  ? 13  ALA B C   1 
ATOM   857  O O   . ALA B 1 14 ? 17.554  -18.599 -30.702 1.00 43.94  ? 13  ALA B O   1 
ATOM   858  C CB  . ALA B 1 14 ? 19.996  -17.059 -31.822 1.00 33.88  ? 13  ALA B CB  1 
ATOM   859  N N   . LYS B 1 15 ? 18.865  -20.276 -31.462 1.00 39.69  ? 14  LYS B N   1 
ATOM   860  C CA  . LYS B 1 15 ? 18.193  -21.312 -30.685 1.00 38.42  ? 14  LYS B CA  1 
ATOM   861  C C   . LYS B 1 15 ? 19.071  -21.665 -29.497 1.00 36.87  ? 14  LYS B C   1 
ATOM   862  O O   . LYS B 1 15 ? 20.239  -22.014 -29.665 1.00 39.42  ? 14  LYS B O   1 
ATOM   863  C CB  . LYS B 1 15 ? 17.939  -22.603 -31.488 1.00 37.15  ? 14  LYS B CB  1 
ATOM   864  C CG  . LYS B 1 15 ? 17.206  -23.724 -30.729 1.00 32.93  ? 14  LYS B CG  1 
ATOM   865  C CD  . LYS B 1 15 ? 15.798  -23.305 -30.284 1.00 38.52  ? 14  LYS B CD  1 
ATOM   866  C CE  . LYS B 1 15 ? 15.009  -24.461 -29.703 1.00 35.99  ? 14  LYS B CE  1 
ATOM   867  N NZ  . LYS B 1 15 ? 15.455  -24.744 -28.330 1.00 34.11  ? 14  LYS B NZ  1 
ATOM   868  N N   . MET B 1 16 ? 18.484  -21.558 -28.307 1.00 43.25  ? 15  MET B N   1 
ATOM   869  C CA  . MET B 1 16 ? 19.121  -21.966 -27.068 1.00 43.15  ? 15  MET B CA  1 
ATOM   870  C C   . MET B 1 16 ? 18.241  -23.047 -26.467 1.00 43.24  ? 15  MET B C   1 
ATOM   871  O O   . MET B 1 16 ? 17.030  -23.056 -26.719 1.00 40.88  ? 15  MET B O   1 
ATOM   872  C CB  . MET B 1 16 ? 19.056  -20.859 -26.007 1.00 48.54  ? 15  MET B CB  1 
ATOM   873  C CG  . MET B 1 16 ? 19.581  -19.511 -26.404 1.00 56.73  ? 15  MET B CG  1 
ATOM   874  S SD  . MET B 1 16 ? 21.368  -19.493 -26.208 1.00 60.83  ? 15  MET B SD  1 
ATOM   875  C CE  . MET B 1 16 ? 21.691  -19.353 -24.443 1.00 52.95  ? 15  MET B CE  1 
ATOM   876  N N   . LYS B 1 17 ? 18.844  -23.886 -25.615 1.00 48.17  ? 16  LYS B N   1 
ATOM   877  C CA  . LYS B 1 17 ? 18.107  -24.950 -24.944 1.00 50.57  ? 16  LYS B CA  1 
ATOM   878  C C   . LYS B 1 17 ? 17.077  -24.326 -24.001 1.00 47.64  ? 16  LYS B C   1 
ATOM   879  O O   . LYS B 1 17 ? 17.371  -23.376 -23.276 1.00 51.92  ? 16  LYS B O   1 
ATOM   880  C CB  . LYS B 1 17 ? 19.104  -25.903 -24.266 1.00 58.39  ? 16  LYS B CB  1 
ATOM   881  C CG  . LYS B 1 17 ? 18.546  -27.285 -23.934 1.00 66.40  ? 16  LYS B CG  1 
ATOM   882  C CD  . LYS B 1 17 ? 19.499  -28.300 -23.303 1.00 74.05  ? 16  LYS B CD  1 
ATOM   883  C CE  . LYS B 1 17 ? 18.793  -29.604 -23.069 1.00 75.04  ? 16  LYS B CE  1 
ATOM   884  N NZ  . LYS B 1 17 ? 17.529  -29.416 -22.349 1.00 77.10  ? 16  LYS B NZ  1 
ATOM   885  N N   . GLY B 1 18 ? 15.841  -24.822 -24.052 1.00 45.82  ? 17  GLY B N   1 
ATOM   886  C CA  . GLY B 1 18 ? 14.807  -24.271 -23.191 1.00 46.96  ? 17  GLY B CA  1 
ATOM   887  C C   . GLY B 1 18 ? 13.964  -23.176 -23.856 1.00 50.81  ? 17  GLY B C   1 
ATOM   888  O O   . GLY B 1 18 ? 12.945  -22.773 -23.296 1.00 51.78  ? 17  GLY B O   1 
ATOM   889  N N   . TYR B 1 19 ? 14.364  -22.669 -25.034 1.00 45.97  ? 18  TYR B N   1 
ATOM   890  C CA  . TYR B 1 19 ? 13.637  -21.523 -25.563 1.00 43.32  ? 18  TYR B CA  1 
ATOM   891  C C   . TYR B 1 19 ? 13.311  -21.714 -27.035 1.00 43.24  ? 18  TYR B C   1 
ATOM   892  O O   . TYR B 1 19 ? 14.026  -22.394 -27.754 1.00 36.50  ? 18  TYR B O   1 
ATOM   893  C CB  . TYR B 1 19 ? 14.454  -20.234 -25.453 1.00 40.42  ? 18  TYR B CB  1 
ATOM   894  C CG  . TYR B 1 19 ? 14.823  -19.971 -24.007 1.00 49.44  ? 18  TYR B CG  1 
ATOM   895  C CD1 . TYR B 1 19 ? 13.951  -19.270 -23.176 1.00 54.87  ? 18  TYR B CD1 1 
ATOM   896  C CD2 . TYR B 1 19 ? 16.011  -20.464 -23.475 1.00 51.39  ? 18  TYR B CD2 1 
ATOM   897  C CE1 . TYR B 1 19 ? 14.266  -19.062 -21.847 1.00 62.90  ? 18  TYR B CE1 1 
ATOM   898  C CE2 . TYR B 1 19 ? 16.326  -20.267 -22.139 1.00 58.90  ? 18  TYR B CE2 1 
ATOM   899  C CZ  . TYR B 1 19 ? 15.452  -19.559 -21.332 1.00 54.84  ? 18  TYR B CZ  1 
ATOM   900  O OH  . TYR B 1 19 ? 15.755  -19.341 -20.032 1.00 57.31  ? 18  TYR B OH  1 
ATOM   901  N N   . PRO B 1 20 ? 12.259  -21.036 -27.529 1.00 36.93  ? 19  PRO B N   1 
ATOM   902  C CA  . PRO B 1 20 ? 12.004  -20.996 -28.968 1.00 38.84  ? 19  PRO B CA  1 
ATOM   903  C C   . PRO B 1 20 ? 13.143  -20.244 -29.671 1.00 39.60  ? 19  PRO B C   1 
ATOM   904  O O   . PRO B 1 20 ? 13.846  -19.421 -29.064 1.00 38.53  ? 19  PRO B O   1 
ATOM   905  C CB  . PRO B 1 20 ? 10.698  -20.199 -28.948 1.00 34.28  ? 19  PRO B CB  1 
ATOM   906  C CG  . PRO B 1 20 ? 10.868  -19.224 -27.772 1.00 33.98  ? 19  PRO B CG  1 
ATOM   907  C CD  . PRO B 1 20 ? 11.366  -20.185 -26.724 1.00 37.40  ? 19  PRO B CD  1 
ATOM   908  N N   . HIS B 1 21 ? 13.347  -20.586 -30.940 1.00 37.70  ? 20  HIS B N   1 
ATOM   909  C CA  . HIS B 1 21 ? 14.191  -19.826 -31.860 1.00 39.25  ? 20  HIS B CA  1 
ATOM   910  C C   . HIS B 1 21 ? 13.935  -18.334 -31.663 1.00 35.96  ? 20  HIS B C   1 
ATOM   911  O O   . HIS B 1 21 ? 12.818  -17.848 -31.914 1.00 34.27  ? 20  HIS B O   1 
ATOM   912  C CB  . HIS B 1 21 ? 13.877  -20.253 -33.298 1.00 36.92  ? 20  HIS B CB  1 
ATOM   913  C CG  . HIS B 1 21 ? 14.027  -21.736 -33.444 1.00 42.54  ? 20  HIS B CG  1 
ATOM   914  N ND1 . HIS B 1 21 ? 13.118  -22.627 -32.914 1.00 45.03  ? 20  HIS B ND1 1 
ATOM   915  C CD2 . HIS B 1 21 ? 15.000  -22.482 -33.998 1.00 41.95  ? 20  HIS B CD2 1 
ATOM   916  C CE1 . HIS B 1 21 ? 13.523  -23.872 -33.179 1.00 48.36  ? 20  HIS B CE1 1 
ATOM   917  N NE2 . HIS B 1 21 ? 14.657  -23.811 -33.849 1.00 37.92  ? 20  HIS B NE2 1 
ATOM   918  N N   . TRP B 1 22 ? 14.984  -17.609 -31.245 1.00 34.18  ? 21  TRP B N   1 
ATOM   919  C CA  . TRP B 1 22 ? 14.778  -16.248 -30.764 1.00 35.17  ? 21  TRP B CA  1 
ATOM   920  C C   . TRP B 1 22 ? 15.304  -15.219 -31.768 1.00 31.70  ? 21  TRP B C   1 
ATOM   921  O O   . TRP B 1 22 ? 16.428  -15.347 -32.222 1.00 36.36  ? 21  TRP B O   1 
ATOM   922  C CB  . TRP B 1 22 ? 15.483  -16.072 -29.415 1.00 33.88  ? 21  TRP B CB  1 
ATOM   923  C CG  . TRP B 1 22 ? 14.905  -14.950 -28.592 1.00 34.90  ? 21  TRP B CG  1 
ATOM   924  C CD1 . TRP B 1 22 ? 15.222  -13.628 -28.700 1.00 33.35  ? 21  TRP B CD1 1 
ATOM   925  C CD2 . TRP B 1 22 ? 13.907  -15.047 -27.546 1.00 37.41  ? 21  TRP B CD2 1 
ATOM   926  N NE1 . TRP B 1 22 ? 14.483  -12.893 -27.804 1.00 39.67  ? 21  TRP B NE1 1 
ATOM   927  C CE2 . TRP B 1 22 ? 13.679  -13.735 -27.072 1.00 36.65  ? 21  TRP B CE2 1 
ATOM   928  C CE3 . TRP B 1 22 ? 13.198  -16.105 -26.957 1.00 40.11  ? 21  TRP B CE3 1 
ATOM   929  C CZ2 . TRP B 1 22 ? 12.769  -13.450 -26.052 1.00 36.07  ? 21  TRP B CZ2 1 
ATOM   930  C CZ3 . TRP B 1 22 ? 12.314  -15.822 -25.936 1.00 38.00  ? 21  TRP B CZ3 1 
ATOM   931  C CH2 . TRP B 1 22 ? 12.095  -14.511 -25.494 1.00 34.97  ? 21  TRP B CH2 1 
ATOM   932  N N   . PRO B 1 23 ? 14.585  -14.104 -32.064 1.00 35.59  ? 22  PRO B N   1 
ATOM   933  C CA  . PRO B 1 23 ? 15.111  -13.039 -32.940 1.00 32.53  ? 22  PRO B CA  1 
ATOM   934  C C   . PRO B 1 23 ? 16.404  -12.476 -32.361 1.00 32.75  ? 22  PRO B C   1 
ATOM   935  O O   . PRO B 1 23 ? 16.463  -12.183 -31.177 1.00 40.59  ? 22  PRO B O   1 
ATOM   936  C CB  . PRO B 1 23 ? 13.983  -11.996 -32.957 1.00 35.10  ? 22  PRO B CB  1 
ATOM   937  C CG  . PRO B 1 23 ? 13.260  -12.269 -31.658 1.00 36.05  ? 22  PRO B CG  1 
ATOM   938  C CD  . PRO B 1 23 ? 13.229  -13.800 -31.583 1.00 34.63  ? 22  PRO B CD  1 
ATOM   939  N N   . ALA B 1 24 ? 17.452  -12.376 -33.188 1.00 36.87  ? 23  ALA B N   1 
ATOM   940  C CA  . ALA B 1 24 ? 18.797  -12.080 -32.708 1.00 33.48  ? 23  ALA B CA  1 
ATOM   941  C C   . ALA B 1 24 ? 19.635  -11.518 -33.861 1.00 33.67  ? 23  ALA B C   1 
ATOM   942  O O   . ALA B 1 24 ? 19.192  -11.501 -35.021 1.00 36.06  ? 23  ALA B O   1 
ATOM   943  C CB  . ALA B 1 24 ? 19.411  -13.355 -32.106 1.00 28.25  ? 23  ALA B CB  1 
ATOM   944  N N   . ARG B 1 25 ? 20.856  -11.076 -33.536 1.00 35.28  ? 24  ARG B N   1 
ATOM   945  C CA  . ARG B 1 25 ? 21.805  -10.611 -34.544 1.00 40.70  ? 24  ARG B CA  1 
ATOM   946  C C   . ARG B 1 25 ? 23.216  -11.041 -34.152 1.00 40.45  ? 24  ARG B C   1 
ATOM   947  O O   . ARG B 1 25 ? 23.498  -11.277 -32.961 1.00 41.17  ? 24  ARG B O   1 
ATOM   948  C CB  . ARG B 1 25 ? 21.759  -9.086  -34.738 1.00 37.71  ? 24  ARG B CB  1 
ATOM   949  C CG  . ARG B 1 25 ? 22.355  -8.298  -33.577 1.00 38.83  ? 24  ARG B CG  1 
ATOM   950  C CD  . ARG B 1 25 ? 22.165  -6.772  -33.719 1.00 33.11  ? 24  ARG B CD  1 
ATOM   951  N NE  . ARG B 1 25 ? 22.776  -6.048  -32.589 1.00 32.42  ? 24  ARG B NE  1 
ATOM   952  C CZ  . ARG B 1 25 ? 22.434  -4.806  -32.233 1.00 32.90  ? 24  ARG B CZ  1 
ATOM   953  N NH1 . ARG B 1 25 ? 21.525  -4.135  -32.929 1.00 31.14  ? 24  ARG B NH1 1 
ATOM   954  N NH2 . ARG B 1 25 ? 22.999  -4.236  -31.183 1.00 36.72  ? 24  ARG B NH2 1 
ATOM   955  N N   . ILE B 1 26 ? 24.095  -11.131 -35.166 1.00 43.54  ? 25  ILE B N   1 
ATOM   956  C CA  . ILE B 1 26 ? 25.508  -11.364 -34.906 1.00 40.23  ? 25  ILE B CA  1 
ATOM   957  C C   . ILE B 1 26 ? 26.106  -10.006 -34.562 1.00 47.07  ? 25  ILE B C   1 
ATOM   958  O O   . ILE B 1 26 ? 25.905  -9.058  -35.317 1.00 41.78  ? 25  ILE B O   1 
ATOM   959  C CB  . ILE B 1 26 ? 26.226  -11.937 -36.152 1.00 46.18  ? 25  ILE B CB  1 
ATOM   960  C CG1 . ILE B 1 26 ? 25.456  -13.081 -36.866 1.00 40.38  ? 25  ILE B CG1 1 
ATOM   961  C CG2 . ILE B 1 26 ? 27.691  -12.282 -35.847 1.00 40.49  ? 25  ILE B CG2 1 
ATOM   962  C CD1 . ILE B 1 26 ? 25.080  -14.272 -36.001 1.00 45.23  ? 25  ILE B CD1 1 
ATOM   963  N N   . ASP B 1 27 ? 26.849  -9.951  -33.447 1.00 54.58  ? 26  ASP B N   1 
ATOM   964  C CA  . ASP B 1 27 ? 27.577  -8.768  -33.005 1.00 58.02  ? 26  ASP B CA  1 
ATOM   965  C C   . ASP B 1 27 ? 29.076  -8.923  -33.284 1.00 60.93  ? 26  ASP B C   1 
ATOM   966  O O   . ASP B 1 27 ? 29.492  -9.968  -33.763 1.00 55.55  ? 26  ASP B O   1 
ATOM   967  C CB  . ASP B 1 27 ? 27.334  -8.576  -31.518 1.00 53.42  ? 26  ASP B CB  1 
ATOM   968  C CG  . ASP B 1 27 ? 26.122  -7.730  -31.167 1.00 51.76  ? 26  ASP B CG  1 
ATOM   969  O OD1 . ASP B 1 27 ? 25.412  -7.293  -32.103 1.00 54.51  ? 26  ASP B OD1 1 
ATOM   970  O OD2 . ASP B 1 27 ? 25.929  -7.482  -29.967 1.00 54.39  ? 26  ASP B OD2 1 
ATOM   971  N N   . ASP B 1 28 ? 29.892  -7.906  -32.941 1.00 76.80  ? 27  ASP B N   1 
ATOM   972  C CA  . ASP B 1 28 ? 31.339  -7.927  -33.159 1.00 78.55  ? 27  ASP B CA  1 
ATOM   973  C C   . ASP B 1 28 ? 32.069  -8.333  -31.883 1.00 79.35  ? 27  ASP B C   1 
ATOM   974  O O   . ASP B 1 28 ? 31.498  -8.230  -30.801 1.00 75.61  ? 27  ASP B O   1 
ATOM   975  C CB  . ASP B 1 28 ? 31.901  -6.553  -33.484 1.00 78.37  ? 27  ASP B CB  1 
ATOM   976  C CG  . ASP B 1 28 ? 31.215  -5.811  -34.618 1.00 83.07  ? 27  ASP B CG  1 
ATOM   977  O OD1 . ASP B 1 28 ? 31.838  -5.692  -35.690 1.00 81.02  ? 27  ASP B OD1 1 
ATOM   978  O OD2 . ASP B 1 28 ? 30.070  -5.351  -34.410 1.00 90.23  ? 27  ASP B OD2 1 
ATOM   979  N N   . ILE B 1 29 ? 33.344  -8.742  -32.011 1.00 73.44  ? 28  ILE B N   1 
ATOM   980  C CA  . ILE B 1 29 ? 34.155  -9.060  -30.843 1.00 72.97  ? 28  ILE B CA  1 
ATOM   981  C C   . ILE B 1 29 ? 34.900  -7.801  -30.359 1.00 79.69  ? 28  ILE B C   1 
ATOM   982  O O   . ILE B 1 29 ? 34.554  -6.687  -30.826 1.00 89.53  ? 28  ILE B O   1 
ATOM   983  C CB  . ILE B 1 29 ? 35.122  -10.229 -31.109 1.00 71.31  ? 28  ILE B CB  1 
ATOM   984  N N   . VAL B 1 34 ? 35.537  -10.610 -23.692 1.00 75.55  ? 33  VAL B N   1 
ATOM   985  C CA  . VAL B 1 34 ? 36.175  -11.899 -24.110 1.00 87.11  ? 33  VAL B CA  1 
ATOM   986  C C   . VAL B 1 34 ? 35.845  -12.132 -25.581 1.00 94.25  ? 33  VAL B C   1 
ATOM   987  O O   . VAL B 1 34 ? 34.708  -11.902 -25.983 1.00 101.16 ? 33  VAL B O   1 
ATOM   988  C CB  . VAL B 1 34 ? 35.707  -13.093 -23.245 1.00 87.85  ? 33  VAL B CB  1 
ATOM   989  C CG1 . VAL B 1 34 ? 34.205  -13.367 -23.350 1.00 78.59  ? 33  VAL B CG1 1 
ATOM   990  C CG2 . VAL B 1 34 ? 36.500  -14.367 -23.538 1.00 84.43  ? 33  VAL B CG2 1 
ATOM   991  N N   . LYS B 1 35 ? 36.828  -12.607 -26.362 1.00 89.62  ? 34  LYS B N   1 
ATOM   992  C CA  . LYS B 1 35 ? 36.575  -13.078 -27.723 1.00 92.23  ? 34  LYS B CA  1 
ATOM   993  C C   . LYS B 1 35 ? 35.872  -14.452 -27.693 1.00 99.00  ? 34  LYS B C   1 
ATOM   994  O O   . LYS B 1 35 ? 36.069  -15.240 -26.757 1.00 93.78  ? 34  LYS B O   1 
ATOM   995  C CB  . LYS B 1 35 ? 37.835  -12.962 -28.598 1.00 68.24  ? 34  LYS B CB  1 
ATOM   996  N N   . PRO B 1 36 ? 35.003  -14.780 -28.694 1.00 91.86  ? 35  PRO B N   1 
ATOM   997  C CA  . PRO B 1 36 ? 34.182  -16.004 -28.657 1.00 74.84  ? 35  PRO B CA  1 
ATOM   998  C C   . PRO B 1 36 ? 35.015  -17.273 -28.725 1.00 64.24  ? 35  PRO B C   1 
ATOM   999  O O   . PRO B 1 36 ? 36.127  -17.222 -29.233 1.00 71.52  ? 35  PRO B O   1 
ATOM   1000 C CB  . PRO B 1 36 ? 33.285  -15.873 -29.907 1.00 71.43  ? 35  PRO B CB  1 
ATOM   1001 C CG  . PRO B 1 36 ? 34.070  -14.977 -30.833 1.00 81.60  ? 35  PRO B CG  1 
ATOM   1002 C CD  . PRO B 1 36 ? 34.747  -13.974 -29.905 1.00 83.30  ? 35  PRO B CD  1 
ATOM   1003 N N   . PRO B 1 37 ? 34.517  -18.449 -28.262 1.00 64.38  ? 36  PRO B N   1 
ATOM   1004 C CA  . PRO B 1 37 ? 35.194  -19.711 -28.552 1.00 62.62  ? 36  PRO B CA  1 
ATOM   1005 C C   . PRO B 1 37 ? 35.264  -19.828 -30.076 1.00 83.15  ? 36  PRO B C   1 
ATOM   1006 O O   . PRO B 1 37 ? 34.503  -19.175 -30.795 1.00 78.01  ? 36  PRO B O   1 
ATOM   1007 C CB  . PRO B 1 37 ? 34.338  -20.824 -27.916 1.00 53.77  ? 36  PRO B CB  1 
ATOM   1008 C CG  . PRO B 1 37 ? 33.325  -20.118 -27.033 1.00 47.65  ? 36  PRO B CG  1 
ATOM   1009 C CD  . PRO B 1 37 ? 33.277  -18.645 -27.486 1.00 58.85  ? 36  PRO B CD  1 
ATOM   1010 N N   . PRO B 1 38 ? 36.219  -20.605 -30.636 1.00 96.21  ? 37  PRO B N   1 
ATOM   1011 C CA  . PRO B 1 38 ? 36.208  -20.895 -32.075 1.00 93.47  ? 37  PRO B CA  1 
ATOM   1012 C C   . PRO B 1 38 ? 34.960  -21.662 -32.526 1.00 88.18  ? 37  PRO B C   1 
ATOM   1013 O O   . PRO B 1 38 ? 34.414  -22.475 -31.775 1.00 74.08  ? 37  PRO B O   1 
ATOM   1014 C CB  . PRO B 1 38 ? 37.508  -21.690 -32.298 1.00 95.50  ? 37  PRO B CB  1 
ATOM   1015 C CG  . PRO B 1 38 ? 38.363  -21.365 -31.083 1.00 98.66  ? 37  PRO B CG  1 
ATOM   1016 C CD  . PRO B 1 38 ? 37.385  -21.174 -29.935 1.00 93.14  ? 37  PRO B CD  1 
ATOM   1017 N N   . ASN B 1 39 ? 34.519  -21.372 -33.760 1.00 80.51  ? 38  ASN B N   1 
ATOM   1018 C CA  . ASN B 1 39 ? 33.326  -21.954 -34.361 1.00 74.33  ? 38  ASN B CA  1 
ATOM   1019 C C   . ASN B 1 39 ? 32.079  -21.218 -33.878 1.00 73.14  ? 38  ASN B C   1 
ATOM   1020 O O   . ASN B 1 39 ? 30.978  -21.518 -34.318 1.00 84.43  ? 38  ASN B O   1 
ATOM   1021 C CB  . ASN B 1 39 ? 33.108  -23.425 -34.005 1.00 70.43  ? 38  ASN B CB  1 
ATOM   1022 C CG  . ASN B 1 39 ? 34.053  -24.405 -34.667 1.00 77.85  ? 38  ASN B CG  1 
ATOM   1023 O OD1 . ASN B 1 39 ? 33.791  -25.615 -34.643 1.00 74.45  ? 38  ASN B OD1 1 
ATOM   1024 N ND2 . ASN B 1 39 ? 35.144  -23.936 -35.260 1.00 73.53  ? 38  ASN B ND2 1 
ATOM   1025 N N   . LYS B 1 40 ? 32.246  -20.283 -32.943 1.00 74.04  ? 39  LYS B N   1 
ATOM   1026 C CA  . LYS B 1 40 ? 31.105  -19.686 -32.270 1.00 61.45  ? 39  LYS B CA  1 
ATOM   1027 C C   . LYS B 1 40 ? 31.067  -18.180 -32.538 1.00 58.69  ? 39  LYS B C   1 
ATOM   1028 O O   . LYS B 1 40 ? 32.077  -17.579 -32.903 1.00 59.90  ? 39  LYS B O   1 
ATOM   1029 C CB  . LYS B 1 40 ? 31.124  -20.109 -30.798 1.00 61.36  ? 39  LYS B CB  1 
ATOM   1030 C CG  . LYS B 1 40 ? 30.703  -21.533 -30.479 1.00 57.43  ? 39  LYS B CG  1 
ATOM   1031 C CD  . LYS B 1 40 ? 30.270  -21.555 -29.022 1.00 61.96  ? 39  LYS B CD  1 
ATOM   1032 C CE  . LYS B 1 40 ? 29.375  -22.687 -28.621 1.00 70.31  ? 39  LYS B CE  1 
ATOM   1033 N NZ  . LYS B 1 40 ? 30.110  -23.845 -28.106 1.00 76.63  ? 39  LYS B NZ  1 
ATOM   1034 N N   . TYR B 1 41 ? 29.886  -17.575 -32.382 1.00 53.90  ? 40  TYR B N   1 
ATOM   1035 C CA  . TYR B 1 41 ? 29.748  -16.157 -32.678 1.00 52.37  ? 40  TYR B CA  1 
ATOM   1036 C C   . TYR B 1 41 ? 29.160  -15.401 -31.488 1.00 47.46  ? 40  TYR B C   1 
ATOM   1037 O O   . TYR B 1 41 ? 28.420  -15.950 -30.678 1.00 46.73  ? 40  TYR B O   1 
ATOM   1038 C CB  . TYR B 1 41 ? 28.777  -15.958 -33.848 1.00 54.19  ? 40  TYR B CB  1 
ATOM   1039 C CG  . TYR B 1 41 ? 29.301  -16.354 -35.216 1.00 52.52  ? 40  TYR B CG  1 
ATOM   1040 C CD1 . TYR B 1 41 ? 29.950  -15.422 -36.016 1.00 56.47  ? 40  TYR B CD1 1 
ATOM   1041 C CD2 . TYR B 1 41 ? 29.108  -17.641 -35.725 1.00 58.32  ? 40  TYR B CD2 1 
ATOM   1042 C CE1 . TYR B 1 41 ? 30.405  -15.765 -37.283 1.00 64.54  ? 40  TYR B CE1 1 
ATOM   1043 C CE2 . TYR B 1 41 ? 29.568  -17.995 -36.988 1.00 55.15  ? 40  TYR B CE2 1 
ATOM   1044 C CZ  . TYR B 1 41 ? 30.230  -17.054 -37.764 1.00 62.44  ? 40  TYR B CZ  1 
ATOM   1045 O OH  . TYR B 1 41 ? 30.701  -17.350 -39.013 1.00 59.25  ? 40  TYR B OH  1 
ATOM   1046 N N   . PRO B 1 42 ? 29.417  -14.082 -31.394 1.00 48.07  ? 41  PRO B N   1 
ATOM   1047 C CA  . PRO B 1 42 ? 28.742  -13.249 -30.407 1.00 44.28  ? 41  PRO B CA  1 
ATOM   1048 C C   . PRO B 1 42 ? 27.335  -12.960 -30.911 1.00 45.98  ? 41  PRO B C   1 
ATOM   1049 O O   . PRO B 1 42 ? 27.193  -12.235 -31.892 1.00 48.45  ? 41  PRO B O   1 
ATOM   1050 C CB  . PRO B 1 42 ? 29.591  -11.956 -30.345 1.00 49.44  ? 41  PRO B CB  1 
ATOM   1051 C CG  . PRO B 1 42 ? 30.450  -11.940 -31.628 1.00 43.67  ? 41  PRO B CG  1 
ATOM   1052 C CD  . PRO B 1 42 ? 30.375  -13.342 -32.235 1.00 45.13  ? 41  PRO B CD  1 
ATOM   1053 N N   . ILE B 1 43 ? 26.324  -13.459 -30.170 1.00 41.29  ? 42  ILE B N   1 
ATOM   1054 C CA  . ILE B 1 43 ? 24.917  -13.237 -30.462 1.00 37.21  ? 42  ILE B CA  1 
ATOM   1055 C C   . ILE B 1 43 ? 24.302  -12.256 -29.471 1.00 43.25  ? 42  ILE B C   1 
ATOM   1056 O O   . ILE B 1 43 ? 24.438  -12.463 -28.265 1.00 41.11  ? 42  ILE B O   1 
ATOM   1057 C CB  . ILE B 1 43 ? 24.152  -14.556 -30.335 1.00 37.91  ? 42  ILE B CB  1 
ATOM   1058 C CG1 . ILE B 1 43 ? 24.788  -15.675 -31.188 1.00 32.80  ? 42  ILE B CG1 1 
ATOM   1059 C CG2 . ILE B 1 43 ? 22.676  -14.316 -30.649 1.00 41.63  ? 42  ILE B CG2 1 
ATOM   1060 C CD1 . ILE B 1 43 ? 25.058  -15.286 -32.640 1.00 32.42  ? 42  ILE B CD1 1 
ATOM   1061 N N   . PHE B 1 44 ? 23.581  -11.254 -30.009 1.00 38.18  ? 43  PHE B N   1 
ATOM   1062 C CA  . PHE B 1 44 ? 22.764  -10.310 -29.263 1.00 39.64  ? 43  PHE B CA  1 
ATOM   1063 C C   . PHE B 1 44 ? 21.301  -10.657 -29.540 1.00 38.19  ? 43  PHE B C   1 
ATOM   1064 O O   . PHE B 1 44 ? 20.926  -10.764 -30.709 1.00 42.81  ? 43  PHE B O   1 
ATOM   1065 C CB  . PHE B 1 44 ? 23.048  -8.854  -29.683 1.00 37.18  ? 43  PHE B CB  1 
ATOM   1066 C CG  . PHE B 1 44 ? 22.179  -7.820  -28.970 1.00 38.37  ? 43  PHE B CG  1 
ATOM   1067 C CD1 . PHE B 1 44 ? 20.975  -7.379  -29.527 1.00 42.84  ? 43  PHE B CD1 1 
ATOM   1068 C CD2 . PHE B 1 44 ? 22.551  -7.290  -27.740 1.00 46.69  ? 43  PHE B CD2 1 
ATOM   1069 C CE1 . PHE B 1 44 ? 20.157  -6.467  -28.862 1.00 41.00  ? 43  PHE B CE1 1 
ATOM   1070 C CE2 . PHE B 1 44 ? 21.746  -6.344  -27.089 1.00 40.21  ? 43  PHE B CE2 1 
ATOM   1071 C CZ  . PHE B 1 44 ? 20.558  -5.940  -27.647 1.00 42.34  ? 43  PHE B CZ  1 
ATOM   1072 N N   . PHE B 1 45 ? 20.499  -10.828 -28.469 1.00 35.42  ? 44  PHE B N   1 
ATOM   1073 C CA  . PHE B 1 45 ? 19.100  -11.245 -28.558 1.00 35.90  ? 44  PHE B CA  1 
ATOM   1074 C C   . PHE B 1 45 ? 18.177  -10.027 -28.462 1.00 36.91  ? 44  PHE B C   1 
ATOM   1075 O O   . PHE B 1 45 ? 18.208  -9.286  -27.483 1.00 40.47  ? 44  PHE B O   1 
ATOM   1076 C CB  . PHE B 1 45 ? 18.827  -12.258 -27.438 1.00 32.08  ? 44  PHE B CB  1 
ATOM   1077 C CG  . PHE B 1 45 ? 19.536  -13.607 -27.576 1.00 33.79  ? 44  PHE B CG  1 
ATOM   1078 C CD1 . PHE B 1 45 ? 20.829  -13.796 -27.105 1.00 34.83  ? 44  PHE B CD1 1 
ATOM   1079 C CD2 . PHE B 1 45 ? 18.889  -14.693 -28.146 1.00 33.41  ? 44  PHE B CD2 1 
ATOM   1080 C CE1 . PHE B 1 45 ? 21.443  -15.048 -27.202 1.00 41.31  ? 44  PHE B CE1 1 
ATOM   1081 C CE2 . PHE B 1 45 ? 19.501  -15.941 -28.240 1.00 37.06  ? 44  PHE B CE2 1 
ATOM   1082 C CZ  . PHE B 1 45 ? 20.789  -16.115 -27.805 1.00 34.60  ? 44  PHE B CZ  1 
ATOM   1083 N N   . PHE B 1 46 ? 17.353  -9.799  -29.483 1.00 35.34  ? 45  PHE B N   1 
ATOM   1084 C CA  . PHE B 1 46 ? 16.393  -8.707  -29.418 1.00 34.85  ? 45  PHE B CA  1 
ATOM   1085 C C   . PHE B 1 46 ? 15.435  -8.948  -28.245 1.00 40.96  ? 45  PHE B C   1 
ATOM   1086 O O   . PHE B 1 46 ? 15.248  -10.096 -27.819 1.00 37.65  ? 45  PHE B O   1 
ATOM   1087 C CB  . PHE B 1 46 ? 15.651  -8.555  -30.742 1.00 33.38  ? 45  PHE B CB  1 
ATOM   1088 C CG  . PHE B 1 46 ? 16.600  -8.089  -31.836 1.00 36.15  ? 45  PHE B CG  1 
ATOM   1089 C CD1 . PHE B 1 46 ? 17.116  -6.785  -31.825 1.00 39.35  ? 45  PHE B CD1 1 
ATOM   1090 C CD2 . PHE B 1 46 ? 17.024  -8.961  -32.833 1.00 32.28  ? 45  PHE B CD2 1 
ATOM   1091 C CE1 . PHE B 1 46 ? 17.992  -6.347  -32.812 1.00 34.50  ? 45  PHE B CE1 1 
ATOM   1092 C CE2 . PHE B 1 46 ? 17.908  -8.529  -33.811 1.00 35.95  ? 45  PHE B CE2 1 
ATOM   1093 C CZ  . PHE B 1 46 ? 18.349  -7.203  -33.822 1.00 31.73  ? 45  PHE B CZ  1 
ATOM   1094 N N   . GLY B 1 47 ? 14.839  -7.856  -27.728 1.00 39.53  ? 46  GLY B N   1 
ATOM   1095 C CA  . GLY B 1 47 ? 13.800  -7.935  -26.708 1.00 38.65  ? 46  GLY B CA  1 
ATOM   1096 C C   . GLY B 1 47 ? 14.406  -8.119  -25.319 1.00 40.09  ? 46  GLY B C   1 
ATOM   1097 O O   . GLY B 1 47 ? 14.157  -7.304  -24.448 1.00 37.54  ? 46  GLY B O   1 
ATOM   1098 N N   . THR B 1 48 ? 15.185  -9.190  -25.106 1.00 41.11  ? 47  THR B N   1 
ATOM   1099 C CA  . THR B 1 48 ? 15.789  -9.446  -23.802 1.00 38.41  ? 47  THR B CA  1 
ATOM   1100 C C   . THR B 1 48 ? 17.079  -8.652  -23.701 1.00 41.56  ? 47  THR B C   1 
ATOM   1101 O O   . THR B 1 48 ? 17.506  -8.315  -22.592 1.00 43.21  ? 47  THR B O   1 
ATOM   1102 C CB  . THR B 1 48 ? 16.101  -10.939 -23.605 1.00 37.76  ? 47  THR B CB  1 
ATOM   1103 O OG1 . THR B 1 48 ? 17.062  -11.255 -24.611 1.00 36.08  ? 47  THR B OG1 1 
ATOM   1104 C CG2 . THR B 1 48 ? 14.867  -11.823 -23.677 1.00 37.48  ? 47  THR B CG2 1 
ATOM   1105 N N   . HIS B 1 49 ? 17.734  -8.454  -24.856 1.00 43.15  ? 48  HIS B N   1 
ATOM   1106 C CA  . HIS B 1 49 ? 18.986  -7.712  -24.968 1.00 42.22  ? 48  HIS B CA  1 
ATOM   1107 C C   . HIS B 1 49 ? 20.104  -8.412  -24.201 1.00 41.17  ? 48  HIS B C   1 
ATOM   1108 O O   . HIS B 1 49 ? 21.036  -7.751  -23.760 1.00 48.00  ? 48  HIS B O   1 
ATOM   1109 C CB  . HIS B 1 49 ? 18.858  -6.272  -24.436 1.00 40.20  ? 48  HIS B CB  1 
ATOM   1110 C CG  . HIS B 1 49 ? 17.758  -5.515  -25.093 1.00 45.05  ? 48  HIS B CG  1 
ATOM   1111 N ND1 . HIS B 1 49 ? 17.010  -4.560  -24.439 1.00 44.46  ? 48  HIS B ND1 1 
ATOM   1112 C CD2 . HIS B 1 49 ? 17.272  -5.582  -26.353 1.00 39.68  ? 48  HIS B CD2 1 
ATOM   1113 C CE1 . HIS B 1 49 ? 16.089  -4.089  -25.274 1.00 53.86  ? 48  HIS B CE1 1 
ATOM   1114 N NE2 . HIS B 1 49 ? 16.230  -4.688  -26.446 1.00 49.00  ? 48  HIS B NE2 1 
ATOM   1115 N N   . GLU B 1 50 ? 20.000  -9.731  -24.015 1.00 46.57  ? 49  GLU B N   1 
ATOM   1116 C CA  . GLU B 1 50 ? 21.113  -10.510 -23.480 1.00 42.02  ? 49  GLU B CA  1 
ATOM   1117 C C   . GLU B 1 50 ? 22.036  -10.974 -24.608 1.00 41.49  ? 49  GLU B C   1 
ATOM   1118 O O   . GLU B 1 50 ? 21.718  -10.796 -25.777 1.00 40.82  ? 49  GLU B O   1 
ATOM   1119 C CB  . GLU B 1 50 ? 20.543  -11.695 -22.707 1.00 46.21  ? 49  GLU B CB  1 
ATOM   1120 C CG  . GLU B 1 50 ? 19.984  -11.289 -21.347 1.00 55.10  ? 49  GLU B CG  1 
ATOM   1121 C CD  . GLU B 1 50 ? 19.284  -12.451 -20.675 1.00 72.95  ? 49  GLU B CD  1 
ATOM   1122 O OE1 . GLU B 1 50 ? 19.298  -13.546 -21.264 1.00 91.29  ? 49  GLU B OE1 1 
ATOM   1123 O OE2 . GLU B 1 50 ? 18.700  -12.270 -19.587 1.00 87.89  ? 49  GLU B OE2 1 
ATOM   1124 N N   . THR B 1 51 ? 23.200  -11.540 -24.242 1.00 40.53  ? 50  THR B N   1 
ATOM   1125 C CA  . THR B 1 51 ? 24.181  -12.042 -25.190 1.00 39.62  ? 50  THR B CA  1 
ATOM   1126 C C   . THR B 1 51 ? 24.586  -13.458 -24.775 1.00 40.14  ? 50  THR B C   1 
ATOM   1127 O O   . THR B 1 51 ? 24.445  -13.841 -23.629 1.00 45.98  ? 50  THR B O   1 
ATOM   1128 C CB  . THR B 1 51 ? 25.406  -11.124 -25.294 1.00 44.60  ? 50  THR B CB  1 
ATOM   1129 O OG1 . THR B 1 51 ? 26.060  -11.113 -24.030 1.00 46.91  ? 50  THR B OG1 1 
ATOM   1130 C CG2 . THR B 1 51 ? 25.073  -9.673  -25.594 1.00 49.22  ? 50  THR B CG2 1 
ATOM   1131 N N   . ALA B 1 52 ? 25.061  -14.235 -25.745 1.00 39.55  ? 51  ALA B N   1 
ATOM   1132 C CA  . ALA B 1 52 ? 25.630  -15.560 -25.567 1.00 40.43  ? 51  ALA B CA  1 
ATOM   1133 C C   . ALA B 1 52 ? 26.469  -15.855 -26.809 1.00 41.61  ? 51  ALA B C   1 
ATOM   1134 O O   . ALA B 1 52 ? 26.383  -15.128 -27.789 1.00 47.91  ? 51  ALA B O   1 
ATOM   1135 C CB  . ALA B 1 52 ? 24.548  -16.598 -25.408 1.00 35.57  ? 51  ALA B CB  1 
ATOM   1136 N N   . PHE B 1 53 ? 27.258  -16.926 -26.761 1.00 45.24  ? 52  PHE B N   1 
ATOM   1137 C CA  . PHE B 1 53 ? 28.005  -17.402 -27.915 1.00 48.54  ? 52  PHE B CA  1 
ATOM   1138 C C   . PHE B 1 53 ? 27.291  -18.628 -28.469 1.00 48.48  ? 52  PHE B C   1 
ATOM   1139 O O   . PHE B 1 53 ? 26.882  -19.500 -27.707 1.00 52.93  ? 52  PHE B O   1 
ATOM   1140 C CB  . PHE B 1 53 ? 29.418  -17.803 -27.468 1.00 50.09  ? 52  PHE B CB  1 
ATOM   1141 C CG  . PHE B 1 53 ? 30.243  -16.637 -26.948 1.00 46.10  ? 52  PHE B CG  1 
ATOM   1142 C CD1 . PHE B 1 53 ? 30.460  -15.519 -27.747 1.00 45.27  ? 52  PHE B CD1 1 
ATOM   1143 C CD2 . PHE B 1 53 ? 30.721  -16.627 -25.638 1.00 48.97  ? 52  PHE B CD2 1 
ATOM   1144 C CE1 . PHE B 1 53 ? 31.168  -14.437 -27.266 1.00 47.41  ? 52  PHE B CE1 1 
ATOM   1145 C CE2 . PHE B 1 53 ? 31.434  -15.534 -25.159 1.00 52.04  ? 52  PHE B CE2 1 
ATOM   1146 C CZ  . PHE B 1 53 ? 31.662  -14.449 -25.972 1.00 52.04  ? 52  PHE B CZ  1 
ATOM   1147 N N   . LEU B 1 54 ? 27.131  -18.680 -29.800 1.00 46.91  ? 53  LEU B N   1 
ATOM   1148 C CA  . LEU B 1 54 ? 26.446  -19.785 -30.450 1.00 39.89  ? 53  LEU B CA  1 
ATOM   1149 C C   . LEU B 1 54 ? 27.182  -20.168 -31.738 1.00 39.16  ? 53  LEU B C   1 
ATOM   1150 O O   . LEU B 1 54 ? 27.667  -19.300 -32.451 1.00 42.79  ? 53  LEU B O   1 
ATOM   1151 C CB  . LEU B 1 54 ? 24.999  -19.374 -30.726 1.00 38.99  ? 53  LEU B CB  1 
ATOM   1152 C CG  . LEU B 1 54 ? 23.974  -19.506 -29.588 1.00 41.06  ? 53  LEU B CG  1 
ATOM   1153 C CD1 . LEU B 1 54 ? 22.600  -19.268 -30.213 1.00 33.24  ? 53  LEU B CD1 1 
ATOM   1154 C CD2 . LEU B 1 54 ? 23.938  -20.854 -28.844 1.00 37.23  ? 53  LEU B CD2 1 
ATOM   1155 N N   . GLY B 1 55 ? 27.256  -21.478 -32.023 1.00 41.08  ? 54  GLY B N   1 
ATOM   1156 C CA  . GLY B 1 55 ? 27.726  -21.963 -33.311 1.00 38.97  ? 54  GLY B CA  1 
ATOM   1157 C C   . GLY B 1 55 ? 26.631  -21.935 -34.382 1.00 36.13  ? 54  GLY B C   1 
ATOM   1158 O O   . GLY B 1 55 ? 25.440  -21.880 -34.084 1.00 43.99  ? 54  GLY B O   1 
ATOM   1159 N N   . PRO B 1 56 ? 26.993  -22.020 -35.678 1.00 38.78  ? 55  PRO B N   1 
ATOM   1160 C CA  . PRO B 1 56 ? 26.007  -21.939 -36.761 1.00 37.98  ? 55  PRO B CA  1 
ATOM   1161 C C   . PRO B 1 56 ? 24.842  -22.919 -36.741 1.00 37.38  ? 55  PRO B C   1 
ATOM   1162 O O   . PRO B 1 56 ? 23.825  -22.648 -37.371 1.00 43.62  ? 55  PRO B O   1 
ATOM   1163 C CB  . PRO B 1 56 ? 26.897  -22.176 -37.979 1.00 40.79  ? 55  PRO B CB  1 
ATOM   1164 C CG  . PRO B 1 56 ? 28.224  -21.640 -37.543 1.00 40.07  ? 55  PRO B CG  1 
ATOM   1165 C CD  . PRO B 1 56 ? 28.368  -22.222 -36.164 1.00 38.19  ? 55  PRO B CD  1 
ATOM   1166 N N   . LYS B 1 57 ? 24.979  -24.052 -36.026 1.00 38.82  ? 56  LYS B N   1 
ATOM   1167 C CA  . LYS B 1 57 ? 23.917  -25.065 -36.029 1.00 38.48  ? 56  LYS B CA  1 
ATOM   1168 C C   . LYS B 1 57 ? 22.639  -24.526 -35.365 1.00 35.83  ? 56  LYS B C   1 
ATOM   1169 O O   . LYS B 1 57 ? 21.538  -25.001 -35.670 1.00 36.33  ? 56  LYS B O   1 
ATOM   1170 C CB  . LYS B 1 57 ? 24.335  -26.404 -35.398 1.00 43.57  ? 56  LYS B CB  1 
ATOM   1171 C CG  . LYS B 1 57 ? 24.562  -26.434 -33.891 1.00 42.53  ? 56  LYS B CG  1 
ATOM   1172 C CD  . LYS B 1 57 ? 24.433  -27.820 -33.266 1.00 49.28  ? 56  LYS B CD  1 
ATOM   1173 C CE  . LYS B 1 57 ? 24.806  -27.893 -31.820 1.00 50.80  ? 56  LYS B CE  1 
ATOM   1174 N NZ  . LYS B 1 57 ? 23.660  -27.471 -31.005 1.00 64.13  ? 56  LYS B NZ  1 
ATOM   1175 N N   . ASP B 1 58 ? 22.823  -23.517 -34.502 1.00 31.21  ? 57  ASP B N   1 
ATOM   1176 C CA  . ASP B 1 58 ? 21.790  -22.862 -33.718 1.00 41.36  ? 57  ASP B CA  1 
ATOM   1177 C C   . ASP B 1 58 ? 21.450  -21.497 -34.303 1.00 38.38  ? 57  ASP B C   1 
ATOM   1178 O O   . ASP B 1 58 ? 20.750  -20.716 -33.652 1.00 40.77  ? 57  ASP B O   1 
ATOM   1179 C CB  . ASP B 1 58 ? 22.189  -22.738 -32.248 1.00 33.61  ? 57  ASP B CB  1 
ATOM   1180 C CG  . ASP B 1 58 ? 22.275  -24.089 -31.550 1.00 40.83  ? 57  ASP B CG  1 
ATOM   1181 O OD1 . ASP B 1 58 ? 21.358  -24.907 -31.758 1.00 42.05  ? 57  ASP B OD1 1 
ATOM   1182 O OD2 . ASP B 1 58 ? 23.274  -24.342 -30.846 1.00 41.94  ? 57  ASP B OD2 1 
ATOM   1183 N N   . LEU B 1 59 ? 21.933  -21.217 -35.518 1.00 34.47  ? 58  LEU B N   1 
ATOM   1184 C CA  . LEU B 1 59 ? 21.734  -19.895 -36.093 1.00 38.48  ? 58  LEU B CA  1 
ATOM   1185 C C   . LEU B 1 59 ? 20.990  -20.006 -37.412 1.00 34.97  ? 58  LEU B C   1 
ATOM   1186 O O   . LEU B 1 59 ? 21.495  -20.620 -38.326 1.00 35.61  ? 58  LEU B O   1 
ATOM   1187 C CB  . LEU B 1 59 ? 23.057  -19.142 -36.266 1.00 34.98  ? 58  LEU B CB  1 
ATOM   1188 C CG  . LEU B 1 59 ? 23.842  -18.866 -34.980 1.00 36.77  ? 58  LEU B CG  1 
ATOM   1189 C CD1 . LEU B 1 59 ? 25.212  -18.248 -35.296 1.00 33.78  ? 58  LEU B CD1 1 
ATOM   1190 C CD2 . LEU B 1 59 ? 23.053  -17.958 -34.021 1.00 32.41  ? 58  LEU B CD2 1 
ATOM   1191 N N   . PHE B 1 60 ? 19.856  -19.314 -37.541 1.00 37.04  ? 59  PHE B N   1 
ATOM   1192 C CA  . PHE B 1 60 ? 18.984  -19.497 -38.694 1.00 34.06  ? 59  PHE B CA  1 
ATOM   1193 C C   . PHE B 1 60 ? 18.774  -18.157 -39.394 1.00 39.53  ? 59  PHE B C   1 
ATOM   1194 O O   . PHE B 1 60 ? 18.074  -17.300 -38.863 1.00 40.29  ? 59  PHE B O   1 
ATOM   1195 C CB  . PHE B 1 60 ? 17.650  -20.064 -38.197 1.00 35.08  ? 59  PHE B CB  1 
ATOM   1196 C CG  . PHE B 1 60 ? 17.694  -21.465 -37.581 1.00 35.55  ? 59  PHE B CG  1 
ATOM   1197 C CD1 . PHE B 1 60 ? 18.118  -21.675 -36.259 1.00 39.79  ? 59  PHE B CD1 1 
ATOM   1198 C CD2 . PHE B 1 60 ? 17.241  -22.571 -38.299 1.00 40.20  ? 59  PHE B CD2 1 
ATOM   1199 C CE1 . PHE B 1 60 ? 18.133  -22.957 -35.695 1.00 34.16  ? 59  PHE B CE1 1 
ATOM   1200 C CE2 . PHE B 1 60 ? 17.246  -23.855 -37.734 1.00 36.14  ? 59  PHE B CE2 1 
ATOM   1201 C CZ  . PHE B 1 60 ? 17.693  -24.043 -36.448 1.00 32.47  ? 59  PHE B CZ  1 
ATOM   1202 N N   . PRO B 1 61 ? 19.349  -17.919 -40.603 1.00 45.45  ? 60  PRO B N   1 
ATOM   1203 C CA  . PRO B 1 61 ? 19.141  -16.649 -41.316 1.00 41.85  ? 60  PRO B CA  1 
ATOM   1204 C C   . PRO B 1 61 ? 17.688  -16.179 -41.273 1.00 45.22  ? 60  PRO B C   1 
ATOM   1205 O O   . PRO B 1 61 ? 16.766  -16.937 -41.589 1.00 42.27  ? 60  PRO B O   1 
ATOM   1206 C CB  . PRO B 1 61 ? 19.619  -17.002 -42.736 1.00 44.64  ? 60  PRO B CB  1 
ATOM   1207 C CG  . PRO B 1 61 ? 20.771  -17.949 -42.459 1.00 47.42  ? 60  PRO B CG  1 
ATOM   1208 C CD  . PRO B 1 61 ? 20.221  -18.848 -41.354 1.00 43.35  ? 60  PRO B CD  1 
ATOM   1209 N N   . TYR B 1 62 ? 17.501  -14.921 -40.845 1.00 40.65  ? 61  TYR B N   1 
ATOM   1210 C CA  . TYR B 1 62 ? 16.181  -14.399 -40.551 1.00 42.17  ? 61  TYR B CA  1 
ATOM   1211 C C   . TYR B 1 62 ? 15.224  -14.534 -41.736 1.00 50.61  ? 61  TYR B C   1 
ATOM   1212 O O   . TYR B 1 62 ? 14.099  -15.024 -41.558 1.00 50.88  ? 61  TYR B O   1 
ATOM   1213 C CB  . TYR B 1 62 ? 16.321  -12.955 -40.086 1.00 43.58  ? 61  TYR B CB  1 
ATOM   1214 C CG  . TYR B 1 62 ? 14.991  -12.255 -39.871 1.00 49.43  ? 61  TYR B CG  1 
ATOM   1215 C CD1 . TYR B 1 62 ? 14.214  -12.533 -38.758 1.00 45.16  ? 61  TYR B CD1 1 
ATOM   1216 C CD2 . TYR B 1 62 ? 14.544  -11.291 -40.766 1.00 57.89  ? 61  TYR B CD2 1 
ATOM   1217 C CE1 . TYR B 1 62 ? 13.013  -11.888 -38.540 1.00 50.35  ? 61  TYR B CE1 1 
ATOM   1218 C CE2 . TYR B 1 62 ? 13.345  -10.634 -40.564 1.00 59.45  ? 61  TYR B CE2 1 
ATOM   1219 C CZ  . TYR B 1 62 ? 12.592  -10.936 -39.444 1.00 50.04  ? 61  TYR B CZ  1 
ATOM   1220 O OH  . TYR B 1 62 ? 11.426  -10.300 -39.251 1.00 54.23  ? 61  TYR B OH  1 
ATOM   1221 N N   . ASP B 1 63 ? 15.665  -14.102 -42.933 1.00 49.36  ? 62  ASP B N   1 
ATOM   1222 C CA  . ASP B 1 63 ? 14.762  -14.029 -44.077 1.00 54.00  ? 62  ASP B CA  1 
ATOM   1223 C C   . ASP B 1 63 ? 14.232  -15.405 -44.469 1.00 47.48  ? 62  ASP B C   1 
ATOM   1224 O O   . ASP B 1 63 ? 13.040  -15.544 -44.699 1.00 52.35  ? 62  ASP B O   1 
ATOM   1225 C CB  . ASP B 1 63 ? 15.275  -13.129 -45.184 1.00 52.63  ? 62  ASP B CB  1 
ATOM   1226 C CG  . ASP B 1 63 ? 15.249  -11.657 -44.798 1.00 71.65  ? 62  ASP B CG  1 
ATOM   1227 O OD1 . ASP B 1 63 ? 16.331  -11.034 -44.788 1.00 77.08  ? 62  ASP B OD1 1 
ATOM   1228 O OD2 . ASP B 1 63 ? 14.146  -11.153 -44.462 1.00 77.78  ? 62  ASP B OD2 1 
ATOM   1229 N N   . LYS B 1 64 ? 15.101  -16.420 -44.490 1.00 48.24  ? 63  LYS B N   1 
ATOM   1230 C CA  . LYS B 1 64 ? 14.665  -17.772 -44.833 1.00 46.30  ? 63  LYS B CA  1 
ATOM   1231 C C   . LYS B 1 64 ? 13.624  -18.298 -43.828 1.00 47.66  ? 63  LYS B C   1 
ATOM   1232 O O   . LYS B 1 64 ? 12.716  -19.043 -44.195 1.00 52.44  ? 63  LYS B O   1 
ATOM   1233 C CB  . LYS B 1 64 ? 15.886  -18.685 -44.997 1.00 43.33  ? 63  LYS B CB  1 
ATOM   1234 C CG  . LYS B 1 64 ? 15.569  -20.151 -45.308 1.00 45.76  ? 63  LYS B CG  1 
ATOM   1235 C CD  . LYS B 1 64 ? 16.844  -20.958 -45.485 1.00 46.96  ? 63  LYS B CD  1 
ATOM   1236 C CE  . LYS B 1 64 ? 16.660  -22.260 -46.186 1.00 50.79  ? 63  LYS B CE  1 
ATOM   1237 N NZ  . LYS B 1 64 ? 15.406  -22.920 -45.849 1.00 50.77  ? 63  LYS B NZ  1 
ATOM   1238 N N   . SER B 1 65 ? 13.752  -17.929 -42.549 1.00 48.23  ? 64  SER B N   1 
ATOM   1239 C CA  . SER B 1 65 ? 13.089  -18.717 -41.520 1.00 44.46  ? 64  SER B CA  1 
ATOM   1240 C C   . SER B 1 65 ? 12.098  -17.895 -40.705 1.00 45.52  ? 64  SER B C   1 
ATOM   1241 O O   . SER B 1 65 ? 11.607  -18.375 -39.702 1.00 40.79  ? 64  SER B O   1 
ATOM   1242 C CB  . SER B 1 65 ? 14.060  -19.496 -40.661 1.00 44.94  ? 64  SER B CB  1 
ATOM   1243 O OG  . SER B 1 65 ? 14.975  -18.650 -39.988 1.00 54.26  ? 64  SER B OG  1 
ATOM   1244 N N   . LYS B 1 66 ? 11.735  -16.710 -41.207 1.00 45.13  ? 65  LYS B N   1 
ATOM   1245 C CA  . LYS B 1 66 ? 10.910  -15.760 -40.481 1.00 49.31  ? 65  LYS B CA  1 
ATOM   1246 C C   . LYS B 1 66 ? 9.450   -16.215 -40.442 1.00 55.43  ? 65  LYS B C   1 
ATOM   1247 O O   . LYS B 1 66 ? 8.706   -15.848 -39.533 1.00 59.33  ? 65  LYS B O   1 
ATOM   1248 C CB  . LYS B 1 66 ? 11.199  -14.394 -41.105 1.00 50.27  ? 65  LYS B CB  1 
ATOM   1249 C CG  . LYS B 1 66 ? 10.081  -13.405 -41.217 1.00 61.19  ? 65  LYS B CG  1 
ATOM   1250 C CD  . LYS B 1 66 ? 10.499  -12.320 -42.199 1.00 69.87  ? 65  LYS B CD  1 
ATOM   1251 C CE  . LYS B 1 66 ? 10.613  -12.836 -43.599 1.00 74.27  ? 65  LYS B CE  1 
ATOM   1252 N NZ  . LYS B 1 66 ? 11.383  -11.861 -44.367 1.00 78.53  ? 65  LYS B NZ  1 
ATOM   1253 N N   . ASP B 1 67 ? 9.027   -17.046 -41.399 1.00 58.21  ? 66  ASP B N   1 
ATOM   1254 C CA  . ASP B 1 67 ? 7.616   -17.402 -41.395 1.00 59.47  ? 66  ASP B CA  1 
ATOM   1255 C C   . ASP B 1 67 ? 7.377   -18.588 -40.460 1.00 57.77  ? 66  ASP B C   1 
ATOM   1256 O O   . ASP B 1 67 ? 6.276   -18.754 -39.945 1.00 59.92  ? 66  ASP B O   1 
ATOM   1257 C CB  . ASP B 1 67 ? 6.994   -17.429 -42.786 1.00 69.95  ? 66  ASP B CB  1 
ATOM   1258 C CG  . ASP B 1 67 ? 7.576   -18.424 -43.777 1.00 81.75  ? 66  ASP B CG  1 
ATOM   1259 O OD1 . ASP B 1 67 ? 7.838   -18.007 -44.925 1.00 93.62  ? 66  ASP B OD1 1 
ATOM   1260 O OD2 . ASP B 1 67 ? 7.738   -19.606 -43.402 1.00 83.35  ? 66  ASP B OD2 1 
ATOM   1261 N N   . LYS B 1 68 ? 8.428   -19.379 -40.208 1.00 47.15  ? 67  LYS B N   1 
ATOM   1262 C CA  . LYS B 1 68 ? 8.368   -20.497 -39.282 1.00 43.41  ? 67  LYS B CA  1 
ATOM   1263 C C   . LYS B 1 68 ? 8.551   -20.012 -37.845 1.00 44.32  ? 67  LYS B C   1 
ATOM   1264 O O   . LYS B 1 68 ? 7.902   -20.518 -36.942 1.00 53.38  ? 67  LYS B O   1 
ATOM   1265 C CB  . LYS B 1 68 ? 9.509   -21.438 -39.684 1.00 45.15  ? 67  LYS B CB  1 
ATOM   1266 C CG  . LYS B 1 68 ? 9.484   -22.849 -39.155 1.00 58.97  ? 67  LYS B CG  1 
ATOM   1267 C CD  . LYS B 1 68 ? 10.204  -23.777 -40.140 1.00 70.08  ? 67  LYS B CD  1 
ATOM   1268 C CE  . LYS B 1 68 ? 10.788  -25.017 -39.508 1.00 75.94  ? 67  LYS B CE  1 
ATOM   1269 N NZ  . LYS B 1 68 ? 9.849   -25.780 -38.672 1.00 74.59  ? 67  LYS B NZ  1 
ATOM   1270 N N   . TYR B 1 69 ? 9.468   -19.065 -37.609 1.00 42.18  ? 68  TYR B N   1 
ATOM   1271 C CA  . TYR B 1 69 ? 9.826   -18.736 -36.231 1.00 42.46  ? 68  TYR B CA  1 
ATOM   1272 C C   . TYR B 1 69 ? 9.282   -17.367 -35.782 1.00 40.34  ? 68  TYR B C   1 
ATOM   1273 O O   . TYR B 1 69 ? 9.258   -17.071 -34.594 1.00 38.19  ? 68  TYR B O   1 
ATOM   1274 C CB  . TYR B 1 69 ? 11.345  -18.885 -36.129 1.00 38.67  ? 68  TYR B CB  1 
ATOM   1275 C CG  . TYR B 1 69 ? 11.924  -20.274 -36.389 1.00 41.46  ? 68  TYR B CG  1 
ATOM   1276 C CD1 . TYR B 1 69 ? 11.426  -21.421 -35.765 1.00 46.30  ? 68  TYR B CD1 1 
ATOM   1277 C CD2 . TYR B 1 69 ? 12.989  -20.428 -37.266 1.00 38.25  ? 68  TYR B CD2 1 
ATOM   1278 C CE1 . TYR B 1 69 ? 11.967  -22.677 -36.007 1.00 42.26  ? 68  TYR B CE1 1 
ATOM   1279 C CE2 . TYR B 1 69 ? 13.544  -21.669 -37.513 1.00 42.98  ? 68  TYR B CE2 1 
ATOM   1280 C CZ  . TYR B 1 69 ? 13.027  -22.793 -36.893 1.00 46.85  ? 68  TYR B CZ  1 
ATOM   1281 O OH  . TYR B 1 69 ? 13.640  -23.978 -37.158 1.00 48.01  ? 68  TYR B OH  1 
ATOM   1282 N N   . GLY B 1 70 ? 8.817   -16.534 -36.714 1.00 42.01  ? 69  GLY B N   1 
ATOM   1283 C CA  . GLY B 1 70 ? 8.435   -15.162 -36.388 1.00 47.95  ? 69  GLY B CA  1 
ATOM   1284 C C   . GLY B 1 70 ? 7.044   -15.003 -35.763 1.00 55.66  ? 69  GLY B C   1 
ATOM   1285 O O   . GLY B 1 70 ? 6.443   -13.943 -35.892 1.00 62.76  ? 69  GLY B O   1 
ATOM   1286 N N   . LYS B 1 71 ? 6.531   -16.019 -35.063 1.00 52.37  ? 70  LYS B N   1 
ATOM   1287 C CA  . LYS B 1 71 ? 5.192   -15.912 -34.508 1.00 61.43  ? 70  LYS B CA  1 
ATOM   1288 C C   . LYS B 1 71 ? 5.224   -15.433 -33.058 1.00 55.33  ? 70  LYS B C   1 
ATOM   1289 O O   . LYS B 1 71 ? 5.959   -15.966 -32.234 1.00 52.24  ? 70  LYS B O   1 
ATOM   1290 C CB  . LYS B 1 71 ? 4.420   -17.233 -34.516 1.00 65.38  ? 70  LYS B CB  1 
ATOM   1291 C CG  . LYS B 1 71 ? 3.471   -17.384 -35.688 1.00 72.95  ? 70  LYS B CG  1 
ATOM   1292 C CD  . LYS B 1 71 ? 4.195   -17.507 -37.015 1.00 75.31  ? 70  LYS B CD  1 
ATOM   1293 C CE  . LYS B 1 71 ? 3.223   -17.672 -38.130 1.00 84.51  ? 70  LYS B CE  1 
ATOM   1294 N NZ  . LYS B 1 71 ? 3.878   -17.476 -39.426 1.00 76.81  ? 70  LYS B NZ  1 
ATOM   1295 N N   . PRO B 1 72 ? 4.390   -14.437 -32.690 1.00 55.75  ? 71  PRO B N   1 
ATOM   1296 C CA  . PRO B 1 72 ? 4.336   -13.953 -31.306 1.00 51.37  ? 71  PRO B CA  1 
ATOM   1297 C C   . PRO B 1 72 ? 4.063   -15.099 -30.336 1.00 53.92  ? 71  PRO B C   1 
ATOM   1298 O O   . PRO B 1 72 ? 3.354   -16.039 -30.678 1.00 51.17  ? 71  PRO B O   1 
ATOM   1299 C CB  . PRO B 1 72 ? 3.227   -12.882 -31.288 1.00 55.79  ? 71  PRO B CB  1 
ATOM   1300 C CG  . PRO B 1 72 ? 2.992   -12.549 -32.750 1.00 62.58  ? 71  PRO B CG  1 
ATOM   1301 C CD  . PRO B 1 72 ? 3.483   -13.717 -33.598 1.00 55.47  ? 71  PRO B CD  1 
ATOM   1302 N N   . ASN B 1 73 ? 4.689   -15.040 -29.155 1.00 46.41  ? 72  ASN B N   1 
ATOM   1303 C CA  . ASN B 1 73 ? 4.453   -16.014 -28.096 1.00 45.51  ? 72  ASN B CA  1 
ATOM   1304 C C   . ASN B 1 73 ? 4.438   -15.310 -26.733 1.00 53.37  ? 72  ASN B C   1 
ATOM   1305 O O   . ASN B 1 73 ? 4.684   -14.102 -26.639 1.00 54.85  ? 72  ASN B O   1 
ATOM   1306 C CB  . ASN B 1 73 ? 5.407   -17.199 -28.182 1.00 39.94  ? 72  ASN B CB  1 
ATOM   1307 C CG  . ASN B 1 73 ? 6.845   -16.825 -27.921 1.00 44.20  ? 72  ASN B CG  1 
ATOM   1308 O OD1 . ASN B 1 73 ? 7.168   -16.253 -26.874 1.00 43.32  ? 72  ASN B OD1 1 
ATOM   1309 N ND2 . ASN B 1 73 ? 7.729   -17.136 -28.855 1.00 45.30  ? 72  ASN B ND2 1 
ATOM   1310 N N   . LYS B 1 74 ? 4.187   -16.092 -25.675 1.00 45.90  ? 73  LYS B N   1 
ATOM   1311 C CA  . LYS B 1 74 ? 3.961   -15.548 -24.347 1.00 49.26  ? 73  LYS B CA  1 
ATOM   1312 C C   . LYS B 1 74 ? 5.280   -15.409 -23.575 1.00 50.86  ? 73  LYS B C   1 
ATOM   1313 O O   . LYS B 1 74 ? 5.270   -15.085 -22.386 1.00 45.57  ? 73  LYS B O   1 
ATOM   1314 C CB  . LYS B 1 74 ? 2.885   -16.380 -23.626 1.00 45.71  ? 73  LYS B CB  1 
ATOM   1315 N N   . ARG B 1 75 ? 6.422   -15.664 -24.230 1.00 46.39  ? 74  ARG B N   1 
ATOM   1316 C CA  . ARG B 1 75 ? 7.693   -15.569 -23.521 1.00 46.45  ? 74  ARG B CA  1 
ATOM   1317 C C   . ARG B 1 75 ? 8.095   -14.099 -23.398 1.00 50.48  ? 74  ARG B C   1 
ATOM   1318 O O   . ARG B 1 75 ? 7.980   -13.331 -24.363 1.00 45.28  ? 74  ARG B O   1 
ATOM   1319 C CB  . ARG B 1 75 ? 8.829   -16.374 -24.162 1.00 44.98  ? 74  ARG B CB  1 
ATOM   1320 C CG  . ARG B 1 75 ? 8.614   -17.847 -24.470 1.00 45.41  ? 74  ARG B CG  1 
ATOM   1321 C CD  . ARG B 1 75 ? 8.390   -18.580 -23.187 1.00 54.60  ? 74  ARG B CD  1 
ATOM   1322 N NE  . ARG B 1 75 ? 8.426   -20.017 -23.463 1.00 58.47  ? 74  ARG B NE  1 
ATOM   1323 C CZ  . ARG B 1 75 ? 9.456   -20.756 -23.153 1.00 51.29  ? 74  ARG B CZ  1 
ATOM   1324 N NH1 . ARG B 1 75 ? 10.507  -20.213 -22.575 1.00 58.56  ? 74  ARG B NH1 1 
ATOM   1325 N NH2 . ARG B 1 75 ? 9.437   -22.030 -23.452 1.00 57.79  ? 74  ARG B NH2 1 
ATOM   1326 N N   . LYS B 1 76 ? 8.558   -13.737 -22.191 1.00 46.42  ? 75  LYS B N   1 
ATOM   1327 C CA  . LYS B 1 76 ? 8.964   -12.382 -21.867 1.00 41.44  ? 75  LYS B CA  1 
ATOM   1328 C C   . LYS B 1 76 ? 10.110  -11.949 -22.780 1.00 36.00  ? 75  LYS B C   1 
ATOM   1329 O O   . LYS B 1 76 ? 11.165  -12.597 -22.799 1.00 36.42  ? 75  LYS B O   1 
ATOM   1330 C CB  . LYS B 1 76 ? 9.480   -12.261 -20.432 1.00 41.14  ? 75  LYS B CB  1 
ATOM   1331 C CG  . LYS B 1 76 ? 9.824   -10.802 -20.066 1.00 45.85  ? 75  LYS B CG  1 
ATOM   1332 C CD  . LYS B 1 76 ? 10.641  -10.631 -18.798 1.00 52.46  ? 75  LYS B CD  1 
ATOM   1333 C CE  . LYS B 1 76 ? 11.138  -9.228  -18.582 1.00 55.53  ? 75  LYS B CE  1 
ATOM   1334 N NZ  . LYS B 1 76 ? 11.768  -9.123  -17.261 1.00 63.35  ? 75  LYS B NZ  1 
ATOM   1335 N N   . GLY B 1 77 ? 9.903   -10.814 -23.460 1.00 36.33  ? 76  GLY B N   1 
ATOM   1336 C CA  . GLY B 1 77 ? 10.886  -10.200 -24.358 1.00 38.26  ? 76  GLY B CA  1 
ATOM   1337 C C   . GLY B 1 77 ? 10.665  -10.559 -25.837 1.00 41.11  ? 76  GLY B C   1 
ATOM   1338 O O   . GLY B 1 77 ? 11.246  -9.936  -26.713 1.00 41.05  ? 76  GLY B O   1 
ATOM   1339 N N   . PHE B 1 78 ? 9.801   -11.547 -26.133 1.00 42.49  ? 77  PHE B N   1 
ATOM   1340 C CA  . PHE B 1 78 ? 9.753   -12.148 -27.460 1.00 37.37  ? 77  PHE B CA  1 
ATOM   1341 C C   . PHE B 1 78 ? 9.106   -11.193 -28.447 1.00 39.89  ? 77  PHE B C   1 
ATOM   1342 O O   . PHE B 1 78 ? 9.646   -10.911 -29.516 1.00 36.20  ? 77  PHE B O   1 
ATOM   1343 C CB  . PHE B 1 78 ? 8.970   -13.464 -27.493 1.00 35.88  ? 77  PHE B CB  1 
ATOM   1344 C CG  . PHE B 1 78 ? 9.303   -14.264 -28.742 1.00 35.99  ? 77  PHE B CG  1 
ATOM   1345 C CD1 . PHE B 1 78 ? 10.472  -15.031 -28.812 1.00 36.45  ? 77  PHE B CD1 1 
ATOM   1346 C CD2 . PHE B 1 78 ? 8.490   -14.182 -29.866 1.00 37.53  ? 77  PHE B CD2 1 
ATOM   1347 C CE1 . PHE B 1 78 ? 10.767  -15.773 -29.955 1.00 35.16  ? 77  PHE B CE1 1 
ATOM   1348 C CE2 . PHE B 1 78 ? 8.812   -14.884 -31.022 1.00 44.25  ? 77  PHE B CE2 1 
ATOM   1349 C CZ  . PHE B 1 78 ? 9.946   -15.692 -31.053 1.00 39.10  ? 77  PHE B CZ  1 
ATOM   1350 N N   . ASN B 1 79 ? 7.938   -10.679 -28.073 1.00 42.46  ? 78  ASN B N   1 
ATOM   1351 C CA  . ASN B 1 79 ? 7.247   -9.794  -28.995 1.00 41.25  ? 78  ASN B CA  1 
ATOM   1352 C C   . ASN B 1 79 ? 8.012   -8.488  -29.176 1.00 37.41  ? 78  ASN B C   1 
ATOM   1353 O O   . ASN B 1 79 ? 7.928   -7.880  -30.230 1.00 42.62  ? 78  ASN B O   1 
ATOM   1354 C CB  . ASN B 1 79 ? 5.792   -9.642  -28.592 1.00 42.56  ? 78  ASN B CB  1 
ATOM   1355 C CG  . ASN B 1 79 ? 5.128   -11.001 -28.634 1.00 51.34  ? 78  ASN B CG  1 
ATOM   1356 O OD1 . ASN B 1 79 ? 5.698   -11.971 -29.157 1.00 47.78  ? 78  ASN B OD1 1 
ATOM   1357 N ND2 . ASN B 1 79 ? 3.919   -11.090 -28.109 1.00 55.64  ? 78  ASN B ND2 1 
ATOM   1358 N N   . GLU B 1 80 ? 8.766   -8.068  -28.155 1.00 38.89  ? 79  GLU B N   1 
ATOM   1359 C CA  . GLU B 1 80 ? 9.547   -6.847  -28.268 1.00 37.91  ? 79  GLU B CA  1 
ATOM   1360 C C   . GLU B 1 80 ? 10.716  -7.116  -29.215 1.00 38.06  ? 79  GLU B C   1 
ATOM   1361 O O   . GLU B 1 80 ? 11.082  -6.258  -30.010 1.00 36.25  ? 79  GLU B O   1 
ATOM   1362 C CB  . GLU B 1 80 ? 10.109  -6.360  -26.934 1.00 35.50  ? 79  GLU B CB  1 
ATOM   1363 C CG  . GLU B 1 80 ? 9.062   -5.665  -26.075 1.00 48.09  ? 79  GLU B CG  1 
ATOM   1364 N N   . GLY B 1 81 ? 11.280  -8.322  -29.109 1.00 30.71  ? 80  GLY B N   1 
ATOM   1365 C CA  . GLY B 1 81 ? 12.379  -8.756  -29.941 1.00 30.03  ? 80  GLY B CA  1 
ATOM   1366 C C   . GLY B 1 81 ? 11.963  -8.797  -31.404 1.00 33.82  ? 80  GLY B C   1 
ATOM   1367 O O   . GLY B 1 81 ? 12.734  -8.380  -32.263 1.00 36.42  ? 80  GLY B O   1 
ATOM   1368 N N   . LEU B 1 82 ? 10.754  -9.316  -31.650 1.00 32.06  ? 81  LEU B N   1 
ATOM   1369 C CA  . LEU B 1 82 ? 10.171  -9.364  -32.982 1.00 36.52  ? 81  LEU B CA  1 
ATOM   1370 C C   . LEU B 1 82 ? 10.040  -7.937  -33.516 1.00 37.89  ? 81  LEU B C   1 
ATOM   1371 O O   . LEU B 1 82 ? 10.285  -7.698  -34.689 1.00 45.39  ? 81  LEU B O   1 
ATOM   1372 C CB  . LEU B 1 82 ? 8.819   -10.083 -33.054 1.00 33.17  ? 81  LEU B CB  1 
ATOM   1373 C CG  . LEU B 1 82 ? 8.810   -11.599 -32.800 1.00 39.04  ? 81  LEU B CG  1 
ATOM   1374 C CD1 . LEU B 1 82 ? 7.362   -12.106 -32.904 1.00 36.61  ? 81  LEU B CD1 1 
ATOM   1375 C CD2 . LEU B 1 82 ? 9.730   -12.383 -33.745 1.00 31.11  ? 81  LEU B CD2 1 
ATOM   1376 N N   . TRP B 1 83 ? 9.603   -7.005  -32.660 1.00 38.53  ? 82  TRP B N   1 
ATOM   1377 C CA  . TRP B 1 83 ? 9.401   -5.640  -33.116 1.00 34.37  ? 82  TRP B CA  1 
ATOM   1378 C C   . TRP B 1 83 ? 10.755  -5.031  -33.452 1.00 35.30  ? 82  TRP B C   1 
ATOM   1379 O O   . TRP B 1 83 ? 10.882  -4.336  -34.459 1.00 38.84  ? 82  TRP B O   1 
ATOM   1380 C CB  . TRP B 1 83 ? 8.678   -4.784  -32.063 1.00 38.93  ? 82  TRP B CB  1 
ATOM   1381 C CG  . TRP B 1 83 ? 8.493   -3.358  -32.525 1.00 39.68  ? 82  TRP B CG  1 
ATOM   1382 C CD1 . TRP B 1 83 ? 7.428   -2.863  -33.208 1.00 39.18  ? 82  TRP B CD1 1 
ATOM   1383 C CD2 . TRP B 1 83 ? 9.448   -2.273  -32.440 1.00 41.84  ? 82  TRP B CD2 1 
ATOM   1384 N NE1 . TRP B 1 83 ? 7.631   -1.550  -33.521 1.00 45.31  ? 82  TRP B NE1 1 
ATOM   1385 C CE2 . TRP B 1 83 ? 8.864   -1.161  -33.076 1.00 41.68  ? 82  TRP B CE2 1 
ATOM   1386 C CE3 . TRP B 1 83 ? 10.737  -2.136  -31.904 1.00 39.96  ? 82  TRP B CE3 1 
ATOM   1387 C CZ2 . TRP B 1 83 ? 9.516   0.067   -33.184 1.00 42.73  ? 82  TRP B CZ2 1 
ATOM   1388 C CZ3 . TRP B 1 83 ? 11.382  -0.920  -32.009 1.00 49.13  ? 82  TRP B CZ3 1 
ATOM   1389 C CH2 . TRP B 1 83 ? 10.785  0.161   -32.656 1.00 44.84  ? 82  TRP B CH2 1 
ATOM   1390 N N   . GLU B 1 84 ? 11.758  -5.316  -32.612 1.00 32.19  ? 83  GLU B N   1 
ATOM   1391 C CA  . GLU B 1 84 ? 13.113  -4.800  -32.791 1.00 36.37  ? 83  GLU B CA  1 
ATOM   1392 C C   . GLU B 1 84 ? 13.752  -5.319  -34.086 1.00 39.16  ? 83  GLU B C   1 
ATOM   1393 O O   . GLU B 1 84 ? 14.370  -4.555  -34.847 1.00 39.04  ? 83  GLU B O   1 
ATOM   1394 C CB  . GLU B 1 84 ? 14.005  -5.132  -31.591 1.00 37.95  ? 83  GLU B CB  1 
ATOM   1395 C CG  . GLU B 1 84 ? 13.590  -4.442  -30.288 1.00 38.35  ? 83  GLU B CG  1 
ATOM   1396 C CD  . GLU B 1 84 ? 14.501  -4.727  -29.105 1.00 39.63  ? 83  GLU B CD  1 
ATOM   1397 O OE1 . GLU B 1 84 ? 15.465  -5.538  -29.200 1.00 38.28  ? 83  GLU B OE1 1 
ATOM   1398 O OE2 . GLU B 1 84 ? 14.243  -4.098  -28.059 1.00 38.09  ? 83  GLU B OE2 1 
ATOM   1399 N N   . ILE B 1 85 ? 13.632  -6.629  -34.345 1.00 37.28  ? 84  ILE B N   1 
ATOM   1400 C CA  . ILE B 1 85 ? 14.340  -7.174  -35.497 1.00 34.90  ? 84  ILE B CA  1 
ATOM   1401 C C   . ILE B 1 85 ? 13.739  -6.629  -36.797 1.00 36.34  ? 84  ILE B C   1 
ATOM   1402 O O   . ILE B 1 85 ? 14.460  -6.518  -37.802 1.00 31.81  ? 84  ILE B O   1 
ATOM   1403 C CB  . ILE B 1 85 ? 14.384  -8.713  -35.482 1.00 38.36  ? 84  ILE B CB  1 
ATOM   1404 C CG1 . ILE B 1 85 ? 15.506  -9.259  -36.404 1.00 32.51  ? 84  ILE B CG1 1 
ATOM   1405 C CG2 . ILE B 1 85 ? 12.994  -9.322  -35.776 1.00 32.20  ? 84  ILE B CG2 1 
ATOM   1406 C CD1 . ILE B 1 85 ? 15.790  -10.749 -36.180 1.00 34.24  ? 84  ILE B CD1 1 
ATOM   1407 N N   . GLN B 1 86 ? 12.430  -6.312  -36.764 1.00 37.07  ? 85  GLN B N   1 
ATOM   1408 C CA  . GLN B 1 86 ? 11.684  -5.826  -37.918 1.00 42.22  ? 85  GLN B CA  1 
ATOM   1409 C C   . GLN B 1 86 ? 11.876  -4.320  -38.120 1.00 45.50  ? 85  GLN B C   1 
ATOM   1410 O O   . GLN B 1 86 ? 11.883  -3.865  -39.262 1.00 48.23  ? 85  GLN B O   1 
ATOM   1411 C CB  . GLN B 1 86 ? 10.176  -6.104  -37.895 1.00 40.99  ? 85  GLN B CB  1 
ATOM   1412 N N   . ASN B 1 87 ? 12.032  -3.537  -37.039 1.00 40.45  ? 86  ASN B N   1 
ATOM   1413 C CA  . ASN B 1 87 ? 11.921  -2.090  -37.179 1.00 34.75  ? 86  ASN B CA  1 
ATOM   1414 C C   . ASN B 1 87 ? 13.240  -1.375  -36.955 1.00 36.42  ? 86  ASN B C   1 
ATOM   1415 O O   . ASN B 1 87 ? 13.418  -0.248  -37.424 1.00 42.66  ? 86  ASN B O   1 
ATOM   1416 C CB  . ASN B 1 87 ? 10.927  -1.495  -36.194 1.00 38.15  ? 86  ASN B CB  1 
ATOM   1417 C CG  . ASN B 1 87 ? 9.537   -1.952  -36.551 1.00 47.28  ? 86  ASN B CG  1 
ATOM   1418 O OD1 . ASN B 1 87 ? 8.861   -1.242  -37.292 1.00 50.66  ? 86  ASN B OD1 1 
ATOM   1419 N ND2 . ASN B 1 87 ? 9.131   -3.150  -36.134 1.00 42.24  ? 86  ASN B ND2 1 
ATOM   1420 N N   . ASN B 1 88 ? 14.142  -1.982  -36.184 1.00 35.19  ? 87  ASN B N   1 
ATOM   1421 C CA  . ASN B 1 88 ? 15.393  -1.277  -35.979 1.00 37.91  ? 87  ASN B CA  1 
ATOM   1422 C C   . ASN B 1 88 ? 16.477  -2.266  -35.577 1.00 35.70  ? 87  ASN B C   1 
ATOM   1423 O O   . ASN B 1 88 ? 17.077  -2.135  -34.502 1.00 36.50  ? 87  ASN B O   1 
ATOM   1424 C CB  . ASN B 1 88 ? 15.207  -0.069  -35.053 1.00 41.09  ? 87  ASN B CB  1 
ATOM   1425 C CG  . ASN B 1 88 ? 16.287  0.976   -35.238 1.00 42.65  ? 87  ASN B CG  1 
ATOM   1426 O OD1 . ASN B 1 88 ? 17.320  0.729   -35.871 1.00 41.53  ? 87  ASN B OD1 1 
ATOM   1427 N ND2 . ASN B 1 88 ? 16.072  2.161   -34.689 1.00 44.76  ? 87  ASN B ND2 1 
ATOM   1428 N N   . PRO B 1 89 ? 16.790  -3.267  -36.437 1.00 34.09  ? 88  PRO B N   1 
ATOM   1429 C CA  . PRO B 1 89 ? 17.737  -4.322  -36.062 1.00 34.72  ? 88  PRO B CA  1 
ATOM   1430 C C   . PRO B 1 89 ? 19.145  -3.853  -35.732 1.00 40.32  ? 88  PRO B C   1 
ATOM   1431 O O   . PRO B 1 89 ? 19.914  -4.593  -35.119 1.00 45.00  ? 88  PRO B O   1 
ATOM   1432 C CB  . PRO B 1 89 ? 17.733  -5.223  -37.299 1.00 33.12  ? 88  PRO B CB  1 
ATOM   1433 C CG  . PRO B 1 89 ? 17.369  -4.264  -38.412 1.00 36.83  ? 88  PRO B CG  1 
ATOM   1434 C CD  . PRO B 1 89 ? 16.220  -3.468  -37.778 1.00 35.96  ? 88  PRO B CD  1 
ATOM   1435 N N   . HIS B 1 90 ? 19.491  -2.634  -36.163 1.00 36.86  ? 89  HIS B N   1 
ATOM   1436 C CA  . HIS B 1 90 ? 20.895  -2.253  -36.130 1.00 38.90  ? 89  HIS B CA  1 
ATOM   1437 C C   . HIS B 1 90 ? 21.133  -1.220  -35.033 1.00 36.23  ? 89  HIS B C   1 
ATOM   1438 O O   . HIS B 1 90 ? 22.214  -0.654  -34.943 1.00 39.29  ? 89  HIS B O   1 
ATOM   1439 C CB  . HIS B 1 90 ? 21.321  -1.833  -37.543 1.00 43.33  ? 89  HIS B CB  1 
ATOM   1440 C CG  . HIS B 1 90 ? 21.206  -2.945  -38.539 1.00 35.17  ? 89  HIS B CG  1 
ATOM   1441 N ND1 . HIS B 1 90 ? 21.839  -4.157  -38.357 1.00 38.16  ? 89  HIS B ND1 1 
ATOM   1442 C CD2 . HIS B 1 90 ? 20.536  -3.031  -39.702 1.00 34.55  ? 89  HIS B CD2 1 
ATOM   1443 C CE1 . HIS B 1 90 ? 21.540  -4.963  -39.387 1.00 36.28  ? 89  HIS B CE1 1 
ATOM   1444 N NE2 . HIS B 1 90 ? 20.750  -4.295  -40.223 1.00 36.42  ? 89  HIS B NE2 1 
ATOM   1445 N N   . ALA B 1 91 ? 20.117  -0.972  -34.201 1.00 36.90  ? 90  ALA B N   1 
ATOM   1446 C CA  . ALA B 1 91 ? 20.212  0.101   -33.218 1.00 39.20  ? 90  ALA B CA  1 
ATOM   1447 C C   . ALA B 1 91 ? 21.123  -0.357  -32.089 1.00 41.36  ? 90  ALA B C   1 
ATOM   1448 O O   . ALA B 1 91 ? 21.382  -1.561  -31.959 1.00 38.38  ? 90  ALA B O   1 
ATOM   1449 C CB  . ALA B 1 91 ? 18.839  0.456   -32.692 1.00 33.58  ? 90  ALA B CB  1 
ATOM   1450 N N   . SER B 1 92 ? 21.599  0.629   -31.317 1.00 42.96  ? 91  SER B N   1 
ATOM   1451 C CA  . SER B 1 92 ? 22.217  0.450   -30.012 1.00 44.53  ? 91  SER B CA  1 
ATOM   1452 C C   . SER B 1 92 ? 21.127  0.222   -28.968 1.00 45.73  ? 91  SER B C   1 
ATOM   1453 O O   . SER B 1 92 ? 20.206  1.035   -28.851 1.00 42.71  ? 91  SER B O   1 
ATOM   1454 C CB  . SER B 1 92 ? 23.020  1.662   -29.625 1.00 43.60  ? 91  SER B CB  1 
ATOM   1455 O OG  . SER B 1 92 ? 23.679  1.414   -28.388 1.00 50.42  ? 91  SER B OG  1 
ATOM   1456 N N   . TYR B 1 93 ? 21.229  -0.894  -28.232 1.00 48.50  ? 92  TYR B N   1 
ATOM   1457 C CA  . TYR B 1 93 ? 20.213  -1.246  -27.252 1.00 48.54  ? 92  TYR B CA  1 
ATOM   1458 C C   . TYR B 1 93 ? 20.818  -1.205  -25.847 1.00 56.13  ? 92  TYR B C   1 
ATOM   1459 O O   . TYR B 1 93 ? 20.099  -1.324  -24.859 1.00 62.17  ? 92  TYR B O   1 
ATOM   1460 C CB  . TYR B 1 93 ? 19.555  -2.574  -27.640 1.00 43.38  ? 92  TYR B CB  1 
ATOM   1461 C CG  . TYR B 1 93 ? 18.547  -2.452  -28.775 1.00 44.97  ? 92  TYR B CG  1 
ATOM   1462 C CD1 . TYR B 1 93 ? 17.251  -1.974  -28.549 1.00 39.40  ? 92  TYR B CD1 1 
ATOM   1463 C CD2 . TYR B 1 93 ? 18.887  -2.852  -30.069 1.00 37.73  ? 92  TYR B CD2 1 
ATOM   1464 C CE1 . TYR B 1 93 ? 16.334  -1.849  -29.585 1.00 41.14  ? 92  TYR B CE1 1 
ATOM   1465 C CE2 . TYR B 1 93 ? 17.962  -2.771  -31.094 1.00 38.37  ? 92  TYR B CE2 1 
ATOM   1466 C CZ  . TYR B 1 93 ? 16.690  -2.270  -30.859 1.00 40.80  ? 92  TYR B CZ  1 
ATOM   1467 O OH  . TYR B 1 93 ? 15.834  -2.167  -31.918 1.00 36.67  ? 92  TYR B OH  1 
ATOM   1468 N N   . SER B 1 94 ? 22.148  -1.081  -25.799 1.00 63.21  ? 93  SER B N   1 
ATOM   1469 C CA  . SER B 1 94 ? 22.929  -0.457  -24.737 1.00 85.84  ? 93  SER B CA  1 
ATOM   1470 C C   . SER B 1 94 ? 22.056  0.044   -23.577 1.00 94.02  ? 93  SER B C   1 
ATOM   1471 O O   . SER B 1 94 ? 22.110  1.264   -23.311 1.00 94.87  ? 93  SER B O   1 
ATOM   1472 C CB  . SER B 1 94 ? 23.767  0.684   -25.285 1.00 95.84  ? 93  SER B CB  1 
ATOM   1473 O OG  . SER B 1 94 ? 24.685  0.235   -26.274 1.00 103.92 ? 93  SER B OG  1 
ATOM   1474 O OXT . SER B 1 94 ? 21.379  -0.805  -22.961 1.00 113.30 ? 93  SER B OXT 1 
ATOM   1475 N N   . ALA C 1 5  ? 29.849  -22.553 28.665  1.00 74.15  ? 4   ALA C N   1 
ATOM   1476 C CA  . ALA C 1 5  ? 28.928  -22.948 29.762  1.00 76.39  ? 4   ALA C CA  1 
ATOM   1477 C C   . ALA C 1 5  ? 27.476  -22.606 29.433  1.00 81.29  ? 4   ALA C C   1 
ATOM   1478 O O   . ALA C 1 5  ? 27.166  -21.524 28.928  1.00 82.56  ? 4   ALA C O   1 
ATOM   1479 C CB  . ALA C 1 5  ? 29.330  -22.235 31.011  1.00 81.24  ? 4   ALA C CB  1 
ATOM   1480 N N   . PHE C 1 6  ? 26.576  -23.520 29.795  1.00 69.56  ? 5   PHE C N   1 
ATOM   1481 C CA  . PHE C 1 6  ? 25.190  -23.360 29.401  1.00 66.80  ? 5   PHE C CA  1 
ATOM   1482 C C   . PHE C 1 6  ? 24.350  -23.266 30.664  1.00 70.41  ? 5   PHE C C   1 
ATOM   1483 O O   . PHE C 1 6  ? 24.799  -23.673 31.725  1.00 78.39  ? 5   PHE C O   1 
ATOM   1484 C CB  . PHE C 1 6  ? 24.799  -24.533 28.497  1.00 61.99  ? 5   PHE C CB  1 
ATOM   1485 C CG  . PHE C 1 6  ? 25.683  -24.714 27.268  1.00 56.12  ? 5   PHE C CG  1 
ATOM   1486 C CD1 . PHE C 1 6  ? 26.737  -25.621 27.272  1.00 53.71  ? 5   PHE C CD1 1 
ATOM   1487 C CD2 . PHE C 1 6  ? 25.468  -23.963 26.113  1.00 60.45  ? 5   PHE C CD2 1 
ATOM   1488 C CE1 . PHE C 1 6  ? 27.544  -25.783 26.150  1.00 59.54  ? 5   PHE C CE1 1 
ATOM   1489 C CE2 . PHE C 1 6  ? 26.271  -24.130 24.992  1.00 60.29  ? 5   PHE C CE2 1 
ATOM   1490 C CZ  . PHE C 1 6  ? 27.311  -25.035 25.014  1.00 64.67  ? 5   PHE C CZ  1 
ATOM   1491 N N   . LYS C 1 7  ? 23.139  -22.723 30.531  1.00 64.33  ? 6   LYS C N   1 
ATOM   1492 C CA  . LYS C 1 7  ? 22.235  -22.567 31.656  1.00 72.63  ? 6   LYS C CA  1 
ATOM   1493 C C   . LYS C 1 7  ? 20.840  -22.947 31.171  1.00 69.86  ? 6   LYS C C   1 
ATOM   1494 O O   . LYS C 1 7  ? 20.551  -22.833 29.980  1.00 67.79  ? 6   LYS C O   1 
ATOM   1495 C CB  . LYS C 1 7  ? 22.335  -21.125 32.179  1.00 76.13  ? 6   LYS C CB  1 
ATOM   1496 N N   . PRO C 1 8  ? 19.928  -23.422 32.048  1.00 71.71  ? 7   PRO C N   1 
ATOM   1497 C CA  . PRO C 1 8  ? 18.610  -23.878 31.589  1.00 75.26  ? 7   PRO C CA  1 
ATOM   1498 C C   . PRO C 1 8  ? 17.901  -22.756 30.831  1.00 73.87  ? 7   PRO C C   1 
ATOM   1499 O O   . PRO C 1 8  ? 17.832  -21.634 31.322  1.00 81.14  ? 7   PRO C O   1 
ATOM   1500 C CB  . PRO C 1 8  ? 17.865  -24.282 32.893  1.00 75.58  ? 7   PRO C CB  1 
ATOM   1501 C CG  . PRO C 1 8  ? 18.974  -24.503 33.904  1.00 61.81  ? 7   PRO C CG  1 
ATOM   1502 C CD  . PRO C 1 8  ? 20.103  -23.546 33.508  1.00 69.35  ? 7   PRO C CD  1 
ATOM   1503 N N   . GLY C 1 9  ? 17.405  -23.057 29.625  1.00 69.86  ? 8   GLY C N   1 
ATOM   1504 C CA  . GLY C 1 9  ? 16.767  -22.051 28.793  1.00 59.03  ? 8   GLY C CA  1 
ATOM   1505 C C   . GLY C 1 9  ? 17.656  -21.535 27.653  1.00 55.60  ? 8   GLY C C   1 
ATOM   1506 O O   . GLY C 1 9  ? 17.139  -20.908 26.727  1.00 57.05  ? 8   GLY C O   1 
ATOM   1507 N N   . ASP C 1 10 ? 18.974  -21.797 27.707  1.00 52.71  ? 9   ASP C N   1 
ATOM   1508 C CA  . ASP C 1 10 ? 19.893  -21.488 26.614  1.00 48.26  ? 9   ASP C CA  1 
ATOM   1509 C C   . ASP C 1 10 ? 19.516  -22.282 25.361  1.00 51.70  ? 9   ASP C C   1 
ATOM   1510 O O   . ASP C 1 10 ? 19.296  -23.491 25.419  1.00 48.80  ? 9   ASP C O   1 
ATOM   1511 C CB  . ASP C 1 10 ? 21.353  -21.709 26.991  1.00 61.37  ? 9   ASP C CB  1 
ATOM   1512 C CG  . ASP C 1 10 ? 22.018  -20.660 27.883  1.00 62.94  ? 9   ASP C CG  1 
ATOM   1513 O OD1 . ASP C 1 10 ? 21.306  -19.742 28.362  1.00 63.96  ? 9   ASP C OD1 1 
ATOM   1514 O OD2 . ASP C 1 10 ? 23.256  -20.760 28.092  1.00 67.15  ? 9   ASP C OD2 1 
ATOM   1515 N N   . LEU C 1 11 ? 19.433  -21.557 24.231  1.00 53.29  ? 10  LEU C N   1 
ATOM   1516 C CA  . LEU C 1 11 ? 19.063  -22.075 22.927  1.00 52.02  ? 10  LEU C CA  1 
ATOM   1517 C C   . LEU C 1 11 ? 20.319  -22.596 22.244  1.00 47.48  ? 10  LEU C C   1 
ATOM   1518 O O   . LEU C 1 11 ? 21.327  -21.903 22.278  1.00 44.55  ? 10  LEU C O   1 
ATOM   1519 C CB  . LEU C 1 11 ? 18.413  -20.924 22.156  1.00 53.64  ? 10  LEU C CB  1 
ATOM   1520 C CG  . LEU C 1 11 ? 17.043  -20.492 22.693  1.00 48.20  ? 10  LEU C CG  1 
ATOM   1521 C CD1 . LEU C 1 11 ? 16.271  -19.541 21.804  1.00 48.44  ? 10  LEU C CD1 1 
ATOM   1522 C CD2 . LEU C 1 11 ? 16.209  -21.710 23.034  1.00 43.19  ? 10  LEU C CD2 1 
ATOM   1523 N N   . VAL C 1 12 ? 20.265  -23.824 21.683  1.00 37.74  ? 11  VAL C N   1 
ATOM   1524 C CA  . VAL C 1 12 ? 21.454  -24.418 21.081  1.00 38.87  ? 11  VAL C CA  1 
ATOM   1525 C C   . VAL C 1 12 ? 21.082  -25.177 19.802  1.00 42.01  ? 11  VAL C C   1 
ATOM   1526 O O   . VAL C 1 12 ? 19.911  -25.352 19.478  1.00 42.43  ? 11  VAL C O   1 
ATOM   1527 C CB  . VAL C 1 12 ? 22.215  -25.360 22.027  1.00 37.84  ? 11  VAL C CB  1 
ATOM   1528 C CG1 . VAL C 1 12 ? 22.656  -24.644 23.290  1.00 39.21  ? 11  VAL C CG1 1 
ATOM   1529 C CG2 . VAL C 1 12 ? 21.375  -26.590 22.379  1.00 34.98  ? 11  VAL C CG2 1 
ATOM   1530 N N   . PHE C 1 13 ? 22.114  -25.618 19.078  1.00 39.85  ? 12  PHE C N   1 
ATOM   1531 C CA  . PHE C 1 13 ? 22.003  -26.755 18.183  1.00 40.39  ? 12  PHE C CA  1 
ATOM   1532 C C   . PHE C 1 13 ? 22.654  -27.943 18.874  1.00 41.18  ? 12  PHE C C   1 
ATOM   1533 O O   . PHE C 1 13 ? 23.780  -27.836 19.418  1.00 41.66  ? 12  PHE C O   1 
ATOM   1534 C CB  . PHE C 1 13 ? 22.591  -26.540 16.783  1.00 41.39  ? 12  PHE C CB  1 
ATOM   1535 C CG  . PHE C 1 13 ? 21.752  -25.575 15.965  1.00 42.80  ? 12  PHE C CG  1 
ATOM   1536 C CD1 . PHE C 1 13 ? 20.670  -26.029 15.227  1.00 44.38  ? 12  PHE C CD1 1 
ATOM   1537 C CD2 . PHE C 1 13 ? 22.034  -24.203 15.964  1.00 44.44  ? 12  PHE C CD2 1 
ATOM   1538 C CE1 . PHE C 1 13 ? 19.891  -25.128 14.510  1.00 49.55  ? 12  PHE C CE1 1 
ATOM   1539 C CE2 . PHE C 1 13 ? 21.258  -23.309 15.242  1.00 44.50  ? 12  PHE C CE2 1 
ATOM   1540 C CZ  . PHE C 1 13 ? 20.190  -23.778 14.514  1.00 52.15  ? 12  PHE C CZ  1 
ATOM   1541 N N   . ALA C 1 14 ? 21.894  -29.048 18.874  1.00 38.78  ? 13  ALA C N   1 
ATOM   1542 C CA  . ALA C 1 14 ? 22.275  -30.245 19.608  1.00 41.72  ? 13  ALA C CA  1 
ATOM   1543 C C   . ALA C 1 14 ? 22.602  -31.354 18.614  1.00 41.41  ? 13  ALA C C   1 
ATOM   1544 O O   . ALA C 1 14 ? 21.771  -31.658 17.764  1.00 39.64  ? 13  ALA C O   1 
ATOM   1545 C CB  . ALA C 1 14 ? 21.153  -30.653 20.549  1.00 37.50  ? 13  ALA C CB  1 
ATOM   1546 N N   . LYS C 1 15 ? 23.793  -31.960 18.750  1.00 38.01  ? 14  LYS C N   1 
ATOM   1547 C CA  . LYS C 1 15 ? 24.211  -32.970 17.799  1.00 34.40  ? 14  LYS C CA  1 
ATOM   1548 C C   . LYS C 1 15 ? 24.261  -34.321 18.499  1.00 38.95  ? 14  LYS C C   1 
ATOM   1549 O O   . LYS C 1 15 ? 25.045  -34.493 19.431  1.00 41.06  ? 14  LYS C O   1 
ATOM   1550 C CB  . LYS C 1 15 ? 25.601  -32.720 17.197  1.00 40.30  ? 14  LYS C CB  1 
ATOM   1551 C CG  . LYS C 1 15 ? 26.091  -33.847 16.244  1.00 38.73  ? 14  LYS C CG  1 
ATOM   1552 C CD  . LYS C 1 15 ? 25.221  -33.869 14.989  1.00 41.24  ? 14  LYS C CD  1 
ATOM   1553 C CE  . LYS C 1 15 ? 25.745  -34.769 13.883  1.00 43.39  ? 14  LYS C CE  1 
ATOM   1554 N NZ  . LYS C 1 15 ? 25.464  -36.192 14.128  1.00 38.46  ? 14  LYS C NZ  1 
ATOM   1555 N N   . MET C 1 16 ? 23.437  -35.252 18.008  1.00 33.52  ? 15  MET C N   1 
ATOM   1556 C CA  . MET C 1 16 ? 23.425  -36.658 18.377  1.00 38.37  ? 15  MET C CA  1 
ATOM   1557 C C   . MET C 1 16 ? 23.869  -37.465 17.158  1.00 42.32  ? 15  MET C C   1 
ATOM   1558 O O   . MET C 1 16 ? 23.652  -37.035 16.026  1.00 40.98  ? 15  MET C O   1 
ATOM   1559 C CB  . MET C 1 16 ? 21.990  -37.117 18.669  1.00 38.42  ? 15  MET C CB  1 
ATOM   1560 C CG  . MET C 1 16 ? 21.406  -36.448 19.887  1.00 45.23  ? 15  MET C CG  1 
ATOM   1561 S SD  . MET C 1 16 ? 19.882  -37.218 20.476  1.00 51.45  ? 15  MET C SD  1 
ATOM   1562 C CE  . MET C 1 16 ? 18.936  -36.962 18.960  1.00 54.42  ? 15  MET C CE  1 
ATOM   1563 N N   . LYS C 1 17 ? 24.484  -38.632 17.402  1.00 40.99  ? 16  LYS C N   1 
ATOM   1564 C CA  . LYS C 1 17 ? 24.858  -39.553 16.337  1.00 43.17  ? 16  LYS C CA  1 
ATOM   1565 C C   . LYS C 1 17 ? 23.597  -39.994 15.594  1.00 38.04  ? 16  LYS C C   1 
ATOM   1566 O O   . LYS C 1 17 ? 22.614  -40.446 16.200  1.00 36.03  ? 16  LYS C O   1 
ATOM   1567 C CB  . LYS C 1 17 ? 25.559  -40.807 16.892  1.00 43.43  ? 16  LYS C CB  1 
ATOM   1568 C CG  . LYS C 1 17 ? 26.265  -41.680 15.843  1.00 49.15  ? 16  LYS C CG  1 
ATOM   1569 C CD  . LYS C 1 17 ? 27.406  -40.927 15.171  1.00 53.51  ? 16  LYS C CD  1 
ATOM   1570 C CE  . LYS C 1 17 ? 28.322  -41.786 14.349  1.00 60.36  ? 16  LYS C CE  1 
ATOM   1571 N NZ  . LYS C 1 17 ? 29.421  -40.990 13.777  1.00 51.95  ? 16  LYS C NZ  1 
ATOM   1572 N N   . GLY C 1 18 ? 23.648  -39.868 14.274  1.00 39.54  ? 17  GLY C N   1 
ATOM   1573 C CA  . GLY C 1 18 ? 22.590  -40.392 13.426  1.00 44.75  ? 17  GLY C CA  1 
ATOM   1574 C C   . GLY C 1 18 ? 21.582  -39.297 13.071  1.00 46.69  ? 17  GLY C C   1 
ATOM   1575 O O   . GLY C 1 18 ? 20.550  -39.604 12.477  1.00 39.49  ? 17  GLY C O   1 
ATOM   1576 N N   . TYR C 1 19 ? 21.908  -38.039 13.434  1.00 45.12  ? 18  TYR C N   1 
ATOM   1577 C CA  . TYR C 1 19 ? 20.998  -36.895 13.335  1.00 43.32  ? 18  TYR C CA  1 
ATOM   1578 C C   . TYR C 1 19 ? 21.789  -35.630 13.022  1.00 40.63  ? 18  TYR C C   1 
ATOM   1579 O O   . TYR C 1 19 ? 22.934  -35.462 13.453  1.00 43.57  ? 18  TYR C O   1 
ATOM   1580 C CB  . TYR C 1 19 ? 20.151  -36.599 14.581  1.00 42.46  ? 18  TYR C CB  1 
ATOM   1581 C CG  . TYR C 1 19 ? 19.298  -37.783 15.003  1.00 44.74  ? 18  TYR C CG  1 
ATOM   1582 C CD1 . TYR C 1 19 ? 19.869  -38.843 15.707  1.00 44.59  ? 18  TYR C CD1 1 
ATOM   1583 C CD2 . TYR C 1 19 ? 17.944  -37.861 14.661  1.00 49.50  ? 18  TYR C CD2 1 
ATOM   1584 C CE1 . TYR C 1 19 ? 19.120  -39.949 16.072  1.00 43.80  ? 18  TYR C CE1 1 
ATOM   1585 C CE2 . TYR C 1 19 ? 17.175  -38.962 15.025  1.00 47.72  ? 18  TYR C CE2 1 
ATOM   1586 C CZ  . TYR C 1 19 ? 17.785  -39.999 15.714  1.00 43.17  ? 18  TYR C CZ  1 
ATOM   1587 O OH  . TYR C 1 19 ? 17.103  -41.094 16.088  1.00 57.64  ? 18  TYR C OH  1 
ATOM   1588 N N   . PRO C 1 20 ? 21.200  -34.725 12.220  1.00 43.20  ? 19  PRO C N   1 
ATOM   1589 C CA  . PRO C 1 20 ? 21.829  -33.427 11.963  1.00 39.48  ? 19  PRO C CA  1 
ATOM   1590 C C   . PRO C 1 20 ? 21.789  -32.558 13.221  1.00 35.36  ? 19  PRO C C   1 
ATOM   1591 O O   . PRO C 1 20 ? 20.981  -32.805 14.115  1.00 32.95  ? 19  PRO C O   1 
ATOM   1592 C CB  . PRO C 1 20 ? 20.941  -32.870 10.816  1.00 34.91  ? 19  PRO C CB  1 
ATOM   1593 C CG  . PRO C 1 20 ? 19.578  -33.533 11.021  1.00 38.16  ? 19  PRO C CG  1 
ATOM   1594 C CD  . PRO C 1 20 ? 19.924  -34.935 11.494  1.00 39.92  ? 19  PRO C CD  1 
ATOM   1595 N N   . HIS C 1 21 ? 22.641  -31.528 13.273  1.00 38.32  ? 20  HIS C N   1 
ATOM   1596 C CA  . HIS C 1 21 ? 22.596  -30.594 14.392  1.00 40.89  ? 20  HIS C CA  1 
ATOM   1597 C C   . HIS C 1 21 ? 21.162  -30.087 14.487  1.00 43.18  ? 20  HIS C C   1 
ATOM   1598 O O   . HIS C 1 21 ? 20.617  -29.603 13.484  1.00 37.29  ? 20  HIS C O   1 
ATOM   1599 C CB  . HIS C 1 21 ? 23.576  -29.440 14.148  1.00 41.81  ? 20  HIS C CB  1 
ATOM   1600 C CG  . HIS C 1 21 ? 24.989  -29.918 14.114  1.00 41.92  ? 20  HIS C CG  1 
ATOM   1601 N ND1 . HIS C 1 21 ? 25.495  -30.659 13.067  1.00 43.67  ? 20  HIS C ND1 1 
ATOM   1602 C CD2 . HIS C 1 21 ? 25.977  -29.835 15.038  1.00 40.98  ? 20  HIS C CD2 1 
ATOM   1603 C CE1 . HIS C 1 21 ? 26.764  -30.975 13.333  1.00 43.83  ? 20  HIS C CE1 1 
ATOM   1604 N NE2 . HIS C 1 21 ? 27.078  -30.472 14.527  1.00 37.59  ? 20  HIS C NE2 1 
ATOM   1605 N N   . TRP C 1 22 ? 20.564  -30.209 15.686  1.00 36.38  ? 21  TRP C N   1 
ATOM   1606 C CA  . TRP C 1 22 ? 19.112  -30.095 15.843  1.00 36.02  ? 21  TRP C CA  1 
ATOM   1607 C C   . TRP C 1 22 ? 18.772  -28.863 16.698  1.00 36.97  ? 21  TRP C C   1 
ATOM   1608 O O   . TRP C 1 22 ? 19.421  -28.613 17.703  1.00 38.61  ? 21  TRP C O   1 
ATOM   1609 C CB  . TRP C 1 22 ? 18.554  -31.376 16.507  1.00 37.56  ? 21  TRP C CB  1 
ATOM   1610 C CG  . TRP C 1 22 ? 17.093  -31.603 16.190  1.00 40.48  ? 21  TRP C CG  1 
ATOM   1611 C CD1 . TRP C 1 22 ? 16.013  -30.972 16.738  1.00 36.10  ? 21  TRP C CD1 1 
ATOM   1612 C CD2 . TRP C 1 22 ? 16.569  -32.496 15.179  1.00 36.12  ? 21  TRP C CD2 1 
ATOM   1613 N NE1 . TRP C 1 22 ? 14.854  -31.400 16.141  1.00 40.30  ? 21  TRP C NE1 1 
ATOM   1614 C CE2 . TRP C 1 22 ? 15.165  -32.336 15.183  1.00 37.80  ? 21  TRP C CE2 1 
ATOM   1615 C CE3 . TRP C 1 22 ? 17.152  -33.406 14.282  1.00 37.49  ? 21  TRP C CE3 1 
ATOM   1616 C CZ2 . TRP C 1 22 ? 14.344  -33.072 14.330  1.00 38.70  ? 21  TRP C CZ2 1 
ATOM   1617 C CZ3 . TRP C 1 22 ? 16.340  -34.144 13.445  1.00 38.82  ? 21  TRP C CZ3 1 
ATOM   1618 C CH2 . TRP C 1 22 ? 14.954  -33.969 13.472  1.00 39.98  ? 21  TRP C CH2 1 
ATOM   1619 N N   . PRO C 1 23 ? 17.740  -28.054 16.366  1.00 38.17  ? 22  PRO C N   1 
ATOM   1620 C CA  . PRO C 1 23 ? 17.375  -26.924 17.222  1.00 37.31  ? 22  PRO C CA  1 
ATOM   1621 C C   . PRO C 1 23 ? 16.822  -27.453 18.545  1.00 39.75  ? 22  PRO C C   1 
ATOM   1622 O O   . PRO C 1 23 ? 15.937  -28.335 18.566  1.00 35.97  ? 22  PRO C O   1 
ATOM   1623 C CB  . PRO C 1 23 ? 16.366  -26.123 16.369  1.00 35.75  ? 22  PRO C CB  1 
ATOM   1624 C CG  . PRO C 1 23 ? 15.749  -27.145 15.450  1.00 32.64  ? 22  PRO C CG  1 
ATOM   1625 C CD  . PRO C 1 23 ? 16.850  -28.187 15.202  1.00 34.88  ? 22  PRO C CD  1 
ATOM   1626 N N   . ALA C 1 24 ? 17.408  -26.954 19.646  1.00 36.19  ? 23  ALA C N   1 
ATOM   1627 C CA  . ALA C 1 24 ? 17.108  -27.484 20.968  1.00 37.52  ? 23  ALA C CA  1 
ATOM   1628 C C   . ALA C 1 24 ? 17.295  -26.418 22.049  1.00 45.62  ? 23  ALA C C   1 
ATOM   1629 O O   . ALA C 1 24 ? 17.816  -25.326 21.799  1.00 48.14  ? 23  ALA C O   1 
ATOM   1630 C CB  . ALA C 1 24 ? 17.990  -28.694 21.260  1.00 34.22  ? 23  ALA C CB  1 
ATOM   1631 N N   . ARG C 1 25 ? 16.922  -26.758 23.289  1.00 40.96  ? 24  ARG C N   1 
ATOM   1632 C CA  . ARG C 1 25 ? 17.333  -25.893 24.380  1.00 48.45  ? 24  ARG C CA  1 
ATOM   1633 C C   . ARG C 1 25 ? 17.776  -26.722 25.586  1.00 47.67  ? 24  ARG C C   1 
ATOM   1634 O O   . ARG C 1 25 ? 17.389  -27.887 25.723  1.00 46.28  ? 24  ARG C O   1 
ATOM   1635 C CB  . ARG C 1 25 ? 16.142  -24.992 24.712  1.00 46.68  ? 24  ARG C CB  1 
ATOM   1636 C CG  . ARG C 1 25 ? 14.976  -25.704 25.386  1.00 45.97  ? 24  ARG C CG  1 
ATOM   1637 C CD  . ARG C 1 25 ? 13.923  -24.746 25.917  1.00 49.09  ? 24  ARG C CD  1 
ATOM   1638 N NE  . ARG C 1 25 ? 12.813  -25.564 26.417  1.00 52.62  ? 24  ARG C NE  1 
ATOM   1639 C CZ  . ARG C 1 25 ? 11.543  -25.390 26.112  1.00 58.07  ? 24  ARG C CZ  1 
ATOM   1640 N NH1 . ARG C 1 25 ? 11.136  -24.247 25.591  1.00 56.67  ? 24  ARG C NH1 1 
ATOM   1641 N NH2 . ARG C 1 25 ? 10.671  -26.348 26.372  1.00 58.37  ? 24  ARG C NH2 1 
ATOM   1642 N N   . ILE C 1 26 ? 18.568  -26.098 26.467  1.00 50.40  ? 25  ILE C N   1 
ATOM   1643 C CA  . ILE C 1 26 ? 18.934  -26.679 27.755  1.00 58.83  ? 25  ILE C CA  1 
ATOM   1644 C C   . ILE C 1 26 ? 17.691  -26.695 28.647  1.00 60.53  ? 25  ILE C C   1 
ATOM   1645 O O   . ILE C 1 26 ? 17.052  -25.650 28.791  1.00 61.18  ? 25  ILE C O   1 
ATOM   1646 C CB  . ILE C 1 26 ? 20.065  -25.865 28.421  1.00 60.06  ? 25  ILE C CB  1 
ATOM   1647 C CG1 . ILE C 1 26 ? 21.162  -25.446 27.442  1.00 56.29  ? 25  ILE C CG1 1 
ATOM   1648 C CG2 . ILE C 1 26 ? 20.637  -26.617 29.625  1.00 53.28  ? 25  ILE C CG2 1 
ATOM   1649 C CD1 . ILE C 1 26 ? 22.100  -26.570 27.052  1.00 56.29  ? 25  ILE C CD1 1 
ATOM   1650 N N   . ASP C 1 27 ? 17.367  -27.859 29.245  1.00 59.02  ? 26  ASP C N   1 
ATOM   1651 C CA  . ASP C 1 27 ? 16.272  -27.995 30.210  1.00 72.73  ? 26  ASP C CA  1 
ATOM   1652 C C   . ASP C 1 27 ? 16.693  -27.701 31.663  1.00 70.68  ? 26  ASP C C   1 
ATOM   1653 O O   . ASP C 1 27 ? 17.759  -27.081 31.864  1.00 61.98  ? 26  ASP C O   1 
ATOM   1654 C CB  . ASP C 1 27 ? 15.656  -29.385 30.206  1.00 74.09  ? 26  ASP C CB  1 
ATOM   1655 C CG  . ASP C 1 27 ? 14.322  -29.517 29.491  1.00 81.62  ? 26  ASP C CG  1 
ATOM   1656 O OD1 . ASP C 1 27 ? 13.908  -28.528 28.848  1.00 80.44  ? 26  ASP C OD1 1 
ATOM   1657 O OD2 . ASP C 1 27 ? 13.699  -30.601 29.607  1.00 74.30  ? 26  ASP C OD2 1 
ATOM   1658 N N   . LYS C 1 35 ? 19.398  -37.867 37.996  1.00 98.95  ? 34  LYS C N   1 
ATOM   1659 C CA  . LYS C 1 35 ? 20.488  -36.881 37.765  1.00 84.33  ? 34  LYS C CA  1 
ATOM   1660 C C   . LYS C 1 35 ? 21.201  -37.210 36.446  1.00 83.93  ? 34  LYS C C   1 
ATOM   1661 O O   . LYS C 1 35 ? 21.325  -38.380 36.064  1.00 73.07  ? 34  LYS C O   1 
ATOM   1662 C CB  . LYS C 1 35 ? 21.364  -36.803 39.023  1.00 71.48  ? 34  LYS C CB  1 
ATOM   1663 N N   . PRO C 1 36 ? 21.650  -36.180 35.685  1.00 83.78  ? 35  PRO C N   1 
ATOM   1664 C CA  . PRO C 1 36 ? 22.366  -36.393 34.419  1.00 76.35  ? 35  PRO C CA  1 
ATOM   1665 C C   . PRO C 1 36 ? 23.651  -37.208 34.571  1.00 78.97  ? 35  PRO C C   1 
ATOM   1666 O O   . PRO C 1 36 ? 24.352  -37.090 35.579  1.00 67.56  ? 35  PRO C O   1 
ATOM   1667 C CB  . PRO C 1 36 ? 22.668  -34.955 33.925  1.00 66.31  ? 35  PRO C CB  1 
ATOM   1668 C CG  . PRO C 1 36 ? 21.639  -34.097 34.631  1.00 65.00  ? 35  PRO C CG  1 
ATOM   1669 C CD  . PRO C 1 36 ? 21.471  -34.749 35.999  1.00 76.60  ? 35  PRO C CD  1 
ATOM   1670 N N   . PRO C 1 37 ? 24.038  -38.022 33.559  1.00 69.50  ? 36  PRO C N   1 
ATOM   1671 C CA  . PRO C 1 37 ? 25.315  -38.726 33.617  1.00 70.81  ? 36  PRO C CA  1 
ATOM   1672 C C   . PRO C 1 37 ? 26.359  -37.610 33.725  1.00 73.03  ? 36  PRO C C   1 
ATOM   1673 O O   . PRO C 1 37 ? 26.111  -36.478 33.297  1.00 73.40  ? 36  PRO C O   1 
ATOM   1674 C CB  . PRO C 1 37 ? 25.372  -39.510 32.287  1.00 61.73  ? 36  PRO C CB  1 
ATOM   1675 C CG  . PRO C 1 37 ? 23.928  -39.553 31.832  1.00 62.86  ? 36  PRO C CG  1 
ATOM   1676 C CD  . PRO C 1 37 ? 23.328  -38.235 32.291  1.00 61.40  ? 36  PRO C CD  1 
ATOM   1677 N N   . PRO C 1 38 ? 27.531  -37.876 34.348  1.00 64.63  ? 37  PRO C N   1 
ATOM   1678 C CA  . PRO C 1 38 ? 28.526  -36.832 34.609  1.00 62.97  ? 37  PRO C CA  1 
ATOM   1679 C C   . PRO C 1 38 ? 28.809  -35.967 33.382  1.00 59.46  ? 37  PRO C C   1 
ATOM   1680 O O   . PRO C 1 38 ? 29.124  -36.472 32.301  1.00 59.45  ? 37  PRO C O   1 
ATOM   1681 C CB  . PRO C 1 38 ? 29.776  -37.622 35.056  1.00 71.11  ? 37  PRO C CB  1 
ATOM   1682 C CG  . PRO C 1 38 ? 29.231  -38.923 35.601  1.00 64.86  ? 37  PRO C CG  1 
ATOM   1683 C CD  . PRO C 1 38 ? 27.947  -39.198 34.840  1.00 63.23  ? 37  PRO C CD  1 
ATOM   1684 N N   . ASN C 1 39 ? 28.635  -34.661 33.571  1.00 52.11  ? 38  ASN C N   1 
ATOM   1685 C CA  . ASN C 1 39 ? 29.018  -33.647 32.607  1.00 53.90  ? 38  ASN C CA  1 
ATOM   1686 C C   . ASN C 1 39 ? 28.061  -33.614 31.408  1.00 54.09  ? 38  ASN C C   1 
ATOM   1687 O O   . ASN C 1 39 ? 28.461  -33.177 30.326  1.00 52.34  ? 38  ASN C O   1 
ATOM   1688 C CB  . ASN C 1 39 ? 30.504  -33.712 32.271  1.00 52.26  ? 38  ASN C CB  1 
ATOM   1689 C CG  . ASN C 1 39 ? 30.937  -32.436 31.583  1.00 77.17  ? 38  ASN C CG  1 
ATOM   1690 O OD1 . ASN C 1 39 ? 30.618  -31.326 32.037  1.00 77.46  ? 38  ASN C OD1 1 
ATOM   1691 N ND2 . ASN C 1 39 ? 31.606  -32.567 30.449  1.00 80.72  ? 38  ASN C ND2 1 
ATOM   1692 N N   . LYS C 1 40 ? 26.810  -34.060 31.612  1.00 45.86  ? 39  LYS C N   1 
ATOM   1693 C CA  . LYS C 1 40 ? 25.792  -33.999 30.574  1.00 54.12  ? 39  LYS C CA  1 
ATOM   1694 C C   . LYS C 1 40 ? 24.695  -33.008 30.960  1.00 53.21  ? 39  LYS C C   1 
ATOM   1695 O O   . LYS C 1 40 ? 24.267  -32.933 32.113  1.00 59.01  ? 39  LYS C O   1 
ATOM   1696 C CB  . LYS C 1 40 ? 25.091  -35.343 30.349  1.00 54.73  ? 39  LYS C CB  1 
ATOM   1697 C CG  . LYS C 1 40 ? 25.984  -36.529 30.071  1.00 56.57  ? 39  LYS C CG  1 
ATOM   1698 C CD  . LYS C 1 40 ? 26.770  -36.398 28.785  1.00 59.15  ? 39  LYS C CD  1 
ATOM   1699 C CE  . LYS C 1 40 ? 27.449  -37.701 28.540  1.00 61.37  ? 39  LYS C CE  1 
ATOM   1700 N NZ  . LYS C 1 40 ? 28.454  -37.527 27.489  1.00 71.73  ? 39  LYS C NZ  1 
ATOM   1701 N N   . TYR C 1 41 ? 24.208  -32.274 29.961  1.00 46.93  ? 40  TYR C N   1 
ATOM   1702 C CA  . TYR C 1 41 ? 23.061  -31.398 30.136  1.00 43.13  ? 40  TYR C CA  1 
ATOM   1703 C C   . TYR C 1 41 ? 21.799  -32.137 29.687  1.00 47.11  ? 40  TYR C C   1 
ATOM   1704 O O   . TYR C 1 41 ? 21.862  -33.024 28.812  1.00 47.48  ? 40  TYR C O   1 
ATOM   1705 C CB  . TYR C 1 41 ? 23.324  -30.145 29.290  1.00 45.32  ? 40  TYR C CB  1 
ATOM   1706 C CG  . TYR C 1 41 ? 24.534  -29.280 29.662  1.00 52.16  ? 40  TYR C CG  1 
ATOM   1707 C CD1 . TYR C 1 41 ? 25.824  -29.621 29.267  1.00 49.96  ? 40  TYR C CD1 1 
ATOM   1708 C CD2 . TYR C 1 41 ? 24.384  -28.093 30.379  1.00 47.69  ? 40  TYR C CD2 1 
ATOM   1709 C CE1 . TYR C 1 41 ? 26.918  -28.833 29.596  1.00 59.39  ? 40  TYR C CE1 1 
ATOM   1710 C CE2 . TYR C 1 41 ? 25.466  -27.283 30.692  1.00 54.60  ? 40  TYR C CE2 1 
ATOM   1711 C CZ  . TYR C 1 41 ? 26.739  -27.652 30.301  1.00 62.07  ? 40  TYR C CZ  1 
ATOM   1712 O OH  . TYR C 1 41 ? 27.800  -26.850 30.614  1.00 66.23  ? 40  TYR C OH  1 
ATOM   1713 N N   . PRO C 1 42 ? 20.615  -31.803 30.269  1.00 45.09  ? 41  PRO C N   1 
ATOM   1714 C CA  . PRO C 1 42 ? 19.338  -32.287 29.755  1.00 43.55  ? 41  PRO C CA  1 
ATOM   1715 C C   . PRO C 1 42 ? 18.977  -31.322 28.629  1.00 45.89  ? 41  PRO C C   1 
ATOM   1716 O O   . PRO C 1 42 ? 19.057  -30.093 28.796  1.00 44.67  ? 41  PRO C O   1 
ATOM   1717 C CB  . PRO C 1 42 ? 18.406  -32.181 30.977  1.00 46.51  ? 41  PRO C CB  1 
ATOM   1718 C CG  . PRO C 1 42 ? 18.923  -30.956 31.707  1.00 48.33  ? 41  PRO C CG  1 
ATOM   1719 C CD  . PRO C 1 42 ? 20.435  -30.925 31.438  1.00 45.19  ? 41  PRO C CD  1 
ATOM   1720 N N   . ILE C 1 43 ? 18.633  -31.903 27.480  1.00 44.03  ? 42  ILE C N   1 
ATOM   1721 C CA  . ILE C 1 43 ? 18.337  -31.163 26.258  1.00 44.60  ? 42  ILE C CA  1 
ATOM   1722 C C   . ILE C 1 43 ? 16.902  -31.482 25.836  1.00 44.52  ? 42  ILE C C   1 
ATOM   1723 O O   . ILE C 1 43 ? 16.523  -32.645 25.818  1.00 49.53  ? 42  ILE C O   1 
ATOM   1724 C CB  . ILE C 1 43 ? 19.334  -31.591 25.162  1.00 40.44  ? 42  ILE C CB  1 
ATOM   1725 C CG1 . ILE C 1 43 ? 20.810  -31.379 25.586  1.00 38.97  ? 42  ILE C CG1 1 
ATOM   1726 C CG2 . ILE C 1 43 ? 18.994  -30.999 23.782  1.00 32.39  ? 42  ILE C CG2 1 
ATOM   1727 C CD1 . ILE C 1 43 ? 21.165  -30.008 26.137  1.00 38.93  ? 42  ILE C CD1 1 
ATOM   1728 N N   . PHE C 1 44 ? 16.111  -30.448 25.509  1.00 44.13  ? 43  PHE C N   1 
ATOM   1729 C CA  . PHE C 1 44 ? 14.822  -30.591 24.844  1.00 42.01  ? 43  PHE C CA  1 
ATOM   1730 C C   . PHE C 1 44 ? 14.983  -30.217 23.367  1.00 39.33  ? 43  PHE C C   1 
ATOM   1731 O O   . PHE C 1 44 ? 15.465  -29.123 23.029  1.00 36.09  ? 43  PHE C O   1 
ATOM   1732 C CB  . PHE C 1 44 ? 13.824  -29.667 25.567  1.00 49.55  ? 43  PHE C CB  1 
ATOM   1733 C CG  . PHE C 1 44 ? 12.419  -29.581 24.982  1.00 49.18  ? 43  PHE C CG  1 
ATOM   1734 C CD1 . PHE C 1 44 ? 11.428  -30.495 25.357  1.00 58.51  ? 43  PHE C CD1 1 
ATOM   1735 C CD2 . PHE C 1 44 ? 12.071  -28.564 24.085  1.00 55.02  ? 43  PHE C CD2 1 
ATOM   1736 C CE1 . PHE C 1 44 ? 10.142  -30.423 24.826  1.00 56.21  ? 43  PHE C CE1 1 
ATOM   1737 C CE2 . PHE C 1 44 ? 10.784  -28.501 23.541  1.00 51.82  ? 43  PHE C CE2 1 
ATOM   1738 C CZ  . PHE C 1 44 ? 9.823   -29.429 23.916  1.00 54.79  ? 43  PHE C CZ  1 
ATOM   1739 N N   . PHE C 1 45 ? 14.565  -31.127 22.486  1.00 36.17  ? 44  PHE C N   1 
ATOM   1740 C CA  . PHE C 1 45 ? 14.696  -30.913 21.052  1.00 42.65  ? 44  PHE C CA  1 
ATOM   1741 C C   . PHE C 1 45 ? 13.410  -30.275 20.531  1.00 44.54  ? 44  PHE C C   1 
ATOM   1742 O O   . PHE C 1 45 ? 12.330  -30.847 20.701  1.00 48.38  ? 44  PHE C O   1 
ATOM   1743 C CB  . PHE C 1 45 ? 14.996  -32.198 20.261  1.00 42.92  ? 44  PHE C CB  1 
ATOM   1744 C CG  . PHE C 1 45 ? 16.352  -32.808 20.593  1.00 41.60  ? 44  PHE C CG  1 
ATOM   1745 C CD1 . PHE C 1 45 ? 17.470  -32.524 19.819  1.00 36.10  ? 44  PHE C CD1 1 
ATOM   1746 C CD2 . PHE C 1 45 ? 16.522  -33.622 21.719  1.00 44.12  ? 44  PHE C CD2 1 
ATOM   1747 C CE1 . PHE C 1 45 ? 18.718  -33.076 20.139  1.00 39.96  ? 44  PHE C CE1 1 
ATOM   1748 C CE2 . PHE C 1 45 ? 17.772  -34.157 22.041  1.00 41.36  ? 44  PHE C CE2 1 
ATOM   1749 C CZ  . PHE C 1 45 ? 18.871  -33.877 21.265  1.00 38.17  ? 44  PHE C CZ  1 
ATOM   1750 N N   . PHE C 1 46 ? 13.540  -29.124 19.851  1.00 38.93  ? 45  PHE C N   1 
ATOM   1751 C CA  . PHE C 1 46 ? 12.387  -28.541 19.182  1.00 38.14  ? 45  PHE C CA  1 
ATOM   1752 C C   . PHE C 1 46 ? 11.835  -29.460 18.084  1.00 44.01  ? 45  PHE C C   1 
ATOM   1753 O O   . PHE C 1 46 ? 12.573  -30.269 17.493  1.00 41.17  ? 45  PHE C O   1 
ATOM   1754 C CB  . PHE C 1 46 ? 12.701  -27.118 18.707  1.00 35.94  ? 45  PHE C CB  1 
ATOM   1755 C CG  . PHE C 1 46 ? 12.925  -26.145 19.850  1.00 39.12  ? 45  PHE C CG  1 
ATOM   1756 C CD1 . PHE C 1 46 ? 11.874  -25.795 20.692  1.00 38.58  ? 45  PHE C CD1 1 
ATOM   1757 C CD2 . PHE C 1 46 ? 14.179  -25.569 20.068  1.00 38.70  ? 45  PHE C CD2 1 
ATOM   1758 C CE1 . PHE C 1 46 ? 12.082  -24.897 21.741  1.00 44.31  ? 45  PHE C CE1 1 
ATOM   1759 C CE2 . PHE C 1 46 ? 14.373  -24.666 21.106  1.00 40.72  ? 45  PHE C CE2 1 
ATOM   1760 C CZ  . PHE C 1 46 ? 13.331  -24.341 21.953  1.00 39.72  ? 45  PHE C CZ  1 
ATOM   1761 N N   . GLY C 1 47 ? 10.524  -29.306 17.813  1.00 39.36  ? 46  GLY C N   1 
ATOM   1762 C CA  . GLY C 1 47 ? 9.877   -30.015 16.715  1.00 46.93  ? 46  GLY C CA  1 
ATOM   1763 C C   . GLY C 1 47 ? 9.475   -31.437 17.112  1.00 57.22  ? 46  GLY C C   1 
ATOM   1764 O O   . GLY C 1 47 ? 8.283   -31.748 17.171  1.00 46.80  ? 46  GLY C O   1 
ATOM   1765 N N   . THR C 1 48 ? 10.475  -32.286 17.407  1.00 53.01  ? 47  THR C N   1 
ATOM   1766 C CA  . THR C 1 48 ? 10.184  -33.621 17.898  1.00 54.00  ? 47  THR C CA  1 
ATOM   1767 C C   . THR C 1 48 ? 9.624   -33.507 19.310  1.00 49.26  ? 47  THR C C   1 
ATOM   1768 O O   . THR C 1 48 ? 8.701   -34.229 19.636  1.00 51.86  ? 47  THR C O   1 
ATOM   1769 C CB  . THR C 1 48 ? 11.396  -34.553 17.830  1.00 47.54  ? 47  THR C CB  1 
ATOM   1770 O OG1 . THR C 1 48 ? 12.341  -34.114 18.809  1.00 52.94  ? 47  THR C OG1 1 
ATOM   1771 C CG2 . THR C 1 48 ? 11.963  -34.606 16.428  1.00 49.02  ? 47  THR C CG2 1 
ATOM   1772 N N   . HIS C 1 49 ? 10.181  -32.582 20.109  1.00 57.26  ? 48  HIS C N   1 
ATOM   1773 C CA  . HIS C 1 49 ? 9.876   -32.372 21.523  1.00 52.28  ? 48  HIS C CA  1 
ATOM   1774 C C   . HIS C 1 49 ? 10.389  -33.526 22.396  1.00 54.11  ? 48  HIS C C   1 
ATOM   1775 O O   . HIS C 1 49 ? 9.868   -33.746 23.483  1.00 57.33  ? 48  HIS C O   1 
ATOM   1776 C CB  . HIS C 1 49 ? 8.394   -32.036 21.759  1.00 55.36  ? 48  HIS C CB  1 
ATOM   1777 C CG  . HIS C 1 49 ? 7.847   -30.961 20.882  1.00 64.56  ? 48  HIS C CG  1 
ATOM   1778 N ND1 . HIS C 1 49 ? 6.887   -31.199 19.920  1.00 67.02  ? 48  HIS C ND1 1 
ATOM   1779 C CD2 . HIS C 1 49 ? 8.118   -29.646 20.815  1.00 66.26  ? 48  HIS C CD2 1 
ATOM   1780 C CE1 . HIS C 1 49 ? 6.590   -30.057 19.303  1.00 69.92  ? 48  HIS C CE1 1 
ATOM   1781 N NE2 . HIS C 1 49 ? 7.328   -29.104 19.831  1.00 69.45  ? 48  HIS C NE2 1 
ATOM   1782 N N   . GLU C 1 50 ? 11.437  -34.231 21.942  1.00 51.56  ? 49  GLU C N   1 
ATOM   1783 C CA  . GLU C 1 50 ? 12.083  -35.260 22.746  1.00 50.07  ? 49  GLU C CA  1 
ATOM   1784 C C   . GLU C 1 50 ? 13.135  -34.640 23.663  1.00 51.14  ? 49  GLU C C   1 
ATOM   1785 O O   . GLU C 1 50 ? 13.295  -33.419 23.682  1.00 50.20  ? 49  GLU C O   1 
ATOM   1786 C CB  . GLU C 1 50 ? 12.602  -36.382 21.854  1.00 49.12  ? 49  GLU C CB  1 
ATOM   1787 C CG  . GLU C 1 50 ? 11.449  -37.193 21.276  1.00 58.54  ? 49  GLU C CG  1 
ATOM   1788 C CD  . GLU C 1 50 ? 11.826  -38.013 20.058  1.00 69.60  ? 49  GLU C CD  1 
ATOM   1789 O OE1 . GLU C 1 50 ? 12.991  -37.984 19.603  1.00 77.81  ? 49  GLU C OE1 1 
ATOM   1790 O OE2 . GLU C 1 50 ? 10.914  -38.678 19.547  1.00 70.42  ? 49  GLU C OE2 1 
ATOM   1791 N N   . THR C 1 51 ? 13.788  -35.487 24.479  1.00 53.25  ? 50  THR C N   1 
ATOM   1792 C CA  . THR C 1 51 ? 14.824  -35.071 25.429  1.00 53.68  ? 50  THR C CA  1 
ATOM   1793 C C   . THR C 1 51 ? 15.945  -36.116 25.459  1.00 48.34  ? 50  THR C C   1 
ATOM   1794 O O   . THR C 1 51 ? 15.743  -37.282 25.157  1.00 48.20  ? 50  THR C O   1 
ATOM   1795 C CB  . THR C 1 51 ? 14.288  -34.764 26.833  1.00 48.56  ? 50  THR C CB  1 
ATOM   1796 O OG1 . THR C 1 51 ? 13.534  -35.905 27.220  1.00 54.93  ? 50  THR C OG1 1 
ATOM   1797 C CG2 . THR C 1 51 ? 13.335  -33.583 26.914  1.00 51.95  ? 50  THR C CG2 1 
ATOM   1798 N N   . ALA C 1 52 ? 17.154  -35.680 25.793  1.00 49.90  ? 51  ALA C N   1 
ATOM   1799 C CA  . ALA C 1 52 ? 18.274  -36.588 25.937  1.00 46.45  ? 51  ALA C CA  1 
ATOM   1800 C C   . ALA C 1 52 ? 19.329  -35.862 26.755  1.00 52.57  ? 51  ALA C C   1 
ATOM   1801 O O   . ALA C 1 52 ? 19.163  -34.670 27.049  1.00 47.39  ? 51  ALA C O   1 
ATOM   1802 C CB  . ALA C 1 52 ? 18.807  -36.994 24.578  1.00 52.08  ? 51  ALA C CB  1 
ATOM   1803 N N   . PHE C 1 53 ? 20.370  -36.616 27.139  1.00 45.16  ? 52  PHE C N   1 
ATOM   1804 C CA  . PHE C 1 53 ? 21.503  -36.071 27.861  1.00 45.40  ? 52  PHE C CA  1 
ATOM   1805 C C   . PHE C 1 53 ? 22.633  -35.929 26.865  1.00 45.92  ? 52  PHE C C   1 
ATOM   1806 O O   . PHE C 1 53 ? 22.914  -36.873 26.136  1.00 47.38  ? 52  PHE C O   1 
ATOM   1807 C CB  . PHE C 1 53 ? 21.859  -37.054 28.976  1.00 48.91  ? 52  PHE C CB  1 
ATOM   1808 C CG  . PHE C 1 53 ? 20.923  -36.902 30.160  1.00 49.48  ? 52  PHE C CG  1 
ATOM   1809 C CD1 . PHE C 1 53 ? 20.745  -35.656 30.765  1.00 54.59  ? 52  PHE C CD1 1 
ATOM   1810 C CD2 . PHE C 1 53 ? 20.184  -37.981 30.635  1.00 57.05  ? 52  PHE C CD2 1 
ATOM   1811 C CE1 . PHE C 1 53 ? 19.863  -35.502 31.829  1.00 47.07  ? 52  PHE C CE1 1 
ATOM   1812 C CE2 . PHE C 1 53 ? 19.320  -37.827 31.717  1.00 52.85  ? 52  PHE C CE2 1 
ATOM   1813 C CZ  . PHE C 1 53 ? 19.158  -36.590 32.306  1.00 51.35  ? 52  PHE C CZ  1 
ATOM   1814 N N   . LEU C 1 54 ? 23.205  -34.726 26.791  1.00 42.97  ? 53  LEU C N   1 
ATOM   1815 C CA  . LEU C 1 54 ? 24.282  -34.465 25.856  1.00 42.61  ? 53  LEU C CA  1 
ATOM   1816 C C   . LEU C 1 54 ? 25.428  -33.801 26.619  1.00 47.06  ? 53  LEU C C   1 
ATOM   1817 O O   . LEU C 1 54 ? 25.193  -33.054 27.579  1.00 42.50  ? 53  LEU C O   1 
ATOM   1818 C CB  . LEU C 1 54 ? 23.852  -33.605 24.653  1.00 40.67  ? 53  LEU C CB  1 
ATOM   1819 C CG  . LEU C 1 54 ? 22.938  -34.246 23.602  1.00 46.97  ? 53  LEU C CG  1 
ATOM   1820 C CD1 . LEU C 1 54 ? 22.889  -33.397 22.324  1.00 42.79  ? 53  LEU C CD1 1 
ATOM   1821 C CD2 . LEU C 1 54 ? 23.346  -35.665 23.268  1.00 41.61  ? 53  LEU C CD2 1 
ATOM   1822 N N   . GLY C 1 55 ? 26.660  -34.077 26.164  1.00 47.98  ? 54  GLY C N   1 
ATOM   1823 C CA  . GLY C 1 55 ? 27.849  -33.388 26.652  1.00 45.42  ? 54  GLY C CA  1 
ATOM   1824 C C   . GLY C 1 55 ? 28.055  -32.083 25.881  1.00 49.18  ? 54  GLY C C   1 
ATOM   1825 O O   . GLY C 1 55 ? 27.541  -31.934 24.763  1.00 47.94  ? 54  GLY C O   1 
ATOM   1826 N N   . PRO C 1 56 ? 28.794  -31.100 26.452  1.00 48.15  ? 55  PRO C N   1 
ATOM   1827 C CA  . PRO C 1 56 ? 28.880  -29.760 25.860  1.00 50.89  ? 55  PRO C CA  1 
ATOM   1828 C C   . PRO C 1 56 ? 29.539  -29.810 24.488  1.00 44.97  ? 55  PRO C C   1 
ATOM   1829 O O   . PRO C 1 56 ? 29.350  -28.925 23.662  1.00 52.23  ? 55  PRO C O   1 
ATOM   1830 C CB  . PRO C 1 56 ? 29.714  -28.957 26.902  1.00 47.43  ? 55  PRO C CB  1 
ATOM   1831 C CG  . PRO C 1 56 ? 30.504  -30.021 27.618  1.00 43.51  ? 55  PRO C CG  1 
ATOM   1832 C CD  . PRO C 1 56 ? 29.538  -31.207 27.723  1.00 44.59  ? 55  PRO C CD  1 
ATOM   1833 N N   . LYS C 1 57 ? 30.279  -30.885 24.230  1.00 43.42  ? 56  LYS C N   1 
ATOM   1834 C CA  . LYS C 1 57 ? 30.929  -31.030 22.942  1.00 50.26  ? 56  LYS C CA  1 
ATOM   1835 C C   . LYS C 1 57 ? 29.884  -31.138 21.829  1.00 53.95  ? 56  LYS C C   1 
ATOM   1836 O O   . LYS C 1 57 ? 30.200  -30.843 20.674  1.00 51.80  ? 56  LYS C O   1 
ATOM   1837 C CB  . LYS C 1 57 ? 31.892  -32.228 22.897  1.00 52.29  ? 56  LYS C CB  1 
ATOM   1838 N N   . ASP C 1 58 ? 28.662  -31.586 22.164  1.00 47.02  ? 57  ASP C N   1 
ATOM   1839 C CA  . ASP C 1 58 ? 27.644  -31.797 21.141  1.00 47.82  ? 57  ASP C CA  1 
ATOM   1840 C C   . ASP C 1 58 ? 26.696  -30.607 21.069  1.00 45.90  ? 57  ASP C C   1 
ATOM   1841 O O   . ASP C 1 58 ? 25.626  -30.705 20.444  1.00 46.43  ? 57  ASP C O   1 
ATOM   1842 C CB  . ASP C 1 58 ? 26.816  -33.051 21.382  1.00 49.76  ? 57  ASP C CB  1 
ATOM   1843 C CG  . ASP C 1 58 ? 27.623  -34.325 21.570  1.00 59.11  ? 57  ASP C CG  1 
ATOM   1844 O OD1 . ASP C 1 58 ? 28.597  -34.522 20.812  1.00 56.33  ? 57  ASP C OD1 1 
ATOM   1845 O OD2 . ASP C 1 58 ? 27.267  -35.103 22.475  1.00 67.70  ? 57  ASP C OD2 1 
ATOM   1846 N N   . LEU C 1 59 ? 27.101  -29.508 21.728  1.00 43.34  ? 58  LEU C N   1 
ATOM   1847 C CA  . LEU C 1 59 ? 26.228  -28.380 21.994  1.00 45.11  ? 58  LEU C CA  1 
ATOM   1848 C C   . LEU C 1 59 ? 26.861  -27.125 21.429  1.00 47.50  ? 58  LEU C C   1 
ATOM   1849 O O   . LEU C 1 59 ? 28.064  -26.953 21.580  1.00 48.85  ? 58  LEU C O   1 
ATOM   1850 C CB  . LEU C 1 59 ? 25.989  -28.228 23.491  1.00 40.63  ? 58  LEU C CB  1 
ATOM   1851 C CG  . LEU C 1 59 ? 25.138  -29.325 24.133  1.00 42.00  ? 58  LEU C CG  1 
ATOM   1852 C CD1 . LEU C 1 59 ? 24.871  -28.945 25.584  1.00 40.61  ? 58  LEU C CD1 1 
ATOM   1853 C CD2 . LEU C 1 59 ? 23.828  -29.565 23.420  1.00 36.33  ? 58  LEU C CD2 1 
ATOM   1854 N N   . PHE C 1 60 ? 26.049  -26.283 20.770  1.00 45.53  ? 59  PHE C N   1 
ATOM   1855 C CA  . PHE C 1 60 ? 26.590  -25.095 20.118  1.00 50.31  ? 59  PHE C CA  1 
ATOM   1856 C C   . PHE C 1 60 ? 25.596  -23.957 20.287  1.00 54.32  ? 59  PHE C C   1 
ATOM   1857 O O   . PHE C 1 60 ? 24.417  -24.138 20.001  1.00 43.58  ? 59  PHE C O   1 
ATOM   1858 C CB  . PHE C 1 60 ? 26.856  -25.299 18.626  1.00 47.33  ? 59  PHE C CB  1 
ATOM   1859 C CG  . PHE C 1 60 ? 27.604  -26.577 18.267  1.00 47.30  ? 59  PHE C CG  1 
ATOM   1860 C CD1 . PHE C 1 60 ? 26.983  -27.825 18.358  1.00 43.50  ? 59  PHE C CD1 1 
ATOM   1861 C CD2 . PHE C 1 60 ? 28.924  -26.522 17.806  1.00 51.87  ? 59  PHE C CD2 1 
ATOM   1862 C CE1 . PHE C 1 60 ? 27.680  -28.986 18.051  1.00 42.96  ? 59  PHE C CE1 1 
ATOM   1863 C CE2 . PHE C 1 60 ? 29.610  -27.687 17.460  1.00 49.03  ? 59  PHE C CE2 1 
ATOM   1864 C CZ  . PHE C 1 60 ? 28.985  -28.911 17.591  1.00 49.80  ? 59  PHE C CZ  1 
ATOM   1865 N N   . PRO C 1 61 ? 26.021  -22.773 20.789  1.00 55.22  ? 60  PRO C N   1 
ATOM   1866 C CA  . PRO C 1 61 ? 25.086  -21.666 21.002  1.00 54.28  ? 60  PRO C CA  1 
ATOM   1867 C C   . PRO C 1 61 ? 24.310  -21.303 19.731  1.00 49.60  ? 60  PRO C C   1 
ATOM   1868 O O   . PRO C 1 61 ? 24.898  -21.232 18.651  1.00 53.87  ? 60  PRO C O   1 
ATOM   1869 C CB  . PRO C 1 61 ? 26.022  -20.545 21.519  1.00 58.88  ? 60  PRO C CB  1 
ATOM   1870 C CG  . PRO C 1 61 ? 27.210  -21.282 22.120  1.00 57.69  ? 60  PRO C CG  1 
ATOM   1871 C CD  . PRO C 1 61 ? 27.409  -22.442 21.158  1.00 61.43  ? 60  PRO C CD  1 
ATOM   1872 N N   . TYR C 1 62 ? 22.980  -21.139 19.882  1.00 45.46  ? 61  TYR C N   1 
ATOM   1873 C CA  . TYR C 1 62 ? 22.039  -20.871 18.801  1.00 48.34  ? 61  TYR C CA  1 
ATOM   1874 C C   . TYR C 1 62 ? 22.424  -19.618 18.014  1.00 54.77  ? 61  TYR C C   1 
ATOM   1875 O O   . TYR C 1 62 ? 22.526  -19.689 16.789  1.00 52.76  ? 61  TYR C O   1 
ATOM   1876 C CB  . TYR C 1 62 ? 20.577  -20.778 19.250  1.00 53.52  ? 61  TYR C CB  1 
ATOM   1877 C CG  . TYR C 1 62 ? 19.603  -20.286 18.187  1.00 53.96  ? 61  TYR C CG  1 
ATOM   1878 C CD1 . TYR C 1 62 ? 19.330  -21.043 17.047  1.00 53.99  ? 61  TYR C CD1 1 
ATOM   1879 C CD2 . TYR C 1 62 ? 18.961  -19.059 18.320  1.00 53.74  ? 61  TYR C CD2 1 
ATOM   1880 C CE1 . TYR C 1 62 ? 18.443  -20.593 16.079  1.00 49.31  ? 61  TYR C CE1 1 
ATOM   1881 C CE2 . TYR C 1 62 ? 18.062  -18.601 17.366  1.00 51.57  ? 61  TYR C CE2 1 
ATOM   1882 C CZ  . TYR C 1 62 ? 17.804  -19.371 16.241  1.00 50.76  ? 61  TYR C CZ  1 
ATOM   1883 O OH  . TYR C 1 62 ? 16.936  -18.904 15.296  1.00 50.27  ? 61  TYR C OH  1 
ATOM   1884 N N   . ASP C 1 63 ? 22.661  -18.497 18.716  1.00 51.64  ? 62  ASP C N   1 
ATOM   1885 C CA  . ASP C 1 63 ? 23.110  -17.267 18.075  1.00 57.53  ? 62  ASP C CA  1 
ATOM   1886 C C   . ASP C 1 63 ? 24.416  -17.446 17.308  1.00 56.47  ? 62  ASP C C   1 
ATOM   1887 O O   . ASP C 1 63 ? 24.452  -17.148 16.115  1.00 66.37  ? 62  ASP C O   1 
ATOM   1888 C CB  . ASP C 1 63 ? 23.065  -16.061 18.998  1.00 62.32  ? 62  ASP C CB  1 
ATOM   1889 C CG  . ASP C 1 63 ? 21.678  -15.453 19.060  1.00 70.62  ? 62  ASP C CG  1 
ATOM   1890 O OD1 . ASP C 1 63 ? 21.034  -15.589 20.117  1.00 71.60  ? 62  ASP C OD1 1 
ATOM   1891 O OD2 . ASP C 1 63 ? 21.236  -14.913 18.019  1.00 83.77  ? 62  ASP C OD2 1 
ATOM   1892 N N   . LYS C 1 64 ? 25.465  -17.945 17.975  1.00 59.20  ? 63  LYS C N   1 
ATOM   1893 C CA  . LYS C 1 64 ? 26.765  -18.119 17.332  1.00 54.25  ? 63  LYS C CA  1 
ATOM   1894 C C   . LYS C 1 64 ? 26.690  -19.033 16.100  1.00 51.45  ? 63  LYS C C   1 
ATOM   1895 O O   . LYS C 1 64 ? 27.471  -18.841 15.169  1.00 54.58  ? 63  LYS C O   1 
ATOM   1896 C CB  . LYS C 1 64 ? 27.886  -18.567 18.284  1.00 50.17  ? 63  LYS C CB  1 
ATOM   1897 N N   . SER C 1 65 ? 25.781  -20.032 16.077  1.00 52.68  ? 64  SER C N   1 
ATOM   1898 C CA  . SER C 1 65 ? 25.989  -21.139 15.145  1.00 50.78  ? 64  SER C CA  1 
ATOM   1899 C C   . SER C 1 65 ? 24.856  -21.326 14.131  1.00 50.85  ? 64  SER C C   1 
ATOM   1900 O O   . SER C 1 65 ? 24.937  -22.228 13.297  1.00 42.41  ? 64  SER C O   1 
ATOM   1901 C CB  . SER C 1 65 ? 26.314  -22.435 15.873  1.00 54.34  ? 64  SER C CB  1 
ATOM   1902 O OG  . SER C 1 65 ? 25.147  -22.944 16.496  1.00 51.18  ? 64  SER C OG  1 
ATOM   1903 N N   . LYS C 1 66 ? 23.821  -20.470 14.188  1.00 48.19  ? 65  LYS C N   1 
ATOM   1904 C CA  . LYS C 1 66 ? 22.619  -20.676 13.385  1.00 48.75  ? 65  LYS C CA  1 
ATOM   1905 C C   . LYS C 1 66 ? 22.864  -20.421 11.897  1.00 49.00  ? 65  LYS C C   1 
ATOM   1906 O O   . LYS C 1 66 ? 22.187  -21.013 11.053  1.00 46.09  ? 65  LYS C O   1 
ATOM   1907 C CB  . LYS C 1 66 ? 21.400  -19.873 13.856  1.00 46.47  ? 65  LYS C CB  1 
ATOM   1908 C CG  . LYS C 1 66 ? 21.550  -18.358 13.838  1.00 48.94  ? 65  LYS C CG  1 
ATOM   1909 C CD  . LYS C 1 66 ? 20.282  -17.616 14.229  1.00 58.71  ? 65  LYS C CD  1 
ATOM   1910 C CE  . LYS C 1 66 ? 20.458  -16.148 14.044  1.00 56.71  ? 65  LYS C CE  1 
ATOM   1911 N NZ  . LYS C 1 66 ? 19.643  -15.421 15.021  1.00 63.95  ? 65  LYS C NZ  1 
ATOM   1912 N N   . ASP C 1 67 ? 23.817  -19.537 11.568  1.00 52.79  ? 66  ASP C N   1 
ATOM   1913 C CA  . ASP C 1 67 ? 24.168  -19.335 10.167  1.00 55.41  ? 66  ASP C CA  1 
ATOM   1914 C C   . ASP C 1 67 ? 24.580  -20.664 9.530   1.00 57.06  ? 66  ASP C C   1 
ATOM   1915 O O   . ASP C 1 67 ? 24.304  -20.886 8.360   1.00 59.40  ? 66  ASP C O   1 
ATOM   1916 C CB  . ASP C 1 67 ? 25.109  -18.161 9.931   1.00 56.86  ? 66  ASP C CB  1 
ATOM   1917 C CG  . ASP C 1 67 ? 26.474  -18.252 10.595  1.00 70.50  ? 66  ASP C CG  1 
ATOM   1918 O OD1 . ASP C 1 67 ? 26.819  -19.346 11.089  1.00 80.84  ? 66  ASP C OD1 1 
ATOM   1919 O OD2 . ASP C 1 67 ? 27.162  -17.212 10.659  1.00 77.87  ? 66  ASP C OD2 1 
ATOM   1920 N N   . LYS C 1 68 ? 25.192  -21.561 10.316  1.00 50.23  ? 67  LYS C N   1 
ATOM   1921 C CA  . LYS C 1 68 ? 25.689  -22.831 9.818   1.00 50.52  ? 67  LYS C CA  1 
ATOM   1922 C C   . LYS C 1 68 ? 24.647  -23.957 9.962   1.00 52.85  ? 67  LYS C C   1 
ATOM   1923 O O   . LYS C 1 68 ? 24.500  -24.789 9.061   1.00 49.60  ? 67  LYS C O   1 
ATOM   1924 C CB  . LYS C 1 68 ? 27.019  -23.069 10.545  1.00 56.96  ? 67  LYS C CB  1 
ATOM   1925 C CG  . LYS C 1 68 ? 27.726  -24.387 10.227  1.00 51.11  ? 67  LYS C CG  1 
ATOM   1926 C CD  . LYS C 1 68 ? 28.996  -24.563 11.053  1.00 69.25  ? 67  LYS C CD  1 
ATOM   1927 C CE  . LYS C 1 68 ? 29.694  -25.895 10.938  1.00 77.57  ? 67  LYS C CE  1 
ATOM   1928 N NZ  . LYS C 1 68 ? 30.030  -26.264 9.558   1.00 81.80  ? 67  LYS C NZ  1 
ATOM   1929 N N   . TYR C 1 69 ? 23.936  -24.042 11.100  1.00 46.35  ? 68  TYR C N   1 
ATOM   1930 C CA  . TYR C 1 69 ? 23.075  -25.206 11.281  1.00 44.68  ? 68  TYR C CA  1 
ATOM   1931 C C   . TYR C 1 69 ? 21.591  -24.866 11.153  1.00 45.21  ? 68  TYR C C   1 
ATOM   1932 O O   . TYR C 1 69 ? 20.770  -25.773 11.076  1.00 42.47  ? 68  TYR C O   1 
ATOM   1933 C CB  . TYR C 1 69 ? 23.237  -25.825 12.665  1.00 44.22  ? 68  TYR C CB  1 
ATOM   1934 C CG  . TYR C 1 69 ? 24.667  -26.251 12.936  1.00 51.21  ? 68  TYR C CG  1 
ATOM   1935 C CD1 . TYR C 1 69 ? 25.353  -27.057 12.037  1.00 51.06  ? 68  TYR C CD1 1 
ATOM   1936 C CD2 . TYR C 1 69 ? 25.336  -25.805 14.066  1.00 46.87  ? 68  TYR C CD2 1 
ATOM   1937 C CE1 . TYR C 1 69 ? 26.650  -27.465 12.288  1.00 48.91  ? 68  TYR C CE1 1 
ATOM   1938 C CE2 . TYR C 1 69 ? 26.642  -26.192 14.314  1.00 50.75  ? 68  TYR C CE2 1 
ATOM   1939 C CZ  . TYR C 1 69 ? 27.299  -27.023 13.426  1.00 48.65  ? 68  TYR C CZ  1 
ATOM   1940 O OH  . TYR C 1 69 ? 28.588  -27.403 13.677  1.00 53.34  ? 68  TYR C OH  1 
ATOM   1941 N N   . GLY C 1 70 ? 21.244  -23.578 11.206  1.00 40.77  ? 69  GLY C N   1 
ATOM   1942 C CA  . GLY C 1 70 ? 19.851  -23.171 11.090  1.00 45.77  ? 69  GLY C CA  1 
ATOM   1943 C C   . GLY C 1 70 ? 19.450  -23.064 9.622   1.00 47.92  ? 69  GLY C C   1 
ATOM   1944 O O   . GLY C 1 70 ? 19.427  -21.976 9.045   1.00 47.57  ? 69  GLY C O   1 
ATOM   1945 N N   . LYS C 1 71 ? 19.173  -24.214 9.019   1.00 44.71  ? 70  LYS C N   1 
ATOM   1946 C CA  . LYS C 1 71 ? 18.861  -24.276 7.600   1.00 50.13  ? 70  LYS C CA  1 
ATOM   1947 C C   . LYS C 1 71 ? 17.993  -25.509 7.409   1.00 49.11  ? 70  LYS C C   1 
ATOM   1948 O O   . LYS C 1 71 ? 18.186  -26.504 8.094   1.00 51.11  ? 70  LYS C O   1 
ATOM   1949 C CB  . LYS C 1 71 ? 20.127  -24.363 6.737   1.00 51.35  ? 70  LYS C CB  1 
ATOM   1950 C CG  . LYS C 1 71 ? 21.021  -25.573 7.041   1.00 60.69  ? 70  LYS C CG  1 
ATOM   1951 C CD  . LYS C 1 71 ? 22.269  -25.769 6.181   1.00 59.17  ? 70  LYS C CD  1 
ATOM   1952 C CE  . LYS C 1 71 ? 23.061  -27.023 6.432   1.00 59.32  ? 70  LYS C CE  1 
ATOM   1953 N N   . PRO C 1 72 ? 16.968  -25.483 6.534   1.00 48.29  ? 71  PRO C N   1 
ATOM   1954 C CA  . PRO C 1 72 ? 15.968  -26.549 6.542   1.00 41.27  ? 71  PRO C CA  1 
ATOM   1955 C C   . PRO C 1 72 ? 16.569  -27.896 6.142   1.00 43.48  ? 71  PRO C C   1 
ATOM   1956 O O   . PRO C 1 72 ? 17.667  -27.984 5.583   1.00 44.62  ? 71  PRO C O   1 
ATOM   1957 C CB  . PRO C 1 72 ? 14.891  -26.043 5.567   1.00 41.35  ? 71  PRO C CB  1 
ATOM   1958 C CG  . PRO C 1 72 ? 15.173  -24.561 5.490   1.00 43.67  ? 71  PRO C CG  1 
ATOM   1959 C CD  . PRO C 1 72 ? 16.696  -24.426 5.546   1.00 46.13  ? 71  PRO C CD  1 
ATOM   1960 N N   . ASN C 1 73 ? 15.870  -28.964 6.511   1.00 41.44  ? 72  ASN C N   1 
ATOM   1961 C CA  . ASN C 1 73 ? 16.165  -30.271 5.949   1.00 51.45  ? 72  ASN C CA  1 
ATOM   1962 C C   . ASN C 1 73 ? 14.982  -31.162 6.263   1.00 47.54  ? 72  ASN C C   1 
ATOM   1963 O O   . ASN C 1 73 ? 14.079  -30.740 6.983   1.00 44.62  ? 72  ASN C O   1 
ATOM   1964 C CB  . ASN C 1 73 ? 17.490  -30.881 6.406   1.00 58.35  ? 72  ASN C CB  1 
ATOM   1965 C CG  . ASN C 1 73 ? 17.413  -31.461 7.796   1.00 52.23  ? 72  ASN C CG  1 
ATOM   1966 O OD1 . ASN C 1 73 ? 16.558  -32.317 8.080   1.00 50.59  ? 72  ASN C OD1 1 
ATOM   1967 N ND2 . ASN C 1 73 ? 18.282  -30.979 8.669   1.00 47.63  ? 72  ASN C ND2 1 
ATOM   1968 N N   . LYS C 1 74 ? 15.051  -32.396 5.755   1.00 49.06  ? 73  LYS C N   1 
ATOM   1969 C CA  . LYS C 1 74 ? 13.858  -33.169 5.475   1.00 51.48  ? 73  LYS C CA  1 
ATOM   1970 C C   . LYS C 1 74 ? 13.504  -34.059 6.657   1.00 51.50  ? 73  LYS C C   1 
ATOM   1971 O O   . LYS C 1 74 ? 12.426  -34.641 6.649   1.00 53.64  ? 73  LYS C O   1 
ATOM   1972 C CB  . LYS C 1 74 ? 14.161  -33.973 4.202   1.00 52.62  ? 73  LYS C CB  1 
ATOM   1973 N N   . ARG C 1 75 ? 14.423  -34.173 7.639   1.00 49.49  ? 74  ARG C N   1 
ATOM   1974 C CA  . ARG C 1 75 ? 14.301  -35.128 8.741   1.00 50.32  ? 74  ARG C CA  1 
ATOM   1975 C C   . ARG C 1 75 ? 13.075  -34.757 9.576   1.00 48.85  ? 74  ARG C C   1 
ATOM   1976 O O   . ARG C 1 75 ? 12.759  -33.574 9.686   1.00 45.72  ? 74  ARG C O   1 
ATOM   1977 C CB  . ARG C 1 75 ? 15.582  -35.179 9.600   1.00 43.06  ? 74  ARG C CB  1 
ATOM   1978 C CG  . ARG C 1 75 ? 16.867  -35.363 8.798   1.00 55.40  ? 74  ARG C CG  1 
ATOM   1979 C CD  . ARG C 1 75 ? 17.100  -36.775 8.231   1.00 49.92  ? 74  ARG C CD  1 
ATOM   1980 N NE  . ARG C 1 75 ? 17.031  -37.670 9.393   1.00 50.75  ? 74  ARG C NE  1 
ATOM   1981 C CZ  . ARG C 1 75 ? 18.106  -38.120 10.039  1.00 41.38  ? 74  ARG C CZ  1 
ATOM   1982 N NH1 . ARG C 1 75 ? 17.967  -38.812 11.155  1.00 44.23  ? 74  ARG C NH1 1 
ATOM   1983 N NH2 . ARG C 1 75 ? 19.306  -37.810 9.574   1.00 43.60  ? 74  ARG C NH2 1 
ATOM   1984 N N   . LYS C 1 76 ? 12.421  -35.750 10.203  1.00 47.72  ? 75  LYS C N   1 
ATOM   1985 C CA  . LYS C 1 76 ? 11.098  -35.537 10.779  1.00 47.41  ? 75  LYS C CA  1 
ATOM   1986 C C   . LYS C 1 76 ? 11.122  -34.510 11.921  1.00 49.74  ? 75  LYS C C   1 
ATOM   1987 O O   . LYS C 1 76 ? 11.832  -34.665 12.923  1.00 45.18  ? 75  LYS C O   1 
ATOM   1988 C CB  . LYS C 1 76 ? 10.402  -36.850 11.153  1.00 54.46  ? 75  LYS C CB  1 
ATOM   1989 C CG  . LYS C 1 76 ? 8.991   -37.012 10.591  1.00 63.90  ? 75  LYS C CG  1 
ATOM   1990 C CD  . LYS C 1 76 ? 8.039   -37.739 11.539  1.00 66.23  ? 75  LYS C CD  1 
ATOM   1991 N N   . GLY C 1 77 ? 10.311  -33.452 11.766  1.00 46.66  ? 76  GLY C N   1 
ATOM   1992 C CA  . GLY C 1 77 ? 10.085  -32.505 12.854  1.00 43.32  ? 76  GLY C CA  1 
ATOM   1993 C C   . GLY C 1 77 ? 11.139  -31.399 12.865  1.00 42.89  ? 76  GLY C C   1 
ATOM   1994 O O   . GLY C 1 77 ? 11.059  -30.483 13.693  1.00 48.21  ? 76  GLY C O   1 
ATOM   1995 N N   . PHE C 1 78 ? 12.118  -31.507 11.940  1.00 39.59  ? 77  PHE C N   1 
ATOM   1996 C CA  . PHE C 1 78 ? 13.241  -30.592 11.870  1.00 36.10  ? 77  PHE C CA  1 
ATOM   1997 C C   . PHE C 1 78 ? 12.716  -29.182 11.602  1.00 39.76  ? 77  PHE C C   1 
ATOM   1998 O O   . PHE C 1 78 ? 13.039  -28.261 12.338  1.00 37.93  ? 77  PHE C O   1 
ATOM   1999 C CB  . PHE C 1 78 ? 14.288  -30.936 10.802  1.00 43.43  ? 77  PHE C CB  1 
ATOM   2000 C CG  . PHE C 1 78 ? 15.574  -30.152 11.034  1.00 39.33  ? 77  PHE C CG  1 
ATOM   2001 C CD1 . PHE C 1 78 ? 15.763  -28.904 10.457  1.00 36.88  ? 77  PHE C CD1 1 
ATOM   2002 C CD2 . PHE C 1 78 ? 16.558  -30.640 11.885  1.00 36.93  ? 77  PHE C CD2 1 
ATOM   2003 C CE1 . PHE C 1 78 ? 16.919  -28.176 10.708  1.00 39.27  ? 77  PHE C CE1 1 
ATOM   2004 C CE2 . PHE C 1 78 ? 17.720  -29.914 12.123  1.00 39.58  ? 77  PHE C CE2 1 
ATOM   2005 C CZ  . PHE C 1 78 ? 17.897  -28.676 11.540  1.00 36.36  ? 77  PHE C CZ  1 
ATOM   2006 N N   . ASN C 1 79 ? 11.887  -29.025 10.563  1.00 39.70  ? 78  ASN C N   1 
ATOM   2007 C CA  . ASN C 1 79 ? 11.511  -27.691 10.132  1.00 40.64  ? 78  ASN C CA  1 
ATOM   2008 C C   . ASN C 1 79 ? 10.548  -27.068 11.133  1.00 41.13  ? 78  ASN C C   1 
ATOM   2009 O O   . ASN C 1 79 ? 10.704  -25.898 11.508  1.00 38.93  ? 78  ASN C O   1 
ATOM   2010 C CB  . ASN C 1 79 ? 11.080  -27.670 8.676   1.00 46.49  ? 78  ASN C CB  1 
ATOM   2011 C CG  . ASN C 1 79 ? 12.211  -28.078 7.768   1.00 44.55  ? 78  ASN C CG  1 
ATOM   2012 O OD1 . ASN C 1 79 ? 13.391  -27.854 8.085   1.00 44.16  ? 78  ASN C OD1 1 
ATOM   2013 N ND2 . ASN C 1 79 ? 11.859  -28.581 6.599   1.00 37.94  ? 78  ASN C ND2 1 
ATOM   2014 N N   . GLU C 1 80 ? 9.630   -27.878 11.663  1.00 46.76  ? 79  GLU C N   1 
ATOM   2015 C CA  . GLU C 1 80 ? 8.842   -27.380 12.788  1.00 42.04  ? 79  GLU C CA  1 
ATOM   2016 C C   . GLU C 1 80 ? 9.762   -26.944 13.936  1.00 43.51  ? 79  GLU C C   1 
ATOM   2017 O O   . GLU C 1 80 ? 9.534   -25.899 14.569  1.00 44.07  ? 79  GLU C O   1 
ATOM   2018 C CB  . GLU C 1 80 ? 7.831   -28.421 13.262  1.00 41.21  ? 79  GLU C CB  1 
ATOM   2019 C CG  . GLU C 1 80 ? 6.996   -27.912 14.427  1.00 44.03  ? 79  GLU C CG  1 
ATOM   2020 C CD  . GLU C 1 80 ? 5.639   -28.585 14.565  1.00 59.55  ? 79  GLU C CD  1 
ATOM   2021 O OE1 . GLU C 1 80 ? 5.358   -29.687 14.029  1.00 59.56  ? 79  GLU C OE1 1 
ATOM   2022 O OE2 . GLU C 1 80 ? 4.824   -27.926 15.230  1.00 63.92  ? 79  GLU C OE2 1 
ATOM   2023 N N   . GLY C 1 81 ? 10.832  -27.724 14.172  1.00 39.85  ? 80  GLY C N   1 
ATOM   2024 C CA  . GLY C 1 81 ? 11.842  -27.364 15.164  1.00 37.54  ? 80  GLY C CA  1 
ATOM   2025 C C   . GLY C 1 81 ? 12.450  -25.972 14.954  1.00 34.56  ? 80  GLY C C   1 
ATOM   2026 O O   . GLY C 1 81 ? 12.647  -25.219 15.916  1.00 33.38  ? 80  GLY C O   1 
ATOM   2027 N N   . LEU C 1 82 ? 12.791  -25.651 13.696  1.00 39.05  ? 81  LEU C N   1 
ATOM   2028 C CA  . LEU C 1 82 ? 13.349  -24.351 13.357  1.00 40.66  ? 81  LEU C CA  1 
ATOM   2029 C C   . LEU C 1 82 ? 12.313  -23.260 13.620  1.00 37.35  ? 81  LEU C C   1 
ATOM   2030 O O   . LEU C 1 82 ? 12.675  -22.174 14.055  1.00 40.69  ? 81  LEU C O   1 
ATOM   2031 C CB  . LEU C 1 82 ? 13.870  -24.237 11.918  1.00 43.63  ? 81  LEU C CB  1 
ATOM   2032 C CG  . LEU C 1 82 ? 14.914  -25.259 11.456  1.00 45.87  ? 81  LEU C CG  1 
ATOM   2033 C CD1 . LEU C 1 82 ? 15.169  -25.092 9.936   1.00 41.30  ? 81  LEU C CD1 1 
ATOM   2034 C CD2 . LEU C 1 82 ? 16.208  -25.085 12.230  1.00 39.25  ? 81  LEU C CD2 1 
ATOM   2035 N N   . TRP C 1 83 ? 11.045  -23.511 13.271  1.00 37.39  ? 82  TRP C N   1 
ATOM   2036 C CA  . TRP C 1 83 ? 10.027  -22.516 13.568  1.00 43.02  ? 82  TRP C CA  1 
ATOM   2037 C C   . TRP C 1 83 ? 9.965   -22.196 15.071  1.00 44.09  ? 82  TRP C C   1 
ATOM   2038 O O   . TRP C 1 83 ? 9.941   -21.025 15.473  1.00 37.77  ? 82  TRP C O   1 
ATOM   2039 C CB  . TRP C 1 83 ? 8.659   -22.875 12.969  1.00 49.04  ? 82  TRP C CB  1 
ATOM   2040 C CG  . TRP C 1 83 ? 7.664   -21.743 13.081  1.00 50.80  ? 82  TRP C CG  1 
ATOM   2041 C CD1 . TRP C 1 83 ? 7.374   -20.780 12.160  1.00 50.41  ? 82  TRP C CD1 1 
ATOM   2042 C CD2 . TRP C 1 83 ? 6.845   -21.447 14.230  1.00 51.59  ? 82  TRP C CD2 1 
ATOM   2043 N NE1 . TRP C 1 83 ? 6.416   -19.920 12.642  1.00 46.04  ? 82  TRP C NE1 1 
ATOM   2044 C CE2 . TRP C 1 83 ? 6.080   -20.306 13.907  1.00 49.79  ? 82  TRP C CE2 1 
ATOM   2045 C CE3 . TRP C 1 83 ? 6.675   -22.054 15.484  1.00 53.57  ? 82  TRP C CE3 1 
ATOM   2046 C CZ2 . TRP C 1 83 ? 5.160   -19.762 14.801  1.00 56.48  ? 82  TRP C CZ2 1 
ATOM   2047 C CZ3 . TRP C 1 83 ? 5.780   -21.507 16.372  1.00 49.75  ? 82  TRP C CZ3 1 
ATOM   2048 C CH2 . TRP C 1 83 ? 5.039   -20.371 16.030  1.00 50.45  ? 82  TRP C CH2 1 
ATOM   2049 N N   . GLU C 1 84 ? 9.995   -23.242 15.901  1.00 41.83  ? 83  GLU C N   1 
ATOM   2050 C CA  . GLU C 1 84 ? 9.854   -23.092 17.348  1.00 43.77  ? 83  GLU C CA  1 
ATOM   2051 C C   . GLU C 1 84 ? 11.028  -22.339 17.967  1.00 41.54  ? 83  GLU C C   1 
ATOM   2052 O O   . GLU C 1 84 ? 10.812  -21.483 18.817  1.00 41.89  ? 83  GLU C O   1 
ATOM   2053 C CB  . GLU C 1 84 ? 9.655   -24.425 18.071  1.00 38.80  ? 83  GLU C CB  1 
ATOM   2054 C CG  . GLU C 1 84 ? 8.318   -25.056 17.702  1.00 43.19  ? 83  GLU C CG  1 
ATOM   2055 C CD  . GLU C 1 84 ? 8.219   -26.470 18.208  1.00 46.08  ? 83  GLU C CD  1 
ATOM   2056 O OE1 . GLU C 1 84 ? 9.188   -26.890 18.881  1.00 40.99  ? 83  GLU C OE1 1 
ATOM   2057 O OE2 . GLU C 1 84 ? 7.180   -27.128 17.943  1.00 46.96  ? 83  GLU C OE2 1 
ATOM   2058 N N   . ILE C 1 85 ? 12.262  -22.617 17.526  1.00 42.51  ? 84  ILE C N   1 
ATOM   2059 C CA  . ILE C 1 85 ? 13.405  -22.014 18.194  1.00 38.51  ? 84  ILE C CA  1 
ATOM   2060 C C   . ILE C 1 85 ? 13.409  -20.497 17.994  1.00 39.02  ? 84  ILE C C   1 
ATOM   2061 O O   . ILE C 1 85 ? 13.860  -19.781 18.876  1.00 39.41  ? 84  ILE C O   1 
ATOM   2062 C CB  . ILE C 1 85 ? 14.741  -22.705 17.830  1.00 36.25  ? 84  ILE C CB  1 
ATOM   2063 C CG1 . ILE C 1 85 ? 15.837  -22.327 18.817  1.00 33.05  ? 84  ILE C CG1 1 
ATOM   2064 C CG2 . ILE C 1 85 ? 15.151  -22.446 16.369  1.00 35.63  ? 84  ILE C CG2 1 
ATOM   2065 C CD1 . ILE C 1 85 ? 17.042  -23.264 18.829  1.00 36.24  ? 84  ILE C CD1 1 
ATOM   2066 N N   . GLN C 1 86 ? 12.917  -20.037 16.837  1.00 44.66  ? 85  GLN C N   1 
ATOM   2067 C CA  . GLN C 1 86 ? 12.970  -18.644 16.398  1.00 42.38  ? 85  GLN C CA  1 
ATOM   2068 C C   . GLN C 1 86 ? 11.699  -17.952 16.880  1.00 45.00  ? 85  GLN C C   1 
ATOM   2069 O O   . GLN C 1 86 ? 11.755  -16.778 17.195  1.00 38.84  ? 85  GLN C O   1 
ATOM   2070 C CB  . GLN C 1 86 ? 13.002  -18.539 14.863  1.00 39.67  ? 85  GLN C CB  1 
ATOM   2071 C CG  . GLN C 1 86 ? 13.357  -17.179 14.251  1.00 45.05  ? 85  GLN C CG  1 
ATOM   2072 C CD  . GLN C 1 86 ? 13.704  -17.255 12.762  1.00 54.79  ? 85  GLN C CD  1 
ATOM   2073 O OE1 . GLN C 1 86 ? 13.481  -18.266 12.070  1.00 53.69  ? 85  GLN C OE1 1 
ATOM   2074 N NE2 . GLN C 1 86 ? 14.285  -16.184 12.231  1.00 50.51  ? 85  GLN C NE2 1 
ATOM   2075 N N   . ASN C 1 87 ? 10.570  -18.688 16.962  1.00 44.85  ? 86  ASN C N   1 
ATOM   2076 C CA  . ASN C 1 87 ? 9.273   -18.032 17.128  1.00 49.08  ? 86  ASN C CA  1 
ATOM   2077 C C   . ASN C 1 87 ? 8.652   -18.276 18.511  1.00 53.68  ? 86  ASN C C   1 
ATOM   2078 O O   . ASN C 1 87 ? 7.944   -17.412 19.016  1.00 56.51  ? 86  ASN C O   1 
ATOM   2079 C CB  . ASN C 1 87 ? 8.369   -18.233 15.910  1.00 41.99  ? 86  ASN C CB  1 
ATOM   2080 C CG  . ASN C 1 87 ? 9.045   -17.695 14.665  1.00 52.74  ? 86  ASN C CG  1 
ATOM   2081 O OD1 . ASN C 1 87 ? 9.328   -16.490 14.591  1.00 58.08  ? 86  ASN C OD1 1 
ATOM   2082 N ND2 . ASN C 1 87 ? 9.400   -18.559 13.721  1.00 40.32  ? 86  ASN C ND2 1 
ATOM   2083 N N   . ASN C 1 88 ? 8.913   -19.435 19.135  1.00 52.65  ? 87  ASN C N   1 
ATOM   2084 C CA  . ASN C 1 88 ? 8.238   -19.796 20.381  1.00 56.37  ? 87  ASN C CA  1 
ATOM   2085 C C   . ASN C 1 88 ? 9.200   -20.619 21.241  1.00 51.18  ? 87  ASN C C   1 
ATOM   2086 O O   . ASN C 1 88 ? 8.899   -21.767 21.571  1.00 56.34  ? 87  ASN C O   1 
ATOM   2087 C CB  . ASN C 1 88 ? 6.940   -20.555 20.081  1.00 69.14  ? 87  ASN C CB  1 
ATOM   2088 C CG  . ASN C 1 88 ? 5.877   -20.446 21.154  1.00 73.56  ? 87  ASN C CG  1 
ATOM   2089 O OD1 . ASN C 1 88 ? 6.026   -19.688 22.119  1.00 74.56  ? 87  ASN C OD1 1 
ATOM   2090 N ND2 . ASN C 1 88 ? 4.787   -21.186 20.998  1.00 72.23  ? 87  ASN C ND2 1 
ATOM   2091 N N   . PRO C 1 89 ? 10.409  -20.092 21.556  1.00 42.16  ? 88  PRO C N   1 
ATOM   2092 C CA  . PRO C 1 89 ? 11.492  -20.908 22.094  1.00 44.98  ? 88  PRO C CA  1 
ATOM   2093 C C   . PRO C 1 89 ? 11.347  -21.342 23.547  1.00 60.80  ? 88  PRO C C   1 
ATOM   2094 O O   . PRO C 1 89 ? 12.067  -22.248 23.978  1.00 55.66  ? 88  PRO C O   1 
ATOM   2095 C CB  . PRO C 1 89 ? 12.742  -20.037 21.898  1.00 41.46  ? 88  PRO C CB  1 
ATOM   2096 C CG  . PRO C 1 89 ? 12.210  -18.625 21.960  1.00 41.95  ? 88  PRO C CG  1 
ATOM   2097 C CD  . PRO C 1 89 ? 10.825  -18.702 21.327  1.00 40.13  ? 88  PRO C CD  1 
ATOM   2098 N N   . HIS C 1 90 ? 10.442  -20.684 24.289  1.00 68.50  ? 89  HIS C N   1 
ATOM   2099 C CA  . HIS C 1 90 ? 10.259  -21.025 25.691  1.00 61.84  ? 89  HIS C CA  1 
ATOM   2100 C C   . HIS C 1 90 ? 8.812   -21.422 25.999  1.00 60.07  ? 89  HIS C C   1 
ATOM   2101 O O   . HIS C 1 90 ? 8.359   -21.256 27.115  1.00 65.75  ? 89  HIS C O   1 
ATOM   2102 C CB  . HIS C 1 90 ? 10.862  -19.969 26.622  1.00 55.79  ? 89  HIS C CB  1 
ATOM   2103 C CG  . HIS C 1 90 ? 12.234  -19.452 26.286  1.00 57.92  ? 89  HIS C CG  1 
ATOM   2104 N ND1 . HIS C 1 90 ? 12.442  -18.223 25.693  1.00 57.67  ? 89  HIS C ND1 1 
ATOM   2105 C CD2 . HIS C 1 90 ? 13.466  -19.930 26.540  1.00 60.82  ? 89  HIS C CD2 1 
ATOM   2106 C CE1 . HIS C 1 90 ? 13.750  -17.989 25.562  1.00 54.03  ? 89  HIS C CE1 1 
ATOM   2107 N NE2 . HIS C 1 90 ? 14.397  -19.022 26.052  1.00 59.68  ? 89  HIS C NE2 1 
ATOM   2108 N N   . ALA C 1 91 ? 8.090   -22.020 25.050  1.00 74.15  ? 90  ALA C N   1 
ATOM   2109 C CA  . ALA C 1 91 ? 6.805   -22.629 25.389  1.00 82.77  ? 90  ALA C CA  1 
ATOM   2110 C C   . ALA C 1 91 ? 7.008   -23.987 26.075  1.00 88.63  ? 90  ALA C C   1 
ATOM   2111 O O   . ALA C 1 91 ? 8.112   -24.527 26.033  1.00 88.71  ? 90  ALA C O   1 
ATOM   2112 C CB  . ALA C 1 91 ? 5.939   -22.745 24.152  1.00 83.61  ? 90  ALA C CB  1 
ATOM   2113 N N   . SER C 1 92 ? 5.936   -24.541 26.675  1.00 81.65  ? 91  SER C N   1 
ATOM   2114 C CA  . SER C 1 92 ? 5.993   -25.750 27.497  1.00 85.97  ? 91  SER C CA  1 
ATOM   2115 C C   . SER C 1 92 ? 5.991   -27.055 26.686  1.00 89.82  ? 91  SER C C   1 
ATOM   2116 O O   . SER C 1 92 ? 6.757   -27.974 26.988  1.00 84.59  ? 91  SER C O   1 
ATOM   2117 C CB  . SER C 1 92 ? 4.925   -25.756 28.579  1.00 83.40  ? 91  SER C CB  1 
ATOM   2118 O OG  . SER C 1 92 ? 5.421   -25.219 29.802  1.00 67.81  ? 91  SER C OG  1 
ATOM   2119 N N   . TYR C 1 93 ? 5.114   -27.161 25.680  1.00 79.59  ? 92  TYR C N   1 
ATOM   2120 C CA  . TYR C 1 93 ? 5.043   -28.367 24.865  1.00 88.43  ? 92  TYR C CA  1 
ATOM   2121 C C   . TYR C 1 93 ? 4.890   -29.599 25.779  1.00 91.40  ? 92  TYR C C   1 
ATOM   2122 O O   . TYR C 1 93 ? 3.960   -30.419 25.570  1.00 86.98  ? 92  TYR C O   1 
ATOM   2123 C CB  . TYR C 1 93 ? 6.290   -28.534 23.989  1.00 85.60  ? 92  TYR C CB  1 
ATOM   2124 C CG  . TYR C 1 93 ? 6.721   -27.307 23.190  1.00 79.49  ? 92  TYR C CG  1 
ATOM   2125 C CD1 . TYR C 1 93 ? 6.176   -27.030 21.936  1.00 74.82  ? 92  TYR C CD1 1 
ATOM   2126 C CD2 . TYR C 1 93 ? 7.689   -26.436 23.682  1.00 71.91  ? 92  TYR C CD2 1 
ATOM   2127 C CE1 . TYR C 1 93 ? 6.572   -25.920 21.203  1.00 69.97  ? 92  TYR C CE1 1 
ATOM   2128 C CE2 . TYR C 1 93 ? 8.101   -25.329 22.954  1.00 74.86  ? 92  TYR C CE2 1 
ATOM   2129 C CZ  . TYR C 1 93 ? 7.538   -25.068 21.714  1.00 68.41  ? 92  TYR C CZ  1 
ATOM   2130 O OH  . TYR C 1 93 ? 7.926   -23.959 21.012  1.00 74.49  ? 92  TYR C OH  1 
HETATM 2131 S S   . SO4 D 2 .  ? 0.084   -33.204 2.325   1.00 109.18 ? 101 SO4 A S   1 
HETATM 2132 O O1  . SO4 D 2 .  ? 0.869   -33.895 1.338   1.00 101.45 ? 101 SO4 A O1  1 
HETATM 2133 O O2  . SO4 D 2 .  ? 0.088   -31.790 2.045   1.00 110.72 ? 101 SO4 A O2  1 
HETATM 2134 O O3  . SO4 D 2 .  ? -1.271  -33.689 2.282   1.00 127.43 ? 101 SO4 A O3  1 
HETATM 2135 O O4  . SO4 D 2 .  ? 0.641   -33.446 3.631   1.00 107.43 ? 101 SO4 A O4  1 
HETATM 2136 S S   . SO4 E 2 .  ? -10.768 -24.124 1.107   1.00 119.53 ? 102 SO4 A S   1 
HETATM 2137 O O1  . SO4 E 2 .  ? -10.698 -24.094 -0.331  1.00 117.01 ? 102 SO4 A O1  1 
HETATM 2138 O O2  . SO4 E 2 .  ? -11.180 -22.833 1.594   1.00 118.05 ? 102 SO4 A O2  1 
HETATM 2139 O O3  . SO4 E 2 .  ? -11.723 -25.121 1.514   1.00 129.93 ? 102 SO4 A O3  1 
HETATM 2140 O O4  . SO4 E 2 .  ? -9.473  -24.449 1.648   1.00 114.65 ? 102 SO4 A O4  1 
HETATM 2141 C C1  . EDO F 3 .  ? 13.343  -19.561 -7.397  1.00 57.04  ? 103 EDO A C1  1 
HETATM 2142 O O1  . EDO F 3 .  ? 14.413  -18.642 -7.115  1.00 47.70  ? 103 EDO A O1  1 
HETATM 2143 C C2  . EDO F 3 .  ? 12.377  -19.207 -8.481  1.00 51.50  ? 103 EDO A C2  1 
HETATM 2144 O O2  . EDO F 3 .  ? 11.780  -17.916 -8.350  1.00 45.06  ? 103 EDO A O2  1 
HETATM 2145 S S   . SO4 G 2 .  ? 7.957   -29.355 5.827   1.00 82.42  ? 104 SO4 A S   1 
HETATM 2146 O O1  . SO4 G 2 .  ? 8.524   -28.414 4.906   1.00 77.22  ? 104 SO4 A O1  1 
HETATM 2147 O O2  . SO4 G 2 .  ? 7.679   -30.589 5.120   1.00 78.26  ? 104 SO4 A O2  1 
HETATM 2148 O O3  . SO4 G 2 .  ? 8.906   -29.577 6.888   1.00 71.46  ? 104 SO4 A O3  1 
HETATM 2149 O O4  . SO4 G 2 .  ? 6.719   -28.842 6.392   1.00 73.75  ? 104 SO4 A O4  1 
HETATM 2150 S S   . SO4 H 2 .  ? 7.450   -8.430  -24.565 1.00 80.21  ? 101 SO4 B S   1 
HETATM 2151 O O1  . SO4 H 2 .  ? 8.428   -8.717  -25.576 1.00 54.59  ? 101 SO4 B O1  1 
HETATM 2152 O O2  . SO4 H 2 .  ? 6.135   -8.734  -25.099 1.00 63.45  ? 101 SO4 B O2  1 
HETATM 2153 O O3  . SO4 H 2 .  ? 7.663   -9.245  -23.380 1.00 65.15  ? 101 SO4 B O3  1 
HETATM 2154 O O4  . SO4 H 2 .  ? 7.573   -7.029  -24.214 1.00 67.04  ? 101 SO4 B O4  1 
HETATM 2155 S S   . SO4 I 2 .  ? 14.376  -27.306 -26.078 1.00 81.97  ? 102 SO4 B S   1 
HETATM 2156 O O1  . SO4 I 2 .  ? 14.989  -26.160 -25.481 1.00 78.15  ? 102 SO4 B O1  1 
HETATM 2157 O O2  . SO4 I 2 .  ? 15.402  -28.161 -26.628 1.00 78.73  ? 102 SO4 B O2  1 
HETATM 2158 O O3  . SO4 I 2 .  ? 13.636  -28.026 -25.078 1.00 103.20 ? 102 SO4 B O3  1 
HETATM 2159 O O4  . SO4 I 2 .  ? 13.462  -26.881 -27.117 1.00 84.78  ? 102 SO4 B O4  1 
HETATM 2160 C C01 . YEB J 4 .  ? 16.851  -16.565 -25.467 0.78 42.81  ? 103 YEB B C01 1 
HETATM 2161 C C03 . YEB J 4 .  ? 15.124  -16.123 -23.758 0.78 46.19  ? 103 YEB B C03 1 
HETATM 2162 C C08 . YEB J 4 .  ? 19.996  -15.060 -23.882 0.78 56.44  ? 103 YEB B C08 1 
HETATM 2163 C C09 . YEB J 4 .  ? 21.070  -16.116 -23.897 0.78 59.62  ? 103 YEB B C09 1 
HETATM 2164 C C11 . YEB J 4 .  ? 20.039  -17.322 -22.199 0.78 55.34  ? 103 YEB B C11 1 
HETATM 2165 C C12 . YEB J 4 .  ? 18.900  -16.348 -22.104 0.78 53.62  ? 103 YEB B C12 1 
HETATM 2166 N N02 . YEB J 4 .  ? 16.537  -16.049 -24.134 0.78 43.90  ? 103 YEB B N02 1 
HETATM 2167 N N07 . YEB J 4 .  ? 18.750  -15.683 -23.410 0.78 49.47  ? 103 YEB B N07 1 
HETATM 2168 O O05 . YEB J 4 .  ? 17.593  -13.888 -24.620 0.78 53.61  ? 103 YEB B O05 1 
HETATM 2169 O O06 . YEB J 4 .  ? 16.958  -14.493 -22.289 0.78 50.56  ? 103 YEB B O06 1 
HETATM 2170 O O10 . YEB J 4 .  ? 21.240  -16.687 -22.611 0.78 54.64  ? 103 YEB B O10 1 
HETATM 2171 S S04 . YEB J 4 .  ? 17.419  -14.840 -23.585 0.78 47.30  ? 103 YEB B S04 1 
HETATM 2172 C C1  . EDO K 3 .  ? 15.998  -35.835 16.567  1.00 51.06  ? 101 EDO C C1  1 
HETATM 2173 O O1  . EDO K 3 .  ? 14.962  -36.760 16.296  1.00 63.26  ? 101 EDO C O1  1 
HETATM 2174 C C2  . EDO K 3 .  ? 15.736  -35.001 17.757  1.00 51.77  ? 101 EDO C C2  1 
HETATM 2175 O O2  . EDO K 3 .  ? 14.717  -35.556 18.571  1.00 49.26  ? 101 EDO C O2  1 
HETATM 2176 S S   . SO4 L 2 .  ? 28.150  -37.954 12.281  1.00 97.93  ? 102 SO4 C S   1 
HETATM 2177 O O1  . SO4 L 2 .  ? 28.505  -36.559 12.213  1.00 102.43 ? 102 SO4 C O1  1 
HETATM 2178 O O2  . SO4 L 2 .  ? 27.176  -38.254 11.261  1.00 74.51  ? 102 SO4 C O2  1 
HETATM 2179 O O3  . SO4 L 2 .  ? 29.317  -38.765 12.084  1.00 89.87  ? 102 SO4 C O3  1 
HETATM 2180 O O4  . SO4 L 2 .  ? 27.603  -38.240 13.580  1.00 116.55 ? 102 SO4 C O4  1 
HETATM 2181 O O   . HOH M 5 .  ? 10.287  -8.448  -12.167 1.00 68.49  ? 201 HOH A O   1 
HETATM 2182 O O   . HOH M 5 .  ? 1.299   -25.079 -5.932  1.00 64.40  ? 202 HOH A O   1 
HETATM 2183 O O   . HOH M 5 .  ? 12.331  -9.508  -7.212  1.00 47.06  ? 203 HOH A O   1 
HETATM 2184 O O   . HOH M 5 .  ? 4.415   -29.025 7.141   1.00 64.84  ? 204 HOH A O   1 
HETATM 2185 O O   . HOH M 5 .  ? 9.687   -18.828 10.560  1.00 63.72  ? 205 HOH A O   1 
HETATM 2186 O O   . HOH M 5 .  ? 1.052   -4.657  -10.090 1.00 41.28  ? 206 HOH A O   1 
HETATM 2187 O O   . HOH M 5 .  ? -2.843  3.639   -2.102  1.00 51.56  ? 207 HOH A O   1 
HETATM 2188 O O   . HOH M 5 .  ? 8.826   -32.130 3.683   1.00 63.84  ? 208 HOH A O   1 
HETATM 2189 O O   . HOH M 5 .  ? 17.152  -8.120  -20.011 1.00 50.62  ? 209 HOH A O   1 
HETATM 2190 O O   . HOH M 5 .  ? -3.514  -30.927 -3.440  1.00 95.29  ? 210 HOH A O   1 
HETATM 2191 O O   . HOH M 5 .  ? 0.387   -24.335 13.829  1.00 66.42  ? 211 HOH A O   1 
HETATM 2192 O O   . HOH M 5 .  ? -6.126  -12.975 -16.672 1.00 69.13  ? 212 HOH A O   1 
HETATM 2193 O O   . HOH M 5 .  ? 10.780  -12.147 5.860   1.00 50.27  ? 213 HOH A O   1 
HETATM 2194 O O   . HOH M 5 .  ? 8.239   -22.714 -9.538  1.00 43.36  ? 214 HOH A O   1 
HETATM 2195 O O   . HOH M 5 .  ? -6.574  -11.192 -11.393 1.00 60.08  ? 215 HOH A O   1 
HETATM 2196 O O   . HOH M 5 .  ? 7.542   -7.940  4.508   1.00 45.46  ? 216 HOH A O   1 
HETATM 2197 O O   . HOH M 5 .  ? 3.858   -3.361  -3.171  1.00 34.82  ? 217 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? -8.635  -15.646 -1.403  1.00 50.03  ? 218 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? 15.623  -17.766 -9.196  1.00 67.25  ? 219 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? -1.514  -10.624 16.159  1.00 66.67  ? 220 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? 1.667   -6.523  5.582   1.00 55.12  ? 221 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 9.990   -5.088  -7.583  1.00 51.70  ? 222 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? 8.369   -18.105 -10.934 1.00 40.45  ? 223 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? -8.120  -17.286 6.756   1.00 68.74  ? 224 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? -2.930  -21.829 -0.658  1.00 36.09  ? 225 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? -6.397  -15.545 -8.125  1.00 40.51  ? 226 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 7.207   -7.961  1.193   1.00 41.65  ? 227 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 3.902   -7.711  1.038   1.00 39.38  ? 228 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 15.259  -24.451 2.215   1.00 50.17  ? 229 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 6.359   -10.390 -11.915 1.00 58.46  ? 230 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? -1.664  -7.937  -16.446 1.00 82.55  ? 231 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? -6.326  -18.886 -5.644  1.00 64.34  ? 232 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 9.108   -13.012 9.849   1.00 51.86  ? 233 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? -6.268  -25.534 -5.773  1.00 61.90  ? 234 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 16.364  -12.853 1.468   1.00 30.01  ? 235 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? -4.327  -26.106 7.708   1.00 60.76  ? 236 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 1.126   0.782   -7.297  1.00 46.60  ? 237 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 12.281  -15.106 -11.689 1.00 51.45  ? 238 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -8.729  -16.564 2.052   1.00 52.34  ? 239 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 19.062  -15.675 7.280   1.00 35.60  ? 240 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? -4.992  -21.072 6.093   1.00 46.03  ? 241 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 8.984   -6.182  -1.803  1.00 63.90  ? 242 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 7.800   -17.843 8.873   1.00 62.12  ? 243 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 10.665  -12.272 -5.927  1.00 44.40  ? 244 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 16.832  -17.750 -10.356 1.00 50.37  ? 245 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 10.472  -29.450 3.264   1.00 57.11  ? 246 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 13.006  -15.619 -9.244  1.00 37.55  ? 247 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? -2.246  -11.803 11.245  1.00 53.45  ? 248 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? -1.528  -20.223 11.124  1.00 66.16  ? 249 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? -9.014  -21.216 -1.591  1.00 73.49  ? 250 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 10.390  -23.466 9.837   1.00 43.05  ? 251 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? -0.687  -23.289 9.576   1.00 54.04  ? 252 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 11.992  -13.522 -8.204  1.00 53.79  ? 253 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 12.467  -11.771 -4.227  1.00 32.44  ? 254 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 0.951   -10.337 11.638  1.00 48.92  ? 255 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 7.272   -17.583 -15.423 1.00 58.96  ? 256 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 15.158  -11.790 -5.200  1.00 59.09  ? 257 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? -1.733  -28.920 10.193  1.00 63.17  ? 258 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? -4.159  -18.717 13.476  1.00 52.26  ? 259 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? -1.558  -20.698 7.088   1.00 50.99  ? 260 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 1.445   -25.063 -10.290 1.00 55.45  ? 261 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? -7.178  -12.692 6.486   1.00 43.77  ? 262 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 0.271   -17.679 -18.921 1.00 65.15  ? 263 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 6.963   -29.395 -5.131  1.00 74.46  ? 264 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 2.466   -29.685 -0.568  1.00 55.93  ? 265 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 10.176  -5.781  -3.641  1.00 57.52  ? 266 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 11.024  -11.906 11.816  1.00 66.69  ? 267 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? -4.874  -10.777 7.122   1.00 64.09  ? 268 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? -2.573  -7.255  11.439  1.00 65.84  ? 269 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 7.354   -2.103  0.026   1.00 81.54  ? 270 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 6.146   -15.302 -14.788 1.00 69.62  ? 271 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 12.514  -11.331 7.444   1.00 60.02  ? 272 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 8.532   -20.236 -18.244 1.00 53.83  ? 273 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 8.744   -9.019  -13.546 1.00 48.13  ? 274 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 16.194  -12.779 -16.568 1.00 61.82  ? 275 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 8.655   -30.108 9.850   1.00 45.72  ? 276 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 10.330  -7.701  0.393   1.00 34.34  ? 277 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 21.586  -16.658 -0.421  1.00 41.98  ? 278 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? -7.905  -20.892 -5.780  1.00 70.73  ? 279 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? -7.375  -20.086 6.757   1.00 118.26 ? 280 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 20.566  -16.601 -3.487  1.00 34.52  ? 281 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? 0.140   -35.148 6.260   1.00 76.07  ? 282 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 2.622   -9.845  -13.343 1.00 74.45  ? 283 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -8.733  -19.426 -3.490  1.00 49.59  ? 284 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 5.349   -6.145  0.656   1.00 52.25  ? 285 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 21.041  -21.007 -4.159  1.00 70.47  ? 286 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 11.035  -28.851 -3.910  1.00 75.29  ? 287 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 8.639   -27.774 -7.729  1.00 66.12  ? 288 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -11.156 -16.181 -3.852  1.00 72.49  ? 289 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? -0.791  -3.435  -11.036 1.00 60.32  ? 290 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? -4.871  -8.673  10.242  1.00 56.44  ? 291 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? -8.044  -11.422 -8.278  1.00 43.05  ? 292 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? -6.850  -26.219 3.819   1.00 55.59  ? 293 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? -6.643  -23.172 -6.932  1.00 74.17  ? 294 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 16.060  -9.453  -9.751  1.00 49.49  ? 295 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 8.310   -9.956  5.675   1.00 65.43  ? 296 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? -8.084  -14.006 -9.390  1.00 60.90  ? 297 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? -9.976  -14.655 -12.747 1.00 57.90  ? 298 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? -0.104  5.086   -3.715  1.00 85.84  ? 299 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 14.988  -28.087 -1.135  1.00 68.09  ? 300 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? 4.369   -7.003  -10.867 1.00 57.49  ? 301 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? -6.939  -22.368 5.725   1.00 59.35  ? 302 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? -11.480 -27.783 -2.104  1.00 91.64  ? 303 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 7.843   -16.881 -13.483 1.00 52.74  ? 304 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? 4.015   -36.418 2.921   1.00 78.90  ? 305 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? 8.598   -7.565  2.611   1.00 61.68  ? 306 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? -9.926  -19.849 4.819   1.00 64.82  ? 307 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 4.237   -9.183  -11.376 1.00 64.16  ? 308 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? -5.988  -13.786 13.927  1.00 60.62  ? 309 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 12.056  -18.249 -14.899 1.00 70.23  ? 310 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? 4.789   -2.911  1.425   1.00 67.16  ? 311 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? -5.846  -20.670 -8.220  1.00 73.34  ? 312 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? 0.716   -21.539 17.489  1.00 69.72  ? 313 HOH A O   1 
HETATM 2294 O O   . HOH N 5 .  ? 30.740  -8.982  -28.904 1.00 67.03  ? 201 HOH B O   1 
HETATM 2295 O O   . HOH N 5 .  ? 39.407  -11.910 -38.665 1.00 75.63  ? 202 HOH B O   1 
HETATM 2296 O O   . HOH N 5 .  ? 19.034  -21.890 -22.885 1.00 66.29  ? 203 HOH B O   1 
HETATM 2297 O O   . HOH N 5 .  ? 22.481  -11.398 -43.132 1.00 59.22  ? 204 HOH B O   1 
HETATM 2298 O O   . HOH N 5 .  ? 9.886   -16.632 -43.584 1.00 74.49  ? 205 HOH B O   1 
HETATM 2299 O O   . HOH N 5 .  ? 13.504  -4.314  -40.957 1.00 91.04  ? 206 HOH B O   1 
HETATM 2300 O O   . HOH N 5 .  ? 29.712  -19.073 -40.339 1.00 56.50  ? 207 HOH B O   1 
HETATM 2301 O O   . HOH N 5 .  ? 25.776  -5.011  -32.814 1.00 57.31  ? 208 HOH B O   1 
HETATM 2302 O O   . HOH N 5 .  ? 35.557  -23.314 -29.730 1.00 73.96  ? 209 HOH B O   1 
HETATM 2303 O O   . HOH N 5 .  ? 25.643  -23.362 -30.548 1.00 42.91  ? 210 HOH B O   1 
HETATM 2304 O O   . HOH N 5 .  ? 11.531  -20.028 -20.211 1.00 117.35 ? 211 HOH B O   1 
HETATM 2305 O O   . HOH N 5 .  ? 25.329  -0.900  -28.529 1.00 46.42  ? 212 HOH B O   1 
HETATM 2306 O O   . HOH N 5 .  ? 24.760  -5.252  -29.282 1.00 52.20  ? 213 HOH B O   1 
HETATM 2307 O O   . HOH N 5 .  ? 17.628  -26.180 -28.489 1.00 53.84  ? 214 HOH B O   1 
HETATM 2308 O O   . HOH N 5 .  ? 6.141   -12.047 -25.742 1.00 46.89  ? 215 HOH B O   1 
HETATM 2309 O O   . HOH N 5 .  ? 27.742  -8.502  -28.329 1.00 54.33  ? 216 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 17.996  -9.851  -43.097 1.00 69.37  ? 217 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 16.494  -19.433 -28.411 1.00 31.42  ? 218 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 28.191  -4.612  -36.159 1.00 54.60  ? 219 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 9.735   -11.914 -37.944 1.00 77.40  ? 220 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 30.235  -13.167 -45.240 1.00 66.45  ? 221 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 10.376  -19.925 -42.886 1.00 58.94  ? 222 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 24.811  -1.840  -24.539 1.00 62.32  ? 223 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 19.712  -3.549  -23.361 1.00 94.18  ? 224 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 5.983   -7.622  -32.102 1.00 65.57  ? 225 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 23.623  -4.449  -36.282 1.00 38.02  ? 226 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 6.921   -18.698 -34.552 1.00 68.64  ? 227 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 18.097  -0.893  -37.967 1.00 41.04  ? 228 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 10.427  -19.006 -32.757 1.00 47.57  ? 229 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 21.121  -13.600 -42.018 1.00 51.77  ? 230 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 7.185   -18.431 -31.525 1.00 54.20  ? 231 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 27.720  -18.160 -24.224 1.00 73.75  ? 232 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 22.316  -23.952 -28.164 1.00 70.75  ? 233 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 1.625   -12.814 -27.901 1.00 55.56  ? 234 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 32.851  -18.605 -41.343 1.00 68.77  ? 235 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 24.684  -1.491  -36.181 1.00 74.20  ? 236 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 10.341  -21.901 -32.496 1.00 52.01  ? 237 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 17.865  -15.891 -45.225 1.00 49.73  ? 238 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 23.598  -2.793  -28.724 1.00 45.10  ? 239 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 4.330   -19.034 -25.490 1.00 68.47  ? 240 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 21.594  3.447   -32.222 1.00 45.42  ? 241 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 24.177  0.888   -36.591 1.00 66.58  ? 242 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 19.285  -25.675 -33.785 1.00 54.64  ? 243 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 16.277  -26.295 -34.399 1.00 55.48  ? 244 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 19.977  -27.534 -36.215 1.00 48.46  ? 245 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 14.518  -6.502  -40.828 1.00 49.25  ? 246 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 21.182  -26.701 -29.318 1.00 78.61  ? 247 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 20.494  -10.041 -42.265 1.00 37.75  ? 248 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 10.071  -23.546 -26.032 1.00 56.04  ? 249 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 12.715  -22.405 -20.211 1.00 64.63  ? 250 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 17.831  4.720   -34.224 1.00 55.64  ? 251 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 14.241  -24.666 -40.172 1.00 51.92  ? 252 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 7.710   -8.574  -20.302 1.00 94.96  ? 253 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 24.958  -6.007  -34.959 1.00 72.67  ? 254 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 2.924   -8.243  -26.950 1.00 65.29  ? 255 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 23.379  -11.212 -21.029 1.00 58.17  ? 256 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 27.287  -10.919 -28.193 1.00 56.94  ? 257 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 8.509   -19.796 -30.583 1.00 105.90 ? 258 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 7.078   -13.007 -39.181 1.00 71.52  ? 259 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 24.996  -7.068  -41.683 1.00 61.24  ? 260 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 17.648  -3.669  -21.325 1.00 57.51  ? 261 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 27.784  -25.093 -34.603 1.00 56.60  ? 262 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 31.929  -22.084 -37.600 1.00 47.73  ? 263 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 15.726  -8.485  -42.491 1.00 63.24  ? 264 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 8.390   -8.714  -16.297 1.00 60.62  ? 265 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 16.606  -0.555  -25.107 1.00 61.28  ? 266 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 17.394  -22.788 -19.722 1.00 70.04  ? 267 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 31.432  -12.238 -36.902 1.00 62.28  ? 268 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 9.982   -7.223  -40.617 1.00 64.05  ? 269 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 28.986  -17.141 -46.673 1.00 61.33  ? 270 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 21.879  -28.828 -35.167 1.00 68.32  ? 271 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 19.238  3.733   -32.842 1.00 58.43  ? 272 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 16.220  1.787   -29.382 1.00 63.15  ? 273 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 7.525   -13.862 -44.428 1.00 69.29  ? 274 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 13.804  -22.512 -41.102 1.00 67.85  ? 275 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 20.013  -21.034 -20.408 1.00 62.32  ? 276 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 7.072   -9.451  -18.022 1.00 60.38  ? 277 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 17.496  4.204   -25.466 1.00 66.74  ? 278 HOH B O   1 
HETATM 2372 O O   . HOH O 5 .  ? 4.749   -26.252 16.771  1.00 54.78  ? 201 HOH C O   1 
HETATM 2373 O O   . HOH O 5 .  ? 29.747  -27.881 31.292  1.00 66.05  ? 202 HOH C O   1 
HETATM 2374 O O   . HOH O 5 .  ? 19.540  -20.288 30.513  1.00 75.21  ? 203 HOH C O   1 
HETATM 2375 O O   . HOH O 5 .  ? 25.380  -38.944 12.582  1.00 48.01  ? 204 HOH C O   1 
HETATM 2376 O O   . HOH O 5 .  ? 17.230  -16.779 14.360  1.00 56.04  ? 205 HOH C O   1 
HETATM 2377 O O   . HOH O 5 .  ? 15.184  -22.202 26.253  1.00 88.86  ? 206 HOH C O   1 
HETATM 2378 O O   . HOH O 5 .  ? 11.970  -31.258 7.986   1.00 52.30  ? 207 HOH C O   1 
HETATM 2379 O O   . HOH O 5 .  ? 14.552  -26.215 28.848  1.00 80.09  ? 208 HOH C O   1 
HETATM 2380 O O   . HOH O 5 .  ? 25.502  -37.029 10.026  1.00 52.77  ? 209 HOH C O   1 
HETATM 2381 O O   . HOH O 5 .  ? 19.154  -41.605 12.339  1.00 44.67  ? 210 HOH C O   1 
HETATM 2382 O O   . HOH O 5 .  ? 8.042   -36.434 18.746  1.00 64.86  ? 211 HOH C O   1 
HETATM 2383 O O   . HOH O 5 .  ? 30.278  -38.865 28.552  1.00 97.55  ? 212 HOH C O   1 
HETATM 2384 O O   . HOH O 5 .  ? 25.142  -17.498 13.730  1.00 48.31  ? 213 HOH C O   1 
HETATM 2385 O O   . HOH O 5 .  ? 22.499  -40.942 18.658  1.00 66.56  ? 214 HOH C O   1 
HETATM 2386 O O   . HOH O 5 .  ? 11.414  -28.312 28.617  1.00 57.98  ? 215 HOH C O   1 
HETATM 2387 O O   . HOH O 5 .  ? 24.583  -31.231 10.770  1.00 46.43  ? 216 HOH C O   1 
HETATM 2388 O O   . HOH O 5 .  ? 24.955  -19.670 6.210   1.00 49.85  ? 217 HOH C O   1 
HETATM 2389 O O   . HOH O 5 .  ? 13.950  -20.788 12.130  1.00 46.48  ? 218 HOH C O   1 
HETATM 2390 O O   . HOH O 5 .  ? 29.848  -29.079 12.164  1.00 58.05  ? 219 HOH C O   1 
HETATM 2391 O O   . HOH O 5 .  ? 15.904  -37.321 20.042  1.00 64.58  ? 220 HOH C O   1 
HETATM 2392 O O   . HOH O 5 .  ? 27.259  -36.339 24.748  1.00 65.27  ? 221 HOH C O   1 
HETATM 2393 O O   . HOH O 5 .  ? 18.026  -40.070 38.013  1.00 79.28  ? 222 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 27.382  -36.958 15.830  1.00 51.29  ? 223 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 21.295  -33.985 16.708  1.00 34.31  ? 224 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 21.411  -28.298 11.098  1.00 39.04  ? 225 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 15.051  -17.430 19.219  1.00 53.35  ? 226 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 2.623   -30.053 27.843  1.00 75.32  ? 227 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 27.394  -15.482 12.680  1.00 46.36  ? 228 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 19.841  -28.608 8.471   1.00 41.94  ? 229 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 8.049   -18.798 23.677  1.00 52.38  ? 230 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 30.370  -36.611 20.981  1.00 51.16  ? 231 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 24.831  -17.880 20.646  1.00 63.11  ? 232 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 5.983   -17.807 10.933  1.00 54.29  ? 233 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 18.322  -19.944 10.637  1.00 52.18  ? 234 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 30.080  -33.315 35.579  1.00 64.28  ? 235 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 29.789  -35.423 28.956  1.00 66.63  ? 236 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 20.269  -29.041 4.722   1.00 61.56  ? 237 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 31.489  -33.131 25.733  1.00 71.39  ? 238 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 29.545  -31.317 15.932  1.00 66.22  ? 239 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 30.594  -42.969 15.662  1.00 81.63  ? 240 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 13.583  -37.007 13.543  1.00 58.06  ? 241 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 29.956  -25.273 31.957  1.00 72.63  ? 242 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 24.493  -39.346 20.332  1.00 41.93  ? 243 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 13.579  -38.510 9.617   1.00 62.05  ? 244 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 13.410  -29.205 4.033   1.00 61.71  ? 245 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 20.485  -13.025 13.249  1.00 42.64  ? 246 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 29.139  -32.366 18.180  1.00 50.00  ? 247 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 15.498  -13.611 10.951  1.00 59.04  ? 248 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 26.025  -33.302 34.677  1.00 69.63  ? 249 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 29.087  -39.437 31.270  1.00 53.30  ? 250 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 2.364   -29.335 13.084  1.00 67.36  ? 251 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 13.920  -32.103 2.817   1.00 55.54  ? 252 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 21.639  -18.239 21.764  1.00 57.77  ? 253 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 27.267  -38.874 24.850  1.00 76.42  ? 254 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 19.046  -18.430 24.765  1.00 55.51  ? 255 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 7.559   -30.630 11.892  1.00 66.45  ? 256 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 31.524  -42.738 12.065  1.00 56.09  ? 257 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 20.525  -39.738 26.072  1.00 58.73  ? 258 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 22.147  -14.731 12.913  1.00 65.66  ? 259 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 23.750  -16.099 11.494  1.00 54.92  ? 260 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 28.259  -40.945 26.864  1.00 52.85  ? 261 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 16.238  -16.555 24.330  1.00 68.63  ? 262 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 7.322   -33.641 9.890   1.00 53.03  ? 263 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 11.277  -20.906 10.848  1.00 50.77  ? 264 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 5.121   -24.245 18.425  1.00 77.07  ? 265 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 20.884  -33.006 7.249   1.00 76.60  ? 266 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 30.532  -17.454 9.425   1.00 68.99  ? 267 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 13.042  -40.053 16.416  1.00 79.65  ? 268 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 16.880  -38.208 28.710  1.00 74.68  ? 269 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 28.668  -17.764 28.661  1.00 70.90  ? 270 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 27.246  -41.200 29.405  1.00 68.60  ? 271 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 34.277  -22.829 27.839  1.00 64.88  ? 272 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 29.432  -40.174 18.578  1.00 59.55  ? 273 HOH C O   1 
# 
